data_8U73
# 
_entry.id   8U73 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8U73         pdb_00008u73 10.2210/pdb8u73/pdb 
WWPDB D_1000277518 ?            ?                   
EMDB  EMD-41967    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-26 ? 
2 'EM metadata'     1 0 2025-03-26 ? 
3 'Additional map'  1 0 2025-03-26 1 
4 FSC               1 0 2025-03-26 ? 
5 'Half map'        1 0 2025-03-26 1 
6 'Half map'        1 0 2025-03-26 2 
7 Image             1 0 2025-03-26 ? 
8 'Primary map'     1 0 2025-03-26 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Additional map'  repository 'Initial release' ? ? 
4 4 FSC               repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 'Half map'        repository 'Initial release' ? ? 
7 7 Image             repository 'Initial release' ? ? 
8 8 'Primary map'     repository 'Initial release' ? ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8U73 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-14 
_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        'R399A sea urchin SLC9C1 pH 8 in Na+' 
_pdbx_database_related.db_id          EMD-41967 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sandipan-chowdhury@uiowa.edu 
_pdbx_contact_author.name_first         Sandipan 
_pdbx_contact_author.name_last          Chowdhury 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0695-7968 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chowdhury, S.' 1 0000-0002-0695-7968 
'Pal, K.'       2 0000-0002-0825-0325 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structure of R399A mutant of sea urchin SLC9C1 at pH 8 in Na+' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chowdhury, S.' 1 0000-0002-0695-7968 
primary 'Pal, K.'       2 0000-0002-0825-0325 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Sperm-specific sodium proton exchanger'                                                         146650.359 2 ? 
R399A ? ? 
2 non-polymer syn '(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate' 760.076    3 ? 
?     ? ? 
3 non-polymer syn Digitonin                                                                                        1229.312   4 ? 
?     ? ? 
# 
_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       
;MKKRVVKLRELVPAVAALAVAVLIQSATGSSGGSGHTPTTQATHADDHDLTTHNGTEEHDDGHDDGHDDLHAHAPKVIVF
ISGSCLFGAISRSLFKKLPIPYTVVLLILGAILGVVASNVPLVEEHTRDVAHMDPHVLLQIFLPVLIFESAFAMDVHTFM
RSFSQVCILALFGLVVASVLTAVLAMNLFNYNWNFSEAMMFGAIMSATDPVAVVALLKDLGASKQLGTIIEGESLLNDGC
AIVIFNVFMKMVFFPQLTSTVGQNVLYFLQVAVAGPLWGYAVAKVTVFFLSHIFNDALVEITITLAATYLTYYIGDIWLE
VSGVLAVVVLGLIVNAEKTSISPEVEVFLHRFWEMLAYLANTLIFMMVGVVVTQKALVAVDKMDWFYLIILYLAITIIAG
MVISLFSPILSRIGYGLTWRNAVIMTWGGLRGAVGLALALVVENLAGNDVIGSKFLFHTAGIVVLTLVINATTIQTLLRI
LGMSDISIPKRLAMAGAVRRIHEGQNRTLNMLKSDRFLADADWDIATAACEISDPYSALSDDENAPADELTLGERKSVCP
GCKAMVPNEPSPREFADMMEEARLRMLKAEKISYWKQFEHGMLAREALRLLVQHAEVAADEKDQFILVDDLKKSWQIKGI
YPWLKRKLEDLISEKKIAAIPMPKYKLGKLMYKICHHMAFEVTINIAIVLNIVPIIMEFVVQDKMASVSTMAAPGSTVSS
EPSSLQKIEDALRISNYVFFVIYAIEAIVKILGLGRHYIVSHWNKFDAFILVVALVDIIIAETLLKGSITINLSSIKVVK
LFRLLRGLRMLRLTKALIPKLILVVNGKINNQLSLGYDVGKGYIIGEEEVGKIIDRMVDNKKILRELKHISETGRLQVVK
ELGLLQREHPGIAVSVKTRQAIRTILNHSRETIHELQGAGLLDEMEAHKLELTVEIKMKRLMNAPSSIPPPPPENLLKNV
SWLAGDMKLIDFIKARASLLHFDYGEVIVREGDESDGLFLIVSGLVKLYGKSAFLDHDNPPVTAGSEENEVFEDYLTVGN
VIGEMGVLTKKPRNATVTCETTVQVYFITAEDMNIAIDTFTLYPSLEYRLWRVVAIRIATPLIMEQMAFQGWTQEKVKLH
LERGYLVDLAESHFQFNIDATLEDVILINGTAYNAHTREEIRSPCLISRTVHKLTFQYTATEEPRLFVVRNAEYNGPILD
GRLDVDSKRSLISITEISSNMCLKHAAELRQKNSKVMLSRKSSGAAAKEEEDCIPNTSDVEQAAGVSPSVPTKTTPKPKS
FLPSLGLSMSKERVNGEAVEESPVKTKQGEETPETEEGAAPRVNV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKKRVVKLRELVPAVAALAVAVLIQSATGSSGGSGHTPTTQATHADDHDLTTHNGTEEHDDGHDDGHDDLHAHAPKVIVF
ISGSCLFGAISRSLFKKLPIPYTVVLLILGAILGVVASNVPLVEEHTRDVAHMDPHVLLQIFLPVLIFESAFAMDVHTFM
RSFSQVCILALFGLVVASVLTAVLAMNLFNYNWNFSEAMMFGAIMSATDPVAVVALLKDLGASKQLGTIIEGESLLNDGC
AIVIFNVFMKMVFFPQLTSTVGQNVLYFLQVAVAGPLWGYAVAKVTVFFLSHIFNDALVEITITLAATYLTYYIGDIWLE
VSGVLAVVVLGLIVNAEKTSISPEVEVFLHRFWEMLAYLANTLIFMMVGVVVTQKALVAVDKMDWFYLIILYLAITIIAG
MVISLFSPILSRIGYGLTWRNAVIMTWGGLRGAVGLALALVVENLAGNDVIGSKFLFHTAGIVVLTLVINATTIQTLLRI
LGMSDISIPKRLAMAGAVRRIHEGQNRTLNMLKSDRFLADADWDIATAACEISDPYSALSDDENAPADELTLGERKSVCP
GCKAMVPNEPSPREFADMMEEARLRMLKAEKISYWKQFEHGMLAREALRLLVQHAEVAADEKDQFILVDDLKKSWQIKGI
YPWLKRKLEDLISEKKIAAIPMPKYKLGKLMYKICHHMAFEVTINIAIVLNIVPIIMEFVVQDKMASVSTMAAPGSTVSS
EPSSLQKIEDALRISNYVFFVIYAIEAIVKILGLGRHYIVSHWNKFDAFILVVALVDIIIAETLLKGSITINLSSIKVVK
LFRLLRGLRMLRLTKALIPKLILVVNGKINNQLSLGYDVGKGYIIGEEEVGKIIDRMVDNKKILRELKHISETGRLQVVK
ELGLLQREHPGIAVSVKTRQAIRTILNHSRETIHELQGAGLLDEMEAHKLELTVEIKMKRLMNAPSSIPPPPPENLLKNV
SWLAGDMKLIDFIKARASLLHFDYGEVIVREGDESDGLFLIVSGLVKLYGKSAFLDHDNPPVTAGSEENEVFEDYLTVGN
VIGEMGVLTKKPRNATVTCETTVQVYFITAEDMNIAIDTFTLYPSLEYRLWRVVAIRIATPLIMEQMAFQGWTQEKVKLH
LERGYLVDLAESHFQFNIDATLEDVILINGTAYNAHTREEIRSPCLISRTVHKLTFQYTATEEPRLFVVRNAEYNGPILD
GRLDVDSKRSLISITEISSNMCLKHAAELRQKNSKVMLSRKSSGAAAKEEEDCIPNTSDVEQAAGVSPSVPTKTTPKPKS
FLPSLGLSMSKERVNGEAVEESPVKTKQGEETPETEEGAAPRVNV
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate' POV 
3 Digitonin                                                                                        AJP 
# 
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    LYS n 
1 3    LYS n 
1 4    ARG n 
1 5    VAL n 
1 6    VAL n 
1 7    LYS n 
1 8    LEU n 
1 9    ARG n 
1 10   GLU n 
1 11   LEU n 
1 12   VAL n 
1 13   PRO n 
1 14   ALA n 
1 15   VAL n 
1 16   ALA n 
1 17   ALA n 
1 18   LEU n 
1 19   ALA n 
1 20   VAL n 
1 21   ALA n 
1 22   VAL n 
1 23   LEU n 
1 24   ILE n 
1 25   GLN n 
1 26   SER n 
1 27   ALA n 
1 28   THR n 
1 29   GLY n 
1 30   SER n 
1 31   SER n 
1 32   GLY n 
1 33   GLY n 
1 34   SER n 
1 35   GLY n 
1 36   HIS n 
1 37   THR n 
1 38   PRO n 
1 39   THR n 
1 40   THR n 
1 41   GLN n 
1 42   ALA n 
1 43   THR n 
1 44   HIS n 
1 45   ALA n 
1 46   ASP n 
1 47   ASP n 
1 48   HIS n 
1 49   ASP n 
1 50   LEU n 
1 51   THR n 
1 52   THR n 
1 53   HIS n 
1 54   ASN n 
1 55   GLY n 
1 56   THR n 
1 57   GLU n 
1 58   GLU n 
1 59   HIS n 
1 60   ASP n 
1 61   ASP n 
1 62   GLY n 
1 63   HIS n 
1 64   ASP n 
1 65   ASP n 
1 66   GLY n 
1 67   HIS n 
1 68   ASP n 
1 69   ASP n 
1 70   LEU n 
1 71   HIS n 
1 72   ALA n 
1 73   HIS n 
1 74   ALA n 
1 75   PRO n 
1 76   LYS n 
1 77   VAL n 
1 78   ILE n 
1 79   VAL n 
1 80   PHE n 
1 81   ILE n 
1 82   SER n 
1 83   GLY n 
1 84   SER n 
1 85   CYS n 
1 86   LEU n 
1 87   PHE n 
1 88   GLY n 
1 89   ALA n 
1 90   ILE n 
1 91   SER n 
1 92   ARG n 
1 93   SER n 
1 94   LEU n 
1 95   PHE n 
1 96   LYS n 
1 97   LYS n 
1 98   LEU n 
1 99   PRO n 
1 100  ILE n 
1 101  PRO n 
1 102  TYR n 
1 103  THR n 
1 104  VAL n 
1 105  VAL n 
1 106  LEU n 
1 107  LEU n 
1 108  ILE n 
1 109  LEU n 
1 110  GLY n 
1 111  ALA n 
1 112  ILE n 
1 113  LEU n 
1 114  GLY n 
1 115  VAL n 
1 116  VAL n 
1 117  ALA n 
1 118  SER n 
1 119  ASN n 
1 120  VAL n 
1 121  PRO n 
1 122  LEU n 
1 123  VAL n 
1 124  GLU n 
1 125  GLU n 
1 126  HIS n 
1 127  THR n 
1 128  ARG n 
1 129  ASP n 
1 130  VAL n 
1 131  ALA n 
1 132  HIS n 
1 133  MET n 
1 134  ASP n 
1 135  PRO n 
1 136  HIS n 
1 137  VAL n 
1 138  LEU n 
1 139  LEU n 
1 140  GLN n 
1 141  ILE n 
1 142  PHE n 
1 143  LEU n 
1 144  PRO n 
1 145  VAL n 
1 146  LEU n 
1 147  ILE n 
1 148  PHE n 
1 149  GLU n 
1 150  SER n 
1 151  ALA n 
1 152  PHE n 
1 153  ALA n 
1 154  MET n 
1 155  ASP n 
1 156  VAL n 
1 157  HIS n 
1 158  THR n 
1 159  PHE n 
1 160  MET n 
1 161  ARG n 
1 162  SER n 
1 163  PHE n 
1 164  SER n 
1 165  GLN n 
1 166  VAL n 
1 167  CYS n 
1 168  ILE n 
1 169  LEU n 
1 170  ALA n 
1 171  LEU n 
1 172  PHE n 
1 173  GLY n 
1 174  LEU n 
1 175  VAL n 
1 176  VAL n 
1 177  ALA n 
1 178  SER n 
1 179  VAL n 
1 180  LEU n 
1 181  THR n 
1 182  ALA n 
1 183  VAL n 
1 184  LEU n 
1 185  ALA n 
1 186  MET n 
1 187  ASN n 
1 188  LEU n 
1 189  PHE n 
1 190  ASN n 
1 191  TYR n 
1 192  ASN n 
1 193  TRP n 
1 194  ASN n 
1 195  PHE n 
1 196  SER n 
1 197  GLU n 
1 198  ALA n 
1 199  MET n 
1 200  MET n 
1 201  PHE n 
1 202  GLY n 
1 203  ALA n 
1 204  ILE n 
1 205  MET n 
1 206  SER n 
1 207  ALA n 
1 208  THR n 
1 209  ASP n 
1 210  PRO n 
1 211  VAL n 
1 212  ALA n 
1 213  VAL n 
1 214  VAL n 
1 215  ALA n 
1 216  LEU n 
1 217  LEU n 
1 218  LYS n 
1 219  ASP n 
1 220  LEU n 
1 221  GLY n 
1 222  ALA n 
1 223  SER n 
1 224  LYS n 
1 225  GLN n 
1 226  LEU n 
1 227  GLY n 
1 228  THR n 
1 229  ILE n 
1 230  ILE n 
1 231  GLU n 
1 232  GLY n 
1 233  GLU n 
1 234  SER n 
1 235  LEU n 
1 236  LEU n 
1 237  ASN n 
1 238  ASP n 
1 239  GLY n 
1 240  CYS n 
1 241  ALA n 
1 242  ILE n 
1 243  VAL n 
1 244  ILE n 
1 245  PHE n 
1 246  ASN n 
1 247  VAL n 
1 248  PHE n 
1 249  MET n 
1 250  LYS n 
1 251  MET n 
1 252  VAL n 
1 253  PHE n 
1 254  PHE n 
1 255  PRO n 
1 256  GLN n 
1 257  LEU n 
1 258  THR n 
1 259  SER n 
1 260  THR n 
1 261  VAL n 
1 262  GLY n 
1 263  GLN n 
1 264  ASN n 
1 265  VAL n 
1 266  LEU n 
1 267  TYR n 
1 268  PHE n 
1 269  LEU n 
1 270  GLN n 
1 271  VAL n 
1 272  ALA n 
1 273  VAL n 
1 274  ALA n 
1 275  GLY n 
1 276  PRO n 
1 277  LEU n 
1 278  TRP n 
1 279  GLY n 
1 280  TYR n 
1 281  ALA n 
1 282  VAL n 
1 283  ALA n 
1 284  LYS n 
1 285  VAL n 
1 286  THR n 
1 287  VAL n 
1 288  PHE n 
1 289  PHE n 
1 290  LEU n 
1 291  SER n 
1 292  HIS n 
1 293  ILE n 
1 294  PHE n 
1 295  ASN n 
1 296  ASP n 
1 297  ALA n 
1 298  LEU n 
1 299  VAL n 
1 300  GLU n 
1 301  ILE n 
1 302  THR n 
1 303  ILE n 
1 304  THR n 
1 305  LEU n 
1 306  ALA n 
1 307  ALA n 
1 308  THR n 
1 309  TYR n 
1 310  LEU n 
1 311  THR n 
1 312  TYR n 
1 313  TYR n 
1 314  ILE n 
1 315  GLY n 
1 316  ASP n 
1 317  ILE n 
1 318  TRP n 
1 319  LEU n 
1 320  GLU n 
1 321  VAL n 
1 322  SER n 
1 323  GLY n 
1 324  VAL n 
1 325  LEU n 
1 326  ALA n 
1 327  VAL n 
1 328  VAL n 
1 329  VAL n 
1 330  LEU n 
1 331  GLY n 
1 332  LEU n 
1 333  ILE n 
1 334  VAL n 
1 335  ASN n 
1 336  ALA n 
1 337  GLU n 
1 338  LYS n 
1 339  THR n 
1 340  SER n 
1 341  ILE n 
1 342  SER n 
1 343  PRO n 
1 344  GLU n 
1 345  VAL n 
1 346  GLU n 
1 347  VAL n 
1 348  PHE n 
1 349  LEU n 
1 350  HIS n 
1 351  ARG n 
1 352  PHE n 
1 353  TRP n 
1 354  GLU n 
1 355  MET n 
1 356  LEU n 
1 357  ALA n 
1 358  TYR n 
1 359  LEU n 
1 360  ALA n 
1 361  ASN n 
1 362  THR n 
1 363  LEU n 
1 364  ILE n 
1 365  PHE n 
1 366  MET n 
1 367  MET n 
1 368  VAL n 
1 369  GLY n 
1 370  VAL n 
1 371  VAL n 
1 372  VAL n 
1 373  THR n 
1 374  GLN n 
1 375  LYS n 
1 376  ALA n 
1 377  LEU n 
1 378  VAL n 
1 379  ALA n 
1 380  VAL n 
1 381  ASP n 
1 382  LYS n 
1 383  MET n 
1 384  ASP n 
1 385  TRP n 
1 386  PHE n 
1 387  TYR n 
1 388  LEU n 
1 389  ILE n 
1 390  ILE n 
1 391  LEU n 
1 392  TYR n 
1 393  LEU n 
1 394  ALA n 
1 395  ILE n 
1 396  THR n 
1 397  ILE n 
1 398  ILE n 
1 399  ALA n 
1 400  GLY n 
1 401  MET n 
1 402  VAL n 
1 403  ILE n 
1 404  SER n 
1 405  LEU n 
1 406  PHE n 
1 407  SER n 
1 408  PRO n 
1 409  ILE n 
1 410  LEU n 
1 411  SER n 
1 412  ARG n 
1 413  ILE n 
1 414  GLY n 
1 415  TYR n 
1 416  GLY n 
1 417  LEU n 
1 418  THR n 
1 419  TRP n 
1 420  ARG n 
1 421  ASN n 
1 422  ALA n 
1 423  VAL n 
1 424  ILE n 
1 425  MET n 
1 426  THR n 
1 427  TRP n 
1 428  GLY n 
1 429  GLY n 
1 430  LEU n 
1 431  ARG n 
1 432  GLY n 
1 433  ALA n 
1 434  VAL n 
1 435  GLY n 
1 436  LEU n 
1 437  ALA n 
1 438  LEU n 
1 439  ALA n 
1 440  LEU n 
1 441  VAL n 
1 442  VAL n 
1 443  GLU n 
1 444  ASN n 
1 445  LEU n 
1 446  ALA n 
1 447  GLY n 
1 448  ASN n 
1 449  ASP n 
1 450  VAL n 
1 451  ILE n 
1 452  GLY n 
1 453  SER n 
1 454  LYS n 
1 455  PHE n 
1 456  LEU n 
1 457  PHE n 
1 458  HIS n 
1 459  THR n 
1 460  ALA n 
1 461  GLY n 
1 462  ILE n 
1 463  VAL n 
1 464  VAL n 
1 465  LEU n 
1 466  THR n 
1 467  LEU n 
1 468  VAL n 
1 469  ILE n 
1 470  ASN n 
1 471  ALA n 
1 472  THR n 
1 473  THR n 
1 474  ILE n 
1 475  GLN n 
1 476  THR n 
1 477  LEU n 
1 478  LEU n 
1 479  ARG n 
1 480  ILE n 
1 481  LEU n 
1 482  GLY n 
1 483  MET n 
1 484  SER n 
1 485  ASP n 
1 486  ILE n 
1 487  SER n 
1 488  ILE n 
1 489  PRO n 
1 490  LYS n 
1 491  ARG n 
1 492  LEU n 
1 493  ALA n 
1 494  MET n 
1 495  ALA n 
1 496  GLY n 
1 497  ALA n 
1 498  VAL n 
1 499  ARG n 
1 500  ARG n 
1 501  ILE n 
1 502  HIS n 
1 503  GLU n 
1 504  GLY n 
1 505  GLN n 
1 506  ASN n 
1 507  ARG n 
1 508  THR n 
1 509  LEU n 
1 510  ASN n 
1 511  MET n 
1 512  LEU n 
1 513  LYS n 
1 514  SER n 
1 515  ASP n 
1 516  ARG n 
1 517  PHE n 
1 518  LEU n 
1 519  ALA n 
1 520  ASP n 
1 521  ALA n 
1 522  ASP n 
1 523  TRP n 
1 524  ASP n 
1 525  ILE n 
1 526  ALA n 
1 527  THR n 
1 528  ALA n 
1 529  ALA n 
1 530  CYS n 
1 531  GLU n 
1 532  ILE n 
1 533  SER n 
1 534  ASP n 
1 535  PRO n 
1 536  TYR n 
1 537  SER n 
1 538  ALA n 
1 539  LEU n 
1 540  SER n 
1 541  ASP n 
1 542  ASP n 
1 543  GLU n 
1 544  ASN n 
1 545  ALA n 
1 546  PRO n 
1 547  ALA n 
1 548  ASP n 
1 549  GLU n 
1 550  LEU n 
1 551  THR n 
1 552  LEU n 
1 553  GLY n 
1 554  GLU n 
1 555  ARG n 
1 556  LYS n 
1 557  SER n 
1 558  VAL n 
1 559  CYS n 
1 560  PRO n 
1 561  GLY n 
1 562  CYS n 
1 563  LYS n 
1 564  ALA n 
1 565  MET n 
1 566  VAL n 
1 567  PRO n 
1 568  ASN n 
1 569  GLU n 
1 570  PRO n 
1 571  SER n 
1 572  PRO n 
1 573  ARG n 
1 574  GLU n 
1 575  PHE n 
1 576  ALA n 
1 577  ASP n 
1 578  MET n 
1 579  MET n 
1 580  GLU n 
1 581  GLU n 
1 582  ALA n 
1 583  ARG n 
1 584  LEU n 
1 585  ARG n 
1 586  MET n 
1 587  LEU n 
1 588  LYS n 
1 589  ALA n 
1 590  GLU n 
1 591  LYS n 
1 592  ILE n 
1 593  SER n 
1 594  TYR n 
1 595  TRP n 
1 596  LYS n 
1 597  GLN n 
1 598  PHE n 
1 599  GLU n 
1 600  HIS n 
1 601  GLY n 
1 602  MET n 
1 603  LEU n 
1 604  ALA n 
1 605  ARG n 
1 606  GLU n 
1 607  ALA n 
1 608  LEU n 
1 609  ARG n 
1 610  LEU n 
1 611  LEU n 
1 612  VAL n 
1 613  GLN n 
1 614  HIS n 
1 615  ALA n 
1 616  GLU n 
1 617  VAL n 
1 618  ALA n 
1 619  ALA n 
1 620  ASP n 
1 621  GLU n 
1 622  LYS n 
1 623  ASP n 
1 624  GLN n 
1 625  PHE n 
1 626  ILE n 
1 627  LEU n 
1 628  VAL n 
1 629  ASP n 
1 630  ASP n 
1 631  LEU n 
1 632  LYS n 
1 633  LYS n 
1 634  SER n 
1 635  TRP n 
1 636  GLN n 
1 637  ILE n 
1 638  LYS n 
1 639  GLY n 
1 640  ILE n 
1 641  TYR n 
1 642  PRO n 
1 643  TRP n 
1 644  LEU n 
1 645  LYS n 
1 646  ARG n 
1 647  LYS n 
1 648  LEU n 
1 649  GLU n 
1 650  ASP n 
1 651  LEU n 
1 652  ILE n 
1 653  SER n 
1 654  GLU n 
1 655  LYS n 
1 656  LYS n 
1 657  ILE n 
1 658  ALA n 
1 659  ALA n 
1 660  ILE n 
1 661  PRO n 
1 662  MET n 
1 663  PRO n 
1 664  LYS n 
1 665  TYR n 
1 666  LYS n 
1 667  LEU n 
1 668  GLY n 
1 669  LYS n 
1 670  LEU n 
1 671  MET n 
1 672  TYR n 
1 673  LYS n 
1 674  ILE n 
1 675  CYS n 
1 676  HIS n 
1 677  HIS n 
1 678  MET n 
1 679  ALA n 
1 680  PHE n 
1 681  GLU n 
1 682  VAL n 
1 683  THR n 
1 684  ILE n 
1 685  ASN n 
1 686  ILE n 
1 687  ALA n 
1 688  ILE n 
1 689  VAL n 
1 690  LEU n 
1 691  ASN n 
1 692  ILE n 
1 693  VAL n 
1 694  PRO n 
1 695  ILE n 
1 696  ILE n 
1 697  MET n 
1 698  GLU n 
1 699  PHE n 
1 700  VAL n 
1 701  VAL n 
1 702  GLN n 
1 703  ASP n 
1 704  LYS n 
1 705  MET n 
1 706  ALA n 
1 707  SER n 
1 708  VAL n 
1 709  SER n 
1 710  THR n 
1 711  MET n 
1 712  ALA n 
1 713  ALA n 
1 714  PRO n 
1 715  GLY n 
1 716  SER n 
1 717  THR n 
1 718  VAL n 
1 719  SER n 
1 720  SER n 
1 721  GLU n 
1 722  PRO n 
1 723  SER n 
1 724  SER n 
1 725  LEU n 
1 726  GLN n 
1 727  LYS n 
1 728  ILE n 
1 729  GLU n 
1 730  ASP n 
1 731  ALA n 
1 732  LEU n 
1 733  ARG n 
1 734  ILE n 
1 735  SER n 
1 736  ASN n 
1 737  TYR n 
1 738  VAL n 
1 739  PHE n 
1 740  PHE n 
1 741  VAL n 
1 742  ILE n 
1 743  TYR n 
1 744  ALA n 
1 745  ILE n 
1 746  GLU n 
1 747  ALA n 
1 748  ILE n 
1 749  VAL n 
1 750  LYS n 
1 751  ILE n 
1 752  LEU n 
1 753  GLY n 
1 754  LEU n 
1 755  GLY n 
1 756  ARG n 
1 757  HIS n 
1 758  TYR n 
1 759  ILE n 
1 760  VAL n 
1 761  SER n 
1 762  HIS n 
1 763  TRP n 
1 764  ASN n 
1 765  LYS n 
1 766  PHE n 
1 767  ASP n 
1 768  ALA n 
1 769  PHE n 
1 770  ILE n 
1 771  LEU n 
1 772  VAL n 
1 773  VAL n 
1 774  ALA n 
1 775  LEU n 
1 776  VAL n 
1 777  ASP n 
1 778  ILE n 
1 779  ILE n 
1 780  ILE n 
1 781  ALA n 
1 782  GLU n 
1 783  THR n 
1 784  LEU n 
1 785  LEU n 
1 786  LYS n 
1 787  GLY n 
1 788  SER n 
1 789  ILE n 
1 790  THR n 
1 791  ILE n 
1 792  ASN n 
1 793  LEU n 
1 794  SER n 
1 795  SER n 
1 796  ILE n 
1 797  LYS n 
1 798  VAL n 
1 799  VAL n 
1 800  LYS n 
1 801  LEU n 
1 802  PHE n 
1 803  ARG n 
1 804  LEU n 
1 805  LEU n 
1 806  ARG n 
1 807  GLY n 
1 808  LEU n 
1 809  ARG n 
1 810  MET n 
1 811  LEU n 
1 812  ARG n 
1 813  LEU n 
1 814  THR n 
1 815  LYS n 
1 816  ALA n 
1 817  LEU n 
1 818  ILE n 
1 819  PRO n 
1 820  LYS n 
1 821  LEU n 
1 822  ILE n 
1 823  LEU n 
1 824  VAL n 
1 825  VAL n 
1 826  ASN n 
1 827  GLY n 
1 828  LYS n 
1 829  ILE n 
1 830  ASN n 
1 831  ASN n 
1 832  GLN n 
1 833  LEU n 
1 834  SER n 
1 835  LEU n 
1 836  GLY n 
1 837  TYR n 
1 838  ASP n 
1 839  VAL n 
1 840  GLY n 
1 841  LYS n 
1 842  GLY n 
1 843  TYR n 
1 844  ILE n 
1 845  ILE n 
1 846  GLY n 
1 847  GLU n 
1 848  GLU n 
1 849  GLU n 
1 850  VAL n 
1 851  GLY n 
1 852  LYS n 
1 853  ILE n 
1 854  ILE n 
1 855  ASP n 
1 856  ARG n 
1 857  MET n 
1 858  VAL n 
1 859  ASP n 
1 860  ASN n 
1 861  LYS n 
1 862  LYS n 
1 863  ILE n 
1 864  LEU n 
1 865  ARG n 
1 866  GLU n 
1 867  LEU n 
1 868  LYS n 
1 869  HIS n 
1 870  ILE n 
1 871  SER n 
1 872  GLU n 
1 873  THR n 
1 874  GLY n 
1 875  ARG n 
1 876  LEU n 
1 877  GLN n 
1 878  VAL n 
1 879  VAL n 
1 880  LYS n 
1 881  GLU n 
1 882  LEU n 
1 883  GLY n 
1 884  LEU n 
1 885  LEU n 
1 886  GLN n 
1 887  ARG n 
1 888  GLU n 
1 889  HIS n 
1 890  PRO n 
1 891  GLY n 
1 892  ILE n 
1 893  ALA n 
1 894  VAL n 
1 895  SER n 
1 896  VAL n 
1 897  LYS n 
1 898  THR n 
1 899  ARG n 
1 900  GLN n 
1 901  ALA n 
1 902  ILE n 
1 903  ARG n 
1 904  THR n 
1 905  ILE n 
1 906  LEU n 
1 907  ASN n 
1 908  HIS n 
1 909  SER n 
1 910  ARG n 
1 911  GLU n 
1 912  THR n 
1 913  ILE n 
1 914  HIS n 
1 915  GLU n 
1 916  LEU n 
1 917  GLN n 
1 918  GLY n 
1 919  ALA n 
1 920  GLY n 
1 921  LEU n 
1 922  LEU n 
1 923  ASP n 
1 924  GLU n 
1 925  MET n 
1 926  GLU n 
1 927  ALA n 
1 928  HIS n 
1 929  LYS n 
1 930  LEU n 
1 931  GLU n 
1 932  LEU n 
1 933  THR n 
1 934  VAL n 
1 935  GLU n 
1 936  ILE n 
1 937  LYS n 
1 938  MET n 
1 939  LYS n 
1 940  ARG n 
1 941  LEU n 
1 942  MET n 
1 943  ASN n 
1 944  ALA n 
1 945  PRO n 
1 946  SER n 
1 947  SER n 
1 948  ILE n 
1 949  PRO n 
1 950  PRO n 
1 951  PRO n 
1 952  PRO n 
1 953  PRO n 
1 954  GLU n 
1 955  ASN n 
1 956  LEU n 
1 957  LEU n 
1 958  LYS n 
1 959  ASN n 
1 960  VAL n 
1 961  SER n 
1 962  TRP n 
1 963  LEU n 
1 964  ALA n 
1 965  GLY n 
1 966  ASP n 
1 967  MET n 
1 968  LYS n 
1 969  LEU n 
1 970  ILE n 
1 971  ASP n 
1 972  PHE n 
1 973  ILE n 
1 974  LYS n 
1 975  ALA n 
1 976  ARG n 
1 977  ALA n 
1 978  SER n 
1 979  LEU n 
1 980  LEU n 
1 981  HIS n 
1 982  PHE n 
1 983  ASP n 
1 984  TYR n 
1 985  GLY n 
1 986  GLU n 
1 987  VAL n 
1 988  ILE n 
1 989  VAL n 
1 990  ARG n 
1 991  GLU n 
1 992  GLY n 
1 993  ASP n 
1 994  GLU n 
1 995  SER n 
1 996  ASP n 
1 997  GLY n 
1 998  LEU n 
1 999  PHE n 
1 1000 LEU n 
1 1001 ILE n 
1 1002 VAL n 
1 1003 SER n 
1 1004 GLY n 
1 1005 LEU n 
1 1006 VAL n 
1 1007 LYS n 
1 1008 LEU n 
1 1009 TYR n 
1 1010 GLY n 
1 1011 LYS n 
1 1012 SER n 
1 1013 ALA n 
1 1014 PHE n 
1 1015 LEU n 
1 1016 ASP n 
1 1017 HIS n 
1 1018 ASP n 
1 1019 ASN n 
1 1020 PRO n 
1 1021 PRO n 
1 1022 VAL n 
1 1023 THR n 
1 1024 ALA n 
1 1025 GLY n 
1 1026 SER n 
1 1027 GLU n 
1 1028 GLU n 
1 1029 ASN n 
1 1030 GLU n 
1 1031 VAL n 
1 1032 PHE n 
1 1033 GLU n 
1 1034 ASP n 
1 1035 TYR n 
1 1036 LEU n 
1 1037 THR n 
1 1038 VAL n 
1 1039 GLY n 
1 1040 ASN n 
1 1041 VAL n 
1 1042 ILE n 
1 1043 GLY n 
1 1044 GLU n 
1 1045 MET n 
1 1046 GLY n 
1 1047 VAL n 
1 1048 LEU n 
1 1049 THR n 
1 1050 LYS n 
1 1051 LYS n 
1 1052 PRO n 
1 1053 ARG n 
1 1054 ASN n 
1 1055 ALA n 
1 1056 THR n 
1 1057 VAL n 
1 1058 THR n 
1 1059 CYS n 
1 1060 GLU n 
1 1061 THR n 
1 1062 THR n 
1 1063 VAL n 
1 1064 GLN n 
1 1065 VAL n 
1 1066 TYR n 
1 1067 PHE n 
1 1068 ILE n 
1 1069 THR n 
1 1070 ALA n 
1 1071 GLU n 
1 1072 ASP n 
1 1073 MET n 
1 1074 ASN n 
1 1075 ILE n 
1 1076 ALA n 
1 1077 ILE n 
1 1078 ASP n 
1 1079 THR n 
1 1080 PHE n 
1 1081 THR n 
1 1082 LEU n 
1 1083 TYR n 
1 1084 PRO n 
1 1085 SER n 
1 1086 LEU n 
1 1087 GLU n 
1 1088 TYR n 
1 1089 ARG n 
1 1090 LEU n 
1 1091 TRP n 
1 1092 ARG n 
1 1093 VAL n 
1 1094 VAL n 
1 1095 ALA n 
1 1096 ILE n 
1 1097 ARG n 
1 1098 ILE n 
1 1099 ALA n 
1 1100 THR n 
1 1101 PRO n 
1 1102 LEU n 
1 1103 ILE n 
1 1104 MET n 
1 1105 GLU n 
1 1106 GLN n 
1 1107 MET n 
1 1108 ALA n 
1 1109 PHE n 
1 1110 GLN n 
1 1111 GLY n 
1 1112 TRP n 
1 1113 THR n 
1 1114 GLN n 
1 1115 GLU n 
1 1116 LYS n 
1 1117 VAL n 
1 1118 LYS n 
1 1119 LEU n 
1 1120 HIS n 
1 1121 LEU n 
1 1122 GLU n 
1 1123 ARG n 
1 1124 GLY n 
1 1125 TYR n 
1 1126 LEU n 
1 1127 VAL n 
1 1128 ASP n 
1 1129 LEU n 
1 1130 ALA n 
1 1131 GLU n 
1 1132 SER n 
1 1133 HIS n 
1 1134 PHE n 
1 1135 GLN n 
1 1136 PHE n 
1 1137 ASN n 
1 1138 ILE n 
1 1139 ASP n 
1 1140 ALA n 
1 1141 THR n 
1 1142 LEU n 
1 1143 GLU n 
1 1144 ASP n 
1 1145 VAL n 
1 1146 ILE n 
1 1147 LEU n 
1 1148 ILE n 
1 1149 ASN n 
1 1150 GLY n 
1 1151 THR n 
1 1152 ALA n 
1 1153 TYR n 
1 1154 ASN n 
1 1155 ALA n 
1 1156 HIS n 
1 1157 THR n 
1 1158 ARG n 
1 1159 GLU n 
1 1160 GLU n 
1 1161 ILE n 
1 1162 ARG n 
1 1163 SER n 
1 1164 PRO n 
1 1165 CYS n 
1 1166 LEU n 
1 1167 ILE n 
1 1168 SER n 
1 1169 ARG n 
1 1170 THR n 
1 1171 VAL n 
1 1172 HIS n 
1 1173 LYS n 
1 1174 LEU n 
1 1175 THR n 
1 1176 PHE n 
1 1177 GLN n 
1 1178 TYR n 
1 1179 THR n 
1 1180 ALA n 
1 1181 THR n 
1 1182 GLU n 
1 1183 GLU n 
1 1184 PRO n 
1 1185 ARG n 
1 1186 LEU n 
1 1187 PHE n 
1 1188 VAL n 
1 1189 VAL n 
1 1190 ARG n 
1 1191 ASN n 
1 1192 ALA n 
1 1193 GLU n 
1 1194 TYR n 
1 1195 ASN n 
1 1196 GLY n 
1 1197 PRO n 
1 1198 ILE n 
1 1199 LEU n 
1 1200 ASP n 
1 1201 GLY n 
1 1202 ARG n 
1 1203 LEU n 
1 1204 ASP n 
1 1205 VAL n 
1 1206 ASP n 
1 1207 SER n 
1 1208 LYS n 
1 1209 ARG n 
1 1210 SER n 
1 1211 LEU n 
1 1212 ILE n 
1 1213 SER n 
1 1214 ILE n 
1 1215 THR n 
1 1216 GLU n 
1 1217 ILE n 
1 1218 SER n 
1 1219 SER n 
1 1220 ASN n 
1 1221 MET n 
1 1222 CYS n 
1 1223 LEU n 
1 1224 LYS n 
1 1225 HIS n 
1 1226 ALA n 
1 1227 ALA n 
1 1228 GLU n 
1 1229 LEU n 
1 1230 ARG n 
1 1231 GLN n 
1 1232 LYS n 
1 1233 ASN n 
1 1234 SER n 
1 1235 LYS n 
1 1236 VAL n 
1 1237 MET n 
1 1238 LEU n 
1 1239 SER n 
1 1240 ARG n 
1 1241 LYS n 
1 1242 SER n 
1 1243 SER n 
1 1244 GLY n 
1 1245 ALA n 
1 1246 ALA n 
1 1247 ALA n 
1 1248 LYS n 
1 1249 GLU n 
1 1250 GLU n 
1 1251 GLU n 
1 1252 ASP n 
1 1253 CYS n 
1 1254 ILE n 
1 1255 PRO n 
1 1256 ASN n 
1 1257 THR n 
1 1258 SER n 
1 1259 ASP n 
1 1260 VAL n 
1 1261 GLU n 
1 1262 GLN n 
1 1263 ALA n 
1 1264 ALA n 
1 1265 GLY n 
1 1266 VAL n 
1 1267 SER n 
1 1268 PRO n 
1 1269 SER n 
1 1270 VAL n 
1 1271 PRO n 
1 1272 THR n 
1 1273 LYS n 
1 1274 THR n 
1 1275 THR n 
1 1276 PRO n 
1 1277 LYS n 
1 1278 PRO n 
1 1279 LYS n 
1 1280 SER n 
1 1281 PHE n 
1 1282 LEU n 
1 1283 PRO n 
1 1284 SER n 
1 1285 LEU n 
1 1286 GLY n 
1 1287 LEU n 
1 1288 SER n 
1 1289 MET n 
1 1290 SER n 
1 1291 LYS n 
1 1292 GLU n 
1 1293 ARG n 
1 1294 VAL n 
1 1295 ASN n 
1 1296 GLY n 
1 1297 GLU n 
1 1298 ALA n 
1 1299 VAL n 
1 1300 GLU n 
1 1301 GLU n 
1 1302 SER n 
1 1303 PRO n 
1 1304 VAL n 
1 1305 LYS n 
1 1306 THR n 
1 1307 LYS n 
1 1308 GLN n 
1 1309 GLY n 
1 1310 GLU n 
1 1311 GLU n 
1 1312 THR n 
1 1313 PRO n 
1 1314 GLU n 
1 1315 THR n 
1 1316 GLU n 
1 1317 GLU n 
1 1318 GLY n 
1 1319 ALA n 
1 1320 ALA n 
1 1321 PRO n 
1 1322 ARG n 
1 1323 VAL n 
1 1324 ASN n 
1 1325 VAL 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                   1325 
_entity_src_gen.gene_src_common_name               'purple sea urchin' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Strongylocentrotus purpuratus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     7668 
_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               human 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_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            HEK293F 
_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 
AJP non-polymer         . Digitonin                                                                                        ?    
'C56 H92 O29'    1229.312 
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  
POV non-polymer         . '(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate' POPC 
'C42 H82 N O8 P' 760.076  
PRO 'L-peptide linking' y PROLINE                                                                                          ?    
'C5 H9 N O2'     115.130  
SER 'L-peptide linking' y SERINE                                                                                           ?    
'C3 H7 N O3'     105.093  
THR 'L-peptide linking' y THREONINE                                                                                        ?    
'C4 H9 N O3'     119.119  
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                       ?    
'C11 H12 N2 O2'  204.225  
TYR 'L-peptide linking' y TYROSINE                                                                                         ?    
'C9 H11 N O3'    181.189  
VAL 'L-peptide linking' y VALINE                                                                                           ?    
'C5 H11 N O2'    117.146  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?    ?   ?   A . n 
A 1 2    LYS 2    2    ?    ?   ?   A . n 
A 1 3    LYS 3    3    ?    ?   ?   A . n 
A 1 4    ARG 4    4    ?    ?   ?   A . n 
A 1 5    VAL 5    5    ?    ?   ?   A . n 
A 1 6    VAL 6    6    ?    ?   ?   A . n 
A 1 7    LYS 7    7    ?    ?   ?   A . n 
A 1 8    LEU 8    8    ?    ?   ?   A . n 
A 1 9    ARG 9    9    ?    ?   ?   A . n 
A 1 10   GLU 10   10   ?    ?   ?   A . n 
A 1 11   LEU 11   11   ?    ?   ?   A . n 
A 1 12   VAL 12   12   ?    ?   ?   A . n 
A 1 13   PRO 13   13   ?    ?   ?   A . n 
A 1 14   ALA 14   14   ?    ?   ?   A . n 
A 1 15   VAL 15   15   ?    ?   ?   A . n 
A 1 16   ALA 16   16   ?    ?   ?   A . n 
A 1 17   ALA 17   17   ?    ?   ?   A . n 
A 1 18   LEU 18   18   ?    ?   ?   A . n 
A 1 19   ALA 19   19   ?    ?   ?   A . n 
A 1 20   VAL 20   20   ?    ?   ?   A . n 
A 1 21   ALA 21   21   ?    ?   ?   A . n 
A 1 22   VAL 22   22   ?    ?   ?   A . n 
A 1 23   LEU 23   23   ?    ?   ?   A . n 
A 1 24   ILE 24   24   ?    ?   ?   A . n 
A 1 25   GLN 25   25   ?    ?   ?   A . n 
A 1 26   SER 26   26   ?    ?   ?   A . n 
A 1 27   ALA 27   27   ?    ?   ?   A . n 
A 1 28   THR 28   28   ?    ?   ?   A . n 
A 1 29   GLY 29   29   ?    ?   ?   A . n 
A 1 30   SER 30   30   ?    ?   ?   A . n 
A 1 31   SER 31   31   ?    ?   ?   A . n 
A 1 32   GLY 32   32   ?    ?   ?   A . n 
A 1 33   GLY 33   33   ?    ?   ?   A . n 
A 1 34   SER 34   34   ?    ?   ?   A . n 
A 1 35   GLY 35   35   ?    ?   ?   A . n 
A 1 36   HIS 36   36   ?    ?   ?   A . n 
A 1 37   THR 37   37   ?    ?   ?   A . n 
A 1 38   PRO 38   38   ?    ?   ?   A . n 
A 1 39   THR 39   39   ?    ?   ?   A . n 
A 1 40   THR 40   40   ?    ?   ?   A . n 
A 1 41   GLN 41   41   ?    ?   ?   A . n 
A 1 42   ALA 42   42   ?    ?   ?   A . n 
A 1 43   THR 43   43   ?    ?   ?   A . n 
A 1 44   HIS 44   44   ?    ?   ?   A . n 
A 1 45   ALA 45   45   ?    ?   ?   A . n 
A 1 46   ASP 46   46   ?    ?   ?   A . n 
A 1 47   ASP 47   47   ?    ?   ?   A . n 
A 1 48   HIS 48   48   ?    ?   ?   A . n 
A 1 49   ASP 49   49   ?    ?   ?   A . n 
A 1 50   LEU 50   50   ?    ?   ?   A . n 
A 1 51   THR 51   51   ?    ?   ?   A . n 
A 1 52   THR 52   52   ?    ?   ?   A . n 
A 1 53   HIS 53   53   ?    ?   ?   A . n 
A 1 54   ASN 54   54   ?    ?   ?   A . n 
A 1 55   GLY 55   55   ?    ?   ?   A . n 
A 1 56   THR 56   56   ?    ?   ?   A . n 
A 1 57   GLU 57   57   ?    ?   ?   A . n 
A 1 58   GLU 58   58   ?    ?   ?   A . n 
A 1 59   HIS 59   59   ?    ?   ?   A . n 
A 1 60   ASP 60   60   ?    ?   ?   A . n 
A 1 61   ASP 61   61   ?    ?   ?   A . n 
A 1 62   GLY 62   62   ?    ?   ?   A . n 
A 1 63   HIS 63   63   ?    ?   ?   A . n 
A 1 64   ASP 64   64   ?    ?   ?   A . n 
A 1 65   ASP 65   65   ?    ?   ?   A . n 
A 1 66   GLY 66   66   ?    ?   ?   A . n 
A 1 67   HIS 67   67   ?    ?   ?   A . n 
A 1 68   ASP 68   68   ?    ?   ?   A . n 
A 1 69   ASP 69   69   ?    ?   ?   A . n 
A 1 70   LEU 70   70   ?    ?   ?   A . n 
A 1 71   HIS 71   71   ?    ?   ?   A . n 
A 1 72   ALA 72   72   ?    ?   ?   A . n 
A 1 73   HIS 73   73   ?    ?   ?   A . n 
A 1 74   ALA 74   74   74   ALA ALA A . n 
A 1 75   PRO 75   75   75   PRO PRO A . n 
A 1 76   LYS 76   76   76   LYS LYS A . n 
A 1 77   VAL 77   77   77   VAL VAL A . n 
A 1 78   ILE 78   78   78   ILE ILE A . n 
A 1 79   VAL 79   79   79   VAL VAL A . n 
A 1 80   PHE 80   80   80   PHE PHE A . n 
A 1 81   ILE 81   81   81   ILE ILE A . n 
A 1 82   SER 82   82   82   SER SER A . n 
A 1 83   GLY 83   83   83   GLY GLY A . n 
A 1 84   SER 84   84   84   SER SER A . n 
A 1 85   CYS 85   85   85   CYS CYS A . n 
A 1 86   LEU 86   86   86   LEU LEU A . n 
A 1 87   PHE 87   87   87   PHE PHE A . n 
A 1 88   GLY 88   88   88   GLY GLY A . n 
A 1 89   ALA 89   89   89   ALA ALA A . n 
A 1 90   ILE 90   90   90   ILE ILE A . n 
A 1 91   SER 91   91   91   SER SER A . n 
A 1 92   ARG 92   92   92   ARG ARG A . n 
A 1 93   SER 93   93   93   SER SER A . n 
A 1 94   LEU 94   94   94   LEU LEU A . n 
A 1 95   PHE 95   95   95   PHE PHE A . n 
A 1 96   LYS 96   96   96   LYS LYS A . n 
A 1 97   LYS 97   97   97   LYS LYS A . n 
A 1 98   LEU 98   98   98   LEU LEU A . n 
A 1 99   PRO 99   99   99   PRO PRO A . n 
A 1 100  ILE 100  100  100  ILE ILE A . n 
A 1 101  PRO 101  101  101  PRO PRO A . n 
A 1 102  TYR 102  102  102  TYR TYR A . n 
A 1 103  THR 103  103  103  THR THR A . n 
A 1 104  VAL 104  104  104  VAL VAL A . n 
A 1 105  VAL 105  105  105  VAL VAL A . n 
A 1 106  LEU 106  106  106  LEU LEU A . n 
A 1 107  LEU 107  107  107  LEU LEU A . n 
A 1 108  ILE 108  108  108  ILE ILE A . n 
A 1 109  LEU 109  109  109  LEU LEU A . n 
A 1 110  GLY 110  110  110  GLY GLY A . n 
A 1 111  ALA 111  111  111  ALA ALA A . n 
A 1 112  ILE 112  112  112  ILE ILE A . n 
A 1 113  LEU 113  113  113  LEU LEU A . n 
A 1 114  GLY 114  114  114  GLY GLY A . n 
A 1 115  VAL 115  115  115  VAL VAL A . n 
A 1 116  VAL 116  116  116  VAL VAL A . n 
A 1 117  ALA 117  117  117  ALA ALA A . n 
A 1 118  SER 118  118  118  SER SER A . n 
A 1 119  ASN 119  119  119  ASN ASN A . n 
A 1 120  VAL 120  120  120  VAL VAL A . n 
A 1 121  PRO 121  121  121  PRO PRO A . n 
A 1 122  LEU 122  122  122  LEU LEU A . n 
A 1 123  VAL 123  123  123  VAL VAL A . n 
A 1 124  GLU 124  124  124  GLU GLU A . n 
A 1 125  GLU 125  125  125  GLU GLU A . n 
A 1 126  HIS 126  126  126  HIS HIS A . n 
A 1 127  THR 127  127  127  THR THR A . n 
A 1 128  ARG 128  128  128  ARG ARG A . n 
A 1 129  ASP 129  129  129  ASP ASP A . n 
A 1 130  VAL 130  130  130  VAL VAL A . n 
A 1 131  ALA 131  131  131  ALA ALA A . n 
A 1 132  HIS 132  132  132  HIS HIS A . n 
A 1 133  MET 133  133  133  MET MET A . n 
A 1 134  ASP 134  134  134  ASP ASP A . n 
A 1 135  PRO 135  135  135  PRO PRO A . n 
A 1 136  HIS 136  136  136  HIS HIS A . n 
A 1 137  VAL 137  137  137  VAL VAL A . n 
A 1 138  LEU 138  138  138  LEU LEU A . n 
A 1 139  LEU 139  139  139  LEU LEU A . n 
A 1 140  GLN 140  140  140  GLN GLN A . n 
A 1 141  ILE 141  141  141  ILE ILE A . n 
A 1 142  PHE 142  142  142  PHE PHE A . n 
A 1 143  LEU 143  143  143  LEU LEU A . n 
A 1 144  PRO 144  144  144  PRO PRO A . n 
A 1 145  VAL 145  145  145  VAL VAL A . n 
A 1 146  LEU 146  146  146  LEU LEU A . n 
A 1 147  ILE 147  147  147  ILE ILE A . n 
A 1 148  PHE 148  148  148  PHE PHE A . n 
A 1 149  GLU 149  149  149  GLU GLU A . n 
A 1 150  SER 150  150  150  SER SER A . n 
A 1 151  ALA 151  151  151  ALA ALA A . n 
A 1 152  PHE 152  152  152  PHE PHE A . n 
A 1 153  ALA 153  153  153  ALA ALA A . n 
A 1 154  MET 154  154  154  MET MET A . n 
A 1 155  ASP 155  155  155  ASP ASP A . n 
A 1 156  VAL 156  156  156  VAL VAL A . n 
A 1 157  HIS 157  157  157  HIS HIS A . n 
A 1 158  THR 158  158  158  THR THR A . n 
A 1 159  PHE 159  159  159  PHE PHE A . n 
A 1 160  MET 160  160  160  MET MET A . n 
A 1 161  ARG 161  161  161  ARG ARG A . n 
A 1 162  SER 162  162  162  SER SER A . n 
A 1 163  PHE 163  163  163  PHE PHE A . n 
A 1 164  SER 164  164  164  SER SER A . n 
A 1 165  GLN 165  165  165  GLN GLN A . n 
A 1 166  VAL 166  166  166  VAL VAL A . n 
A 1 167  CYS 167  167  167  CYS CYS A . n 
A 1 168  ILE 168  168  168  ILE ILE A . n 
A 1 169  LEU 169  169  169  LEU LEU A . n 
A 1 170  ALA 170  170  170  ALA ALA A . n 
A 1 171  LEU 171  171  171  LEU LEU A . n 
A 1 172  PHE 172  172  172  PHE PHE A . n 
A 1 173  GLY 173  173  173  GLY GLY A . n 
A 1 174  LEU 174  174  174  LEU LEU A . n 
A 1 175  VAL 175  175  175  VAL VAL A . n 
A 1 176  VAL 176  176  176  VAL VAL A . n 
A 1 177  ALA 177  177  177  ALA ALA A . n 
A 1 178  SER 178  178  178  SER SER A . n 
A 1 179  VAL 179  179  179  VAL VAL A . n 
A 1 180  LEU 180  180  180  LEU LEU A . n 
A 1 181  THR 181  181  181  THR THR A . n 
A 1 182  ALA 182  182  182  ALA ALA A . n 
A 1 183  VAL 183  183  183  VAL VAL A . n 
A 1 184  LEU 184  184  184  LEU LEU A . n 
A 1 185  ALA 185  185  185  ALA ALA A . n 
A 1 186  MET 186  186  186  MET MET A . n 
A 1 187  ASN 187  187  187  ASN ASN A . n 
A 1 188  LEU 188  188  188  LEU LEU A . n 
A 1 189  PHE 189  189  189  PHE PHE A . n 
A 1 190  ASN 190  190  190  ASN ASN A . n 
A 1 191  TYR 191  191  191  TYR TYR A . n 
A 1 192  ASN 192  192  192  ASN ASN A . n 
A 1 193  TRP 193  193  193  TRP TRP A . n 
A 1 194  ASN 194  194  194  ASN ASN A . n 
A 1 195  PHE 195  195  195  PHE PHE A . n 
A 1 196  SER 196  196  196  SER SER A . n 
A 1 197  GLU 197  197  197  GLU GLU A . n 
A 1 198  ALA 198  198  198  ALA ALA A . n 
A 1 199  MET 199  199  199  MET MET A . n 
A 1 200  MET 200  200  200  MET MET A . n 
A 1 201  PHE 201  201  201  PHE PHE A . n 
A 1 202  GLY 202  202  202  GLY GLY A . n 
A 1 203  ALA 203  203  203  ALA ALA A . n 
A 1 204  ILE 204  204  204  ILE ILE A . n 
A 1 205  MET 205  205  205  MET MET A . n 
A 1 206  SER 206  206  206  SER SER A . n 
A 1 207  ALA 207  207  207  ALA ALA A . n 
A 1 208  THR 208  208  208  THR THR A . n 
A 1 209  ASP 209  209  209  ASP ASP A . n 
A 1 210  PRO 210  210  210  PRO PRO A . n 
A 1 211  VAL 211  211  211  VAL VAL A . n 
A 1 212  ALA 212  212  212  ALA ALA A . n 
A 1 213  VAL 213  213  213  VAL VAL A . n 
A 1 214  VAL 214  214  214  VAL VAL A . n 
A 1 215  ALA 215  215  215  ALA ALA A . n 
A 1 216  LEU 216  216  216  LEU LEU A . n 
A 1 217  LEU 217  217  217  LEU LEU A . n 
A 1 218  LYS 218  218  218  LYS LYS A . n 
A 1 219  ASP 219  219  219  ASP ASP A . n 
A 1 220  LEU 220  220  220  LEU LEU A . n 
A 1 221  GLY 221  221  221  GLY GLY A . n 
A 1 222  ALA 222  222  222  ALA ALA A . n 
A 1 223  SER 223  223  223  SER SER A . n 
A 1 224  LYS 224  224  224  LYS LYS A . n 
A 1 225  GLN 225  225  225  GLN GLN A . n 
A 1 226  LEU 226  226  226  LEU LEU A . n 
A 1 227  GLY 227  227  227  GLY GLY A . n 
A 1 228  THR 228  228  228  THR THR A . n 
A 1 229  ILE 229  229  229  ILE ILE A . n 
A 1 230  ILE 230  230  230  ILE ILE A . n 
A 1 231  GLU 231  231  231  GLU GLU A . n 
A 1 232  GLY 232  232  232  GLY GLY A . n 
A 1 233  GLU 233  233  233  GLU GLU A . n 
A 1 234  SER 234  234  234  SER SER A . n 
A 1 235  LEU 235  235  235  LEU LEU A . n 
A 1 236  LEU 236  236  236  LEU LEU A . n 
A 1 237  ASN 237  237  237  ASN ASN A . n 
A 1 238  ASP 238  238  238  ASP ASP A . n 
A 1 239  GLY 239  239  239  GLY GLY A . n 
A 1 240  CYS 240  240  240  CYS CYS A . n 
A 1 241  ALA 241  241  241  ALA ALA A . n 
A 1 242  ILE 242  242  242  ILE ILE A . n 
A 1 243  VAL 243  243  243  VAL VAL A . n 
A 1 244  ILE 244  244  244  ILE ILE A . n 
A 1 245  PHE 245  245  245  PHE PHE A . n 
A 1 246  ASN 246  246  246  ASN ASN A . n 
A 1 247  VAL 247  247  247  VAL VAL A . n 
A 1 248  PHE 248  248  248  PHE PHE A . n 
A 1 249  MET 249  249  249  MET MET A . n 
A 1 250  LYS 250  250  250  LYS LYS A . n 
A 1 251  MET 251  251  251  MET MET A . n 
A 1 252  VAL 252  252  252  VAL VAL A . n 
A 1 253  PHE 253  253  253  PHE PHE A . n 
A 1 254  PHE 254  254  254  PHE PHE A . n 
A 1 255  PRO 255  255  255  PRO PRO A . n 
A 1 256  GLN 256  256  256  GLN GLN A . n 
A 1 257  LEU 257  257  257  LEU LEU A . n 
A 1 258  THR 258  258  258  THR THR A . n 
A 1 259  SER 259  259  259  SER SER A . n 
A 1 260  THR 260  260  260  THR THR A . n 
A 1 261  VAL 261  261  261  VAL VAL A . n 
A 1 262  GLY 262  262  262  GLY GLY A . n 
A 1 263  GLN 263  263  263  GLN GLN A . n 
A 1 264  ASN 264  264  264  ASN ASN A . n 
A 1 265  VAL 265  265  265  VAL VAL A . n 
A 1 266  LEU 266  266  266  LEU LEU A . n 
A 1 267  TYR 267  267  267  TYR TYR A . n 
A 1 268  PHE 268  268  268  PHE PHE A . n 
A 1 269  LEU 269  269  269  LEU LEU A . n 
A 1 270  GLN 270  270  270  GLN GLN A . n 
A 1 271  VAL 271  271  271  VAL VAL A . n 
A 1 272  ALA 272  272  272  ALA ALA A . n 
A 1 273  VAL 273  273  273  VAL VAL A . n 
A 1 274  ALA 274  274  274  ALA ALA A . n 
A 1 275  GLY 275  275  275  GLY GLY A . n 
A 1 276  PRO 276  276  276  PRO PRO A . n 
A 1 277  LEU 277  277  277  LEU LEU A . n 
A 1 278  TRP 278  278  278  TRP TRP A . n 
A 1 279  GLY 279  279  279  GLY GLY A . n 
A 1 280  TYR 280  280  280  TYR TYR A . n 
A 1 281  ALA 281  281  281  ALA ALA A . n 
A 1 282  VAL 282  282  282  VAL VAL A . n 
A 1 283  ALA 283  283  283  ALA ALA A . n 
A 1 284  LYS 284  284  284  LYS LYS A . n 
A 1 285  VAL 285  285  285  VAL VAL A . n 
A 1 286  THR 286  286  286  THR THR A . n 
A 1 287  VAL 287  287  287  VAL VAL A . n 
A 1 288  PHE 288  288  288  PHE PHE A . n 
A 1 289  PHE 289  289  289  PHE PHE A . n 
A 1 290  LEU 290  290  290  LEU LEU A . n 
A 1 291  SER 291  291  291  SER SER A . n 
A 1 292  HIS 292  292  292  HIS HIS A . n 
A 1 293  ILE 293  293  293  ILE ILE A . n 
A 1 294  PHE 294  294  294  PHE PHE A . n 
A 1 295  ASN 295  295  295  ASN ASN A . n 
A 1 296  ASP 296  296  296  ASP ASP A . n 
A 1 297  ALA 297  297  297  ALA ALA A . n 
A 1 298  LEU 298  298  298  LEU LEU A . n 
A 1 299  VAL 299  299  299  VAL VAL A . n 
A 1 300  GLU 300  300  300  GLU GLU A . n 
A 1 301  ILE 301  301  301  ILE ILE A . n 
A 1 302  THR 302  302  302  THR THR A . n 
A 1 303  ILE 303  303  303  ILE ILE A . n 
A 1 304  THR 304  304  304  THR THR A . n 
A 1 305  LEU 305  305  305  LEU LEU A . n 
A 1 306  ALA 306  306  306  ALA ALA A . n 
A 1 307  ALA 307  307  307  ALA ALA A . n 
A 1 308  THR 308  308  308  THR THR A . n 
A 1 309  TYR 309  309  309  TYR TYR A . n 
A 1 310  LEU 310  310  310  LEU LEU A . n 
A 1 311  THR 311  311  311  THR THR A . n 
A 1 312  TYR 312  312  312  TYR TYR A . n 
A 1 313  TYR 313  313  313  TYR TYR A . n 
A 1 314  ILE 314  314  314  ILE ILE A . n 
A 1 315  GLY 315  315  315  GLY GLY A . n 
A 1 316  ASP 316  316  316  ASP ASP A . n 
A 1 317  ILE 317  317  317  ILE ILE A . n 
A 1 318  TRP 318  318  318  TRP TRP A . n 
A 1 319  LEU 319  319  319  LEU LEU A . n 
A 1 320  GLU 320  320  320  GLU GLU A . n 
A 1 321  VAL 321  321  321  VAL VAL A . n 
A 1 322  SER 322  322  322  SER SER A . n 
A 1 323  GLY 323  323  323  GLY GLY A . n 
A 1 324  VAL 324  324  324  VAL VAL A . n 
A 1 325  LEU 325  325  325  LEU LEU A . n 
A 1 326  ALA 326  326  326  ALA ALA A . n 
A 1 327  VAL 327  327  327  VAL VAL A . n 
A 1 328  VAL 328  328  328  VAL VAL A . n 
A 1 329  VAL 329  329  329  VAL VAL A . n 
A 1 330  LEU 330  330  330  LEU LEU A . n 
A 1 331  GLY 331  331  331  GLY GLY A . n 
A 1 332  LEU 332  332  332  LEU LEU A . n 
A 1 333  ILE 333  333  333  ILE ILE A . n 
A 1 334  VAL 334  334  334  VAL VAL A . n 
A 1 335  ASN 335  335  335  ASN ASN A . n 
A 1 336  ALA 336  336  336  ALA ALA A . n 
A 1 337  GLU 337  337  337  GLU GLU A . n 
A 1 338  LYS 338  338  338  LYS LYS A . n 
A 1 339  THR 339  339  339  THR THR A . n 
A 1 340  SER 340  340  340  SER SER A . n 
A 1 341  ILE 341  341  341  ILE ILE A . n 
A 1 342  SER 342  342  342  SER SER A . n 
A 1 343  PRO 343  343  343  PRO PRO A . n 
A 1 344  GLU 344  344  344  GLU GLU A . n 
A 1 345  VAL 345  345  345  VAL VAL A . n 
A 1 346  GLU 346  346  346  GLU GLU A . n 
A 1 347  VAL 347  347  347  VAL VAL A . n 
A 1 348  PHE 348  348  348  PHE PHE A . n 
A 1 349  LEU 349  349  349  LEU LEU A . n 
A 1 350  HIS 350  350  350  HIS HIS A . n 
A 1 351  ARG 351  351  351  ARG ARG A . n 
A 1 352  PHE 352  352  352  PHE PHE A . n 
A 1 353  TRP 353  353  353  TRP TRP A . n 
A 1 354  GLU 354  354  354  GLU GLU A . n 
A 1 355  MET 355  355  355  MET MET A . n 
A 1 356  LEU 356  356  356  LEU LEU A . n 
A 1 357  ALA 357  357  357  ALA ALA A . n 
A 1 358  TYR 358  358  358  TYR TYR A . n 
A 1 359  LEU 359  359  359  LEU LEU A . n 
A 1 360  ALA 360  360  360  ALA ALA A . n 
A 1 361  ASN 361  361  361  ASN ASN A . n 
A 1 362  THR 362  362  362  THR THR A . n 
A 1 363  LEU 363  363  363  LEU LEU A . n 
A 1 364  ILE 364  364  364  ILE ILE A . n 
A 1 365  PHE 365  365  365  PHE PHE A . n 
A 1 366  MET 366  366  366  MET MET A . n 
A 1 367  MET 367  367  367  MET MET A . n 
A 1 368  VAL 368  368  368  VAL VAL A . n 
A 1 369  GLY 369  369  369  GLY GLY A . n 
A 1 370  VAL 370  370  370  VAL VAL A . n 
A 1 371  VAL 371  371  371  VAL VAL A . n 
A 1 372  VAL 372  372  372  VAL VAL A . n 
A 1 373  THR 373  373  373  THR THR A . n 
A 1 374  GLN 374  374  374  GLN GLN A . n 
A 1 375  LYS 375  375  375  LYS LYS A . n 
A 1 376  ALA 376  376  376  ALA ALA A . n 
A 1 377  LEU 377  377  377  LEU LEU A . n 
A 1 378  VAL 378  378  378  VAL VAL A . n 
A 1 379  ALA 379  379  379  ALA ALA A . n 
A 1 380  VAL 380  380  380  VAL VAL A . n 
A 1 381  ASP 381  381  381  ASP ASP A . n 
A 1 382  LYS 382  382  382  LYS LYS A . n 
A 1 383  MET 383  383  383  MET MET A . n 
A 1 384  ASP 384  384  384  ASP ASP A . n 
A 1 385  TRP 385  385  385  TRP TRP A . n 
A 1 386  PHE 386  386  386  PHE PHE A . n 
A 1 387  TYR 387  387  387  TYR TYR A . n 
A 1 388  LEU 388  388  388  LEU LEU A . n 
A 1 389  ILE 389  389  389  ILE ILE A . n 
A 1 390  ILE 390  390  390  ILE ILE A . n 
A 1 391  LEU 391  391  391  LEU LEU A . n 
A 1 392  TYR 392  392  392  TYR TYR A . n 
A 1 393  LEU 393  393  393  LEU LEU A . n 
A 1 394  ALA 394  394  394  ALA ALA A . n 
A 1 395  ILE 395  395  395  ILE ILE A . n 
A 1 396  THR 396  396  396  THR THR A . n 
A 1 397  ILE 397  397  397  ILE ILE A . n 
A 1 398  ILE 398  398  398  ILE ILE A . n 
A 1 399  ALA 399  399  399  ALA ALA A . n 
A 1 400  GLY 400  400  400  GLY GLY A . n 
A 1 401  MET 401  401  401  MET MET A . n 
A 1 402  VAL 402  402  402  VAL VAL A . n 
A 1 403  ILE 403  403  403  ILE ILE A . n 
A 1 404  SER 404  404  404  SER SER A . n 
A 1 405  LEU 405  405  405  LEU LEU A . n 
A 1 406  PHE 406  406  406  PHE PHE A . n 
A 1 407  SER 407  407  407  SER SER A . n 
A 1 408  PRO 408  408  408  PRO PRO A . n 
A 1 409  ILE 409  409  409  ILE ILE A . n 
A 1 410  LEU 410  410  410  LEU LEU A . n 
A 1 411  SER 411  411  411  SER SER A . n 
A 1 412  ARG 412  412  412  ARG ARG A . n 
A 1 413  ILE 413  413  413  ILE ILE A . n 
A 1 414  GLY 414  414  414  GLY GLY A . n 
A 1 415  TYR 415  415  415  TYR TYR A . n 
A 1 416  GLY 416  416  416  GLY GLY A . n 
A 1 417  LEU 417  417  417  LEU LEU A . n 
A 1 418  THR 418  418  418  THR THR A . n 
A 1 419  TRP 419  419  419  TRP TRP A . n 
A 1 420  ARG 420  420  420  ARG ARG A . n 
A 1 421  ASN 421  421  421  ASN ASN A . n 
A 1 422  ALA 422  422  422  ALA ALA A . n 
A 1 423  VAL 423  423  423  VAL VAL A . n 
A 1 424  ILE 424  424  424  ILE ILE A . n 
A 1 425  MET 425  425  425  MET MET A . n 
A 1 426  THR 426  426  426  THR THR A . n 
A 1 427  TRP 427  427  427  TRP TRP A . n 
A 1 428  GLY 428  428  428  GLY GLY A . n 
A 1 429  GLY 429  429  429  GLY GLY A . n 
A 1 430  LEU 430  430  430  LEU LEU A . n 
A 1 431  ARG 431  431  431  ARG ARG A . n 
A 1 432  GLY 432  432  432  GLY GLY A . n 
A 1 433  ALA 433  433  433  ALA ALA A . n 
A 1 434  VAL 434  434  434  VAL VAL A . n 
A 1 435  GLY 435  435  435  GLY GLY A . n 
A 1 436  LEU 436  436  436  LEU LEU A . n 
A 1 437  ALA 437  437  437  ALA ALA A . n 
A 1 438  LEU 438  438  438  LEU LEU A . n 
A 1 439  ALA 439  439  439  ALA ALA A . n 
A 1 440  LEU 440  440  440  LEU LEU A . n 
A 1 441  VAL 441  441  441  VAL VAL A . n 
A 1 442  VAL 442  442  442  VAL VAL A . n 
A 1 443  GLU 443  443  443  GLU GLU A . n 
A 1 444  ASN 444  444  444  ASN ASN A . n 
A 1 445  LEU 445  445  445  LEU LEU A . n 
A 1 446  ALA 446  446  446  ALA ALA A . n 
A 1 447  GLY 447  447  447  GLY GLY A . n 
A 1 448  ASN 448  448  448  ASN ASN A . n 
A 1 449  ASP 449  449  449  ASP ASP A . n 
A 1 450  VAL 450  450  450  VAL VAL A . n 
A 1 451  ILE 451  451  451  ILE ILE A . n 
A 1 452  GLY 452  452  452  GLY GLY A . n 
A 1 453  SER 453  453  453  SER SER A . n 
A 1 454  LYS 454  454  454  LYS LYS A . n 
A 1 455  PHE 455  455  455  PHE PHE A . n 
A 1 456  LEU 456  456  456  LEU LEU A . n 
A 1 457  PHE 457  457  457  PHE PHE A . n 
A 1 458  HIS 458  458  458  HIS HIS A . n 
A 1 459  THR 459  459  459  THR THR A . n 
A 1 460  ALA 460  460  460  ALA ALA A . n 
A 1 461  GLY 461  461  461  GLY GLY A . n 
A 1 462  ILE 462  462  462  ILE ILE A . n 
A 1 463  VAL 463  463  463  VAL VAL A . n 
A 1 464  VAL 464  464  464  VAL VAL A . n 
A 1 465  LEU 465  465  465  LEU LEU A . n 
A 1 466  THR 466  466  466  THR THR A . n 
A 1 467  LEU 467  467  467  LEU LEU A . n 
A 1 468  VAL 468  468  468  VAL VAL A . n 
A 1 469  ILE 469  469  469  ILE ILE A . n 
A 1 470  ASN 470  470  470  ASN ASN A . n 
A 1 471  ALA 471  471  471  ALA ALA A . n 
A 1 472  THR 472  472  472  THR THR A . n 
A 1 473  THR 473  473  473  THR THR A . n 
A 1 474  ILE 474  474  474  ILE ILE A . n 
A 1 475  GLN 475  475  475  GLN GLN A . n 
A 1 476  THR 476  476  476  THR THR A . n 
A 1 477  LEU 477  477  477  LEU LEU A . n 
A 1 478  LEU 478  478  478  LEU LEU A . n 
A 1 479  ARG 479  479  479  ARG ARG A . n 
A 1 480  ILE 480  480  480  ILE ILE A . n 
A 1 481  LEU 481  481  481  LEU LEU A . n 
A 1 482  GLY 482  482  482  GLY GLY A . n 
A 1 483  MET 483  483  483  MET MET A . n 
A 1 484  SER 484  484  484  SER SER A . n 
A 1 485  ASP 485  485  485  ASP ASP A . n 
A 1 486  ILE 486  486  486  ILE ILE A . n 
A 1 487  SER 487  487  487  SER SER A . n 
A 1 488  ILE 488  488  488  ILE ILE A . n 
A 1 489  PRO 489  489  489  PRO PRO A . n 
A 1 490  LYS 490  490  490  LYS LYS A . n 
A 1 491  ARG 491  491  491  ARG ARG A . n 
A 1 492  LEU 492  492  492  LEU LEU A . n 
A 1 493  ALA 493  493  493  ALA ALA A . n 
A 1 494  MET 494  494  494  MET MET A . n 
A 1 495  ALA 495  495  495  ALA ALA A . n 
A 1 496  GLY 496  496  496  GLY GLY A . n 
A 1 497  ALA 497  497  497  ALA ALA A . n 
A 1 498  VAL 498  498  498  VAL VAL A . n 
A 1 499  ARG 499  499  499  ARG ARG A . n 
A 1 500  ARG 500  500  500  ARG ARG A . n 
A 1 501  ILE 501  501  501  ILE ILE A . n 
A 1 502  HIS 502  502  502  HIS HIS A . n 
A 1 503  GLU 503  503  503  GLU GLU A . n 
A 1 504  GLY 504  504  504  GLY GLY A . n 
A 1 505  GLN 505  505  505  GLN GLN A . n 
A 1 506  ASN 506  506  506  ASN ASN A . n 
A 1 507  ARG 507  507  507  ARG ARG A . n 
A 1 508  THR 508  508  508  THR THR A . n 
A 1 509  LEU 509  509  509  LEU LEU A . n 
A 1 510  ASN 510  510  510  ASN ASN A . n 
A 1 511  MET 511  511  511  MET MET A . n 
A 1 512  LEU 512  512  512  LEU LEU A . n 
A 1 513  LYS 513  513  513  LYS LYS A . n 
A 1 514  SER 514  514  514  SER SER A . n 
A 1 515  ASP 515  515  515  ASP ASP A . n 
A 1 516  ARG 516  516  516  ARG ARG A . n 
A 1 517  PHE 517  517  517  PHE PHE A . n 
A 1 518  LEU 518  518  518  LEU LEU A . n 
A 1 519  ALA 519  519  519  ALA ALA A . n 
A 1 520  ASP 520  520  520  ASP ASP A . n 
A 1 521  ALA 521  521  521  ALA ALA A . n 
A 1 522  ASP 522  522  522  ASP ASP A . n 
A 1 523  TRP 523  523  523  TRP TRP A . n 
A 1 524  ASP 524  524  524  ASP ASP A . n 
A 1 525  ILE 525  525  525  ILE ILE A . n 
A 1 526  ALA 526  526  526  ALA ALA A . n 
A 1 527  THR 527  527  527  THR THR A . n 
A 1 528  ALA 528  528  528  ALA ALA A . n 
A 1 529  ALA 529  529  529  ALA ALA A . n 
A 1 530  CYS 530  530  530  CYS CYS A . n 
A 1 531  GLU 531  531  531  GLU GLU A . n 
A 1 532  ILE 532  532  532  ILE ILE A . n 
A 1 533  SER 533  533  533  SER SER A . n 
A 1 534  ASP 534  534  534  ASP ASP A . n 
A 1 535  PRO 535  535  535  PRO PRO A . n 
A 1 536  TYR 536  536  536  TYR TYR A . n 
A 1 537  SER 537  537  ?    ?   ?   A . n 
A 1 538  ALA 538  538  ?    ?   ?   A . n 
A 1 539  LEU 539  539  ?    ?   ?   A . n 
A 1 540  SER 540  540  ?    ?   ?   A . n 
A 1 541  ASP 541  541  ?    ?   ?   A . n 
A 1 542  ASP 542  542  ?    ?   ?   A . n 
A 1 543  GLU 543  543  ?    ?   ?   A . n 
A 1 544  ASN 544  544  ?    ?   ?   A . n 
A 1 545  ALA 545  545  ?    ?   ?   A . n 
A 1 546  PRO 546  546  ?    ?   ?   A . n 
A 1 547  ALA 547  547  ?    ?   ?   A . n 
A 1 548  ASP 548  548  ?    ?   ?   A . n 
A 1 549  GLU 549  549  ?    ?   ?   A . n 
A 1 550  LEU 550  550  ?    ?   ?   A . n 
A 1 551  THR 551  551  ?    ?   ?   A . n 
A 1 552  LEU 552  552  ?    ?   ?   A . n 
A 1 553  GLY 553  553  ?    ?   ?   A . n 
A 1 554  GLU 554  554  ?    ?   ?   A . n 
A 1 555  ARG 555  555  ?    ?   ?   A . n 
A 1 556  LYS 556  556  ?    ?   ?   A . n 
A 1 557  SER 557  557  ?    ?   ?   A . n 
A 1 558  VAL 558  558  ?    ?   ?   A . n 
A 1 559  CYS 559  559  ?    ?   ?   A . n 
A 1 560  PRO 560  560  ?    ?   ?   A . n 
A 1 561  GLY 561  561  ?    ?   ?   A . n 
A 1 562  CYS 562  562  ?    ?   ?   A . n 
A 1 563  LYS 563  563  ?    ?   ?   A . n 
A 1 564  ALA 564  564  ?    ?   ?   A . n 
A 1 565  MET 565  565  ?    ?   ?   A . n 
A 1 566  VAL 566  566  ?    ?   ?   A . n 
A 1 567  PRO 567  567  ?    ?   ?   A . n 
A 1 568  ASN 568  568  ?    ?   ?   A . n 
A 1 569  GLU 569  569  ?    ?   ?   A . n 
A 1 570  PRO 570  570  570  PRO PRO A . n 
A 1 571  SER 571  571  571  SER SER A . n 
A 1 572  PRO 572  572  572  PRO PRO A . n 
A 1 573  ARG 573  573  573  ARG ARG A . n 
A 1 574  GLU 574  574  574  GLU GLU A . n 
A 1 575  PHE 575  575  575  PHE PHE A . n 
A 1 576  ALA 576  576  576  ALA ALA A . n 
A 1 577  ASP 577  577  577  ASP ASP A . n 
A 1 578  MET 578  578  578  MET MET A . n 
A 1 579  MET 579  579  579  MET MET A . n 
A 1 580  GLU 580  580  580  GLU GLU A . n 
A 1 581  GLU 581  581  581  GLU GLU A . n 
A 1 582  ALA 582  582  582  ALA ALA A . n 
A 1 583  ARG 583  583  583  ARG ARG A . n 
A 1 584  LEU 584  584  584  LEU LEU A . n 
A 1 585  ARG 585  585  585  ARG ARG A . n 
A 1 586  MET 586  586  586  MET MET A . n 
A 1 587  LEU 587  587  587  LEU LEU A . n 
A 1 588  LYS 588  588  588  LYS LYS A . n 
A 1 589  ALA 589  589  589  ALA ALA A . n 
A 1 590  GLU 590  590  590  GLU GLU A . n 
A 1 591  LYS 591  591  591  LYS LYS A . n 
A 1 592  ILE 592  592  592  ILE ILE A . n 
A 1 593  SER 593  593  593  SER SER A . n 
A 1 594  TYR 594  594  594  TYR TYR A . n 
A 1 595  TRP 595  595  595  TRP TRP A . n 
A 1 596  LYS 596  596  596  LYS LYS A . n 
A 1 597  GLN 597  597  597  GLN GLN A . n 
A 1 598  PHE 598  598  598  PHE PHE A . n 
A 1 599  GLU 599  599  599  GLU GLU A . n 
A 1 600  HIS 600  600  600  HIS HIS A . n 
A 1 601  GLY 601  601  601  GLY GLY A . n 
A 1 602  MET 602  602  602  MET MET A . n 
A 1 603  LEU 603  603  603  LEU LEU A . n 
A 1 604  ALA 604  604  604  ALA ALA A . n 
A 1 605  ARG 605  605  605  ARG ARG A . n 
A 1 606  GLU 606  606  606  GLU GLU A . n 
A 1 607  ALA 607  607  607  ALA ALA A . n 
A 1 608  LEU 608  608  608  LEU LEU A . n 
A 1 609  ARG 609  609  609  ARG ARG A . n 
A 1 610  LEU 610  610  610  LEU LEU A . n 
A 1 611  LEU 611  611  611  LEU LEU A . n 
A 1 612  VAL 612  612  612  VAL VAL A . n 
A 1 613  GLN 613  613  613  GLN GLN A . n 
A 1 614  HIS 614  614  614  HIS HIS A . n 
A 1 615  ALA 615  615  615  ALA ALA A . n 
A 1 616  GLU 616  616  616  GLU GLU A . n 
A 1 617  VAL 617  617  617  VAL VAL A . n 
A 1 618  ALA 618  618  618  ALA ALA A . n 
A 1 619  ALA 619  619  619  ALA ALA A . n 
A 1 620  ASP 620  620  620  ASP ASP A . n 
A 1 621  GLU 621  621  621  GLU GLU A . n 
A 1 622  LYS 622  622  622  LYS LYS A . n 
A 1 623  ASP 623  623  623  ASP ASP A . n 
A 1 624  GLN 624  624  624  GLN GLN A . n 
A 1 625  PHE 625  625  625  PHE PHE A . n 
A 1 626  ILE 626  626  626  ILE ILE A . n 
A 1 627  LEU 627  627  627  LEU LEU A . n 
A 1 628  VAL 628  628  628  VAL VAL A . n 
A 1 629  ASP 629  629  629  ASP ASP A . n 
A 1 630  ASP 630  630  630  ASP ASP A . n 
A 1 631  LEU 631  631  631  LEU LEU A . n 
A 1 632  LYS 632  632  632  LYS LYS A . n 
A 1 633  LYS 633  633  633  LYS LYS A . n 
A 1 634  SER 634  634  634  SER SER A . n 
A 1 635  TRP 635  635  635  TRP TRP A . n 
A 1 636  GLN 636  636  636  GLN GLN A . n 
A 1 637  ILE 637  637  637  ILE ILE A . n 
A 1 638  LYS 638  638  638  LYS LYS A . n 
A 1 639  GLY 639  639  639  GLY GLY A . n 
A 1 640  ILE 640  640  640  ILE ILE A . n 
A 1 641  TYR 641  641  641  TYR TYR A . n 
A 1 642  PRO 642  642  642  PRO PRO A . n 
A 1 643  TRP 643  643  643  TRP TRP A . n 
A 1 644  LEU 644  644  644  LEU LEU A . n 
A 1 645  LYS 645  645  645  LYS LYS A . n 
A 1 646  ARG 646  646  646  ARG ARG A . n 
A 1 647  LYS 647  647  647  LYS LYS A . n 
A 1 648  LEU 648  648  648  LEU LEU A . n 
A 1 649  GLU 649  649  649  GLU GLU A . n 
A 1 650  ASP 650  650  650  ASP ASP A . n 
A 1 651  LEU 651  651  651  LEU LEU A . n 
A 1 652  ILE 652  652  652  ILE ILE A . n 
A 1 653  SER 653  653  653  SER SER A . n 
A 1 654  GLU 654  654  ?    ?   ?   A . n 
A 1 655  LYS 655  655  ?    ?   ?   A . n 
A 1 656  LYS 656  656  ?    ?   ?   A . n 
A 1 657  ILE 657  657  ?    ?   ?   A . n 
A 1 658  ALA 658  658  ?    ?   ?   A . n 
A 1 659  ALA 659  659  ?    ?   ?   A . n 
A 1 660  ILE 660  660  ?    ?   ?   A . n 
A 1 661  PRO 661  661  ?    ?   ?   A . n 
A 1 662  MET 662  662  ?    ?   ?   A . n 
A 1 663  PRO 663  663  ?    ?   ?   A . n 
A 1 664  LYS 664  664  ?    ?   ?   A . n 
A 1 665  TYR 665  665  ?    ?   ?   A . n 
A 1 666  LYS 666  666  ?    ?   ?   A . n 
A 1 667  LEU 667  667  ?    ?   ?   A . n 
A 1 668  GLY 668  668  ?    ?   ?   A . n 
A 1 669  LYS 669  669  ?    ?   ?   A . n 
A 1 670  LEU 670  670  670  LEU LEU A . n 
A 1 671  MET 671  671  671  MET MET A . n 
A 1 672  TYR 672  672  672  TYR TYR A . n 
A 1 673  LYS 673  673  673  LYS LYS A . n 
A 1 674  ILE 674  674  674  ILE ILE A . n 
A 1 675  CYS 675  675  675  CYS CYS A . n 
A 1 676  HIS 676  676  676  HIS HIS A . n 
A 1 677  HIS 677  677  677  HIS HIS A . n 
A 1 678  MET 678  678  678  MET MET A . n 
A 1 679  ALA 679  679  679  ALA ALA A . n 
A 1 680  PHE 680  680  680  PHE PHE A . n 
A 1 681  GLU 681  681  681  GLU GLU A . n 
A 1 682  VAL 682  682  682  VAL VAL A . n 
A 1 683  THR 683  683  683  THR THR A . n 
A 1 684  ILE 684  684  684  ILE ILE A . n 
A 1 685  ASN 685  685  685  ASN ASN A . n 
A 1 686  ILE 686  686  686  ILE ILE A . n 
A 1 687  ALA 687  687  687  ALA ALA A . n 
A 1 688  ILE 688  688  688  ILE ILE A . n 
A 1 689  VAL 689  689  689  VAL VAL A . n 
A 1 690  LEU 690  690  690  LEU LEU A . n 
A 1 691  ASN 691  691  691  ASN ASN A . n 
A 1 692  ILE 692  692  692  ILE ILE A . n 
A 1 693  VAL 693  693  693  VAL VAL A . n 
A 1 694  PRO 694  694  694  PRO PRO A . n 
A 1 695  ILE 695  695  695  ILE ILE A . n 
A 1 696  ILE 696  696  696  ILE ILE A . n 
A 1 697  MET 697  697  697  MET MET A . n 
A 1 698  GLU 698  698  698  GLU GLU A . n 
A 1 699  PHE 699  699  699  PHE PHE A . n 
A 1 700  VAL 700  700  700  VAL VAL A . n 
A 1 701  VAL 701  701  ?    ?   ?   A . n 
A 1 702  GLN 702  702  ?    ?   ?   A . n 
A 1 703  ASP 703  703  ?    ?   ?   A . n 
A 1 704  LYS 704  704  ?    ?   ?   A . n 
A 1 705  MET 705  705  ?    ?   ?   A . n 
A 1 706  ALA 706  706  ?    ?   ?   A . n 
A 1 707  SER 707  707  ?    ?   ?   A . n 
A 1 708  VAL 708  708  ?    ?   ?   A . n 
A 1 709  SER 709  709  ?    ?   ?   A . n 
A 1 710  THR 710  710  ?    ?   ?   A . n 
A 1 711  MET 711  711  ?    ?   ?   A . n 
A 1 712  ALA 712  712  ?    ?   ?   A . n 
A 1 713  ALA 713  713  ?    ?   ?   A . n 
A 1 714  PRO 714  714  ?    ?   ?   A . n 
A 1 715  GLY 715  715  ?    ?   ?   A . n 
A 1 716  SER 716  716  ?    ?   ?   A . n 
A 1 717  THR 717  717  ?    ?   ?   A . n 
A 1 718  VAL 718  718  ?    ?   ?   A . n 
A 1 719  SER 719  719  ?    ?   ?   A . n 
A 1 720  SER 720  720  ?    ?   ?   A . n 
A 1 721  GLU 721  721  ?    ?   ?   A . n 
A 1 722  PRO 722  722  ?    ?   ?   A . n 
A 1 723  SER 723  723  ?    ?   ?   A . n 
A 1 724  SER 724  724  ?    ?   ?   A . n 
A 1 725  LEU 725  725  ?    ?   ?   A . n 
A 1 726  GLN 726  726  ?    ?   ?   A . n 
A 1 727  LYS 727  727  ?    ?   ?   A . n 
A 1 728  ILE 728  728  ?    ?   ?   A . n 
A 1 729  GLU 729  729  ?    ?   ?   A . n 
A 1 730  ASP 730  730  730  ASP ASP A . n 
A 1 731  ALA 731  731  731  ALA ALA A . n 
A 1 732  LEU 732  732  732  LEU LEU A . n 
A 1 733  ARG 733  733  733  ARG ARG A . n 
A 1 734  ILE 734  734  734  ILE ILE A . n 
A 1 735  SER 735  735  735  SER SER A . n 
A 1 736  ASN 736  736  736  ASN ASN A . n 
A 1 737  TYR 737  737  737  TYR TYR A . n 
A 1 738  VAL 738  738  738  VAL VAL A . n 
A 1 739  PHE 739  739  739  PHE PHE A . n 
A 1 740  PHE 740  740  740  PHE PHE A . n 
A 1 741  VAL 741  741  741  VAL VAL A . n 
A 1 742  ILE 742  742  742  ILE ILE A . n 
A 1 743  TYR 743  743  743  TYR TYR A . n 
A 1 744  ALA 744  744  744  ALA ALA A . n 
A 1 745  ILE 745  745  745  ILE ILE A . n 
A 1 746  GLU 746  746  746  GLU GLU A . n 
A 1 747  ALA 747  747  747  ALA ALA A . n 
A 1 748  ILE 748  748  748  ILE ILE A . n 
A 1 749  VAL 749  749  749  VAL VAL A . n 
A 1 750  LYS 750  750  750  LYS LYS A . n 
A 1 751  ILE 751  751  751  ILE ILE A . n 
A 1 752  LEU 752  752  752  LEU LEU A . n 
A 1 753  GLY 753  753  753  GLY GLY A . n 
A 1 754  LEU 754  754  754  LEU LEU A . n 
A 1 755  GLY 755  755  755  GLY GLY A . n 
A 1 756  ARG 756  756  756  ARG ARG A . n 
A 1 757  HIS 757  757  757  HIS HIS A . n 
A 1 758  TYR 758  758  758  TYR TYR A . n 
A 1 759  ILE 759  759  759  ILE ILE A . n 
A 1 760  VAL 760  760  760  VAL VAL A . n 
A 1 761  SER 761  761  761  SER SER A . n 
A 1 762  HIS 762  762  762  HIS HIS A . n 
A 1 763  TRP 763  763  763  TRP TRP A . n 
A 1 764  ASN 764  764  764  ASN ASN A . n 
A 1 765  LYS 765  765  765  LYS LYS A . n 
A 1 766  PHE 766  766  766  PHE PHE A . n 
A 1 767  ASP 767  767  767  ASP ASP A . n 
A 1 768  ALA 768  768  768  ALA ALA A . n 
A 1 769  PHE 769  769  769  PHE PHE A . n 
A 1 770  ILE 770  770  770  ILE ILE A . n 
A 1 771  LEU 771  771  771  LEU LEU A . n 
A 1 772  VAL 772  772  772  VAL VAL A . n 
A 1 773  VAL 773  773  773  VAL VAL A . n 
A 1 774  ALA 774  774  774  ALA ALA A . n 
A 1 775  LEU 775  775  775  LEU LEU A . n 
A 1 776  VAL 776  776  776  VAL VAL A . n 
A 1 777  ASP 777  777  ?    ?   ?   A . n 
A 1 778  ILE 778  778  ?    ?   ?   A . n 
A 1 779  ILE 779  779  ?    ?   ?   A . n 
A 1 780  ILE 780  780  ?    ?   ?   A . n 
A 1 781  ALA 781  781  ?    ?   ?   A . n 
A 1 782  GLU 782  782  ?    ?   ?   A . n 
A 1 783  THR 783  783  ?    ?   ?   A . n 
A 1 784  LEU 784  784  ?    ?   ?   A . n 
A 1 785  LEU 785  785  ?    ?   ?   A . n 
A 1 786  LYS 786  786  ?    ?   ?   A . n 
A 1 787  GLY 787  787  ?    ?   ?   A . n 
A 1 788  SER 788  788  ?    ?   ?   A . n 
A 1 789  ILE 789  789  ?    ?   ?   A . n 
A 1 790  THR 790  790  ?    ?   ?   A . n 
A 1 791  ILE 791  791  ?    ?   ?   A . n 
A 1 792  ASN 792  792  ?    ?   ?   A . n 
A 1 793  LEU 793  793  ?    ?   ?   A . n 
A 1 794  SER 794  794  ?    ?   ?   A . n 
A 1 795  SER 795  795  ?    ?   ?   A . n 
A 1 796  ILE 796  796  ?    ?   ?   A . n 
A 1 797  LYS 797  797  797  LYS LYS A . n 
A 1 798  VAL 798  798  798  VAL VAL A . n 
A 1 799  VAL 799  799  799  VAL VAL A . n 
A 1 800  LYS 800  800  800  LYS LYS A . n 
A 1 801  LEU 801  801  801  LEU LEU A . n 
A 1 802  PHE 802  802  802  PHE PHE A . n 
A 1 803  ARG 803  803  803  ARG ARG A . n 
A 1 804  LEU 804  804  804  LEU LEU A . n 
A 1 805  LEU 805  805  805  LEU LEU A . n 
A 1 806  ARG 806  806  806  ARG ARG A . n 
A 1 807  GLY 807  807  807  GLY GLY A . n 
A 1 808  LEU 808  808  808  LEU LEU A . n 
A 1 809  ARG 809  809  809  ARG ARG A . n 
A 1 810  MET 810  810  810  MET MET A . n 
A 1 811  LEU 811  811  811  LEU LEU A . n 
A 1 812  ARG 812  812  812  ARG ARG A . n 
A 1 813  LEU 813  813  813  LEU LEU A . n 
A 1 814  THR 814  814  814  THR THR A . n 
A 1 815  LYS 815  815  815  LYS LYS A . n 
A 1 816  ALA 816  816  816  ALA ALA A . n 
A 1 817  LEU 817  817  817  LEU LEU A . n 
A 1 818  ILE 818  818  818  ILE ILE A . n 
A 1 819  PRO 819  819  819  PRO PRO A . n 
A 1 820  LYS 820  820  820  LYS LYS A . n 
A 1 821  LEU 821  821  821  LEU LEU A . n 
A 1 822  ILE 822  822  822  ILE ILE A . n 
A 1 823  LEU 823  823  823  LEU LEU A . n 
A 1 824  VAL 824  824  824  VAL VAL A . n 
A 1 825  VAL 825  825  825  VAL VAL A . n 
A 1 826  ASN 826  826  826  ASN ASN A . n 
A 1 827  GLY 827  827  827  GLY GLY A . n 
A 1 828  LYS 828  828  828  LYS LYS A . n 
A 1 829  ILE 829  829  829  ILE ILE A . n 
A 1 830  ASN 830  830  830  ASN ASN A . n 
A 1 831  ASN 831  831  831  ASN ASN A . n 
A 1 832  GLN 832  832  832  GLN GLN A . n 
A 1 833  LEU 833  833  833  LEU LEU A . n 
A 1 834  SER 834  834  834  SER SER A . n 
A 1 835  LEU 835  835  835  LEU LEU A . n 
A 1 836  GLY 836  836  836  GLY GLY A . n 
A 1 837  TYR 837  837  837  TYR TYR A . n 
A 1 838  ASP 838  838  838  ASP ASP A . n 
A 1 839  VAL 839  839  839  VAL VAL A . n 
A 1 840  GLY 840  840  840  GLY GLY A . n 
A 1 841  LYS 841  841  841  LYS LYS A . n 
A 1 842  GLY 842  842  842  GLY GLY A . n 
A 1 843  TYR 843  843  843  TYR TYR A . n 
A 1 844  ILE 844  844  844  ILE ILE A . n 
A 1 845  ILE 845  845  845  ILE ILE A . n 
A 1 846  GLY 846  846  846  GLY GLY A . n 
A 1 847  GLU 847  847  847  GLU GLU A . n 
A 1 848  GLU 848  848  848  GLU GLU A . n 
A 1 849  GLU 849  849  849  GLU GLU A . n 
A 1 850  VAL 850  850  850  VAL VAL A . n 
A 1 851  GLY 851  851  851  GLY GLY A . n 
A 1 852  LYS 852  852  852  LYS LYS A . n 
A 1 853  ILE 853  853  853  ILE ILE A . n 
A 1 854  ILE 854  854  854  ILE ILE A . n 
A 1 855  ASP 855  855  855  ASP ASP A . n 
A 1 856  ARG 856  856  856  ARG ARG A . n 
A 1 857  MET 857  857  857  MET MET A . n 
A 1 858  VAL 858  858  858  VAL VAL A . n 
A 1 859  ASP 859  859  859  ASP ASP A . n 
A 1 860  ASN 860  860  860  ASN ASN A . n 
A 1 861  LYS 861  861  861  LYS LYS A . n 
A 1 862  LYS 862  862  862  LYS LYS A . n 
A 1 863  ILE 863  863  863  ILE ILE A . n 
A 1 864  LEU 864  864  864  LEU LEU A . n 
A 1 865  ARG 865  865  865  ARG ARG A . n 
A 1 866  GLU 866  866  866  GLU GLU A . n 
A 1 867  LEU 867  867  867  LEU LEU A . n 
A 1 868  LYS 868  868  868  LYS LYS A . n 
A 1 869  HIS 869  869  869  HIS HIS A . n 
A 1 870  ILE 870  870  870  ILE ILE A . n 
A 1 871  SER 871  871  871  SER SER A . n 
A 1 872  GLU 872  872  872  GLU GLU A . n 
A 1 873  THR 873  873  873  THR THR A . n 
A 1 874  GLY 874  874  874  GLY GLY A . n 
A 1 875  ARG 875  875  875  ARG ARG A . n 
A 1 876  LEU 876  876  876  LEU LEU A . n 
A 1 877  GLN 877  877  877  GLN GLN A . n 
A 1 878  VAL 878  878  878  VAL VAL A . n 
A 1 879  VAL 879  879  879  VAL VAL A . n 
A 1 880  LYS 880  880  880  LYS LYS A . n 
A 1 881  GLU 881  881  881  GLU GLU A . n 
A 1 882  LEU 882  882  882  LEU LEU A . n 
A 1 883  GLY 883  883  883  GLY GLY A . n 
A 1 884  LEU 884  884  884  LEU LEU A . n 
A 1 885  LEU 885  885  885  LEU LEU A . n 
A 1 886  GLN 886  886  886  GLN GLN A . n 
A 1 887  ARG 887  887  887  ARG ARG A . n 
A 1 888  GLU 888  888  888  GLU GLU A . n 
A 1 889  HIS 889  889  889  HIS HIS A . n 
A 1 890  PRO 890  890  890  PRO PRO A . n 
A 1 891  GLY 891  891  891  GLY GLY A . n 
A 1 892  ILE 892  892  892  ILE ILE A . n 
A 1 893  ALA 893  893  893  ALA ALA A . n 
A 1 894  VAL 894  894  894  VAL VAL A . n 
A 1 895  SER 895  895  895  SER SER A . n 
A 1 896  VAL 896  896  896  VAL VAL A . n 
A 1 897  LYS 897  897  897  LYS LYS A . n 
A 1 898  THR 898  898  898  THR THR A . n 
A 1 899  ARG 899  899  899  ARG ARG A . n 
A 1 900  GLN 900  900  900  GLN GLN A . n 
A 1 901  ALA 901  901  901  ALA ALA A . n 
A 1 902  ILE 902  902  902  ILE ILE A . n 
A 1 903  ARG 903  903  903  ARG ARG A . n 
A 1 904  THR 904  904  904  THR THR A . n 
A 1 905  ILE 905  905  905  ILE ILE A . n 
A 1 906  LEU 906  906  906  LEU LEU A . n 
A 1 907  ASN 907  907  907  ASN ASN A . n 
A 1 908  HIS 908  908  908  HIS HIS A . n 
A 1 909  SER 909  909  909  SER SER A . n 
A 1 910  ARG 910  910  910  ARG ARG A . n 
A 1 911  GLU 911  911  911  GLU GLU A . n 
A 1 912  THR 912  912  912  THR THR A . n 
A 1 913  ILE 913  913  913  ILE ILE A . n 
A 1 914  HIS 914  914  914  HIS HIS A . n 
A 1 915  GLU 915  915  915  GLU GLU A . n 
A 1 916  LEU 916  916  916  LEU LEU A . n 
A 1 917  GLN 917  917  917  GLN GLN A . n 
A 1 918  GLY 918  918  918  GLY GLY A . n 
A 1 919  ALA 919  919  919  ALA ALA A . n 
A 1 920  GLY 920  920  920  GLY GLY A . n 
A 1 921  LEU 921  921  921  LEU LEU A . n 
A 1 922  LEU 922  922  922  LEU LEU A . n 
A 1 923  ASP 923  923  923  ASP ASP A . n 
A 1 924  GLU 924  924  924  GLU GLU A . n 
A 1 925  MET 925  925  925  MET MET A . n 
A 1 926  GLU 926  926  926  GLU GLU A . n 
A 1 927  ALA 927  927  927  ALA ALA A . n 
A 1 928  HIS 928  928  928  HIS HIS A . n 
A 1 929  LYS 929  929  929  LYS LYS A . n 
A 1 930  LEU 930  930  930  LEU LEU A . n 
A 1 931  GLU 931  931  931  GLU GLU A . n 
A 1 932  LEU 932  932  932  LEU LEU A . n 
A 1 933  THR 933  933  933  THR THR A . n 
A 1 934  VAL 934  934  934  VAL VAL A . n 
A 1 935  GLU 935  935  935  GLU GLU A . n 
A 1 936  ILE 936  936  936  ILE ILE A . n 
A 1 937  LYS 937  937  937  LYS LYS A . n 
A 1 938  MET 938  938  938  MET MET A . n 
A 1 939  LYS 939  939  939  LYS LYS A . n 
A 1 940  ARG 940  940  940  ARG ARG A . n 
A 1 941  LEU 941  941  941  LEU LEU A . n 
A 1 942  MET 942  942  942  MET MET A . n 
A 1 943  ASN 943  943  943  ASN ASN A . n 
A 1 944  ALA 944  944  944  ALA ALA A . n 
A 1 945  PRO 945  945  945  PRO PRO A . n 
A 1 946  SER 946  946  946  SER SER A . n 
A 1 947  SER 947  947  947  SER SER A . n 
A 1 948  ILE 948  948  948  ILE ILE A . n 
A 1 949  PRO 949  949  949  PRO PRO A . n 
A 1 950  PRO 950  950  950  PRO PRO A . n 
A 1 951  PRO 951  951  951  PRO PRO A . n 
A 1 952  PRO 952  952  952  PRO PRO A . n 
A 1 953  PRO 953  953  953  PRO PRO A . n 
A 1 954  GLU 954  954  954  GLU GLU A . n 
A 1 955  ASN 955  955  955  ASN ASN A . n 
A 1 956  LEU 956  956  956  LEU LEU A . n 
A 1 957  LEU 957  957  957  LEU LEU A . n 
A 1 958  LYS 958  958  958  LYS LYS A . n 
A 1 959  ASN 959  959  959  ASN ASN A . n 
A 1 960  VAL 960  960  960  VAL VAL A . n 
A 1 961  SER 961  961  961  SER SER A . n 
A 1 962  TRP 962  962  962  TRP TRP A . n 
A 1 963  LEU 963  963  963  LEU LEU A . n 
A 1 964  ALA 964  964  964  ALA ALA A . n 
A 1 965  GLY 965  965  965  GLY GLY A . n 
A 1 966  ASP 966  966  966  ASP ASP A . n 
A 1 967  MET 967  967  967  MET MET A . n 
A 1 968  LYS 968  968  968  LYS LYS A . n 
A 1 969  LEU 969  969  969  LEU LEU A . n 
A 1 970  ILE 970  970  970  ILE ILE A . n 
A 1 971  ASP 971  971  971  ASP ASP A . n 
A 1 972  PHE 972  972  972  PHE PHE A . n 
A 1 973  ILE 973  973  973  ILE ILE A . n 
A 1 974  LYS 974  974  974  LYS LYS A . n 
A 1 975  ALA 975  975  975  ALA ALA A . n 
A 1 976  ARG 976  976  976  ARG ARG A . n 
A 1 977  ALA 977  977  977  ALA ALA A . n 
A 1 978  SER 978  978  978  SER SER A . n 
A 1 979  LEU 979  979  979  LEU LEU A . n 
A 1 980  LEU 980  980  980  LEU LEU A . n 
A 1 981  HIS 981  981  981  HIS HIS A . n 
A 1 982  PHE 982  982  982  PHE PHE A . n 
A 1 983  ASP 983  983  983  ASP ASP A . n 
A 1 984  TYR 984  984  984  TYR TYR A . n 
A 1 985  GLY 985  985  985  GLY GLY A . n 
A 1 986  GLU 986  986  986  GLU GLU A . n 
A 1 987  VAL 987  987  987  VAL VAL A . n 
A 1 988  ILE 988  988  988  ILE ILE A . n 
A 1 989  VAL 989  989  989  VAL VAL A . n 
A 1 990  ARG 990  990  990  ARG ARG A . n 
A 1 991  GLU 991  991  991  GLU GLU A . n 
A 1 992  GLY 992  992  992  GLY GLY A . n 
A 1 993  ASP 993  993  993  ASP ASP A . n 
A 1 994  GLU 994  994  994  GLU GLU A . n 
A 1 995  SER 995  995  995  SER SER A . n 
A 1 996  ASP 996  996  996  ASP ASP A . n 
A 1 997  GLY 997  997  997  GLY GLY A . n 
A 1 998  LEU 998  998  998  LEU LEU A . n 
A 1 999  PHE 999  999  999  PHE PHE A . n 
A 1 1000 LEU 1000 1000 1000 LEU LEU A . n 
A 1 1001 ILE 1001 1001 1001 ILE ILE A . n 
A 1 1002 VAL 1002 1002 1002 VAL VAL A . n 
A 1 1003 SER 1003 1003 1003 SER SER A . n 
A 1 1004 GLY 1004 1004 1004 GLY GLY A . n 
A 1 1005 LEU 1005 1005 1005 LEU LEU A . n 
A 1 1006 VAL 1006 1006 1006 VAL VAL A . n 
A 1 1007 LYS 1007 1007 1007 LYS LYS A . n 
A 1 1008 LEU 1008 1008 1008 LEU LEU A . n 
A 1 1009 TYR 1009 1009 1009 TYR TYR A . n 
A 1 1010 GLY 1010 1010 1010 GLY GLY A . n 
A 1 1011 LYS 1011 1011 1011 LYS LYS A . n 
A 1 1012 SER 1012 1012 ?    ?   ?   A . n 
A 1 1013 ALA 1013 1013 ?    ?   ?   A . n 
A 1 1014 PHE 1014 1014 ?    ?   ?   A . n 
A 1 1015 LEU 1015 1015 ?    ?   ?   A . n 
A 1 1016 ASP 1016 1016 ?    ?   ?   A . n 
A 1 1017 HIS 1017 1017 ?    ?   ?   A . n 
A 1 1018 ASP 1018 1018 ?    ?   ?   A . n 
A 1 1019 ASN 1019 1019 ?    ?   ?   A . n 
A 1 1020 PRO 1020 1020 ?    ?   ?   A . n 
A 1 1021 PRO 1021 1021 ?    ?   ?   A . n 
A 1 1022 VAL 1022 1022 ?    ?   ?   A . n 
A 1 1023 THR 1023 1023 ?    ?   ?   A . n 
A 1 1024 ALA 1024 1024 ?    ?   ?   A . n 
A 1 1025 GLY 1025 1025 ?    ?   ?   A . n 
A 1 1026 SER 1026 1026 ?    ?   ?   A . n 
A 1 1027 GLU 1027 1027 ?    ?   ?   A . n 
A 1 1028 GLU 1028 1028 ?    ?   ?   A . n 
A 1 1029 ASN 1029 1029 ?    ?   ?   A . n 
A 1 1030 GLU 1030 1030 ?    ?   ?   A . n 
A 1 1031 VAL 1031 1031 1031 VAL VAL A . n 
A 1 1032 PHE 1032 1032 1032 PHE PHE A . n 
A 1 1033 GLU 1033 1033 1033 GLU GLU A . n 
A 1 1034 ASP 1034 1034 1034 ASP ASP A . n 
A 1 1035 TYR 1035 1035 1035 TYR TYR A . n 
A 1 1036 LEU 1036 1036 1036 LEU LEU A . n 
A 1 1037 THR 1037 1037 1037 THR THR A . n 
A 1 1038 VAL 1038 1038 1038 VAL VAL A . n 
A 1 1039 GLY 1039 1039 1039 GLY GLY A . n 
A 1 1040 ASN 1040 1040 1040 ASN ASN A . n 
A 1 1041 VAL 1041 1041 1041 VAL VAL A . n 
A 1 1042 ILE 1042 1042 1042 ILE ILE A . n 
A 1 1043 GLY 1043 1043 1043 GLY GLY A . n 
A 1 1044 GLU 1044 1044 1044 GLU GLU A . n 
A 1 1045 MET 1045 1045 1045 MET MET A . n 
A 1 1046 GLY 1046 1046 1046 GLY GLY A . n 
A 1 1047 VAL 1047 1047 1047 VAL VAL A . n 
A 1 1048 LEU 1048 1048 1048 LEU LEU A . n 
A 1 1049 THR 1049 1049 1049 THR THR A . n 
A 1 1050 LYS 1050 1050 1050 LYS LYS A . n 
A 1 1051 LYS 1051 1051 1051 LYS LYS A . n 
A 1 1052 PRO 1052 1052 1052 PRO PRO A . n 
A 1 1053 ARG 1053 1053 1053 ARG ARG A . n 
A 1 1054 ASN 1054 1054 1054 ASN ASN A . n 
A 1 1055 ALA 1055 1055 1055 ALA ALA A . n 
A 1 1056 THR 1056 1056 1056 THR THR A . n 
A 1 1057 VAL 1057 1057 1057 VAL VAL A . n 
A 1 1058 THR 1058 1058 1058 THR THR A . n 
A 1 1059 CYS 1059 1059 1059 CYS CYS A . n 
A 1 1060 GLU 1060 1060 1060 GLU GLU A . n 
A 1 1061 THR 1061 1061 1061 THR THR A . n 
A 1 1062 THR 1062 1062 1062 THR THR A . n 
A 1 1063 VAL 1063 1063 1063 VAL VAL A . n 
A 1 1064 GLN 1064 1064 1064 GLN GLN A . n 
A 1 1065 VAL 1065 1065 1065 VAL VAL A . n 
A 1 1066 TYR 1066 1066 1066 TYR TYR A . n 
A 1 1067 PHE 1067 1067 1067 PHE PHE A . n 
A 1 1068 ILE 1068 1068 1068 ILE ILE A . n 
A 1 1069 THR 1069 1069 1069 THR THR A . n 
A 1 1070 ALA 1070 1070 1070 ALA ALA A . n 
A 1 1071 GLU 1071 1071 1071 GLU GLU A . n 
A 1 1072 ASP 1072 1072 1072 ASP ASP A . n 
A 1 1073 MET 1073 1073 1073 MET MET A . n 
A 1 1074 ASN 1074 1074 1074 ASN ASN A . n 
A 1 1075 ILE 1075 1075 1075 ILE ILE A . n 
A 1 1076 ALA 1076 1076 1076 ALA ALA A . n 
A 1 1077 ILE 1077 1077 1077 ILE ILE A . n 
A 1 1078 ASP 1078 1078 1078 ASP ASP A . n 
A 1 1079 THR 1079 1079 1079 THR THR A . n 
A 1 1080 PHE 1080 1080 1080 PHE PHE A . n 
A 1 1081 THR 1081 1081 1081 THR THR A . n 
A 1 1082 LEU 1082 1082 1082 LEU LEU A . n 
A 1 1083 TYR 1083 1083 1083 TYR TYR A . n 
A 1 1084 PRO 1084 1084 1084 PRO PRO A . n 
A 1 1085 SER 1085 1085 1085 SER SER A . n 
A 1 1086 LEU 1086 1086 1086 LEU LEU A . n 
A 1 1087 GLU 1087 1087 1087 GLU GLU A . n 
A 1 1088 TYR 1088 1088 1088 TYR TYR A . n 
A 1 1089 ARG 1089 1089 1089 ARG ARG A . n 
A 1 1090 LEU 1090 1090 1090 LEU LEU A . n 
A 1 1091 TRP 1091 1091 1091 TRP TRP A . n 
A 1 1092 ARG 1092 1092 1092 ARG ARG A . n 
A 1 1093 VAL 1093 1093 1093 VAL VAL A . n 
A 1 1094 VAL 1094 1094 1094 VAL VAL A . n 
A 1 1095 ALA 1095 1095 1095 ALA ALA A . n 
A 1 1096 ILE 1096 1096 1096 ILE ILE A . n 
A 1 1097 ARG 1097 1097 1097 ARG ARG A . n 
A 1 1098 ILE 1098 1098 1098 ILE ILE A . n 
A 1 1099 ALA 1099 1099 1099 ALA ALA A . n 
A 1 1100 THR 1100 1100 1100 THR THR A . n 
A 1 1101 PRO 1101 1101 1101 PRO PRO A . n 
A 1 1102 LEU 1102 1102 1102 LEU LEU A . n 
A 1 1103 ILE 1103 1103 1103 ILE ILE A . n 
A 1 1104 MET 1104 1104 1104 MET MET A . n 
A 1 1105 GLU 1105 1105 1105 GLU GLU A . n 
A 1 1106 GLN 1106 1106 1106 GLN GLN A . n 
A 1 1107 MET 1107 1107 1107 MET MET A . n 
A 1 1108 ALA 1108 1108 1108 ALA ALA A . n 
A 1 1109 PHE 1109 1109 1109 PHE PHE A . n 
A 1 1110 GLN 1110 1110 1110 GLN GLN A . n 
A 1 1111 GLY 1111 1111 1111 GLY GLY A . n 
A 1 1112 TRP 1112 1112 1112 TRP TRP A . n 
A 1 1113 THR 1113 1113 1113 THR THR A . n 
A 1 1114 GLN 1114 1114 1114 GLN GLN A . n 
A 1 1115 GLU 1115 1115 1115 GLU GLU A . n 
A 1 1116 LYS 1116 1116 1116 LYS LYS A . n 
A 1 1117 VAL 1117 1117 1117 VAL VAL A . n 
A 1 1118 LYS 1118 1118 1118 LYS LYS A . n 
A 1 1119 LEU 1119 1119 1119 LEU LEU A . n 
A 1 1120 HIS 1120 1120 1120 HIS HIS A . n 
A 1 1121 LEU 1121 1121 1121 LEU LEU A . n 
A 1 1122 GLU 1122 1122 1122 GLU GLU A . n 
A 1 1123 ARG 1123 1123 1123 ARG ARG A . n 
A 1 1124 GLY 1124 1124 1124 GLY GLY A . n 
A 1 1125 TYR 1125 1125 1125 TYR TYR A . n 
A 1 1126 LEU 1126 1126 1126 LEU LEU A . n 
A 1 1127 VAL 1127 1127 1127 VAL VAL A . n 
A 1 1128 ASP 1128 1128 1128 ASP ASP A . n 
A 1 1129 LEU 1129 1129 1129 LEU LEU A . n 
A 1 1130 ALA 1130 1130 1130 ALA ALA A . n 
A 1 1131 GLU 1131 1131 1131 GLU GLU A . n 
A 1 1132 SER 1132 1132 1132 SER SER A . n 
A 1 1133 HIS 1133 1133 1133 HIS HIS A . n 
A 1 1134 PHE 1134 1134 1134 PHE PHE A . n 
A 1 1135 GLN 1135 1135 1135 GLN GLN A . n 
A 1 1136 PHE 1136 1136 1136 PHE PHE A . n 
A 1 1137 ASN 1137 1137 1137 ASN ASN A . n 
A 1 1138 ILE 1138 1138 1138 ILE ILE A . n 
A 1 1139 ASP 1139 1139 1139 ASP ASP A . n 
A 1 1140 ALA 1140 1140 1140 ALA ALA A . n 
A 1 1141 THR 1141 1141 1141 THR THR A . n 
A 1 1142 LEU 1142 1142 1142 LEU LEU A . n 
A 1 1143 GLU 1143 1143 1143 GLU GLU A . n 
A 1 1144 ASP 1144 1144 1144 ASP ASP A . n 
A 1 1145 VAL 1145 1145 1145 VAL VAL A . n 
A 1 1146 ILE 1146 1146 1146 ILE ILE A . n 
A 1 1147 LEU 1147 1147 1147 LEU LEU A . n 
A 1 1148 ILE 1148 1148 1148 ILE ILE A . n 
A 1 1149 ASN 1149 1149 1149 ASN ASN A . n 
A 1 1150 GLY 1150 1150 1150 GLY GLY A . n 
A 1 1151 THR 1151 1151 1151 THR THR A . n 
A 1 1152 ALA 1152 1152 1152 ALA ALA A . n 
A 1 1153 TYR 1153 1153 1153 TYR TYR A . n 
A 1 1154 ASN 1154 1154 1154 ASN ASN A . n 
A 1 1155 ALA 1155 1155 1155 ALA ALA A . n 
A 1 1156 HIS 1156 1156 1156 HIS HIS A . n 
A 1 1157 THR 1157 1157 1157 THR THR A . n 
A 1 1158 ARG 1158 1158 1158 ARG ARG A . n 
A 1 1159 GLU 1159 1159 1159 GLU GLU A . n 
A 1 1160 GLU 1160 1160 1160 GLU GLU A . n 
A 1 1161 ILE 1161 1161 1161 ILE ILE A . n 
A 1 1162 ARG 1162 1162 1162 ARG ARG A . n 
A 1 1163 SER 1163 1163 1163 SER SER A . n 
A 1 1164 PRO 1164 1164 1164 PRO PRO A . n 
A 1 1165 CYS 1165 1165 1165 CYS CYS A . n 
A 1 1166 LEU 1166 1166 1166 LEU LEU A . n 
A 1 1167 ILE 1167 1167 1167 ILE ILE A . n 
A 1 1168 SER 1168 1168 1168 SER SER A . n 
A 1 1169 ARG 1169 1169 1169 ARG ARG A . n 
A 1 1170 THR 1170 1170 1170 THR THR A . n 
A 1 1171 VAL 1171 1171 1171 VAL VAL A . n 
A 1 1172 HIS 1172 1172 1172 HIS HIS A . n 
A 1 1173 LYS 1173 1173 1173 LYS LYS A . n 
A 1 1174 LEU 1174 1174 1174 LEU LEU A . n 
A 1 1175 THR 1175 1175 1175 THR THR A . n 
A 1 1176 PHE 1176 1176 1176 PHE PHE A . n 
A 1 1177 GLN 1177 1177 1177 GLN GLN A . n 
A 1 1178 TYR 1178 1178 1178 TYR TYR A . n 
A 1 1179 THR 1179 1179 1179 THR THR A . n 
A 1 1180 ALA 1180 1180 1180 ALA ALA A . n 
A 1 1181 THR 1181 1181 1181 THR THR A . n 
A 1 1182 GLU 1182 1182 1182 GLU GLU A . n 
A 1 1183 GLU 1183 1183 1183 GLU GLU A . n 
A 1 1184 PRO 1184 1184 1184 PRO PRO A . n 
A 1 1185 ARG 1185 1185 1185 ARG ARG A . n 
A 1 1186 LEU 1186 1186 1186 LEU LEU A . n 
A 1 1187 PHE 1187 1187 1187 PHE PHE A . n 
A 1 1188 VAL 1188 1188 1188 VAL VAL A . n 
A 1 1189 VAL 1189 1189 1189 VAL VAL A . n 
A 1 1190 ARG 1190 1190 1190 ARG ARG A . n 
A 1 1191 ASN 1191 1191 1191 ASN ASN A . n 
A 1 1192 ALA 1192 1192 1192 ALA ALA A . n 
A 1 1193 GLU 1193 1193 1193 GLU GLU A . n 
A 1 1194 TYR 1194 1194 ?    ?   ?   A . n 
A 1 1195 ASN 1195 1195 ?    ?   ?   A . n 
A 1 1196 GLY 1196 1196 ?    ?   ?   A . n 
A 1 1197 PRO 1197 1197 ?    ?   ?   A . n 
A 1 1198 ILE 1198 1198 ?    ?   ?   A . n 
A 1 1199 LEU 1199 1199 ?    ?   ?   A . n 
A 1 1200 ASP 1200 1200 ?    ?   ?   A . n 
A 1 1201 GLY 1201 1201 ?    ?   ?   A . n 
A 1 1202 ARG 1202 1202 ?    ?   ?   A . n 
A 1 1203 LEU 1203 1203 ?    ?   ?   A . n 
A 1 1204 ASP 1204 1204 ?    ?   ?   A . n 
A 1 1205 VAL 1205 1205 ?    ?   ?   A . n 
A 1 1206 ASP 1206 1206 ?    ?   ?   A . n 
A 1 1207 SER 1207 1207 ?    ?   ?   A . n 
A 1 1208 LYS 1208 1208 ?    ?   ?   A . n 
A 1 1209 ARG 1209 1209 ?    ?   ?   A . n 
A 1 1210 SER 1210 1210 ?    ?   ?   A . n 
A 1 1211 LEU 1211 1211 ?    ?   ?   A . n 
A 1 1212 ILE 1212 1212 ?    ?   ?   A . n 
A 1 1213 SER 1213 1213 ?    ?   ?   A . n 
A 1 1214 ILE 1214 1214 ?    ?   ?   A . n 
A 1 1215 THR 1215 1215 ?    ?   ?   A . n 
A 1 1216 GLU 1216 1216 ?    ?   ?   A . n 
A 1 1217 ILE 1217 1217 ?    ?   ?   A . n 
A 1 1218 SER 1218 1218 ?    ?   ?   A . n 
A 1 1219 SER 1219 1219 ?    ?   ?   A . n 
A 1 1220 ASN 1220 1220 ?    ?   ?   A . n 
A 1 1221 MET 1221 1221 ?    ?   ?   A . n 
A 1 1222 CYS 1222 1222 ?    ?   ?   A . n 
A 1 1223 LEU 1223 1223 ?    ?   ?   A . n 
A 1 1224 LYS 1224 1224 ?    ?   ?   A . n 
A 1 1225 HIS 1225 1225 ?    ?   ?   A . n 
A 1 1226 ALA 1226 1226 ?    ?   ?   A . n 
A 1 1227 ALA 1227 1227 ?    ?   ?   A . n 
A 1 1228 GLU 1228 1228 ?    ?   ?   A . n 
A 1 1229 LEU 1229 1229 ?    ?   ?   A . n 
A 1 1230 ARG 1230 1230 ?    ?   ?   A . n 
A 1 1231 GLN 1231 1231 ?    ?   ?   A . n 
A 1 1232 LYS 1232 1232 ?    ?   ?   A . n 
A 1 1233 ASN 1233 1233 ?    ?   ?   A . n 
A 1 1234 SER 1234 1234 ?    ?   ?   A . n 
A 1 1235 LYS 1235 1235 ?    ?   ?   A . n 
A 1 1236 VAL 1236 1236 ?    ?   ?   A . n 
A 1 1237 MET 1237 1237 ?    ?   ?   A . n 
A 1 1238 LEU 1238 1238 ?    ?   ?   A . n 
A 1 1239 SER 1239 1239 ?    ?   ?   A . n 
A 1 1240 ARG 1240 1240 ?    ?   ?   A . n 
A 1 1241 LYS 1241 1241 ?    ?   ?   A . n 
A 1 1242 SER 1242 1242 ?    ?   ?   A . n 
A 1 1243 SER 1243 1243 ?    ?   ?   A . n 
A 1 1244 GLY 1244 1244 ?    ?   ?   A . n 
A 1 1245 ALA 1245 1245 ?    ?   ?   A . n 
A 1 1246 ALA 1246 1246 ?    ?   ?   A . n 
A 1 1247 ALA 1247 1247 ?    ?   ?   A . n 
A 1 1248 LYS 1248 1248 ?    ?   ?   A . n 
A 1 1249 GLU 1249 1249 ?    ?   ?   A . n 
A 1 1250 GLU 1250 1250 ?    ?   ?   A . n 
A 1 1251 GLU 1251 1251 ?    ?   ?   A . n 
A 1 1252 ASP 1252 1252 ?    ?   ?   A . n 
A 1 1253 CYS 1253 1253 ?    ?   ?   A . n 
A 1 1254 ILE 1254 1254 ?    ?   ?   A . n 
A 1 1255 PRO 1255 1255 ?    ?   ?   A . n 
A 1 1256 ASN 1256 1256 ?    ?   ?   A . n 
A 1 1257 THR 1257 1257 ?    ?   ?   A . n 
A 1 1258 SER 1258 1258 ?    ?   ?   A . n 
A 1 1259 ASP 1259 1259 ?    ?   ?   A . n 
A 1 1260 VAL 1260 1260 ?    ?   ?   A . n 
A 1 1261 GLU 1261 1261 ?    ?   ?   A . n 
A 1 1262 GLN 1262 1262 ?    ?   ?   A . n 
A 1 1263 ALA 1263 1263 ?    ?   ?   A . n 
A 1 1264 ALA 1264 1264 ?    ?   ?   A . n 
A 1 1265 GLY 1265 1265 ?    ?   ?   A . n 
A 1 1266 VAL 1266 1266 ?    ?   ?   A . n 
A 1 1267 SER 1267 1267 ?    ?   ?   A . n 
A 1 1268 PRO 1268 1268 ?    ?   ?   A . n 
A 1 1269 SER 1269 1269 ?    ?   ?   A . n 
A 1 1270 VAL 1270 1270 ?    ?   ?   A . n 
A 1 1271 PRO 1271 1271 ?    ?   ?   A . n 
A 1 1272 THR 1272 1272 ?    ?   ?   A . n 
A 1 1273 LYS 1273 1273 ?    ?   ?   A . n 
A 1 1274 THR 1274 1274 ?    ?   ?   A . n 
A 1 1275 THR 1275 1275 ?    ?   ?   A . n 
A 1 1276 PRO 1276 1276 ?    ?   ?   A . n 
A 1 1277 LYS 1277 1277 ?    ?   ?   A . n 
A 1 1278 PRO 1278 1278 ?    ?   ?   A . n 
A 1 1279 LYS 1279 1279 ?    ?   ?   A . n 
A 1 1280 SER 1280 1280 ?    ?   ?   A . n 
A 1 1281 PHE 1281 1281 ?    ?   ?   A . n 
A 1 1282 LEU 1282 1282 ?    ?   ?   A . n 
A 1 1283 PRO 1283 1283 ?    ?   ?   A . n 
A 1 1284 SER 1284 1284 ?    ?   ?   A . n 
A 1 1285 LEU 1285 1285 ?    ?   ?   A . n 
A 1 1286 GLY 1286 1286 ?    ?   ?   A . n 
A 1 1287 LEU 1287 1287 ?    ?   ?   A . n 
A 1 1288 SER 1288 1288 ?    ?   ?   A . n 
A 1 1289 MET 1289 1289 ?    ?   ?   A . n 
A 1 1290 SER 1290 1290 ?    ?   ?   A . n 
A 1 1291 LYS 1291 1291 ?    ?   ?   A . n 
A 1 1292 GLU 1292 1292 ?    ?   ?   A . n 
A 1 1293 ARG 1293 1293 ?    ?   ?   A . n 
A 1 1294 VAL 1294 1294 ?    ?   ?   A . n 
A 1 1295 ASN 1295 1295 ?    ?   ?   A . n 
A 1 1296 GLY 1296 1296 ?    ?   ?   A . n 
A 1 1297 GLU 1297 1297 ?    ?   ?   A . n 
A 1 1298 ALA 1298 1298 ?    ?   ?   A . n 
A 1 1299 VAL 1299 1299 ?    ?   ?   A . n 
A 1 1300 GLU 1300 1300 ?    ?   ?   A . n 
A 1 1301 GLU 1301 1301 ?    ?   ?   A . n 
A 1 1302 SER 1302 1302 ?    ?   ?   A . n 
A 1 1303 PRO 1303 1303 ?    ?   ?   A . n 
A 1 1304 VAL 1304 1304 ?    ?   ?   A . n 
A 1 1305 LYS 1305 1305 ?    ?   ?   A . n 
A 1 1306 THR 1306 1306 ?    ?   ?   A . n 
A 1 1307 LYS 1307 1307 ?    ?   ?   A . n 
A 1 1308 GLN 1308 1308 ?    ?   ?   A . n 
A 1 1309 GLY 1309 1309 ?    ?   ?   A . n 
A 1 1310 GLU 1310 1310 ?    ?   ?   A . n 
A 1 1311 GLU 1311 1311 ?    ?   ?   A . n 
A 1 1312 THR 1312 1312 ?    ?   ?   A . n 
A 1 1313 PRO 1313 1313 ?    ?   ?   A . n 
A 1 1314 GLU 1314 1314 ?    ?   ?   A . n 
A 1 1315 THR 1315 1315 ?    ?   ?   A . n 
A 1 1316 GLU 1316 1316 ?    ?   ?   A . n 
A 1 1317 GLU 1317 1317 ?    ?   ?   A . n 
A 1 1318 GLY 1318 1318 ?    ?   ?   A . n 
A 1 1319 ALA 1319 1319 ?    ?   ?   A . n 
A 1 1320 ALA 1320 1320 ?    ?   ?   A . n 
A 1 1321 PRO 1321 1321 ?    ?   ?   A . n 
A 1 1322 ARG 1322 1322 ?    ?   ?   A . n 
A 1 1323 VAL 1323 1323 ?    ?   ?   A . n 
A 1 1324 ASN 1324 1324 ?    ?   ?   A . n 
A 1 1325 VAL 1325 1325 ?    ?   ?   A . n 
B 1 1    MET 1    1    ?    ?   ?   B . n 
B 1 2    LYS 2    2    ?    ?   ?   B . n 
B 1 3    LYS 3    3    ?    ?   ?   B . n 
B 1 4    ARG 4    4    ?    ?   ?   B . n 
B 1 5    VAL 5    5    ?    ?   ?   B . n 
B 1 6    VAL 6    6    ?    ?   ?   B . n 
B 1 7    LYS 7    7    ?    ?   ?   B . n 
B 1 8    LEU 8    8    ?    ?   ?   B . n 
B 1 9    ARG 9    9    ?    ?   ?   B . n 
B 1 10   GLU 10   10   ?    ?   ?   B . n 
B 1 11   LEU 11   11   ?    ?   ?   B . n 
B 1 12   VAL 12   12   ?    ?   ?   B . n 
B 1 13   PRO 13   13   ?    ?   ?   B . n 
B 1 14   ALA 14   14   ?    ?   ?   B . n 
B 1 15   VAL 15   15   ?    ?   ?   B . n 
B 1 16   ALA 16   16   ?    ?   ?   B . n 
B 1 17   ALA 17   17   ?    ?   ?   B . n 
B 1 18   LEU 18   18   ?    ?   ?   B . n 
B 1 19   ALA 19   19   ?    ?   ?   B . n 
B 1 20   VAL 20   20   ?    ?   ?   B . n 
B 1 21   ALA 21   21   ?    ?   ?   B . n 
B 1 22   VAL 22   22   ?    ?   ?   B . n 
B 1 23   LEU 23   23   ?    ?   ?   B . n 
B 1 24   ILE 24   24   ?    ?   ?   B . n 
B 1 25   GLN 25   25   ?    ?   ?   B . n 
B 1 26   SER 26   26   ?    ?   ?   B . n 
B 1 27   ALA 27   27   ?    ?   ?   B . n 
B 1 28   THR 28   28   ?    ?   ?   B . n 
B 1 29   GLY 29   29   ?    ?   ?   B . n 
B 1 30   SER 30   30   ?    ?   ?   B . n 
B 1 31   SER 31   31   ?    ?   ?   B . n 
B 1 32   GLY 32   32   ?    ?   ?   B . n 
B 1 33   GLY 33   33   ?    ?   ?   B . n 
B 1 34   SER 34   34   ?    ?   ?   B . n 
B 1 35   GLY 35   35   ?    ?   ?   B . n 
B 1 36   HIS 36   36   ?    ?   ?   B . n 
B 1 37   THR 37   37   ?    ?   ?   B . n 
B 1 38   PRO 38   38   ?    ?   ?   B . n 
B 1 39   THR 39   39   ?    ?   ?   B . n 
B 1 40   THR 40   40   ?    ?   ?   B . n 
B 1 41   GLN 41   41   ?    ?   ?   B . n 
B 1 42   ALA 42   42   ?    ?   ?   B . n 
B 1 43   THR 43   43   ?    ?   ?   B . n 
B 1 44   HIS 44   44   ?    ?   ?   B . n 
B 1 45   ALA 45   45   ?    ?   ?   B . n 
B 1 46   ASP 46   46   ?    ?   ?   B . n 
B 1 47   ASP 47   47   ?    ?   ?   B . n 
B 1 48   HIS 48   48   ?    ?   ?   B . n 
B 1 49   ASP 49   49   ?    ?   ?   B . n 
B 1 50   LEU 50   50   ?    ?   ?   B . n 
B 1 51   THR 51   51   ?    ?   ?   B . n 
B 1 52   THR 52   52   ?    ?   ?   B . n 
B 1 53   HIS 53   53   ?    ?   ?   B . n 
B 1 54   ASN 54   54   ?    ?   ?   B . n 
B 1 55   GLY 55   55   ?    ?   ?   B . n 
B 1 56   THR 56   56   ?    ?   ?   B . n 
B 1 57   GLU 57   57   ?    ?   ?   B . n 
B 1 58   GLU 58   58   ?    ?   ?   B . n 
B 1 59   HIS 59   59   ?    ?   ?   B . n 
B 1 60   ASP 60   60   ?    ?   ?   B . n 
B 1 61   ASP 61   61   ?    ?   ?   B . n 
B 1 62   GLY 62   62   ?    ?   ?   B . n 
B 1 63   HIS 63   63   ?    ?   ?   B . n 
B 1 64   ASP 64   64   ?    ?   ?   B . n 
B 1 65   ASP 65   65   ?    ?   ?   B . n 
B 1 66   GLY 66   66   ?    ?   ?   B . n 
B 1 67   HIS 67   67   ?    ?   ?   B . n 
B 1 68   ASP 68   68   ?    ?   ?   B . n 
B 1 69   ASP 69   69   ?    ?   ?   B . n 
B 1 70   LEU 70   70   ?    ?   ?   B . n 
B 1 71   HIS 71   71   ?    ?   ?   B . n 
B 1 72   ALA 72   72   ?    ?   ?   B . n 
B 1 73   HIS 73   73   ?    ?   ?   B . n 
B 1 74   ALA 74   74   74   ALA ALA B . n 
B 1 75   PRO 75   75   75   PRO PRO B . n 
B 1 76   LYS 76   76   76   LYS LYS B . n 
B 1 77   VAL 77   77   77   VAL VAL B . n 
B 1 78   ILE 78   78   78   ILE ILE B . n 
B 1 79   VAL 79   79   79   VAL VAL B . n 
B 1 80   PHE 80   80   80   PHE PHE B . n 
B 1 81   ILE 81   81   81   ILE ILE B . n 
B 1 82   SER 82   82   82   SER SER B . n 
B 1 83   GLY 83   83   83   GLY GLY B . n 
B 1 84   SER 84   84   84   SER SER B . n 
B 1 85   CYS 85   85   85   CYS CYS B . n 
B 1 86   LEU 86   86   86   LEU LEU B . n 
B 1 87   PHE 87   87   87   PHE PHE B . n 
B 1 88   GLY 88   88   88   GLY GLY B . n 
B 1 89   ALA 89   89   89   ALA ALA B . n 
B 1 90   ILE 90   90   90   ILE ILE B . n 
B 1 91   SER 91   91   91   SER SER B . n 
B 1 92   ARG 92   92   92   ARG ARG B . n 
B 1 93   SER 93   93   93   SER SER B . n 
B 1 94   LEU 94   94   94   LEU LEU B . n 
B 1 95   PHE 95   95   95   PHE PHE B . n 
B 1 96   LYS 96   96   96   LYS LYS B . n 
B 1 97   LYS 97   97   97   LYS LYS B . n 
B 1 98   LEU 98   98   98   LEU LEU B . n 
B 1 99   PRO 99   99   99   PRO PRO B . n 
B 1 100  ILE 100  100  100  ILE ILE B . n 
B 1 101  PRO 101  101  101  PRO PRO B . n 
B 1 102  TYR 102  102  102  TYR TYR B . n 
B 1 103  THR 103  103  103  THR THR B . n 
B 1 104  VAL 104  104  104  VAL VAL B . n 
B 1 105  VAL 105  105  105  VAL VAL B . n 
B 1 106  LEU 106  106  106  LEU LEU B . n 
B 1 107  LEU 107  107  107  LEU LEU B . n 
B 1 108  ILE 108  108  108  ILE ILE B . n 
B 1 109  LEU 109  109  109  LEU LEU B . n 
B 1 110  GLY 110  110  110  GLY GLY B . n 
B 1 111  ALA 111  111  111  ALA ALA B . n 
B 1 112  ILE 112  112  112  ILE ILE B . n 
B 1 113  LEU 113  113  113  LEU LEU B . n 
B 1 114  GLY 114  114  114  GLY GLY B . n 
B 1 115  VAL 115  115  115  VAL VAL B . n 
B 1 116  VAL 116  116  116  VAL VAL B . n 
B 1 117  ALA 117  117  117  ALA ALA B . n 
B 1 118  SER 118  118  118  SER SER B . n 
B 1 119  ASN 119  119  119  ASN ASN B . n 
B 1 120  VAL 120  120  120  VAL VAL B . n 
B 1 121  PRO 121  121  121  PRO PRO B . n 
B 1 122  LEU 122  122  122  LEU LEU B . n 
B 1 123  VAL 123  123  123  VAL VAL B . n 
B 1 124  GLU 124  124  124  GLU GLU B . n 
B 1 125  GLU 125  125  125  GLU GLU B . n 
B 1 126  HIS 126  126  126  HIS HIS B . n 
B 1 127  THR 127  127  127  THR THR B . n 
B 1 128  ARG 128  128  128  ARG ARG B . n 
B 1 129  ASP 129  129  129  ASP ASP B . n 
B 1 130  VAL 130  130  130  VAL VAL B . n 
B 1 131  ALA 131  131  131  ALA ALA B . n 
B 1 132  HIS 132  132  132  HIS HIS B . n 
B 1 133  MET 133  133  133  MET MET B . n 
B 1 134  ASP 134  134  134  ASP ASP B . n 
B 1 135  PRO 135  135  135  PRO PRO B . n 
B 1 136  HIS 136  136  136  HIS HIS B . n 
B 1 137  VAL 137  137  137  VAL VAL B . n 
B 1 138  LEU 138  138  138  LEU LEU B . n 
B 1 139  LEU 139  139  139  LEU LEU B . n 
B 1 140  GLN 140  140  140  GLN GLN B . n 
B 1 141  ILE 141  141  141  ILE ILE B . n 
B 1 142  PHE 142  142  142  PHE PHE B . n 
B 1 143  LEU 143  143  143  LEU LEU B . n 
B 1 144  PRO 144  144  144  PRO PRO B . n 
B 1 145  VAL 145  145  145  VAL VAL B . n 
B 1 146  LEU 146  146  146  LEU LEU B . n 
B 1 147  ILE 147  147  147  ILE ILE B . n 
B 1 148  PHE 148  148  148  PHE PHE B . n 
B 1 149  GLU 149  149  149  GLU GLU B . n 
B 1 150  SER 150  150  150  SER SER B . n 
B 1 151  ALA 151  151  151  ALA ALA B . n 
B 1 152  PHE 152  152  152  PHE PHE B . n 
B 1 153  ALA 153  153  153  ALA ALA B . n 
B 1 154  MET 154  154  154  MET MET B . n 
B 1 155  ASP 155  155  155  ASP ASP B . n 
B 1 156  VAL 156  156  156  VAL VAL B . n 
B 1 157  HIS 157  157  157  HIS HIS B . n 
B 1 158  THR 158  158  158  THR THR B . n 
B 1 159  PHE 159  159  159  PHE PHE B . n 
B 1 160  MET 160  160  160  MET MET B . n 
B 1 161  ARG 161  161  161  ARG ARG B . n 
B 1 162  SER 162  162  162  SER SER B . n 
B 1 163  PHE 163  163  163  PHE PHE B . n 
B 1 164  SER 164  164  164  SER SER B . n 
B 1 165  GLN 165  165  165  GLN GLN B . n 
B 1 166  VAL 166  166  166  VAL VAL B . n 
B 1 167  CYS 167  167  167  CYS CYS B . n 
B 1 168  ILE 168  168  168  ILE ILE B . n 
B 1 169  LEU 169  169  169  LEU LEU B . n 
B 1 170  ALA 170  170  170  ALA ALA B . n 
B 1 171  LEU 171  171  171  LEU LEU B . n 
B 1 172  PHE 172  172  172  PHE PHE B . n 
B 1 173  GLY 173  173  173  GLY GLY B . n 
B 1 174  LEU 174  174  174  LEU LEU B . n 
B 1 175  VAL 175  175  175  VAL VAL B . n 
B 1 176  VAL 176  176  176  VAL VAL B . n 
B 1 177  ALA 177  177  177  ALA ALA B . n 
B 1 178  SER 178  178  178  SER SER B . n 
B 1 179  VAL 179  179  179  VAL VAL B . n 
B 1 180  LEU 180  180  180  LEU LEU B . n 
B 1 181  THR 181  181  181  THR THR B . n 
B 1 182  ALA 182  182  182  ALA ALA B . n 
B 1 183  VAL 183  183  183  VAL VAL B . n 
B 1 184  LEU 184  184  184  LEU LEU B . n 
B 1 185  ALA 185  185  185  ALA ALA B . n 
B 1 186  MET 186  186  186  MET MET B . n 
B 1 187  ASN 187  187  187  ASN ASN B . n 
B 1 188  LEU 188  188  188  LEU LEU B . n 
B 1 189  PHE 189  189  189  PHE PHE B . n 
B 1 190  ASN 190  190  190  ASN ASN B . n 
B 1 191  TYR 191  191  191  TYR TYR B . n 
B 1 192  ASN 192  192  192  ASN ASN B . n 
B 1 193  TRP 193  193  193  TRP TRP B . n 
B 1 194  ASN 194  194  194  ASN ASN B . n 
B 1 195  PHE 195  195  195  PHE PHE B . n 
B 1 196  SER 196  196  196  SER SER B . n 
B 1 197  GLU 197  197  197  GLU GLU B . n 
B 1 198  ALA 198  198  198  ALA ALA B . n 
B 1 199  MET 199  199  199  MET MET B . n 
B 1 200  MET 200  200  200  MET MET B . n 
B 1 201  PHE 201  201  201  PHE PHE B . n 
B 1 202  GLY 202  202  202  GLY GLY B . n 
B 1 203  ALA 203  203  203  ALA ALA B . n 
B 1 204  ILE 204  204  204  ILE ILE B . n 
B 1 205  MET 205  205  205  MET MET B . n 
B 1 206  SER 206  206  206  SER SER B . n 
B 1 207  ALA 207  207  207  ALA ALA B . n 
B 1 208  THR 208  208  208  THR THR B . n 
B 1 209  ASP 209  209  209  ASP ASP B . n 
B 1 210  PRO 210  210  210  PRO PRO B . n 
B 1 211  VAL 211  211  211  VAL VAL B . n 
B 1 212  ALA 212  212  212  ALA ALA B . n 
B 1 213  VAL 213  213  213  VAL VAL B . n 
B 1 214  VAL 214  214  214  VAL VAL B . n 
B 1 215  ALA 215  215  215  ALA ALA B . n 
B 1 216  LEU 216  216  216  LEU LEU B . n 
B 1 217  LEU 217  217  217  LEU LEU B . n 
B 1 218  LYS 218  218  218  LYS LYS B . n 
B 1 219  ASP 219  219  219  ASP ASP B . n 
B 1 220  LEU 220  220  220  LEU LEU B . n 
B 1 221  GLY 221  221  221  GLY GLY B . n 
B 1 222  ALA 222  222  222  ALA ALA B . n 
B 1 223  SER 223  223  223  SER SER B . n 
B 1 224  LYS 224  224  224  LYS LYS B . n 
B 1 225  GLN 225  225  225  GLN GLN B . n 
B 1 226  LEU 226  226  226  LEU LEU B . n 
B 1 227  GLY 227  227  227  GLY GLY B . n 
B 1 228  THR 228  228  228  THR THR B . n 
B 1 229  ILE 229  229  229  ILE ILE B . n 
B 1 230  ILE 230  230  230  ILE ILE B . n 
B 1 231  GLU 231  231  231  GLU GLU B . n 
B 1 232  GLY 232  232  232  GLY GLY B . n 
B 1 233  GLU 233  233  233  GLU GLU B . n 
B 1 234  SER 234  234  234  SER SER B . n 
B 1 235  LEU 235  235  235  LEU LEU B . n 
B 1 236  LEU 236  236  236  LEU LEU B . n 
B 1 237  ASN 237  237  237  ASN ASN B . n 
B 1 238  ASP 238  238  238  ASP ASP B . n 
B 1 239  GLY 239  239  239  GLY GLY B . n 
B 1 240  CYS 240  240  240  CYS CYS B . n 
B 1 241  ALA 241  241  241  ALA ALA B . n 
B 1 242  ILE 242  242  242  ILE ILE B . n 
B 1 243  VAL 243  243  243  VAL VAL B . n 
B 1 244  ILE 244  244  244  ILE ILE B . n 
B 1 245  PHE 245  245  245  PHE PHE B . n 
B 1 246  ASN 246  246  246  ASN ASN B . n 
B 1 247  VAL 247  247  247  VAL VAL B . n 
B 1 248  PHE 248  248  248  PHE PHE B . n 
B 1 249  MET 249  249  249  MET MET B . n 
B 1 250  LYS 250  250  250  LYS LYS B . n 
B 1 251  MET 251  251  251  MET MET B . n 
B 1 252  VAL 252  252  252  VAL VAL B . n 
B 1 253  PHE 253  253  253  PHE PHE B . n 
B 1 254  PHE 254  254  254  PHE PHE B . n 
B 1 255  PRO 255  255  255  PRO PRO B . n 
B 1 256  GLN 256  256  256  GLN GLN B . n 
B 1 257  LEU 257  257  257  LEU LEU B . n 
B 1 258  THR 258  258  258  THR THR B . n 
B 1 259  SER 259  259  259  SER SER B . n 
B 1 260  THR 260  260  260  THR THR B . n 
B 1 261  VAL 261  261  261  VAL VAL B . n 
B 1 262  GLY 262  262  262  GLY GLY B . n 
B 1 263  GLN 263  263  263  GLN GLN B . n 
B 1 264  ASN 264  264  264  ASN ASN B . n 
B 1 265  VAL 265  265  265  VAL VAL B . n 
B 1 266  LEU 266  266  266  LEU LEU B . n 
B 1 267  TYR 267  267  267  TYR TYR B . n 
B 1 268  PHE 268  268  268  PHE PHE B . n 
B 1 269  LEU 269  269  269  LEU LEU B . n 
B 1 270  GLN 270  270  270  GLN GLN B . n 
B 1 271  VAL 271  271  271  VAL VAL B . n 
B 1 272  ALA 272  272  272  ALA ALA B . n 
B 1 273  VAL 273  273  273  VAL VAL B . n 
B 1 274  ALA 274  274  274  ALA ALA B . n 
B 1 275  GLY 275  275  275  GLY GLY B . n 
B 1 276  PRO 276  276  276  PRO PRO B . n 
B 1 277  LEU 277  277  277  LEU LEU B . n 
B 1 278  TRP 278  278  278  TRP TRP B . n 
B 1 279  GLY 279  279  279  GLY GLY B . n 
B 1 280  TYR 280  280  280  TYR TYR B . n 
B 1 281  ALA 281  281  281  ALA ALA B . n 
B 1 282  VAL 282  282  282  VAL VAL B . n 
B 1 283  ALA 283  283  283  ALA ALA B . n 
B 1 284  LYS 284  284  284  LYS LYS B . n 
B 1 285  VAL 285  285  285  VAL VAL B . n 
B 1 286  THR 286  286  286  THR THR B . n 
B 1 287  VAL 287  287  287  VAL VAL B . n 
B 1 288  PHE 288  288  288  PHE PHE B . n 
B 1 289  PHE 289  289  289  PHE PHE B . n 
B 1 290  LEU 290  290  290  LEU LEU B . n 
B 1 291  SER 291  291  291  SER SER B . n 
B 1 292  HIS 292  292  292  HIS HIS B . n 
B 1 293  ILE 293  293  293  ILE ILE B . n 
B 1 294  PHE 294  294  294  PHE PHE B . n 
B 1 295  ASN 295  295  295  ASN ASN B . n 
B 1 296  ASP 296  296  296  ASP ASP B . n 
B 1 297  ALA 297  297  297  ALA ALA B . n 
B 1 298  LEU 298  298  298  LEU LEU B . n 
B 1 299  VAL 299  299  299  VAL VAL B . n 
B 1 300  GLU 300  300  300  GLU GLU B . n 
B 1 301  ILE 301  301  301  ILE ILE B . n 
B 1 302  THR 302  302  302  THR THR B . n 
B 1 303  ILE 303  303  303  ILE ILE B . n 
B 1 304  THR 304  304  304  THR THR B . n 
B 1 305  LEU 305  305  305  LEU LEU B . n 
B 1 306  ALA 306  306  306  ALA ALA B . n 
B 1 307  ALA 307  307  307  ALA ALA B . n 
B 1 308  THR 308  308  308  THR THR B . n 
B 1 309  TYR 309  309  309  TYR TYR B . n 
B 1 310  LEU 310  310  310  LEU LEU B . n 
B 1 311  THR 311  311  311  THR THR B . n 
B 1 312  TYR 312  312  312  TYR TYR B . n 
B 1 313  TYR 313  313  313  TYR TYR B . n 
B 1 314  ILE 314  314  314  ILE ILE B . n 
B 1 315  GLY 315  315  315  GLY GLY B . n 
B 1 316  ASP 316  316  316  ASP ASP B . n 
B 1 317  ILE 317  317  317  ILE ILE B . n 
B 1 318  TRP 318  318  318  TRP TRP B . n 
B 1 319  LEU 319  319  319  LEU LEU B . n 
B 1 320  GLU 320  320  320  GLU GLU B . n 
B 1 321  VAL 321  321  321  VAL VAL B . n 
B 1 322  SER 322  322  322  SER SER B . n 
B 1 323  GLY 323  323  323  GLY GLY B . n 
B 1 324  VAL 324  324  324  VAL VAL B . n 
B 1 325  LEU 325  325  325  LEU LEU B . n 
B 1 326  ALA 326  326  326  ALA ALA B . n 
B 1 327  VAL 327  327  327  VAL VAL B . n 
B 1 328  VAL 328  328  328  VAL VAL B . n 
B 1 329  VAL 329  329  329  VAL VAL B . n 
B 1 330  LEU 330  330  330  LEU LEU B . n 
B 1 331  GLY 331  331  331  GLY GLY B . n 
B 1 332  LEU 332  332  332  LEU LEU B . n 
B 1 333  ILE 333  333  333  ILE ILE B . n 
B 1 334  VAL 334  334  334  VAL VAL B . n 
B 1 335  ASN 335  335  335  ASN ASN B . n 
B 1 336  ALA 336  336  336  ALA ALA B . n 
B 1 337  GLU 337  337  337  GLU GLU B . n 
B 1 338  LYS 338  338  338  LYS LYS B . n 
B 1 339  THR 339  339  339  THR THR B . n 
B 1 340  SER 340  340  340  SER SER B . n 
B 1 341  ILE 341  341  341  ILE ILE B . n 
B 1 342  SER 342  342  342  SER SER B . n 
B 1 343  PRO 343  343  343  PRO PRO B . n 
B 1 344  GLU 344  344  344  GLU GLU B . n 
B 1 345  VAL 345  345  345  VAL VAL B . n 
B 1 346  GLU 346  346  346  GLU GLU B . n 
B 1 347  VAL 347  347  347  VAL VAL B . n 
B 1 348  PHE 348  348  348  PHE PHE B . n 
B 1 349  LEU 349  349  349  LEU LEU B . n 
B 1 350  HIS 350  350  350  HIS HIS B . n 
B 1 351  ARG 351  351  351  ARG ARG B . n 
B 1 352  PHE 352  352  352  PHE PHE B . n 
B 1 353  TRP 353  353  353  TRP TRP B . n 
B 1 354  GLU 354  354  354  GLU GLU B . n 
B 1 355  MET 355  355  355  MET MET B . n 
B 1 356  LEU 356  356  356  LEU LEU B . n 
B 1 357  ALA 357  357  357  ALA ALA B . n 
B 1 358  TYR 358  358  358  TYR TYR B . n 
B 1 359  LEU 359  359  359  LEU LEU B . n 
B 1 360  ALA 360  360  360  ALA ALA B . n 
B 1 361  ASN 361  361  361  ASN ASN B . n 
B 1 362  THR 362  362  362  THR THR B . n 
B 1 363  LEU 363  363  363  LEU LEU B . n 
B 1 364  ILE 364  364  364  ILE ILE B . n 
B 1 365  PHE 365  365  365  PHE PHE B . n 
B 1 366  MET 366  366  366  MET MET B . n 
B 1 367  MET 367  367  367  MET MET B . n 
B 1 368  VAL 368  368  368  VAL VAL B . n 
B 1 369  GLY 369  369  369  GLY GLY B . n 
B 1 370  VAL 370  370  370  VAL VAL B . n 
B 1 371  VAL 371  371  371  VAL VAL B . n 
B 1 372  VAL 372  372  372  VAL VAL B . n 
B 1 373  THR 373  373  373  THR THR B . n 
B 1 374  GLN 374  374  374  GLN GLN B . n 
B 1 375  LYS 375  375  375  LYS LYS B . n 
B 1 376  ALA 376  376  376  ALA ALA B . n 
B 1 377  LEU 377  377  377  LEU LEU B . n 
B 1 378  VAL 378  378  378  VAL VAL B . n 
B 1 379  ALA 379  379  379  ALA ALA B . n 
B 1 380  VAL 380  380  380  VAL VAL B . n 
B 1 381  ASP 381  381  381  ASP ASP B . n 
B 1 382  LYS 382  382  382  LYS LYS B . n 
B 1 383  MET 383  383  383  MET MET B . n 
B 1 384  ASP 384  384  384  ASP ASP B . n 
B 1 385  TRP 385  385  385  TRP TRP B . n 
B 1 386  PHE 386  386  386  PHE PHE B . n 
B 1 387  TYR 387  387  387  TYR TYR B . n 
B 1 388  LEU 388  388  388  LEU LEU B . n 
B 1 389  ILE 389  389  389  ILE ILE B . n 
B 1 390  ILE 390  390  390  ILE ILE B . n 
B 1 391  LEU 391  391  391  LEU LEU B . n 
B 1 392  TYR 392  392  392  TYR TYR B . n 
B 1 393  LEU 393  393  393  LEU LEU B . n 
B 1 394  ALA 394  394  394  ALA ALA B . n 
B 1 395  ILE 395  395  395  ILE ILE B . n 
B 1 396  THR 396  396  396  THR THR B . n 
B 1 397  ILE 397  397  397  ILE ILE B . n 
B 1 398  ILE 398  398  398  ILE ILE B . n 
B 1 399  ALA 399  399  399  ALA ALA B . n 
B 1 400  GLY 400  400  400  GLY GLY B . n 
B 1 401  MET 401  401  401  MET MET B . n 
B 1 402  VAL 402  402  402  VAL VAL B . n 
B 1 403  ILE 403  403  403  ILE ILE B . n 
B 1 404  SER 404  404  404  SER SER B . n 
B 1 405  LEU 405  405  405  LEU LEU B . n 
B 1 406  PHE 406  406  406  PHE PHE B . n 
B 1 407  SER 407  407  407  SER SER B . n 
B 1 408  PRO 408  408  408  PRO PRO B . n 
B 1 409  ILE 409  409  409  ILE ILE B . n 
B 1 410  LEU 410  410  410  LEU LEU B . n 
B 1 411  SER 411  411  411  SER SER B . n 
B 1 412  ARG 412  412  412  ARG ARG B . n 
B 1 413  ILE 413  413  413  ILE ILE B . n 
B 1 414  GLY 414  414  414  GLY GLY B . n 
B 1 415  TYR 415  415  415  TYR TYR B . n 
B 1 416  GLY 416  416  416  GLY GLY B . n 
B 1 417  LEU 417  417  417  LEU LEU B . n 
B 1 418  THR 418  418  418  THR THR B . n 
B 1 419  TRP 419  419  419  TRP TRP B . n 
B 1 420  ARG 420  420  420  ARG ARG B . n 
B 1 421  ASN 421  421  421  ASN ASN B . n 
B 1 422  ALA 422  422  422  ALA ALA B . n 
B 1 423  VAL 423  423  423  VAL VAL B . n 
B 1 424  ILE 424  424  424  ILE ILE B . n 
B 1 425  MET 425  425  425  MET MET B . n 
B 1 426  THR 426  426  426  THR THR B . n 
B 1 427  TRP 427  427  427  TRP TRP B . n 
B 1 428  GLY 428  428  428  GLY GLY B . n 
B 1 429  GLY 429  429  429  GLY GLY B . n 
B 1 430  LEU 430  430  430  LEU LEU B . n 
B 1 431  ARG 431  431  431  ARG ARG B . n 
B 1 432  GLY 432  432  432  GLY GLY B . n 
B 1 433  ALA 433  433  433  ALA ALA B . n 
B 1 434  VAL 434  434  434  VAL VAL B . n 
B 1 435  GLY 435  435  435  GLY GLY B . n 
B 1 436  LEU 436  436  436  LEU LEU B . n 
B 1 437  ALA 437  437  437  ALA ALA B . n 
B 1 438  LEU 438  438  438  LEU LEU B . n 
B 1 439  ALA 439  439  439  ALA ALA B . n 
B 1 440  LEU 440  440  440  LEU LEU B . n 
B 1 441  VAL 441  441  441  VAL VAL B . n 
B 1 442  VAL 442  442  442  VAL VAL B . n 
B 1 443  GLU 443  443  443  GLU GLU B . n 
B 1 444  ASN 444  444  444  ASN ASN B . n 
B 1 445  LEU 445  445  445  LEU LEU B . n 
B 1 446  ALA 446  446  446  ALA ALA B . n 
B 1 447  GLY 447  447  447  GLY GLY B . n 
B 1 448  ASN 448  448  448  ASN ASN B . n 
B 1 449  ASP 449  449  449  ASP ASP B . n 
B 1 450  VAL 450  450  450  VAL VAL B . n 
B 1 451  ILE 451  451  451  ILE ILE B . n 
B 1 452  GLY 452  452  452  GLY GLY B . n 
B 1 453  SER 453  453  453  SER SER B . n 
B 1 454  LYS 454  454  454  LYS LYS B . n 
B 1 455  PHE 455  455  455  PHE PHE B . n 
B 1 456  LEU 456  456  456  LEU LEU B . n 
B 1 457  PHE 457  457  457  PHE PHE B . n 
B 1 458  HIS 458  458  458  HIS HIS B . n 
B 1 459  THR 459  459  459  THR THR B . n 
B 1 460  ALA 460  460  460  ALA ALA B . n 
B 1 461  GLY 461  461  461  GLY GLY B . n 
B 1 462  ILE 462  462  462  ILE ILE B . n 
B 1 463  VAL 463  463  463  VAL VAL B . n 
B 1 464  VAL 464  464  464  VAL VAL B . n 
B 1 465  LEU 465  465  465  LEU LEU B . n 
B 1 466  THR 466  466  466  THR THR B . n 
B 1 467  LEU 467  467  467  LEU LEU B . n 
B 1 468  VAL 468  468  468  VAL VAL B . n 
B 1 469  ILE 469  469  469  ILE ILE B . n 
B 1 470  ASN 470  470  470  ASN ASN B . n 
B 1 471  ALA 471  471  471  ALA ALA B . n 
B 1 472  THR 472  472  472  THR THR B . n 
B 1 473  THR 473  473  473  THR THR B . n 
B 1 474  ILE 474  474  474  ILE ILE B . n 
B 1 475  GLN 475  475  475  GLN GLN B . n 
B 1 476  THR 476  476  476  THR THR B . n 
B 1 477  LEU 477  477  477  LEU LEU B . n 
B 1 478  LEU 478  478  478  LEU LEU B . n 
B 1 479  ARG 479  479  479  ARG ARG B . n 
B 1 480  ILE 480  480  480  ILE ILE B . n 
B 1 481  LEU 481  481  481  LEU LEU B . n 
B 1 482  GLY 482  482  482  GLY GLY B . n 
B 1 483  MET 483  483  483  MET MET B . n 
B 1 484  SER 484  484  484  SER SER B . n 
B 1 485  ASP 485  485  485  ASP ASP B . n 
B 1 486  ILE 486  486  486  ILE ILE B . n 
B 1 487  SER 487  487  487  SER SER B . n 
B 1 488  ILE 488  488  488  ILE ILE B . n 
B 1 489  PRO 489  489  489  PRO PRO B . n 
B 1 490  LYS 490  490  490  LYS LYS B . n 
B 1 491  ARG 491  491  491  ARG ARG B . n 
B 1 492  LEU 492  492  492  LEU LEU B . n 
B 1 493  ALA 493  493  493  ALA ALA B . n 
B 1 494  MET 494  494  494  MET MET B . n 
B 1 495  ALA 495  495  495  ALA ALA B . n 
B 1 496  GLY 496  496  496  GLY GLY B . n 
B 1 497  ALA 497  497  497  ALA ALA B . n 
B 1 498  VAL 498  498  498  VAL VAL B . n 
B 1 499  ARG 499  499  499  ARG ARG B . n 
B 1 500  ARG 500  500  500  ARG ARG B . n 
B 1 501  ILE 501  501  501  ILE ILE B . n 
B 1 502  HIS 502  502  502  HIS HIS B . n 
B 1 503  GLU 503  503  503  GLU GLU B . n 
B 1 504  GLY 504  504  504  GLY GLY B . n 
B 1 505  GLN 505  505  505  GLN GLN B . n 
B 1 506  ASN 506  506  506  ASN ASN B . n 
B 1 507  ARG 507  507  507  ARG ARG B . n 
B 1 508  THR 508  508  508  THR THR B . n 
B 1 509  LEU 509  509  509  LEU LEU B . n 
B 1 510  ASN 510  510  510  ASN ASN B . n 
B 1 511  MET 511  511  511  MET MET B . n 
B 1 512  LEU 512  512  512  LEU LEU B . n 
B 1 513  LYS 513  513  513  LYS LYS B . n 
B 1 514  SER 514  514  514  SER SER B . n 
B 1 515  ASP 515  515  515  ASP ASP B . n 
B 1 516  ARG 516  516  516  ARG ARG B . n 
B 1 517  PHE 517  517  517  PHE PHE B . n 
B 1 518  LEU 518  518  518  LEU LEU B . n 
B 1 519  ALA 519  519  519  ALA ALA B . n 
B 1 520  ASP 520  520  520  ASP ASP B . n 
B 1 521  ALA 521  521  521  ALA ALA B . n 
B 1 522  ASP 522  522  522  ASP ASP B . n 
B 1 523  TRP 523  523  523  TRP TRP B . n 
B 1 524  ASP 524  524  524  ASP ASP B . n 
B 1 525  ILE 525  525  525  ILE ILE B . n 
B 1 526  ALA 526  526  526  ALA ALA B . n 
B 1 527  THR 527  527  527  THR THR B . n 
B 1 528  ALA 528  528  528  ALA ALA B . n 
B 1 529  ALA 529  529  529  ALA ALA B . n 
B 1 530  CYS 530  530  530  CYS CYS B . n 
B 1 531  GLU 531  531  531  GLU GLU B . n 
B 1 532  ILE 532  532  532  ILE ILE B . n 
B 1 533  SER 533  533  533  SER SER B . n 
B 1 534  ASP 534  534  534  ASP ASP B . n 
B 1 535  PRO 535  535  535  PRO PRO B . n 
B 1 536  TYR 536  536  536  TYR TYR B . n 
B 1 537  SER 537  537  ?    ?   ?   B . n 
B 1 538  ALA 538  538  ?    ?   ?   B . n 
B 1 539  LEU 539  539  ?    ?   ?   B . n 
B 1 540  SER 540  540  ?    ?   ?   B . n 
B 1 541  ASP 541  541  ?    ?   ?   B . n 
B 1 542  ASP 542  542  ?    ?   ?   B . n 
B 1 543  GLU 543  543  ?    ?   ?   B . n 
B 1 544  ASN 544  544  ?    ?   ?   B . n 
B 1 545  ALA 545  545  ?    ?   ?   B . n 
B 1 546  PRO 546  546  ?    ?   ?   B . n 
B 1 547  ALA 547  547  ?    ?   ?   B . n 
B 1 548  ASP 548  548  ?    ?   ?   B . n 
B 1 549  GLU 549  549  ?    ?   ?   B . n 
B 1 550  LEU 550  550  ?    ?   ?   B . n 
B 1 551  THR 551  551  ?    ?   ?   B . n 
B 1 552  LEU 552  552  ?    ?   ?   B . n 
B 1 553  GLY 553  553  ?    ?   ?   B . n 
B 1 554  GLU 554  554  ?    ?   ?   B . n 
B 1 555  ARG 555  555  ?    ?   ?   B . n 
B 1 556  LYS 556  556  ?    ?   ?   B . n 
B 1 557  SER 557  557  ?    ?   ?   B . n 
B 1 558  VAL 558  558  ?    ?   ?   B . n 
B 1 559  CYS 559  559  ?    ?   ?   B . n 
B 1 560  PRO 560  560  ?    ?   ?   B . n 
B 1 561  GLY 561  561  ?    ?   ?   B . n 
B 1 562  CYS 562  562  ?    ?   ?   B . n 
B 1 563  LYS 563  563  ?    ?   ?   B . n 
B 1 564  ALA 564  564  ?    ?   ?   B . n 
B 1 565  MET 565  565  ?    ?   ?   B . n 
B 1 566  VAL 566  566  ?    ?   ?   B . n 
B 1 567  PRO 567  567  ?    ?   ?   B . n 
B 1 568  ASN 568  568  ?    ?   ?   B . n 
B 1 569  GLU 569  569  ?    ?   ?   B . n 
B 1 570  PRO 570  570  570  PRO PRO B . n 
B 1 571  SER 571  571  571  SER SER B . n 
B 1 572  PRO 572  572  572  PRO PRO B . n 
B 1 573  ARG 573  573  573  ARG ARG B . n 
B 1 574  GLU 574  574  574  GLU GLU B . n 
B 1 575  PHE 575  575  575  PHE PHE B . n 
B 1 576  ALA 576  576  576  ALA ALA B . n 
B 1 577  ASP 577  577  577  ASP ASP B . n 
B 1 578  MET 578  578  578  MET MET B . n 
B 1 579  MET 579  579  579  MET MET B . n 
B 1 580  GLU 580  580  580  GLU GLU B . n 
B 1 581  GLU 581  581  581  GLU GLU B . n 
B 1 582  ALA 582  582  582  ALA ALA B . n 
B 1 583  ARG 583  583  583  ARG ARG B . n 
B 1 584  LEU 584  584  584  LEU LEU B . n 
B 1 585  ARG 585  585  585  ARG ARG B . n 
B 1 586  MET 586  586  586  MET MET B . n 
B 1 587  LEU 587  587  587  LEU LEU B . n 
B 1 588  LYS 588  588  588  LYS LYS B . n 
B 1 589  ALA 589  589  589  ALA ALA B . n 
B 1 590  GLU 590  590  590  GLU GLU B . n 
B 1 591  LYS 591  591  591  LYS LYS B . n 
B 1 592  ILE 592  592  592  ILE ILE B . n 
B 1 593  SER 593  593  593  SER SER B . n 
B 1 594  TYR 594  594  594  TYR TYR B . n 
B 1 595  TRP 595  595  595  TRP TRP B . n 
B 1 596  LYS 596  596  596  LYS LYS B . n 
B 1 597  GLN 597  597  597  GLN GLN B . n 
B 1 598  PHE 598  598  598  PHE PHE B . n 
B 1 599  GLU 599  599  599  GLU GLU B . n 
B 1 600  HIS 600  600  600  HIS HIS B . n 
B 1 601  GLY 601  601  601  GLY GLY B . n 
B 1 602  MET 602  602  602  MET MET B . n 
B 1 603  LEU 603  603  603  LEU LEU B . n 
B 1 604  ALA 604  604  604  ALA ALA B . n 
B 1 605  ARG 605  605  605  ARG ARG B . n 
B 1 606  GLU 606  606  606  GLU GLU B . n 
B 1 607  ALA 607  607  607  ALA ALA B . n 
B 1 608  LEU 608  608  608  LEU LEU B . n 
B 1 609  ARG 609  609  609  ARG ARG B . n 
B 1 610  LEU 610  610  610  LEU LEU B . n 
B 1 611  LEU 611  611  611  LEU LEU B . n 
B 1 612  VAL 612  612  612  VAL VAL B . n 
B 1 613  GLN 613  613  613  GLN GLN B . n 
B 1 614  HIS 614  614  614  HIS HIS B . n 
B 1 615  ALA 615  615  615  ALA ALA B . n 
B 1 616  GLU 616  616  616  GLU GLU B . n 
B 1 617  VAL 617  617  617  VAL VAL B . n 
B 1 618  ALA 618  618  618  ALA ALA B . n 
B 1 619  ALA 619  619  619  ALA ALA B . n 
B 1 620  ASP 620  620  620  ASP ASP B . n 
B 1 621  GLU 621  621  621  GLU GLU B . n 
B 1 622  LYS 622  622  622  LYS LYS B . n 
B 1 623  ASP 623  623  623  ASP ASP B . n 
B 1 624  GLN 624  624  624  GLN GLN B . n 
B 1 625  PHE 625  625  625  PHE PHE B . n 
B 1 626  ILE 626  626  626  ILE ILE B . n 
B 1 627  LEU 627  627  627  LEU LEU B . n 
B 1 628  VAL 628  628  628  VAL VAL B . n 
B 1 629  ASP 629  629  629  ASP ASP B . n 
B 1 630  ASP 630  630  630  ASP ASP B . n 
B 1 631  LEU 631  631  631  LEU LEU B . n 
B 1 632  LYS 632  632  632  LYS LYS B . n 
B 1 633  LYS 633  633  633  LYS LYS B . n 
B 1 634  SER 634  634  634  SER SER B . n 
B 1 635  TRP 635  635  635  TRP TRP B . n 
B 1 636  GLN 636  636  636  GLN GLN B . n 
B 1 637  ILE 637  637  637  ILE ILE B . n 
B 1 638  LYS 638  638  638  LYS LYS B . n 
B 1 639  GLY 639  639  639  GLY GLY B . n 
B 1 640  ILE 640  640  640  ILE ILE B . n 
B 1 641  TYR 641  641  641  TYR TYR B . n 
B 1 642  PRO 642  642  642  PRO PRO B . n 
B 1 643  TRP 643  643  643  TRP TRP B . n 
B 1 644  LEU 644  644  644  LEU LEU B . n 
B 1 645  LYS 645  645  645  LYS LYS B . n 
B 1 646  ARG 646  646  646  ARG ARG B . n 
B 1 647  LYS 647  647  647  LYS LYS B . n 
B 1 648  LEU 648  648  648  LEU LEU B . n 
B 1 649  GLU 649  649  649  GLU GLU B . n 
B 1 650  ASP 650  650  650  ASP ASP B . n 
B 1 651  LEU 651  651  651  LEU LEU B . n 
B 1 652  ILE 652  652  652  ILE ILE B . n 
B 1 653  SER 653  653  653  SER SER B . n 
B 1 654  GLU 654  654  ?    ?   ?   B . n 
B 1 655  LYS 655  655  ?    ?   ?   B . n 
B 1 656  LYS 656  656  ?    ?   ?   B . n 
B 1 657  ILE 657  657  ?    ?   ?   B . n 
B 1 658  ALA 658  658  ?    ?   ?   B . n 
B 1 659  ALA 659  659  ?    ?   ?   B . n 
B 1 660  ILE 660  660  ?    ?   ?   B . n 
B 1 661  PRO 661  661  ?    ?   ?   B . n 
B 1 662  MET 662  662  ?    ?   ?   B . n 
B 1 663  PRO 663  663  ?    ?   ?   B . n 
B 1 664  LYS 664  664  ?    ?   ?   B . n 
B 1 665  TYR 665  665  ?    ?   ?   B . n 
B 1 666  LYS 666  666  ?    ?   ?   B . n 
B 1 667  LEU 667  667  ?    ?   ?   B . n 
B 1 668  GLY 668  668  ?    ?   ?   B . n 
B 1 669  LYS 669  669  ?    ?   ?   B . n 
B 1 670  LEU 670  670  670  LEU LEU B . n 
B 1 671  MET 671  671  671  MET MET B . n 
B 1 672  TYR 672  672  672  TYR TYR B . n 
B 1 673  LYS 673  673  673  LYS LYS B . n 
B 1 674  ILE 674  674  674  ILE ILE B . n 
B 1 675  CYS 675  675  675  CYS CYS B . n 
B 1 676  HIS 676  676  676  HIS HIS B . n 
B 1 677  HIS 677  677  677  HIS HIS B . n 
B 1 678  MET 678  678  678  MET MET B . n 
B 1 679  ALA 679  679  679  ALA ALA B . n 
B 1 680  PHE 680  680  680  PHE PHE B . n 
B 1 681  GLU 681  681  681  GLU GLU B . n 
B 1 682  VAL 682  682  682  VAL VAL B . n 
B 1 683  THR 683  683  683  THR THR B . n 
B 1 684  ILE 684  684  684  ILE ILE B . n 
B 1 685  ASN 685  685  685  ASN ASN B . n 
B 1 686  ILE 686  686  686  ILE ILE B . n 
B 1 687  ALA 687  687  687  ALA ALA B . n 
B 1 688  ILE 688  688  688  ILE ILE B . n 
B 1 689  VAL 689  689  689  VAL VAL B . n 
B 1 690  LEU 690  690  690  LEU LEU B . n 
B 1 691  ASN 691  691  691  ASN ASN B . n 
B 1 692  ILE 692  692  692  ILE ILE B . n 
B 1 693  VAL 693  693  693  VAL VAL B . n 
B 1 694  PRO 694  694  694  PRO PRO B . n 
B 1 695  ILE 695  695  695  ILE ILE B . n 
B 1 696  ILE 696  696  696  ILE ILE B . n 
B 1 697  MET 697  697  697  MET MET B . n 
B 1 698  GLU 698  698  698  GLU GLU B . n 
B 1 699  PHE 699  699  699  PHE PHE B . n 
B 1 700  VAL 700  700  700  VAL VAL B . n 
B 1 701  VAL 701  701  ?    ?   ?   B . n 
B 1 702  GLN 702  702  ?    ?   ?   B . n 
B 1 703  ASP 703  703  ?    ?   ?   B . n 
B 1 704  LYS 704  704  ?    ?   ?   B . n 
B 1 705  MET 705  705  ?    ?   ?   B . n 
B 1 706  ALA 706  706  ?    ?   ?   B . n 
B 1 707  SER 707  707  ?    ?   ?   B . n 
B 1 708  VAL 708  708  ?    ?   ?   B . n 
B 1 709  SER 709  709  ?    ?   ?   B . n 
B 1 710  THR 710  710  ?    ?   ?   B . n 
B 1 711  MET 711  711  ?    ?   ?   B . n 
B 1 712  ALA 712  712  ?    ?   ?   B . n 
B 1 713  ALA 713  713  ?    ?   ?   B . n 
B 1 714  PRO 714  714  ?    ?   ?   B . n 
B 1 715  GLY 715  715  ?    ?   ?   B . n 
B 1 716  SER 716  716  ?    ?   ?   B . n 
B 1 717  THR 717  717  ?    ?   ?   B . n 
B 1 718  VAL 718  718  ?    ?   ?   B . n 
B 1 719  SER 719  719  ?    ?   ?   B . n 
B 1 720  SER 720  720  ?    ?   ?   B . n 
B 1 721  GLU 721  721  ?    ?   ?   B . n 
B 1 722  PRO 722  722  ?    ?   ?   B . n 
B 1 723  SER 723  723  ?    ?   ?   B . n 
B 1 724  SER 724  724  ?    ?   ?   B . n 
B 1 725  LEU 725  725  ?    ?   ?   B . n 
B 1 726  GLN 726  726  ?    ?   ?   B . n 
B 1 727  LYS 727  727  ?    ?   ?   B . n 
B 1 728  ILE 728  728  ?    ?   ?   B . n 
B 1 729  GLU 729  729  ?    ?   ?   B . n 
B 1 730  ASP 730  730  730  ASP ASP B . n 
B 1 731  ALA 731  731  731  ALA ALA B . n 
B 1 732  LEU 732  732  732  LEU LEU B . n 
B 1 733  ARG 733  733  733  ARG ARG B . n 
B 1 734  ILE 734  734  734  ILE ILE B . n 
B 1 735  SER 735  735  735  SER SER B . n 
B 1 736  ASN 736  736  736  ASN ASN B . n 
B 1 737  TYR 737  737  737  TYR TYR B . n 
B 1 738  VAL 738  738  738  VAL VAL B . n 
B 1 739  PHE 739  739  739  PHE PHE B . n 
B 1 740  PHE 740  740  740  PHE PHE B . n 
B 1 741  VAL 741  741  741  VAL VAL B . n 
B 1 742  ILE 742  742  742  ILE ILE B . n 
B 1 743  TYR 743  743  743  TYR TYR B . n 
B 1 744  ALA 744  744  744  ALA ALA B . n 
B 1 745  ILE 745  745  745  ILE ILE B . n 
B 1 746  GLU 746  746  746  GLU GLU B . n 
B 1 747  ALA 747  747  747  ALA ALA B . n 
B 1 748  ILE 748  748  748  ILE ILE B . n 
B 1 749  VAL 749  749  749  VAL VAL B . n 
B 1 750  LYS 750  750  750  LYS LYS B . n 
B 1 751  ILE 751  751  751  ILE ILE B . n 
B 1 752  LEU 752  752  752  LEU LEU B . n 
B 1 753  GLY 753  753  753  GLY GLY B . n 
B 1 754  LEU 754  754  754  LEU LEU B . n 
B 1 755  GLY 755  755  755  GLY GLY B . n 
B 1 756  ARG 756  756  756  ARG ARG B . n 
B 1 757  HIS 757  757  757  HIS HIS B . n 
B 1 758  TYR 758  758  758  TYR TYR B . n 
B 1 759  ILE 759  759  759  ILE ILE B . n 
B 1 760  VAL 760  760  760  VAL VAL B . n 
B 1 761  SER 761  761  761  SER SER B . n 
B 1 762  HIS 762  762  762  HIS HIS B . n 
B 1 763  TRP 763  763  763  TRP TRP B . n 
B 1 764  ASN 764  764  764  ASN ASN B . n 
B 1 765  LYS 765  765  765  LYS LYS B . n 
B 1 766  PHE 766  766  766  PHE PHE B . n 
B 1 767  ASP 767  767  767  ASP ASP B . n 
B 1 768  ALA 768  768  768  ALA ALA B . n 
B 1 769  PHE 769  769  769  PHE PHE B . n 
B 1 770  ILE 770  770  770  ILE ILE B . n 
B 1 771  LEU 771  771  771  LEU LEU B . n 
B 1 772  VAL 772  772  772  VAL VAL B . n 
B 1 773  VAL 773  773  773  VAL VAL B . n 
B 1 774  ALA 774  774  774  ALA ALA B . n 
B 1 775  LEU 775  775  775  LEU LEU B . n 
B 1 776  VAL 776  776  776  VAL VAL B . n 
B 1 777  ASP 777  777  ?    ?   ?   B . n 
B 1 778  ILE 778  778  ?    ?   ?   B . n 
B 1 779  ILE 779  779  ?    ?   ?   B . n 
B 1 780  ILE 780  780  ?    ?   ?   B . n 
B 1 781  ALA 781  781  ?    ?   ?   B . n 
B 1 782  GLU 782  782  ?    ?   ?   B . n 
B 1 783  THR 783  783  ?    ?   ?   B . n 
B 1 784  LEU 784  784  ?    ?   ?   B . n 
B 1 785  LEU 785  785  ?    ?   ?   B . n 
B 1 786  LYS 786  786  ?    ?   ?   B . n 
B 1 787  GLY 787  787  ?    ?   ?   B . n 
B 1 788  SER 788  788  ?    ?   ?   B . n 
B 1 789  ILE 789  789  ?    ?   ?   B . n 
B 1 790  THR 790  790  ?    ?   ?   B . n 
B 1 791  ILE 791  791  ?    ?   ?   B . n 
B 1 792  ASN 792  792  ?    ?   ?   B . n 
B 1 793  LEU 793  793  ?    ?   ?   B . n 
B 1 794  SER 794  794  ?    ?   ?   B . n 
B 1 795  SER 795  795  ?    ?   ?   B . n 
B 1 796  ILE 796  796  ?    ?   ?   B . n 
B 1 797  LYS 797  797  797  LYS LYS B . n 
B 1 798  VAL 798  798  798  VAL VAL B . n 
B 1 799  VAL 799  799  799  VAL VAL B . n 
B 1 800  LYS 800  800  800  LYS LYS B . n 
B 1 801  LEU 801  801  801  LEU LEU B . n 
B 1 802  PHE 802  802  802  PHE PHE B . n 
B 1 803  ARG 803  803  803  ARG ARG B . n 
B 1 804  LEU 804  804  804  LEU LEU B . n 
B 1 805  LEU 805  805  805  LEU LEU B . n 
B 1 806  ARG 806  806  806  ARG ARG B . n 
B 1 807  GLY 807  807  807  GLY GLY B . n 
B 1 808  LEU 808  808  808  LEU LEU B . n 
B 1 809  ARG 809  809  809  ARG ARG B . n 
B 1 810  MET 810  810  810  MET MET B . n 
B 1 811  LEU 811  811  811  LEU LEU B . n 
B 1 812  ARG 812  812  812  ARG ARG B . n 
B 1 813  LEU 813  813  813  LEU LEU B . n 
B 1 814  THR 814  814  814  THR THR B . n 
B 1 815  LYS 815  815  815  LYS LYS B . n 
B 1 816  ALA 816  816  816  ALA ALA B . n 
B 1 817  LEU 817  817  817  LEU LEU B . n 
B 1 818  ILE 818  818  818  ILE ILE B . n 
B 1 819  PRO 819  819  819  PRO PRO B . n 
B 1 820  LYS 820  820  820  LYS LYS B . n 
B 1 821  LEU 821  821  821  LEU LEU B . n 
B 1 822  ILE 822  822  822  ILE ILE B . n 
B 1 823  LEU 823  823  823  LEU LEU B . n 
B 1 824  VAL 824  824  824  VAL VAL B . n 
B 1 825  VAL 825  825  825  VAL VAL B . n 
B 1 826  ASN 826  826  826  ASN ASN B . n 
B 1 827  GLY 827  827  827  GLY GLY B . n 
B 1 828  LYS 828  828  828  LYS LYS B . n 
B 1 829  ILE 829  829  829  ILE ILE B . n 
B 1 830  ASN 830  830  830  ASN ASN B . n 
B 1 831  ASN 831  831  831  ASN ASN B . n 
B 1 832  GLN 832  832  832  GLN GLN B . n 
B 1 833  LEU 833  833  833  LEU LEU B . n 
B 1 834  SER 834  834  834  SER SER B . n 
B 1 835  LEU 835  835  835  LEU LEU B . n 
B 1 836  GLY 836  836  836  GLY GLY B . n 
B 1 837  TYR 837  837  837  TYR TYR B . n 
B 1 838  ASP 838  838  838  ASP ASP B . n 
B 1 839  VAL 839  839  839  VAL VAL B . n 
B 1 840  GLY 840  840  840  GLY GLY B . n 
B 1 841  LYS 841  841  841  LYS LYS B . n 
B 1 842  GLY 842  842  842  GLY GLY B . n 
B 1 843  TYR 843  843  843  TYR TYR B . n 
B 1 844  ILE 844  844  844  ILE ILE B . n 
B 1 845  ILE 845  845  845  ILE ILE B . n 
B 1 846  GLY 846  846  846  GLY GLY B . n 
B 1 847  GLU 847  847  847  GLU GLU B . n 
B 1 848  GLU 848  848  848  GLU GLU B . n 
B 1 849  GLU 849  849  849  GLU GLU B . n 
B 1 850  VAL 850  850  850  VAL VAL B . n 
B 1 851  GLY 851  851  851  GLY GLY B . n 
B 1 852  LYS 852  852  852  LYS LYS B . n 
B 1 853  ILE 853  853  853  ILE ILE B . n 
B 1 854  ILE 854  854  854  ILE ILE B . n 
B 1 855  ASP 855  855  855  ASP ASP B . n 
B 1 856  ARG 856  856  856  ARG ARG B . n 
B 1 857  MET 857  857  857  MET MET B . n 
B 1 858  VAL 858  858  858  VAL VAL B . n 
B 1 859  ASP 859  859  859  ASP ASP B . n 
B 1 860  ASN 860  860  860  ASN ASN B . n 
B 1 861  LYS 861  861  861  LYS LYS B . n 
B 1 862  LYS 862  862  862  LYS LYS B . n 
B 1 863  ILE 863  863  863  ILE ILE B . n 
B 1 864  LEU 864  864  864  LEU LEU B . n 
B 1 865  ARG 865  865  865  ARG ARG B . n 
B 1 866  GLU 866  866  866  GLU GLU B . n 
B 1 867  LEU 867  867  867  LEU LEU B . n 
B 1 868  LYS 868  868  868  LYS LYS B . n 
B 1 869  HIS 869  869  869  HIS HIS B . n 
B 1 870  ILE 870  870  870  ILE ILE B . n 
B 1 871  SER 871  871  871  SER SER B . n 
B 1 872  GLU 872  872  872  GLU GLU B . n 
B 1 873  THR 873  873  873  THR THR B . n 
B 1 874  GLY 874  874  874  GLY GLY B . n 
B 1 875  ARG 875  875  875  ARG ARG B . n 
B 1 876  LEU 876  876  876  LEU LEU B . n 
B 1 877  GLN 877  877  877  GLN GLN B . n 
B 1 878  VAL 878  878  878  VAL VAL B . n 
B 1 879  VAL 879  879  879  VAL VAL B . n 
B 1 880  LYS 880  880  880  LYS LYS B . n 
B 1 881  GLU 881  881  881  GLU GLU B . n 
B 1 882  LEU 882  882  882  LEU LEU B . n 
B 1 883  GLY 883  883  883  GLY GLY B . n 
B 1 884  LEU 884  884  884  LEU LEU B . n 
B 1 885  LEU 885  885  885  LEU LEU B . n 
B 1 886  GLN 886  886  886  GLN GLN B . n 
B 1 887  ARG 887  887  887  ARG ARG B . n 
B 1 888  GLU 888  888  888  GLU GLU B . n 
B 1 889  HIS 889  889  889  HIS HIS B . n 
B 1 890  PRO 890  890  890  PRO PRO B . n 
B 1 891  GLY 891  891  891  GLY GLY B . n 
B 1 892  ILE 892  892  892  ILE ILE B . n 
B 1 893  ALA 893  893  893  ALA ALA B . n 
B 1 894  VAL 894  894  894  VAL VAL B . n 
B 1 895  SER 895  895  895  SER SER B . n 
B 1 896  VAL 896  896  896  VAL VAL B . n 
B 1 897  LYS 897  897  897  LYS LYS B . n 
B 1 898  THR 898  898  898  THR THR B . n 
B 1 899  ARG 899  899  899  ARG ARG B . n 
B 1 900  GLN 900  900  900  GLN GLN B . n 
B 1 901  ALA 901  901  901  ALA ALA B . n 
B 1 902  ILE 902  902  902  ILE ILE B . n 
B 1 903  ARG 903  903  903  ARG ARG B . n 
B 1 904  THR 904  904  904  THR THR B . n 
B 1 905  ILE 905  905  905  ILE ILE B . n 
B 1 906  LEU 906  906  906  LEU LEU B . n 
B 1 907  ASN 907  907  907  ASN ASN B . n 
B 1 908  HIS 908  908  908  HIS HIS B . n 
B 1 909  SER 909  909  909  SER SER B . n 
B 1 910  ARG 910  910  910  ARG ARG B . n 
B 1 911  GLU 911  911  911  GLU GLU B . n 
B 1 912  THR 912  912  912  THR THR B . n 
B 1 913  ILE 913  913  913  ILE ILE B . n 
B 1 914  HIS 914  914  914  HIS HIS B . n 
B 1 915  GLU 915  915  915  GLU GLU B . n 
B 1 916  LEU 916  916  916  LEU LEU B . n 
B 1 917  GLN 917  917  917  GLN GLN B . n 
B 1 918  GLY 918  918  918  GLY GLY B . n 
B 1 919  ALA 919  919  919  ALA ALA B . n 
B 1 920  GLY 920  920  920  GLY GLY B . n 
B 1 921  LEU 921  921  921  LEU LEU B . n 
B 1 922  LEU 922  922  922  LEU LEU B . n 
B 1 923  ASP 923  923  923  ASP ASP B . n 
B 1 924  GLU 924  924  924  GLU GLU B . n 
B 1 925  MET 925  925  925  MET MET B . n 
B 1 926  GLU 926  926  926  GLU GLU B . n 
B 1 927  ALA 927  927  927  ALA ALA B . n 
B 1 928  HIS 928  928  928  HIS HIS B . n 
B 1 929  LYS 929  929  929  LYS LYS B . n 
B 1 930  LEU 930  930  930  LEU LEU B . n 
B 1 931  GLU 931  931  931  GLU GLU B . n 
B 1 932  LEU 932  932  932  LEU LEU B . n 
B 1 933  THR 933  933  933  THR THR B . n 
B 1 934  VAL 934  934  934  VAL VAL B . n 
B 1 935  GLU 935  935  935  GLU GLU B . n 
B 1 936  ILE 936  936  936  ILE ILE B . n 
B 1 937  LYS 937  937  937  LYS LYS B . n 
B 1 938  MET 938  938  938  MET MET B . n 
B 1 939  LYS 939  939  939  LYS LYS B . n 
B 1 940  ARG 940  940  940  ARG ARG B . n 
B 1 941  LEU 941  941  941  LEU LEU B . n 
B 1 942  MET 942  942  942  MET MET B . n 
B 1 943  ASN 943  943  943  ASN ASN B . n 
B 1 944  ALA 944  944  944  ALA ALA B . n 
B 1 945  PRO 945  945  945  PRO PRO B . n 
B 1 946  SER 946  946  946  SER SER B . n 
B 1 947  SER 947  947  947  SER SER B . n 
B 1 948  ILE 948  948  948  ILE ILE B . n 
B 1 949  PRO 949  949  949  PRO PRO B . n 
B 1 950  PRO 950  950  950  PRO PRO B . n 
B 1 951  PRO 951  951  951  PRO PRO B . n 
B 1 952  PRO 952  952  952  PRO PRO B . n 
B 1 953  PRO 953  953  953  PRO PRO B . n 
B 1 954  GLU 954  954  954  GLU GLU B . n 
B 1 955  ASN 955  955  955  ASN ASN B . n 
B 1 956  LEU 956  956  956  LEU LEU B . n 
B 1 957  LEU 957  957  957  LEU LEU B . n 
B 1 958  LYS 958  958  958  LYS LYS B . n 
B 1 959  ASN 959  959  959  ASN ASN B . n 
B 1 960  VAL 960  960  960  VAL VAL B . n 
B 1 961  SER 961  961  961  SER SER B . n 
B 1 962  TRP 962  962  962  TRP TRP B . n 
B 1 963  LEU 963  963  963  LEU LEU B . n 
B 1 964  ALA 964  964  964  ALA ALA B . n 
B 1 965  GLY 965  965  965  GLY GLY B . n 
B 1 966  ASP 966  966  966  ASP ASP B . n 
B 1 967  MET 967  967  967  MET MET B . n 
B 1 968  LYS 968  968  968  LYS LYS B . n 
B 1 969  LEU 969  969  969  LEU LEU B . n 
B 1 970  ILE 970  970  970  ILE ILE B . n 
B 1 971  ASP 971  971  971  ASP ASP B . n 
B 1 972  PHE 972  972  972  PHE PHE B . n 
B 1 973  ILE 973  973  973  ILE ILE B . n 
B 1 974  LYS 974  974  974  LYS LYS B . n 
B 1 975  ALA 975  975  975  ALA ALA B . n 
B 1 976  ARG 976  976  976  ARG ARG B . n 
B 1 977  ALA 977  977  977  ALA ALA B . n 
B 1 978  SER 978  978  978  SER SER B . n 
B 1 979  LEU 979  979  979  LEU LEU B . n 
B 1 980  LEU 980  980  980  LEU LEU B . n 
B 1 981  HIS 981  981  981  HIS HIS B . n 
B 1 982  PHE 982  982  982  PHE PHE B . n 
B 1 983  ASP 983  983  983  ASP ASP B . n 
B 1 984  TYR 984  984  984  TYR TYR B . n 
B 1 985  GLY 985  985  985  GLY GLY B . n 
B 1 986  GLU 986  986  986  GLU GLU B . n 
B 1 987  VAL 987  987  987  VAL VAL B . n 
B 1 988  ILE 988  988  988  ILE ILE B . n 
B 1 989  VAL 989  989  989  VAL VAL B . n 
B 1 990  ARG 990  990  990  ARG ARG B . n 
B 1 991  GLU 991  991  991  GLU GLU B . n 
B 1 992  GLY 992  992  992  GLY GLY B . n 
B 1 993  ASP 993  993  993  ASP ASP B . n 
B 1 994  GLU 994  994  994  GLU GLU B . n 
B 1 995  SER 995  995  995  SER SER B . n 
B 1 996  ASP 996  996  996  ASP ASP B . n 
B 1 997  GLY 997  997  997  GLY GLY B . n 
B 1 998  LEU 998  998  998  LEU LEU B . n 
B 1 999  PHE 999  999  999  PHE PHE B . n 
B 1 1000 LEU 1000 1000 1000 LEU LEU B . n 
B 1 1001 ILE 1001 1001 1001 ILE ILE B . n 
B 1 1002 VAL 1002 1002 1002 VAL VAL B . n 
B 1 1003 SER 1003 1003 1003 SER SER B . n 
B 1 1004 GLY 1004 1004 1004 GLY GLY B . n 
B 1 1005 LEU 1005 1005 1005 LEU LEU B . n 
B 1 1006 VAL 1006 1006 1006 VAL VAL B . n 
B 1 1007 LYS 1007 1007 1007 LYS LYS B . n 
B 1 1008 LEU 1008 1008 1008 LEU LEU B . n 
B 1 1009 TYR 1009 1009 1009 TYR TYR B . n 
B 1 1010 GLY 1010 1010 1010 GLY GLY B . n 
B 1 1011 LYS 1011 1011 1011 LYS LYS B . n 
B 1 1012 SER 1012 1012 ?    ?   ?   B . n 
B 1 1013 ALA 1013 1013 ?    ?   ?   B . n 
B 1 1014 PHE 1014 1014 ?    ?   ?   B . n 
B 1 1015 LEU 1015 1015 ?    ?   ?   B . n 
B 1 1016 ASP 1016 1016 ?    ?   ?   B . n 
B 1 1017 HIS 1017 1017 ?    ?   ?   B . n 
B 1 1018 ASP 1018 1018 ?    ?   ?   B . n 
B 1 1019 ASN 1019 1019 ?    ?   ?   B . n 
B 1 1020 PRO 1020 1020 ?    ?   ?   B . n 
B 1 1021 PRO 1021 1021 ?    ?   ?   B . n 
B 1 1022 VAL 1022 1022 ?    ?   ?   B . n 
B 1 1023 THR 1023 1023 ?    ?   ?   B . n 
B 1 1024 ALA 1024 1024 ?    ?   ?   B . n 
B 1 1025 GLY 1025 1025 ?    ?   ?   B . n 
B 1 1026 SER 1026 1026 ?    ?   ?   B . n 
B 1 1027 GLU 1027 1027 ?    ?   ?   B . n 
B 1 1028 GLU 1028 1028 ?    ?   ?   B . n 
B 1 1029 ASN 1029 1029 ?    ?   ?   B . n 
B 1 1030 GLU 1030 1030 ?    ?   ?   B . n 
B 1 1031 VAL 1031 1031 1031 VAL VAL B . n 
B 1 1032 PHE 1032 1032 1032 PHE PHE B . n 
B 1 1033 GLU 1033 1033 1033 GLU GLU B . n 
B 1 1034 ASP 1034 1034 1034 ASP ASP B . n 
B 1 1035 TYR 1035 1035 1035 TYR TYR B . n 
B 1 1036 LEU 1036 1036 1036 LEU LEU B . n 
B 1 1037 THR 1037 1037 1037 THR THR B . n 
B 1 1038 VAL 1038 1038 1038 VAL VAL B . n 
B 1 1039 GLY 1039 1039 1039 GLY GLY B . n 
B 1 1040 ASN 1040 1040 1040 ASN ASN B . n 
B 1 1041 VAL 1041 1041 1041 VAL VAL B . n 
B 1 1042 ILE 1042 1042 1042 ILE ILE B . n 
B 1 1043 GLY 1043 1043 1043 GLY GLY B . n 
B 1 1044 GLU 1044 1044 1044 GLU GLU B . n 
B 1 1045 MET 1045 1045 1045 MET MET B . n 
B 1 1046 GLY 1046 1046 1046 GLY GLY B . n 
B 1 1047 VAL 1047 1047 1047 VAL VAL B . n 
B 1 1048 LEU 1048 1048 1048 LEU LEU B . n 
B 1 1049 THR 1049 1049 1049 THR THR B . n 
B 1 1050 LYS 1050 1050 1050 LYS LYS B . n 
B 1 1051 LYS 1051 1051 1051 LYS LYS B . n 
B 1 1052 PRO 1052 1052 1052 PRO PRO B . n 
B 1 1053 ARG 1053 1053 1053 ARG ARG B . n 
B 1 1054 ASN 1054 1054 1054 ASN ASN B . n 
B 1 1055 ALA 1055 1055 1055 ALA ALA B . n 
B 1 1056 THR 1056 1056 1056 THR THR B . n 
B 1 1057 VAL 1057 1057 1057 VAL VAL B . n 
B 1 1058 THR 1058 1058 1058 THR THR B . n 
B 1 1059 CYS 1059 1059 1059 CYS CYS B . n 
B 1 1060 GLU 1060 1060 1060 GLU GLU B . n 
B 1 1061 THR 1061 1061 1061 THR THR B . n 
B 1 1062 THR 1062 1062 1062 THR THR B . n 
B 1 1063 VAL 1063 1063 1063 VAL VAL B . n 
B 1 1064 GLN 1064 1064 1064 GLN GLN B . n 
B 1 1065 VAL 1065 1065 1065 VAL VAL B . n 
B 1 1066 TYR 1066 1066 1066 TYR TYR B . n 
B 1 1067 PHE 1067 1067 1067 PHE PHE B . n 
B 1 1068 ILE 1068 1068 1068 ILE ILE B . n 
B 1 1069 THR 1069 1069 1069 THR THR B . n 
B 1 1070 ALA 1070 1070 1070 ALA ALA B . n 
B 1 1071 GLU 1071 1071 1071 GLU GLU B . n 
B 1 1072 ASP 1072 1072 1072 ASP ASP B . n 
B 1 1073 MET 1073 1073 1073 MET MET B . n 
B 1 1074 ASN 1074 1074 1074 ASN ASN B . n 
B 1 1075 ILE 1075 1075 1075 ILE ILE B . n 
B 1 1076 ALA 1076 1076 1076 ALA ALA B . n 
B 1 1077 ILE 1077 1077 1077 ILE ILE B . n 
B 1 1078 ASP 1078 1078 1078 ASP ASP B . n 
B 1 1079 THR 1079 1079 1079 THR THR B . n 
B 1 1080 PHE 1080 1080 1080 PHE PHE B . n 
B 1 1081 THR 1081 1081 1081 THR THR B . n 
B 1 1082 LEU 1082 1082 1082 LEU LEU B . n 
B 1 1083 TYR 1083 1083 1083 TYR TYR B . n 
B 1 1084 PRO 1084 1084 1084 PRO PRO B . n 
B 1 1085 SER 1085 1085 1085 SER SER B . n 
B 1 1086 LEU 1086 1086 1086 LEU LEU B . n 
B 1 1087 GLU 1087 1087 1087 GLU GLU B . n 
B 1 1088 TYR 1088 1088 1088 TYR TYR B . n 
B 1 1089 ARG 1089 1089 1089 ARG ARG B . n 
B 1 1090 LEU 1090 1090 1090 LEU LEU B . n 
B 1 1091 TRP 1091 1091 1091 TRP TRP B . n 
B 1 1092 ARG 1092 1092 1092 ARG ARG B . n 
B 1 1093 VAL 1093 1093 1093 VAL VAL B . n 
B 1 1094 VAL 1094 1094 1094 VAL VAL B . n 
B 1 1095 ALA 1095 1095 1095 ALA ALA B . n 
B 1 1096 ILE 1096 1096 1096 ILE ILE B . n 
B 1 1097 ARG 1097 1097 1097 ARG ARG B . n 
B 1 1098 ILE 1098 1098 1098 ILE ILE B . n 
B 1 1099 ALA 1099 1099 1099 ALA ALA B . n 
B 1 1100 THR 1100 1100 1100 THR THR B . n 
B 1 1101 PRO 1101 1101 1101 PRO PRO B . n 
B 1 1102 LEU 1102 1102 1102 LEU LEU B . n 
B 1 1103 ILE 1103 1103 1103 ILE ILE B . n 
B 1 1104 MET 1104 1104 1104 MET MET B . n 
B 1 1105 GLU 1105 1105 1105 GLU GLU B . n 
B 1 1106 GLN 1106 1106 1106 GLN GLN B . n 
B 1 1107 MET 1107 1107 1107 MET MET B . n 
B 1 1108 ALA 1108 1108 1108 ALA ALA B . n 
B 1 1109 PHE 1109 1109 1109 PHE PHE B . n 
B 1 1110 GLN 1110 1110 1110 GLN GLN B . n 
B 1 1111 GLY 1111 1111 1111 GLY GLY B . n 
B 1 1112 TRP 1112 1112 1112 TRP TRP B . n 
B 1 1113 THR 1113 1113 1113 THR THR B . n 
B 1 1114 GLN 1114 1114 1114 GLN GLN B . n 
B 1 1115 GLU 1115 1115 1115 GLU GLU B . n 
B 1 1116 LYS 1116 1116 1116 LYS LYS B . n 
B 1 1117 VAL 1117 1117 1117 VAL VAL B . n 
B 1 1118 LYS 1118 1118 1118 LYS LYS B . n 
B 1 1119 LEU 1119 1119 1119 LEU LEU B . n 
B 1 1120 HIS 1120 1120 1120 HIS HIS B . n 
B 1 1121 LEU 1121 1121 1121 LEU LEU B . n 
B 1 1122 GLU 1122 1122 1122 GLU GLU B . n 
B 1 1123 ARG 1123 1123 1123 ARG ARG B . n 
B 1 1124 GLY 1124 1124 1124 GLY GLY B . n 
B 1 1125 TYR 1125 1125 1125 TYR TYR B . n 
B 1 1126 LEU 1126 1126 1126 LEU LEU B . n 
B 1 1127 VAL 1127 1127 1127 VAL VAL B . n 
B 1 1128 ASP 1128 1128 1128 ASP ASP B . n 
B 1 1129 LEU 1129 1129 1129 LEU LEU B . n 
B 1 1130 ALA 1130 1130 1130 ALA ALA B . n 
B 1 1131 GLU 1131 1131 1131 GLU GLU B . n 
B 1 1132 SER 1132 1132 1132 SER SER B . n 
B 1 1133 HIS 1133 1133 1133 HIS HIS B . n 
B 1 1134 PHE 1134 1134 1134 PHE PHE B . n 
B 1 1135 GLN 1135 1135 1135 GLN GLN B . n 
B 1 1136 PHE 1136 1136 1136 PHE PHE B . n 
B 1 1137 ASN 1137 1137 1137 ASN ASN B . n 
B 1 1138 ILE 1138 1138 1138 ILE ILE B . n 
B 1 1139 ASP 1139 1139 1139 ASP ASP B . n 
B 1 1140 ALA 1140 1140 1140 ALA ALA B . n 
B 1 1141 THR 1141 1141 1141 THR THR B . n 
B 1 1142 LEU 1142 1142 1142 LEU LEU B . n 
B 1 1143 GLU 1143 1143 1143 GLU GLU B . n 
B 1 1144 ASP 1144 1144 1144 ASP ASP B . n 
B 1 1145 VAL 1145 1145 1145 VAL VAL B . n 
B 1 1146 ILE 1146 1146 1146 ILE ILE B . n 
B 1 1147 LEU 1147 1147 1147 LEU LEU B . n 
B 1 1148 ILE 1148 1148 1148 ILE ILE B . n 
B 1 1149 ASN 1149 1149 1149 ASN ASN B . n 
B 1 1150 GLY 1150 1150 1150 GLY GLY B . n 
B 1 1151 THR 1151 1151 1151 THR THR B . n 
B 1 1152 ALA 1152 1152 1152 ALA ALA B . n 
B 1 1153 TYR 1153 1153 1153 TYR TYR B . n 
B 1 1154 ASN 1154 1154 1154 ASN ASN B . n 
B 1 1155 ALA 1155 1155 1155 ALA ALA B . n 
B 1 1156 HIS 1156 1156 1156 HIS HIS B . n 
B 1 1157 THR 1157 1157 1157 THR THR B . n 
B 1 1158 ARG 1158 1158 1158 ARG ARG B . n 
B 1 1159 GLU 1159 1159 1159 GLU GLU B . n 
B 1 1160 GLU 1160 1160 1160 GLU GLU B . n 
B 1 1161 ILE 1161 1161 1161 ILE ILE B . n 
B 1 1162 ARG 1162 1162 1162 ARG ARG B . n 
B 1 1163 SER 1163 1163 1163 SER SER B . n 
B 1 1164 PRO 1164 1164 1164 PRO PRO B . n 
B 1 1165 CYS 1165 1165 1165 CYS CYS B . n 
B 1 1166 LEU 1166 1166 1166 LEU LEU B . n 
B 1 1167 ILE 1167 1167 1167 ILE ILE B . n 
B 1 1168 SER 1168 1168 1168 SER SER B . n 
B 1 1169 ARG 1169 1169 1169 ARG ARG B . n 
B 1 1170 THR 1170 1170 1170 THR THR B . n 
B 1 1171 VAL 1171 1171 1171 VAL VAL B . n 
B 1 1172 HIS 1172 1172 1172 HIS HIS B . n 
B 1 1173 LYS 1173 1173 1173 LYS LYS B . n 
B 1 1174 LEU 1174 1174 1174 LEU LEU B . n 
B 1 1175 THR 1175 1175 1175 THR THR B . n 
B 1 1176 PHE 1176 1176 1176 PHE PHE B . n 
B 1 1177 GLN 1177 1177 1177 GLN GLN B . n 
B 1 1178 TYR 1178 1178 1178 TYR TYR B . n 
B 1 1179 THR 1179 1179 1179 THR THR B . n 
B 1 1180 ALA 1180 1180 1180 ALA ALA B . n 
B 1 1181 THR 1181 1181 1181 THR THR B . n 
B 1 1182 GLU 1182 1182 1182 GLU GLU B . n 
B 1 1183 GLU 1183 1183 1183 GLU GLU B . n 
B 1 1184 PRO 1184 1184 1184 PRO PRO B . n 
B 1 1185 ARG 1185 1185 1185 ARG ARG B . n 
B 1 1186 LEU 1186 1186 1186 LEU LEU B . n 
B 1 1187 PHE 1187 1187 1187 PHE PHE B . n 
B 1 1188 VAL 1188 1188 1188 VAL VAL B . n 
B 1 1189 VAL 1189 1189 1189 VAL VAL B . n 
B 1 1190 ARG 1190 1190 1190 ARG ARG B . n 
B 1 1191 ASN 1191 1191 1191 ASN ASN B . n 
B 1 1192 ALA 1192 1192 1192 ALA ALA B . n 
B 1 1193 GLU 1193 1193 1193 GLU GLU B . n 
B 1 1194 TYR 1194 1194 ?    ?   ?   B . n 
B 1 1195 ASN 1195 1195 ?    ?   ?   B . n 
B 1 1196 GLY 1196 1196 ?    ?   ?   B . n 
B 1 1197 PRO 1197 1197 ?    ?   ?   B . n 
B 1 1198 ILE 1198 1198 ?    ?   ?   B . n 
B 1 1199 LEU 1199 1199 ?    ?   ?   B . n 
B 1 1200 ASP 1200 1200 ?    ?   ?   B . n 
B 1 1201 GLY 1201 1201 ?    ?   ?   B . n 
B 1 1202 ARG 1202 1202 ?    ?   ?   B . n 
B 1 1203 LEU 1203 1203 ?    ?   ?   B . n 
B 1 1204 ASP 1204 1204 ?    ?   ?   B . n 
B 1 1205 VAL 1205 1205 ?    ?   ?   B . n 
B 1 1206 ASP 1206 1206 ?    ?   ?   B . n 
B 1 1207 SER 1207 1207 ?    ?   ?   B . n 
B 1 1208 LYS 1208 1208 ?    ?   ?   B . n 
B 1 1209 ARG 1209 1209 ?    ?   ?   B . n 
B 1 1210 SER 1210 1210 ?    ?   ?   B . n 
B 1 1211 LEU 1211 1211 ?    ?   ?   B . n 
B 1 1212 ILE 1212 1212 ?    ?   ?   B . n 
B 1 1213 SER 1213 1213 ?    ?   ?   B . n 
B 1 1214 ILE 1214 1214 ?    ?   ?   B . n 
B 1 1215 THR 1215 1215 ?    ?   ?   B . n 
B 1 1216 GLU 1216 1216 ?    ?   ?   B . n 
B 1 1217 ILE 1217 1217 ?    ?   ?   B . n 
B 1 1218 SER 1218 1218 ?    ?   ?   B . n 
B 1 1219 SER 1219 1219 ?    ?   ?   B . n 
B 1 1220 ASN 1220 1220 ?    ?   ?   B . n 
B 1 1221 MET 1221 1221 ?    ?   ?   B . n 
B 1 1222 CYS 1222 1222 ?    ?   ?   B . n 
B 1 1223 LEU 1223 1223 ?    ?   ?   B . n 
B 1 1224 LYS 1224 1224 ?    ?   ?   B . n 
B 1 1225 HIS 1225 1225 ?    ?   ?   B . n 
B 1 1226 ALA 1226 1226 ?    ?   ?   B . n 
B 1 1227 ALA 1227 1227 ?    ?   ?   B . n 
B 1 1228 GLU 1228 1228 ?    ?   ?   B . n 
B 1 1229 LEU 1229 1229 ?    ?   ?   B . n 
B 1 1230 ARG 1230 1230 ?    ?   ?   B . n 
B 1 1231 GLN 1231 1231 ?    ?   ?   B . n 
B 1 1232 LYS 1232 1232 ?    ?   ?   B . n 
B 1 1233 ASN 1233 1233 ?    ?   ?   B . n 
B 1 1234 SER 1234 1234 ?    ?   ?   B . n 
B 1 1235 LYS 1235 1235 ?    ?   ?   B . n 
B 1 1236 VAL 1236 1236 ?    ?   ?   B . n 
B 1 1237 MET 1237 1237 ?    ?   ?   B . n 
B 1 1238 LEU 1238 1238 ?    ?   ?   B . n 
B 1 1239 SER 1239 1239 ?    ?   ?   B . n 
B 1 1240 ARG 1240 1240 ?    ?   ?   B . n 
B 1 1241 LYS 1241 1241 ?    ?   ?   B . n 
B 1 1242 SER 1242 1242 ?    ?   ?   B . n 
B 1 1243 SER 1243 1243 ?    ?   ?   B . n 
B 1 1244 GLY 1244 1244 ?    ?   ?   B . n 
B 1 1245 ALA 1245 1245 ?    ?   ?   B . n 
B 1 1246 ALA 1246 1246 ?    ?   ?   B . n 
B 1 1247 ALA 1247 1247 ?    ?   ?   B . n 
B 1 1248 LYS 1248 1248 ?    ?   ?   B . n 
B 1 1249 GLU 1249 1249 ?    ?   ?   B . n 
B 1 1250 GLU 1250 1250 ?    ?   ?   B . n 
B 1 1251 GLU 1251 1251 ?    ?   ?   B . n 
B 1 1252 ASP 1252 1252 ?    ?   ?   B . n 
B 1 1253 CYS 1253 1253 ?    ?   ?   B . n 
B 1 1254 ILE 1254 1254 ?    ?   ?   B . n 
B 1 1255 PRO 1255 1255 ?    ?   ?   B . n 
B 1 1256 ASN 1256 1256 ?    ?   ?   B . n 
B 1 1257 THR 1257 1257 ?    ?   ?   B . n 
B 1 1258 SER 1258 1258 ?    ?   ?   B . n 
B 1 1259 ASP 1259 1259 ?    ?   ?   B . n 
B 1 1260 VAL 1260 1260 ?    ?   ?   B . n 
B 1 1261 GLU 1261 1261 ?    ?   ?   B . n 
B 1 1262 GLN 1262 1262 ?    ?   ?   B . n 
B 1 1263 ALA 1263 1263 ?    ?   ?   B . n 
B 1 1264 ALA 1264 1264 ?    ?   ?   B . n 
B 1 1265 GLY 1265 1265 ?    ?   ?   B . n 
B 1 1266 VAL 1266 1266 ?    ?   ?   B . n 
B 1 1267 SER 1267 1267 ?    ?   ?   B . n 
B 1 1268 PRO 1268 1268 ?    ?   ?   B . n 
B 1 1269 SER 1269 1269 ?    ?   ?   B . n 
B 1 1270 VAL 1270 1270 ?    ?   ?   B . n 
B 1 1271 PRO 1271 1271 ?    ?   ?   B . n 
B 1 1272 THR 1272 1272 ?    ?   ?   B . n 
B 1 1273 LYS 1273 1273 ?    ?   ?   B . n 
B 1 1274 THR 1274 1274 ?    ?   ?   B . n 
B 1 1275 THR 1275 1275 ?    ?   ?   B . n 
B 1 1276 PRO 1276 1276 ?    ?   ?   B . n 
B 1 1277 LYS 1277 1277 ?    ?   ?   B . n 
B 1 1278 PRO 1278 1278 ?    ?   ?   B . n 
B 1 1279 LYS 1279 1279 ?    ?   ?   B . n 
B 1 1280 SER 1280 1280 ?    ?   ?   B . n 
B 1 1281 PHE 1281 1281 ?    ?   ?   B . n 
B 1 1282 LEU 1282 1282 ?    ?   ?   B . n 
B 1 1283 PRO 1283 1283 ?    ?   ?   B . n 
B 1 1284 SER 1284 1284 ?    ?   ?   B . n 
B 1 1285 LEU 1285 1285 ?    ?   ?   B . n 
B 1 1286 GLY 1286 1286 ?    ?   ?   B . n 
B 1 1287 LEU 1287 1287 ?    ?   ?   B . n 
B 1 1288 SER 1288 1288 ?    ?   ?   B . n 
B 1 1289 MET 1289 1289 ?    ?   ?   B . n 
B 1 1290 SER 1290 1290 ?    ?   ?   B . n 
B 1 1291 LYS 1291 1291 ?    ?   ?   B . n 
B 1 1292 GLU 1292 1292 ?    ?   ?   B . n 
B 1 1293 ARG 1293 1293 ?    ?   ?   B . n 
B 1 1294 VAL 1294 1294 ?    ?   ?   B . n 
B 1 1295 ASN 1295 1295 ?    ?   ?   B . n 
B 1 1296 GLY 1296 1296 ?    ?   ?   B . n 
B 1 1297 GLU 1297 1297 ?    ?   ?   B . n 
B 1 1298 ALA 1298 1298 ?    ?   ?   B . n 
B 1 1299 VAL 1299 1299 ?    ?   ?   B . n 
B 1 1300 GLU 1300 1300 ?    ?   ?   B . n 
B 1 1301 GLU 1301 1301 ?    ?   ?   B . n 
B 1 1302 SER 1302 1302 ?    ?   ?   B . n 
B 1 1303 PRO 1303 1303 ?    ?   ?   B . n 
B 1 1304 VAL 1304 1304 ?    ?   ?   B . n 
B 1 1305 LYS 1305 1305 ?    ?   ?   B . n 
B 1 1306 THR 1306 1306 ?    ?   ?   B . n 
B 1 1307 LYS 1307 1307 ?    ?   ?   B . n 
B 1 1308 GLN 1308 1308 ?    ?   ?   B . n 
B 1 1309 GLY 1309 1309 ?    ?   ?   B . n 
B 1 1310 GLU 1310 1310 ?    ?   ?   B . n 
B 1 1311 GLU 1311 1311 ?    ?   ?   B . n 
B 1 1312 THR 1312 1312 ?    ?   ?   B . n 
B 1 1313 PRO 1313 1313 ?    ?   ?   B . n 
B 1 1314 GLU 1314 1314 ?    ?   ?   B . n 
B 1 1315 THR 1315 1315 ?    ?   ?   B . n 
B 1 1316 GLU 1316 1316 ?    ?   ?   B . n 
B 1 1317 GLU 1317 1317 ?    ?   ?   B . n 
B 1 1318 GLY 1318 1318 ?    ?   ?   B . n 
B 1 1319 ALA 1319 1319 ?    ?   ?   B . n 
B 1 1320 ALA 1320 1320 ?    ?   ?   B . n 
B 1 1321 PRO 1321 1321 ?    ?   ?   B . n 
B 1 1322 ARG 1322 1322 ?    ?   ?   B . n 
B 1 1323 VAL 1323 1323 ?    ?   ?   B . n 
B 1 1324 ASN 1324 1324 ?    ?   ?   B . n 
B 1 1325 VAL 1325 1325 ?    ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 AJP ? ? AJP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 POV ? ? POV ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 POV 1 1401 1 POV POV A . 
D 2 POV 1 1402 2 POV POV A . 
E 3 AJP 1 1403 5 AJP AJP A . 
F 3 AJP 1 1404 6 AJP AJP A . 
G 2 POV 1 1401 3 POV POV B . 
H 3 AJP 1 1402 7 AJP AJP B . 
I 3 AJP 1 1403 8 AJP AJP B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ARG 756  ? CG   ? A ARG 756 CG   
2   1 Y 1 A ARG 756  ? CD   ? A ARG 756 CD   
3   1 Y 1 A ARG 756  ? NE   ? A ARG 756 NE   
4   1 Y 1 A ARG 756  ? CZ   ? A ARG 756 CZ   
5   1 Y 1 A ARG 756  ? NH1  ? A ARG 756 NH1  
6   1 Y 1 A ARG 756  ? NH2  ? A ARG 756 NH2  
7   1 Y 1 A ILE 759  ? CG1  ? A ILE 759 CG1  
8   1 Y 1 A ILE 759  ? CG2  ? A ILE 759 CG2  
9   1 Y 1 A ILE 759  ? CD1  ? A ILE 759 CD1  
10  1 Y 1 B ARG 756  ? CG   ? B ARG 756 CG   
11  1 Y 1 B ARG 756  ? CD   ? B ARG 756 CD   
12  1 Y 1 B ARG 756  ? NE   ? B ARG 756 NE   
13  1 Y 1 B ARG 756  ? CZ   ? B ARG 756 CZ   
14  1 Y 1 B ARG 756  ? NH1  ? B ARG 756 NH1  
15  1 Y 1 B ARG 756  ? NH2  ? B ARG 756 NH2  
16  1 Y 1 B ILE 759  ? CG1  ? B ILE 759 CG1  
17  1 Y 1 B ILE 759  ? CG2  ? B ILE 759 CG2  
18  1 Y 1 B ILE 759  ? CD1  ? B ILE 759 CD1  
19  1 N 1 A POV 1401 ? N    ? C POV 1   N    
20  1 N 1 A POV 1401 ? P    ? C POV 1   P    
21  1 N 1 A POV 1401 ? C11  ? C POV 1   C11  
22  1 N 1 A POV 1401 ? C12  ? C POV 1   C12  
23  1 N 1 A POV 1401 ? O12  ? C POV 1   O12  
24  1 N 1 A POV 1401 ? C13  ? C POV 1   C13  
25  1 N 1 A POV 1401 ? O13  ? C POV 1   O13  
26  1 N 1 A POV 1401 ? C14  ? C POV 1   C14  
27  1 N 1 A POV 1401 ? O14  ? C POV 1   O14  
28  1 N 1 A POV 1401 ? C15  ? C POV 1   C15  
29  1 N 1 A POV 1401 ? C217 ? C POV 1   C217 
30  1 N 1 A POV 1401 ? C218 ? C POV 1   C218 
31  1 N 1 A POV 1402 ? N    ? D POV 1   N    
32  1 N 1 A POV 1402 ? C11  ? D POV 1   C11  
33  1 N 1 A POV 1402 ? C12  ? D POV 1   C12  
34  1 N 1 A POV 1402 ? C13  ? D POV 1   C13  
35  1 N 1 A POV 1402 ? C14  ? D POV 1   C14  
36  1 N 1 A POV 1402 ? C15  ? D POV 1   C15  
37  1 N 1 A AJP 1403 ? C46  ? E AJP 1   C46  
38  1 N 1 A AJP 1403 ? C47  ? E AJP 1   C47  
39  1 N 1 A AJP 1403 ? C48  ? E AJP 1   C48  
40  1 N 1 A AJP 1403 ? C49  ? E AJP 1   C49  
41  1 N 1 A AJP 1403 ? O50  ? E AJP 1   O50  
42  1 N 1 A AJP 1403 ? O51  ? E AJP 1   O51  
43  1 N 1 A AJP 1403 ? O52  ? E AJP 1   O52  
44  1 N 1 A AJP 1403 ? O53  ? E AJP 1   O53  
45  1 N 1 A AJP 1403 ? C65  ? E AJP 1   C65  
46  1 N 1 A AJP 1403 ? C66  ? E AJP 1   C66  
47  1 N 1 A AJP 1403 ? C67  ? E AJP 1   C67  
48  1 N 1 A AJP 1403 ? C68  ? E AJP 1   C68  
49  1 N 1 A AJP 1403 ? C69  ? E AJP 1   C69  
50  1 N 1 A AJP 1403 ? O70  ? E AJP 1   O70  
51  1 N 1 A AJP 1403 ? C71  ? E AJP 1   C71  
52  1 N 1 A AJP 1403 ? O72  ? E AJP 1   O72  
53  1 N 1 A AJP 1403 ? O73  ? E AJP 1   O73  
54  1 N 1 A AJP 1403 ? O74  ? E AJP 1   O74  
55  1 N 1 A AJP 1403 ? O75  ? E AJP 1   O75  
56  1 N 1 A AJP 1404 ? C45  ? F AJP 1   C45  
57  1 N 1 A AJP 1404 ? C46  ? F AJP 1   C46  
58  1 N 1 A AJP 1404 ? C47  ? F AJP 1   C47  
59  1 N 1 A AJP 1404 ? C48  ? F AJP 1   C48  
60  1 N 1 A AJP 1404 ? C49  ? F AJP 1   C49  
61  1 N 1 A AJP 1404 ? O50  ? F AJP 1   O50  
62  1 N 1 A AJP 1404 ? O51  ? F AJP 1   O51  
63  1 N 1 A AJP 1404 ? O52  ? F AJP 1   O52  
64  1 N 1 A AJP 1404 ? O53  ? F AJP 1   O53  
65  1 N 1 A AJP 1404 ? C65  ? F AJP 1   C65  
66  1 N 1 A AJP 1404 ? C66  ? F AJP 1   C66  
67  1 N 1 A AJP 1404 ? C67  ? F AJP 1   C67  
68  1 N 1 A AJP 1404 ? C68  ? F AJP 1   C68  
69  1 N 1 A AJP 1404 ? C69  ? F AJP 1   C69  
70  1 N 1 A AJP 1404 ? O70  ? F AJP 1   O70  
71  1 N 1 A AJP 1404 ? C71  ? F AJP 1   C71  
72  1 N 1 A AJP 1404 ? O72  ? F AJP 1   O72  
73  1 N 1 A AJP 1404 ? O73  ? F AJP 1   O73  
74  1 N 1 A AJP 1404 ? O74  ? F AJP 1   O74  
75  1 N 1 A AJP 1404 ? O75  ? F AJP 1   O75  
76  1 N 1 B POV 1401 ? N    ? G POV 1   N    
77  1 N 1 B POV 1401 ? P    ? G POV 1   P    
78  1 N 1 B POV 1401 ? C11  ? G POV 1   C11  
79  1 N 1 B POV 1401 ? C12  ? G POV 1   C12  
80  1 N 1 B POV 1401 ? O12  ? G POV 1   O12  
81  1 N 1 B POV 1401 ? C13  ? G POV 1   C13  
82  1 N 1 B POV 1401 ? O13  ? G POV 1   O13  
83  1 N 1 B POV 1401 ? C14  ? G POV 1   C14  
84  1 N 1 B POV 1401 ? O14  ? G POV 1   O14  
85  1 N 1 B POV 1401 ? C15  ? G POV 1   C15  
86  1 N 1 B POV 1401 ? C217 ? G POV 1   C217 
87  1 N 1 B POV 1401 ? C218 ? G POV 1   C218 
88  1 N 1 B AJP 1402 ? C45  ? H AJP 1   C45  
89  1 N 1 B AJP 1402 ? C46  ? H AJP 1   C46  
90  1 N 1 B AJP 1402 ? C47  ? H AJP 1   C47  
91  1 N 1 B AJP 1402 ? C48  ? H AJP 1   C48  
92  1 N 1 B AJP 1402 ? C49  ? H AJP 1   C49  
93  1 N 1 B AJP 1402 ? O50  ? H AJP 1   O50  
94  1 N 1 B AJP 1402 ? O51  ? H AJP 1   O51  
95  1 N 1 B AJP 1402 ? O52  ? H AJP 1   O52  
96  1 N 1 B AJP 1402 ? O53  ? H AJP 1   O53  
97  1 N 1 B AJP 1402 ? C55  ? H AJP 1   C55  
98  1 N 1 B AJP 1402 ? C56  ? H AJP 1   C56  
99  1 N 1 B AJP 1402 ? C57  ? H AJP 1   C57  
100 1 N 1 B AJP 1402 ? C58  ? H AJP 1   C58  
101 1 N 1 B AJP 1402 ? C59  ? H AJP 1   C59  
102 1 N 1 B AJP 1402 ? O60  ? H AJP 1   O60  
103 1 N 1 B AJP 1402 ? C61  ? H AJP 1   C61  
104 1 N 1 B AJP 1402 ? O62  ? H AJP 1   O62  
105 1 N 1 B AJP 1402 ? O63  ? H AJP 1   O63  
106 1 N 1 B AJP 1402 ? O64  ? H AJP 1   O64  
107 1 N 1 B AJP 1402 ? C65  ? H AJP 1   C65  
108 1 N 1 B AJP 1402 ? C66  ? H AJP 1   C66  
109 1 N 1 B AJP 1402 ? C67  ? H AJP 1   C67  
110 1 N 1 B AJP 1402 ? C68  ? H AJP 1   C68  
111 1 N 1 B AJP 1402 ? C69  ? H AJP 1   C69  
112 1 N 1 B AJP 1402 ? O70  ? H AJP 1   O70  
113 1 N 1 B AJP 1402 ? C71  ? H AJP 1   C71  
114 1 N 1 B AJP 1402 ? O72  ? H AJP 1   O72  
115 1 N 1 B AJP 1402 ? O73  ? H AJP 1   O73  
116 1 N 1 B AJP 1402 ? O74  ? H AJP 1   O74  
117 1 N 1 B AJP 1402 ? O75  ? H AJP 1   O75  
118 1 N 1 B AJP 1402 ? O76  ? H AJP 1   O76  
119 1 N 1 B AJP 1403 ? C45  ? I AJP 1   C45  
120 1 N 1 B AJP 1403 ? C46  ? I AJP 1   C46  
121 1 N 1 B AJP 1403 ? C47  ? I AJP 1   C47  
122 1 N 1 B AJP 1403 ? C48  ? I AJP 1   C48  
123 1 N 1 B AJP 1403 ? C49  ? I AJP 1   C49  
124 1 N 1 B AJP 1403 ? O50  ? I AJP 1   O50  
125 1 N 1 B AJP 1403 ? O51  ? I AJP 1   O51  
126 1 N 1 B AJP 1403 ? O52  ? I AJP 1   O52  
127 1 N 1 B AJP 1403 ? O53  ? I AJP 1   O53  
128 1 N 1 B AJP 1403 ? O62  ? I AJP 1   O62  
129 1 N 1 B AJP 1403 ? C65  ? I AJP 1   C65  
130 1 N 1 B AJP 1403 ? C66  ? I AJP 1   C66  
131 1 N 1 B AJP 1403 ? C67  ? I AJP 1   C67  
132 1 N 1 B AJP 1403 ? C68  ? I AJP 1   C68  
133 1 N 1 B AJP 1403 ? C69  ? I AJP 1   C69  
134 1 N 1 B AJP 1403 ? O70  ? I AJP 1   O70  
135 1 N 1 B AJP 1403 ? C71  ? I AJP 1   C71  
136 1 N 1 B AJP 1403 ? O72  ? I AJP 1   O72  
137 1 N 1 B AJP 1403 ? O73  ? I AJP 1   O73  
138 1 N 1 B AJP 1403 ? O74  ? I AJP 1   O74  
139 1 N 1 B AJP 1403 ? O75  ? I AJP 1   O75  
# 
_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                     8U73 
_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                         8U73 
_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                   8U73 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 8U73 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.005 ? 16539 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.888 ? 22468 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 7.425 ? 2450  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.046 ? 2746  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.005 ? 2701  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     8U73 
_struct.title                        'R399A sea urchin SLC9C1 pH 8 in Na+' 
_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        8U73 
_struct_keywords.text            'ion transporter, SLC9, voltage-sensor, cAMP regulated, sperm capacitation, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 2 ? 
H N N 3 ? 
I N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A3RL54_STRPU 
_struct_ref.pdbx_db_accession          A3RL54 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKKRVVKLRELVPAVAALAVAVLIQSATGSSGGSGHTPTTQATHADDHDLTTHNGTEEHDDGHDDGHDDLHAHAPKVIVF
ISGSCLFGAISRSLFKKLPIPYTVVLLILGAILGVVASNVPLVEEHTRDVAHMDPHVLLQIFLPVLIFESAFAMDVHTFM
RSFSQVCILALFGLVVASVLTAVLAMNLFNYNWNFSEAMMFGAIMSATDPVAVVALLKDLGASKQLGTIIEGESLLNDGC
AIVIFNVFMKMVFFPQLTSTVGQNVLYFLQVAVAGPLWGYAVAKVTVFFLSHIFNDALVEITITLAATYLTYYIGDIWLE
VSGVLAVVVLGLIVNAEKTSISPEVEVFLHRFWEMLAYLANTLIFMMVGVVVTQKALVAVDKMDWFYLIILYLAITIIRG
MVISLFSPILSRIGYGLTWRNAVIMTWGGLRGAVGLALALVVENLAGNDVIGSKFLFHTAGIVVLTLVINATTIQTLLRI
LGMSDISIPKRLAMAGAVRRIHEGQNRTLNMLKSDRFLADADWDIATAACEISDPYSALSDDENAPADELTLGERKSVCP
GCKAMVPNEPSPREFADMMEEARLRMLKAEKISYWKQFEHGMLAREALRLLVQHAEVAADEKDQFILVDDLKKSWQIKGI
YPWLKRKLEDLISEKKIAAIPMPKYKLGKLMYKICHHMAFEVTINIAIVLNIVPIIMEFVVQDKMASVSTMAAPGSTVSS
EPSSLQKIEDALRISNYVFFVIYAIEAIVKILGLGRHYIVSHWNKFDAFILVVALVDIIIAETLLKGSITINLSSIKVVK
LFRLLRGLRMLRLTKALIPKLILVVNGKINNQLSLGYDVGKGYIIGEEEVGKIIDRMVDNKKILRELKHISETGRLQVVK
ELGLLQREHPGIAVSVKTRQAIRTILNHSRETIHELQGAGLLDEMEAHKLELTVEIKMKRLMNAPSSIPPPPPENLLKNV
SWLAGDMKLIDFIKARASLLHFDYGEVIVREGDESDGLFLIVSGLVKLYGKSAFLDHDNPPVTAGSEENEVFEDYLTVGN
VIGEMGVLTKKPRNATVTCETTVQVYFITAEDMNIAIDTFTLYPSLEYRLWRVVAIRIATPLIMEQMAFQGWTQEKVKLH
LERGYLVDLAESHFQFNIDATLEDVILINGTAYNAHTREEIRSPCLISRTVHKLTFQYTATEEPRLFVVRNAEYNGPILD
GRLDVDSKRSLISITEISSNMCLKHAAELRQKNSKVMLSRKSSGAAAKEEEDCIPNTSDVEQAAGVSPSVPTKTTPKPKS
FLPSLGLSMSKERVNGEAVEESPVKTKQGEETPETEEGAAPRVNV
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8U73 A 1 ? 1325 ? A3RL54 1 ? 1325 ? 1 1325 
2 1 8U73 B 1 ? 1325 ? A3RL54 1 ? 1325 ? 1 1325 
# 
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 8U73 ALA A 399 ? UNP A3RL54 ARG 399 'engineered mutation' 399 1 
2 8U73 ALA B 399 ? UNP A3RL54 ARG 399 'engineered mutation' 399 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 VAL A 77   ? PHE A 95   ? VAL A 77   PHE A 95   1 ? 19 
HELX_P HELX_P2  AA2 TYR A 102  ? VAL A 120  ? TYR A 102  VAL A 120  1 ? 19 
HELX_P HELX_P3  AA3 VAL A 120  ? HIS A 132  ? VAL A 120  HIS A 132  1 ? 13 
HELX_P HELX_P4  AA4 ASP A 134  ? ILE A 141  ? ASP A 134  ILE A 141  1 ? 8  
HELX_P HELX_P5  AA5 ILE A 141  ? MET A 154  ? ILE A 141  MET A 154  1 ? 14 
HELX_P HELX_P6  AA6 PHE A 159  ? ARG A 161  ? PHE A 159  ARG A 161  5 ? 3  
HELX_P HELX_P7  AA7 SER A 162  ? LEU A 188  ? SER A 162  LEU A 188  1 ? 27 
HELX_P HELX_P8  AA8 ASN A 194  ? MET A 205  ? ASN A 194  MET A 205  1 ? 12 
HELX_P HELX_P9  AA9 PRO A 210  ? ASP A 219  ? PRO A 210  ASP A 219  1 ? 10 
HELX_P HELX_P10 AB1 LEU A 226  ? PHE A 254  ? LEU A 226  PHE A 254  1 ? 29 
HELX_P HELX_P11 AB2 THR A 260  ? VAL A 273  ? THR A 260  VAL A 273  1 ? 14 
HELX_P HELX_P12 AB3 VAL A 273  ? SER A 291  ? VAL A 273  SER A 291  1 ? 19 
HELX_P HELX_P13 AB4 ASP A 296  ? GLU A 320  ? ASP A 296  GLU A 320  1 ? 25 
HELX_P HELX_P14 AB5 GLY A 323  ? GLU A 337  ? GLY A 323  GLU A 337  1 ? 15 
HELX_P HELX_P15 AB6 SER A 342  ? LYS A 375  ? SER A 342  LYS A 375  1 ? 34 
HELX_P HELX_P16 AB7 ASP A 381  ? SER A 407  ? ASP A 381  SER A 407  1 ? 27 
HELX_P HELX_P17 AB8 THR A 418  ? GLY A 428  ? THR A 418  GLY A 428  1 ? 11 
HELX_P HELX_P18 AB9 GLY A 432  ? GLY A 447  ? GLY A 432  GLY A 447  1 ? 16 
HELX_P HELX_P19 AC1 ASP A 449  ? MET A 483  ? ASP A 449  MET A 483  1 ? 35 
HELX_P HELX_P20 AC2 ILE A 486  ? LEU A 492  ? ILE A 486  LEU A 492  1 ? 7  
HELX_P HELX_P21 AC3 LEU A 492  ? SER A 514  ? LEU A 492  SER A 514  1 ? 23 
HELX_P HELX_P22 AC4 ASP A 522  ? GLU A 531  ? ASP A 522  GLU A 531  1 ? 10 
HELX_P HELX_P23 AC5 SER A 571  ? HIS A 600  ? SER A 571  HIS A 600  1 ? 30 
HELX_P HELX_P24 AC6 ALA A 604  ? GLU A 621  ? ALA A 604  GLU A 621  1 ? 18 
HELX_P HELX_P25 AC7 LEU A 627  ? LYS A 632  ? LEU A 627  LYS A 632  1 ? 6  
HELX_P HELX_P26 AC8 LYS A 633  ? GLY A 639  ? LYS A 633  GLY A 639  5 ? 7  
HELX_P HELX_P27 AC9 ILE A 640  ? SER A 653  ? ILE A 640  SER A 653  1 ? 14 
HELX_P HELX_P28 AD1 ALA A 679  ? MET A 697  ? ALA A 679  MET A 697  1 ? 19 
HELX_P HELX_P29 AD2 ALA A 731  ? LEU A 754  ? ALA A 731  LEU A 754  1 ? 24 
HELX_P HELX_P30 AD3 GLY A 755  ? HIS A 757  ? GLY A 755  HIS A 757  5 ? 3  
HELX_P HELX_P31 AD4 SER A 761  ? VAL A 776  ? SER A 761  VAL A 776  1 ? 16 
HELX_P HELX_P32 AD5 VAL A 798  ? ARG A 806  ? VAL A 798  ARG A 806  1 ? 9  
HELX_P HELX_P33 AD6 ARG A 812  ? ILE A 854  ? ARG A 812  ILE A 854  1 ? 43 
HELX_P HELX_P34 AD7 ASP A 855  ? MET A 857  ? ASP A 855  MET A 857  5 ? 3  
HELX_P HELX_P35 AD8 ASN A 860  ? HIS A 889  ? ASN A 860  HIS A 889  1 ? 30 
HELX_P HELX_P36 AD9 HIS A 889  ? ALA A 919  ? HIS A 889  ALA A 919  1 ? 31 
HELX_P HELX_P37 AE1 ASP A 923  ? MET A 942  ? ASP A 923  MET A 942  1 ? 20 
HELX_P HELX_P38 AE2 PRO A 952  ? ASN A 959  ? PRO A 952  ASN A 959  1 ? 8  
HELX_P HELX_P39 AE3 ASP A 966  ? ARG A 976  ? ASP A 966  ARG A 976  1 ? 11 
HELX_P HELX_P40 AE4 GLY A 1043 ? LYS A 1050 ? GLY A 1043 LYS A 1050 1 ? 8  
HELX_P HELX_P41 AE5 ALA A 1070 ? PHE A 1080 ? ALA A 1070 PHE A 1080 1 ? 11 
HELX_P HELX_P42 AE6 SER A 1085 ? MET A 1107 ? SER A 1085 MET A 1107 1 ? 23 
HELX_P HELX_P43 AE7 THR A 1113 ? GLY A 1124 ? THR A 1113 GLY A 1124 1 ? 12 
HELX_P HELX_P44 AE8 VAL B 77   ? PHE B 95   ? VAL B 77   PHE B 95   1 ? 19 
HELX_P HELX_P45 AE9 TYR B 102  ? VAL B 120  ? TYR B 102  VAL B 120  1 ? 19 
HELX_P HELX_P46 AF1 VAL B 120  ? HIS B 132  ? VAL B 120  HIS B 132  1 ? 13 
HELX_P HELX_P47 AF2 ASP B 134  ? ILE B 141  ? ASP B 134  ILE B 141  1 ? 8  
HELX_P HELX_P48 AF3 ILE B 141  ? MET B 154  ? ILE B 141  MET B 154  1 ? 14 
HELX_P HELX_P49 AF4 PHE B 159  ? ARG B 161  ? PHE B 159  ARG B 161  5 ? 3  
HELX_P HELX_P50 AF5 SER B 162  ? LEU B 188  ? SER B 162  LEU B 188  1 ? 27 
HELX_P HELX_P51 AF6 ASN B 194  ? MET B 205  ? ASN B 194  MET B 205  1 ? 12 
HELX_P HELX_P52 AF7 PRO B 210  ? GLY B 221  ? PRO B 210  GLY B 221  1 ? 12 
HELX_P HELX_P53 AF8 LEU B 226  ? PHE B 254  ? LEU B 226  PHE B 254  1 ? 29 
HELX_P HELX_P54 AF9 THR B 260  ? VAL B 273  ? THR B 260  VAL B 273  1 ? 14 
HELX_P HELX_P55 AG1 VAL B 273  ? SER B 291  ? VAL B 273  SER B 291  1 ? 19 
HELX_P HELX_P56 AG2 ASP B 296  ? GLU B 320  ? ASP B 296  GLU B 320  1 ? 25 
HELX_P HELX_P57 AG3 GLY B 323  ? GLU B 337  ? GLY B 323  GLU B 337  1 ? 15 
HELX_P HELX_P58 AG4 SER B 342  ? LYS B 375  ? SER B 342  LYS B 375  1 ? 34 
HELX_P HELX_P59 AG5 ASP B 381  ? SER B 407  ? ASP B 381  SER B 407  1 ? 27 
HELX_P HELX_P60 AG6 LEU B 410  ? GLY B 414  ? LEU B 410  GLY B 414  5 ? 5  
HELX_P HELX_P61 AG7 THR B 418  ? GLY B 428  ? THR B 418  GLY B 428  1 ? 11 
HELX_P HELX_P62 AG8 GLY B 432  ? GLY B 447  ? GLY B 432  GLY B 447  1 ? 16 
HELX_P HELX_P63 AG9 ASP B 449  ? MET B 483  ? ASP B 449  MET B 483  1 ? 35 
HELX_P HELX_P64 AH1 ILE B 486  ? LEU B 492  ? ILE B 486  LEU B 492  1 ? 7  
HELX_P HELX_P65 AH2 LEU B 492  ? SER B 514  ? LEU B 492  SER B 514  1 ? 23 
HELX_P HELX_P66 AH3 ASP B 522  ? GLU B 531  ? ASP B 522  GLU B 531  1 ? 10 
HELX_P HELX_P67 AH4 SER B 571  ? HIS B 600  ? SER B 571  HIS B 600  1 ? 30 
HELX_P HELX_P68 AH5 ALA B 604  ? ASP B 620  ? ALA B 604  ASP B 620  1 ? 17 
HELX_P HELX_P69 AH6 LEU B 627  ? LYS B 632  ? LEU B 627  LYS B 632  1 ? 6  
HELX_P HELX_P70 AH7 LYS B 633  ? GLY B 639  ? LYS B 633  GLY B 639  5 ? 7  
HELX_P HELX_P71 AH8 ILE B 640  ? SER B 653  ? ILE B 640  SER B 653  1 ? 14 
HELX_P HELX_P72 AH9 ALA B 679  ? MET B 697  ? ALA B 679  MET B 697  1 ? 19 
HELX_P HELX_P73 AI1 ALA B 731  ? LEU B 754  ? ALA B 731  LEU B 754  1 ? 24 
HELX_P HELX_P74 AI2 GLY B 755  ? HIS B 757  ? GLY B 755  HIS B 757  5 ? 3  
HELX_P HELX_P75 AI3 HIS B 762  ? VAL B 776  ? HIS B 762  VAL B 776  1 ? 15 
HELX_P HELX_P76 AI4 VAL B 798  ? ARG B 806  ? VAL B 798  ARG B 806  1 ? 9  
HELX_P HELX_P77 AI5 ARG B 812  ? ILE B 854  ? ARG B 812  ILE B 854  1 ? 43 
HELX_P HELX_P78 AI6 ASP B 855  ? MET B 857  ? ASP B 855  MET B 857  5 ? 3  
HELX_P HELX_P79 AI7 ASN B 860  ? HIS B 889  ? ASN B 860  HIS B 889  1 ? 30 
HELX_P HELX_P80 AI8 HIS B 889  ? ALA B 919  ? HIS B 889  ALA B 919  1 ? 31 
HELX_P HELX_P81 AI9 ASP B 923  ? MET B 942  ? ASP B 923  MET B 942  1 ? 20 
HELX_P HELX_P82 AJ1 PRO B 952  ? ASN B 959  ? PRO B 952  ASN B 959  1 ? 8  
HELX_P HELX_P83 AJ2 ASP B 966  ? ARG B 976  ? ASP B 966  ARG B 976  1 ? 11 
HELX_P HELX_P84 AJ3 GLY B 1043 ? LYS B 1050 ? GLY B 1043 LYS B 1050 1 ? 8  
HELX_P HELX_P85 AJ4 ALA B 1070 ? PHE B 1080 ? ALA B 1070 PHE B 1080 1 ? 11 
HELX_P HELX_P86 AJ5 SER B 1085 ? MET B 1107 ? SER B 1085 MET B 1107 1 ? 23 
HELX_P HELX_P87 AJ6 THR B 1113 ? GLY B 1124 ? THR B 1113 GLY B 1124 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 3 ? 
AA9 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 977  ? PHE A 982  ? ALA A 977  PHE A 982  
AA1 2 VAL A 1063 ? THR A 1069 ? VAL A 1063 THR A 1069 
AA1 3 GLY A 997  ? SER A 1003 ? GLY A 997  SER A 1003 
AA1 4 VAL A 1041 ? ILE A 1042 ? VAL A 1041 ILE A 1042 
AA2 1 VAL A 987  ? VAL A 989  ? VAL A 987  VAL A 989  
AA2 2 ALA A 1055 ? CYS A 1059 ? ALA A 1055 CYS A 1059 
AA2 3 VAL A 1006 ? GLY A 1010 ? VAL A 1006 GLY A 1010 
AA2 4 PHE A 1032 ? LEU A 1036 ? PHE A 1032 LEU A 1036 
AA3 1 GLN A 1135 ? PHE A 1136 ? GLN A 1135 PHE A 1136 
AA3 2 LEU A 1174 ? THR A 1175 ? LEU A 1174 THR A 1175 
AA3 3 THR A 1151 ? ASN A 1154 ? THR A 1151 ASN A 1154 
AA3 4 GLU A 1160 ? ARG A 1162 ? GLU A 1160 ARG A 1162 
AA4 1 CYS A 1165 ? LEU A 1166 ? CYS A 1165 LEU A 1166 
AA4 2 LEU A 1142 ? LEU A 1147 ? LEU A 1142 LEU A 1147 
AA4 3 LEU A 1186 ? ARG A 1190 ? LEU A 1186 ARG A 1190 
AA5 1 THR B 208  ? ASP B 209  ? THR B 208  ASP B 209  
AA5 2 LEU B 430  ? ARG B 431  ? LEU B 430  ARG B 431  
AA6 1 ALA B 977  ? PHE B 982  ? ALA B 977  PHE B 982  
AA6 2 VAL B 1063 ? THR B 1069 ? VAL B 1063 THR B 1069 
AA6 3 GLY B 997  ? SER B 1003 ? GLY B 997  SER B 1003 
AA6 4 VAL B 1041 ? ILE B 1042 ? VAL B 1041 ILE B 1042 
AA7 1 VAL B 987  ? VAL B 989  ? VAL B 987  VAL B 989  
AA7 2 ALA B 1055 ? CYS B 1059 ? ALA B 1055 CYS B 1059 
AA7 3 VAL B 1006 ? GLY B 1010 ? VAL B 1006 GLY B 1010 
AA7 4 PHE B 1032 ? LEU B 1036 ? PHE B 1032 LEU B 1036 
AA8 1 GLN B 1135 ? PHE B 1136 ? GLN B 1135 PHE B 1136 
AA8 2 LEU B 1174 ? THR B 1175 ? LEU B 1174 THR B 1175 
AA8 3 TYR B 1153 ? ASN B 1154 ? TYR B 1153 ASN B 1154 
AA9 1 CYS B 1165 ? LEU B 1166 ? CYS B 1165 LEU B 1166 
AA9 2 LEU B 1142 ? LEU B 1147 ? LEU B 1142 LEU B 1147 
AA9 3 LEU B 1186 ? ARG B 1190 ? LEU B 1186 ARG B 1190 
# 
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 SER A 978  ? N SER A 978  O PHE A 1067 ? O PHE A 1067 
AA1 2 3 O GLN A 1064 ? O GLN A 1064 N VAL A 1002 ? N VAL A 1002 
AA1 3 4 N PHE A 999  ? N PHE A 999  O ILE A 1042 ? O ILE A 1042 
AA2 1 2 N ILE A 988  ? N ILE A 988  O VAL A 1057 ? O VAL A 1057 
AA2 2 3 O THR A 1058 ? O THR A 1058 N LYS A 1007 ? N LYS A 1007 
AA2 3 4 N GLY A 1010 ? N GLY A 1010 O PHE A 1032 ? O PHE A 1032 
AA3 1 2 N PHE A 1136 ? N PHE A 1136 O LEU A 1174 ? O LEU A 1174 
AA3 2 3 O THR A 1175 ? O THR A 1175 N TYR A 1153 ? N TYR A 1153 
AA3 3 4 N ALA A 1152 ? N ALA A 1152 O ILE A 1161 ? O ILE A 1161 
AA4 1 2 O CYS A 1165 ? O CYS A 1165 N LEU A 1147 ? N LEU A 1147 
AA4 2 3 N ILE A 1146 ? N ILE A 1146 O PHE A 1187 ? O PHE A 1187 
AA5 1 2 N ASP B 209  ? N ASP B 209  O LEU B 430  ? O LEU B 430  
AA6 1 2 N SER B 978  ? N SER B 978  O PHE B 1067 ? O PHE B 1067 
AA6 2 3 O GLN B 1064 ? O GLN B 1064 N VAL B 1002 ? N VAL B 1002 
AA6 3 4 N PHE B 999  ? N PHE B 999  O ILE B 1042 ? O ILE B 1042 
AA7 1 2 N ILE B 988  ? N ILE B 988  O VAL B 1057 ? O VAL B 1057 
AA7 2 3 O THR B 1058 ? O THR B 1058 N LYS B 1007 ? N LYS B 1007 
AA7 3 4 N GLY B 1010 ? N GLY B 1010 O PHE B 1032 ? O PHE B 1032 
AA8 1 2 N PHE B 1136 ? N PHE B 1136 O LEU B 1174 ? O LEU B 1174 
AA8 2 3 O THR B 1175 ? O THR B 1175 N TYR B 1153 ? N TYR B 1153 
AA9 1 2 O CYS B 1165 ? O CYS B 1165 N LEU B 1147 ? N LEU B 1147 
AA9 2 3 N ILE B 1146 ? N ILE B 1146 O PHE B 1187 ? O PHE B 1187 
# 
_pdbx_entry_details.entry_id                   8U73 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
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 VAL A 273  ? ? -123.68 -54.86  
2  1 GLU A 320  ? ? 57.65   -127.72 
3  1 SER A 484  ? ? 46.50   23.66   
4  1 SER A 487  ? ? 66.72   -159.94 
5  1 MET A 810  ? ? -91.43  52.01   
6  1 THR A 1037 ? ? -124.88 -167.95 
7  1 THR A 1157 ? ? 58.71   15.78   
8  1 SER B 223  ? ? -170.90 140.91  
9  1 VAL B 273  ? ? -123.73 -54.82  
10 1 GLU B 320  ? ? 55.71   -131.36 
11 1 SER B 484  ? ? 46.48   23.66   
12 1 SER B 487  ? ? 67.77   -161.56 
13 1 THR B 1037 ? ? -125.01 -167.68 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 SER A 1163 ? ? PRO A 1164 ? ? -34.95 
2 1 SER B 1163 ? ? PRO B 1164 ? ? -37.36 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8U73 
_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                    8U73 
_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                  3.1 
_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               2251538 
_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 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 'ORGANELLE OR CELLULAR COMPONENT' 
_em_entity_assembly.name                 'R399A mutant of sea urchin SLC9C1' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        8U73 
_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               'SPOT SCAN' 
_em_imaging.mode                            OTHER 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             900 
_em_imaging.nominal_defocus_max             1700 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              8U73 
_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                8U73 
_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 1    ? A MET 1    
2   1 Y 1 A LYS 2    ? A LYS 2    
3   1 Y 1 A LYS 3    ? A LYS 3    
4   1 Y 1 A ARG 4    ? A ARG 4    
5   1 Y 1 A VAL 5    ? A VAL 5    
6   1 Y 1 A VAL 6    ? A VAL 6    
7   1 Y 1 A LYS 7    ? A LYS 7    
8   1 Y 1 A LEU 8    ? A LEU 8    
9   1 Y 1 A ARG 9    ? A ARG 9    
10  1 Y 1 A GLU 10   ? A GLU 10   
11  1 Y 1 A LEU 11   ? A LEU 11   
12  1 Y 1 A VAL 12   ? A VAL 12   
13  1 Y 1 A PRO 13   ? A PRO 13   
14  1 Y 1 A ALA 14   ? A ALA 14   
15  1 Y 1 A VAL 15   ? A VAL 15   
16  1 Y 1 A ALA 16   ? A ALA 16   
17  1 Y 1 A ALA 17   ? A ALA 17   
18  1 Y 1 A LEU 18   ? A LEU 18   
19  1 Y 1 A ALA 19   ? A ALA 19   
20  1 Y 1 A VAL 20   ? A VAL 20   
21  1 Y 1 A ALA 21   ? A ALA 21   
22  1 Y 1 A VAL 22   ? A VAL 22   
23  1 Y 1 A LEU 23   ? A LEU 23   
24  1 Y 1 A ILE 24   ? A ILE 24   
25  1 Y 1 A GLN 25   ? A GLN 25   
26  1 Y 1 A SER 26   ? A SER 26   
27  1 Y 1 A ALA 27   ? A ALA 27   
28  1 Y 1 A THR 28   ? A THR 28   
29  1 Y 1 A GLY 29   ? A GLY 29   
30  1 Y 1 A SER 30   ? A SER 30   
31  1 Y 1 A SER 31   ? A SER 31   
32  1 Y 1 A GLY 32   ? A GLY 32   
33  1 Y 1 A GLY 33   ? A GLY 33   
34  1 Y 1 A SER 34   ? A SER 34   
35  1 Y 1 A GLY 35   ? A GLY 35   
36  1 Y 1 A HIS 36   ? A HIS 36   
37  1 Y 1 A THR 37   ? A THR 37   
38  1 Y 1 A PRO 38   ? A PRO 38   
39  1 Y 1 A THR 39   ? A THR 39   
40  1 Y 1 A THR 40   ? A THR 40   
41  1 Y 1 A GLN 41   ? A GLN 41   
42  1 Y 1 A ALA 42   ? A ALA 42   
43  1 Y 1 A THR 43   ? A THR 43   
44  1 Y 1 A HIS 44   ? A HIS 44   
45  1 Y 1 A ALA 45   ? A ALA 45   
46  1 Y 1 A ASP 46   ? A ASP 46   
47  1 Y 1 A ASP 47   ? A ASP 47   
48  1 Y 1 A HIS 48   ? A HIS 48   
49  1 Y 1 A ASP 49   ? A ASP 49   
50  1 Y 1 A LEU 50   ? A LEU 50   
51  1 Y 1 A THR 51   ? A THR 51   
52  1 Y 1 A THR 52   ? A THR 52   
53  1 Y 1 A HIS 53   ? A HIS 53   
54  1 Y 1 A ASN 54   ? A ASN 54   
55  1 Y 1 A GLY 55   ? A GLY 55   
56  1 Y 1 A THR 56   ? A THR 56   
57  1 Y 1 A GLU 57   ? A GLU 57   
58  1 Y 1 A GLU 58   ? A GLU 58   
59  1 Y 1 A HIS 59   ? A HIS 59   
60  1 Y 1 A ASP 60   ? A ASP 60   
61  1 Y 1 A ASP 61   ? A ASP 61   
62  1 Y 1 A GLY 62   ? A GLY 62   
63  1 Y 1 A HIS 63   ? A HIS 63   
64  1 Y 1 A ASP 64   ? A ASP 64   
65  1 Y 1 A ASP 65   ? A ASP 65   
66  1 Y 1 A GLY 66   ? A GLY 66   
67  1 Y 1 A HIS 67   ? A HIS 67   
68  1 Y 1 A ASP 68   ? A ASP 68   
69  1 Y 1 A ASP 69   ? A ASP 69   
70  1 Y 1 A LEU 70   ? A LEU 70   
71  1 Y 1 A HIS 71   ? A HIS 71   
72  1 Y 1 A ALA 72   ? A ALA 72   
73  1 Y 1 A HIS 73   ? A HIS 73   
74  1 Y 1 A SER 537  ? A SER 537  
75  1 Y 1 A ALA 538  ? A ALA 538  
76  1 Y 1 A LEU 539  ? A LEU 539  
77  1 Y 1 A SER 540  ? A SER 540  
78  1 Y 1 A ASP 541  ? A ASP 541  
79  1 Y 1 A ASP 542  ? A ASP 542  
80  1 Y 1 A GLU 543  ? A GLU 543  
81  1 Y 1 A ASN 544  ? A ASN 544  
82  1 Y 1 A ALA 545  ? A ALA 545  
83  1 Y 1 A PRO 546  ? A PRO 546  
84  1 Y 1 A ALA 547  ? A ALA 547  
85  1 Y 1 A ASP 548  ? A ASP 548  
86  1 Y 1 A GLU 549  ? A GLU 549  
87  1 Y 1 A LEU 550  ? A LEU 550  
88  1 Y 1 A THR 551  ? A THR 551  
89  1 Y 1 A LEU 552  ? A LEU 552  
90  1 Y 1 A GLY 553  ? A GLY 553  
91  1 Y 1 A GLU 554  ? A GLU 554  
92  1 Y 1 A ARG 555  ? A ARG 555  
93  1 Y 1 A LYS 556  ? A LYS 556  
94  1 Y 1 A SER 557  ? A SER 557  
95  1 Y 1 A VAL 558  ? A VAL 558  
96  1 Y 1 A CYS 559  ? A CYS 559  
97  1 Y 1 A PRO 560  ? A PRO 560  
98  1 Y 1 A GLY 561  ? A GLY 561  
99  1 Y 1 A CYS 562  ? A CYS 562  
100 1 Y 1 A LYS 563  ? A LYS 563  
101 1 Y 1 A ALA 564  ? A ALA 564  
102 1 Y 1 A MET 565  ? A MET 565  
103 1 Y 1 A VAL 566  ? A VAL 566  
104 1 Y 1 A PRO 567  ? A PRO 567  
105 1 Y 1 A ASN 568  ? A ASN 568  
106 1 Y 1 A GLU 569  ? A GLU 569  
107 1 Y 1 A GLU 654  ? A GLU 654  
108 1 Y 1 A LYS 655  ? A LYS 655  
109 1 Y 1 A LYS 656  ? A LYS 656  
110 1 Y 1 A ILE 657  ? A ILE 657  
111 1 Y 1 A ALA 658  ? A ALA 658  
112 1 Y 1 A ALA 659  ? A ALA 659  
113 1 Y 1 A ILE 660  ? A ILE 660  
114 1 Y 1 A PRO 661  ? A PRO 661  
115 1 Y 1 A MET 662  ? A MET 662  
116 1 Y 1 A PRO 663  ? A PRO 663  
117 1 Y 1 A LYS 664  ? A LYS 664  
118 1 Y 1 A TYR 665  ? A TYR 665  
119 1 Y 1 A LYS 666  ? A LYS 666  
120 1 Y 1 A LEU 667  ? A LEU 667  
121 1 Y 1 A GLY 668  ? A GLY 668  
122 1 Y 1 A LYS 669  ? A LYS 669  
123 1 Y 1 A VAL 701  ? A VAL 701  
124 1 Y 1 A GLN 702  ? A GLN 702  
125 1 Y 1 A ASP 703  ? A ASP 703  
126 1 Y 1 A LYS 704  ? A LYS 704  
127 1 Y 1 A MET 705  ? A MET 705  
128 1 Y 1 A ALA 706  ? A ALA 706  
129 1 Y 1 A SER 707  ? A SER 707  
130 1 Y 1 A VAL 708  ? A VAL 708  
131 1 Y 1 A SER 709  ? A SER 709  
132 1 Y 1 A THR 710  ? A THR 710  
133 1 Y 1 A MET 711  ? A MET 711  
134 1 Y 1 A ALA 712  ? A ALA 712  
135 1 Y 1 A ALA 713  ? A ALA 713  
136 1 Y 1 A PRO 714  ? A PRO 714  
137 1 Y 1 A GLY 715  ? A GLY 715  
138 1 Y 1 A SER 716  ? A SER 716  
139 1 Y 1 A THR 717  ? A THR 717  
140 1 Y 1 A VAL 718  ? A VAL 718  
141 1 Y 1 A SER 719  ? A SER 719  
142 1 Y 1 A SER 720  ? A SER 720  
143 1 Y 1 A GLU 721  ? A GLU 721  
144 1 Y 1 A PRO 722  ? A PRO 722  
145 1 Y 1 A SER 723  ? A SER 723  
146 1 Y 1 A SER 724  ? A SER 724  
147 1 Y 1 A LEU 725  ? A LEU 725  
148 1 Y 1 A GLN 726  ? A GLN 726  
149 1 Y 1 A LYS 727  ? A LYS 727  
150 1 Y 1 A ILE 728  ? A ILE 728  
151 1 Y 1 A GLU 729  ? A GLU 729  
152 1 Y 1 A ASP 777  ? A ASP 777  
153 1 Y 1 A ILE 778  ? A ILE 778  
154 1 Y 1 A ILE 779  ? A ILE 779  
155 1 Y 1 A ILE 780  ? A ILE 780  
156 1 Y 1 A ALA 781  ? A ALA 781  
157 1 Y 1 A GLU 782  ? A GLU 782  
158 1 Y 1 A THR 783  ? A THR 783  
159 1 Y 1 A LEU 784  ? A LEU 784  
160 1 Y 1 A LEU 785  ? A LEU 785  
161 1 Y 1 A LYS 786  ? A LYS 786  
162 1 Y 1 A GLY 787  ? A GLY 787  
163 1 Y 1 A SER 788  ? A SER 788  
164 1 Y 1 A ILE 789  ? A ILE 789  
165 1 Y 1 A THR 790  ? A THR 790  
166 1 Y 1 A ILE 791  ? A ILE 791  
167 1 Y 1 A ASN 792  ? A ASN 792  
168 1 Y 1 A LEU 793  ? A LEU 793  
169 1 Y 1 A SER 794  ? A SER 794  
170 1 Y 1 A SER 795  ? A SER 795  
171 1 Y 1 A ILE 796  ? A ILE 796  
172 1 Y 1 A SER 1012 ? A SER 1012 
173 1 Y 1 A ALA 1013 ? A ALA 1013 
174 1 Y 1 A PHE 1014 ? A PHE 1014 
175 1 Y 1 A LEU 1015 ? A LEU 1015 
176 1 Y 1 A ASP 1016 ? A ASP 1016 
177 1 Y 1 A HIS 1017 ? A HIS 1017 
178 1 Y 1 A ASP 1018 ? A ASP 1018 
179 1 Y 1 A ASN 1019 ? A ASN 1019 
180 1 Y 1 A PRO 1020 ? A PRO 1020 
181 1 Y 1 A PRO 1021 ? A PRO 1021 
182 1 Y 1 A VAL 1022 ? A VAL 1022 
183 1 Y 1 A THR 1023 ? A THR 1023 
184 1 Y 1 A ALA 1024 ? A ALA 1024 
185 1 Y 1 A GLY 1025 ? A GLY 1025 
186 1 Y 1 A SER 1026 ? A SER 1026 
187 1 Y 1 A GLU 1027 ? A GLU 1027 
188 1 Y 1 A GLU 1028 ? A GLU 1028 
189 1 Y 1 A ASN 1029 ? A ASN 1029 
190 1 Y 1 A GLU 1030 ? A GLU 1030 
191 1 Y 1 A TYR 1194 ? A TYR 1194 
192 1 Y 1 A ASN 1195 ? A ASN 1195 
193 1 Y 1 A GLY 1196 ? A GLY 1196 
194 1 Y 1 A PRO 1197 ? A PRO 1197 
195 1 Y 1 A ILE 1198 ? A ILE 1198 
196 1 Y 1 A LEU 1199 ? A LEU 1199 
197 1 Y 1 A ASP 1200 ? A ASP 1200 
198 1 Y 1 A GLY 1201 ? A GLY 1201 
199 1 Y 1 A ARG 1202 ? A ARG 1202 
200 1 Y 1 A LEU 1203 ? A LEU 1203 
201 1 Y 1 A ASP 1204 ? A ASP 1204 
202 1 Y 1 A VAL 1205 ? A VAL 1205 
203 1 Y 1 A ASP 1206 ? A ASP 1206 
204 1 Y 1 A SER 1207 ? A SER 1207 
205 1 Y 1 A LYS 1208 ? A LYS 1208 
206 1 Y 1 A ARG 1209 ? A ARG 1209 
207 1 Y 1 A SER 1210 ? A SER 1210 
208 1 Y 1 A LEU 1211 ? A LEU 1211 
209 1 Y 1 A ILE 1212 ? A ILE 1212 
210 1 Y 1 A SER 1213 ? A SER 1213 
211 1 Y 1 A ILE 1214 ? A ILE 1214 
212 1 Y 1 A THR 1215 ? A THR 1215 
213 1 Y 1 A GLU 1216 ? A GLU 1216 
214 1 Y 1 A ILE 1217 ? A ILE 1217 
215 1 Y 1 A SER 1218 ? A SER 1218 
216 1 Y 1 A SER 1219 ? A SER 1219 
217 1 Y 1 A ASN 1220 ? A ASN 1220 
218 1 Y 1 A MET 1221 ? A MET 1221 
219 1 Y 1 A CYS 1222 ? A CYS 1222 
220 1 Y 1 A LEU 1223 ? A LEU 1223 
221 1 Y 1 A LYS 1224 ? A LYS 1224 
222 1 Y 1 A HIS 1225 ? A HIS 1225 
223 1 Y 1 A ALA 1226 ? A ALA 1226 
224 1 Y 1 A ALA 1227 ? A ALA 1227 
225 1 Y 1 A GLU 1228 ? A GLU 1228 
226 1 Y 1 A LEU 1229 ? A LEU 1229 
227 1 Y 1 A ARG 1230 ? A ARG 1230 
228 1 Y 1 A GLN 1231 ? A GLN 1231 
229 1 Y 1 A LYS 1232 ? A LYS 1232 
230 1 Y 1 A ASN 1233 ? A ASN 1233 
231 1 Y 1 A SER 1234 ? A SER 1234 
232 1 Y 1 A LYS 1235 ? A LYS 1235 
233 1 Y 1 A VAL 1236 ? A VAL 1236 
234 1 Y 1 A MET 1237 ? A MET 1237 
235 1 Y 1 A LEU 1238 ? A LEU 1238 
236 1 Y 1 A SER 1239 ? A SER 1239 
237 1 Y 1 A ARG 1240 ? A ARG 1240 
238 1 Y 1 A LYS 1241 ? A LYS 1241 
239 1 Y 1 A SER 1242 ? A SER 1242 
240 1 Y 1 A SER 1243 ? A SER 1243 
241 1 Y 1 A GLY 1244 ? A GLY 1244 
242 1 Y 1 A ALA 1245 ? A ALA 1245 
243 1 Y 1 A ALA 1246 ? A ALA 1246 
244 1 Y 1 A ALA 1247 ? A ALA 1247 
245 1 Y 1 A LYS 1248 ? A LYS 1248 
246 1 Y 1 A GLU 1249 ? A GLU 1249 
247 1 Y 1 A GLU 1250 ? A GLU 1250 
248 1 Y 1 A GLU 1251 ? A GLU 1251 
249 1 Y 1 A ASP 1252 ? A ASP 1252 
250 1 Y 1 A CYS 1253 ? A CYS 1253 
251 1 Y 1 A ILE 1254 ? A ILE 1254 
252 1 Y 1 A PRO 1255 ? A PRO 1255 
253 1 Y 1 A ASN 1256 ? A ASN 1256 
254 1 Y 1 A THR 1257 ? A THR 1257 
255 1 Y 1 A SER 1258 ? A SER 1258 
256 1 Y 1 A ASP 1259 ? A ASP 1259 
257 1 Y 1 A VAL 1260 ? A VAL 1260 
258 1 Y 1 A GLU 1261 ? A GLU 1261 
259 1 Y 1 A GLN 1262 ? A GLN 1262 
260 1 Y 1 A ALA 1263 ? A ALA 1263 
261 1 Y 1 A ALA 1264 ? A ALA 1264 
262 1 Y 1 A GLY 1265 ? A GLY 1265 
263 1 Y 1 A VAL 1266 ? A VAL 1266 
264 1 Y 1 A SER 1267 ? A SER 1267 
265 1 Y 1 A PRO 1268 ? A PRO 1268 
266 1 Y 1 A SER 1269 ? A SER 1269 
267 1 Y 1 A VAL 1270 ? A VAL 1270 
268 1 Y 1 A PRO 1271 ? A PRO 1271 
269 1 Y 1 A THR 1272 ? A THR 1272 
270 1 Y 1 A LYS 1273 ? A LYS 1273 
271 1 Y 1 A THR 1274 ? A THR 1274 
272 1 Y 1 A THR 1275 ? A THR 1275 
273 1 Y 1 A PRO 1276 ? A PRO 1276 
274 1 Y 1 A LYS 1277 ? A LYS 1277 
275 1 Y 1 A PRO 1278 ? A PRO 1278 
276 1 Y 1 A LYS 1279 ? A LYS 1279 
277 1 Y 1 A SER 1280 ? A SER 1280 
278 1 Y 1 A PHE 1281 ? A PHE 1281 
279 1 Y 1 A LEU 1282 ? A LEU 1282 
280 1 Y 1 A PRO 1283 ? A PRO 1283 
281 1 Y 1 A SER 1284 ? A SER 1284 
282 1 Y 1 A LEU 1285 ? A LEU 1285 
283 1 Y 1 A GLY 1286 ? A GLY 1286 
284 1 Y 1 A LEU 1287 ? A LEU 1287 
285 1 Y 1 A SER 1288 ? A SER 1288 
286 1 Y 1 A MET 1289 ? A MET 1289 
287 1 Y 1 A SER 1290 ? A SER 1290 
288 1 Y 1 A LYS 1291 ? A LYS 1291 
289 1 Y 1 A GLU 1292 ? A GLU 1292 
290 1 Y 1 A ARG 1293 ? A ARG 1293 
291 1 Y 1 A VAL 1294 ? A VAL 1294 
292 1 Y 1 A ASN 1295 ? A ASN 1295 
293 1 Y 1 A GLY 1296 ? A GLY 1296 
294 1 Y 1 A GLU 1297 ? A GLU 1297 
295 1 Y 1 A ALA 1298 ? A ALA 1298 
296 1 Y 1 A VAL 1299 ? A VAL 1299 
297 1 Y 1 A GLU 1300 ? A GLU 1300 
298 1 Y 1 A GLU 1301 ? A GLU 1301 
299 1 Y 1 A SER 1302 ? A SER 1302 
300 1 Y 1 A PRO 1303 ? A PRO 1303 
301 1 Y 1 A VAL 1304 ? A VAL 1304 
302 1 Y 1 A LYS 1305 ? A LYS 1305 
303 1 Y 1 A THR 1306 ? A THR 1306 
304 1 Y 1 A LYS 1307 ? A LYS 1307 
305 1 Y 1 A GLN 1308 ? A GLN 1308 
306 1 Y 1 A GLY 1309 ? A GLY 1309 
307 1 Y 1 A GLU 1310 ? A GLU 1310 
308 1 Y 1 A GLU 1311 ? A GLU 1311 
309 1 Y 1 A THR 1312 ? A THR 1312 
310 1 Y 1 A PRO 1313 ? A PRO 1313 
311 1 Y 1 A GLU 1314 ? A GLU 1314 
312 1 Y 1 A THR 1315 ? A THR 1315 
313 1 Y 1 A GLU 1316 ? A GLU 1316 
314 1 Y 1 A GLU 1317 ? A GLU 1317 
315 1 Y 1 A GLY 1318 ? A GLY 1318 
316 1 Y 1 A ALA 1319 ? A ALA 1319 
317 1 Y 1 A ALA 1320 ? A ALA 1320 
318 1 Y 1 A PRO 1321 ? A PRO 1321 
319 1 Y 1 A ARG 1322 ? A ARG 1322 
320 1 Y 1 A VAL 1323 ? A VAL 1323 
321 1 Y 1 A ASN 1324 ? A ASN 1324 
322 1 Y 1 A VAL 1325 ? A VAL 1325 
323 1 Y 1 B MET 1    ? B MET 1    
324 1 Y 1 B LYS 2    ? B LYS 2    
325 1 Y 1 B LYS 3    ? B LYS 3    
326 1 Y 1 B ARG 4    ? B ARG 4    
327 1 Y 1 B VAL 5    ? B VAL 5    
328 1 Y 1 B VAL 6    ? B VAL 6    
329 1 Y 1 B LYS 7    ? B LYS 7    
330 1 Y 1 B LEU 8    ? B LEU 8    
331 1 Y 1 B ARG 9    ? B ARG 9    
332 1 Y 1 B GLU 10   ? B GLU 10   
333 1 Y 1 B LEU 11   ? B LEU 11   
334 1 Y 1 B VAL 12   ? B VAL 12   
335 1 Y 1 B PRO 13   ? B PRO 13   
336 1 Y 1 B ALA 14   ? B ALA 14   
337 1 Y 1 B VAL 15   ? B VAL 15   
338 1 Y 1 B ALA 16   ? B ALA 16   
339 1 Y 1 B ALA 17   ? B ALA 17   
340 1 Y 1 B LEU 18   ? B LEU 18   
341 1 Y 1 B ALA 19   ? B ALA 19   
342 1 Y 1 B VAL 20   ? B VAL 20   
343 1 Y 1 B ALA 21   ? B ALA 21   
344 1 Y 1 B VAL 22   ? B VAL 22   
345 1 Y 1 B LEU 23   ? B LEU 23   
346 1 Y 1 B ILE 24   ? B ILE 24   
347 1 Y 1 B GLN 25   ? B GLN 25   
348 1 Y 1 B SER 26   ? B SER 26   
349 1 Y 1 B ALA 27   ? B ALA 27   
350 1 Y 1 B THR 28   ? B THR 28   
351 1 Y 1 B GLY 29   ? B GLY 29   
352 1 Y 1 B SER 30   ? B SER 30   
353 1 Y 1 B SER 31   ? B SER 31   
354 1 Y 1 B GLY 32   ? B GLY 32   
355 1 Y 1 B GLY 33   ? B GLY 33   
356 1 Y 1 B SER 34   ? B SER 34   
357 1 Y 1 B GLY 35   ? B GLY 35   
358 1 Y 1 B HIS 36   ? B HIS 36   
359 1 Y 1 B THR 37   ? B THR 37   
360 1 Y 1 B PRO 38   ? B PRO 38   
361 1 Y 1 B THR 39   ? B THR 39   
362 1 Y 1 B THR 40   ? B THR 40   
363 1 Y 1 B GLN 41   ? B GLN 41   
364 1 Y 1 B ALA 42   ? B ALA 42   
365 1 Y 1 B THR 43   ? B THR 43   
366 1 Y 1 B HIS 44   ? B HIS 44   
367 1 Y 1 B ALA 45   ? B ALA 45   
368 1 Y 1 B ASP 46   ? B ASP 46   
369 1 Y 1 B ASP 47   ? B ASP 47   
370 1 Y 1 B HIS 48   ? B HIS 48   
371 1 Y 1 B ASP 49   ? B ASP 49   
372 1 Y 1 B LEU 50   ? B LEU 50   
373 1 Y 1 B THR 51   ? B THR 51   
374 1 Y 1 B THR 52   ? B THR 52   
375 1 Y 1 B HIS 53   ? B HIS 53   
376 1 Y 1 B ASN 54   ? B ASN 54   
377 1 Y 1 B GLY 55   ? B GLY 55   
378 1 Y 1 B THR 56   ? B THR 56   
379 1 Y 1 B GLU 57   ? B GLU 57   
380 1 Y 1 B GLU 58   ? B GLU 58   
381 1 Y 1 B HIS 59   ? B HIS 59   
382 1 Y 1 B ASP 60   ? B ASP 60   
383 1 Y 1 B ASP 61   ? B ASP 61   
384 1 Y 1 B GLY 62   ? B GLY 62   
385 1 Y 1 B HIS 63   ? B HIS 63   
386 1 Y 1 B ASP 64   ? B ASP 64   
387 1 Y 1 B ASP 65   ? B ASP 65   
388 1 Y 1 B GLY 66   ? B GLY 66   
389 1 Y 1 B HIS 67   ? B HIS 67   
390 1 Y 1 B ASP 68   ? B ASP 68   
391 1 Y 1 B ASP 69   ? B ASP 69   
392 1 Y 1 B LEU 70   ? B LEU 70   
393 1 Y 1 B HIS 71   ? B HIS 71   
394 1 Y 1 B ALA 72   ? B ALA 72   
395 1 Y 1 B HIS 73   ? B HIS 73   
396 1 Y 1 B SER 537  ? B SER 537  
397 1 Y 1 B ALA 538  ? B ALA 538  
398 1 Y 1 B LEU 539  ? B LEU 539  
399 1 Y 1 B SER 540  ? B SER 540  
400 1 Y 1 B ASP 541  ? B ASP 541  
401 1 Y 1 B ASP 542  ? B ASP 542  
402 1 Y 1 B GLU 543  ? B GLU 543  
403 1 Y 1 B ASN 544  ? B ASN 544  
404 1 Y 1 B ALA 545  ? B ALA 545  
405 1 Y 1 B PRO 546  ? B PRO 546  
406 1 Y 1 B ALA 547  ? B ALA 547  
407 1 Y 1 B ASP 548  ? B ASP 548  
408 1 Y 1 B GLU 549  ? B GLU 549  
409 1 Y 1 B LEU 550  ? B LEU 550  
410 1 Y 1 B THR 551  ? B THR 551  
411 1 Y 1 B LEU 552  ? B LEU 552  
412 1 Y 1 B GLY 553  ? B GLY 553  
413 1 Y 1 B GLU 554  ? B GLU 554  
414 1 Y 1 B ARG 555  ? B ARG 555  
415 1 Y 1 B LYS 556  ? B LYS 556  
416 1 Y 1 B SER 557  ? B SER 557  
417 1 Y 1 B VAL 558  ? B VAL 558  
418 1 Y 1 B CYS 559  ? B CYS 559  
419 1 Y 1 B PRO 560  ? B PRO 560  
420 1 Y 1 B GLY 561  ? B GLY 561  
421 1 Y 1 B CYS 562  ? B CYS 562  
422 1 Y 1 B LYS 563  ? B LYS 563  
423 1 Y 1 B ALA 564  ? B ALA 564  
424 1 Y 1 B MET 565  ? B MET 565  
425 1 Y 1 B VAL 566  ? B VAL 566  
426 1 Y 1 B PRO 567  ? B PRO 567  
427 1 Y 1 B ASN 568  ? B ASN 568  
428 1 Y 1 B GLU 569  ? B GLU 569  
429 1 Y 1 B GLU 654  ? B GLU 654  
430 1 Y 1 B LYS 655  ? B LYS 655  
431 1 Y 1 B LYS 656  ? B LYS 656  
432 1 Y 1 B ILE 657  ? B ILE 657  
433 1 Y 1 B ALA 658  ? B ALA 658  
434 1 Y 1 B ALA 659  ? B ALA 659  
435 1 Y 1 B ILE 660  ? B ILE 660  
436 1 Y 1 B PRO 661  ? B PRO 661  
437 1 Y 1 B MET 662  ? B MET 662  
438 1 Y 1 B PRO 663  ? B PRO 663  
439 1 Y 1 B LYS 664  ? B LYS 664  
440 1 Y 1 B TYR 665  ? B TYR 665  
441 1 Y 1 B LYS 666  ? B LYS 666  
442 1 Y 1 B LEU 667  ? B LEU 667  
443 1 Y 1 B GLY 668  ? B GLY 668  
444 1 Y 1 B LYS 669  ? B LYS 669  
445 1 Y 1 B VAL 701  ? B VAL 701  
446 1 Y 1 B GLN 702  ? B GLN 702  
447 1 Y 1 B ASP 703  ? B ASP 703  
448 1 Y 1 B LYS 704  ? B LYS 704  
449 1 Y 1 B MET 705  ? B MET 705  
450 1 Y 1 B ALA 706  ? B ALA 706  
451 1 Y 1 B SER 707  ? B SER 707  
452 1 Y 1 B VAL 708  ? B VAL 708  
453 1 Y 1 B SER 709  ? B SER 709  
454 1 Y 1 B THR 710  ? B THR 710  
455 1 Y 1 B MET 711  ? B MET 711  
456 1 Y 1 B ALA 712  ? B ALA 712  
457 1 Y 1 B ALA 713  ? B ALA 713  
458 1 Y 1 B PRO 714  ? B PRO 714  
459 1 Y 1 B GLY 715  ? B GLY 715  
460 1 Y 1 B SER 716  ? B SER 716  
461 1 Y 1 B THR 717  ? B THR 717  
462 1 Y 1 B VAL 718  ? B VAL 718  
463 1 Y 1 B SER 719  ? B SER 719  
464 1 Y 1 B SER 720  ? B SER 720  
465 1 Y 1 B GLU 721  ? B GLU 721  
466 1 Y 1 B PRO 722  ? B PRO 722  
467 1 Y 1 B SER 723  ? B SER 723  
468 1 Y 1 B SER 724  ? B SER 724  
469 1 Y 1 B LEU 725  ? B LEU 725  
470 1 Y 1 B GLN 726  ? B GLN 726  
471 1 Y 1 B LYS 727  ? B LYS 727  
472 1 Y 1 B ILE 728  ? B ILE 728  
473 1 Y 1 B GLU 729  ? B GLU 729  
474 1 Y 1 B ASP 777  ? B ASP 777  
475 1 Y 1 B ILE 778  ? B ILE 778  
476 1 Y 1 B ILE 779  ? B ILE 779  
477 1 Y 1 B ILE 780  ? B ILE 780  
478 1 Y 1 B ALA 781  ? B ALA 781  
479 1 Y 1 B GLU 782  ? B GLU 782  
480 1 Y 1 B THR 783  ? B THR 783  
481 1 Y 1 B LEU 784  ? B LEU 784  
482 1 Y 1 B LEU 785  ? B LEU 785  
483 1 Y 1 B LYS 786  ? B LYS 786  
484 1 Y 1 B GLY 787  ? B GLY 787  
485 1 Y 1 B SER 788  ? B SER 788  
486 1 Y 1 B ILE 789  ? B ILE 789  
487 1 Y 1 B THR 790  ? B THR 790  
488 1 Y 1 B ILE 791  ? B ILE 791  
489 1 Y 1 B ASN 792  ? B ASN 792  
490 1 Y 1 B LEU 793  ? B LEU 793  
491 1 Y 1 B SER 794  ? B SER 794  
492 1 Y 1 B SER 795  ? B SER 795  
493 1 Y 1 B ILE 796  ? B ILE 796  
494 1 Y 1 B SER 1012 ? B SER 1012 
495 1 Y 1 B ALA 1013 ? B ALA 1013 
496 1 Y 1 B PHE 1014 ? B PHE 1014 
497 1 Y 1 B LEU 1015 ? B LEU 1015 
498 1 Y 1 B ASP 1016 ? B ASP 1016 
499 1 Y 1 B HIS 1017 ? B HIS 1017 
500 1 Y 1 B ASP 1018 ? B ASP 1018 
501 1 Y 1 B ASN 1019 ? B ASN 1019 
502 1 Y 1 B PRO 1020 ? B PRO 1020 
503 1 Y 1 B PRO 1021 ? B PRO 1021 
504 1 Y 1 B VAL 1022 ? B VAL 1022 
505 1 Y 1 B THR 1023 ? B THR 1023 
506 1 Y 1 B ALA 1024 ? B ALA 1024 
507 1 Y 1 B GLY 1025 ? B GLY 1025 
508 1 Y 1 B SER 1026 ? B SER 1026 
509 1 Y 1 B GLU 1027 ? B GLU 1027 
510 1 Y 1 B GLU 1028 ? B GLU 1028 
511 1 Y 1 B ASN 1029 ? B ASN 1029 
512 1 Y 1 B GLU 1030 ? B GLU 1030 
513 1 Y 1 B TYR 1194 ? B TYR 1194 
514 1 Y 1 B ASN 1195 ? B ASN 1195 
515 1 Y 1 B GLY 1196 ? B GLY 1196 
516 1 Y 1 B PRO 1197 ? B PRO 1197 
517 1 Y 1 B ILE 1198 ? B ILE 1198 
518 1 Y 1 B LEU 1199 ? B LEU 1199 
519 1 Y 1 B ASP 1200 ? B ASP 1200 
520 1 Y 1 B GLY 1201 ? B GLY 1201 
521 1 Y 1 B ARG 1202 ? B ARG 1202 
522 1 Y 1 B LEU 1203 ? B LEU 1203 
523 1 Y 1 B ASP 1204 ? B ASP 1204 
524 1 Y 1 B VAL 1205 ? B VAL 1205 
525 1 Y 1 B ASP 1206 ? B ASP 1206 
526 1 Y 1 B SER 1207 ? B SER 1207 
527 1 Y 1 B LYS 1208 ? B LYS 1208 
528 1 Y 1 B ARG 1209 ? B ARG 1209 
529 1 Y 1 B SER 1210 ? B SER 1210 
530 1 Y 1 B LEU 1211 ? B LEU 1211 
531 1 Y 1 B ILE 1212 ? B ILE 1212 
532 1 Y 1 B SER 1213 ? B SER 1213 
533 1 Y 1 B ILE 1214 ? B ILE 1214 
534 1 Y 1 B THR 1215 ? B THR 1215 
535 1 Y 1 B GLU 1216 ? B GLU 1216 
536 1 Y 1 B ILE 1217 ? B ILE 1217 
537 1 Y 1 B SER 1218 ? B SER 1218 
538 1 Y 1 B SER 1219 ? B SER 1219 
539 1 Y 1 B ASN 1220 ? B ASN 1220 
540 1 Y 1 B MET 1221 ? B MET 1221 
541 1 Y 1 B CYS 1222 ? B CYS 1222 
542 1 Y 1 B LEU 1223 ? B LEU 1223 
543 1 Y 1 B LYS 1224 ? B LYS 1224 
544 1 Y 1 B HIS 1225 ? B HIS 1225 
545 1 Y 1 B ALA 1226 ? B ALA 1226 
546 1 Y 1 B ALA 1227 ? B ALA 1227 
547 1 Y 1 B GLU 1228 ? B GLU 1228 
548 1 Y 1 B LEU 1229 ? B LEU 1229 
549 1 Y 1 B ARG 1230 ? B ARG 1230 
550 1 Y 1 B GLN 1231 ? B GLN 1231 
551 1 Y 1 B LYS 1232 ? B LYS 1232 
552 1 Y 1 B ASN 1233 ? B ASN 1233 
553 1 Y 1 B SER 1234 ? B SER 1234 
554 1 Y 1 B LYS 1235 ? B LYS 1235 
555 1 Y 1 B VAL 1236 ? B VAL 1236 
556 1 Y 1 B MET 1237 ? B MET 1237 
557 1 Y 1 B LEU 1238 ? B LEU 1238 
558 1 Y 1 B SER 1239 ? B SER 1239 
559 1 Y 1 B ARG 1240 ? B ARG 1240 
560 1 Y 1 B LYS 1241 ? B LYS 1241 
561 1 Y 1 B SER 1242 ? B SER 1242 
562 1 Y 1 B SER 1243 ? B SER 1243 
563 1 Y 1 B GLY 1244 ? B GLY 1244 
564 1 Y 1 B ALA 1245 ? B ALA 1245 
565 1 Y 1 B ALA 1246 ? B ALA 1246 
566 1 Y 1 B ALA 1247 ? B ALA 1247 
567 1 Y 1 B LYS 1248 ? B LYS 1248 
568 1 Y 1 B GLU 1249 ? B GLU 1249 
569 1 Y 1 B GLU 1250 ? B GLU 1250 
570 1 Y 1 B GLU 1251 ? B GLU 1251 
571 1 Y 1 B ASP 1252 ? B ASP 1252 
572 1 Y 1 B CYS 1253 ? B CYS 1253 
573 1 Y 1 B ILE 1254 ? B ILE 1254 
574 1 Y 1 B PRO 1255 ? B PRO 1255 
575 1 Y 1 B ASN 1256 ? B ASN 1256 
576 1 Y 1 B THR 1257 ? B THR 1257 
577 1 Y 1 B SER 1258 ? B SER 1258 
578 1 Y 1 B ASP 1259 ? B ASP 1259 
579 1 Y 1 B VAL 1260 ? B VAL 1260 
580 1 Y 1 B GLU 1261 ? B GLU 1261 
581 1 Y 1 B GLN 1262 ? B GLN 1262 
582 1 Y 1 B ALA 1263 ? B ALA 1263 
583 1 Y 1 B ALA 1264 ? B ALA 1264 
584 1 Y 1 B GLY 1265 ? B GLY 1265 
585 1 Y 1 B VAL 1266 ? B VAL 1266 
586 1 Y 1 B SER 1267 ? B SER 1267 
587 1 Y 1 B PRO 1268 ? B PRO 1268 
588 1 Y 1 B SER 1269 ? B SER 1269 
589 1 Y 1 B VAL 1270 ? B VAL 1270 
590 1 Y 1 B PRO 1271 ? B PRO 1271 
591 1 Y 1 B THR 1272 ? B THR 1272 
592 1 Y 1 B LYS 1273 ? B LYS 1273 
593 1 Y 1 B THR 1274 ? B THR 1274 
594 1 Y 1 B THR 1275 ? B THR 1275 
595 1 Y 1 B PRO 1276 ? B PRO 1276 
596 1 Y 1 B LYS 1277 ? B LYS 1277 
597 1 Y 1 B PRO 1278 ? B PRO 1278 
598 1 Y 1 B LYS 1279 ? B LYS 1279 
599 1 Y 1 B SER 1280 ? B SER 1280 
600 1 Y 1 B PHE 1281 ? B PHE 1281 
601 1 Y 1 B LEU 1282 ? B LEU 1282 
602 1 Y 1 B PRO 1283 ? B PRO 1283 
603 1 Y 1 B SER 1284 ? B SER 1284 
604 1 Y 1 B LEU 1285 ? B LEU 1285 
605 1 Y 1 B GLY 1286 ? B GLY 1286 
606 1 Y 1 B LEU 1287 ? B LEU 1287 
607 1 Y 1 B SER 1288 ? B SER 1288 
608 1 Y 1 B MET 1289 ? B MET 1289 
609 1 Y 1 B SER 1290 ? B SER 1290 
610 1 Y 1 B LYS 1291 ? B LYS 1291 
611 1 Y 1 B GLU 1292 ? B GLU 1292 
612 1 Y 1 B ARG 1293 ? B ARG 1293 
613 1 Y 1 B VAL 1294 ? B VAL 1294 
614 1 Y 1 B ASN 1295 ? B ASN 1295 
615 1 Y 1 B GLY 1296 ? B GLY 1296 
616 1 Y 1 B GLU 1297 ? B GLU 1297 
617 1 Y 1 B ALA 1298 ? B ALA 1298 
618 1 Y 1 B VAL 1299 ? B VAL 1299 
619 1 Y 1 B GLU 1300 ? B GLU 1300 
620 1 Y 1 B GLU 1301 ? B GLU 1301 
621 1 Y 1 B SER 1302 ? B SER 1302 
622 1 Y 1 B PRO 1303 ? B PRO 1303 
623 1 Y 1 B VAL 1304 ? B VAL 1304 
624 1 Y 1 B LYS 1305 ? B LYS 1305 
625 1 Y 1 B THR 1306 ? B THR 1306 
626 1 Y 1 B LYS 1307 ? B LYS 1307 
627 1 Y 1 B GLN 1308 ? B GLN 1308 
628 1 Y 1 B GLY 1309 ? B GLY 1309 
629 1 Y 1 B GLU 1310 ? B GLU 1310 
630 1 Y 1 B GLU 1311 ? B GLU 1311 
631 1 Y 1 B THR 1312 ? B THR 1312 
632 1 Y 1 B PRO 1313 ? B PRO 1313 
633 1 Y 1 B GLU 1314 ? B GLU 1314 
634 1 Y 1 B THR 1315 ? B THR 1315 
635 1 Y 1 B GLU 1316 ? B GLU 1316 
636 1 Y 1 B GLU 1317 ? B GLU 1317 
637 1 Y 1 B GLY 1318 ? B GLY 1318 
638 1 Y 1 B ALA 1319 ? B ALA 1319 
639 1 Y 1 B ALA 1320 ? B ALA 1320 
640 1 Y 1 B PRO 1321 ? B PRO 1321 
641 1 Y 1 B ARG 1322 ? B ARG 1322 
642 1 Y 1 B VAL 1323 ? B VAL 1323 
643 1 Y 1 B ASN 1324 ? B ASN 1324 
644 1 Y 1 B VAL 1325 ? B VAL 1325 
# 
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 
AJP C01  C N N 1   
AJP C02  C N R 2   
AJP C03  C N N 3   
AJP C04  C N N 4   
AJP C05  C N R 5   
AJP C06  C N S 6   
AJP C07  C N R 7   
AJP C08  C N R 8   
AJP O09  O N N 9   
AJP C10  C N S 10  
AJP C11  C N S 11  
AJP C12  C N S 12  
AJP C13  C N N 13  
AJP C14  C N N 14  
AJP C15  C N S 15  
AJP C16  C N R 16  
AJP C17  C N N 17  
AJP C18  C N N 18  
AJP C19  C N S 19  
AJP C20  C N S 20  
AJP C21  C N N 21  
AJP C22  C N R 22  
AJP C23  C N R 23  
AJP C24  C N N 24  
AJP O25  O N N 25  
AJP C26  C N R 26  
AJP C27  C N R 27  
AJP C28  C N R 28  
AJP C29  C N R 29  
AJP C30  C N R 30  
AJP O31  O N N 31  
AJP C32  C N N 32  
AJP O33  O N N 33  
AJP O34  O N N 34  
AJP C35  C N S 35  
AJP C36  C N R 36  
AJP C37  C N S 37  
AJP C38  C N R 38  
AJP C39  C N R 39  
AJP O40  O N N 40  
AJP C41  C N N 41  
AJP O42  O N N 42  
AJP O43  O N N 43  
AJP O44  O N N 44  
AJP C45  C N S 45  
AJP C46  C N R 46  
AJP C47  C N S 47  
AJP C48  C N R 48  
AJP C49  C N N 49  
AJP O50  O N N 50  
AJP O51  O N N 51  
AJP O52  O N N 52  
AJP O53  O N N 53  
AJP O54  O N N 54  
AJP C55  C N S 55  
AJP C56  C N R 56  
AJP C57  C N S 57  
AJP C58  C N S 58  
AJP C59  C N R 59  
AJP O60  O N N 60  
AJP C61  C N N 61  
AJP O62  O N N 62  
AJP O63  O N N 63  
AJP O64  O N N 64  
AJP C65  C N S 65  
AJP C66  C N R 66  
AJP C67  C N S 67  
AJP C68  C N S 68  
AJP C69  C N R 69  
AJP O70  O N N 70  
AJP C71  C N N 71  
AJP O72  O N N 72  
AJP O73  O N N 73  
AJP O74  O N N 74  
AJP O75  O N N 75  
AJP O76  O N N 76  
AJP O77  O N N 77  
AJP O78  O N N 78  
AJP O79  O N N 79  
AJP C80  C N N 80  
AJP C81  C N N 81  
AJP O82  O N N 82  
AJP C83  C N N 83  
AJP O84  O N N 84  
AJP C85  C N N 85  
AJP H1   H N N 86  
AJP H2   H N N 87  
AJP H3   H N N 88  
AJP H4   H N N 89  
AJP H5   H N N 90  
AJP H6   H N N 91  
AJP H7   H N N 92  
AJP H8   H N N 93  
AJP H9   H N N 94  
AJP H10  H N N 95  
AJP H11  H N N 96  
AJP H12  H N N 97  
AJP H13  H N N 98  
AJP H14  H N N 99  
AJP H15  H N N 100 
AJP H16  H N N 101 
AJP H17  H N N 102 
AJP H18  H N N 103 
AJP H19  H N N 104 
AJP H20  H N N 105 
AJP H21  H N N 106 
AJP H22  H N N 107 
AJP H23  H N N 108 
AJP H24  H N N 109 
AJP H25  H N N 110 
AJP H26  H N N 111 
AJP H27  H N N 112 
AJP H28  H N N 113 
AJP H29  H N N 114 
AJP H30  H N N 115 
AJP H31  H N N 116 
AJP H32  H N N 117 
AJP H33  H N N 118 
AJP H34  H N N 119 
AJP H35  H N N 120 
AJP H36  H N N 121 
AJP H37  H N N 122 
AJP H38  H N N 123 
AJP H39  H N N 124 
AJP H40  H N N 125 
AJP H41  H N N 126 
AJP H42  H N N 127 
AJP H43  H N N 128 
AJP H44  H N N 129 
AJP H45  H N N 130 
AJP H46  H N N 131 
AJP H47  H N N 132 
AJP H48  H N N 133 
AJP H49  H N N 134 
AJP H50  H N N 135 
AJP H51  H N N 136 
AJP H52  H N N 137 
AJP H53  H N N 138 
AJP H54  H N N 139 
AJP H55  H N N 140 
AJP H56  H N N 141 
AJP H57  H N N 142 
AJP H58  H N N 143 
AJP H59  H N N 144 
AJP H60  H N N 145 
AJP H61  H N N 146 
AJP H62  H N N 147 
AJP H63  H N N 148 
AJP H64  H N N 149 
AJP H65  H N N 150 
AJP H66  H N N 151 
AJP H67  H N N 152 
AJP H68  H N N 153 
AJP H69  H N N 154 
AJP H70  H N N 155 
AJP H71  H N N 156 
AJP H72  H N N 157 
AJP H73  H N N 158 
AJP H74  H N N 159 
AJP H75  H N N 160 
AJP H76  H N N 161 
AJP H77  H N N 162 
AJP H78  H N N 163 
AJP H79  H N N 164 
AJP H80  H N N 165 
AJP H81  H N N 166 
AJP H82  H N N 167 
AJP H83  H N N 168 
AJP H84  H N N 169 
AJP H85  H N N 170 
AJP H86  H N N 171 
AJP H87  H N N 172 
AJP H88  H N N 173 
AJP H89  H N N 174 
AJP H90  H N N 175 
AJP H91  H N N 176 
AJP H92  H N N 177 
ALA N    N N N 178 
ALA CA   C N S 179 
ALA C    C N N 180 
ALA O    O N N 181 
ALA CB   C N N 182 
ALA OXT  O N N 183 
ALA H    H N N 184 
ALA H2   H N N 185 
ALA HA   H N N 186 
ALA HB1  H N N 187 
ALA HB2  H N N 188 
ALA HB3  H N N 189 
ALA HXT  H N N 190 
ARG N    N N N 191 
ARG CA   C N S 192 
ARG C    C N N 193 
ARG O    O N N 194 
ARG CB   C N N 195 
ARG CG   C N N 196 
ARG CD   C N N 197 
ARG NE   N N N 198 
ARG CZ   C N N 199 
ARG NH1  N N N 200 
ARG NH2  N N N 201 
ARG OXT  O N N 202 
ARG H    H N N 203 
ARG H2   H N N 204 
ARG HA   H N N 205 
ARG HB2  H N N 206 
ARG HB3  H N N 207 
ARG HG2  H N N 208 
ARG HG3  H N N 209 
ARG HD2  H N N 210 
ARG HD3  H N N 211 
ARG HE   H N N 212 
ARG HH11 H N N 213 
ARG HH12 H N N 214 
ARG HH21 H N N 215 
ARG HH22 H N N 216 
ARG HXT  H N N 217 
ASN N    N N N 218 
ASN CA   C N S 219 
ASN C    C N N 220 
ASN O    O N N 221 
ASN CB   C N N 222 
ASN CG   C N N 223 
ASN OD1  O N N 224 
ASN ND2  N N N 225 
ASN OXT  O N N 226 
ASN H    H N N 227 
ASN H2   H N N 228 
ASN HA   H N N 229 
ASN HB2  H N N 230 
ASN HB3  H N N 231 
ASN HD21 H N N 232 
ASN HD22 H N N 233 
ASN HXT  H N N 234 
ASP N    N N N 235 
ASP CA   C N S 236 
ASP C    C N N 237 
ASP O    O N N 238 
ASP CB   C N N 239 
ASP CG   C N N 240 
ASP OD1  O N N 241 
ASP OD2  O N N 242 
ASP OXT  O N N 243 
ASP H    H N N 244 
ASP H2   H N N 245 
ASP HA   H N N 246 
ASP HB2  H N N 247 
ASP HB3  H N N 248 
ASP HD2  H N N 249 
ASP HXT  H N N 250 
CYS N    N N N 251 
CYS CA   C N R 252 
CYS C    C N N 253 
CYS O    O N N 254 
CYS CB   C N N 255 
CYS SG   S N N 256 
CYS OXT  O N N 257 
CYS H    H N N 258 
CYS H2   H N N 259 
CYS HA   H N N 260 
CYS HB2  H N N 261 
CYS HB3  H N N 262 
CYS HG   H N N 263 
CYS HXT  H N N 264 
GLN N    N N N 265 
GLN CA   C N S 266 
GLN C    C N N 267 
GLN O    O N N 268 
GLN CB   C N N 269 
GLN CG   C N N 270 
GLN CD   C N N 271 
GLN OE1  O N N 272 
GLN NE2  N N N 273 
GLN OXT  O N N 274 
GLN H    H N N 275 
GLN H2   H N N 276 
GLN HA   H N N 277 
GLN HB2  H N N 278 
GLN HB3  H N N 279 
GLN HG2  H N N 280 
GLN HG3  H N N 281 
GLN HE21 H N N 282 
GLN HE22 H N N 283 
GLN HXT  H N N 284 
GLU N    N N N 285 
GLU CA   C N S 286 
GLU C    C N N 287 
GLU O    O N N 288 
GLU CB   C N N 289 
GLU CG   C N N 290 
GLU CD   C N N 291 
GLU OE1  O N N 292 
GLU OE2  O N N 293 
GLU OXT  O N N 294 
GLU H    H N N 295 
GLU H2   H N N 296 
GLU HA   H N N 297 
GLU HB2  H N N 298 
GLU HB3  H N N 299 
GLU HG2  H N N 300 
GLU HG3  H N N 301 
GLU HE2  H N N 302 
GLU HXT  H N N 303 
GLY N    N N N 304 
GLY CA   C N N 305 
GLY C    C N N 306 
GLY O    O N N 307 
GLY OXT  O N N 308 
GLY H    H N N 309 
GLY H2   H N N 310 
GLY HA2  H N N 311 
GLY HA3  H N N 312 
GLY HXT  H N N 313 
HIS N    N N N 314 
HIS CA   C N S 315 
HIS C    C N N 316 
HIS O    O N N 317 
HIS CB   C N N 318 
HIS CG   C Y N 319 
HIS ND1  N Y N 320 
HIS CD2  C Y N 321 
HIS CE1  C Y N 322 
HIS NE2  N Y N 323 
HIS OXT  O N N 324 
HIS H    H N N 325 
HIS H2   H N N 326 
HIS HA   H N N 327 
HIS HB2  H N N 328 
HIS HB3  H N N 329 
HIS HD1  H N N 330 
HIS HD2  H N N 331 
HIS HE1  H N N 332 
HIS HE2  H N N 333 
HIS HXT  H N N 334 
ILE N    N N N 335 
ILE CA   C N S 336 
ILE C    C N N 337 
ILE O    O N N 338 
ILE CB   C N S 339 
ILE CG1  C N N 340 
ILE CG2  C N N 341 
ILE CD1  C N N 342 
ILE OXT  O N N 343 
ILE H    H N N 344 
ILE H2   H N N 345 
ILE HA   H N N 346 
ILE HB   H N N 347 
ILE HG12 H N N 348 
ILE HG13 H N N 349 
ILE HG21 H N N 350 
ILE HG22 H N N 351 
ILE HG23 H N N 352 
ILE HD11 H N N 353 
ILE HD12 H N N 354 
ILE HD13 H N N 355 
ILE HXT  H N N 356 
LEU N    N N N 357 
LEU CA   C N S 358 
LEU C    C N N 359 
LEU O    O N N 360 
LEU CB   C N N 361 
LEU CG   C N N 362 
LEU CD1  C N N 363 
LEU CD2  C N N 364 
LEU OXT  O N N 365 
LEU H    H N N 366 
LEU H2   H N N 367 
LEU HA   H N N 368 
LEU HB2  H N N 369 
LEU HB3  H N N 370 
LEU HG   H N N 371 
LEU HD11 H N N 372 
LEU HD12 H N N 373 
LEU HD13 H N N 374 
LEU HD21 H N N 375 
LEU HD22 H N N 376 
LEU HD23 H N N 377 
LEU HXT  H N N 378 
LYS N    N N N 379 
LYS CA   C N S 380 
LYS C    C N N 381 
LYS O    O N N 382 
LYS CB   C N N 383 
LYS CG   C N N 384 
LYS CD   C N N 385 
LYS CE   C N N 386 
LYS NZ   N N N 387 
LYS OXT  O N N 388 
LYS H    H N N 389 
LYS H2   H N N 390 
LYS HA   H N N 391 
LYS HB2  H N N 392 
LYS HB3  H N N 393 
LYS HG2  H N N 394 
LYS HG3  H N N 395 
LYS HD2  H N N 396 
LYS HD3  H N N 397 
LYS HE2  H N N 398 
LYS HE3  H N N 399 
LYS HZ1  H N N 400 
LYS HZ2  H N N 401 
LYS HZ3  H N N 402 
LYS HXT  H N N 403 
MET N    N N N 404 
MET CA   C N S 405 
MET C    C N N 406 
MET O    O N N 407 
MET CB   C N N 408 
MET CG   C N N 409 
MET SD   S N N 410 
MET CE   C N N 411 
MET OXT  O N N 412 
MET H    H N N 413 
MET H2   H N N 414 
MET HA   H N N 415 
MET HB2  H N N 416 
MET HB3  H N N 417 
MET HG2  H N N 418 
MET HG3  H N N 419 
MET HE1  H N N 420 
MET HE2  H N N 421 
MET HE3  H N N 422 
MET HXT  H N N 423 
PHE N    N N N 424 
PHE CA   C N S 425 
PHE C    C N N 426 
PHE O    O N N 427 
PHE CB   C N N 428 
PHE CG   C Y N 429 
PHE CD1  C Y N 430 
PHE CD2  C Y N 431 
PHE CE1  C Y N 432 
PHE CE2  C Y N 433 
PHE CZ   C Y N 434 
PHE OXT  O N N 435 
PHE H    H N N 436 
PHE H2   H N N 437 
PHE HA   H N N 438 
PHE HB2  H N N 439 
PHE HB3  H N N 440 
PHE HD1  H N N 441 
PHE HD2  H N N 442 
PHE HE1  H N N 443 
PHE HE2  H N N 444 
PHE HZ   H N N 445 
PHE HXT  H N N 446 
POV N    N N N 447 
POV P    P N N 448 
POV C1   C N N 449 
POV C2   C N S 450 
POV C3   C N N 451 
POV C210 C N N 452 
POV C310 C N N 453 
POV C11  C N N 454 
POV O11  O N N 455 
POV C211 C N N 456 
POV C311 C N N 457 
POV C12  C N N 458 
POV O12  O N N 459 
POV C212 C N N 460 
POV C312 C N N 461 
POV C13  C N N 462 
POV O13  O N N 463 
POV C213 C N N 464 
POV C313 C N N 465 
POV C14  C N N 466 
POV O14  O N N 467 
POV C214 C N N 468 
POV C314 C N N 469 
POV C15  C N N 470 
POV C215 C N N 471 
POV C315 C N N 472 
POV C216 C N N 473 
POV C316 C N N 474 
POV C217 C N N 475 
POV C218 C N N 476 
POV C21  C N N 477 
POV O21  O N N 478 
POV C22  C N N 479 
POV O22  O N N 480 
POV C23  C N N 481 
POV C24  C N N 482 
POV C25  C N N 483 
POV C26  C N N 484 
POV C27  C N N 485 
POV C28  C N N 486 
POV C29  C N N 487 
POV C31  C N N 488 
POV O31  O N N 489 
POV C32  C N N 490 
POV O32  O N N 491 
POV C33  C N N 492 
POV C34  C N N 493 
POV C35  C N N 494 
POV C36  C N N 495 
POV C37  C N N 496 
POV C38  C N N 497 
POV C39  C N N 498 
POV H29  H N N 499 
POV H1   H N N 500 
POV H1A  H N N 501 
POV H2   H N N 502 
POV H3   H N N 503 
POV H3A  H N N 504 
POV H310 H N N 505 
POV H31A H N N 506 
POV H210 H N N 507 
POV H11  H N N 508 
POV H11A H N N 509 
POV H211 H N N 510 
POV H21A H N N 511 
POV H311 H N N 512 
POV H31B H N N 513 
POV H12  H N N 514 
POV H12A H N N 515 
POV H22  H N N 516 
POV H212 H N N 517 
POV H22A H N N 518 
POV H21B H N N 519 
POV H32  H N N 520 
POV H312 H N N 521 
POV H32A H N N 522 
POV H31C H N N 523 
POV H13  H N N 524 
POV H13A H N N 525 
POV H13B H N N 526 
POV H23  H N N 527 
POV H213 H N N 528 
POV H23A H N N 529 
POV H21C H N N 530 
POV H33  H N N 531 
POV H313 H N N 532 
POV H33A H N N 533 
POV H31D H N N 534 
POV H14  H N N 535 
POV H14A H N N 536 
POV H14B H N N 537 
POV H24  H N N 538 
POV H214 H N N 539 
POV H24A H N N 540 
POV H21D H N N 541 
POV H34  H N N 542 
POV H314 H N N 543 
POV H34A H N N 544 
POV H31E H N N 545 
POV H15  H N N 546 
POV H15A H N N 547 
POV H15B H N N 548 
POV H25  H N N 549 
POV H215 H N N 550 
POV H25A H N N 551 
POV H21E H N N 552 
POV H35  H N N 553 
POV H315 H N N 554 
POV H35A H N N 555 
POV H31F H N N 556 
POV H26  H N N 557 
POV H216 H N N 558 
POV H26A H N N 559 
POV H21F H N N 560 
POV H36  H N N 561 
POV H316 H N N 562 
POV H36A H N N 563 
POV H31G H N N 564 
POV H31H H N N 565 
POV H27  H N N 566 
POV H217 H N N 567 
POV H27A H N N 568 
POV H21G H N N 569 
POV H37  H N N 570 
POV H37A H N N 571 
POV H28  H N N 572 
POV H218 H N N 573 
POV H28A H N N 574 
POV H21H H N N 575 
POV H21J H N N 576 
POV H38  H N N 577 
POV H38A H N N 578 
POV H39  H N N 579 
POV H39A H N N 580 
PRO N    N N N 581 
PRO CA   C N S 582 
PRO C    C N N 583 
PRO O    O N N 584 
PRO CB   C N N 585 
PRO CG   C N N 586 
PRO CD   C N N 587 
PRO OXT  O N N 588 
PRO H    H N N 589 
PRO HA   H N N 590 
PRO HB2  H N N 591 
PRO HB3  H N N 592 
PRO HG2  H N N 593 
PRO HG3  H N N 594 
PRO HD2  H N N 595 
PRO HD3  H N N 596 
PRO HXT  H N N 597 
SER N    N N N 598 
SER CA   C N S 599 
SER C    C N N 600 
SER O    O N N 601 
SER CB   C N N 602 
SER OG   O N N 603 
SER OXT  O N N 604 
SER H    H N N 605 
SER H2   H N N 606 
SER HA   H N N 607 
SER HB2  H N N 608 
SER HB3  H N N 609 
SER HG   H N N 610 
SER HXT  H N N 611 
THR N    N N N 612 
THR CA   C N S 613 
THR C    C N N 614 
THR O    O N N 615 
THR CB   C N R 616 
THR OG1  O N N 617 
THR CG2  C N N 618 
THR OXT  O N N 619 
THR H    H N N 620 
THR H2   H N N 621 
THR HA   H N N 622 
THR HB   H N N 623 
THR HG1  H N N 624 
THR HG21 H N N 625 
THR HG22 H N N 626 
THR HG23 H N N 627 
THR HXT  H N N 628 
TRP N    N N N 629 
TRP CA   C N S 630 
TRP C    C N N 631 
TRP O    O N N 632 
TRP CB   C N N 633 
TRP CG   C Y N 634 
TRP CD1  C Y N 635 
TRP CD2  C Y N 636 
TRP NE1  N Y N 637 
TRP CE2  C Y N 638 
TRP CE3  C Y N 639 
TRP CZ2  C Y N 640 
TRP CZ3  C Y N 641 
TRP CH2  C Y N 642 
TRP OXT  O N N 643 
TRP H    H N N 644 
TRP H2   H N N 645 
TRP HA   H N N 646 
TRP HB2  H N N 647 
TRP HB3  H N N 648 
TRP HD1  H N N 649 
TRP HE1  H N N 650 
TRP HE3  H N N 651 
TRP HZ2  H N N 652 
TRP HZ3  H N N 653 
TRP HH2  H N N 654 
TRP HXT  H N N 655 
TYR N    N N N 656 
TYR CA   C N S 657 
TYR C    C N N 658 
TYR O    O N N 659 
TYR CB   C N N 660 
TYR CG   C Y N 661 
TYR CD1  C Y N 662 
TYR CD2  C Y N 663 
TYR CE1  C Y N 664 
TYR CE2  C Y N 665 
TYR CZ   C Y N 666 
TYR OH   O N N 667 
TYR OXT  O N N 668 
TYR H    H N N 669 
TYR H2   H N N 670 
TYR HA   H N N 671 
TYR HB2  H N N 672 
TYR HB3  H N N 673 
TYR HD1  H N N 674 
TYR HD2  H N N 675 
TYR HE1  H N N 676 
TYR HE2  H N N 677 
TYR HH   H N N 678 
TYR HXT  H N N 679 
VAL N    N N N 680 
VAL CA   C N S 681 
VAL C    C N N 682 
VAL O    O N N 683 
VAL CB   C N N 684 
VAL CG1  C N N 685 
VAL CG2  C N N 686 
VAL OXT  O N N 687 
VAL H    H N N 688 
VAL H2   H N N 689 
VAL HA   H N N 690 
VAL HB   H N N 691 
VAL HG11 H N N 692 
VAL HG12 H N N 693 
VAL HG13 H N N 694 
VAL HG21 H N N 695 
VAL HG22 H N N 696 
VAL HG23 H N N 697 
VAL HXT  H N N 698 
# 
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 
AJP C01  C02  sing N N 1   
AJP C02  C85  sing N N 2   
AJP C02  C03  sing N N 3   
AJP C85  O84  sing N N 4   
AJP C03  C04  sing N N 5   
AJP O84  C05  sing N N 6   
AJP C05  C04  sing N N 7   
AJP C05  O09  sing N N 8   
AJP C05  C06  sing N N 9   
AJP O09  C08  sing N N 10  
AJP C08  C10  sing N N 11  
AJP C08  C07  sing N N 12  
AJP C83  C06  sing N N 13  
AJP C06  C07  sing N N 14  
AJP C10  O82  sing N N 15  
AJP C10  C11  sing N N 16  
AJP C07  C12  sing N N 17  
AJP C11  C12  sing N N 18  
AJP C11  C16  sing N N 19  
AJP C12  C81  sing N N 20  
AJP C12  C13  sing N N 21  
AJP C17  C16  sing N N 22  
AJP C17  C18  sing N N 23  
AJP C13  C14  sing N N 24  
AJP C16  C15  sing N N 25  
AJP C15  C14  sing N N 26  
AJP C15  C20  sing N N 27  
AJP C18  C19  sing N N 28  
AJP C19  C20  sing N N 29  
AJP C19  C24  sing N N 30  
AJP C20  C21  sing N N 31  
AJP C20  C80  sing N N 32  
AJP C21  C22  sing N N 33  
AJP C24  C23  sing N N 34  
AJP O33  C32  sing N N 35  
AJP C23  C22  sing N N 36  
AJP C23  O25  sing N N 37  
AJP C32  C30  sing N N 38  
AJP C22  O79  sing N N 39  
AJP C30  O31  sing N N 40  
AJP C30  C29  sing N N 41  
AJP O31  C26  sing N N 42  
AJP C26  O25  sing N N 43  
AJP C26  C27  sing N N 44  
AJP C29  C28  sing N N 45  
AJP C29  O34  sing N N 46  
AJP C41  C39  sing N N 47  
AJP C41  O42  sing N N 48  
AJP C28  C27  sing N N 49  
AJP C28  O77  sing N N 50  
AJP C27  O78  sing N N 51  
AJP O40  C39  sing N N 52  
AJP O40  C35  sing N N 53  
AJP C39  C38  sing N N 54  
AJP O34  C35  sing N N 55  
AJP C35  C36  sing N N 56  
AJP C38  O43  sing N N 57  
AJP C38  C37  sing N N 58  
AJP C36  C37  sing N N 59  
AJP C36  O54  sing N N 60  
AJP C37  O44  sing N N 61  
AJP O54  C55  sing N N 62  
AJP O76  C56  sing N N 63  
AJP O50  C49  sing N N 64  
AJP O50  C45  sing N N 65  
AJP C56  C55  sing N N 66  
AJP C56  C57  sing N N 67  
AJP O44  C45  sing N N 68  
AJP C55  O60  sing N N 69  
AJP C49  C48  sing N N 70  
AJP C45  C46  sing N N 71  
AJP O60  C59  sing N N 72  
AJP O63  C58  sing N N 73  
AJP O75  C66  sing N N 74  
AJP O64  C57  sing N N 75  
AJP O64  C65  sing N N 76  
AJP C57  C58  sing N N 77  
AJP O62  C61  sing N N 78  
AJP C48  O51  sing N N 79  
AJP C48  C47  sing N N 80  
AJP C58  C59  sing N N 81  
AJP C59  C61  sing N N 82  
AJP C46  C47  sing N N 83  
AJP C46  O53  sing N N 84  
AJP C66  C65  sing N N 85  
AJP C66  C67  sing N N 86  
AJP C65  O70  sing N N 87  
AJP C47  O52  sing N N 88  
AJP O74  C67  sing N N 89  
AJP C67  C68  sing N N 90  
AJP O70  C69  sing N N 91  
AJP C68  C69  sing N N 92  
AJP C68  O73  sing N N 93  
AJP C69  C71  sing N N 94  
AJP C71  O72  sing N N 95  
AJP C01  H1   sing N N 96  
AJP C01  H2   sing N N 97  
AJP C01  H3   sing N N 98  
AJP C02  H4   sing N N 99  
AJP C03  H5   sing N N 100 
AJP C03  H6   sing N N 101 
AJP C04  H7   sing N N 102 
AJP C04  H8   sing N N 103 
AJP C06  H9   sing N N 104 
AJP C07  H10  sing N N 105 
AJP C08  H11  sing N N 106 
AJP C10  H12  sing N N 107 
AJP C11  H13  sing N N 108 
AJP C13  H14  sing N N 109 
AJP C13  H15  sing N N 110 
AJP C14  H16  sing N N 111 
AJP C14  H17  sing N N 112 
AJP C15  H18  sing N N 113 
AJP C16  H19  sing N N 114 
AJP C17  H20  sing N N 115 
AJP C17  H21  sing N N 116 
AJP C18  H22  sing N N 117 
AJP C18  H23  sing N N 118 
AJP C19  H24  sing N N 119 
AJP C21  H25  sing N N 120 
AJP C21  H26  sing N N 121 
AJP C22  H27  sing N N 122 
AJP C23  H28  sing N N 123 
AJP C24  H29  sing N N 124 
AJP C24  H30  sing N N 125 
AJP C26  H31  sing N N 126 
AJP C27  H32  sing N N 127 
AJP C28  H33  sing N N 128 
AJP C29  H34  sing N N 129 
AJP C30  H35  sing N N 130 
AJP C32  H36  sing N N 131 
AJP C32  H37  sing N N 132 
AJP O33  H38  sing N N 133 
AJP C35  H39  sing N N 134 
AJP C36  H40  sing N N 135 
AJP C37  H41  sing N N 136 
AJP C38  H42  sing N N 137 
AJP C39  H43  sing N N 138 
AJP C41  H44  sing N N 139 
AJP C41  H45  sing N N 140 
AJP O42  H46  sing N N 141 
AJP O43  H47  sing N N 142 
AJP C45  H48  sing N N 143 
AJP C46  H49  sing N N 144 
AJP C47  H50  sing N N 145 
AJP C48  H51  sing N N 146 
AJP C49  H52  sing N N 147 
AJP C49  H53  sing N N 148 
AJP O51  H54  sing N N 149 
AJP O52  H55  sing N N 150 
AJP O53  H56  sing N N 151 
AJP C55  H57  sing N N 152 
AJP C56  H58  sing N N 153 
AJP C57  H59  sing N N 154 
AJP C58  H60  sing N N 155 
AJP C59  H61  sing N N 156 
AJP C61  H62  sing N N 157 
AJP C61  H63  sing N N 158 
AJP O62  H64  sing N N 159 
AJP O63  H65  sing N N 160 
AJP C65  H66  sing N N 161 
AJP C66  H67  sing N N 162 
AJP C67  H68  sing N N 163 
AJP C68  H69  sing N N 164 
AJP C69  H70  sing N N 165 
AJP C71  H71  sing N N 166 
AJP C71  H72  sing N N 167 
AJP O72  H73  sing N N 168 
AJP O73  H74  sing N N 169 
AJP O74  H75  sing N N 170 
AJP O75  H76  sing N N 171 
AJP O76  H77  sing N N 172 
AJP O77  H78  sing N N 173 
AJP O78  H79  sing N N 174 
AJP O79  H80  sing N N 175 
AJP C80  H81  sing N N 176 
AJP C80  H82  sing N N 177 
AJP C80  H83  sing N N 178 
AJP C81  H84  sing N N 179 
AJP C81  H85  sing N N 180 
AJP C81  H86  sing N N 181 
AJP O82  H87  sing N N 182 
AJP C83  H88  sing N N 183 
AJP C83  H89  sing N N 184 
AJP C83  H90  sing N N 185 
AJP C85  H91  sing N N 186 
AJP C85  H92  sing N N 187 
ALA N    CA   sing N N 188 
ALA N    H    sing N N 189 
ALA N    H2   sing N N 190 
ALA CA   C    sing N N 191 
ALA CA   CB   sing N N 192 
ALA CA   HA   sing N N 193 
ALA C    O    doub N N 194 
ALA C    OXT  sing N N 195 
ALA CB   HB1  sing N N 196 
ALA CB   HB2  sing N N 197 
ALA CB   HB3  sing N N 198 
ALA OXT  HXT  sing N N 199 
ARG N    CA   sing N N 200 
ARG N    H    sing N N 201 
ARG N    H2   sing N N 202 
ARG CA   C    sing N N 203 
ARG CA   CB   sing N N 204 
ARG CA   HA   sing N N 205 
ARG C    O    doub N N 206 
ARG C    OXT  sing N N 207 
ARG CB   CG   sing N N 208 
ARG CB   HB2  sing N N 209 
ARG CB   HB3  sing N N 210 
ARG CG   CD   sing N N 211 
ARG CG   HG2  sing N N 212 
ARG CG   HG3  sing N N 213 
ARG CD   NE   sing N N 214 
ARG CD   HD2  sing N N 215 
ARG CD   HD3  sing N N 216 
ARG NE   CZ   sing N N 217 
ARG NE   HE   sing N N 218 
ARG CZ   NH1  sing N N 219 
ARG CZ   NH2  doub N N 220 
ARG NH1  HH11 sing N N 221 
ARG NH1  HH12 sing N N 222 
ARG NH2  HH21 sing N N 223 
ARG NH2  HH22 sing N N 224 
ARG OXT  HXT  sing N N 225 
ASN N    CA   sing N N 226 
ASN N    H    sing N N 227 
ASN N    H2   sing N N 228 
ASN CA   C    sing N N 229 
ASN CA   CB   sing N N 230 
ASN CA   HA   sing N N 231 
ASN C    O    doub N N 232 
ASN C    OXT  sing N N 233 
ASN CB   CG   sing N N 234 
ASN CB   HB2  sing N N 235 
ASN CB   HB3  sing N N 236 
ASN CG   OD1  doub N N 237 
ASN CG   ND2  sing N N 238 
ASN ND2  HD21 sing N N 239 
ASN ND2  HD22 sing N N 240 
ASN OXT  HXT  sing N N 241 
ASP N    CA   sing N N 242 
ASP N    H    sing N N 243 
ASP N    H2   sing N N 244 
ASP CA   C    sing N N 245 
ASP CA   CB   sing N N 246 
ASP CA   HA   sing N N 247 
ASP C    O    doub N N 248 
ASP C    OXT  sing N N 249 
ASP CB   CG   sing N N 250 
ASP CB   HB2  sing N N 251 
ASP CB   HB3  sing N N 252 
ASP CG   OD1  doub N N 253 
ASP CG   OD2  sing N N 254 
ASP OD2  HD2  sing N N 255 
ASP OXT  HXT  sing N N 256 
CYS N    CA   sing N N 257 
CYS N    H    sing N N 258 
CYS N    H2   sing N N 259 
CYS CA   C    sing N N 260 
CYS CA   CB   sing N N 261 
CYS CA   HA   sing N N 262 
CYS C    O    doub N N 263 
CYS C    OXT  sing N N 264 
CYS CB   SG   sing N N 265 
CYS CB   HB2  sing N N 266 
CYS CB   HB3  sing N N 267 
CYS SG   HG   sing N N 268 
CYS OXT  HXT  sing N N 269 
GLN N    CA   sing N N 270 
GLN N    H    sing N N 271 
GLN N    H2   sing N N 272 
GLN CA   C    sing N N 273 
GLN CA   CB   sing N N 274 
GLN CA   HA   sing N N 275 
GLN C    O    doub N N 276 
GLN C    OXT  sing N N 277 
GLN CB   CG   sing N N 278 
GLN CB   HB2  sing N N 279 
GLN CB   HB3  sing N N 280 
GLN CG   CD   sing N N 281 
GLN CG   HG2  sing N N 282 
GLN CG   HG3  sing N N 283 
GLN CD   OE1  doub N N 284 
GLN CD   NE2  sing N N 285 
GLN NE2  HE21 sing N N 286 
GLN NE2  HE22 sing N N 287 
GLN OXT  HXT  sing N N 288 
GLU N    CA   sing N N 289 
GLU N    H    sing N N 290 
GLU N    H2   sing N N 291 
GLU CA   C    sing N N 292 
GLU CA   CB   sing N N 293 
GLU CA   HA   sing N N 294 
GLU C    O    doub N N 295 
GLU C    OXT  sing N N 296 
GLU CB   CG   sing N N 297 
GLU CB   HB2  sing N N 298 
GLU CB   HB3  sing N N 299 
GLU CG   CD   sing N N 300 
GLU CG   HG2  sing N N 301 
GLU CG   HG3  sing N N 302 
GLU CD   OE1  doub N N 303 
GLU CD   OE2  sing N N 304 
GLU OE2  HE2  sing N N 305 
GLU OXT  HXT  sing N N 306 
GLY N    CA   sing N N 307 
GLY N    H    sing N N 308 
GLY N    H2   sing N N 309 
GLY CA   C    sing N N 310 
GLY CA   HA2  sing N N 311 
GLY CA   HA3  sing N N 312 
GLY C    O    doub N N 313 
GLY C    OXT  sing N N 314 
GLY OXT  HXT  sing N N 315 
HIS N    CA   sing N N 316 
HIS N    H    sing N N 317 
HIS N    H2   sing N N 318 
HIS CA   C    sing N N 319 
HIS CA   CB   sing N N 320 
HIS CA   HA   sing N N 321 
HIS C    O    doub N N 322 
HIS C    OXT  sing N N 323 
HIS CB   CG   sing N N 324 
HIS CB   HB2  sing N N 325 
HIS CB   HB3  sing N N 326 
HIS CG   ND1  sing Y N 327 
HIS CG   CD2  doub Y N 328 
HIS ND1  CE1  doub Y N 329 
HIS ND1  HD1  sing N N 330 
HIS CD2  NE2  sing Y N 331 
HIS CD2  HD2  sing N N 332 
HIS CE1  NE2  sing Y N 333 
HIS CE1  HE1  sing N N 334 
HIS NE2  HE2  sing N N 335 
HIS OXT  HXT  sing N N 336 
ILE N    CA   sing N N 337 
ILE N    H    sing N N 338 
ILE N    H2   sing N N 339 
ILE CA   C    sing N N 340 
ILE CA   CB   sing N N 341 
ILE CA   HA   sing N N 342 
ILE C    O    doub N N 343 
ILE C    OXT  sing N N 344 
ILE CB   CG1  sing N N 345 
ILE CB   CG2  sing N N 346 
ILE CB   HB   sing N N 347 
ILE CG1  CD1  sing N N 348 
ILE CG1  HG12 sing N N 349 
ILE CG1  HG13 sing N N 350 
ILE CG2  HG21 sing N N 351 
ILE CG2  HG22 sing N N 352 
ILE CG2  HG23 sing N N 353 
ILE CD1  HD11 sing N N 354 
ILE CD1  HD12 sing N N 355 
ILE CD1  HD13 sing N N 356 
ILE OXT  HXT  sing N N 357 
LEU N    CA   sing N N 358 
LEU N    H    sing N N 359 
LEU N    H2   sing N N 360 
LEU CA   C    sing N N 361 
LEU CA   CB   sing N N 362 
LEU CA   HA   sing N N 363 
LEU C    O    doub N N 364 
LEU C    OXT  sing N N 365 
LEU CB   CG   sing N N 366 
LEU CB   HB2  sing N N 367 
LEU CB   HB3  sing N N 368 
LEU CG   CD1  sing N N 369 
LEU CG   CD2  sing N N 370 
LEU CG   HG   sing N N 371 
LEU CD1  HD11 sing N N 372 
LEU CD1  HD12 sing N N 373 
LEU CD1  HD13 sing N N 374 
LEU CD2  HD21 sing N N 375 
LEU CD2  HD22 sing N N 376 
LEU CD2  HD23 sing N N 377 
LEU OXT  HXT  sing N N 378 
LYS N    CA   sing N N 379 
LYS N    H    sing N N 380 
LYS N    H2   sing N N 381 
LYS CA   C    sing N N 382 
LYS CA   CB   sing N N 383 
LYS CA   HA   sing N N 384 
LYS C    O    doub N N 385 
LYS C    OXT  sing N N 386 
LYS CB   CG   sing N N 387 
LYS CB   HB2  sing N N 388 
LYS CB   HB3  sing N N 389 
LYS CG   CD   sing N N 390 
LYS CG   HG2  sing N N 391 
LYS CG   HG3  sing N N 392 
LYS CD   CE   sing N N 393 
LYS CD   HD2  sing N N 394 
LYS CD   HD3  sing N N 395 
LYS CE   NZ   sing N N 396 
LYS CE   HE2  sing N N 397 
LYS CE   HE3  sing N N 398 
LYS NZ   HZ1  sing N N 399 
LYS NZ   HZ2  sing N N 400 
LYS NZ   HZ3  sing N N 401 
LYS OXT  HXT  sing N N 402 
MET N    CA   sing N N 403 
MET N    H    sing N N 404 
MET N    H2   sing N N 405 
MET CA   C    sing N N 406 
MET CA   CB   sing N N 407 
MET CA   HA   sing N N 408 
MET C    O    doub N N 409 
MET C    OXT  sing N N 410 
MET CB   CG   sing N N 411 
MET CB   HB2  sing N N 412 
MET CB   HB3  sing N N 413 
MET CG   SD   sing N N 414 
MET CG   HG2  sing N N 415 
MET CG   HG3  sing N N 416 
MET SD   CE   sing N N 417 
MET CE   HE1  sing N N 418 
MET CE   HE2  sing N N 419 
MET CE   HE3  sing N N 420 
MET OXT  HXT  sing N N 421 
PHE N    CA   sing N N 422 
PHE N    H    sing N N 423 
PHE N    H2   sing N N 424 
PHE CA   C    sing N N 425 
PHE CA   CB   sing N N 426 
PHE CA   HA   sing N N 427 
PHE C    O    doub N N 428 
PHE C    OXT  sing N N 429 
PHE CB   CG   sing N N 430 
PHE CB   HB2  sing N N 431 
PHE CB   HB3  sing N N 432 
PHE CG   CD1  doub Y N 433 
PHE CG   CD2  sing Y N 434 
PHE CD1  CE1  sing Y N 435 
PHE CD1  HD1  sing N N 436 
PHE CD2  CE2  doub Y N 437 
PHE CD2  HD2  sing N N 438 
PHE CE1  CZ   doub Y N 439 
PHE CE1  HE1  sing N N 440 
PHE CE2  CZ   sing Y N 441 
PHE CE2  HE2  sing N N 442 
PHE CZ   HZ   sing N N 443 
PHE OXT  HXT  sing N N 444 
POV N    C12  sing N N 445 
POV N    C13  sing N N 446 
POV N    C14  sing N N 447 
POV N    C15  sing N N 448 
POV P    O11  sing N N 449 
POV P    O12  sing N N 450 
POV P    O13  sing N N 451 
POV P    O14  doub N N 452 
POV C1   C2   sing N N 453 
POV C1   O11  sing N N 454 
POV C1   H1   sing N N 455 
POV C1   H1A  sing N N 456 
POV C2   C3   sing N N 457 
POV C2   O21  sing N N 458 
POV C2   H2   sing N N 459 
POV C3   O31  sing N N 460 
POV C3   H3   sing N N 461 
POV C3   H3A  sing N N 462 
POV C210 C211 sing N N 463 
POV C210 C29  doub N Z 464 
POV C210 H210 sing N N 465 
POV C310 C311 sing N N 466 
POV C310 C39  sing N N 467 
POV C310 H310 sing N N 468 
POV C310 H31A sing N N 469 
POV C11  C12  sing N N 470 
POV C11  O12  sing N N 471 
POV C11  H11  sing N N 472 
POV C11  H11A sing N N 473 
POV C211 C212 sing N N 474 
POV C211 H211 sing N N 475 
POV C211 H21A sing N N 476 
POV C311 C312 sing N N 477 
POV C311 H311 sing N N 478 
POV C311 H31B sing N N 479 
POV C12  H12  sing N N 480 
POV C12  H12A sing N N 481 
POV C212 C213 sing N N 482 
POV C212 H212 sing N N 483 
POV C212 H21B sing N N 484 
POV C312 C313 sing N N 485 
POV C312 H312 sing N N 486 
POV C312 H31C sing N N 487 
POV C13  H13  sing N N 488 
POV C13  H13A sing N N 489 
POV C13  H13B sing N N 490 
POV C213 C214 sing N N 491 
POV C213 H213 sing N N 492 
POV C213 H21C sing N N 493 
POV C313 C314 sing N N 494 
POV C313 H313 sing N N 495 
POV C313 H31D sing N N 496 
POV C14  H14  sing N N 497 
POV C14  H14A sing N N 498 
POV C14  H14B sing N N 499 
POV C214 C215 sing N N 500 
POV C214 H214 sing N N 501 
POV C214 H21D sing N N 502 
POV C314 C315 sing N N 503 
POV C314 H314 sing N N 504 
POV C314 H31E sing N N 505 
POV C15  H15  sing N N 506 
POV C15  H15A sing N N 507 
POV C15  H15B sing N N 508 
POV C215 C216 sing N N 509 
POV C215 H215 sing N N 510 
POV C215 H21E sing N N 511 
POV C315 C316 sing N N 512 
POV C315 H315 sing N N 513 
POV C315 H31F sing N N 514 
POV C216 C217 sing N N 515 
POV C216 H216 sing N N 516 
POV C216 H21F sing N N 517 
POV C316 H316 sing N N 518 
POV C316 H31G sing N N 519 
POV C316 H31H sing N N 520 
POV C217 C218 sing N N 521 
POV C217 H217 sing N N 522 
POV C217 H21G sing N N 523 
POV C218 H218 sing N N 524 
POV C218 H21H sing N N 525 
POV C218 H21J sing N N 526 
POV C21  O21  sing N N 527 
POV C21  C22  sing N N 528 
POV C21  O22  doub N N 529 
POV C22  C23  sing N N 530 
POV C22  H22  sing N N 531 
POV C22  H22A sing N N 532 
POV C23  C24  sing N N 533 
POV C23  H23  sing N N 534 
POV C23  H23A sing N N 535 
POV C24  C25  sing N N 536 
POV C24  H24  sing N N 537 
POV C24  H24A sing N N 538 
POV C25  C26  sing N N 539 
POV C25  H25  sing N N 540 
POV C25  H25A sing N N 541 
POV C26  C27  sing N N 542 
POV C26  H26  sing N N 543 
POV C26  H26A sing N N 544 
POV C27  C28  sing N N 545 
POV C27  H27  sing N N 546 
POV C27  H27A sing N N 547 
POV C28  C29  sing N N 548 
POV C28  H28  sing N N 549 
POV C28  H28A sing N N 550 
POV C29  H29  sing N N 551 
POV C31  O31  sing N N 552 
POV C31  C32  sing N N 553 
POV C31  O32  doub N N 554 
POV C32  C33  sing N N 555 
POV C32  H32  sing N N 556 
POV C32  H32A sing N N 557 
POV C33  C34  sing N N 558 
POV C33  H33  sing N N 559 
POV C33  H33A sing N N 560 
POV C34  C35  sing N N 561 
POV C34  H34  sing N N 562 
POV C34  H34A sing N N 563 
POV C35  C36  sing N N 564 
POV C35  H35  sing N N 565 
POV C35  H35A sing N N 566 
POV C36  C37  sing N N 567 
POV C36  H36  sing N N 568 
POV C36  H36A sing N N 569 
POV C37  C38  sing N N 570 
POV C37  H37  sing N N 571 
POV C37  H37A sing N N 572 
POV C38  C39  sing N N 573 
POV C38  H38  sing N N 574 
POV C38  H38A sing N N 575 
POV C39  H39  sing N N 576 
POV C39  H39A sing N N 577 
PRO N    CA   sing N N 578 
PRO N    CD   sing N N 579 
PRO N    H    sing N N 580 
PRO CA   C    sing N N 581 
PRO CA   CB   sing N N 582 
PRO CA   HA   sing N N 583 
PRO C    O    doub N N 584 
PRO C    OXT  sing N N 585 
PRO CB   CG   sing N N 586 
PRO CB   HB2  sing N N 587 
PRO CB   HB3  sing N N 588 
PRO CG   CD   sing N N 589 
PRO CG   HG2  sing N N 590 
PRO CG   HG3  sing N N 591 
PRO CD   HD2  sing N N 592 
PRO CD   HD3  sing N N 593 
PRO OXT  HXT  sing N N 594 
SER N    CA   sing N N 595 
SER N    H    sing N N 596 
SER N    H2   sing N N 597 
SER CA   C    sing N N 598 
SER CA   CB   sing N N 599 
SER CA   HA   sing N N 600 
SER C    O    doub N N 601 
SER C    OXT  sing N N 602 
SER CB   OG   sing N N 603 
SER CB   HB2  sing N N 604 
SER CB   HB3  sing N N 605 
SER OG   HG   sing N N 606 
SER OXT  HXT  sing N N 607 
THR N    CA   sing N N 608 
THR N    H    sing N N 609 
THR N    H2   sing N N 610 
THR CA   C    sing N N 611 
THR CA   CB   sing N N 612 
THR CA   HA   sing N N 613 
THR C    O    doub N N 614 
THR C    OXT  sing N N 615 
THR CB   OG1  sing N N 616 
THR CB   CG2  sing N N 617 
THR CB   HB   sing N N 618 
THR OG1  HG1  sing N N 619 
THR CG2  HG21 sing N N 620 
THR CG2  HG22 sing N N 621 
THR CG2  HG23 sing N N 622 
THR OXT  HXT  sing N N 623 
TRP N    CA   sing N N 624 
TRP N    H    sing N N 625 
TRP N    H2   sing N N 626 
TRP CA   C    sing N N 627 
TRP CA   CB   sing N N 628 
TRP CA   HA   sing N N 629 
TRP C    O    doub N N 630 
TRP C    OXT  sing N N 631 
TRP CB   CG   sing N N 632 
TRP CB   HB2  sing N N 633 
TRP CB   HB3  sing N N 634 
TRP CG   CD1  doub Y N 635 
TRP CG   CD2  sing Y N 636 
TRP CD1  NE1  sing Y N 637 
TRP CD1  HD1  sing N N 638 
TRP CD2  CE2  doub Y N 639 
TRP CD2  CE3  sing Y N 640 
TRP NE1  CE2  sing Y N 641 
TRP NE1  HE1  sing N N 642 
TRP CE2  CZ2  sing Y N 643 
TRP CE3  CZ3  doub Y N 644 
TRP CE3  HE3  sing N N 645 
TRP CZ2  CH2  doub Y N 646 
TRP CZ2  HZ2  sing N N 647 
TRP CZ3  CH2  sing Y N 648 
TRP CZ3  HZ3  sing N N 649 
TRP CH2  HH2  sing N N 650 
TRP OXT  HXT  sing N N 651 
TYR N    CA   sing N N 652 
TYR N    H    sing N N 653 
TYR N    H2   sing N N 654 
TYR CA   C    sing N N 655 
TYR CA   CB   sing N N 656 
TYR CA   HA   sing N N 657 
TYR C    O    doub N N 658 
TYR C    OXT  sing N N 659 
TYR CB   CG   sing N N 660 
TYR CB   HB2  sing N N 661 
TYR CB   HB3  sing N N 662 
TYR CG   CD1  doub Y N 663 
TYR CG   CD2  sing Y N 664 
TYR CD1  CE1  sing Y N 665 
TYR CD1  HD1  sing N N 666 
TYR CD2  CE2  doub Y N 667 
TYR CD2  HD2  sing N N 668 
TYR CE1  CZ   doub Y N 669 
TYR CE1  HE1  sing N N 670 
TYR CE2  CZ   sing Y N 671 
TYR CE2  HE2  sing N N 672 
TYR CZ   OH   sing N N 673 
TYR OH   HH   sing N N 674 
TYR OXT  HXT  sing N N 675 
VAL N    CA   sing N N 676 
VAL N    H    sing N N 677 
VAL N    H2   sing N N 678 
VAL CA   C    sing N N 679 
VAL CA   CB   sing N N 680 
VAL CA   HA   sing N N 681 
VAL C    O    doub N N 682 
VAL C    OXT  sing N N 683 
VAL CB   CG1  sing N N 684 
VAL CB   CG2  sing N N 685 
VAL CB   HB   sing N N 686 
VAL CG1  HG11 sing N N 687 
VAL CG1  HG12 sing N N 688 
VAL CG1  HG13 sing N N 689 
VAL CG2  HG21 sing N N 690 
VAL CG2  HG22 sing N N 691 
VAL CG2  HG23 sing N N 692 
VAL OXT  HXT  sing N N 693 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2023-09-14 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           8U73 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-26 
_em_admin.title              'R399A sea urchin SLC9C1 pH 8 in Na+' 
# 
_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          7668 
_em_entity_assembly_naturalsource.organism             'Strongylocentrotus purpuratus' 
_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                 HEK293F 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_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         66 
_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 ? ? ?      ?            
'MODEL REFINEMENT'              ? 2  ? ? ? PHENIX 1.20.1_4487: 
'IMAGE ACQUISITION'             ? 3  ? ? 1 ?      ?            
MASKING                         ? 4  ? ? ? ?      ?            
'CTF CORRECTION'                ? 5  1 ? ? ?      ?            
'LAYERLINE INDEXING'            ? 6  ? ? ? ?      ?            
'DIFFRACTION INDEXING'          ? 7  ? ? ? ?      ?            
'MODEL FITTING'                 ? 8  ? ? ? ?      ?            
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           R01GM145719 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8U73 
_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 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N    . ALA A 1 74   ? 126.231 132.474 157.167 1.00 18.86 ?  74   ALA A N    1 
ATOM   2     C CA   . ALA A 1 74   ? 125.948 131.885 155.864 1.00 17.36 ?  74   ALA A CA   1 
ATOM   3     C C    . ALA A 1 74   ? 127.093 132.146 154.893 1.00 14.66 ?  74   ALA A C    1 
ATOM   4     O O    . ALA A 1 74   ? 127.573 133.275 154.789 1.00 19.09 ?  74   ALA A O    1 
ATOM   5     C CB   . ALA A 1 74   ? 124.644 132.429 155.307 1.00 19.34 ?  74   ALA A CB   1 
ATOM   6     N N    . PRO A 1 75   ? 127.535 131.099 154.195 1.00 14.63 ?  75   PRO A N    1 
ATOM   7     C CA   . PRO A 1 75   ? 128.645 131.256 153.246 1.00 14.06 ?  75   PRO A CA   1 
ATOM   8     C C    . PRO A 1 75   ? 128.278 132.165 152.082 1.00 15.80 ?  75   PRO A C    1 
ATOM   9     O O    . PRO A 1 75   ? 127.124 132.235 151.654 1.00 14.46 ?  75   PRO A O    1 
ATOM   10    C CB   . PRO A 1 75   ? 128.909 129.822 152.771 1.00 12.35 ?  75   PRO A CB   1 
ATOM   11    C CG   . PRO A 1 75   ? 128.346 128.955 153.848 1.00 12.32 ?  75   PRO A CG   1 
ATOM   12    C CD   . PRO A 1 75   ? 127.148 129.689 154.361 1.00 13.79 ?  75   PRO A CD   1 
ATOM   13    N N    . LYS A 1 76   ? 129.288 132.865 151.568 1.00 9.57  ?  76   LYS A N    1 
ATOM   14    C CA   . LYS A 1 76   ? 129.136 133.798 150.457 1.00 10.18 ?  76   LYS A CA   1 
ATOM   15    C C    . LYS A 1 76   ? 129.893 133.234 149.260 1.00 9.91  ?  76   LYS A C    1 
ATOM   16    O O    . LYS A 1 76   ? 131.127 133.178 149.272 1.00 17.94 ?  76   LYS A O    1 
ATOM   17    C CB   . LYS A 1 76   ? 129.657 135.181 150.837 1.00 13.30 ?  76   LYS A CB   1 
ATOM   18    C CG   . LYS A 1 76   ? 129.393 135.562 152.285 1.00 13.31 ?  76   LYS A CG   1 
ATOM   19    C CD   . LYS A 1 76   ? 129.852 136.978 152.579 1.00 14.00 ?  76   LYS A CD   1 
ATOM   20    C CE   . LYS A 1 76   ? 129.043 137.595 153.708 1.00 10.34 ?  76   LYS A CE   1 
ATOM   21    N NZ   . LYS A 1 76   ? 127.644 137.893 153.300 1.00 15.89 ?  76   LYS A NZ   1 
ATOM   22    N N    . VAL A 1 77   ? 129.157 132.816 148.232 1.00 6.44  ?  77   VAL A N    1 
ATOM   23    C CA   . VAL A 1 77   ? 129.754 132.170 147.067 1.00 2.01  ?  77   VAL A CA   1 
ATOM   24    C C    . VAL A 1 77   ? 129.408 132.854 145.753 1.00 5.23  ?  77   VAL A C    1 
ATOM   25    O O    . VAL A 1 77   ? 130.071 132.574 144.745 1.00 14.57 ?  77   VAL A O    1 
ATOM   26    C CB   . VAL A 1 77   ? 129.370 130.675 146.987 1.00 3.91  ?  77   VAL A CB   1 
ATOM   27    C CG1  . VAL A 1 77   ? 129.688 129.956 148.291 1.00 10.08 ?  77   VAL A CG1  1 
ATOM   28    C CG2  . VAL A 1 77   ? 127.901 130.522 146.631 1.00 5.73  ?  77   VAL A CG2  1 
ATOM   29    N N    . ILE A 1 78   ? 128.406 133.738 145.720 1.00 2.49  ?  78   ILE A N    1 
ATOM   30    C CA   . ILE A 1 78   ? 127.926 134.290 144.453 1.00 0.92  ?  78   ILE A CA   1 
ATOM   31    C C    . ILE A 1 78   ? 129.006 135.124 143.774 1.00 0.00  ?  78   ILE A C    1 
ATOM   32    O O    . ILE A 1 78   ? 129.237 134.999 142.562 1.00 0.00  ?  78   ILE A O    1 
ATOM   33    C CB   . ILE A 1 78   ? 126.641 135.108 144.689 1.00 2.35  ?  78   ILE A CB   1 
ATOM   34    C CG1  . ILE A 1 78   ? 125.440 134.178 144.856 1.00 4.03  ?  78   ILE A CG1  1 
ATOM   35    C CG2  . ILE A 1 78   ? 126.393 136.092 143.556 1.00 0.75  ?  78   ILE A CG2  1 
ATOM   36    C CD1  . ILE A 1 78   ? 124.284 134.814 145.579 1.00 2.47  ?  78   ILE A CD1  1 
ATOM   37    N N    . VAL A 1 79   ? 129.698 135.967 144.544 1.00 2.63  ?  79   VAL A N    1 
ATOM   38    C CA   . VAL A 1 79   ? 130.683 136.877 143.970 1.00 0.22  ?  79   VAL A CA   1 
ATOM   39    C C    . VAL A 1 79   ? 131.860 136.104 143.387 1.00 0.30  ?  79   VAL A C    1 
ATOM   40    O O    . VAL A 1 79   ? 132.339 136.421 142.294 1.00 3.99  ?  79   VAL A O    1 
ATOM   41    C CB   . VAL A 1 79   ? 131.137 137.903 145.025 1.00 4.68  ?  79   VAL A CB   1 
ATOM   42    C CG1  . VAL A 1 79   ? 132.289 138.746 144.501 1.00 5.97  ?  79   VAL A CG1  1 
ATOM   43    C CG2  . VAL A 1 79   ? 129.971 138.790 145.428 1.00 0.01  ?  79   VAL A CG2  1 
ATOM   44    N N    . PHE A 1 80   ? 132.327 135.066 144.087 1.00 0.62  ?  80   PHE A N    1 
ATOM   45    C CA   . PHE A 1 80   ? 133.476 134.302 143.606 1.00 0.00  ?  80   PHE A CA   1 
ATOM   46    C C    . PHE A 1 80   ? 133.162 133.574 142.303 1.00 0.00  ?  80   PHE A C    1 
ATOM   47    O O    . PHE A 1 80   ? 133.941 133.640 141.348 1.00 2.22  ?  80   PHE A O    1 
ATOM   48    C CB   . PHE A 1 80   ? 133.942 133.318 144.680 1.00 0.69  ?  80   PHE A CB   1 
ATOM   49    C CG   . PHE A 1 80   ? 135.307 132.737 144.422 1.00 3.80  ?  80   PHE A CG   1 
ATOM   50    C CD1  . PHE A 1 80   ? 136.443 133.367 144.898 1.00 0.47  ?  80   PHE A CD1  1 
ATOM   51    C CD2  . PHE A 1 80   ? 135.455 131.566 143.694 1.00 9.85  ?  80   PHE A CD2  1 
ATOM   52    C CE1  . PHE A 1 80   ? 137.698 132.837 144.658 1.00 1.11  ?  80   PHE A CE1  1 
ATOM   53    C CE2  . PHE A 1 80   ? 136.708 131.033 143.454 1.00 0.00  ?  80   PHE A CE2  1 
ATOM   54    C CZ   . PHE A 1 80   ? 137.829 131.670 143.937 1.00 0.00  ?  80   PHE A CZ   1 
ATOM   55    N N    . ILE A 1 81   ? 132.017 132.887 142.238 1.00 0.00  ?  81   ILE A N    1 
ATOM   56    C CA   . ILE A 1 81   ? 131.650 132.160 141.023 1.00 0.00  ?  81   ILE A CA   1 
ATOM   57    C C    . ILE A 1 81   ? 131.403 133.122 139.865 1.00 5.63  ?  81   ILE A C    1 
ATOM   58    O O    . ILE A 1 81   ? 131.848 132.879 138.734 1.00 10.64 ?  81   ILE A O    1 
ATOM   59    C CB   . ILE A 1 81   ? 130.426 131.261 141.280 1.00 0.00  ?  81   ILE A CB   1 
ATOM   60    C CG1  . ILE A 1 81   ? 130.631 130.398 142.527 1.00 0.00  ?  81   ILE A CG1  1 
ATOM   61    C CG2  . ILE A 1 81   ? 130.133 130.395 140.064 1.00 1.38  ?  81   ILE A CG2  1 
ATOM   62    C CD1  . ILE A 1 81   ? 131.560 129.232 142.331 1.00 0.00  ?  81   ILE A CD1  1 
ATOM   63    N N    . SER A 1 82   ? 130.685 134.223 140.120 1.00 3.38  ?  82   SER A N    1 
ATOM   64    C CA   . SER A 1 82   ? 130.394 135.182 139.058 1.00 0.00  ?  82   SER A CA   1 
ATOM   65    C C    . SER A 1 82   ? 131.665 135.848 138.543 1.00 1.53  ?  82   SER A C    1 
ATOM   66    O O    . SER A 1 82   ? 131.841 136.014 137.329 1.00 8.41  ?  82   SER A O    1 
ATOM   67    C CB   . SER A 1 82   ? 129.406 136.233 139.560 1.00 4.93  ?  82   SER A CB   1 
ATOM   68    O OG   . SER A 1 82   ? 128.416 135.646 140.384 1.00 12.17 ?  82   SER A OG   1 
ATOM   69    N N    . GLY A 1 83   ? 132.563 136.236 139.451 1.00 1.69  ?  83   GLY A N    1 
ATOM   70    C CA   . GLY A 1 83   ? 133.829 136.808 139.034 1.00 4.56  ?  83   GLY A CA   1 
ATOM   71    C C    . GLY A 1 83   ? 134.708 135.811 138.306 1.00 9.54  ?  83   GLY A C    1 
ATOM   72    O O    . GLY A 1 83   ? 135.436 136.180 137.386 1.00 15.23 ?  83   GLY A O    1 
ATOM   73    N N    . SER A 1 84   ? 134.654 134.537 138.707 1.00 8.23  ?  84   SER A N    1 
ATOM   74    C CA   . SER A 1 84   ? 135.395 133.507 137.990 1.00 8.21  ?  84   SER A CA   1 
ATOM   75    C C    . SER A 1 84   ? 134.884 133.357 136.565 1.00 7.63  ?  84   SER A C    1 
ATOM   76    O O    . SER A 1 84   ? 135.677 133.246 135.625 1.00 14.60 ?  84   SER A O    1 
ATOM   77    C CB   . SER A 1 84   ? 135.303 132.176 138.736 1.00 9.26  ?  84   SER A CB   1 
ATOM   78    O OG   . SER A 1 84   ? 136.365 132.036 139.663 1.00 8.49  ?  84   SER A OG   1 
ATOM   79    N N    . CYS A 1 85   ? 133.560 133.370 136.384 1.00 3.68  ?  85   CYS A N    1 
ATOM   80    C CA   . CYS A 1 85   ? 132.990 133.295 135.040 1.00 2.52  ?  85   CYS A CA   1 
ATOM   81    C C    . CYS A 1 85   ? 133.386 134.508 134.203 1.00 5.08  ?  85   CYS A C    1 
ATOM   82    O O    . CYS A 1 85   ? 133.796 134.374 133.041 1.00 11.04 ?  85   CYS A O    1 
ATOM   83    C CB   . CYS A 1 85   ? 131.467 133.180 135.127 1.00 6.65  ?  85   CYS A CB   1 
ATOM   84    S SG   . CYS A 1 85   ? 130.837 131.497 135.299 1.00 6.61  ?  85   CYS A SG   1 
ATOM   85    N N    . LEU A 1 86   ? 133.287 135.705 134.792 1.00 7.67  ?  86   LEU A N    1 
ATOM   86    C CA   . LEU A 1 86   ? 133.619 136.931 134.070 1.00 6.47  ?  86   LEU A CA   1 
ATOM   87    C C    . LEU A 1 86   ? 135.096 136.978 133.695 1.00 7.16  ?  86   LEU A C    1 
ATOM   88    O O    . LEU A 1 86   ? 135.447 137.331 132.562 1.00 11.62 ?  86   LEU A O    1 
ATOM   89    C CB   . LEU A 1 86   ? 133.238 138.145 134.916 1.00 9.48  ?  86   LEU A CB   1 
ATOM   90    C CG   . LEU A 1 86   ? 133.848 139.503 134.565 1.00 11.12 ?  86   LEU A CG   1 
ATOM   91    C CD1  . LEU A 1 86   ? 133.137 140.119 133.372 1.00 7.63  ?  86   LEU A CD1  1 
ATOM   92    C CD2  . LEU A 1 86   ? 133.795 140.434 135.765 1.00 8.51  ?  86   LEU A CD2  1 
ATOM   93    N N    . PHE A 1 87   ? 135.978 136.612 134.629 1.00 5.87  ?  87   PHE A N    1 
ATOM   94    C CA   . PHE A 1 87   ? 137.409 136.626 134.357 1.00 0.85  ?  87   PHE A CA   1 
ATOM   95    C C    . PHE A 1 87   ? 137.807 135.534 133.376 1.00 0.00  ?  87   PHE A C    1 
ATOM   96    O O    . PHE A 1 87   ? 138.728 135.735 132.580 1.00 10.48 ?  87   PHE A O    1 
ATOM   97    C CB   . PHE A 1 87   ? 138.194 136.476 135.658 1.00 7.79  ?  87   PHE A CB   1 
ATOM   98    C CG   . PHE A 1 87   ? 138.148 137.693 136.538 1.00 13.85 ?  87   PHE A CG   1 
ATOM   99    C CD1  . PHE A 1 87   ? 138.034 138.959 135.990 1.00 13.56 ?  87   PHE A CD1  1 
ATOM   100   C CD2  . PHE A 1 87   ? 138.228 137.569 137.914 1.00 8.17  ?  87   PHE A CD2  1 
ATOM   101   C CE1  . PHE A 1 87   ? 137.993 140.077 136.800 1.00 12.00 ?  87   PHE A CE1  1 
ATOM   102   C CE2  . PHE A 1 87   ? 138.188 138.682 138.729 1.00 8.57  ?  87   PHE A CE2  1 
ATOM   103   C CZ   . PHE A 1 87   ? 138.070 139.938 138.171 1.00 12.64 ?  87   PHE A CZ   1 
ATOM   104   N N    . GLY A 1 88   ? 137.141 134.378 133.420 1.00 3.80  ?  88   GLY A N    1 
ATOM   105   C CA   . GLY A 1 88   ? 137.387 133.360 132.415 1.00 0.33  ?  88   GLY A CA   1 
ATOM   106   C C    . GLY A 1 88   ? 137.008 133.827 131.026 1.00 0.00  ?  88   GLY A C    1 
ATOM   107   O O    . GLY A 1 88   ? 137.748 133.606 130.066 1.00 4.24  ?  88   GLY A O    1 
ATOM   108   N N    . ALA A 1 89   ? 135.862 134.506 130.906 1.00 2.59  ?  89   ALA A N    1 
ATOM   109   C CA   . ALA A 1 89   ? 135.474 135.084 129.622 1.00 2.06  ?  89   ALA A CA   1 
ATOM   110   C C    . ALA A 1 89   ? 136.480 136.130 129.154 1.00 0.99  ?  89   ALA A C    1 
ATOM   111   O O    . ALA A 1 89   ? 136.861 136.153 127.976 1.00 4.77  ?  89   ALA A O    1 
ATOM   112   C CB   . ALA A 1 89   ? 134.078 135.695 129.724 1.00 6.84  ?  89   ALA A CB   1 
ATOM   113   N N    . ILE A 1 90   ? 136.932 136.992 130.069 1.00 4.03  ?  90   ILE A N    1 
ATOM   114   C CA   . ILE A 1 90   ? 137.866 138.059 129.710 1.00 2.67  ?  90   ILE A CA   1 
ATOM   115   C C    . ILE A 1 90   ? 139.198 137.477 129.248 1.00 5.37  ?  90   ILE A C    1 
ATOM   116   O O    . ILE A 1 90   ? 139.742 137.874 128.211 1.00 12.53 ?  90   ILE A O    1 
ATOM   117   C CB   . ILE A 1 90   ? 138.049 139.027 130.893 1.00 4.39  ?  90   ILE A CB   1 
ATOM   118   C CG1  . ILE A 1 90   ? 136.845 139.962 131.010 1.00 10.30 ?  90   ILE A CG1  1 
ATOM   119   C CG2  . ILE A 1 90   ? 139.331 139.833 130.749 1.00 5.76  ?  90   ILE A CG2  1 
ATOM   120   C CD1  . ILE A 1 90   ? 136.789 140.716 132.318 1.00 8.29  ?  90   ILE A CD1  1 
ATOM   121   N N    . SER A 1 91   ? 139.738 136.519 130.007 1.00 4.83  ?  91   SER A N    1 
ATOM   122   C CA   . SER A 1 91   ? 141.015 135.909 129.650 1.00 0.00  ?  91   SER A CA   1 
ATOM   123   C C    . SER A 1 91   ? 140.906 135.096 128.367 1.00 0.00  ?  91   SER A C    1 
ATOM   124   O O    . SER A 1 91   ? 141.843 135.068 127.562 1.00 3.09  ?  91   SER A O    1 
ATOM   125   C CB   . SER A 1 91   ? 141.512 135.030 130.797 1.00 3.22  ?  91   SER A CB   1 
ATOM   126   O OG   . SER A 1 91   ? 141.604 135.766 132.003 1.00 11.52 ?  91   SER A OG   1 
ATOM   127   N N    . ARG A 1 92   ? 139.777 134.413 128.167 1.00 5.18  ?  92   ARG A N    1 
ATOM   128   C CA   . ARG A 1 92   ? 139.591 133.605 126.969 1.00 1.57  ?  92   ARG A CA   1 
ATOM   129   C C    . ARG A 1 92   ? 139.493 134.481 125.726 1.00 7.08  ?  92   ARG A C    1 
ATOM   130   O O    . ARG A 1 92   ? 140.049 134.149 124.673 1.00 8.54  ?  92   ARG A O    1 
ATOM   131   C CB   . ARG A 1 92   ? 138.339 132.743 127.133 1.00 0.00  ?  92   ARG A CB   1 
ATOM   132   C CG   . ARG A 1 92   ? 138.243 131.541 126.215 1.00 4.79  ?  92   ARG A CG   1 
ATOM   133   C CD   . ARG A 1 92   ? 137.014 130.723 126.577 1.00 0.00  ?  92   ARG A CD   1 
ATOM   134   N NE   . ARG A 1 92   ? 136.877 129.505 125.788 1.00 0.80  ?  92   ARG A NE   1 
ATOM   135   C CZ   . ARG A 1 92   ? 137.349 128.322 126.152 1.00 7.58  ?  92   ARG A CZ   1 
ATOM   136   N NH1  . ARG A 1 92   ? 137.995 128.158 127.294 1.00 8.58  ?  92   ARG A NH1  1 
ATOM   137   N NH2  . ARG A 1 92   ? 137.160 127.274 125.355 1.00 11.49 ?  92   ARG A NH2  1 
ATOM   138   N N    . SER A 1 93   ? 138.787 135.612 125.828 1.00 13.38 ?  93   SER A N    1 
ATOM   139   C CA   . SER A 1 93   ? 138.641 136.495 124.675 1.00 10.96 ?  93   SER A CA   1 
ATOM   140   C C    . SER A 1 93   ? 139.920 137.275 124.397 1.00 7.53  ?  93   SER A C    1 
ATOM   141   O O    . SER A 1 93   ? 140.305 137.450 123.235 1.00 8.56  ?  93   SER A O    1 
ATOM   142   C CB   . SER A 1 93   ? 137.469 137.451 124.892 1.00 8.58  ?  93   SER A CB   1 
ATOM   143   O OG   . SER A 1 93   ? 136.264 136.741 125.116 1.00 9.23  ?  93   SER A OG   1 
ATOM   144   N N    . LEU A 1 94   ? 140.592 137.754 125.446 1.00 8.96  ?  94   LEU A N    1 
ATOM   145   C CA   . LEU A 1 94   ? 141.756 138.613 125.263 1.00 5.04  ?  94   LEU A CA   1 
ATOM   146   C C    . LEU A 1 94   ? 142.995 137.850 124.813 1.00 10.18 ?  94   LEU A C    1 
ATOM   147   O O    . LEU A 1 94   ? 143.905 138.459 124.241 1.00 11.12 ?  94   LEU A O    1 
ATOM   148   C CB   . LEU A 1 94   ? 142.059 139.363 126.562 1.00 6.01  ?  94   LEU A CB   1 
ATOM   149   C CG   . LEU A 1 94   ? 143.130 140.454 126.519 1.00 9.25  ?  94   LEU A CG   1 
ATOM   150   C CD1  . LEU A 1 94   ? 142.789 141.573 127.488 1.00 12.25 ?  94   LEU A CD1  1 
ATOM   151   C CD2  . LEU A 1 94   ? 144.499 139.872 126.824 1.00 10.32 ?  94   LEU A CD2  1 
ATOM   152   N N    . PHE A 1 95   ? 143.059 136.540 125.052 1.00 13.76 ?  95   PHE A N    1 
ATOM   153   C CA   . PHE A 1 95   ? 144.253 135.755 124.763 1.00 7.50  ?  95   PHE A CA   1 
ATOM   154   C C    . PHE A 1 95   ? 144.024 134.747 123.640 1.00 13.16 ?  95   PHE A C    1 
ATOM   155   O O    . PHE A 1 95   ? 144.672 133.699 123.598 1.00 12.86 ?  95   PHE A O    1 
ATOM   156   C CB   . PHE A 1 95   ? 144.744 135.047 126.024 1.00 7.25  ?  95   PHE A CB   1 
ATOM   157   C CG   . PHE A 1 95   ? 145.614 135.903 126.896 1.00 10.31 ?  95   PHE A CG   1 
ATOM   158   C CD1  . PHE A 1 95   ? 145.088 137.002 127.553 1.00 11.42 ?  95   PHE A CD1  1 
ATOM   159   C CD2  . PHE A 1 95   ? 146.958 135.616 127.053 1.00 13.81 ?  95   PHE A CD2  1 
ATOM   160   C CE1  . PHE A 1 95   ? 145.884 137.796 128.354 1.00 14.74 ?  95   PHE A CE1  1 
ATOM   161   C CE2  . PHE A 1 95   ? 147.761 136.407 127.853 1.00 11.64 ?  95   PHE A CE2  1 
ATOM   162   C CZ   . PHE A 1 95   ? 147.223 137.498 128.503 1.00 16.19 ?  95   PHE A CZ   1 
ATOM   163   N N    . LYS A 1 96   ? 143.096 135.049 122.729 1.00 12.89 ?  96   LYS A N    1 
ATOM   164   C CA   . LYS A 1 96   ? 142.873 134.185 121.574 1.00 13.84 ?  96   LYS A CA   1 
ATOM   165   C C    . LYS A 1 96   ? 144.071 134.205 120.632 1.00 18.13 ?  96   LYS A C    1 
ATOM   166   O O    . LYS A 1 96   ? 144.540 133.154 120.181 1.00 18.45 ?  96   LYS A O    1 
ATOM   167   C CB   . LYS A 1 96   ? 141.610 134.621 120.830 1.00 16.41 ?  96   LYS A CB   1 
ATOM   168   C CG   . LYS A 1 96   ? 140.333 133.942 121.286 1.00 20.14 ?  96   LYS A CG   1 
ATOM   169   C CD   . LYS A 1 96   ? 139.210 134.165 120.283 1.00 21.11 ?  96   LYS A CD   1 
ATOM   170   C CE   . LYS A 1 96   ? 138.260 135.258 120.750 1.00 16.66 ?  96   LYS A CE   1 
ATOM   171   N NZ   . LYS A 1 96   ? 136.859 135.010 120.311 1.00 13.06 ?  96   LYS A NZ   1 
ATOM   172   N N    . LYS A 1 97   ? 144.573 135.400 120.319 1.00 14.37 ?  97   LYS A N    1 
ATOM   173   C CA   . LYS A 1 97   ? 145.657 135.535 119.353 1.00 14.35 ?  97   LYS A CA   1 
ATOM   174   C C    . LYS A 1 97   ? 147.012 135.173 119.946 1.00 17.68 ?  97   LYS A C    1 
ATOM   175   O O    . LYS A 1 97   ? 147.885 134.681 119.221 1.00 20.78 ?  97   LYS A O    1 
ATOM   176   C CB   . LYS A 1 97   ? 145.692 136.963 118.805 1.00 17.85 ?  97   LYS A CB   1 
ATOM   177   C CG   . LYS A 1 97   ? 144.430 137.386 118.063 1.00 19.28 ?  97   LYS A CG   1 
ATOM   178   C CD   . LYS A 1 97   ? 143.914 136.290 117.144 1.00 15.30 ?  97   LYS A CD   1 
ATOM   179   C CE   . LYS A 1 97   ? 142.411 136.407 116.945 1.00 16.17 ?  97   LYS A CE   1 
ATOM   180   N NZ   . LYS A 1 97   ? 141.856 135.241 116.206 1.00 17.23 ?  97   LYS A NZ   1 
ATOM   181   N N    . LEU A 1 98   ? 147.209 135.421 121.238 1.00 16.78 ?  98   LEU A N    1 
ATOM   182   C CA   . LEU A 1 98   ? 148.506 135.187 121.858 1.00 15.22 ?  98   LEU A CA   1 
ATOM   183   C C    . LEU A 1 98   ? 148.818 133.691 121.898 1.00 15.10 ?  98   LEU A C    1 
ATOM   184   O O    . LEU A 1 98   ? 147.910 132.870 122.057 1.00 16.62 ?  98   LEU A O    1 
ATOM   185   C CB   . LEU A 1 98   ? 148.533 135.764 123.273 1.00 14.08 ?  98   LEU A CB   1 
ATOM   186   C CG   . LEU A 1 98   ? 148.920 137.237 123.414 1.00 16.03 ?  98   LEU A CG   1 
ATOM   187   C CD1  . LEU A 1 98   ? 147.717 138.141 123.195 1.00 17.23 ?  98   LEU A CD1  1 
ATOM   188   C CD2  . LEU A 1 98   ? 149.552 137.496 124.773 1.00 17.31 ?  98   LEU A CD2  1 
ATOM   189   N N    . PRO A 1 99   ? 150.090 133.306 121.752 1.00 18.19 ?  99   PRO A N    1 
ATOM   190   C CA   . PRO A 1 99   ? 150.429 131.875 121.794 1.00 21.93 ?  99   PRO A CA   1 
ATOM   191   C C    . PRO A 1 99   ? 150.310 131.259 123.176 1.00 19.20 ?  99   PRO A C    1 
ATOM   192   O O    . PRO A 1 99   ? 150.155 130.036 123.275 1.00 15.85 ?  99   PRO A O    1 
ATOM   193   C CB   . PRO A 1 99   ? 151.879 131.847 121.297 1.00 20.63 ?  99   PRO A CB   1 
ATOM   194   C CG   . PRO A 1 99   ? 152.425 133.173 121.705 1.00 17.49 ?  99   PRO A CG   1 
ATOM   195   C CD   . PRO A 1 99   ? 151.285 134.151 121.570 1.00 17.17 ?  99   PRO A CD   1 
ATOM   196   N N    . ILE A 1 100  ? 150.379 132.056 124.238 1.00 17.93 ?  100  ILE A N    1 
ATOM   197   C CA   . ILE A 1 100  ? 150.347 131.540 125.604 1.00 20.76 ?  100  ILE A CA   1 
ATOM   198   C C    . ILE A 1 100  ? 148.924 131.075 125.909 1.00 20.38 ?  100  ILE A C    1 
ATOM   199   O O    . ILE A 1 100  ? 147.959 131.630 125.359 1.00 19.12 ?  100  ILE A O    1 
ATOM   200   C CB   . ILE A 1 100  ? 150.859 132.598 126.603 1.00 18.20 ?  100  ILE A CB   1 
ATOM   201   C CG1  . ILE A 1 100  ? 151.720 131.954 127.691 1.00 17.82 ?  100  ILE A CG1  1 
ATOM   202   C CG2  . ILE A 1 100  ? 149.724 133.381 127.246 1.00 16.47 ?  100  ILE A CG2  1 
ATOM   203   C CD1  . ILE A 1 100  ? 152.562 132.945 128.457 1.00 19.19 ?  100  ILE A CD1  1 
ATOM   204   N N    . PRO A 1 101  ? 148.746 130.023 126.706 1.00 15.94 ?  101  PRO A N    1 
ATOM   205   C CA   . PRO A 1 101  ? 147.392 129.635 127.117 1.00 12.88 ?  101  PRO A CA   1 
ATOM   206   C C    . PRO A 1 101  ? 146.777 130.656 128.058 1.00 8.61  ?  101  PRO A C    1 
ATOM   207   O O    . PRO A 1 101  ? 147.473 131.358 128.795 1.00 10.30 ?  101  PRO A O    1 
ATOM   208   C CB   . PRO A 1 101  ? 147.604 128.287 127.817 1.00 12.38 ?  101  PRO A CB   1 
ATOM   209   C CG   . PRO A 1 101  ? 149.046 128.275 128.194 1.00 15.33 ?  101  PRO A CG   1 
ATOM   210   C CD   . PRO A 1 101  ? 149.748 129.026 127.112 1.00 13.54 ?  101  PRO A CD   1 
ATOM   211   N N    . TYR A 1 102  ? 145.447 130.731 128.027 1.00 3.72  ?  102  TYR A N    1 
ATOM   212   C CA   . TYR A 1 102  ? 144.725 131.714 128.824 1.00 1.36  ?  102  TYR A CA   1 
ATOM   213   C C    . TYR A 1 102  ? 144.603 131.321 130.290 1.00 5.98  ?  102  TYR A C    1 
ATOM   214   O O    . TYR A 1 102  ? 144.215 132.162 131.106 1.00 9.03  ?  102  TYR A O    1 
ATOM   215   C CB   . TYR A 1 102  ? 143.326 131.941 128.240 1.00 3.22  ?  102  TYR A CB   1 
ATOM   216   C CG   . TYR A 1 102  ? 142.293 130.911 128.650 1.00 5.51  ?  102  TYR A CG   1 
ATOM   217   C CD1  . TYR A 1 102  ? 142.205 129.688 128.001 1.00 4.02  ?  102  TYR A CD1  1 
ATOM   218   C CD2  . TYR A 1 102  ? 141.381 131.180 129.664 1.00 4.47  ?  102  TYR A CD2  1 
ATOM   219   C CE1  . TYR A 1 102  ? 141.259 128.750 128.369 1.00 0.00  ?  102  TYR A CE1  1 
ATOM   220   C CE2  . TYR A 1 102  ? 140.433 130.251 130.037 1.00 4.98  ?  102  TYR A CE2  1 
ATOM   221   C CZ   . TYR A 1 102  ? 140.375 129.039 129.386 1.00 3.04  ?  102  TYR A CZ   1 
ATOM   222   O OH   . TYR A 1 102  ? 139.428 128.113 129.756 1.00 9.86  ?  102  TYR A OH   1 
ATOM   223   N N    . THR A 1 103  ? 144.912 130.072 130.642 1.00 7.49  ?  103  THR A N    1 
ATOM   224   C CA   . THR A 1 103  ? 144.725 129.614 132.014 1.00 0.55  ?  103  THR A CA   1 
ATOM   225   C C    . THR A 1 103  ? 145.788 130.163 132.959 1.00 0.00  ?  103  THR A C    1 
ATOM   226   O O    . THR A 1 103  ? 145.532 130.297 134.164 1.00 7.69  ?  103  THR A O    1 
ATOM   227   C CB   . THR A 1 103  ? 144.713 128.086 132.056 1.00 0.00  ?  103  THR A CB   1 
ATOM   228   O OG1  . THR A 1 103  ? 145.755 127.574 131.218 1.00 2.95  ?  103  THR A OG1  1 
ATOM   229   C CG2  . THR A 1 103  ? 143.373 127.549 131.575 1.00 0.00  ?  103  THR A CG2  1 
ATOM   230   N N    . VAL A 1 104  ? 146.974 130.495 132.443 1.00 0.00  ?  104  VAL A N    1 
ATOM   231   C CA   . VAL A 1 104  ? 147.980 131.125 133.292 1.00 3.27  ?  104  VAL A CA   1 
ATOM   232   C C    . VAL A 1 104  ? 147.520 132.517 133.715 1.00 8.81  ?  104  VAL A C    1 
ATOM   233   O O    . VAL A 1 104  ? 147.865 132.988 134.806 1.00 17.31 ?  104  VAL A O    1 
ATOM   234   C CB   . VAL A 1 104  ? 149.349 131.150 132.582 1.00 5.05  ?  104  VAL A CB   1 
ATOM   235   C CG1  . VAL A 1 104  ? 149.352 132.113 131.404 1.00 7.31  ?  104  VAL A CG1  1 
ATOM   236   C CG2  . VAL A 1 104  ? 150.456 131.497 133.565 1.00 3.97  ?  104  VAL A CG2  1 
ATOM   237   N N    . VAL A 1 105  ? 146.712 133.179 132.884 1.00 3.70  ?  105  VAL A N    1 
ATOM   238   C CA   . VAL A 1 105  ? 146.116 134.451 133.275 1.00 3.80  ?  105  VAL A CA   1 
ATOM   239   C C    . VAL A 1 105  ? 145.157 134.245 134.437 1.00 7.08  ?  105  VAL A C    1 
ATOM   240   O O    . VAL A 1 105  ? 145.098 135.062 135.364 1.00 10.06 ?  105  VAL A O    1 
ATOM   241   C CB   . VAL A 1 105  ? 145.412 135.096 132.070 1.00 5.90  ?  105  VAL A CB   1 
ATOM   242   C CG1  . VAL A 1 105  ? 145.146 136.567 132.334 1.00 10.54 ?  105  VAL A CG1  1 
ATOM   243   C CG2  . VAL A 1 105  ? 146.236 134.896 130.810 1.00 7.34  ?  105  VAL A CG2  1 
ATOM   244   N N    . LEU A 1 106  ? 144.397 133.146 134.404 1.00 6.66  ?  106  LEU A N    1 
ATOM   245   C CA   . LEU A 1 106  ? 143.536 132.794 135.527 1.00 0.00  ?  106  LEU A CA   1 
ATOM   246   C C    . LEU A 1 106  ? 144.363 132.575 136.785 1.00 0.00  ?  106  LEU A C    1 
ATOM   247   O O    . LEU A 1 106  ? 143.965 132.988 137.881 1.00 7.67  ?  106  LEU A O    1 
ATOM   248   C CB   . LEU A 1 106  ? 142.736 131.534 135.197 1.00 0.00  ?  106  LEU A CB   1 
ATOM   249   C CG   . LEU A 1 106  ? 141.458 131.662 134.368 1.00 0.00  ?  106  LEU A CG   1 
ATOM   250   C CD1  . LEU A 1 106  ? 141.096 130.324 133.740 1.00 0.00  ?  106  LEU A CD1  1 
ATOM   251   C CD2  . LEU A 1 106  ? 140.315 132.184 135.203 1.00 2.07  ?  106  LEU A CD2  1 
ATOM   252   N N    . LEU A 1 107  ? 145.530 131.941 136.637 1.00 0.00  ?  107  LEU A N    1 
ATOM   253   C CA   . LEU A 1 107  ? 146.399 131.698 137.786 1.00 0.00  ?  107  LEU A CA   1 
ATOM   254   C C    . LEU A 1 107  ? 146.923 132.997 138.394 1.00 7.20  ?  107  LEU A C    1 
ATOM   255   O O    . LEU A 1 107  ? 146.900 133.166 139.619 1.00 11.79 ?  107  LEU A O    1 
ATOM   256   C CB   . LEU A 1 107  ? 147.558 130.790 137.380 1.00 0.29  ?  107  LEU A CB   1 
ATOM   257   C CG   . LEU A 1 107  ? 147.801 129.600 138.305 1.00 0.24  ?  107  LEU A CG   1 
ATOM   258   C CD1  . LEU A 1 107  ? 146.521 128.832 138.502 1.00 3.62  ?  107  LEU A CD1  1 
ATOM   259   C CD2  . LEU A 1 107  ? 148.865 128.693 137.739 1.00 1.63  ?  107  LEU A CD2  1 
ATOM   260   N N    . ILE A 1 108  ? 147.398 133.930 137.560 1.00 9.86  ?  108  ILE A N    1 
ATOM   261   C CA   . ILE A 1 108  ? 147.909 135.196 138.096 1.00 10.48 ?  108  ILE A CA   1 
ATOM   262   C C    . ILE A 1 108  ? 146.783 136.034 138.695 1.00 9.11  ?  108  ILE A C    1 
ATOM   263   O O    . ILE A 1 108  ? 146.978 136.716 139.710 1.00 11.88 ?  108  ILE A O    1 
ATOM   264   C CB   . ILE A 1 108  ? 148.699 135.994 137.038 1.00 11.26 ?  108  ILE A CB   1 
ATOM   265   C CG1  . ILE A 1 108  ? 149.628 135.100 136.217 1.00 9.53  ?  108  ILE A CG1  1 
ATOM   266   C CG2  . ILE A 1 108  ? 149.499 137.110 137.696 1.00 11.19 ?  108  ILE A CG2  1 
ATOM   267   C CD1  . ILE A 1 108  ? 150.613 134.291 137.044 1.00 5.74  ?  108  ILE A CD1  1 
ATOM   268   N N    . LEU A 1 109  ? 145.595 136.011 138.081 1.00 6.77  ?  109  LEU A N    1 
ATOM   269   C CA   . LEU A 1 109  ? 144.463 136.735 138.655 1.00 3.06  ?  109  LEU A CA   1 
ATOM   270   C C    . LEU A 1 109  ? 144.083 136.167 140.018 1.00 7.29  ?  109  LEU A C    1 
ATOM   271   O O    . LEU A 1 109  ? 143.818 136.923 140.964 1.00 11.78 ?  109  LEU A O    1 
ATOM   272   C CB   . LEU A 1 109  ? 143.269 136.692 137.703 1.00 4.51  ?  109  LEU A CB   1 
ATOM   273   C CG   . LEU A 1 109  ? 143.246 137.713 136.564 1.00 9.50  ?  109  LEU A CG   1 
ATOM   274   C CD1  . LEU A 1 109  ? 142.335 137.243 135.440 1.00 8.07  ?  109  LEU A CD1  1 
ATOM   275   C CD2  . LEU A 1 109  ? 142.817 139.080 137.072 1.00 10.43 ?  109  LEU A CD2  1 
ATOM   276   N N    . GLY A 1 110  ? 144.068 134.837 140.141 1.00 7.40  ?  110  GLY A N    1 
ATOM   277   C CA   . GLY A 1 110  ? 143.822 134.224 141.435 1.00 4.63  ?  110  GLY A CA   1 
ATOM   278   C C    . GLY A 1 110  ? 144.901 134.547 142.450 1.00 8.46  ?  110  GLY A C    1 
ATOM   279   O O    . GLY A 1 110  ? 144.619 134.701 143.637 1.00 15.93 ?  110  GLY A O    1 
ATOM   280   N N    . ALA A 1 111  ? 146.152 134.660 141.996 1.00 7.60  ?  111  ALA A N    1 
ATOM   281   C CA   . ALA A 1 111  ? 147.243 135.028 142.897 1.00 6.95  ?  111  ALA A CA   1 
ATOM   282   C C    . ALA A 1 111  ? 147.078 136.446 143.432 1.00 13.26 ?  111  ALA A C    1 
ATOM   283   O O    . ALA A 1 111  ? 147.279 136.696 144.631 1.00 11.40 ?  111  ALA A O    1 
ATOM   284   C CB   . ALA A 1 111  ? 148.582 134.880 142.176 1.00 10.11 ?  111  ALA A CB   1 
ATOM   285   N N    . ILE A 1 112  ? 146.722 137.388 142.554 1.00 19.89 ?  112  ILE A N    1 
ATOM   286   C CA   . ILE A 1 112  ? 146.485 138.765 142.983 1.00 11.63 ?  112  ILE A CA   1 
ATOM   287   C C    . ILE A 1 112  ? 145.310 138.827 143.951 1.00 9.85  ?  112  ILE A C    1 
ATOM   288   O O    . ILE A 1 112  ? 145.374 139.503 144.988 1.00 16.97 ?  112  ILE A O    1 
ATOM   289   C CB   . ILE A 1 112  ? 146.266 139.677 141.761 1.00 7.62  ?  112  ILE A CB   1 
ATOM   290   C CG1  . ILE A 1 112  ? 147.509 139.692 140.867 1.00 9.36  ?  112  ILE A CG1  1 
ATOM   291   C CG2  . ILE A 1 112  ? 145.915 141.088 142.198 1.00 10.79 ?  112  ILE A CG2  1 
ATOM   292   C CD1  . ILE A 1 112  ? 148.788 140.049 141.595 1.00 13.50 ?  112  ILE A CD1  1 
ATOM   293   N N    . LEU A 1 113  ? 144.227 138.106 143.639 1.00 6.82  ?  113  LEU A N    1 
ATOM   294   C CA   . LEU A 1 113  ? 143.077 138.060 144.539 1.00 9.58  ?  113  LEU A CA   1 
ATOM   295   C C    . LEU A 1 113  ? 143.449 137.439 145.880 1.00 9.00  ?  113  LEU A C    1 
ATOM   296   O O    . LEU A 1 113  ? 142.954 137.866 146.929 1.00 13.69 ?  113  LEU A O    1 
ATOM   297   C CB   . LEU A 1 113  ? 141.935 137.283 143.882 1.00 10.70 ?  113  LEU A CB   1 
ATOM   298   C CG   . LEU A 1 113  ? 140.739 136.886 144.748 1.00 10.77 ?  113  LEU A CG   1 
ATOM   299   C CD1  . LEU A 1 113  ? 139.745 138.030 144.843 1.00 11.98 ?  113  LEU A CD1  1 
ATOM   300   C CD2  . LEU A 1 113  ? 140.073 135.637 144.196 1.00 11.42 ?  113  LEU A CD2  1 
ATOM   301   N N    . GLY A 1 114  ? 144.333 136.440 145.867 1.00 7.54  ?  114  GLY A N    1 
ATOM   302   C CA   . GLY A 1 114  ? 144.762 135.820 147.107 1.00 8.98  ?  114  GLY A CA   1 
ATOM   303   C C    . GLY A 1 114  ? 145.571 136.748 147.987 1.00 13.71 ?  114  GLY A C    1 
ATOM   304   O O    . GLY A 1 114  ? 145.368 136.793 149.202 1.00 16.71 ?  114  GLY A O    1 
ATOM   305   N N    . VAL A 1 115  ? 146.497 137.504 147.391 1.00 17.72 ?  115  VAL A N    1 
ATOM   306   C CA   . VAL A 1 115  ? 147.268 138.443 148.205 1.00 16.31 ?  115  VAL A CA   1 
ATOM   307   C C    . VAL A 1 115  ? 146.377 139.586 148.702 1.00 16.05 ?  115  VAL A C    1 
ATOM   308   O O    . VAL A 1 115  ? 146.552 140.073 149.830 1.00 16.23 ?  115  VAL A O    1 
ATOM   309   C CB   . VAL A 1 115  ? 148.519 138.936 147.442 1.00 13.95 ?  115  VAL A CB   1 
ATOM   310   C CG1  . VAL A 1 115  ? 149.507 137.816 147.143 1.00 12.69 ?  115  VAL A CG1  1 
ATOM   311   C CG2  . VAL A 1 115  ? 148.108 139.644 146.161 1.00 14.02 ?  115  VAL A CG2  1 
ATOM   312   N N    . VAL A 1 116  ? 145.381 139.994 147.905 1.00 10.24 ?  116  VAL A N    1 
ATOM   313   C CA   . VAL A 1 116  ? 144.456 141.034 148.348 1.00 8.85  ?  116  VAL A CA   1 
ATOM   314   C C    . VAL A 1 116  ? 143.612 140.540 149.518 1.00 13.52 ?  116  VAL A C    1 
ATOM   315   O O    . VAL A 1 116  ? 143.426 141.252 150.512 1.00 19.91 ?  116  VAL A O    1 
ATOM   316   C CB   . VAL A 1 116  ? 143.588 141.507 147.168 1.00 7.15  ?  116  VAL A CB   1 
ATOM   317   C CG1  . VAL A 1 116  ? 142.361 142.259 147.660 1.00 9.98  ?  116  VAL A CG1  1 
ATOM   318   C CG2  . VAL A 1 116  ? 144.405 142.382 146.232 1.00 6.53  ?  116  VAL A CG2  1 
ATOM   319   N N    . ALA A 1 117  ? 143.100 139.308 149.427 1.00 11.96 ?  117  ALA A N    1 
ATOM   320   C CA   . ALA A 1 117  ? 142.331 138.732 150.525 1.00 12.42 ?  117  ALA A CA   1 
ATOM   321   C C    . ALA A 1 117  ? 143.193 138.510 151.760 1.00 14.45 ?  117  ALA A C    1 
ATOM   322   O O    . ALA A 1 117  ? 142.703 138.638 152.887 1.00 15.62 ?  117  ALA A O    1 
ATOM   323   C CB   . ALA A 1 117  ? 141.688 137.419 150.084 1.00 13.62 ?  117  ALA A CB   1 
ATOM   324   N N    . SER A 1 118  ? 144.471 138.174 151.572 1.00 11.43 ?  118  SER A N    1 
ATOM   325   C CA   . SER A 1 118  ? 145.384 138.088 152.704 1.00 13.93 ?  118  SER A CA   1 
ATOM   326   C C    . SER A 1 118  ? 145.605 139.451 153.344 1.00 19.55 ?  118  SER A C    1 
ATOM   327   O O    . SER A 1 118  ? 145.898 139.531 154.542 1.00 21.05 ?  118  SER A O    1 
ATOM   328   C CB   . SER A 1 118  ? 146.716 137.484 152.263 1.00 15.17 ?  118  SER A CB   1 
ATOM   329   O OG   . SER A 1 118  ? 147.557 137.238 153.376 1.00 16.67 ?  118  SER A OG   1 
ATOM   330   N N    . ASN A 1 119  ? 145.470 140.530 152.571 1.00 21.10 ?  119  ASN A N    1 
ATOM   331   C CA   . ASN A 1 119  ? 145.560 141.869 153.147 1.00 16.80 ?  119  ASN A CA   1 
ATOM   332   C C    . ASN A 1 119  ? 144.196 142.391 153.604 1.00 15.35 ?  119  ASN A C    1 
ATOM   333   O O    . ASN A 1 119  ? 144.011 142.707 154.783 1.00 13.29 ?  119  ASN A O    1 
ATOM   334   C CB   . ASN A 1 119  ? 146.202 142.830 152.141 1.00 16.61 ?  119  ASN A CB   1 
ATOM   335   C CG   . ASN A 1 119  ? 147.691 142.994 152.367 1.00 20.00 ?  119  ASN A CG   1 
ATOM   336   O OD1  . ASN A 1 119  ? 148.270 142.348 153.241 1.00 18.91 ?  119  ASN A OD1  1 
ATOM   337   N ND2  . ASN A 1 119  ? 148.319 143.859 151.580 1.00 23.73 ?  119  ASN A ND2  1 
ATOM   338   N N    . VAL A 1 120  ? 143.237 142.481 152.687 1.00 17.08 ?  120  VAL A N    1 
ATOM   339   C CA   . VAL A 1 120  ? 141.919 143.049 152.977 1.00 17.19 ?  120  VAL A CA   1 
ATOM   340   C C    . VAL A 1 120  ? 141.009 141.989 153.592 1.00 18.92 ?  120  VAL A C    1 
ATOM   341   O O    . VAL A 1 120  ? 140.879 140.889 153.035 1.00 18.43 ?  120  VAL A O    1 
ATOM   342   C CB   . VAL A 1 120  ? 141.288 143.646 151.710 1.00 15.96 ?  120  VAL A CB   1 
ATOM   343   C CG1  . VAL A 1 120  ? 140.077 144.493 152.064 1.00 16.15 ?  120  VAL A CG1  1 
ATOM   344   C CG2  . VAL A 1 120  ? 142.315 144.470 150.952 1.00 14.44 ?  120  VAL A CG2  1 
ATOM   345   N N    . PRO A 1 121  ? 140.355 142.270 154.730 1.00 20.19 ?  121  PRO A N    1 
ATOM   346   C CA   . PRO A 1 121  ? 139.524 141.243 155.378 1.00 17.87 ?  121  PRO A CA   1 
ATOM   347   C C    . PRO A 1 121  ? 138.181 141.000 154.700 1.00 19.99 ?  121  PRO A C    1 
ATOM   348   O O    . PRO A 1 121  ? 137.640 139.895 154.793 1.00 18.49 ?  121  PRO A O    1 
ATOM   349   C CB   . PRO A 1 121  ? 139.333 141.797 156.795 1.00 14.79 ?  121  PRO A CB   1 
ATOM   350   C CG   . PRO A 1 121  ? 139.455 143.269 156.638 1.00 21.51 ?  121  PRO A CG   1 
ATOM   351   C CD   . PRO A 1 121  ? 140.456 143.496 155.541 1.00 21.56 ?  121  PRO A CD   1 
ATOM   352   N N    . LEU A 1 122  ? 137.623 142.017 154.036 1.00 21.46 ?  122  LEU A N    1 
ATOM   353   C CA   . LEU A 1 122  ? 136.338 141.844 153.359 1.00 20.13 ?  122  LEU A CA   1 
ATOM   354   C C    . LEU A 1 122  ? 136.458 140.881 152.182 1.00 16.61 ?  122  LEU A C    1 
ATOM   355   O O    . LEU A 1 122  ? 135.610 139.995 151.999 1.00 20.28 ?  122  LEU A O    1 
ATOM   356   C CB   . LEU A 1 122  ? 135.813 143.203 152.894 1.00 15.37 ?  122  LEU A CB   1 
ATOM   357   C CG   . LEU A 1 122  ? 134.428 143.265 152.247 1.00 14.23 ?  122  LEU A CG   1 
ATOM   358   C CD1  . LEU A 1 122  ? 133.355 143.503 153.299 1.00 15.38 ?  122  LEU A CD1  1 
ATOM   359   C CD2  . LEU A 1 122  ? 134.385 144.346 151.179 1.00 15.13 ?  122  LEU A CD2  1 
ATOM   360   N N    . VAL A 1 123  ? 137.516 141.034 151.383 1.00 13.29 ?  123  VAL A N    1 
ATOM   361   C CA   . VAL A 1 123  ? 137.771 140.106 150.288 1.00 13.55 ?  123  VAL A CA   1 
ATOM   362   C C    . VAL A 1 123  ? 138.069 138.717 150.832 1.00 13.04 ?  123  VAL A C    1 
ATOM   363   O O    . VAL A 1 123  ? 137.696 137.710 150.220 1.00 13.84 ?  123  VAL A O    1 
ATOM   364   C CB   . VAL A 1 123  ? 138.917 140.635 149.403 1.00 16.16 ?  123  VAL A CB   1 
ATOM   365   C CG1  . VAL A 1 123  ? 139.053 139.798 148.140 1.00 14.07 ?  123  VAL A CG1  1 
ATOM   366   C CG2  . VAL A 1 123  ? 138.684 142.098 149.059 1.00 14.94 ?  123  VAL A CG2  1 
ATOM   367   N N    . GLU A 1 124  ? 138.731 138.635 151.990 1.00 14.79 ?  124  GLU A N    1 
ATOM   368   C CA   . GLU A 1 124  ? 138.958 137.341 152.628 1.00 15.47 ?  124  GLU A CA   1 
ATOM   369   C C    . GLU A 1 124  ? 137.642 136.678 153.015 1.00 12.45 ?  124  GLU A C    1 
ATOM   370   O O    . GLU A 1 124  ? 137.466 135.469 152.821 1.00 17.07 ?  124  GLU A O    1 
ATOM   371   C CB   . GLU A 1 124  ? 139.855 137.514 153.854 1.00 17.36 ?  124  GLU A CB   1 
ATOM   372   C CG   . GLU A 1 124  ? 139.635 136.489 154.956 1.00 19.84 ?  124  GLU A CG   1 
ATOM   373   C CD   . GLU A 1 124  ? 140.311 136.872 156.257 1.00 22.35 ?  124  GLU A CD   1 
ATOM   374   O OE1  . GLU A 1 124  ? 141.370 137.531 156.209 1.00 20.56 ?  124  GLU A OE1  1 
ATOM   375   O OE2  . GLU A 1 124  ? 139.781 136.511 157.329 1.00 21.66 ?  124  GLU A OE2  1 
ATOM   376   N N    . GLU A 1 125  ? 136.703 137.457 153.558 1.00 13.54 ?  125  GLU A N    1 
ATOM   377   C CA   . GLU A 1 125  ? 135.399 136.914 153.925 1.00 17.41 ?  125  GLU A CA   1 
ATOM   378   C C    . GLU A 1 125  ? 134.640 136.433 152.694 1.00 14.07 ?  125  GLU A C    1 
ATOM   379   O O    . GLU A 1 125  ? 133.977 135.389 152.731 1.00 14.22 ?  125  GLU A O    1 
ATOM   380   C CB   . GLU A 1 125  ? 134.592 137.968 154.688 1.00 18.82 ?  125  GLU A CB   1 
ATOM   381   C CG   . GLU A 1 125  ? 133.235 137.495 155.189 1.00 16.20 ?  125  GLU A CG   1 
ATOM   382   C CD   . GLU A 1 125  ? 132.495 138.557 155.979 1.00 17.75 ?  125  GLU A CD   1 
ATOM   383   O OE1  . GLU A 1 125  ? 133.021 139.683 156.108 1.00 18.08 ?  125  GLU A OE1  1 
ATOM   384   O OE2  . GLU A 1 125  ? 131.386 138.265 156.472 1.00 21.58 ?  125  GLU A OE2  1 
ATOM   385   N N    . HIS A 1 126  ? 134.741 137.169 151.588 1.00 10.67 ?  126  HIS A N    1 
ATOM   386   C CA   . HIS A 1 126  ? 134.060 136.751 150.367 1.00 7.38  ?  126  HIS A CA   1 
ATOM   387   C C    . HIS A 1 126  ? 134.795 135.654 149.599 1.00 14.24 ?  126  HIS A C    1 
ATOM   388   O O    . HIS A 1 126  ? 134.203 135.064 148.689 1.00 12.68 ?  126  HIS A O    1 
ATOM   389   C CB   . HIS A 1 126  ? 133.835 137.953 149.449 1.00 9.72  ?  126  HIS A CB   1 
ATOM   390   C CG   . HIS A 1 126  ? 132.620 138.755 149.795 1.00 10.65 ?  126  HIS A CG   1 
ATOM   391   N ND1  . HIS A 1 126  ? 131.405 138.565 149.175 1.00 9.81  ?  126  HIS A ND1  1 
ATOM   392   C CD2  . HIS A 1 126  ? 132.430 139.743 150.701 1.00 12.27 ?  126  HIS A CD2  1 
ATOM   393   C CE1  . HIS A 1 126  ? 130.519 139.403 149.681 1.00 12.97 ?  126  HIS A CE1  1 
ATOM   394   N NE2  . HIS A 1 126  ? 131.115 140.130 150.609 1.00 13.85 ?  126  HIS A NE2  1 
ATOM   395   N N    . THR A 1 127  ? 136.054 135.368 149.930 1.00 17.87 ?  127  THR A N    1 
ATOM   396   C CA   . THR A 1 127  ? 136.836 134.370 149.205 1.00 7.18  ?  127  THR A CA   1 
ATOM   397   C C    . THR A 1 127  ? 136.994 133.047 149.947 1.00 6.52  ?  127  THR A C    1 
ATOM   398   O O    . THR A 1 127  ? 137.116 132.001 149.298 1.00 13.01 ?  127  THR A O    1 
ATOM   399   C CB   . THR A 1 127  ? 138.231 134.930 148.888 1.00 3.35  ?  127  THR A CB   1 
ATOM   400   O OG1  . THR A 1 127  ? 138.119 136.305 148.502 1.00 14.97 ?  127  THR A OG1  1 
ATOM   401   C CG2  . THR A 1 127  ? 138.887 134.162 147.757 1.00 9.54  ?  127  THR A CG2  1 
ATOM   402   N N    . ARG A 1 128  ? 136.968 133.064 151.284 1.00 8.37  ?  128  ARG A N    1 
ATOM   403   C CA   . ARG A 1 128  ? 137.354 131.900 152.075 1.00 8.91  ?  128  ARG A CA   1 
ATOM   404   C C    . ARG A 1 128  ? 136.388 130.726 151.950 1.00 12.94 ?  128  ARG A C    1 
ATOM   405   O O    . ARG A 1 128  ? 136.772 129.595 152.264 1.00 13.88 ?  128  ARG A O    1 
ATOM   406   C CB   . ARG A 1 128  ? 137.489 132.304 153.547 1.00 12.63 ?  128  ARG A CB   1 
ATOM   407   C CG   . ARG A 1 128  ? 136.210 132.154 154.360 1.00 14.13 ?  128  ARG A CG   1 
ATOM   408   C CD   . ARG A 1 128  ? 136.483 132.093 155.853 1.00 12.79 ?  128  ARG A CD   1 
ATOM   409   N NE   . ARG A 1 128  ? 136.527 133.420 156.455 1.00 14.59 ?  128  ARG A NE   1 
ATOM   410   C CZ   . ARG A 1 128  ? 135.457 134.115 156.817 1.00 18.77 ?  128  ARG A CZ   1 
ATOM   411   N NH1  . ARG A 1 128  ? 134.234 133.634 156.660 1.00 16.40 ?  128  ARG A NH1  1 
ATOM   412   N NH2  . ARG A 1 128  ? 135.617 135.322 157.352 1.00 21.28 ?  128  ARG A NH2  1 
ATOM   413   N N    . ASP A 1 129  ? 135.155 130.955 151.502 1.00 13.56 ?  129  ASP A N    1 
ATOM   414   C CA   . ASP A 1 129  ? 134.168 129.886 151.450 1.00 10.74 ?  129  ASP A CA   1 
ATOM   415   C C    . ASP A 1 129  ? 134.213 129.082 150.159 1.00 10.19 ?  129  ASP A C    1 
ATOM   416   O O    . ASP A 1 129  ? 133.611 128.005 150.100 1.00 14.32 ?  129  ASP A O    1 
ATOM   417   C CB   . ASP A 1 129  ? 132.761 130.458 151.645 1.00 13.29 ?  129  ASP A CB   1 
ATOM   418   C CG   . ASP A 1 129  ? 132.467 130.793 153.092 1.00 17.93 ?  129  ASP A CG   1 
ATOM   419   O OD1  . ASP A 1 129  ? 132.617 129.899 153.951 1.00 23.60 ?  129  ASP A OD1  1 
ATOM   420   O OD2  . ASP A 1 129  ? 132.088 131.949 153.374 1.00 15.26 ?  129  ASP A OD2  1 
ATOM   421   N N    . VAL A 1 130  ? 134.905 129.568 149.130 1.00 10.33 ?  130  VAL A N    1 
ATOM   422   C CA   . VAL A 1 130  ? 135.029 128.833 147.877 1.00 4.30  ?  130  VAL A CA   1 
ATOM   423   C C    . VAL A 1 130  ? 136.494 128.489 147.651 1.00 2.99  ?  130  VAL A C    1 
ATOM   424   O O    . VAL A 1 130  ? 136.814 127.514 146.963 1.00 2.08  ?  130  VAL A O    1 
ATOM   425   C CB   . VAL A 1 130  ? 134.461 129.629 146.688 1.00 0.50  ?  130  VAL A CB   1 
ATOM   426   C CG1  . VAL A 1 130  ? 134.104 128.693 145.545 1.00 2.42  ?  130  VAL A CG1  1 
ATOM   427   C CG2  . VAL A 1 130  ? 133.246 130.438 147.111 1.00 5.09  ?  130  VAL A CG2  1 
ATOM   428   N N    . ALA A 1 131  ? 137.396 129.288 148.228 1.00 7.08  ?  131  ALA A N    1 
ATOM   429   C CA   . ALA A 1 131  ? 138.820 129.010 148.077 1.00 1.77  ?  131  ALA A CA   1 
ATOM   430   C C    . ALA A 1 131  ? 139.223 127.756 148.840 1.00 4.86  ?  131  ALA A C    1 
ATOM   431   O O    . ALA A 1 131  ? 139.979 126.924 148.324 1.00 8.76  ?  131  ALA A O    1 
ATOM   432   C CB   . ALA A 1 131  ? 139.642 130.210 148.544 1.00 6.84  ?  131  ALA A CB   1 
ATOM   433   N N    . HIS A 1 132  ? 138.729 127.597 150.063 1.00 5.13  ?  132  HIS A N    1 
ATOM   434   C CA   . HIS A 1 132  ? 139.034 126.442 150.903 1.00 5.86  ?  132  HIS A CA   1 
ATOM   435   C C    . HIS A 1 132  ? 137.744 125.646 151.080 1.00 7.22  ?  132  HIS A C    1 
ATOM   436   O O    . HIS A 1 132  ? 136.999 125.843 152.042 1.00 13.32 ?  132  HIS A O    1 
ATOM   437   C CB   . HIS A 1 132  ? 139.619 126.879 152.238 1.00 7.69  ?  132  HIS A CB   1 
ATOM   438   C CG   . HIS A 1 132  ? 140.686 127.921 152.113 1.00 8.34  ?  132  HIS A CG   1 
ATOM   439   N ND1  . HIS A 1 132  ? 140.432 129.267 152.257 1.00 11.40 ?  132  HIS A ND1  1 
ATOM   440   C CD2  . HIS A 1 132  ? 142.007 127.814 151.841 1.00 9.19  ?  132  HIS A CD2  1 
ATOM   441   C CE1  . HIS A 1 132  ? 141.553 129.945 152.089 1.00 8.83  ?  132  HIS A CE1  1 
ATOM   442   N NE2  . HIS A 1 132  ? 142.524 129.087 151.835 1.00 6.87  ?  132  HIS A NE2  1 
ATOM   443   N N    . MET A 1 133  ? 137.491 124.740 150.143 1.00 10.79 ?  133  MET A N    1 
ATOM   444   C CA   . MET A 1 133  ? 136.287 123.930 150.125 1.00 10.41 ?  133  MET A CA   1 
ATOM   445   C C    . MET A 1 133  ? 136.578 122.549 150.706 1.00 14.04 ?  133  MET A C    1 
ATOM   446   O O    . MET A 1 133  ? 137.702 122.233 151.100 1.00 17.26 ?  133  MET A O    1 
ATOM   447   C CB   . MET A 1 133  ? 135.752 123.824 148.697 1.00 6.73  ?  133  MET A CB   1 
ATOM   448   C CG   . MET A 1 133  ? 134.793 124.930 148.305 1.00 11.38 ?  133  MET A CG   1 
ATOM   449   S SD   . MET A 1 133  ? 133.878 124.518 146.810 1.00 12.00 ?  133  MET A SD   1 
ATOM   450   C CE   . MET A 1 133  ? 135.182 123.803 145.813 1.00 8.71  ?  133  MET A CE   1 
ATOM   451   N N    . ASP A 1 134  ? 135.544 121.717 150.758 1.00 6.71  ?  134  ASP A N    1 
ATOM   452   C CA   . ASP A 1 134  ? 135.730 120.337 151.176 1.00 3.84  ?  134  ASP A CA   1 
ATOM   453   C C    . ASP A 1 134  ? 136.415 119.548 150.061 1.00 9.84  ?  134  ASP A C    1 
ATOM   454   O O    . ASP A 1 134  ? 136.126 119.768 148.881 1.00 12.23 ?  134  ASP A O    1 
ATOM   455   C CB   . ASP A 1 134  ? 134.386 119.699 151.526 1.00 0.00  ?  134  ASP A CB   1 
ATOM   456   C CG   . ASP A 1 134  ? 134.514 118.587 152.547 1.00 7.76  ?  134  ASP A CG   1 
ATOM   457   O OD1  . ASP A 1 134  ? 135.141 118.818 153.602 1.00 7.96  ?  134  ASP A OD1  1 
ATOM   458   O OD2  . ASP A 1 134  ? 133.983 117.484 152.300 1.00 12.85 ?  134  ASP A OD2  1 
ATOM   459   N N    . PRO A 1 135  ? 137.337 118.641 150.399 1.00 2.93  ?  135  PRO A N    1 
ATOM   460   C CA   . PRO A 1 135  ? 137.979 117.824 149.354 1.00 0.00  ?  135  PRO A CA   1 
ATOM   461   C C    . PRO A 1 135  ? 137.014 116.921 148.606 1.00 4.71  ?  135  PRO A C    1 
ATOM   462   O O    . PRO A 1 135  ? 137.308 116.529 147.469 1.00 4.94  ?  135  PRO A O    1 
ATOM   463   C CB   . PRO A 1 135  ? 139.018 117.004 150.132 1.00 0.00  ?  135  PRO A CB   1 
ATOM   464   C CG   . PRO A 1 135  ? 138.587 117.073 151.559 1.00 0.95  ?  135  PRO A CG   1 
ATOM   465   C CD   . PRO A 1 135  ? 137.918 118.396 151.728 1.00 1.20  ?  135  PRO A CD   1 
ATOM   466   N N    . HIS A 1 136  ? 135.870 116.583 149.201 1.00 0.00  ?  136  HIS A N    1 
ATOM   467   C CA   . HIS A 1 136  ? 134.905 115.729 148.522 1.00 6.68  ?  136  HIS A CA   1 
ATOM   468   C C    . HIS A 1 136  ? 134.139 116.469 147.437 1.00 4.57  ?  136  HIS A C    1 
ATOM   469   O O    . HIS A 1 136  ? 133.557 115.821 146.564 1.00 5.17  ?  136  HIS A O    1 
ATOM   470   C CB   . HIS A 1 136  ? 133.938 115.121 149.536 1.00 1.90  ?  136  HIS A CB   1 
ATOM   471   C CG   . HIS A 1 136  ? 134.605 114.244 150.548 1.00 3.69  ?  136  HIS A CG   1 
ATOM   472   N ND1  . HIS A 1 136  ? 135.066 112.982 150.247 1.00 5.39  ?  136  HIS A ND1  1 
ATOM   473   C CD2  . HIS A 1 136  ? 134.896 114.450 151.854 1.00 4.01  ?  136  HIS A CD2  1 
ATOM   474   C CE1  . HIS A 1 136  ? 135.610 112.445 151.324 1.00 3.51  ?  136  HIS A CE1  1 
ATOM   475   N NE2  . HIS A 1 136  ? 135.519 113.315 152.313 1.00 6.02  ?  136  HIS A NE2  1 
ATOM   476   N N    . VAL A 1 137  ? 134.131 117.802 147.462 1.00 1.13  ?  137  VAL A N    1 
ATOM   477   C CA   . VAL A 1 137  ? 133.585 118.554 146.338 1.00 0.00  ?  137  VAL A CA   1 
ATOM   478   C C    . VAL A 1 137  ? 134.455 118.359 145.104 1.00 7.24  ?  137  VAL A C    1 
ATOM   479   O O    . VAL A 1 137  ? 133.952 118.201 143.986 1.00 7.54  ?  137  VAL A O    1 
ATOM   480   C CB   . VAL A 1 137  ? 133.447 120.040 146.711 1.00 0.00  ?  137  VAL A CB   1 
ATOM   481   C CG1  . VAL A 1 137  ? 132.932 120.843 145.532 1.00 0.81  ?  137  VAL A CG1  1 
ATOM   482   C CG2  . VAL A 1 137  ? 132.530 120.198 147.909 1.00 4.98  ?  137  VAL A CG2  1 
ATOM   483   N N    . LEU A 1 138  ? 135.776 118.352 145.290 1.00 0.00  ?  138  LEU A N    1 
ATOM   484   C CA   . LEU A 1 138  ? 136.683 118.109 144.175 1.00 0.00  ?  138  LEU A CA   1 
ATOM   485   C C    . LEU A 1 138  ? 136.689 116.642 143.768 1.00 0.00  ?  138  LEU A C    1 
ATOM   486   O O    . LEU A 1 138  ? 136.751 116.325 142.575 1.00 0.00  ?  138  LEU A O    1 
ATOM   487   C CB   . LEU A 1 138  ? 138.091 118.570 144.545 1.00 0.00  ?  138  LEU A CB   1 
ATOM   488   C CG   . LEU A 1 138  ? 138.283 120.075 144.712 1.00 0.00  ?  138  LEU A CG   1 
ATOM   489   C CD1  . LEU A 1 138  ? 139.195 120.387 145.884 1.00 0.00  ?  138  LEU A CD1  1 
ATOM   490   C CD2  . LEU A 1 138  ? 138.859 120.630 143.431 1.00 0.14  ?  138  LEU A CD2  1 
ATOM   491   N N    . LEU A 1 139  ? 136.629 115.730 144.741 1.00 0.00  ?  139  LEU A N    1 
ATOM   492   C CA   . LEU A 1 139  ? 136.707 114.309 144.419 1.00 0.39  ?  139  LEU A CA   1 
ATOM   493   C C    . LEU A 1 139  ? 135.405 113.773 143.832 1.00 4.07  ?  139  LEU A C    1 
ATOM   494   O O    . LEU A 1 139  ? 135.433 112.818 143.048 1.00 2.45  ?  139  LEU A O    1 
ATOM   495   C CB   . LEU A 1 139  ? 137.091 113.507 145.662 1.00 0.00  ?  139  LEU A CB   1 
ATOM   496   C CG   . LEU A 1 139  ? 138.547 113.596 146.119 1.00 0.00  ?  139  LEU A CG   1 
ATOM   497   C CD1  . LEU A 1 139  ? 138.705 113.019 147.515 1.00 0.00  ?  139  LEU A CD1  1 
ATOM   498   C CD2  . LEU A 1 139  ? 139.460 112.885 145.137 1.00 0.00  ?  139  LEU A CD2  1 
ATOM   499   N N    . GLN A 1 140  ? 134.263 114.364 144.187 1.00 5.11  ?  140  GLN A N    1 
ATOM   500   C CA   . GLN A 1 140  ? 132.966 113.817 143.821 1.00 0.00  ?  140  GLN A CA   1 
ATOM   501   C C    . GLN A 1 140  ? 132.260 114.571 142.703 1.00 0.00  ?  140  GLN A C    1 
ATOM   502   O O    . GLN A 1 140  ? 131.346 114.010 142.093 1.00 3.54  ?  140  GLN A O    1 
ATOM   503   C CB   . GLN A 1 140  ? 132.041 113.786 145.047 1.00 2.10  ?  140  GLN A CB   1 
ATOM   504   C CG   . GLN A 1 140  ? 132.430 112.761 146.103 1.00 9.01  ?  140  GLN A CG   1 
ATOM   505   C CD   . GLN A 1 140  ? 131.402 112.641 147.213 1.00 9.60  ?  140  GLN A CD   1 
ATOM   506   O OE1  . GLN A 1 140  ? 130.226 112.949 147.022 1.00 4.02  ?  140  GLN A OE1  1 
ATOM   507   N NE2  . GLN A 1 140  ? 131.844 112.195 148.383 1.00 7.02  ?  140  GLN A NE2  1 
ATOM   508   N N    . ILE A 1 141  ? 132.645 115.815 142.420 1.00 1.11  ?  141  ILE A N    1 
ATOM   509   C CA   . ILE A 1 141  ? 131.970 116.644 141.429 1.00 0.54  ?  141  ILE A CA   1 
ATOM   510   C C    . ILE A 1 141  ? 132.909 117.053 140.301 1.00 2.64  ?  141  ILE A C    1 
ATOM   511   O O    . ILE A 1 141  ? 132.563 116.945 139.122 1.00 4.81  ?  141  ILE A O    1 
ATOM   512   C CB   . ILE A 1 141  ? 131.327 117.891 142.080 1.00 1.05  ?  141  ILE A CB   1 
ATOM   513   C CG1  . ILE A 1 141  ? 130.435 117.491 143.254 1.00 0.00  ?  141  ILE A CG1  1 
ATOM   514   C CG2  . ILE A 1 141  ? 130.538 118.688 141.054 1.00 0.00  ?  141  ILE A CG2  1 
ATOM   515   C CD1  . ILE A 1 141  ? 129.868 118.665 144.003 1.00 0.00  ?  141  ILE A CD1  1 
ATOM   516   N N    . PHE A 1 142  ? 134.109 117.522 140.644 1.00 3.80  ?  142  PHE A N    1 
ATOM   517   C CA   . PHE A 1 142  ? 134.954 118.160 139.638 1.00 0.00  ?  142  PHE A CA   1 
ATOM   518   C C    . PHE A 1 142  ? 135.691 117.136 138.786 1.00 0.00  ?  142  PHE A C    1 
ATOM   519   O O    . PHE A 1 142  ? 135.658 117.206 137.552 1.00 11.73 ?  142  PHE A O    1 
ATOM   520   C CB   . PHE A 1 142  ? 135.947 119.113 140.307 1.00 0.12  ?  142  PHE A CB   1 
ATOM   521   C CG   . PHE A 1 142  ? 135.352 120.436 140.704 1.00 0.00  ?  142  PHE A CG   1 
ATOM   522   C CD1  . PHE A 1 142  ? 133.984 120.643 140.670 1.00 0.00  ?  142  PHE A CD1  1 
ATOM   523   C CD2  . PHE A 1 142  ? 136.164 121.480 141.098 1.00 0.74  ?  142  PHE A CD2  1 
ATOM   524   C CE1  . PHE A 1 142  ? 133.444 121.855 141.035 1.00 0.00  ?  142  PHE A CE1  1 
ATOM   525   C CE2  . PHE A 1 142  ? 135.622 122.696 141.456 1.00 0.00  ?  142  PHE A CE2  1 
ATOM   526   C CZ   . PHE A 1 142  ? 134.264 122.882 141.425 1.00 1.22  ?  142  PHE A CZ   1 
ATOM   527   N N    . LEU A 1 143  ? 136.379 116.193 139.428 1.00 0.00  ?  143  LEU A N    1 
ATOM   528   C CA   . LEU A 1 143  ? 137.106 115.170 138.681 1.00 0.94  ?  143  LEU A CA   1 
ATOM   529   C C    . LEU A 1 143  ? 136.206 114.266 137.837 1.00 2.80  ?  143  LEU A C    1 
ATOM   530   O O    . LEU A 1 143  ? 136.585 113.989 136.685 1.00 1.52  ?  143  LEU A O    1 
ATOM   531   C CB   . LEU A 1 143  ? 137.984 114.354 139.640 1.00 1.71  ?  143  LEU A CB   1 
ATOM   532   C CG   . LEU A 1 143  ? 139.196 115.075 140.229 1.00 0.15  ?  143  LEU A CG   1 
ATOM   533   C CD1  . LEU A 1 143  ? 139.888 114.195 141.251 1.00 0.00  ?  143  LEU A CD1  1 
ATOM   534   C CD2  . LEU A 1 143  ? 140.156 115.487 139.132 1.00 4.74  ?  143  LEU A CD2  1 
ATOM   535   N N    . PRO A 1 144  ? 135.054 113.756 138.320 1.00 0.00  ?  144  PRO A N    1 
ATOM   536   C CA   . PRO A 1 144  ? 134.177 112.998 137.409 1.00 0.00  ?  144  PRO A CA   1 
ATOM   537   C C    . PRO A 1 144  ? 133.745 113.774 136.178 1.00 0.00  ?  144  PRO A C    1 
ATOM   538   O O    . PRO A 1 144  ? 133.717 113.207 135.081 1.00 4.70  ?  144  PRO A O    1 
ATOM   539   C CB   . PRO A 1 144  ? 132.978 112.652 138.298 1.00 0.00  ?  144  PRO A CB   1 
ATOM   540   C CG   . PRO A 1 144  ? 133.535 112.562 139.642 1.00 0.00  ?  144  PRO A CG   1 
ATOM   541   C CD   . PRO A 1 144  ? 134.607 113.601 139.721 1.00 0.29  ?  144  PRO A CD   1 
ATOM   542   N N    . VAL A 1 145  ? 133.438 115.065 136.322 1.00 6.13  ?  145  VAL A N    1 
ATOM   543   C CA   . VAL A 1 145  ? 133.050 115.871 135.167 1.00 2.67  ?  145  VAL A CA   1 
ATOM   544   C C    . VAL A 1 145  ? 134.226 116.049 134.215 1.00 0.99  ?  145  VAL A C    1 
ATOM   545   O O    . VAL A 1 145  ? 134.085 115.886 132.995 1.00 12.36 ?  145  VAL A O    1 
ATOM   546   C CB   . VAL A 1 145  ? 132.486 117.227 135.632 1.00 0.00  ?  145  VAL A CB   1 
ATOM   547   C CG1  . VAL A 1 145  ? 132.440 118.211 134.479 1.00 4.84  ?  145  VAL A CG1  1 
ATOM   548   C CG2  . VAL A 1 145  ? 131.099 117.046 136.217 1.00 0.00  ?  145  VAL A CG2  1 
ATOM   549   N N    . LEU A 1 146  ? 135.406 116.366 134.757 1.00 8.47  ?  146  LEU A N    1 
ATOM   550   C CA   . LEU A 1 146  ? 136.567 116.623 133.910 1.00 1.07  ?  146  LEU A CA   1 
ATOM   551   C C    . LEU A 1 146  ? 137.029 115.373 133.174 1.00 0.00  ?  146  LEU A C    1 
ATOM   552   O O    . LEU A 1 146  ? 137.597 115.479 132.082 1.00 0.00  ?  146  LEU A O    1 
ATOM   553   C CB   . LEU A 1 146  ? 137.715 117.194 134.740 1.00 1.64  ?  146  LEU A CB   1 
ATOM   554   C CG   . LEU A 1 146  ? 137.607 118.661 135.155 1.00 0.00  ?  146  LEU A CG   1 
ATOM   555   C CD1  . LEU A 1 146  ? 138.809 119.063 135.988 1.00 0.00  ?  146  LEU A CD1  1 
ATOM   556   C CD2  . LEU A 1 146  ? 137.477 119.549 133.933 1.00 0.00  ?  146  LEU A CD2  1 
ATOM   557   N N    . ILE A 1 147  ? 136.809 114.191 133.743 1.00 6.75  ?  147  ILE A N    1 
ATOM   558   C CA   . ILE A 1 147  ? 137.199 112.966 133.051 1.00 0.88  ?  147  ILE A CA   1 
ATOM   559   C C    . ILE A 1 147  ? 136.107 112.489 132.094 1.00 0.00  ?  147  ILE A C    1 
ATOM   560   O O    . ILE A 1 147  ? 136.404 112.018 130.989 1.00 5.24  ?  147  ILE A O    1 
ATOM   561   C CB   . ILE A 1 147  ? 137.582 111.880 134.076 1.00 2.38  ?  147  ILE A CB   1 
ATOM   562   C CG1  . ILE A 1 147  ? 138.684 112.391 135.004 1.00 0.00  ?  147  ILE A CG1  1 
ATOM   563   C CG2  . ILE A 1 147  ? 138.106 110.657 133.381 1.00 0.00  ?  147  ILE A CG2  1 
ATOM   564   C CD1  . ILE A 1 147  ? 139.998 112.671 134.312 1.00 6.05  ?  147  ILE A CD1  1 
ATOM   565   N N    . PHE A 1 148  ? 134.832 112.612 132.483 1.00 4.71  ?  148  PHE A N    1 
ATOM   566   C CA   . PHE A 1 148  ? 133.744 112.209 131.600 1.00 3.01  ?  148  PHE A CA   1 
ATOM   567   C C    . PHE A 1 148  ? 133.662 113.081 130.359 1.00 0.00  ?  148  PHE A C    1 
ATOM   568   O O    . PHE A 1 148  ? 133.304 112.580 129.291 1.00 8.64  ?  148  PHE A O    1 
ATOM   569   C CB   . PHE A 1 148  ? 132.408 112.231 132.344 1.00 1.32  ?  148  PHE A CB   1 
ATOM   570   C CG   . PHE A 1 148  ? 131.239 111.775 131.507 1.00 0.00  ?  148  PHE A CG   1 
ATOM   571   C CD1  . PHE A 1 148  ? 130.955 110.430 131.365 1.00 0.00  ?  148  PHE A CD1  1 
ATOM   572   C CD2  . PHE A 1 148  ? 130.414 112.693 130.877 1.00 1.17  ?  148  PHE A CD2  1 
ATOM   573   C CE1  . PHE A 1 148  ? 129.883 110.008 130.604 1.00 0.00  ?  148  PHE A CE1  1 
ATOM   574   C CE2  . PHE A 1 148  ? 129.343 112.274 130.112 1.00 0.00  ?  148  PHE A CE2  1 
ATOM   575   C CZ   . PHE A 1 148  ? 129.077 110.932 129.977 1.00 0.00  ?  148  PHE A CZ   1 
ATOM   576   N N    . GLU A 1 149  ? 133.962 114.379 130.468 1.00 5.05  ?  149  GLU A N    1 
ATOM   577   C CA   . GLU A 1 149  ? 133.949 115.221 129.275 1.00 0.93  ?  149  GLU A CA   1 
ATOM   578   C C    . GLU A 1 149  ? 135.024 114.788 128.285 1.00 5.78  ?  149  GLU A C    1 
ATOM   579   O O    . GLU A 1 149  ? 134.784 114.756 127.072 1.00 10.32 ?  149  GLU A O    1 
ATOM   580   C CB   . GLU A 1 149  ? 134.131 116.688 129.655 1.00 0.00  ?  149  GLU A CB   1 
ATOM   581   C CG   . GLU A 1 149  ? 133.706 117.647 128.557 1.00 7.68  ?  149  GLU A CG   1 
ATOM   582   C CD   . GLU A 1 149  ? 134.880 118.197 127.771 1.00 8.64  ?  149  GLU A CD   1 
ATOM   583   O OE1  . GLU A 1 149  ? 135.932 118.468 128.385 1.00 10.47 ?  149  GLU A OE1  1 
ATOM   584   O OE2  . GLU A 1 149  ? 134.749 118.358 126.540 1.00 5.87  ?  149  GLU A OE2  1 
ATOM   585   N N    . SER A 1 150  ? 136.213 114.447 128.787 1.00 4.23  ?  150  SER A N    1 
ATOM   586   C CA   . SER A 1 150  ? 137.277 113.958 127.916 1.00 0.20  ?  150  SER A CA   1 
ATOM   587   C C    . SER A 1 150  ? 136.898 112.635 127.265 1.00 4.80  ?  150  SER A C    1 
ATOM   588   O O    . SER A 1 150  ? 137.164 112.423 126.076 1.00 8.73  ?  150  SER A O    1 
ATOM   589   C CB   . SER A 1 150  ? 138.576 113.812 128.707 1.00 1.75  ?  150  SER A CB   1 
ATOM   590   O OG   . SER A 1 150  ? 138.825 114.962 129.494 1.00 10.55 ?  150  SER A OG   1 
ATOM   591   N N    . ALA A 1 151  ? 136.285 111.728 128.030 1.00 9.77  ?  151  ALA A N    1 
ATOM   592   C CA   . ALA A 1 151  ? 135.876 110.445 127.462 1.00 0.03  ?  151  ALA A CA   1 
ATOM   593   C C    . ALA A 1 151  ? 134.761 110.612 126.433 1.00 0.00  ?  151  ALA A C    1 
ATOM   594   O O    . ALA A 1 151  ? 134.764 109.946 125.392 1.00 7.31  ?  151  ALA A O    1 
ATOM   595   C CB   . ALA A 1 151  ? 135.441 109.494 128.576 1.00 0.00  ?  151  ALA A CB   1 
ATOM   596   N N    . PHE A 1 152  ? 133.801 111.495 126.707 1.00 1.07  ?  152  PHE A N    1 
ATOM   597   C CA   . PHE A 1 152  ? 132.627 111.663 125.859 1.00 1.24  ?  152  PHE A CA   1 
ATOM   598   C C    . PHE A 1 152  ? 132.922 112.471 124.601 1.00 3.01  ?  152  PHE A C    1 
ATOM   599   O O    . PHE A 1 152  ? 132.258 112.276 123.578 1.00 4.00  ?  152  PHE A O    1 
ATOM   600   C CB   . PHE A 1 152  ? 131.516 112.331 126.671 1.00 0.71  ?  152  PHE A CB   1 
ATOM   601   C CG   . PHE A 1 152  ? 130.170 112.316 126.006 1.00 0.84  ?  152  PHE A CG   1 
ATOM   602   C CD1  . PHE A 1 152  ? 129.567 111.123 125.651 1.00 2.67  ?  152  PHE A CD1  1 
ATOM   603   C CD2  . PHE A 1 152  ? 129.495 113.501 125.761 1.00 5.43  ?  152  PHE A CD2  1 
ATOM   604   C CE1  . PHE A 1 152  ? 128.322 111.113 125.049 1.00 9.10  ?  152  PHE A CE1  1 
ATOM   605   C CE2  . PHE A 1 152  ? 128.252 113.496 125.160 1.00 5.85  ?  152  PHE A CE2  1 
ATOM   606   C CZ   . PHE A 1 152  ? 127.665 112.301 124.804 1.00 6.26  ?  152  PHE A CZ   1 
ATOM   607   N N    . ALA A 1 153  ? 133.897 113.383 124.656 1.00 6.57  ?  153  ALA A N    1 
ATOM   608   C CA   . ALA A 1 153  ? 134.133 114.281 123.529 1.00 8.91  ?  153  ALA A CA   1 
ATOM   609   C C    . ALA A 1 153  ? 134.822 113.571 122.368 1.00 16.72 ?  153  ALA A C    1 
ATOM   610   O O    . ALA A 1 153  ? 134.480 113.806 121.203 1.00 17.96 ?  153  ALA A O    1 
ATOM   611   C CB   . ALA A 1 153  ? 134.959 115.482 123.985 1.00 9.93  ?  153  ALA A CB   1 
ATOM   612   N N    . MET A 1 154  ? 135.795 112.712 122.662 1.00 18.10 ?  154  MET A N    1 
ATOM   613   C CA   . MET A 1 154  ? 136.627 112.120 121.623 1.00 15.02 ?  154  MET A CA   1 
ATOM   614   C C    . MET A 1 154  ? 135.840 111.132 120.768 1.00 17.90 ?  154  MET A C    1 
ATOM   615   O O    . MET A 1 154  ? 134.878 110.509 121.222 1.00 19.41 ?  154  MET A O    1 
ATOM   616   C CB   . MET A 1 154  ? 137.831 111.411 122.245 1.00 12.29 ?  154  MET A CB   1 
ATOM   617   C CG   . MET A 1 154  ? 137.471 110.185 123.072 1.00 13.67 ?  154  MET A CG   1 
ATOM   618   S SD   . MET A 1 154  ? 138.897 109.340 123.774 1.00 30.19 ?  154  MET A SD   1 
ATOM   619   C CE   . MET A 1 154  ? 139.804 110.718 124.467 1.00 13.86 ?  154  MET A CE   1 
ATOM   620   N N    . ASP A 1 155  ? 136.256 111.003 119.511 1.00 20.05 ?  155  ASP A N    1 
ATOM   621   C CA   . ASP A 1 155  ? 135.744 109.943 118.656 1.00 19.60 ?  155  ASP A CA   1 
ATOM   622   C C    . ASP A 1 155  ? 136.455 108.634 118.977 1.00 22.76 ?  155  ASP A C    1 
ATOM   623   O O    . ASP A 1 155  ? 137.633 108.616 119.345 1.00 26.44 ?  155  ASP A O    1 
ATOM   624   C CB   . ASP A 1 155  ? 135.907 110.307 117.177 1.00 19.23 ?  155  ASP A CB   1 
ATOM   625   C CG   . ASP A 1 155  ? 137.331 110.141 116.682 1.00 22.44 ?  155  ASP A CG   1 
ATOM   626   O OD1  . ASP A 1 155  ? 138.263 110.596 117.378 1.00 22.47 ?  155  ASP A OD1  1 
ATOM   627   O OD2  . ASP A 1 155  ? 137.518 109.560 115.592 1.00 28.40 ?  155  ASP A OD2  1 
ATOM   628   N N    . VAL A 1 156  ? 135.722 107.532 118.855 1.00 20.12 ?  156  VAL A N    1 
ATOM   629   C CA   . VAL A 1 156  ? 136.185 106.255 119.381 1.00 19.65 ?  156  VAL A CA   1 
ATOM   630   C C    . VAL A 1 156  ? 136.345 105.178 118.319 1.00 21.43 ?  156  VAL A C    1 
ATOM   631   O O    . VAL A 1 156  ? 137.029 104.177 118.584 1.00 20.78 ?  156  VAL A O    1 
ATOM   632   C CB   . VAL A 1 156  ? 135.248 105.754 120.499 1.00 19.12 ?  156  VAL A CB   1 
ATOM   633   C CG1  . VAL A 1 156  ? 135.412 106.602 121.743 1.00 19.03 ?  156  VAL A CG1  1 
ATOM   634   C CG2  . VAL A 1 156  ? 133.813 105.776 120.022 1.00 17.00 ?  156  VAL A CG2  1 
ATOM   635   N N    . HIS A 1 157  ? 135.755 105.330 117.130 1.00 22.93 ?  157  HIS A N    1 
ATOM   636   C CA   . HIS A 1 157  ? 135.775 104.254 116.142 1.00 21.94 ?  157  HIS A CA   1 
ATOM   637   C C    . HIS A 1 157  ? 137.175 103.954 115.622 1.00 18.50 ?  157  HIS A C    1 
ATOM   638   O O    . HIS A 1 157  ? 137.407 102.855 115.107 1.00 19.83 ?  157  HIS A O    1 
ATOM   639   C CB   . HIS A 1 157  ? 134.842 104.592 114.980 1.00 22.77 ?  157  HIS A CB   1 
ATOM   640   C CG   . HIS A 1 157  ? 133.393 104.394 115.298 1.00 24.05 ?  157  HIS A CG   1 
ATOM   641   N ND1  . HIS A 1 157  ? 132.890 103.196 115.759 1.00 24.27 ?  157  HIS A ND1  1 
ATOM   642   C CD2  . HIS A 1 157  ? 132.339 105.241 115.225 1.00 22.12 ?  157  HIS A CD2  1 
ATOM   643   C CE1  . HIS A 1 157  ? 131.589 103.313 115.955 1.00 23.54 ?  157  HIS A CE1  1 
ATOM   644   N NE2  . HIS A 1 157  ? 131.230 104.544 115.638 1.00 25.33 ?  157  HIS A NE2  1 
ATOM   645   N N    . THR A 1 158  ? 138.109 104.895 115.744 1.00 17.90 ?  158  THR A N    1 
ATOM   646   C CA   . THR A 1 158  ? 139.509 104.616 115.457 1.00 20.67 ?  158  THR A CA   1 
ATOM   647   C C    . THR A 1 158  ? 140.282 104.201 116.700 1.00 21.05 ?  158  THR A C    1 
ATOM   648   O O    . THR A 1 158  ? 141.217 103.397 116.602 1.00 23.66 ?  158  THR A O    1 
ATOM   649   C CB   . THR A 1 158  ? 140.178 105.840 114.826 1.00 20.36 ?  158  THR A CB   1 
ATOM   650   O OG1  . THR A 1 158  ? 140.058 106.959 115.712 1.00 18.27 ?  158  THR A OG1  1 
ATOM   651   C CG2  . THR A 1 158  ? 139.523 106.179 113.496 1.00 20.03 ?  158  THR A CG2  1 
ATOM   652   N N    . PHE A 1 159  ? 139.910 104.733 117.866 1.00 19.26 ?  159  PHE A N    1 
ATOM   653   C CA   . PHE A 1 159  ? 140.581 104.388 119.114 1.00 15.37 ?  159  PHE A CA   1 
ATOM   654   C C    . PHE A 1 159  ? 140.169 103.011 119.623 1.00 18.82 ?  159  PHE A C    1 
ATOM   655   O O    . PHE A 1 159  ? 140.993 102.300 120.207 1.00 22.10 ?  159  PHE A O    1 
ATOM   656   C CB   . PHE A 1 159  ? 140.293 105.465 120.164 1.00 18.01 ?  159  PHE A CB   1 
ATOM   657   C CG   . PHE A 1 159  ? 140.502 105.017 121.585 1.00 22.18 ?  159  PHE A CG   1 
ATOM   658   C CD1  . PHE A 1 159  ? 141.771 104.715 122.057 1.00 21.08 ?  159  PHE A CD1  1 
ATOM   659   C CD2  . PHE A 1 159  ? 139.428 104.909 122.454 1.00 18.87 ?  159  PHE A CD2  1 
ATOM   660   C CE1  . PHE A 1 159  ? 141.960 104.306 123.364 1.00 18.83 ?  159  PHE A CE1  1 
ATOM   661   C CE2  . PHE A 1 159  ? 139.612 104.502 123.761 1.00 12.90 ?  159  PHE A CE2  1 
ATOM   662   C CZ   . PHE A 1 159  ? 140.879 104.201 124.216 1.00 14.19 ?  159  PHE A CZ   1 
ATOM   663   N N    . MET A 1 160  ? 138.919 102.609 119.398 1.00 21.32 ?  160  MET A N    1 
ATOM   664   C CA   . MET A 1 160  ? 138.435 101.322 119.885 1.00 21.74 ?  160  MET A CA   1 
ATOM   665   C C    . MET A 1 160  ? 138.791 100.164 118.963 1.00 24.44 ?  160  MET A C    1 
ATOM   666   O O    . MET A 1 160  ? 138.435 99.021  119.270 1.00 26.44 ?  160  MET A O    1 
ATOM   667   C CB   . MET A 1 160  ? 136.918 101.370 120.090 1.00 24.27 ?  160  MET A CB   1 
ATOM   668   C CG   . MET A 1 160  ? 136.494 102.002 121.409 1.00 27.73 ?  160  MET A CG   1 
ATOM   669   S SD   . MET A 1 160  ? 134.709 101.992 121.664 1.00 34.29 ?  160  MET A SD   1 
ATOM   670   C CE   . MET A 1 160  ? 134.613 101.322 123.321 1.00 25.82 ?  160  MET A CE   1 
ATOM   671   N N    . ARG A 1 161  ? 139.465 100.425 117.840 1.00 22.54 ?  161  ARG A N    1 
ATOM   672   C CA   . ARG A 1 161  ? 139.960 99.334  117.007 1.00 21.50 ?  161  ARG A CA   1 
ATOM   673   C C    . ARG A 1 161  ? 141.097 98.591  117.698 1.00 19.75 ?  161  ARG A C    1 
ATOM   674   O O    . ARG A 1 161  ? 141.155 97.356  117.660 1.00 20.33 ?  161  ARG A O    1 
ATOM   675   C CB   . ARG A 1 161  ? 140.416 99.870  115.650 1.00 25.59 ?  161  ARG A CB   1 
ATOM   676   C CG   . ARG A 1 161  ? 139.317 99.928  114.602 1.00 26.04 ?  161  ARG A CG   1 
ATOM   677   C CD   . ARG A 1 161  ? 139.879 100.268 113.231 1.00 22.02 ?  161  ARG A CD   1 
ATOM   678   N NE   . ARG A 1 161  ? 139.080 101.281 112.552 1.00 23.78 ?  161  ARG A NE   1 
ATOM   679   C CZ   . ARG A 1 161  ? 139.547 102.453 112.143 1.00 24.51 ?  161  ARG A CZ   1 
ATOM   680   N NH1  . ARG A 1 161  ? 140.813 102.793 112.321 1.00 22.58 ?  161  ARG A NH1  1 
ATOM   681   N NH2  . ARG A 1 161  ? 138.722 103.305 111.541 1.00 23.68 ?  161  ARG A NH2  1 
ATOM   682   N N    . SER A 1 162  ? 142.010 99.327  118.334 1.00 15.24 ?  162  SER A N    1 
ATOM   683   C CA   . SER A 1 162  ? 143.118 98.753  119.088 1.00 22.53 ?  162  SER A CA   1 
ATOM   684   C C    . SER A 1 162  ? 143.015 99.064  120.577 1.00 21.28 ?  162  SER A C    1 
ATOM   685   O O    . SER A 1 162  ? 144.022 99.402  121.206 1.00 18.53 ?  162  SER A O    1 
ATOM   686   C CB   . SER A 1 162  ? 144.451 99.250  118.530 1.00 23.85 ?  162  SER A CB   1 
ATOM   687   O OG   . SER A 1 162  ? 144.516 100.665 118.548 1.00 21.35 ?  162  SER A OG   1 
ATOM   688   N N    . PHE A 1 163  ? 141.813 98.949  121.146 1.00 20.80 ?  163  PHE A N    1 
ATOM   689   C CA   . PHE A 1 163  ? 141.511 99.431  122.490 1.00 15.75 ?  163  PHE A CA   1 
ATOM   690   C C    . PHE A 1 163  ? 142.362 98.778  123.578 1.00 19.56 ?  163  PHE A C    1 
ATOM   691   O O    . PHE A 1 163  ? 142.916 99.464  124.447 1.00 21.32 ?  163  PHE A O    1 
ATOM   692   C CB   . PHE A 1 163  ? 140.019 99.204  122.760 1.00 16.55 ?  163  PHE A CB   1 
ATOM   693   C CG   . PHE A 1 163  ? 139.567 99.643  124.120 1.00 22.54 ?  163  PHE A CG   1 
ATOM   694   C CD1  . PHE A 1 163  ? 139.417 100.988 124.414 1.00 26.18 ?  163  PHE A CD1  1 
ATOM   695   C CD2  . PHE A 1 163  ? 139.273 98.710  125.100 1.00 20.16 ?  163  PHE A CD2  1 
ATOM   696   C CE1  . PHE A 1 163  ? 138.995 101.395 125.665 1.00 20.30 ?  163  PHE A CE1  1 
ATOM   697   C CE2  . PHE A 1 163  ? 138.850 99.110  126.352 1.00 21.78 ?  163  PHE A CE2  1 
ATOM   698   C CZ   . PHE A 1 163  ? 138.710 100.454 126.635 1.00 18.88 ?  163  PHE A CZ   1 
ATOM   699   N N    . SER A 1 164  ? 142.476 97.447  123.540 1.00 24.96 ?  164  SER A N    1 
ATOM   700   C CA   . SER A 1 164  ? 143.168 96.715  124.599 1.00 22.36 ?  164  SER A CA   1 
ATOM   701   C C    . SER A 1 164  ? 144.657 97.050  124.633 1.00 20.04 ?  164  SER A C    1 
ATOM   702   O O    . SER A 1 164  ? 145.244 97.239  125.708 1.00 22.66 ?  164  SER A O    1 
ATOM   703   C CB   . SER A 1 164  ? 142.958 95.212  124.409 1.00 17.32 ?  164  SER A CB   1 
ATOM   704   O OG   . SER A 1 164  ? 141.581 94.905  124.270 1.00 18.30 ?  164  SER A OG   1 
ATOM   705   N N    . GLN A 1 165  ? 145.282 97.126  123.456 1.00 16.10 ?  165  GLN A N    1 
ATOM   706   C CA   . GLN A 1 165  ? 146.707 97.433  123.380 1.00 17.64 ?  165  GLN A CA   1 
ATOM   707   C C    . GLN A 1 165  ? 146.994 98.845  123.882 1.00 20.39 ?  165  GLN A C    1 
ATOM   708   O O    . GLN A 1 165  ? 147.977 99.075  124.599 1.00 22.27 ?  165  GLN A O    1 
ATOM   709   C CB   . GLN A 1 165  ? 147.193 97.251  121.941 1.00 18.19 ?  165  GLN A CB   1 
ATOM   710   C CG   . GLN A 1 165  ? 148.611 97.723  121.678 1.00 19.74 ?  165  GLN A CG   1 
ATOM   711   C CD   . GLN A 1 165  ? 148.657 99.131  121.125 1.00 21.56 ?  165  GLN A CD   1 
ATOM   712   O OE1  . GLN A 1 165  ? 147.640 99.667  120.689 1.00 21.16 ?  165  GLN A OE1  1 
ATOM   713   N NE2  . GLN A 1 165  ? 149.839 99.736  121.135 1.00 24.06 ?  165  GLN A NE2  1 
ATOM   714   N N    . VAL A 1 166  ? 146.143 99.806  123.511 1.00 21.81 ?  166  VAL A N    1 
ATOM   715   C CA   . VAL A 1 166  ? 146.317 101.182 123.973 1.00 24.64 ?  166  VAL A CA   1 
ATOM   716   C C    . VAL A 1 166  ? 146.125 101.265 125.483 1.00 17.16 ?  166  VAL A C    1 
ATOM   717   O O    . VAL A 1 166  ? 146.840 102.004 126.174 1.00 16.19 ?  166  VAL A O    1 
ATOM   718   C CB   . VAL A 1 166  ? 145.361 102.126 123.216 1.00 23.16 ?  166  VAL A CB   1 
ATOM   719   C CG1  . VAL A 1 166  ? 145.470 103.545 123.746 1.00 18.72 ?  166  VAL A CG1  1 
ATOM   720   C CG2  . VAL A 1 166  ? 145.672 102.110 121.729 1.00 18.36 ?  166  VAL A CG2  1 
ATOM   721   N N    . CYS A 1 167  ? 145.169 100.498 126.020 1.00 15.06 ?  167  CYS A N    1 
ATOM   722   C CA   . CYS A 1 167  ? 144.987 100.436 127.468 1.00 20.93 ?  167  CYS A CA   1 
ATOM   723   C C    . CYS A 1 167  ? 146.245 99.924  128.162 1.00 25.45 ?  167  CYS A C    1 
ATOM   724   O O    . CYS A 1 167  ? 146.707 100.508 129.152 1.00 24.93 ?  167  CYS A O    1 
ATOM   725   C CB   . CYS A 1 167  ? 143.791 99.545  127.809 1.00 18.93 ?  167  CYS A CB   1 
ATOM   726   S SG   . CYS A 1 167  ? 142.175 100.270 127.462 1.00 33.01 ?  167  CYS A SG   1 
ATOM   727   N N    . ILE A 1 168  ? 146.819 98.838  127.634 1.00 20.45 ?  168  ILE A N    1 
ATOM   728   C CA   . ILE A 1 168  ? 148.031 98.263  128.219 1.00 17.97 ?  168  ILE A CA   1 
ATOM   729   C C    . ILE A 1 168  ? 149.175 99.272  128.176 1.00 19.89 ?  168  ILE A C    1 
ATOM   730   O O    . ILE A 1 168  ? 149.897 99.466  129.165 1.00 26.54 ?  168  ILE A O    1 
ATOM   731   C CB   . ILE A 1 168  ? 148.402 96.953  127.496 1.00 22.67 ?  168  ILE A CB   1 
ATOM   732   C CG1  . ILE A 1 168  ? 147.387 95.852  127.816 1.00 20.46 ?  168  ILE A CG1  1 
ATOM   733   C CG2  . ILE A 1 168  ? 149.810 96.506  127.863 1.00 22.21 ?  168  ILE A CG2  1 
ATOM   734   C CD1  . ILE A 1 168  ? 147.440 95.361  129.249 1.00 18.86 ?  168  ILE A CD1  1 
ATOM   735   N N    . LEU A 1 169  ? 149.336 99.946  127.032 1.00 14.70 ?  169  LEU A N    1 
ATOM   736   C CA   . LEU A 1 169  ? 150.405 100.928 126.864 1.00 18.12 ?  169  LEU A CA   1 
ATOM   737   C C    . LEU A 1 169  ? 150.271 102.079 127.857 1.00 18.26 ?  169  LEU A C    1 
ATOM   738   O O    . LEU A 1 169  ? 151.248 102.466 128.515 1.00 19.88 ?  169  LEU A O    1 
ATOM   739   C CB   . LEU A 1 169  ? 150.390 101.451 125.425 1.00 20.53 ?  169  LEU A CB   1 
ATOM   740   C CG   . LEU A 1 169  ? 150.899 102.865 125.126 1.00 22.39 ?  169  LEU A CG   1 
ATOM   741   C CD1  . LEU A 1 169  ? 152.418 102.947 125.208 1.00 24.51 ?  169  LEU A CD1  1 
ATOM   742   C CD2  . LEU A 1 169  ? 150.399 103.336 123.767 1.00 18.43 ?  169  LEU A CD2  1 
ATOM   743   N N    . ALA A 1 170  ? 149.058 102.627 127.986 1.00 19.21 ?  170  ALA A N    1 
ATOM   744   C CA   . ALA A 1 170  ? 148.838 103.757 128.885 1.00 19.51 ?  170  ALA A CA   1 
ATOM   745   C C    . ALA A 1 170  ? 149.086 103.369 130.338 1.00 19.90 ?  170  ALA A C    1 
ATOM   746   O O    . ALA A 1 170  ? 149.747 104.107 131.085 1.00 18.74 ?  170  ALA A O    1 
ATOM   747   C CB   . ALA A 1 170  ? 147.419 104.296 128.705 1.00 16.58 ?  170  ALA A CB   1 
ATOM   748   N N    . LEU A 1 171  ? 148.571 102.205 130.753 1.00 19.50 ?  171  LEU A N    1 
ATOM   749   C CA   . LEU A 1 171  ? 148.764 101.766 132.133 1.00 21.64 ?  171  LEU A CA   1 
ATOM   750   C C    . LEU A 1 171  ? 150.241 101.551 132.441 1.00 17.84 ?  171  LEU A C    1 
ATOM   751   O O    . LEU A 1 171  ? 150.740 101.997 133.484 1.00 17.77 ?  171  LEU A O    1 
ATOM   752   C CB   . LEU A 1 171  ? 147.966 100.488 132.403 1.00 19.06 ?  171  LEU A CB   1 
ATOM   753   C CG   . LEU A 1 171  ? 146.436 100.546 132.334 1.00 17.14 ?  171  LEU A CG   1 
ATOM   754   C CD1  . LEU A 1 171  ? 145.818 99.336  133.019 1.00 19.63 ?  171  LEU A CD1  1 
ATOM   755   C CD2  . LEU A 1 171  ? 145.898 101.836 132.931 1.00 17.78 ?  171  LEU A CD2  1 
ATOM   756   N N    . PHE A 1 172  ? 150.967 100.896 131.527 1.00 14.39 ?  172  PHE A N    1 
ATOM   757   C CA   . PHE A 1 172  ? 152.380 100.618 131.767 1.00 20.60 ?  172  PHE A CA   1 
ATOM   758   C C    . PHE A 1 172  ? 153.198 101.903 131.835 1.00 22.33 ?  172  PHE A C    1 
ATOM   759   O O    . PHE A 1 172  ? 154.057 102.057 132.720 1.00 22.36 ?  172  PHE A O    1 
ATOM   760   C CB   . PHE A 1 172  ? 152.920 99.688  130.681 1.00 22.09 ?  172  PHE A CB   1 
ATOM   761   C CG   . PHE A 1 172  ? 152.726 98.226  130.979 1.00 25.92 ?  172  PHE A CG   1 
ATOM   762   C CD1  . PHE A 1 172  ? 151.490 97.740  131.379 1.00 21.99 ?  172  PHE A CD1  1 
ATOM   763   C CD2  . PHE A 1 172  ? 153.780 97.335  130.857 1.00 24.14 ?  172  PHE A CD2  1 
ATOM   764   C CE1  . PHE A 1 172  ? 151.309 96.396  131.653 1.00 18.62 ?  172  PHE A CE1  1 
ATOM   765   C CE2  . PHE A 1 172  ? 153.607 95.989  131.130 1.00 21.12 ?  172  PHE A CE2  1 
ATOM   766   C CZ   . PHE A 1 172  ? 152.370 95.520  131.528 1.00 22.03 ?  172  PHE A CZ   1 
ATOM   767   N N    . GLY A 1 173  ? 152.937 102.843 130.922 1.00 15.62 ?  173  GLY A N    1 
ATOM   768   C CA   . GLY A 1 173  ? 153.637 104.112 130.923 1.00 14.47 ?  173  GLY A CA   1 
ATOM   769   C C    . GLY A 1 173  ? 153.415 104.921 132.185 1.00 15.71 ?  173  GLY A C    1 
ATOM   770   O O    . GLY A 1 173  ? 154.375 105.437 132.778 1.00 18.28 ?  173  GLY A O    1 
ATOM   771   N N    . LEU A 1 174  ? 152.153 105.025 132.619 1.00 14.94 ?  174  LEU A N    1 
ATOM   772   C CA   . LEU A 1 174  ? 151.884 105.754 133.854 1.00 14.10 ?  174  LEU A CA   1 
ATOM   773   C C    . LEU A 1 174  ? 152.551 105.084 135.046 1.00 16.41 ?  174  LEU A C    1 
ATOM   774   O O    . LEU A 1 174  ? 153.125 105.768 135.904 1.00 21.34 ?  174  LEU A O    1 
ATOM   775   C CB   . LEU A 1 174  ? 150.383 105.892 134.098 1.00 15.77 ?  174  LEU A CB   1 
ATOM   776   C CG   . LEU A 1 174  ? 150.133 106.725 135.362 1.00 17.28 ?  174  LEU A CG   1 
ATOM   777   C CD1  . LEU A 1 174  ? 149.266 107.918 135.081 1.00 15.48 ?  174  LEU A CD1  1 
ATOM   778   C CD2  . LEU A 1 174  ? 149.544 105.892 136.487 1.00 10.58 ?  174  LEU A CD2  1 
ATOM   779   N N    . VAL A 1 175  ? 152.497 103.749 135.113 1.00 18.54 ?  175  VAL A N    1 
ATOM   780   C CA   . VAL A 1 175  ? 153.065 103.045 136.260 1.00 20.38 ?  175  VAL A CA   1 
ATOM   781   C C    . VAL A 1 175  ? 154.567 103.299 136.353 1.00 14.43 ?  175  VAL A C    1 
ATOM   782   O O    . VAL A 1 175  ? 155.082 103.685 137.414 1.00 12.07 ?  175  VAL A O    1 
ATOM   783   C CB   . VAL A 1 175  ? 152.740 101.541 136.181 1.00 22.45 ?  175  VAL A CB   1 
ATOM   784   C CG1  . VAL A 1 175  ? 153.680 100.736 137.063 1.00 17.20 ?  175  VAL A CG1  1 
ATOM   785   C CG2  . VAL A 1 175  ? 151.295 101.293 136.590 1.00 20.02 ?  175  VAL A CG2  1 
ATOM   786   N N    . VAL A 1 176  ? 155.282 103.155 135.229 1.00 11.23 ?  176  VAL A N    1 
ATOM   787   C CA   . VAL A 1 176  ? 156.733 103.327 135.278 1.00 16.27 ?  176  VAL A CA   1 
ATOM   788   C C    . VAL A 1 176  ? 157.100 104.776 135.598 1.00 18.00 ?  176  VAL A C    1 
ATOM   789   O O    . VAL A 1 176  ? 157.995 105.028 136.420 1.00 17.74 ?  176  VAL A O    1 
ATOM   790   C CB   . VAL A 1 176  ? 157.408 102.824 133.982 1.00 18.17 ?  176  VAL A CB   1 
ATOM   791   C CG1  . VAL A 1 176  ? 157.189 101.326 133.819 1.00 19.12 ?  176  VAL A CG1  1 
ATOM   792   C CG2  . VAL A 1 176  ? 156.940 103.575 132.745 1.00 19.41 ?  176  VAL A CG2  1 
ATOM   793   N N    . ALA A 1 177  ? 156.398 105.750 134.995 1.00 16.39 ?  177  ALA A N    1 
ATOM   794   C CA   . ALA A 1 177  ? 156.734 107.150 135.247 1.00 13.98 ?  177  ALA A CA   1 
ATOM   795   C C    . ALA A 1 177  ? 156.475 107.526 136.700 1.00 14.32 ?  177  ALA A C    1 
ATOM   796   O O    . ALA A 1 177  ? 157.255 108.275 137.307 1.00 14.52 ?  177  ALA A O    1 
ATOM   797   C CB   . ALA A 1 177  ? 155.952 108.060 134.301 1.00 9.51  ?  177  ALA A CB   1 
ATOM   798   N N    . SER A 1 178  ? 155.396 106.993 137.281 1.00 12.27 ?  178  SER A N    1 
ATOM   799   C CA   . SER A 1 178  ? 155.120 107.227 138.692 1.00 6.20  ?  178  SER A CA   1 
ATOM   800   C C    . SER A 1 178  ? 156.222 106.656 139.574 1.00 9.17  ?  178  SER A C    1 
ATOM   801   O O    . SER A 1 178  ? 156.625 107.292 140.556 1.00 12.74 ?  178  SER A O    1 
ATOM   802   C CB   . SER A 1 178  ? 153.766 106.627 139.066 1.00 8.08  ?  178  SER A CB   1 
ATOM   803   O OG   . SER A 1 178  ? 152.823 106.835 138.031 1.00 9.91  ?  178  SER A OG   1 
ATOM   804   N N    . VAL A 1 179  ? 156.720 105.476 139.226 1.00 11.60 ?  179  VAL A N    1 
ATOM   805   C CA   . VAL A 1 179  ? 157.810 104.881 139.985 1.00 10.93 ?  179  VAL A CA   1 
ATOM   806   C C    . VAL A 1 179  ? 159.035 105.775 139.930 1.00 16.90 ?  179  VAL A C    1 
ATOM   807   O O    . VAL A 1 179  ? 159.624 106.097 140.962 1.00 18.64 ?  179  VAL A O    1 
ATOM   808   C CB   . VAL A 1 179  ? 158.182 103.494 139.437 1.00 12.72 ?  179  VAL A CB   1 
ATOM   809   C CG1  . VAL A 1 179  ? 159.423 102.962 140.137 1.00 15.33 ?  179  VAL A CG1  1 
ATOM   810   C CG2  . VAL A 1 179  ? 157.015 102.532 139.594 1.00 12.14 ?  179  VAL A CG2  1 
ATOM   811   N N    . LEU A 1 180  ? 159.413 106.188 138.726 1.00 11.65 ?  180  LEU A N    1 
ATOM   812   C CA   . LEU A 1 180  ? 160.592 107.030 138.565 1.00 13.50 ?  180  LEU A CA   1 
ATOM   813   C C    . LEU A 1 180  ? 160.461 108.300 139.385 1.00 11.56 ?  180  LEU A C    1 
ATOM   814   O O    . LEU A 1 180  ? 161.398 108.699 140.078 1.00 12.61 ?  180  LEU A O    1 
ATOM   815   C CB   . LEU A 1 180  ? 160.798 107.377 137.090 1.00 13.49 ?  180  LEU A CB   1 
ATOM   816   C CG   . LEU A 1 180  ? 161.504 106.345 136.205 1.00 14.18 ?  180  LEU A CG   1 
ATOM   817   C CD1  . LEU A 1 180  ? 161.052 104.922 136.494 1.00 12.04 ?  180  LEU A CD1  1 
ATOM   818   C CD2  . LEU A 1 180  ? 161.335 106.682 134.732 1.00 14.68 ?  180  LEU A CD2  1 
ATOM   819   N N    . THR A 1 181  ? 159.297 108.934 139.316 1.00 12.45 ?  181  THR A N    1 
ATOM   820   C CA   . THR A 1 181  ? 159.076 110.160 140.070 1.00 13.70 ?  181  THR A CA   1 
ATOM   821   C C    . THR A 1 181  ? 159.222 109.904 141.560 1.00 13.10 ?  181  THR A C    1 
ATOM   822   O O    . THR A 1 181  ? 159.891 110.661 142.263 1.00 11.41 ?  181  THR A O    1 
ATOM   823   C CB   . THR A 1 181  ? 157.680 110.744 139.794 1.00 16.15 ?  181  THR A CB   1 
ATOM   824   O OG1  . THR A 1 181  ? 157.503 110.919 138.382 1.00 15.87 ?  181  THR A OG1  1 
ATOM   825   C CG2  . THR A 1 181  ? 157.517 112.085 140.494 1.00 11.32 ?  181  THR A CG2  1 
ATOM   826   N N    . ALA A 1 182  ? 158.604 108.833 142.045 1.00 11.23 ?  182  ALA A N    1 
ATOM   827   C CA   . ALA A 1 182  ? 158.658 108.526 143.472 1.00 10.70 ?  182  ALA A CA   1 
ATOM   828   C C    . ALA A 1 182  ? 160.093 108.317 143.948 1.00 18.74 ?  182  ALA A C    1 
ATOM   829   O O    . ALA A 1 182  ? 160.463 108.761 145.043 1.00 18.43 ?  182  ALA A O    1 
ATOM   830   C CB   . ALA A 1 182  ? 157.808 107.294 143.774 1.00 8.13  ?  182  ALA A CB   1 
ATOM   831   N N    . VAL A 1 183  ? 160.912 107.633 143.143 1.00 19.65 ?  183  VAL A N    1 
ATOM   832   C CA   . VAL A 1 183  ? 162.319 107.442 143.497 1.00 15.99 ?  183  VAL A CA   1 
ATOM   833   C C    . VAL A 1 183  ? 163.042 108.785 143.562 1.00 16.27 ?  183  VAL A C    1 
ATOM   834   O O    . VAL A 1 183  ? 163.838 109.040 144.481 1.00 17.35 ?  183  VAL A O    1 
ATOM   835   C CB   . VAL A 1 183  ? 162.992 106.476 142.503 1.00 12.58 ?  183  VAL A CB   1 
ATOM   836   C CG1  . VAL A 1 183  ? 164.495 106.436 142.717 1.00 14.12 ?  183  VAL A CG1  1 
ATOM   837   C CG2  . VAL A 1 183  ? 162.412 105.083 142.655 1.00 15.38 ?  183  VAL A CG2  1 
ATOM   838   N N    . LEU A 1 184  ? 162.769 109.666 142.594 1.00 16.68 ?  184  LEU A N    1 
ATOM   839   C CA   . LEU A 1 184  ? 163.334 111.011 142.617 1.00 16.22 ?  184  LEU A CA   1 
ATOM   840   C C    . LEU A 1 184  ? 162.899 111.800 143.845 1.00 17.65 ?  184  LEU A C    1 
ATOM   841   O O    . LEU A 1 184  ? 163.733 112.472 144.461 1.00 17.13 ?  184  LEU A O    1 
ATOM   842   C CB   . LEU A 1 184  ? 162.934 111.770 141.352 1.00 16.77 ?  184  LEU A CB   1 
ATOM   843   C CG   . LEU A 1 184  ? 163.293 113.256 141.301 1.00 18.14 ?  184  LEU A CG   1 
ATOM   844   C CD1  . LEU A 1 184  ? 164.741 113.449 140.876 1.00 17.02 ?  184  LEU A CD1  1 
ATOM   845   C CD2  . LEU A 1 184  ? 162.345 114.008 140.385 1.00 16.89 ?  184  LEU A CD2  1 
ATOM   846   N N    . ALA A 1 185  ? 161.622 111.723 144.223 1.00 17.57 ?  185  ALA A N    1 
ATOM   847   C CA   . ALA A 1 185  ? 161.147 112.402 145.421 1.00 17.03 ?  185  ALA A CA   1 
ATOM   848   C C    . ALA A 1 185  ? 161.722 111.813 146.702 1.00 17.17 ?  185  ALA A C    1 
ATOM   849   O O    . ALA A 1 185  ? 161.813 112.528 147.705 1.00 12.78 ?  185  ALA A O    1 
ATOM   850   C CB   . ALA A 1 185  ? 159.619 112.365 145.479 1.00 13.76 ?  185  ALA A CB   1 
ATOM   851   N N    . MET A 1 186  ? 162.113 110.538 146.695 1.00 19.75 ?  186  MET A N    1 
ATOM   852   C CA   . MET A 1 186  ? 162.824 109.971 147.839 1.00 17.38 ?  186  MET A CA   1 
ATOM   853   C C    . MET A 1 186  ? 164.254 110.489 147.940 1.00 22.03 ?  186  MET A C    1 
ATOM   854   O O    . MET A 1 186  ? 164.616 111.151 148.918 1.00 24.01 ?  186  MET A O    1 
ATOM   855   C CB   . MET A 1 186  ? 162.871 108.441 147.767 1.00 18.74 ?  186  MET A CB   1 
ATOM   856   C CG   . MET A 1 186  ? 161.628 107.704 148.189 1.00 20.17 ?  186  MET A CG   1 
ATOM   857   S SD   . MET A 1 186  ? 162.049 105.955 148.308 1.00 34.30 ?  186  MET A SD   1 
ATOM   858   C CE   . MET A 1 186  ? 160.431 105.218 148.401 1.00 20.82 ?  186  MET A CE   1 
ATOM   859   N N    . ASN A 1 187  ? 165.080 110.184 146.938 1.00 23.15 ?  187  ASN A N    1 
ATOM   860   C CA   . ASN A 1 187  ? 166.520 110.349 147.116 1.00 20.37 ?  187  ASN A CA   1 
ATOM   861   C C    . ASN A 1 187  ? 166.955 111.809 147.049 1.00 21.64 ?  187  ASN A C    1 
ATOM   862   O O    . ASN A 1 187  ? 167.841 112.225 147.803 1.00 22.01 ?  187  ASN A O    1 
ATOM   863   C CB   . ASN A 1 187  ? 167.274 109.514 146.083 1.00 17.47 ?  187  ASN A CB   1 
ATOM   864   C CG   . ASN A 1 187  ? 166.945 108.039 146.180 1.00 20.74 ?  187  ASN A CG   1 
ATOM   865   O OD1  . ASN A 1 187  ? 167.623 107.285 146.877 1.00 25.32 ?  187  ASN A OD1  1 
ATOM   866   N ND2  . ASN A 1 187  ? 165.895 107.620 145.488 1.00 19.29 ?  187  ASN A ND2  1 
ATOM   867   N N    . LEU A 1 188  ? 166.347 112.602 146.170 1.00 18.46 ?  188  LEU A N    1 
ATOM   868   C CA   . LEU A 1 188  ? 166.818 113.965 145.957 1.00 17.86 ?  188  LEU A CA   1 
ATOM   869   C C    . LEU A 1 188  ? 166.272 114.943 146.995 1.00 17.11 ?  188  LEU A C    1 
ATOM   870   O O    . LEU A 1 188  ? 167.034 115.726 147.570 1.00 18.98 ?  188  LEU A O    1 
ATOM   871   C CB   . LEU A 1 188  ? 166.448 114.432 144.548 1.00 20.09 ?  188  LEU A CB   1 
ATOM   872   C CG   . LEU A 1 188  ? 166.716 115.908 144.263 1.00 20.64 ?  188  LEU A CG   1 
ATOM   873   C CD1  . LEU A 1 188  ? 168.134 116.104 143.745 1.00 18.16 ?  188  LEU A CD1  1 
ATOM   874   C CD2  . LEU A 1 188  ? 165.696 116.456 143.283 1.00 20.87 ?  188  LEU A CD2  1 
ATOM   875   N N    . PHE A 1 189  ? 164.964 114.915 147.237 1.00 18.01 ?  189  PHE A N    1 
ATOM   876   C CA   . PHE A 1 189  ? 164.348 115.857 148.163 1.00 19.15 ?  189  PHE A CA   1 
ATOM   877   C C    . PHE A 1 189  ? 164.792 115.574 149.594 1.00 18.70 ?  189  PHE A C    1 
ATOM   878   O O    . PHE A 1 189  ? 165.015 114.422 149.976 1.00 21.61 ?  189  PHE A O    1 
ATOM   879   C CB   . PHE A 1 189  ? 162.822 115.783 148.067 1.00 16.93 ?  189  PHE A CB   1 
ATOM   880   C CG   . PHE A 1 189  ? 162.250 116.329 146.779 1.00 17.86 ?  189  PHE A CG   1 
ATOM   881   C CD1  . PHE A 1 189  ? 163.055 116.954 145.839 1.00 18.43 ?  189  PHE A CD1  1 
ATOM   882   C CD2  . PHE A 1 189  ? 160.896 116.209 146.513 1.00 19.55 ?  189  PHE A CD2  1 
ATOM   883   C CE1  . PHE A 1 189  ? 162.517 117.446 144.663 1.00 18.16 ?  189  PHE A CE1  1 
ATOM   884   C CE2  . PHE A 1 189  ? 160.355 116.701 145.340 1.00 15.75 ?  189  PHE A CE2  1 
ATOM   885   C CZ   . PHE A 1 189  ? 161.167 117.321 144.415 1.00 15.08 ?  189  PHE A CZ   1 
ATOM   886   N N    . ASN A 1 190  ? 164.923 116.636 150.389 1.00 15.68 ?  190  ASN A N    1 
ATOM   887   C CA   . ASN A 1 190  ? 165.372 116.499 151.768 1.00 16.28 ?  190  ASN A CA   1 
ATOM   888   C C    . ASN A 1 190  ? 164.241 116.210 152.744 1.00 18.80 ?  190  ASN A C    1 
ATOM   889   O O    . ASN A 1 190  ? 164.515 115.938 153.918 1.00 20.59 ?  190  ASN A O    1 
ATOM   890   C CB   . ASN A 1 190  ? 166.118 117.763 152.218 1.00 16.03 ?  190  ASN A CB   1 
ATOM   891   C CG   . ASN A 1 190  ? 165.323 119.032 151.979 1.00 20.64 ?  190  ASN A CG   1 
ATOM   892   O OD1  . ASN A 1 190  ? 164.226 118.999 151.422 1.00 23.13 ?  190  ASN A OD1  1 
ATOM   893   N ND2  . ASN A 1 190  ? 165.875 120.162 152.406 1.00 21.24 ?  190  ASN A ND2  1 
ATOM   894   N N    . TYR A 1 191  ? 162.987 116.265 152.300 1.00 16.89 ?  191  TYR A N    1 
ATOM   895   C CA   . TYR A 1 191  ? 161.873 115.948 153.181 1.00 17.32 ?  191  TYR A CA   1 
ATOM   896   C C    . TYR A 1 191  ? 161.845 114.456 153.490 1.00 18.49 ?  191  TYR A C    1 
ATOM   897   O O    . TYR A 1 191  ? 162.085 113.619 152.615 1.00 19.18 ?  191  TYR A O    1 
ATOM   898   C CB   . TYR A 1 191  ? 160.546 116.372 152.551 1.00 15.27 ?  191  TYR A CB   1 
ATOM   899   C CG   . TYR A 1 191  ? 160.634 117.559 151.617 1.00 15.29 ?  191  TYR A CG   1 
ATOM   900   C CD1  . TYR A 1 191  ? 160.838 118.841 152.108 1.00 14.77 ?  191  TYR A CD1  1 
ATOM   901   C CD2  . TYR A 1 191  ? 160.490 117.398 150.246 1.00 14.72 ?  191  TYR A CD2  1 
ATOM   902   C CE1  . TYR A 1 191  ? 160.910 119.929 151.256 1.00 14.88 ?  191  TYR A CE1  1 
ATOM   903   C CE2  . TYR A 1 191  ? 160.561 118.478 149.388 1.00 12.73 ?  191  TYR A CE2  1 
ATOM   904   C CZ   . TYR A 1 191  ? 160.770 119.740 149.897 1.00 13.88 ?  191  TYR A CZ   1 
ATOM   905   O OH   . TYR A 1 191  ? 160.840 120.816 149.043 1.00 18.75 ?  191  TYR A OH   1 
ATOM   906   N N    . ASN A 1 192  ? 161.551 114.125 154.745 1.00 17.50 ?  192  ASN A N    1 
ATOM   907   C CA   . ASN A 1 192  ? 161.440 112.730 155.171 1.00 18.16 ?  192  ASN A CA   1 
ATOM   908   C C    . ASN A 1 192  ? 160.111 112.190 154.660 1.00 21.01 ?  192  ASN A C    1 
ATOM   909   O O    . ASN A 1 192  ? 159.093 112.218 155.353 1.00 25.61 ?  192  ASN A O    1 
ATOM   910   C CB   . ASN A 1 192  ? 161.550 112.615 156.686 1.00 22.14 ?  192  ASN A CB   1 
ATOM   911   C CG   . ASN A 1 192  ? 162.748 113.359 157.243 1.00 26.18 ?  192  ASN A CG   1 
ATOM   912   O OD1  . ASN A 1 192  ? 163.591 113.851 156.495 1.00 22.58 ?  192  ASN A OD1  1 
ATOM   913   N ND2  . ASN A 1 192  ? 162.825 113.447 158.566 1.00 25.25 ?  192  ASN A ND2  1 
ATOM   914   N N    . TRP A 1 193  ? 160.123 111.689 153.428 1.00 13.60 ?  193  TRP A N    1 
ATOM   915   C CA   . TRP A 1 193  ? 158.922 111.212 152.757 1.00 9.27  ?  193  TRP A CA   1 
ATOM   916   C C    . TRP A 1 193  ? 158.962 109.695 152.640 1.00 14.75 ?  193  TRP A C    1 
ATOM   917   O O    . TRP A 1 193  ? 159.992 109.122 152.268 1.00 18.67 ?  193  TRP A O    1 
ATOM   918   C CB   . TRP A 1 193  ? 158.784 111.845 151.371 1.00 8.90  ?  193  TRP A CB   1 
ATOM   919   C CG   . TRP A 1 193  ? 158.122 113.188 151.391 1.00 13.63 ?  193  TRP A CG   1 
ATOM   920   C CD1  . TRP A 1 193  ? 157.747 113.900 152.492 1.00 12.45 ?  193  TRP A CD1  1 
ATOM   921   C CD2  . TRP A 1 193  ? 157.752 113.979 150.257 1.00 10.33 ?  193  TRP A CD2  1 
ATOM   922   N NE1  . TRP A 1 193  ? 157.169 115.086 152.114 1.00 10.65 ?  193  TRP A NE1  1 
ATOM   923   C CE2  . TRP A 1 193  ? 157.159 115.159 150.746 1.00 11.19 ?  193  TRP A CE2  1 
ATOM   924   C CE3  . TRP A 1 193  ? 157.865 113.805 148.875 1.00 10.01 ?  193  TRP A CE3  1 
ATOM   925   C CZ2  . TRP A 1 193  ? 156.681 116.159 149.904 1.00 14.18 ?  193  TRP A CZ2  1 
ATOM   926   C CZ3  . TRP A 1 193  ? 157.391 114.799 148.042 1.00 5.94  ?  193  TRP A CZ3  1 
ATOM   927   C CH2  . TRP A 1 193  ? 156.806 115.960 148.558 1.00 10.47 ?  193  TRP A CH2  1 
ATOM   928   N N    . ASN A 1 194  ? 157.840 109.052 152.956 1.00 16.65 ?  194  ASN A N    1 
ATOM   929   C CA   . ASN A 1 194  ? 157.712 107.606 152.869 1.00 10.46 ?  194  ASN A CA   1 
ATOM   930   C C    . ASN A 1 194  ? 157.487 107.190 151.414 1.00 14.57 ?  194  ASN A C    1 
ATOM   931   O O    . ASN A 1 194  ? 157.460 108.017 150.500 1.00 20.30 ?  194  ASN A O    1 
ATOM   932   C CB   . ASN A 1 194  ? 156.574 107.132 153.772 1.00 13.07 ?  194  ASN A CB   1 
ATOM   933   C CG   . ASN A 1 194  ? 156.772 105.716 154.272 1.00 24.42 ?  194  ASN A CG   1 
ATOM   934   O OD1  . ASN A 1 194  ? 157.896 105.220 154.339 1.00 25.90 ?  194  ASN A OD1  1 
ATOM   935   N ND2  . ASN A 1 194  ? 155.675 105.058 154.631 1.00 20.29 ?  194  ASN A ND2  1 
ATOM   936   N N    . PHE A 1 195  ? 157.326 105.882 151.190 1.00 20.17 ?  195  PHE A N    1 
ATOM   937   C CA   . PHE A 1 195  ? 157.025 105.398 149.845 1.00 18.06 ?  195  PHE A CA   1 
ATOM   938   C C    . PHE A 1 195  ? 155.615 105.767 149.409 1.00 16.47 ?  195  PHE A C    1 
ATOM   939   O O    . PHE A 1 195  ? 155.392 106.050 148.228 1.00 17.69 ?  195  PHE A O    1 
ATOM   940   C CB   . PHE A 1 195  ? 157.218 103.883 149.770 1.00 16.74 ?  195  PHE A CB   1 
ATOM   941   C CG   . PHE A 1 195  ? 156.865 103.285 148.430 1.00 17.31 ?  195  PHE A CG   1 
ATOM   942   C CD1  . PHE A 1 195  ? 157.556 103.636 147.281 1.00 11.20 ?  195  PHE A CD1  1 
ATOM   943   C CD2  . PHE A 1 195  ? 155.841 102.358 148.328 1.00 19.79 ?  195  PHE A CD2  1 
ATOM   944   C CE1  . PHE A 1 195  ? 157.229 103.080 146.058 1.00 13.56 ?  195  PHE A CE1  1 
ATOM   945   C CE2  . PHE A 1 195  ? 155.508 101.798 147.109 1.00 18.28 ?  195  PHE A CE2  1 
ATOM   946   C CZ   . PHE A 1 195  ? 156.204 102.158 145.973 1.00 16.43 ?  195  PHE A CZ   1 
ATOM   947   N N    . SER A 1 196  ? 154.656 105.773 150.336 1.00 14.48 ?  196  SER A N    1 
ATOM   948   C CA   . SER A 1 196  ? 153.278 106.083 149.968 1.00 10.72 ?  196  SER A CA   1 
ATOM   949   C C    . SER A 1 196  ? 153.120 107.552 149.594 1.00 15.13 ?  196  SER A C    1 
ATOM   950   O O    . SER A 1 196  ? 152.463 107.879 148.596 1.00 16.99 ?  196  SER A O    1 
ATOM   951   C CB   . SER A 1 196  ? 152.342 105.713 151.116 1.00 11.35 ?  196  SER A CB   1 
ATOM   952   O OG   . SER A 1 196  ? 152.915 106.057 152.365 1.00 15.11 ?  196  SER A OG   1 
ATOM   953   N N    . GLU A 1 197  ? 153.726 108.449 150.376 1.00 15.59 ?  197  GLU A N    1 
ATOM   954   C CA   . GLU A 1 197  ? 153.671 109.874 150.067 1.00 13.67 ?  197  GLU A CA   1 
ATOM   955   C C    . GLU A 1 197  ? 154.374 110.179 148.749 1.00 14.11 ?  197  GLU A C    1 
ATOM   956   O O    . GLU A 1 197  ? 153.872 110.964 147.934 1.00 17.82 ?  197  GLU A O    1 
ATOM   957   C CB   . GLU A 1 197  ? 154.290 110.670 151.215 1.00 9.01  ?  197  GLU A CB   1 
ATOM   958   C CG   . GLU A 1 197  ? 154.101 110.006 152.574 1.00 15.01 ?  197  GLU A CG   1 
ATOM   959   C CD   . GLU A 1 197  ? 154.677 110.814 153.719 1.00 17.99 ?  197  GLU A CD   1 
ATOM   960   O OE1  . GLU A 1 197  ? 154.125 111.888 154.026 1.00 15.33 ?  197  GLU A OE1  1 
ATOM   961   O OE2  . GLU A 1 197  ? 155.678 110.368 154.318 1.00 19.22 ?  197  GLU A OE2  1 
ATOM   962   N N    . ALA A 1 198  ? 155.523 109.542 148.509 1.00 7.16  ?  198  ALA A N    1 
ATOM   963   C CA   . ALA A 1 198  ? 156.246 109.746 147.257 1.00 7.15  ?  198  ALA A CA   1 
ATOM   964   C C    . ALA A 1 198  ? 155.477 109.183 146.066 1.00 13.07 ?  198  ALA A C    1 
ATOM   965   O O    . ALA A 1 198  ? 155.505 109.762 144.974 1.00 21.85 ?  198  ALA A O    1 
ATOM   966   C CB   . ALA A 1 198  ? 157.633 109.114 147.345 1.00 15.30 ?  198  ALA A CB   1 
ATOM   967   N N    . MET A 1 199  ? 154.791 108.053 146.249 1.00 8.56  ?  199  MET A N    1 
ATOM   968   C CA   . MET A 1 199  ? 154.020 107.481 145.150 1.00 6.07  ?  199  MET A CA   1 
ATOM   969   C C    . MET A 1 199  ? 152.796 108.329 144.836 1.00 6.88  ?  199  MET A C    1 
ATOM   970   O O    . MET A 1 199  ? 152.411 108.463 143.670 1.00 14.70 ?  199  MET A O    1 
ATOM   971   C CB   . MET A 1 199  ? 153.613 106.047 145.479 1.00 10.75 ?  199  MET A CB   1 
ATOM   972   C CG   . MET A 1 199  ? 154.436 104.997 144.756 1.00 12.35 ?  199  MET A CG   1 
ATOM   973   S SD   . MET A 1 199  ? 154.577 105.306 142.986 1.00 18.82 ?  199  MET A SD   1 
ATOM   974   C CE   . MET A 1 199  ? 152.876 105.103 142.468 1.00 9.14  ?  199  MET A CE   1 
ATOM   975   N N    . MET A 1 200  ? 152.172 108.911 145.862 1.00 1.77  ?  200  MET A N    1 
ATOM   976   C CA   . MET A 1 200  ? 151.077 109.849 145.629 1.00 2.21  ?  200  MET A CA   1 
ATOM   977   C C    . MET A 1 200  ? 151.577 111.114 144.932 1.00 8.96  ?  200  MET A C    1 
ATOM   978   O O    . MET A 1 200  ? 150.900 111.653 144.047 1.00 12.90 ?  200  MET A O    1 
ATOM   979   C CB   . MET A 1 200  ? 150.382 110.150 146.960 1.00 3.66  ?  200  MET A CB   1 
ATOM   980   C CG   . MET A 1 200  ? 149.570 111.425 147.026 1.00 7.89  ?  200  MET A CG   1 
ATOM   981   S SD   . MET A 1 200  ? 148.841 111.649 148.665 1.00 12.92 ?  200  MET A SD   1 
ATOM   982   C CE   . MET A 1 200  ? 150.253 112.174 149.630 1.00 9.73  ?  200  MET A CE   1 
ATOM   983   N N    . PHE A 1 201  ? 152.779 111.573 145.296 1.00 5.48  ?  201  PHE A N    1 
ATOM   984   C CA   . PHE A 1 201  ? 153.445 112.668 144.590 1.00 1.01  ?  201  PHE A CA   1 
ATOM   985   C C    . PHE A 1 201  ? 153.629 112.346 143.107 1.00 1.96  ?  201  PHE A C    1 
ATOM   986   O O    . PHE A 1 201  ? 153.293 113.155 142.229 1.00 8.41  ?  201  PHE A O    1 
ATOM   987   C CB   . PHE A 1 201  ? 154.793 112.924 145.269 1.00 5.69  ?  201  PHE A CB   1 
ATOM   988   C CG   . PHE A 1 201  ? 155.541 114.122 144.761 1.00 11.12 ?  201  PHE A CG   1 
ATOM   989   C CD1  . PHE A 1 201  ? 155.341 115.368 145.328 1.00 8.89  ?  201  PHE A CD1  1 
ATOM   990   C CD2  . PHE A 1 201  ? 156.488 113.992 143.758 1.00 8.24  ?  201  PHE A CD2  1 
ATOM   991   C CE1  . PHE A 1 201  ? 156.046 116.468 144.887 1.00 2.45  ?  201  PHE A CE1  1 
ATOM   992   C CE2  . PHE A 1 201  ? 157.193 115.091 143.306 1.00 8.33  ?  201  PHE A CE2  1 
ATOM   993   C CZ   . PHE A 1 201  ? 156.973 116.329 143.873 1.00 9.77  ?  201  PHE A CZ   1 
ATOM   994   N N    . GLY A 1 202  ? 154.159 111.157 142.813 1.00 0.00  ?  202  GLY A N    1 
ATOM   995   C CA   . GLY A 1 202  ? 154.379 110.768 141.429 1.00 0.00  ?  202  GLY A CA   1 
ATOM   996   C C    . GLY A 1 202  ? 153.091 110.591 140.647 1.00 0.00  ?  202  GLY A C    1 
ATOM   997   O O    . GLY A 1 202  ? 153.023 110.929 139.462 1.00 10.26 ?  202  GLY A O    1 
ATOM   998   N N    . ALA A 1 203  ? 152.053 110.052 141.294 1.00 0.84  ?  203  ALA A N    1 
ATOM   999   C CA   . ALA A 1 203  ? 150.757 109.922 140.639 1.00 0.00  ?  203  ALA A CA   1 
ATOM   1000  C C    . ALA A 1 203  ? 150.135 111.281 140.357 1.00 1.78  ?  203  ALA A C    1 
ATOM   1001  O O    . ALA A 1 203  ? 149.422 111.439 139.360 1.00 3.76  ?  203  ALA A O    1 
ATOM   1002  C CB   . ALA A 1 203  ? 149.815 109.078 141.495 1.00 0.46  ?  203  ALA A CB   1 
ATOM   1003  N N    . ILE A 1 204  ? 150.378 112.262 141.228 1.00 7.04  ?  204  ILE A N    1 
ATOM   1004  C CA   . ILE A 1 204  ? 149.930 113.624 140.957 1.00 2.54  ?  204  ILE A CA   1 
ATOM   1005  C C    . ILE A 1 204  ? 150.655 114.188 139.741 1.00 2.78  ?  204  ILE A C    1 
ATOM   1006  O O    . ILE A 1 204  ? 150.035 114.757 138.835 1.00 4.79  ?  204  ILE A O    1 
ATOM   1007  C CB   . ILE A 1 204  ? 150.131 114.506 142.204 1.00 1.97  ?  204  ILE A CB   1 
ATOM   1008  C CG1  . ILE A 1 204  ? 148.933 114.376 143.142 1.00 3.18  ?  204  ILE A CG1  1 
ATOM   1009  C CG2  . ILE A 1 204  ? 150.339 115.965 141.825 1.00 2.19  ?  204  ILE A CG2  1 
ATOM   1010  C CD1  . ILE A 1 204  ? 149.056 115.203 144.395 1.00 5.42  ?  204  ILE A CD1  1 
ATOM   1011  N N    . MET A 1 205  ? 151.975 114.011 139.686 1.00 9.00  ?  205  MET A N    1 
ATOM   1012  C CA   . MET A 1 205  ? 152.778 114.613 138.628 1.00 6.95  ?  205  MET A CA   1 
ATOM   1013  C C    . MET A 1 205  ? 153.007 113.692 137.432 1.00 6.26  ?  205  MET A C    1 
ATOM   1014  O O    . MET A 1 205  ? 153.932 113.933 136.649 1.00 8.12  ?  205  MET A O    1 
ATOM   1015  C CB   . MET A 1 205  ? 154.110 115.100 139.194 1.00 0.93  ?  205  MET A CB   1 
ATOM   1016  C CG   . MET A 1 205  ? 154.126 116.599 139.406 1.00 5.85  ?  205  MET A CG   1 
ATOM   1017  S SD   . MET A 1 205  ? 155.197 117.130 140.741 1.00 28.37 ?  205  MET A SD   1 
ATOM   1018  C CE   . MET A 1 205  ? 154.024 117.052 142.090 1.00 11.50 ?  205  MET A CE   1 
ATOM   1019  N N    . SER A 1 206  ? 152.190 112.653 137.268 1.00 11.11 ?  206  SER A N    1 
ATOM   1020  C CA   . SER A 1 206  ? 152.239 111.808 136.081 1.00 9.86  ?  206  SER A CA   1 
ATOM   1021  C C    . SER A 1 206  ? 150.983 111.929 135.223 1.00 11.13 ?  206  SER A C    1 
ATOM   1022  O O    . SER A 1 206  ? 150.741 111.074 134.367 1.00 10.19 ?  206  SER A O    1 
ATOM   1023  C CB   . SER A 1 206  ? 152.467 110.349 136.476 1.00 7.25  ?  206  SER A CB   1 
ATOM   1024  O OG   . SER A 1 206  ? 153.848 110.034 136.475 1.00 11.68 ?  206  SER A OG   1 
ATOM   1025  N N    . ALA A 1 207  ? 150.182 112.971 135.430 1.00 11.05 ?  207  ALA A N    1 
ATOM   1026  C CA   . ALA A 1 207  ? 148.955 113.195 134.674 1.00 8.02  ?  207  ALA A CA   1 
ATOM   1027  C C    . ALA A 1 207  ? 149.169 114.372 133.730 1.00 14.87 ?  207  ALA A C    1 
ATOM   1028  O O    . ALA A 1 207  ? 149.474 115.482 134.178 1.00 20.86 ?  207  ALA A O    1 
ATOM   1029  C CB   . ALA A 1 207  ? 147.775 113.456 135.609 1.00 3.88  ?  207  ALA A CB   1 
ATOM   1030  N N    . THR A 1 208  ? 148.999 114.130 132.432 1.00 14.57 ?  208  THR A N    1 
ATOM   1031  C CA   . THR A 1 208  ? 149.339 115.084 131.385 1.00 10.19 ?  208  THR A CA   1 
ATOM   1032  C C    . THR A 1 208  ? 148.077 115.603 130.695 1.00 13.26 ?  208  THR A C    1 
ATOM   1033  O O    . THR A 1 208  ? 146.949 115.281 131.076 1.00 17.73 ?  208  THR A O    1 
ATOM   1034  C CB   . THR A 1 208  ? 150.285 114.448 130.363 1.00 12.78 ?  208  THR A CB   1 
ATOM   1035  O OG1  . THR A 1 208  ? 149.519 113.798 129.342 1.00 15.33 ?  208  THR A OG1  1 
ATOM   1036  C CG2  . THR A 1 208  ? 151.192 113.424 131.030 1.00 15.98 ?  208  THR A CG2  1 
ATOM   1037  N N    . ASP A 1 209  ? 148.289 116.390 129.638 1.00 13.38 ?  209  ASP A N    1 
ATOM   1038  C CA   . ASP A 1 209  ? 147.180 116.942 128.863 1.00 10.49 ?  209  ASP A CA   1 
ATOM   1039  C C    . ASP A 1 209  ? 147.681 117.112 127.433 1.00 14.72 ?  209  ASP A C    1 
ATOM   1040  O O    . ASP A 1 209  ? 148.661 117.823 127.211 1.00 16.68 ?  209  ASP A O    1 
ATOM   1041  C CB   . ASP A 1 209  ? 146.726 118.274 129.447 1.00 11.93 ?  209  ASP A CB   1 
ATOM   1042  C CG   . ASP A 1 209  ? 145.422 118.760 128.850 1.00 16.80 ?  209  ASP A CG   1 
ATOM   1043  O OD1  . ASP A 1 209  ? 144.798 118.006 128.076 1.00 18.52 ?  209  ASP A OD1  1 
ATOM   1044  O OD2  . ASP A 1 209  ? 145.014 119.898 129.163 1.00 16.54 ?  209  ASP A OD2  1 
ATOM   1045  N N    . PRO A 1 210  ? 147.026 116.471 126.451 1.00 16.65 ?  210  PRO A N    1 
ATOM   1046  C CA   . PRO A 1 210  ? 147.494 116.498 125.060 1.00 14.57 ?  210  PRO A CA   1 
ATOM   1047  C C    . PRO A 1 210  ? 146.858 117.586 124.210 1.00 15.19 ?  210  PRO A C    1 
ATOM   1048  O O    . PRO A 1 210  ? 146.952 117.520 122.980 1.00 15.91 ?  210  PRO A O    1 
ATOM   1049  C CB   . PRO A 1 210  ? 147.093 115.113 124.552 1.00 13.08 ?  210  PRO A CB   1 
ATOM   1050  C CG   . PRO A 1 210  ? 145.782 114.875 125.249 1.00 17.62 ?  210  PRO A CG   1 
ATOM   1051  C CD   . PRO A 1 210  ? 145.854 115.591 126.599 1.00 15.42 ?  210  PRO A CD   1 
ATOM   1052  N N    . VAL A 1 211  ? 146.196 118.562 124.840 1.00 19.77 ?  211  VAL A N    1 
ATOM   1053  C CA   . VAL A 1 211  ? 145.336 119.495 124.107 1.00 19.02 ?  211  VAL A CA   1 
ATOM   1054  C C    . VAL A 1 211  ? 146.133 120.294 123.078 1.00 20.15 ?  211  VAL A C    1 
ATOM   1055  O O    . VAL A 1 211  ? 145.706 120.443 121.924 1.00 20.33 ?  211  VAL A O    1 
ATOM   1056  C CB   . VAL A 1 211  ? 144.579 120.407 125.092 1.00 17.06 ?  211  VAL A CB   1 
ATOM   1057  C CG1  . VAL A 1 211  ? 143.465 119.629 125.769 1.00 13.01 ?  211  VAL A CG1  1 
ATOM   1058  C CG2  . VAL A 1 211  ? 145.519 120.964 126.152 1.00 16.43 ?  211  VAL A CG2  1 
ATOM   1059  N N    . ALA A 1 212  ? 147.310 120.794 123.463 1.00 20.00 ?  212  ALA A N    1 
ATOM   1060  C CA   . ALA A 1 212  ? 148.152 121.517 122.516 1.00 16.90 ?  212  ALA A CA   1 
ATOM   1061  C C    . ALA A 1 212  ? 148.643 120.604 121.399 1.00 16.99 ?  212  ALA A C    1 
ATOM   1062  O O    . ALA A 1 212  ? 148.649 120.999 120.228 1.00 19.04 ?  212  ALA A O    1 
ATOM   1063  C CB   . ALA A 1 212  ? 149.332 122.158 123.244 1.00 17.16 ?  212  ALA A CB   1 
ATOM   1064  N N    . VAL A 1 213  ? 149.047 119.378 121.741 1.00 15.04 ?  213  VAL A N    1 
ATOM   1065  C CA   . VAL A 1 213  ? 149.585 118.458 120.743 1.00 12.98 ?  213  VAL A CA   1 
ATOM   1066  C C    . VAL A 1 213  ? 148.511 118.070 119.733 1.00 17.03 ?  213  VAL A C    1 
ATOM   1067  O O    . VAL A 1 213  ? 148.744 118.094 118.520 1.00 19.21 ?  213  VAL A O    1 
ATOM   1068  C CB   . VAL A 1 213  ? 150.194 117.220 121.427 1.00 15.70 ?  213  VAL A CB   1 
ATOM   1069  C CG1  . VAL A 1 213  ? 150.312 116.061 120.447 1.00 17.65 ?  213  VAL A CG1  1 
ATOM   1070  C CG2  . VAL A 1 213  ? 151.550 117.559 122.010 1.00 17.82 ?  213  VAL A CG2  1 
ATOM   1071  N N    . VAL A 1 214  ? 147.314 117.722 120.213 1.00 19.54 ?  214  VAL A N    1 
ATOM   1072  C CA   . VAL A 1 214  ? 146.253 117.327 119.290 1.00 19.41 ?  214  VAL A CA   1 
ATOM   1073  C C    . VAL A 1 214  ? 145.771 118.524 118.472 1.00 17.09 ?  214  VAL A C    1 
ATOM   1074  O O    . VAL A 1 214  ? 145.443 118.379 117.285 1.00 17.87 ?  214  VAL A O    1 
ATOM   1075  C CB   . VAL A 1 214  ? 145.105 116.620 120.046 1.00 19.38 ?  214  VAL A CB   1 
ATOM   1076  C CG1  . VAL A 1 214  ? 144.364 117.567 120.984 1.00 18.29 ?  214  VAL A CG1  1 
ATOM   1077  C CG2  . VAL A 1 214  ? 144.142 115.964 119.066 1.00 18.46 ?  214  VAL A CG2  1 
ATOM   1078  N N    . ALA A 1 215  ? 145.751 119.725 119.066 1.00 17.73 ?  215  ALA A N    1 
ATOM   1079  C CA   . ALA A 1 215  ? 145.342 120.911 118.319 1.00 24.50 ?  215  ALA A CA   1 
ATOM   1080  C C    . ALA A 1 215  ? 146.340 121.248 117.217 1.00 23.37 ?  215  ALA A C    1 
ATOM   1081  O O    . ALA A 1 215  ? 145.942 121.609 116.103 1.00 17.88 ?  215  ALA A O    1 
ATOM   1082  C CB   . ALA A 1 215  ? 145.169 122.095 119.269 1.00 20.65 ?  215  ALA A CB   1 
ATOM   1083  N N    . LEU A 1 216  ? 147.637 121.134 117.504 1.00 24.37 ?  216  LEU A N    1 
ATOM   1084  C CA   . LEU A 1 216  ? 148.661 121.435 116.512 1.00 22.05 ?  216  LEU A CA   1 
ATOM   1085  C C    . LEU A 1 216  ? 148.918 120.283 115.551 1.00 20.04 ?  216  LEU A C    1 
ATOM   1086  O O    . LEU A 1 216  ? 149.598 120.484 114.540 1.00 21.52 ?  216  LEU A O    1 
ATOM   1087  C CB   . LEU A 1 216  ? 149.964 121.826 117.213 1.00 21.33 ?  216  LEU A CB   1 
ATOM   1088  C CG   . LEU A 1 216  ? 149.918 123.092 118.073 1.00 24.19 ?  216  LEU A CG   1 
ATOM   1089  C CD1  . LEU A 1 216  ? 151.320 123.565 118.397 1.00 22.07 ?  216  LEU A CD1  1 
ATOM   1090  C CD2  . LEU A 1 216  ? 149.127 124.197 117.386 1.00 21.45 ?  216  LEU A CD2  1 
ATOM   1091  N N    . LEU A 1 217  ? 148.405 119.088 115.841 1.00 17.17 ?  217  LEU A N    1 
ATOM   1092  C CA   . LEU A 1 217  ? 148.516 117.971 114.915 1.00 18.16 ?  217  LEU A CA   1 
ATOM   1093  C C    . LEU A 1 217  ? 147.295 117.819 114.022 1.00 20.83 ?  217  LEU A C    1 
ATOM   1094  O O    . LEU A 1 217  ? 147.399 117.194 112.960 1.00 23.22 ?  217  LEU A O    1 
ATOM   1095  C CB   . LEU A 1 217  ? 148.743 116.666 115.685 1.00 21.19 ?  217  LEU A CB   1 
ATOM   1096  C CG   . LEU A 1 217  ? 150.130 116.035 115.562 1.00 21.60 ?  217  LEU A CG   1 
ATOM   1097  C CD1  . LEU A 1 217  ? 151.186 116.957 116.145 1.00 18.99 ?  217  LEU A CD1  1 
ATOM   1098  C CD2  . LEU A 1 217  ? 150.165 114.678 116.246 1.00 20.15 ?  217  LEU A CD2  1 
ATOM   1099  N N    . LYS A 1 218  ? 146.143 118.360 114.428 1.00 19.72 ?  218  LYS A N    1 
ATOM   1100  C CA   . LYS A 1 218  ? 144.960 118.297 113.575 1.00 18.48 ?  218  LYS A CA   1 
ATOM   1101  C C    . LYS A 1 218  ? 145.135 119.144 112.319 1.00 22.84 ?  218  LYS A C    1 
ATOM   1102  O O    . LYS A 1 218  ? 144.904 118.668 111.201 1.00 21.15 ?  218  LYS A O    1 
ATOM   1103  C CB   . LYS A 1 218  ? 143.725 118.746 114.357 1.00 18.34 ?  218  LYS A CB   1 
ATOM   1104  C CG   . LYS A 1 218  ? 142.706 117.645 114.590 1.00 24.98 ?  218  LYS A CG   1 
ATOM   1105  C CD   . LYS A 1 218  ? 141.363 118.218 115.007 1.00 26.02 ?  218  LYS A CD   1 
ATOM   1106  C CE   . LYS A 1 218  ? 140.234 117.246 114.712 1.00 21.13 ?  218  LYS A CE   1 
ATOM   1107  N NZ   . LYS A 1 218  ? 138.921 117.939 114.599 1.00 18.62 ?  218  LYS A NZ   1 
ATOM   1108  N N    . ASP A 1 219  ? 145.543 120.404 112.481 1.00 27.86 ?  219  ASP A N    1 
ATOM   1109  C CA   . ASP A 1 219  ? 145.656 121.300 111.335 1.00 26.14 ?  219  ASP A CA   1 
ATOM   1110  C C    . ASP A 1 219  ? 146.914 121.041 110.515 1.00 25.24 ?  219  ASP A C    1 
ATOM   1111  O O    . ASP A 1 219  ? 146.929 121.322 109.311 1.00 27.78 ?  219  ASP A O    1 
ATOM   1112  C CB   . ASP A 1 219  ? 145.614 122.759 111.798 1.00 27.39 ?  219  ASP A CB   1 
ATOM   1113  C CG   . ASP A 1 219  ? 146.922 123.218 112.412 1.00 28.74 ?  219  ASP A CG   1 
ATOM   1114  O OD1  . ASP A 1 219  ? 147.516 122.453 113.200 1.00 27.77 ?  219  ASP A OD1  1 
ATOM   1115  O OD2  . ASP A 1 219  ? 147.358 124.347 112.102 1.00 30.37 ?  219  ASP A OD2  1 
ATOM   1116  N N    . LEU A 1 220  ? 147.974 120.519 111.139 1.00 19.86 ?  220  LEU A N    1 
ATOM   1117  C CA   . LEU A 1 220  ? 149.208 120.255 110.406 1.00 22.59 ?  220  LEU A CA   1 
ATOM   1118  C C    . LEU A 1 220  ? 149.041 119.103 109.424 1.00 21.50 ?  220  LEU A C    1 
ATOM   1119  O O    . LEU A 1 220  ? 149.741 119.051 108.405 1.00 19.78 ?  220  LEU A O    1 
ATOM   1120  C CB   . LEU A 1 220  ? 150.347 119.964 111.384 1.00 26.25 ?  220  LEU A CB   1 
ATOM   1121  C CG   . LEU A 1 220  ? 151.765 119.873 110.816 1.00 26.61 ?  220  LEU A CG   1 
ATOM   1122  C CD1  . LEU A 1 220  ? 152.207 121.215 110.252 1.00 22.18 ?  220  LEU A CD1  1 
ATOM   1123  C CD2  . LEU A 1 220  ? 152.739 119.384 111.875 1.00 25.84 ?  220  LEU A CD2  1 
ATOM   1124  N N    . GLY A 1 221  ? 148.120 118.185 109.700 1.00 18.19 ?  221  GLY A N    1 
ATOM   1125  C CA   . GLY A 1 221  ? 147.897 117.065 108.810 1.00 18.55 ?  221  GLY A CA   1 
ATOM   1126  C C    . GLY A 1 221  ? 148.923 115.963 108.911 1.00 21.87 ?  221  GLY A C    1 
ATOM   1127  O O    . GLY A 1 221  ? 149.169 115.265 107.922 1.00 20.88 ?  221  GLY A O    1 
ATOM   1128  N N    . ALA A 1 222  ? 149.550 115.798 110.079 1.00 23.22 ?  222  ALA A N    1 
ATOM   1129  C CA   . ALA A 1 222  ? 150.499 114.704 110.263 1.00 22.63 ?  222  ALA A CA   1 
ATOM   1130  C C    . ALA A 1 222  ? 149.802 113.353 110.165 1.00 23.28 ?  222  ALA A C    1 
ATOM   1131  O O    . ALA A 1 222  ? 150.215 112.484 109.388 1.00 22.56 ?  222  ALA A O    1 
ATOM   1132  C CB   . ALA A 1 222  ? 151.211 114.849 111.609 1.00 21.85 ?  222  ALA A CB   1 
ATOM   1133  N N    . SER A 1 223  ? 148.728 113.170 110.933 1.00 22.93 ?  223  SER A N    1 
ATOM   1134  C CA   . SER A 1 223  ? 147.932 111.951 110.905 1.00 21.92 ?  223  SER A CA   1 
ATOM   1135  C C    . SER A 1 223  ? 146.628 112.198 111.644 1.00 20.42 ?  223  SER A C    1 
ATOM   1136  O O    . SER A 1 223  ? 146.622 112.834 112.701 1.00 22.33 ?  223  SER A O    1 
ATOM   1137  C CB   . SER A 1 223  ? 148.677 110.772 111.546 1.00 19.47 ?  223  SER A CB   1 
ATOM   1138  O OG   . SER A 1 223  ? 147.842 109.630 111.631 1.00 23.89 ?  223  SER A OG   1 
ATOM   1139  N N    . LYS A 1 224  ? 145.531 111.696 111.083 1.00 20.90 ?  224  LYS A N    1 
ATOM   1140  C CA   . LYS A 1 224  ? 144.257 111.675 111.786 1.00 18.62 ?  224  LYS A CA   1 
ATOM   1141  C C    . LYS A 1 224  ? 144.101 110.441 112.663 1.00 18.32 ?  224  LYS A C    1 
ATOM   1142  O O    . LYS A 1 224  ? 143.148 110.369 113.445 1.00 22.40 ?  224  LYS A O    1 
ATOM   1143  C CB   . LYS A 1 224  ? 143.090 111.748 110.792 1.00 20.77 ?  224  LYS A CB   1 
ATOM   1144  C CG   . LYS A 1 224  ? 142.808 113.145 110.250 1.00 19.81 ?  224  LYS A CG   1 
ATOM   1145  C CD   . LYS A 1 224  ? 143.680 113.473 109.047 1.00 23.57 ?  224  LYS A CD   1 
ATOM   1146  C CE   . LYS A 1 224  ? 143.594 114.945 108.685 1.00 23.14 ?  224  LYS A CE   1 
ATOM   1147  N NZ   . LYS A 1 224  ? 144.534 115.295 107.584 1.00 19.11 ?  224  LYS A NZ   1 
ATOM   1148  N N    . GLN A 1 225  ? 145.013 109.478 112.549 1.00 21.15 ?  225  GLN A N    1 
ATOM   1149  C CA   . GLN A 1 225  ? 145.031 108.295 113.394 1.00 21.77 ?  225  GLN A CA   1 
ATOM   1150  C C    . GLN A 1 225  ? 146.045 108.394 114.525 1.00 23.51 ?  225  GLN A C    1 
ATOM   1151  O O    . GLN A 1 225  ? 146.211 107.427 115.274 1.00 26.70 ?  225  GLN A O    1 
ATOM   1152  C CB   . GLN A 1 225  ? 145.319 107.049 112.551 1.00 21.16 ?  225  GLN A CB   1 
ATOM   1153  C CG   . GLN A 1 225  ? 144.373 106.858 111.378 1.00 22.67 ?  225  GLN A CG   1 
ATOM   1154  C CD   . GLN A 1 225  ? 143.139 106.059 111.751 1.00 24.68 ?  225  GLN A CD   1 
ATOM   1155  O OE1  . GLN A 1 225  ? 143.012 105.585 112.880 1.00 26.48 ?  225  GLN A OE1  1 
ATOM   1156  N NE2  . GLN A 1 225  ? 142.222 105.906 110.803 1.00 21.23 ?  225  GLN A NE2  1 
ATOM   1157  N N    . LEU A 1 226  ? 146.730 109.528 114.664 1.00 14.22 ?  226  LEU A N    1 
ATOM   1158  C CA   . LEU A 1 226  ? 147.670 109.730 115.759 1.00 15.55 ?  226  LEU A CA   1 
ATOM   1159  C C    . LEU A 1 226  ? 147.134 110.648 116.846 1.00 19.67 ?  226  LEU A C    1 
ATOM   1160  O O    . LEU A 1 226  ? 147.494 110.477 118.016 1.00 22.01 ?  226  LEU A O    1 
ATOM   1161  C CB   . LEU A 1 226  ? 148.994 110.294 115.231 1.00 16.45 ?  226  LEU A CB   1 
ATOM   1162  C CG   . LEU A 1 226  ? 150.214 110.107 116.136 1.00 17.97 ?  226  LEU A CG   1 
ATOM   1163  C CD1  . LEU A 1 226  ? 150.726 108.676 116.066 1.00 16.70 ?  226  LEU A CD1  1 
ATOM   1164  C CD2  . LEU A 1 226  ? 151.314 111.092 115.771 1.00 17.50 ?  226  LEU A CD2  1 
ATOM   1165  N N    . GLY A 1 227  ? 146.292 111.622 116.492 1.00 18.31 ?  227  GLY A N    1 
ATOM   1166  C CA   . GLY A 1 227  ? 145.683 112.463 117.510 1.00 16.96 ?  227  GLY A CA   1 
ATOM   1167  C C    . GLY A 1 227  ? 144.708 111.701 118.388 1.00 17.64 ?  227  GLY A C    1 
ATOM   1168  O O    . GLY A 1 227  ? 144.655 111.914 119.603 1.00 17.20 ?  227  GLY A O    1 
ATOM   1169  N N    . THR A 1 228  ? 143.926 110.801 117.787 1.00 16.25 ?  228  THR A N    1 
ATOM   1170  C CA   . THR A 1 228  ? 142.989 109.996 118.562 1.00 17.32 ?  228  THR A CA   1 
ATOM   1171  C C    . THR A 1 228  ? 143.719 109.044 119.501 1.00 17.53 ?  228  THR A C    1 
ATOM   1172  O O    . THR A 1 228  ? 143.279 108.824 120.637 1.00 22.11 ?  228  THR A O    1 
ATOM   1173  C CB   . THR A 1 228  ? 142.066 109.218 117.627 1.00 18.49 ?  228  THR A CB   1 
ATOM   1174  O OG1  . THR A 1 228  ? 141.665 110.060 116.538 1.00 18.68 ?  228  THR A OG1  1 
ATOM   1175  C CG2  . THR A 1 228  ? 140.834 108.741 118.377 1.00 16.27 ?  228  THR A CG2  1 
ATOM   1176  N N    . ILE A 1 229  ? 144.838 108.476 119.043 1.00 15.21 ?  229  ILE A N    1 
ATOM   1177  C CA   . ILE A 1 229  ? 145.597 107.535 119.864 1.00 15.97 ?  229  ILE A CA   1 
ATOM   1178  C C    . ILE A 1 229  ? 146.156 108.232 121.098 1.00 17.39 ?  229  ILE A C    1 
ATOM   1179  O O    . ILE A 1 229  ? 146.015 107.742 122.225 1.00 24.92 ?  229  ILE A O    1 
ATOM   1180  C CB   . ILE A 1 229  ? 146.710 106.875 119.029 1.00 19.30 ?  229  ILE A CB   1 
ATOM   1181  C CG1  . ILE A 1 229  ? 146.124 105.814 118.095 1.00 20.19 ?  229  ILE A CG1  1 
ATOM   1182  C CG2  . ILE A 1 229  ? 147.775 106.264 119.927 1.00 17.58 ?  229  ILE A CG2  1 
ATOM   1183  C CD1  . ILE A 1 229  ? 145.277 104.777 118.797 1.00 22.10 ?  229  ILE A CD1  1 
ATOM   1184  N N    . ILE A 1 230  ? 146.778 109.400 120.908 1.00 12.15 ?  230  ILE A N    1 
ATOM   1185  C CA   . ILE A 1 230  ? 147.345 110.115 122.047 1.00 17.71 ?  230  ILE A CA   1 
ATOM   1186  C C    . ILE A 1 230  ? 146.241 110.670 122.943 1.00 17.13 ?  230  ILE A C    1 
ATOM   1187  O O    . ILE A 1 230  ? 146.403 110.726 124.170 1.00 20.29 ?  230  ILE A O    1 
ATOM   1188  C CB   . ILE A 1 230  ? 148.327 111.208 121.567 1.00 17.48 ?  230  ILE A CB   1 
ATOM   1189  C CG1  . ILE A 1 230  ? 149.098 111.802 122.748 1.00 15.35 ?  230  ILE A CG1  1 
ATOM   1190  C CG2  . ILE A 1 230  ? 147.624 112.299 120.775 1.00 18.34 ?  230  ILE A CG2  1 
ATOM   1191  C CD1  . ILE A 1 230  ? 150.080 112.878 122.351 1.00 18.14 ?  230  ILE A CD1  1 
ATOM   1192  N N    . GLU A 1 231  ? 145.091 111.040 122.366 1.00 10.70 ?  231  GLU A N    1 
ATOM   1193  C CA   . GLU A 1 231  ? 143.961 111.500 123.169 1.00 12.42 ?  231  GLU A CA   1 
ATOM   1194  C C    . GLU A 1 231  ? 143.455 110.396 124.094 1.00 18.67 ?  231  GLU A C    1 
ATOM   1195  O O    . GLU A 1 231  ? 143.287 110.607 125.304 1.00 25.90 ?  231  GLU A O    1 
ATOM   1196  C CB   . GLU A 1 231  ? 142.843 111.988 122.247 1.00 14.73 ?  231  GLU A CB   1 
ATOM   1197  C CG   . GLU A 1 231  ? 142.258 113.342 122.611 1.00 18.90 ?  231  GLU A CG   1 
ATOM   1198  C CD   . GLU A 1 231  ? 141.125 113.754 121.687 1.00 18.37 ?  231  GLU A CD   1 
ATOM   1199  O OE1  . GLU A 1 231  ? 140.740 112.944 120.818 1.00 14.34 ?  231  GLU A OE1  1 
ATOM   1200  O OE2  . GLU A 1 231  ? 140.621 114.887 121.829 1.00 16.72 ?  231  GLU A OE2  1 
ATOM   1201  N N    . GLY A 1 232  ? 143.224 109.202 123.541 1.00 13.96 ?  232  GLY A N    1 
ATOM   1202  C CA   . GLY A 1 232  ? 142.776 108.088 124.361 1.00 8.19  ?  232  GLY A CA   1 
ATOM   1203  C C    . GLY A 1 232  ? 143.814 107.645 125.375 1.00 9.31  ?  232  GLY A C    1 
ATOM   1204  O O    . GLY A 1 232  ? 143.474 107.279 126.506 1.00 16.84 ?  232  GLY A O    1 
ATOM   1205  N N    . GLU A 1 233  ? 145.094 107.676 124.987 1.00 7.52  ?  233  GLU A N    1 
ATOM   1206  C CA   . GLU A 1 233  ? 146.158 107.317 125.918 1.00 11.00 ?  233  GLU A CA   1 
ATOM   1207  C C    . GLU A 1 233  ? 146.203 108.279 127.096 1.00 16.33 ?  233  GLU A C    1 
ATOM   1208  O O    . GLU A 1 233  ? 146.350 107.851 128.246 1.00 26.58 ?  233  GLU A O    1 
ATOM   1209  C CB   . GLU A 1 233  ? 147.504 107.289 125.193 1.00 15.06 ?  233  GLU A CB   1 
ATOM   1210  C CG   . GLU A 1 233  ? 148.708 107.182 126.118 1.00 20.71 ?  233  GLU A CG   1 
ATOM   1211  C CD   . GLU A 1 233  ? 150.024 107.387 125.393 1.00 24.57 ?  233  GLU A CD   1 
ATOM   1212  O OE1  . GLU A 1 233  ? 149.999 107.630 124.169 1.00 24.13 ?  233  GLU A OE1  1 
ATOM   1213  O OE2  . GLU A 1 233  ? 151.084 107.302 126.049 1.00 24.69 ?  233  GLU A OE2  1 
ATOM   1214  N N    . SER A 1 234  ? 146.046 109.580 126.836 1.00 10.88 ?  234  SER A N    1 
ATOM   1215  C CA   . SER A 1 234  ? 146.026 110.550 127.925 1.00 10.80 ?  234  SER A CA   1 
ATOM   1216  C C    . SER A 1 234  ? 144.784 110.405 128.797 1.00 9.96  ?  234  SER A C    1 
ATOM   1217  O O    . SER A 1 234  ? 144.859 110.615 130.014 1.00 18.36 ?  234  SER A O    1 
ATOM   1218  C CB   . SER A 1 234  ? 146.105 111.966 127.368 1.00 13.66 ?  234  SER A CB   1 
ATOM   1219  O OG   . SER A 1 234  ? 144.814 112.544 127.308 1.00 13.40 ?  234  SER A OG   1 
ATOM   1220  N N    . LEU A 1 235  ? 143.638 110.063 128.200 1.00 6.03  ?  235  LEU A N    1 
ATOM   1221  C CA   . LEU A 1 235  ? 142.429 109.840 128.991 1.00 5.77  ?  235  LEU A CA   1 
ATOM   1222  C C    . LEU A 1 235  ? 142.609 108.669 129.955 1.00 6.69  ?  235  LEU A C    1 
ATOM   1223  O O    . LEU A 1 235  ? 142.298 108.771 131.154 1.00 15.33 ?  235  LEU A O    1 
ATOM   1224  C CB   . LEU A 1 235  ? 141.243 109.599 128.055 1.00 3.97  ?  235  LEU A CB   1 
ATOM   1225  C CG   . LEU A 1 235  ? 140.065 108.762 128.553 1.00 4.91  ?  235  LEU A CG   1 
ATOM   1226  C CD1  . LEU A 1 235  ? 139.219 109.549 129.542 1.00 6.84  ?  235  LEU A CD1  1 
ATOM   1227  C CD2  . LEU A 1 235  ? 139.225 108.275 127.382 1.00 4.66  ?  235  LEU A CD2  1 
ATOM   1228  N N    . LEU A 1 236  ? 143.133 107.548 129.449 1.00 1.89  ?  236  LEU A N    1 
ATOM   1229  C CA   . LEU A 1 236  ? 143.397 106.399 130.310 1.00 3.72  ?  236  LEU A CA   1 
ATOM   1230  C C    . LEU A 1 236  ? 144.470 106.712 131.346 1.00 2.44  ?  236  LEU A C    1 
ATOM   1231  O O    . LEU A 1 236  ? 144.396 106.228 132.483 1.00 11.51 ?  236  LEU A O    1 
ATOM   1232  C CB   . LEU A 1 236  ? 143.800 105.196 129.461 1.00 8.30  ?  236  LEU A CB   1 
ATOM   1233  C CG   . LEU A 1 236  ? 142.733 104.721 128.471 1.00 11.29 ?  236  LEU A CG   1 
ATOM   1234  C CD1  . LEU A 1 236  ? 143.318 103.738 127.476 1.00 10.81 ?  236  LEU A CD1  1 
ATOM   1235  C CD2  . LEU A 1 236  ? 141.554 104.104 129.205 1.00 8.34  ?  236  LEU A CD2  1 
ATOM   1236  N N    . ASN A 1 237  ? 145.456 107.530 130.967 1.00 1.50  ?  237  ASN A N    1 
ATOM   1237  C CA   . ASN A 1 237  ? 146.481 107.991 131.897 1.00 1.45  ?  237  ASN A CA   1 
ATOM   1238  C C    . ASN A 1 237  ? 145.868 108.758 133.063 1.00 7.01  ?  237  ASN A C    1 
ATOM   1239  O O    . ASN A 1 237  ? 146.209 108.516 134.227 1.00 12.49 ?  237  ASN A O    1 
ATOM   1240  C CB   . ASN A 1 237  ? 147.484 108.857 131.132 1.00 8.25  ?  237  ASN A CB   1 
ATOM   1241  C CG   . ASN A 1 237  ? 148.680 109.246 131.962 1.00 12.13 ?  237  ASN A CG   1 
ATOM   1242  O OD1  . ASN A 1 237  ? 148.586 110.111 132.830 1.00 17.46 ?  237  ASN A OD1  1 
ATOM   1243  N ND2  . ASN A 1 237  ? 149.815 108.608 131.706 1.00 10.52 ?  237  ASN A ND2  1 
ATOM   1244  N N    . ASP A 1 238  ? 144.949 109.679 132.767 1.00 9.25  ?  238  ASP A N    1 
ATOM   1245  C CA   . ASP A 1 238  ? 144.289 110.439 133.825 1.00 3.72  ?  238  ASP A CA   1 
ATOM   1246  C C    . ASP A 1 238  ? 143.472 109.529 134.735 1.00 9.67  ?  238  ASP A C    1 
ATOM   1247  O O    . ASP A 1 238  ? 143.515 109.668 135.968 1.00 16.47 ?  238  ASP A O    1 
ATOM   1248  C CB   . ASP A 1 238  ? 143.399 111.521 133.213 1.00 8.64  ?  238  ASP A CB   1 
ATOM   1249  C CG   . ASP A 1 238  ? 144.193 112.704 132.692 1.00 17.45 ?  238  ASP A CG   1 
ATOM   1250  O OD1  . ASP A 1 238  ? 145.332 112.912 133.159 1.00 20.92 ?  238  ASP A OD1  1 
ATOM   1251  O OD2  . ASP A 1 238  ? 143.677 113.425 131.812 1.00 12.97 ?  238  ASP A OD2  1 
ATOM   1252  N N    . GLY A 1 239  ? 142.736 108.581 134.146 1.00 9.57  ?  239  GLY A N    1 
ATOM   1253  C CA   . GLY A 1 239  ? 141.930 107.676 134.958 1.00 1.19  ?  239  GLY A CA   1 
ATOM   1254  C C    . GLY A 1 239  ? 142.760 106.828 135.908 1.00 0.83  ?  239  GLY A C    1 
ATOM   1255  O O    . GLY A 1 239  ? 142.465 106.737 137.109 1.00 11.59 ?  239  GLY A O    1 
ATOM   1256  N N    . CYS A 1 240  ? 143.829 106.212 135.393 1.00 1.22  ?  240  CYS A N    1 
ATOM   1257  C CA   . CYS A 1 240  ? 144.651 105.373 136.259 1.00 6.77  ?  240  CYS A CA   1 
ATOM   1258  C C    . CYS A 1 240  ? 145.440 106.203 137.265 1.00 7.32  ?  240  CYS A C    1 
ATOM   1259  O O    . CYS A 1 240  ? 145.710 105.727 138.377 1.00 14.18 ?  240  CYS A O    1 
ATOM   1260  C CB   . CYS A 1 240  ? 145.585 104.494 135.429 1.00 11.12 ?  240  CYS A CB   1 
ATOM   1261  S SG   . CYS A 1 240  ? 146.751 105.367 134.382 1.00 26.90 ?  240  CYS A SG   1 
ATOM   1262  N N    . ALA A 1 241  ? 145.796 107.444 136.912 1.00 4.26  ?  241  ALA A N    1 
ATOM   1263  C CA   . ALA A 1 241  ? 146.428 108.331 137.882 1.00 0.92  ?  241  ALA A CA   1 
ATOM   1264  C C    . ALA A 1 241  ? 145.499 108.613 139.052 1.00 0.71  ?  241  ALA A C    1 
ATOM   1265  O O    . ALA A 1 241  ? 145.925 108.583 140.213 1.00 3.01  ?  241  ALA A O    1 
ATOM   1266  C CB   . ALA A 1 241  ? 146.845 109.637 137.208 1.00 7.30  ?  241  ALA A CB   1 
ATOM   1267  N N    . ILE A 1 242  ? 144.218 108.864 138.765 1.00 4.13  ?  242  ILE A N    1 
ATOM   1268  C CA   . ILE A 1 242  ? 143.241 109.079 139.833 1.00 2.98  ?  242  ILE A CA   1 
ATOM   1269  C C    . ILE A 1 242  ? 143.107 107.831 140.700 1.00 2.13  ?  242  ILE A C    1 
ATOM   1270  O O    . ILE A 1 242  ? 143.049 107.918 141.937 1.00 3.49  ?  242  ILE A O    1 
ATOM   1271  C CB   . ILE A 1 242  ? 141.887 109.510 139.238 1.00 0.07  ?  242  ILE A CB   1 
ATOM   1272  C CG1  . ILE A 1 242  ? 142.003 110.893 138.597 1.00 0.23  ?  242  ILE A CG1  1 
ATOM   1273  C CG2  . ILE A 1 242  ? 140.796 109.503 140.295 1.00 3.18  ?  242  ILE A CG2  1 
ATOM   1274  C CD1  . ILE A 1 242  ? 140.775 111.308 137.832 1.00 2.88  ?  242  ILE A CD1  1 
ATOM   1275  N N    . VAL A 1 243  ? 143.074 106.653 140.068 1.00 5.64  ?  243  VAL A N    1 
ATOM   1276  C CA   . VAL A 1 243  ? 142.889 105.408 140.820 1.00 2.50  ?  243  VAL A CA   1 
ATOM   1277  C C    . VAL A 1 243  ? 144.050 105.175 141.788 1.00 4.56  ?  243  VAL A C    1 
ATOM   1278  O O    . VAL A 1 243  ? 143.845 104.920 142.986 1.00 9.20  ?  243  VAL A O    1 
ATOM   1279  C CB   . VAL A 1 243  ? 142.714 104.221 139.855 1.00 0.00  ?  243  VAL A CB   1 
ATOM   1280  C CG1  . VAL A 1 243  ? 142.852 102.906 140.601 1.00 2.72  ?  243  VAL A CG1  1 
ATOM   1281  C CG2  . VAL A 1 243  ? 141.370 104.302 139.155 1.00 2.23  ?  243  VAL A CG2  1 
ATOM   1282  N N    . ILE A 1 244  ? 145.288 105.270 141.291 1.00 5.03  ?  244  ILE A N    1 
ATOM   1283  C CA   . ILE A 1 244  ? 146.438 105.041 142.167 1.00 1.01  ?  244  ILE A CA   1 
ATOM   1284  C C    . ILE A 1 244  ? 146.587 106.152 143.204 1.00 1.87  ?  244  ILE A C    1 
ATOM   1285  O O    . ILE A 1 244  ? 147.030 105.893 144.336 1.00 5.21  ?  244  ILE A O    1 
ATOM   1286  C CB   . ILE A 1 244  ? 147.726 104.839 141.343 1.00 1.40  ?  244  ILE A CB   1 
ATOM   1287  C CG1  . ILE A 1 244  ? 147.480 103.848 140.208 1.00 7.72  ?  244  ILE A CG1  1 
ATOM   1288  C CG2  . ILE A 1 244  ? 148.867 104.357 142.214 1.00 4.71  ?  244  ILE A CG2  1 
ATOM   1289  C CD1  . ILE A 1 244  ? 148.634 103.722 139.251 1.00 7.83  ?  244  ILE A CD1  1 
ATOM   1290  N N    . PHE A 1 245  ? 146.209 107.391 142.862 1.00 5.11  ?  245  PHE A N    1 
ATOM   1291  C CA   . PHE A 1 245  ? 146.213 108.453 143.862 1.00 0.00  ?  245  PHE A CA   1 
ATOM   1292  C C    . PHE A 1 245  ? 145.273 108.130 145.010 1.00 3.10  ?  245  PHE A C    1 
ATOM   1293  O O    . PHE A 1 245  ? 145.615 108.352 146.174 1.00 7.08  ?  245  PHE A O    1 
ATOM   1294  C CB   . PHE A 1 245  ? 145.826 109.792 143.236 1.00 1.75  ?  245  PHE A CB   1 
ATOM   1295  C CG   . PHE A 1 245  ? 145.564 110.876 144.250 1.00 3.67  ?  245  PHE A CG   1 
ATOM   1296  C CD1  . PHE A 1 245  ? 146.613 111.575 144.816 1.00 5.60  ?  245  PHE A CD1  1 
ATOM   1297  C CD2  . PHE A 1 245  ? 144.269 111.193 144.639 1.00 0.95  ?  245  PHE A CD2  1 
ATOM   1298  C CE1  . PHE A 1 245  ? 146.380 112.562 145.747 1.00 1.94  ?  245  PHE A CE1  1 
ATOM   1299  C CE2  . PHE A 1 245  ? 144.033 112.181 145.573 1.00 0.03  ?  245  PHE A CE2  1 
ATOM   1300  C CZ   . PHE A 1 245  ? 145.089 112.867 146.126 1.00 0.29  ?  245  PHE A CZ   1 
ATOM   1301  N N    . ASN A 1 246  ? 144.076 107.624 144.703 1.00 7.82  ?  246  ASN A N    1 
ATOM   1302  C CA   . ASN A 1 246  ? 143.146 107.253 145.766 1.00 4.47  ?  246  ASN A CA   1 
ATOM   1303  C C    . ASN A 1 246  ? 143.695 106.108 146.607 1.00 6.88  ?  246  ASN A C    1 
ATOM   1304  O O    . ASN A 1 246  ? 143.607 106.136 147.846 1.00 8.12  ?  246  ASN A O    1 
ATOM   1305  C CB   . ASN A 1 246  ? 141.795 106.881 145.165 1.00 2.76  ?  246  ASN A CB   1 
ATOM   1306  C CG   . ASN A 1 246  ? 140.788 107.994 145.292 1.00 14.73 ?  246  ASN A CG   1 
ATOM   1307  O OD1  . ASN A 1 246  ? 139.941 107.982 146.184 1.00 18.57 ?  246  ASN A OD1  1 
ATOM   1308  N ND2  . ASN A 1 246  ? 140.899 108.989 144.420 1.00 11.63 ?  246  ASN A ND2  1 
ATOM   1309  N N    . VAL A 1 247  ? 144.287 105.106 145.945 1.00 9.62  ?  247  VAL A N    1 
ATOM   1310  C CA   . VAL A 1 247  ? 144.826 103.944 146.651 1.00 5.17  ?  247  VAL A CA   1 
ATOM   1311  C C    . VAL A 1 247  ? 145.903 104.366 147.645 1.00 3.47  ?  247  VAL A C    1 
ATOM   1312  O O    . VAL A 1 247  ? 145.932 103.894 148.788 1.00 2.63  ?  247  VAL A O    1 
ATOM   1313  C CB   . VAL A 1 247  ? 145.353 102.907 145.641 1.00 6.46  ?  247  VAL A CB   1 
ATOM   1314  C CG1  . VAL A 1 247  ? 146.317 101.933 146.306 1.00 4.17  ?  247  VAL A CG1  1 
ATOM   1315  C CG2  . VAL A 1 247  ? 144.196 102.157 145.007 1.00 8.33  ?  247  VAL A CG2  1 
ATOM   1316  N N    . PHE A 1 248  ? 146.787 105.279 147.241 1.00 9.02  ?  248  PHE A N    1 
ATOM   1317  C CA   . PHE A 1 248  ? 147.846 105.699 148.155 1.00 0.67  ?  248  PHE A CA   1 
ATOM   1318  C C    . PHE A 1 248  ? 147.391 106.775 149.140 1.00 7.11  ?  248  PHE A C    1 
ATOM   1319  O O    . PHE A 1 248  ? 147.961 106.884 150.232 1.00 12.94 ?  248  PHE A O    1 
ATOM   1320  C CB   . PHE A 1 248  ? 149.063 106.172 147.362 1.00 0.33  ?  248  PHE A CB   1 
ATOM   1321  C CG   . PHE A 1 248  ? 149.949 105.052 146.904 1.00 1.82  ?  248  PHE A CG   1 
ATOM   1322  C CD1  . PHE A 1 248  ? 150.919 104.534 147.743 1.00 6.99  ?  248  PHE A CD1  1 
ATOM   1323  C CD2  . PHE A 1 248  ? 149.800 104.502 145.645 1.00 2.80  ?  248  PHE A CD2  1 
ATOM   1324  C CE1  . PHE A 1 248  ? 151.735 103.498 147.330 1.00 10.70 ?  248  PHE A CE1  1 
ATOM   1325  C CE2  . PHE A 1 248  ? 150.612 103.464 145.226 1.00 7.25  ?  248  PHE A CE2  1 
ATOM   1326  C CZ   . PHE A 1 248  ? 151.580 102.963 146.070 1.00 9.19  ?  248  PHE A CZ   1 
ATOM   1327  N N    . MET A 1 249  ? 146.371 107.565 148.791 1.00 11.54 ?  249  MET A N    1 
ATOM   1328  C CA   . MET A 1 249  ? 145.851 108.566 149.717 1.00 7.03  ?  249  MET A CA   1 
ATOM   1329  C C    . MET A 1 249  ? 145.175 107.906 150.909 1.00 8.34  ?  249  MET A C    1 
ATOM   1330  O O    . MET A 1 249  ? 145.288 108.394 152.043 1.00 7.55  ?  249  MET A O    1 
ATOM   1331  C CB   . MET A 1 249  ? 144.885 109.499 148.984 1.00 7.48  ?  249  MET A CB   1 
ATOM   1332  C CG   . MET A 1 249  ? 143.861 110.200 149.868 1.00 12.85 ?  249  MET A CG   1 
ATOM   1333  S SD   . MET A 1 249  ? 142.555 111.009 148.926 1.00 12.42 ?  249  MET A SD   1 
ATOM   1334  C CE   . MET A 1 249  ? 141.187 109.890 149.204 1.00 6.45  ?  249  MET A CE   1 
ATOM   1335  N N    . LYS A 1 250  ? 144.477 106.787 150.673 1.00 12.38 ?  250  LYS A N    1 
ATOM   1336  C CA   . LYS A 1 250  ? 143.915 106.026 151.788 1.00 10.90 ?  250  LYS A CA   1 
ATOM   1337  C C    . LYS A 1 250  ? 145.003 105.559 152.748 1.00 10.74 ?  250  LYS A C    1 
ATOM   1338  O O    . LYS A 1 250  ? 144.817 105.588 153.969 1.00 16.03 ?  250  LYS A O    1 
ATOM   1339  C CB   . LYS A 1 250  ? 143.119 104.828 151.272 1.00 13.63 ?  250  LYS A CB   1 
ATOM   1340  C CG   . LYS A 1 250  ? 141.931 105.176 150.395 1.00 13.64 ?  250  LYS A CG   1 
ATOM   1341  C CD   . LYS A 1 250  ? 141.068 106.253 151.022 1.00 14.36 ?  250  LYS A CD   1 
ATOM   1342  C CE   . LYS A 1 250  ? 139.795 106.462 150.221 1.00 15.91 ?  250  LYS A CE   1 
ATOM   1343  N NZ   . LYS A 1 250  ? 139.281 105.183 149.657 1.00 16.29 ?  250  LYS A NZ   1 
ATOM   1344  N N    . MET A 1 251  ? 146.150 105.130 152.216 1.00 11.75 ?  251  MET A N    1 
ATOM   1345  C CA   . MET A 1 251  ? 147.230 104.650 153.072 1.00 8.69  ?  251  MET A CA   1 
ATOM   1346  C C    . MET A 1 251  ? 147.915 105.796 153.808 1.00 12.65 ?  251  MET A C    1 
ATOM   1347  O O    . MET A 1 251  ? 148.333 105.636 154.960 1.00 21.10 ?  251  MET A O    1 
ATOM   1348  C CB   . MET A 1 251  ? 148.243 103.865 152.243 1.00 9.08  ?  251  MET A CB   1 
ATOM   1349  C CG   . MET A 1 251  ? 147.635 102.715 151.458 1.00 12.82 ?  251  MET A CG   1 
ATOM   1350  S SD   . MET A 1 251  ? 148.758 101.961 150.263 1.00 24.17 ?  251  MET A SD   1 
ATOM   1351  C CE   . MET A 1 251  ? 150.356 102.409 150.936 1.00 14.49 ?  251  MET A CE   1 
ATOM   1352  N N    . VAL A 1 252  ? 148.046 106.954 153.162 1.00 11.19 ?  252  VAL A N    1 
ATOM   1353  C CA   . VAL A 1 252  ? 148.748 108.076 153.785 1.00 10.90 ?  252  VAL A CA   1 
ATOM   1354  C C    . VAL A 1 252  ? 147.893 108.720 154.869 1.00 12.62 ?  252  VAL A C    1 
ATOM   1355  O O    . VAL A 1 252  ? 148.308 108.826 156.029 1.00 11.08 ?  252  VAL A O    1 
ATOM   1356  C CB   . VAL A 1 252  ? 149.167 109.114 152.728 1.00 10.53 ?  252  VAL A CB   1 
ATOM   1357  C CG1  . VAL A 1 252  ? 149.666 110.379 153.407 1.00 12.42 ?  252  VAL A CG1  1 
ATOM   1358  C CG2  . VAL A 1 252  ? 150.242 108.554 151.834 1.00 9.12  ?  252  VAL A CG2  1 
ATOM   1359  N N    . PHE A 1 253  ? 146.688 109.160 154.510 1.00 15.11 ?  253  PHE A N    1 
ATOM   1360  C CA   . PHE A 1 253  ? 145.928 110.039 155.389 1.00 10.54 ?  253  PHE A CA   1 
ATOM   1361  C C    . PHE A 1 253  ? 144.949 109.306 156.294 1.00 11.07 ?  253  PHE A C    1 
ATOM   1362  O O    . PHE A 1 253  ? 144.503 109.885 157.291 1.00 11.54 ?  253  PHE A O    1 
ATOM   1363  C CB   . PHE A 1 253  ? 145.177 111.083 154.559 1.00 9.70  ?  253  PHE A CB   1 
ATOM   1364  C CG   . PHE A 1 253  ? 146.067 112.143 153.978 1.00 8.87  ?  253  PHE A CG   1 
ATOM   1365  C CD1  . PHE A 1 253  ? 146.891 112.898 154.796 1.00 6.51  ?  253  PHE A CD1  1 
ATOM   1366  C CD2  . PHE A 1 253  ? 146.091 112.376 152.614 1.00 10.41 ?  253  PHE A CD2  1 
ATOM   1367  C CE1  . PHE A 1 253  ? 147.714 113.871 154.266 1.00 6.26  ?  253  PHE A CE1  1 
ATOM   1368  C CE2  . PHE A 1 253  ? 146.913 113.347 152.079 1.00 13.24 ?  253  PHE A CE2  1 
ATOM   1369  C CZ   . PHE A 1 253  ? 147.725 114.095 152.907 1.00 9.86  ?  253  PHE A CZ   1 
ATOM   1370  N N    . PHE A 1 254  ? 144.609 108.058 155.986 1.00 10.50 ?  254  PHE A N    1 
ATOM   1371  C CA   . PHE A 1 254  ? 143.690 107.265 156.802 1.00 10.32 ?  254  PHE A CA   1 
ATOM   1372  C C    . PHE A 1 254  ? 144.348 105.932 157.135 1.00 13.07 ?  254  PHE A C    1 
ATOM   1373  O O    . PHE A 1 254  ? 143.964 104.882 156.607 1.00 16.33 ?  254  PHE A O    1 
ATOM   1374  C CB   . PHE A 1 254  ? 142.357 107.062 156.080 1.00 9.55  ?  254  PHE A CB   1 
ATOM   1375  C CG   . PHE A 1 254  ? 141.762 108.331 155.535 1.00 9.25  ?  254  PHE A CG   1 
ATOM   1376  C CD1  . PHE A 1 254  ? 141.279 109.309 156.387 1.00 10.61 ?  254  PHE A CD1  1 
ATOM   1377  C CD2  . PHE A 1 254  ? 141.690 108.546 154.169 1.00 10.38 ?  254  PHE A CD2  1 
ATOM   1378  C CE1  . PHE A 1 254  ? 140.731 110.478 155.885 1.00 10.67 ?  254  PHE A CE1  1 
ATOM   1379  C CE2  . PHE A 1 254  ? 141.145 109.711 153.662 1.00 8.92  ?  254  PHE A CE2  1 
ATOM   1380  C CZ   . PHE A 1 254  ? 140.666 110.678 154.521 1.00 8.05  ?  254  PHE A CZ   1 
ATOM   1381  N N    . PRO A 1 255  ? 145.340 105.937 158.029 1.00 15.76 ?  255  PRO A N    1 
ATOM   1382  C CA   . PRO A 1 255  ? 146.091 104.710 158.315 1.00 16.83 ?  255  PRO A CA   1 
ATOM   1383  C C    . PRO A 1 255  ? 145.419 103.785 159.316 1.00 19.86 ?  255  PRO A C    1 
ATOM   1384  O O    . PRO A 1 255  ? 146.015 102.766 159.684 1.00 20.25 ?  255  PRO A O    1 
ATOM   1385  C CB   . PRO A 1 255  ? 147.414 105.252 158.870 1.00 15.02 ?  255  PRO A CB   1 
ATOM   1386  C CG   . PRO A 1 255  ? 147.030 106.533 159.549 1.00 16.14 ?  255  PRO A CG   1 
ATOM   1387  C CD   . PRO A 1 255  ? 145.767 107.052 158.893 1.00 14.78 ?  255  PRO A CD   1 
ATOM   1388  N N    . GLN A 1 256  ? 144.203 104.107 159.764 1.00 25.57 ?  256  GLN A N    1 
ATOM   1389  C CA   . GLN A 1 256  ? 143.478 103.229 160.673 1.00 23.20 ?  256  GLN A CA   1 
ATOM   1390  C C    . GLN A 1 256  ? 143.027 101.940 159.997 1.00 22.18 ?  256  GLN A C    1 
ATOM   1391  O O    . GLN A 1 256  ? 142.769 100.950 160.691 1.00 23.66 ?  256  GLN A O    1 
ATOM   1392  C CB   . GLN A 1 256  ? 142.262 103.957 161.249 1.00 20.38 ?  256  GLN A CB   1 
ATOM   1393  C CG   . GLN A 1 256  ? 141.826 103.473 162.622 1.00 21.69 ?  256  GLN A CG   1 
ATOM   1394  C CD   . GLN A 1 256  ? 140.517 104.096 163.066 1.00 23.63 ?  256  GLN A CD   1 
ATOM   1395  O OE1  . GLN A 1 256  ? 139.820 104.733 162.275 1.00 25.59 ?  256  GLN A OE1  1 
ATOM   1396  N NE2  . GLN A 1 256  ? 140.173 103.915 164.336 1.00 23.15 ?  256  GLN A NE2  1 
ATOM   1397  N N    . LEU A 1 257  ? 142.921 101.930 158.670 1.00 21.11 ?  257  LEU A N    1 
ATOM   1398  C CA   . LEU A 1 257  ? 142.457 100.746 157.960 1.00 24.63 ?  257  LEU A CA   1 
ATOM   1399  C C    . LEU A 1 257  ? 143.555 99.691  157.881 1.00 24.69 ?  257  LEU A C    1 
ATOM   1400  O O    . LEU A 1 257  ? 144.750 99.997  157.913 1.00 25.18 ?  257  LEU A O    1 
ATOM   1401  C CB   . LEU A 1 257  ? 141.992 101.098 156.544 1.00 24.66 ?  257  LEU A CB   1 
ATOM   1402  C CG   . LEU A 1 257  ? 140.620 101.731 156.266 1.00 23.50 ?  257  LEU A CG   1 
ATOM   1403  C CD1  . LEU A 1 257  ? 139.484 100.764 156.592 1.00 24.23 ?  257  LEU A CD1  1 
ATOM   1404  C CD2  . LEU A 1 257  ? 140.422 103.073 156.958 1.00 19.31 ?  257  LEU A CD2  1 
ATOM   1405  N N    . THR A 1 258  ? 143.133 98.434  157.756 1.00 24.52 ?  258  THR A N    1 
ATOM   1406  C CA   . THR A 1 258  ? 144.031 97.290  157.663 1.00 25.64 ?  258  THR A CA   1 
ATOM   1407  C C    . THR A 1 258  ? 143.753 96.537  156.371 1.00 23.54 ?  258  THR A C    1 
ATOM   1408  O O    . THR A 1 258  ? 142.592 96.278  156.038 1.00 25.08 ?  258  THR A O    1 
ATOM   1409  C CB   . THR A 1 258  ? 143.856 96.351  158.859 1.00 26.83 ?  258  THR A CB   1 
ATOM   1410  O OG1  . THR A 1 258  ? 142.467 96.272  159.206 1.00 26.07 ?  258  THR A OG1  1 
ATOM   1411  C CG2  . THR A 1 258  ? 144.648 96.852  160.055 1.00 22.04 ?  258  THR A CG2  1 
ATOM   1412  N N    . SER A 1 259  ? 144.816 96.175  155.655 1.00 24.42 ?  259  SER A N    1 
ATOM   1413  C CA   . SER A 1 259  ? 144.701 95.494  154.373 1.00 26.21 ?  259  SER A CA   1 
ATOM   1414  C C    . SER A 1 259  ? 145.508 94.204  154.386 1.00 24.16 ?  259  SER A C    1 
ATOM   1415  O O    . SER A 1 259  ? 146.633 94.168  154.892 1.00 22.81 ?  259  SER A O    1 
ATOM   1416  C CB   . SER A 1 259  ? 145.178 96.391  153.224 1.00 22.50 ?  259  SER A CB   1 
ATOM   1417  O OG   . SER A 1 259  ? 144.351 97.533  153.088 1.00 27.19 ?  259  SER A OG   1 
ATOM   1418  N N    . THR A 1 260  ? 144.928 93.148  153.822 1.00 24.36 ?  260  THR A N    1 
ATOM   1419  C CA   . THR A 1 260  ? 145.596 91.867  153.640 1.00 26.50 ?  260  THR A CA   1 
ATOM   1420  C C    . THR A 1 260  ? 145.838 91.630  152.152 1.00 25.01 ?  260  THR A C    1 
ATOM   1421  O O    . THR A 1 260  ? 145.507 92.462  151.303 1.00 24.68 ?  260  THR A O    1 
ATOM   1422  C CB   . THR A 1 260  ? 144.775 90.728  154.250 1.00 26.75 ?  260  THR A CB   1 
ATOM   1423  O OG1  . THR A 1 260  ? 143.841 90.235  153.281 1.00 23.99 ?  260  THR A OG1  1 
ATOM   1424  C CG2  . THR A 1 260  ? 144.016 91.208  155.480 1.00 25.00 ?  260  THR A CG2  1 
ATOM   1425  N N    . VAL A 1 261  ? 146.434 90.478  151.839 1.00 21.22 ?  261  VAL A N    1 
ATOM   1426  C CA   . VAL A 1 261  ? 146.671 90.123  150.442 1.00 22.14 ?  261  VAL A CA   1 
ATOM   1427  C C    . VAL A 1 261  ? 145.351 89.833  149.737 1.00 24.41 ?  261  VAL A C    1 
ATOM   1428  O O    . VAL A 1 261  ? 145.090 90.337  148.637 1.00 24.93 ?  261  VAL A O    1 
ATOM   1429  C CB   . VAL A 1 261  ? 147.635 88.927  150.350 1.00 22.30 ?  261  VAL A CB   1 
ATOM   1430  C CG1  . VAL A 1 261  ? 147.846 88.522  148.899 1.00 20.99 ?  261  VAL A CG1  1 
ATOM   1431  C CG2  . VAL A 1 261  ? 148.960 89.265  151.014 1.00 23.61 ?  261  VAL A CG2  1 
ATOM   1432  N N    . GLY A 1 262  ? 144.494 89.027  150.368 1.00 21.60 ?  262  GLY A N    1 
ATOM   1433  C CA   . GLY A 1 262  ? 143.216 88.694  149.759 1.00 21.44 ?  262  GLY A CA   1 
ATOM   1434  C C    . GLY A 1 262  ? 142.288 89.887  149.645 1.00 24.31 ?  262  GLY A C    1 
ATOM   1435  O O    . GLY A 1 262  ? 141.588 90.045  148.641 1.00 24.94 ?  262  GLY A O    1 
ATOM   1436  N N    . GLN A 1 263  ? 142.270 90.745  150.670 1.00 23.95 ?  263  GLN A N    1 
ATOM   1437  C CA   . GLN A 1 263  ? 141.446 91.948  150.618 1.00 23.66 ?  263  GLN A CA   1 
ATOM   1438  C C    . GLN A 1 263  ? 141.912 92.890  149.515 1.00 24.77 ?  263  GLN A C    1 
ATOM   1439  O O    . GLN A 1 263  ? 141.090 93.468  148.795 1.00 22.72 ?  263  GLN A O    1 
ATOM   1440  C CB   . GLN A 1 263  ? 141.462 92.657  151.972 1.00 20.70 ?  263  GLN A CB   1 
ATOM   1441  C CG   . GLN A 1 263  ? 140.929 91.825  153.132 1.00 21.60 ?  263  GLN A CG   1 
ATOM   1442  C CD   . GLN A 1 263  ? 139.453 91.497  152.999 1.00 24.73 ?  263  GLN A CD   1 
ATOM   1443  O OE1  . GLN A 1 263  ? 139.076 90.512  152.364 1.00 27.25 ?  263  GLN A OE1  1 
ATOM   1444  N NE2  . GLN A 1 263  ? 138.608 92.325  153.604 1.00 24.96 ?  263  GLN A NE2  1 
ATOM   1445  N N    . ASN A 1 264  ? 143.230 93.049  149.359 1.00 20.85 ?  264  ASN A N    1 
ATOM   1446  C CA   . ASN A 1 264  ? 143.754 93.901  148.295 1.00 21.97 ?  264  ASN A CA   1 
ATOM   1447  C C    . ASN A 1 264  ? 143.460 93.318  146.918 1.00 23.55 ?  264  ASN A C    1 
ATOM   1448  O O    . ASN A 1 264  ? 143.143 94.061  145.982 1.00 29.06 ?  264  ASN A O    1 
ATOM   1449  C CB   . ASN A 1 264  ? 145.255 94.112  148.481 1.00 23.99 ?  264  ASN A CB   1 
ATOM   1450  C CG   . ASN A 1 264  ? 145.568 95.191  149.497 1.00 25.45 ?  264  ASN A CG   1 
ATOM   1451  O OD1  . ASN A 1 264  ? 144.669 95.865  150.000 1.00 22.64 ?  264  ASN A OD1  1 
ATOM   1452  N ND2  . ASN A 1 264  ? 146.848 95.360  149.807 1.00 25.48 ?  264  ASN A ND2  1 
ATOM   1453  N N    . VAL A 1 265  ? 143.558 91.994  146.774 1.00 17.99 ?  265  VAL A N    1 
ATOM   1454  C CA   . VAL A 1 265  ? 143.244 91.357  145.496 1.00 18.57 ?  265  VAL A CA   1 
ATOM   1455  C C    . VAL A 1 265  ? 141.767 91.536  145.157 1.00 19.67 ?  265  VAL A C    1 
ATOM   1456  O O    . VAL A 1 265  ? 141.407 91.849  144.012 1.00 23.39 ?  265  VAL A O    1 
ATOM   1457  C CB   . VAL A 1 265  ? 143.652 89.871  145.530 1.00 18.06 ?  265  VAL A CB   1 
ATOM   1458  C CG1  . VAL A 1 265  ? 142.948 89.082  144.435 1.00 16.78 ?  265  VAL A CG1  1 
ATOM   1459  C CG2  . VAL A 1 265  ? 145.161 89.737  145.393 1.00 15.90 ?  265  VAL A CG2  1 
ATOM   1460  N N    . LEU A 1 266  ? 140.890 91.359  146.150 1.00 15.62 ?  266  LEU A N    1 
ATOM   1461  C CA   . LEU A 1 266  ? 139.460 91.548  145.925 1.00 19.02 ?  266  LEU A CA   1 
ATOM   1462  C C    . LEU A 1 266  ? 139.137 93.002  145.595 1.00 17.79 ?  266  LEU A C    1 
ATOM   1463  O O    . LEU A 1 266  ? 138.276 93.272  144.752 1.00 17.31 ?  266  LEU A O    1 
ATOM   1464  C CB   . LEU A 1 266  ? 138.674 91.084  147.150 1.00 21.12 ?  266  LEU A CB   1 
ATOM   1465  C CG   . LEU A 1 266  ? 137.236 90.627  146.902 1.00 20.17 ?  266  LEU A CG   1 
ATOM   1466  C CD1  . LEU A 1 266  ? 137.203 89.488  145.895 1.00 14.02 ?  266  LEU A CD1  1 
ATOM   1467  C CD2  . LEU A 1 266  ? 136.570 90.216  148.205 1.00 17.35 ?  266  LEU A CD2  1 
ATOM   1468  N N    . TYR A 1 267  ? 139.818 93.949  146.246 1.00 16.24 ?  267  TYR A N    1 
ATOM   1469  C CA   . TYR A 1 267  ? 139.627 95.361  145.926 1.00 19.55 ?  267  TYR A CA   1 
ATOM   1470  C C    . TYR A 1 267  ? 140.088 95.679  144.508 1.00 15.25 ?  267  TYR A C    1 
ATOM   1471  O O    . TYR A 1 267  ? 139.441 96.460  143.799 1.00 20.99 ?  267  TYR A O    1 
ATOM   1472  C CB   . TYR A 1 267  ? 140.372 96.230  146.938 1.00 20.95 ?  267  TYR A CB   1 
ATOM   1473  C CG   . TYR A 1 267  ? 140.157 97.714  146.754 1.00 19.80 ?  267  TYR A CG   1 
ATOM   1474  C CD1  . TYR A 1 267  ? 138.941 98.304  147.072 1.00 19.91 ?  267  TYR A CD1  1 
ATOM   1475  C CD2  . TYR A 1 267  ? 141.171 98.524  146.262 1.00 19.83 ?  267  TYR A CD2  1 
ATOM   1476  C CE1  . TYR A 1 267  ? 138.741 99.662  146.905 1.00 21.32 ?  267  TYR A CE1  1 
ATOM   1477  C CE2  . TYR A 1 267  ? 140.982 99.882  146.092 1.00 17.93 ?  267  TYR A CE2  1 
ATOM   1478  C CZ   . TYR A 1 267  ? 139.766 100.446 146.415 1.00 21.78 ?  267  TYR A CZ   1 
ATOM   1479  O OH   . TYR A 1 267  ? 139.574 101.798 146.247 1.00 23.19 ?  267  TYR A OH   1 
ATOM   1480  N N    . PHE A 1 268  ? 141.212 95.093  144.085 1.00 9.86  ?  268  PHE A N    1 
ATOM   1481  C CA   . PHE A 1 268  ? 141.688 95.288  142.719 1.00 13.49 ?  268  PHE A CA   1 
ATOM   1482  C C    . PHE A 1 268  ? 140.700 94.725  141.706 1.00 12.82 ?  268  PHE A C    1 
ATOM   1483  O O    . PHE A 1 268  ? 140.454 95.337  140.660 1.00 18.75 ?  268  PHE A O    1 
ATOM   1484  C CB   . PHE A 1 268  ? 143.062 94.640  142.550 1.00 19.38 ?  268  PHE A CB   1 
ATOM   1485  C CG   . PHE A 1 268  ? 143.446 94.388  141.119 1.00 17.85 ?  268  PHE A CG   1 
ATOM   1486  C CD1  . PHE A 1 268  ? 143.742 95.442  140.270 1.00 16.79 ?  268  PHE A CD1  1 
ATOM   1487  C CD2  . PHE A 1 268  ? 143.516 93.095  140.624 1.00 17.37 ?  268  PHE A CD2  1 
ATOM   1488  C CE1  . PHE A 1 268  ? 144.098 95.213  138.954 1.00 18.16 ?  268  PHE A CE1  1 
ATOM   1489  C CE2  . PHE A 1 268  ? 143.871 92.860  139.308 1.00 20.26 ?  268  PHE A CE2  1 
ATOM   1490  C CZ   . PHE A 1 268  ? 144.162 93.920  138.472 1.00 21.51 ?  268  PHE A CZ   1 
ATOM   1491  N N    . LEU A 1 269  ? 140.125 93.555  141.999 1.00 9.96  ?  269  LEU A N    1 
ATOM   1492  C CA   . LEU A 1 269  ? 139.110 92.989  141.114 1.00 11.57 ?  269  LEU A CA   1 
ATOM   1493  C C    . LEU A 1 269  ? 137.851 93.849  141.089 1.00 14.43 ?  269  LEU A C    1 
ATOM   1494  O O    . LEU A 1 269  ? 137.210 93.988  140.041 1.00 20.43 ?  269  LEU A O    1 
ATOM   1495  C CB   . LEU A 1 269  ? 138.775 91.558  141.536 1.00 14.95 ?  269  LEU A CB   1 
ATOM   1496  C CG   . LEU A 1 269  ? 139.872 90.509  141.347 1.00 14.67 ?  269  LEU A CG   1 
ATOM   1497  C CD1  . LEU A 1 269  ? 139.385 89.140  141.788 1.00 15.30 ?  269  LEU A CD1  1 
ATOM   1498  C CD2  . LEU A 1 269  ? 140.331 90.473  139.898 1.00 13.54 ?  269  LEU A CD2  1 
ATOM   1499  N N    . GLN A 1 270  ? 137.476 94.423  142.235 1.00 12.70 ?  270  GLN A N    1 
ATOM   1500  C CA   . GLN A 1 270  ? 136.315 95.308  142.285 1.00 11.65 ?  270  GLN A CA   1 
ATOM   1501  C C    . GLN A 1 270  ? 136.539 96.567  141.458 1.00 10.79 ?  270  GLN A C    1 
ATOM   1502  O O    . GLN A 1 270  ? 135.635 97.019  140.746 1.00 13.71 ?  270  GLN A O    1 
ATOM   1503  C CB   . GLN A 1 270  ? 136.001 95.679  143.735 1.00 10.78 ?  270  GLN A CB   1 
ATOM   1504  C CG   . GLN A 1 270  ? 134.920 94.836  144.388 1.00 12.41 ?  270  GLN A CG   1 
ATOM   1505  C CD   . GLN A 1 270  ? 134.647 95.251  145.821 1.00 17.30 ?  270  GLN A CD   1 
ATOM   1506  O OE1  . GLN A 1 270  ? 133.729 96.024  146.091 1.00 19.30 ?  270  GLN A OE1  1 
ATOM   1507  N NE2  . GLN A 1 270  ? 135.447 94.738  146.748 1.00 14.53 ?  270  GLN A NE2  1 
ATOM   1508  N N    . VAL A 1 271  ? 137.736 97.146  141.536 1.00 11.81 ?  271  VAL A N    1 
ATOM   1509  C CA   . VAL A 1 271  ? 137.990 98.422  140.876 1.00 12.59 ?  271  VAL A CA   1 
ATOM   1510  C C    . VAL A 1 271  ? 138.220 98.230  139.382 1.00 12.29 ?  271  VAL A C    1 
ATOM   1511  O O    . VAL A 1 271  ? 137.580 98.887  138.552 1.00 18.09 ?  271  VAL A O    1 
ATOM   1512  C CB   . VAL A 1 271  ? 139.181 99.137  141.542 1.00 9.93  ?  271  VAL A CB   1 
ATOM   1513  C CG1  . VAL A 1 271  ? 139.662 100.291 140.677 1.00 7.05  ?  271  VAL A CG1  1 
ATOM   1514  C CG2  . VAL A 1 271  ? 138.794 99.629  142.925 1.00 11.59 ?  271  VAL A CG2  1 
ATOM   1515  N N    . ALA A 1 272  ? 139.126 97.326  139.012 1.00 9.41  ?  272  ALA A N    1 
ATOM   1516  C CA   . ALA A 1 272  ? 139.597 97.232  137.637 1.00 10.96 ?  272  ALA A CA   1 
ATOM   1517  C C    . ALA A 1 272  ? 138.710 96.385  136.733 1.00 13.76 ?  272  ALA A C    1 
ATOM   1518  O O    . ALA A 1 272  ? 138.917 96.395  135.515 1.00 15.05 ?  272  ALA A O    1 
ATOM   1519  C CB   . ALA A 1 272  ? 141.021 96.669  137.609 1.00 13.96 ?  272  ALA A CB   1 
ATOM   1520  N N    . VAL A 1 273  ? 137.737 95.656  137.280 1.00 13.29 ?  273  VAL A N    1 
ATOM   1521  C CA   . VAL A 1 273  ? 136.882 94.771  136.498 1.00 11.80 ?  273  VAL A CA   1 
ATOM   1522  C C    . VAL A 1 273  ? 135.407 95.110  136.678 1.00 7.99  ?  273  VAL A C    1 
ATOM   1523  O O    . VAL A 1 273  ? 134.690 95.348  135.701 1.00 8.99  ?  273  VAL A O    1 
ATOM   1524  C CB   . VAL A 1 273  ? 137.143 93.286  136.840 1.00 12.78 ?  273  VAL A CB   1 
ATOM   1525  C CG1  . VAL A 1 273  ? 136.161 92.392  136.099 1.00 13.35 ?  273  VAL A CG1  1 
ATOM   1526  C CG2  . VAL A 1 273  ? 138.574 92.902  136.503 1.00 14.37 ?  273  VAL A CG2  1 
ATOM   1527  N N    . ALA A 1 274  ? 134.935 95.138  137.926 1.00 5.91  ?  274  ALA A N    1 
ATOM   1528  C CA   . ALA A 1 274  ? 133.503 95.254  138.182 1.00 5.81  ?  274  ALA A CA   1 
ATOM   1529  C C    . ALA A 1 274  ? 132.958 96.630  137.817 1.00 11.39 ?  274  ALA A C    1 
ATOM   1530  O O    . ALA A 1 274  ? 131.818 96.736  137.349 1.00 14.70 ?  274  ALA A O    1 
ATOM   1531  C CB   . ALA A 1 274  ? 133.211 94.937  139.647 1.00 6.84  ?  274  ALA A CB   1 
ATOM   1532  N N    . GLY A 1 275  ? 133.741 97.686  138.023 1.00 8.10  ?  275  GLY A N    1 
ATOM   1533  C CA   . GLY A 1 275  ? 133.325 99.031  137.697 1.00 3.41  ?  275  GLY A CA   1 
ATOM   1534  C C    . GLY A 1 275  ? 133.070 99.259  136.217 1.00 9.55  ?  275  GLY A C    1 
ATOM   1535  O O    . GLY A 1 275  ? 131.993 99.721  135.817 1.00 11.45 ?  275  GLY A O    1 
ATOM   1536  N N    . PRO A 1 276  ? 134.073 98.975  135.378 1.00 9.94  ?  276  PRO A N    1 
ATOM   1537  C CA   . PRO A 1 276  ? 133.843 99.025  133.925 1.00 3.58  ?  276  PRO A CA   1 
ATOM   1538  C C    . PRO A 1 276  ? 132.708 98.132  133.455 1.00 4.07  ?  276  PRO A C    1 
ATOM   1539  O O    . PRO A 1 276  ? 131.991 98.509  132.522 1.00 8.88  ?  276  PRO A O    1 
ATOM   1540  C CB   . PRO A 1 276  ? 135.187 98.574  133.335 1.00 2.37  ?  276  PRO A CB   1 
ATOM   1541  C CG   . PRO A 1 276  ? 136.178 98.597  134.460 1.00 2.03  ?  276  PRO A CG   1 
ATOM   1542  C CD   . PRO A 1 276  ? 135.505 99.059  135.708 1.00 4.01  ?  276  PRO A CD   1 
ATOM   1543  N N    . LEU A 1 277  ? 132.516 96.963  134.075 1.00 4.21  ?  277  LEU A N    1 
ATOM   1544  C CA   . LEU A 1 277  ? 131.387 96.109  133.715 1.00 1.13  ?  277  LEU A CA   1 
ATOM   1545  C C    . LEU A 1 277  ? 130.054 96.768  134.053 1.00 2.46  ?  277  LEU A C    1 
ATOM   1546  O O    . LEU A 1 277  ? 129.102 96.687  133.267 1.00 8.92  ?  277  LEU A O    1 
ATOM   1547  C CB   . LEU A 1 277  ? 131.504 94.757  134.415 1.00 4.30  ?  277  LEU A CB   1 
ATOM   1548  C CG   . LEU A 1 277  ? 131.930 93.564  133.557 1.00 6.42  ?  277  LEU A CG   1 
ATOM   1549  C CD1  . LEU A 1 277  ? 133.416 93.607  133.239 1.00 8.93  ?  277  LEU A CD1  1 
ATOM   1550  C CD2  . LEU A 1 277  ? 131.562 92.265  134.254 1.00 9.45  ?  277  LEU A CD2  1 
ATOM   1551  N N    . TRP A 1 278  ? 129.966 97.418  135.218 1.00 1.66  ?  278  TRP A N    1 
ATOM   1552  C CA   . TRP A 1 278  ? 128.746 98.134  135.585 1.00 2.92  ?  278  TRP A CA   1 
ATOM   1553  C C    . TRP A 1 278  ? 128.464 99.270  134.611 1.00 2.25  ?  278  TRP A C    1 
ATOM   1554  O O    . TRP A 1 278  ? 127.320 99.457  134.172 1.00 5.85  ?  278  TRP A O    1 
ATOM   1555  C CB   . TRP A 1 278  ? 128.864 98.667  137.014 1.00 5.02  ?  278  TRP A CB   1 
ATOM   1556  C CG   . TRP A 1 278  ? 127.848 99.717  137.369 1.00 5.25  ?  278  TRP A CG   1 
ATOM   1557  C CD1  . TRP A 1 278  ? 128.073 101.053 137.533 1.00 3.68  ?  278  TRP A CD1  1 
ATOM   1558  C CD2  . TRP A 1 278  ? 126.451 99.514  137.617 1.00 6.18  ?  278  TRP A CD2  1 
ATOM   1559  N NE1  . TRP A 1 278  ? 126.904 101.695 137.858 1.00 3.50  ?  278  TRP A NE1  1 
ATOM   1560  C CE2  . TRP A 1 278  ? 125.893 100.773 137.917 1.00 0.98  ?  278  TRP A CE2  1 
ATOM   1561  C CE3  . TRP A 1 278  ? 125.618 98.392  137.610 1.00 2.73  ?  278  TRP A CE3  1 
ATOM   1562  C CZ2  . TRP A 1 278  ? 124.541 100.940 138.206 1.00 0.00  ?  278  TRP A CZ2  1 
ATOM   1563  C CZ3  . TRP A 1 278  ? 124.276 98.560  137.899 1.00 3.50  ?  278  TRP A CZ3  1 
ATOM   1564  C CH2  . TRP A 1 278  ? 123.751 99.824  138.193 1.00 4.26  ?  278  TRP A CH2  1 
ATOM   1565  N N    . GLY A 1 279  ? 129.503 100.026 134.249 1.00 0.00  ?  279  GLY A N    1 
ATOM   1566  C CA   . GLY A 1 279  ? 129.328 101.098 133.282 1.00 0.00  ?  279  GLY A CA   1 
ATOM   1567  C C    . GLY A 1 279  ? 128.893 100.589 131.921 1.00 0.54  ?  279  GLY A C    1 
ATOM   1568  O O    . GLY A 1 279  ? 128.013 101.172 131.282 1.00 5.69  ?  279  GLY A O    1 
ATOM   1569  N N    . TYR A 1 280  ? 129.486 99.477  131.474 1.00 4.63  ?  280  TYR A N    1 
ATOM   1570  C CA   . TYR A 1 280  ? 129.121 98.875  130.196 1.00 0.00  ?  280  TYR A CA   1 
ATOM   1571  C C    . TYR A 1 280  ? 127.676 98.391  130.194 1.00 1.45  ?  280  TYR A C    1 
ATOM   1572  O O    . TYR A 1 280  ? 126.951 98.590  129.212 1.00 9.63  ?  280  TYR A O    1 
ATOM   1573  C CB   . TYR A 1 280  ? 130.080 97.725  129.884 1.00 2.92  ?  280  TYR A CB   1 
ATOM   1574  C CG   . TYR A 1 280  ? 129.701 96.885  128.684 1.00 5.90  ?  280  TYR A CG   1 
ATOM   1575  C CD1  . TYR A 1 280  ? 129.968 97.322  127.394 1.00 8.43  ?  280  TYR A CD1  1 
ATOM   1576  C CD2  . TYR A 1 280  ? 129.093 95.646  128.842 1.00 4.33  ?  280  TYR A CD2  1 
ATOM   1577  C CE1  . TYR A 1 280  ? 129.628 96.556  126.296 1.00 8.27  ?  280  TYR A CE1  1 
ATOM   1578  C CE2  . TYR A 1 280  ? 128.748 94.874  127.751 1.00 6.99  ?  280  TYR A CE2  1 
ATOM   1579  C CZ   . TYR A 1 280  ? 129.019 95.333  126.480 1.00 12.06 ?  280  TYR A CZ   1 
ATOM   1580  O OH   . TYR A 1 280  ? 128.679 94.568  125.389 1.00 17.64 ?  280  TYR A OH   1 
ATOM   1581  N N    . ALA A 1 281  ? 127.240 97.750  131.283 1.00 0.00  ?  281  ALA A N    1 
ATOM   1582  C CA   . ALA A 1 281  ? 125.866 97.261  131.356 1.00 0.00  ?  281  ALA A CA   1 
ATOM   1583  C C    . ALA A 1 281  ? 124.861 98.407  131.358 1.00 0.00  ?  281  ALA A C    1 
ATOM   1584  O O    . ALA A 1 281  ? 123.842 98.350  130.651 1.00 5.05  ?  281  ALA A O    1 
ATOM   1585  C CB   . ALA A 1 281  ? 125.686 96.389  132.597 1.00 0.10  ?  281  ALA A CB   1 
ATOM   1586  N N    . VAL A 1 282  ? 125.128 99.457  132.142 1.00 2.73  ?  282  VAL A N    1 
ATOM   1587  C CA   . VAL A 1 282  ? 124.221 100.601 132.170 1.00 1.07  ?  282  VAL A CA   1 
ATOM   1588  C C    . VAL A 1 282  ? 124.180 101.282 130.807 1.00 0.24  ?  282  VAL A C    1 
ATOM   1589  O O    . VAL A 1 282  ? 123.113 101.696 130.335 1.00 0.72  ?  282  VAL A O    1 
ATOM   1590  C CB   . VAL A 1 282  ? 124.622 101.579 133.290 1.00 0.00  ?  282  VAL A CB   1 
ATOM   1591  C CG1  . VAL A 1 282  ? 123.773 102.832 133.232 1.00 0.00  ?  282  VAL A CG1  1 
ATOM   1592  C CG2  . VAL A 1 282  ? 124.468 100.918 134.641 1.00 0.38  ?  282  VAL A CG2  1 
ATOM   1593  N N    . ALA A 1 283  ? 125.334 101.379 130.138 1.00 0.90  ?  283  ALA A N    1 
ATOM   1594  C CA   . ALA A 1 283  ? 125.379 101.970 128.805 1.00 0.00  ?  283  ALA A CA   1 
ATOM   1595  C C    . ALA A 1 283  ? 124.574 101.154 127.801 1.00 2.63  ?  283  ALA A C    1 
ATOM   1596  O O    . ALA A 1 283  ? 123.841 101.719 126.984 1.00 4.87  ?  283  ALA A O    1 
ATOM   1597  C CB   . ALA A 1 283  ? 126.830 102.105 128.349 1.00 0.00  ?  283  ALA A CB   1 
ATOM   1598  N N    . LYS A 1 284  ? 124.698 99.824  127.847 1.00 8.59  ?  284  LYS A N    1 
ATOM   1599  C CA   . LYS A 1 284  ? 123.941 98.972  126.932 1.00 1.41  ?  284  LYS A CA   1 
ATOM   1600  C C    . LYS A 1 284  ? 122.439 99.113  127.149 1.00 3.07  ?  284  LYS A C    1 
ATOM   1601  O O    . LYS A 1 284  ? 121.672 99.207  126.181 1.00 5.28  ?  284  LYS A O    1 
ATOM   1602  C CB   . LYS A 1 284  ? 124.372 97.516  127.097 1.00 0.00  ?  284  LYS A CB   1 
ATOM   1603  C CG   . LYS A 1 284  ? 125.646 97.165  126.358 1.00 0.78  ?  284  LYS A CG   1 
ATOM   1604  C CD   . LYS A 1 284  ? 125.524 97.501  124.882 1.00 3.40  ?  284  LYS A CD   1 
ATOM   1605  C CE   . LYS A 1 284  ? 126.873 97.819  124.269 1.00 1.68  ?  284  LYS A CE   1 
ATOM   1606  N NZ   . LYS A 1 284  ? 126.730 98.634  123.034 1.00 6.03  ?  284  LYS A NZ   1 
ATOM   1607  N N    . VAL A 1 285  ? 122.004 99.149  128.412 1.00 1.26  ?  285  VAL A N    1 
ATOM   1608  C CA   . VAL A 1 285  ? 120.581 99.334  128.698 1.00 0.00  ?  285  VAL A CA   1 
ATOM   1609  C C    . VAL A 1 285  ? 120.110 100.700 128.204 1.00 3.13  ?  285  VAL A C    1 
ATOM   1610  O O    . VAL A 1 285  ? 119.002 100.838 127.660 1.00 8.47  ?  285  VAL A O    1 
ATOM   1611  C CB   . VAL A 1 285  ? 120.313 99.142  130.203 1.00 3.14  ?  285  VAL A CB   1 
ATOM   1612  C CG1  . VAL A 1 285  ? 118.882 99.515  130.554 1.00 10.39 ?  285  VAL A CG1  1 
ATOM   1613  C CG2  . VAL A 1 285  ? 120.603 97.708  130.613 1.00 2.84  ?  285  VAL A CG2  1 
ATOM   1614  N N    . THR A 1 286  ? 120.951 101.727 128.366 1.00 3.98  ?  286  THR A N    1 
ATOM   1615  C CA   . THR A 1 286  ? 120.582 103.074 127.940 1.00 2.36  ?  286  THR A CA   1 
ATOM   1616  C C    . THR A 1 286  ? 120.411 103.159 126.426 1.00 2.03  ?  286  THR A C    1 
ATOM   1617  O O    . THR A 1 286  ? 119.444 103.750 125.940 1.00 3.66  ?  286  THR A O    1 
ATOM   1618  C CB   . THR A 1 286  ? 121.626 104.079 128.424 1.00 8.19  ?  286  THR A CB   1 
ATOM   1619  O OG1  . THR A 1 286  ? 121.837 103.905 129.830 1.00 9.64  ?  286  THR A OG1  1 
ATOM   1620  C CG2  . THR A 1 286  ? 121.157 105.503 128.163 1.00 4.83  ?  286  THR A CG2  1 
ATOM   1621  N N    . VAL A 1 287  ? 121.340 102.573 125.661 1.00 4.19  ?  287  VAL A N    1 
ATOM   1622  C CA   . VAL A 1 287  ? 121.185 102.577 124.203 1.00 0.00  ?  287  VAL A CA   1 
ATOM   1623  C C    . VAL A 1 287  ? 119.991 101.735 123.772 1.00 1.18  ?  287  VAL A C    1 
ATOM   1624  O O    . VAL A 1 287  ? 119.293 102.083 122.809 1.00 2.52  ?  287  VAL A O    1 
ATOM   1625  C CB   . VAL A 1 287  ? 122.473 102.130 123.486 1.00 4.55  ?  287  VAL A CB   1 
ATOM   1626  C CG1  . VAL A 1 287  ? 122.455 102.616 122.061 1.00 13.33 ?  287  VAL A CG1  1 
ATOM   1627  C CG2  . VAL A 1 287  ? 123.673 102.758 124.123 1.00 6.97  ?  287  VAL A CG2  1 
ATOM   1628  N N    . PHE A 1 288  ? 119.728 100.622 124.469 1.00 2.85  ?  288  PHE A N    1 
ATOM   1629  C CA   . PHE A 1 288  ? 118.567 99.807  124.119 1.00 0.00  ?  288  PHE A CA   1 
ATOM   1630  C C    . PHE A 1 288  ? 117.272 100.586 124.295 1.00 2.40  ?  288  PHE A C    1 
ATOM   1631  O O    . PHE A 1 288  ? 116.381 100.522 123.440 1.00 6.49  ?  288  PHE A O    1 
ATOM   1632  C CB   . PHE A 1 288  ? 118.525 98.531  124.958 1.00 7.88  ?  288  PHE A CB   1 
ATOM   1633  C CG   . PHE A 1 288  ? 117.208 97.807  124.879 1.00 9.11  ?  288  PHE A CG   1 
ATOM   1634  C CD1  . PHE A 1 288  ? 116.818 97.181  123.706 1.00 8.96  ?  288  PHE A CD1  1 
ATOM   1635  C CD2  . PHE A 1 288  ? 116.355 97.763  125.969 1.00 8.11  ?  288  PHE A CD2  1 
ATOM   1636  C CE1  . PHE A 1 288  ? 115.606 96.522  123.623 1.00 7.51  ?  288  PHE A CE1  1 
ATOM   1637  C CE2  . PHE A 1 288  ? 115.140 97.104  125.891 1.00 8.40  ?  288  PHE A CE2  1 
ATOM   1638  C CZ   . PHE A 1 288  ? 114.767 96.483  124.717 1.00 7.46  ?  288  PHE A CZ   1 
ATOM   1639  N N    . PHE A 1 289  ? 117.148 101.333 125.392 1.00 6.96  ?  289  PHE A N    1 
ATOM   1640  C CA   . PHE A 1 289  ? 115.930 102.112 125.590 1.00 2.92  ?  289  PHE A CA   1 
ATOM   1641  C C    . PHE A 1 289  ? 115.900 103.378 124.739 1.00 0.00  ?  289  PHE A C    1 
ATOM   1642  O O    . PHE A 1 289  ? 114.815 103.879 124.428 1.00 0.00  ?  289  PHE A O    1 
ATOM   1643  C CB   . PHE A 1 289  ? 115.755 102.451 127.069 1.00 3.30  ?  289  PHE A CB   1 
ATOM   1644  C CG   . PHE A 1 289  ? 115.149 101.334 127.871 1.00 10.70 ?  289  PHE A CG   1 
ATOM   1645  C CD1  . PHE A 1 289  ? 113.884 100.856 127.567 1.00 8.24  ?  289  PHE A CD1  1 
ATOM   1646  C CD2  . PHE A 1 289  ? 115.843 100.756 128.920 1.00 10.07 ?  289  PHE A CD2  1 
ATOM   1647  C CE1  . PHE A 1 289  ? 113.322 99.826  128.297 1.00 6.97  ?  289  PHE A CE1  1 
ATOM   1648  C CE2  . PHE A 1 289  ? 115.286 99.725  129.655 1.00 7.95  ?  289  PHE A CE2  1 
ATOM   1649  C CZ   . PHE A 1 289  ? 114.024 99.260  129.342 1.00 8.94  ?  289  PHE A CZ   1 
ATOM   1650  N N    . LEU A 1 290  ? 117.062 103.906 124.348 1.00 5.62  ?  290  LEU A N    1 
ATOM   1651  C CA   . LEU A 1 290  ? 117.095 105.095 123.504 1.00 1.22  ?  290  LEU A CA   1 
ATOM   1652  C C    . LEU A 1 290  ? 116.764 104.784 122.051 1.00 3.39  ?  290  LEU A C    1 
ATOM   1653  O O    . LEU A 1 290  ? 116.237 105.651 121.346 1.00 4.74  ?  290  LEU A O    1 
ATOM   1654  C CB   . LEU A 1 290  ? 118.468 105.766 123.587 1.00 1.33  ?  290  LEU A CB   1 
ATOM   1655  C CG   . LEU A 1 290  ? 118.718 106.748 124.734 1.00 0.00  ?  290  LEU A CG   1 
ATOM   1656  C CD1  . LEU A 1 290  ? 119.909 107.638 124.424 1.00 0.00  ?  290  LEU A CD1  1 
ATOM   1657  C CD2  . LEU A 1 290  ? 117.483 107.588 125.009 1.00 3.42  ?  290  LEU A CD2  1 
ATOM   1658  N N    . SER A 1 291  ? 117.063 103.569 121.586 1.00 8.25  ?  291  SER A N    1 
ATOM   1659  C CA   . SER A 1 291  ? 116.801 103.218 120.194 1.00 2.28  ?  291  SER A CA   1 
ATOM   1660  C C    . SER A 1 291  ? 115.316 103.123 119.865 1.00 7.20  ?  291  SER A C    1 
ATOM   1661  O O    . SER A 1 291  ? 114.965 103.119 118.681 1.00 8.37  ?  291  SER A O    1 
ATOM   1662  C CB   . SER A 1 291  ? 117.482 101.894 119.849 1.00 4.78  ?  291  SER A CB   1 
ATOM   1663  O OG   . SER A 1 291  ? 116.711 100.793 120.297 1.00 4.94  ?  291  SER A OG   1 
ATOM   1664  N N    . HIS A 1 292  ? 114.441 103.054 120.866 1.00 13.78 ?  292  HIS A N    1 
ATOM   1665  C CA   . HIS A 1 292  ? 113.011 102.892 120.649 1.00 6.53  ?  292  HIS A CA   1 
ATOM   1666  C C    . HIS A 1 292  ? 112.237 104.198 120.778 1.00 9.56  ?  292  HIS A C    1 
ATOM   1667  O O    . HIS A 1 292  ? 111.004 104.172 120.819 1.00 14.48 ?  292  HIS A O    1 
ATOM   1668  C CB   . HIS A 1 292  ? 112.448 101.856 121.622 1.00 4.53  ?  292  HIS A CB   1 
ATOM   1669  C CG   . HIS A 1 292  ? 112.828 100.448 121.286 1.00 13.77 ?  292  HIS A CG   1 
ATOM   1670  N ND1  . HIS A 1 292  ? 112.630 99.903  120.036 1.00 16.54 ?  292  HIS A ND1  1 
ATOM   1671  C CD2  . HIS A 1 292  ? 113.401 99.476  122.034 1.00 14.63 ?  292  HIS A CD2  1 
ATOM   1672  C CE1  . HIS A 1 292  ? 113.061 98.654  120.029 1.00 13.90 ?  292  HIS A CE1  1 
ATOM   1673  N NE2  . HIS A 1 292  ? 113.534 98.371  121.230 1.00 13.04 ?  292  HIS A NE2  1 
ATOM   1674  N N    . ILE A 1 293  ? 112.926 105.333 120.843 1.00 6.49  ?  293  ILE A N    1 
ATOM   1675  C CA   . ILE A 1 293  ? 112.293 106.640 120.984 1.00 4.41  ?  293  ILE A CA   1 
ATOM   1676  C C    . ILE A 1 293  ? 112.487 107.403 119.682 1.00 4.42  ?  293  ILE A C    1 
ATOM   1677  O O    . ILE A 1 293  ? 113.624 107.638 119.255 1.00 8.51  ?  293  ILE A O    1 
ATOM   1678  C CB   . ILE A 1 293  ? 112.866 107.422 122.175 1.00 11.13 ?  293  ILE A CB   1 
ATOM   1679  C CG1  . ILE A 1 293  ? 112.481 106.750 123.493 1.00 5.13  ?  293  ILE A CG1  1 
ATOM   1680  C CG2  . ILE A 1 293  ? 112.391 108.863 122.153 1.00 8.27  ?  293  ILE A CG2  1 
ATOM   1681  C CD1  . ILE A 1 293  ? 113.491 106.955 124.593 1.00 4.09  ?  293  ILE A CD1  1 
ATOM   1682  N N    . PHE A 1 294  ? 111.379 107.792 119.056 1.00 5.73  ?  294  PHE A N    1 
ATOM   1683  C CA   . PHE A 1 294  ? 111.391 108.525 117.798 1.00 6.46  ?  294  PHE A CA   1 
ATOM   1684  C C    . PHE A 1 294  ? 110.748 109.889 118.004 1.00 8.96  ?  294  PHE A C    1 
ATOM   1685  O O    . PHE A 1 294  ? 109.665 109.983 118.592 1.00 13.20 ?  294  PHE A O    1 
ATOM   1686  C CB   . PHE A 1 294  ? 110.651 107.752 116.700 1.00 10.10 ?  294  PHE A CB   1 
ATOM   1687  C CG   . PHE A 1 294  ? 111.149 106.347 116.501 1.00 12.07 ?  294  PHE A CG   1 
ATOM   1688  C CD1  . PHE A 1 294  ? 112.312 106.103 115.793 1.00 5.39  ?  294  PHE A CD1  1 
ATOM   1689  C CD2  . PHE A 1 294  ? 110.450 105.269 117.019 1.00 14.32 ?  294  PHE A CD2  1 
ATOM   1690  C CE1  . PHE A 1 294  ? 112.771 104.813 115.611 1.00 6.94  ?  294  PHE A CE1  1 
ATOM   1691  C CE2  . PHE A 1 294  ? 110.905 103.977 116.837 1.00 9.27  ?  294  PHE A CE2  1 
ATOM   1692  C CZ   . PHE A 1 294  ? 112.068 103.750 116.133 1.00 6.56  ?  294  PHE A CZ   1 
ATOM   1693  N N    . ASN A 1 295  ? 111.428 110.937 117.526 1.00 9.22  ?  295  ASN A N    1 
ATOM   1694  C CA   . ASN A 1 295  ? 110.917 112.312 117.528 1.00 12.24 ?  295  ASN A CA   1 
ATOM   1695  C C    . ASN A 1 295  ? 110.619 112.808 118.945 1.00 16.28 ?  295  ASN A C    1 
ATOM   1696  O O    . ASN A 1 295  ? 109.524 113.290 119.243 1.00 14.53 ?  295  ASN A O    1 
ATOM   1697  C CB   . ASN A 1 295  ? 109.684 112.444 116.628 1.00 16.76 ?  295  ASN A CB   1 
ATOM   1698  C CG   . ASN A 1 295  ? 109.452 113.867 116.160 1.00 19.80 ?  295  ASN A CG   1 
ATOM   1699  O OD1  . ASN A 1 295  ? 110.377 114.678 116.116 1.00 20.38 ?  295  ASN A OD1  1 
ATOM   1700  N ND2  . ASN A 1 295  ? 108.208 114.180 115.817 1.00 14.88 ?  295  ASN A ND2  1 
ATOM   1701  N N    . ASP A 1 296  ? 111.613 112.685 119.826 1.00 12.67 ?  296  ASP A N    1 
ATOM   1702  C CA   . ASP A 1 296  ? 111.496 113.205 121.189 1.00 6.05  ?  296  ASP A CA   1 
ATOM   1703  C C    . ASP A 1 296  ? 112.903 113.531 121.681 1.00 3.55  ?  296  ASP A C    1 
ATOM   1704  O O    . ASP A 1 296  ? 113.624 112.638 122.131 1.00 9.97  ?  296  ASP A O    1 
ATOM   1705  C CB   . ASP A 1 296  ? 110.805 112.203 122.103 1.00 8.93  ?  296  ASP A CB   1 
ATOM   1706  C CG   . ASP A 1 296  ? 109.731 112.841 122.958 1.00 14.38 ?  296  ASP A CG   1 
ATOM   1707  O OD1  . ASP A 1 296  ? 109.927 113.991 123.403 1.00 14.16 ?  296  ASP A OD1  1 
ATOM   1708  O OD2  . ASP A 1 296  ? 108.690 112.190 123.186 1.00 13.86 ?  296  ASP A OD2  1 
ATOM   1709  N N    . ALA A 1 297  ? 113.281 114.807 121.598 1.00 4.04  ?  297  ALA A N    1 
ATOM   1710  C CA   . ALA A 1 297  ? 114.608 115.214 122.047 1.00 0.00  ?  297  ALA A CA   1 
ATOM   1711  C C    . ALA A 1 297  ? 114.691 115.303 123.565 1.00 0.04  ?  297  ALA A C    1 
ATOM   1712  O O    . ALA A 1 297  ? 115.716 114.940 124.156 1.00 6.79  ?  297  ALA A O    1 
ATOM   1713  C CB   . ALA A 1 297  ? 114.987 116.553 121.416 1.00 0.00  ?  297  ALA A CB   1 
ATOM   1714  N N    . LEU A 1 298  ? 113.623 115.781 124.210 1.00 0.00  ?  298  LEU A N    1 
ATOM   1715  C CA   . LEU A 1 298  ? 113.639 115.959 125.658 1.00 0.00  ?  298  LEU A CA   1 
ATOM   1716  C C    . LEU A 1 298  ? 113.745 114.625 126.383 1.00 0.00  ?  298  LEU A C    1 
ATOM   1717  O O    . LEU A 1 298  ? 114.496 114.502 127.358 1.00 0.28  ?  298  LEU A O    1 
ATOM   1718  C CB   . LEU A 1 298  ? 112.386 116.710 126.105 1.00 0.94  ?  298  LEU A CB   1 
ATOM   1719  C CG   . LEU A 1 298  ? 112.255 118.173 125.675 1.00 0.00  ?  298  LEU A CG   1 
ATOM   1720  C CD1  . LEU A 1 298  ? 111.154 118.855 126.462 1.00 1.03  ?  298  LEU A CD1  1 
ATOM   1721  C CD2  . LEU A 1 298  ? 113.571 118.908 125.851 1.00 1.64  ?  298  LEU A CD2  1 
ATOM   1722  N N    . VAL A 1 299  ? 113.008 113.615 125.915 1.00 0.29  ?  299  VAL A N    1 
ATOM   1723  C CA   . VAL A 1 299  ? 113.049 112.298 126.545 1.00 0.79  ?  299  VAL A CA   1 
ATOM   1724  C C    . VAL A 1 299  ? 114.443 111.697 126.435 1.00 3.04  ?  299  VAL A C    1 
ATOM   1725  O O    . VAL A 1 299  ? 114.991 111.181 127.416 1.00 10.50 ?  299  VAL A O    1 
ATOM   1726  C CB   . VAL A 1 299  ? 111.985 111.375 125.924 1.00 0.00  ?  299  VAL A CB   1 
ATOM   1727  C CG1  . VAL A 1 299  ? 112.164 109.953 126.416 1.00 0.87  ?  299  VAL A CG1  1 
ATOM   1728  C CG2  . VAL A 1 299  ? 110.592 111.878 126.254 1.00 0.44  ?  299  VAL A CG2  1 
ATOM   1729  N N    . GLU A 1 300  ? 115.050 111.783 125.248 1.00 0.00  ?  300  GLU A N    1 
ATOM   1730  C CA   . GLU A 1 300  ? 116.391 111.242 125.050 1.00 0.00  ?  300  GLU A CA   1 
ATOM   1731  C C    . GLU A 1 300  ? 117.419 111.969 125.909 1.00 2.44  ?  300  GLU A C    1 
ATOM   1732  O O    . GLU A 1 300  ? 118.276 111.331 126.534 1.00 8.57  ?  300  GLU A O    1 
ATOM   1733  C CB   . GLU A 1 300  ? 116.770 111.326 123.571 1.00 0.00  ?  300  GLU A CB   1 
ATOM   1734  C CG   . GLU A 1 300  ? 115.929 110.443 122.659 1.00 7.99  ?  300  GLU A CG   1 
ATOM   1735  C CD   . GLU A 1 300  ? 116.587 110.188 121.315 1.00 9.45  ?  300  GLU A CD   1 
ATOM   1736  O OE1  . GLU A 1 300  ? 117.748 109.730 121.296 1.00 8.03  ?  300  GLU A OE1  1 
ATOM   1737  O OE2  . GLU A 1 300  ? 115.941 110.444 120.277 1.00 8.88  ?  300  GLU A OE2  1 
ATOM   1738  N N    . ILE A 1 301  ? 117.332 113.302 125.970 1.00 2.73  ?  301  ILE A N    1 
ATOM   1739  C CA   . ILE A 1 301  ? 118.299 114.087 126.736 1.00 0.00  ?  301  ILE A CA   1 
ATOM   1740  C C    . ILE A 1 301  ? 118.189 113.770 128.224 1.00 4.99  ?  301  ILE A C    1 
ATOM   1741  O O    . ILE A 1 301  ? 119.198 113.530 128.903 1.00 0.00  ?  301  ILE A O    1 
ATOM   1742  C CB   . ILE A 1 301  ? 118.100 115.589 126.461 1.00 0.00  ?  301  ILE A CB   1 
ATOM   1743  C CG1  . ILE A 1 301  ? 118.725 115.976 125.121 1.00 0.00  ?  301  ILE A CG1  1 
ATOM   1744  C CG2  . ILE A 1 301  ? 118.692 116.434 127.578 1.00 0.00  ?  301  ILE A CG2  1 
ATOM   1745  C CD1  . ILE A 1 301  ? 118.122 117.214 124.509 1.00 0.00  ?  301  ILE A CD1  1 
ATOM   1746  N N    . THR A 1 302  ? 116.959 113.737 128.748 1.00 3.22  ?  302  THR A N    1 
ATOM   1747  C CA   . THR A 1 302  ? 116.777 113.477 130.172 1.00 0.00  ?  302  THR A CA   1 
ATOM   1748  C C    . THR A 1 302  ? 117.144 112.044 130.533 1.00 0.00  ?  302  THR A C    1 
ATOM   1749  O O    . THR A 1 302  ? 117.721 111.804 131.598 1.00 7.68  ?  302  THR A O    1 
ATOM   1750  C CB   . THR A 1 302  ? 115.340 113.785 130.593 1.00 0.00  ?  302  THR A CB   1 
ATOM   1751  O OG1  . THR A 1 302  ? 114.428 113.023 129.794 1.00 0.00  ?  302  THR A OG1  1 
ATOM   1752  C CG2  . THR A 1 302  ? 115.042 115.272 130.447 1.00 2.33  ?  302  THR A CG2  1 
ATOM   1753  N N    . ILE A 1 303  ? 116.842 111.080 129.656 1.00 2.47  ?  303  ILE A N    1 
ATOM   1754  C CA   . ILE A 1 303  ? 117.217 109.694 129.919 1.00 0.00  ?  303  ILE A CA   1 
ATOM   1755  C C    . ILE A 1 303  ? 118.732 109.541 129.934 1.00 11.04 ?  303  ILE A C    1 
ATOM   1756  O O    . ILE A 1 303  ? 119.289 108.881 130.819 1.00 0.00  ?  303  ILE A O    1 
ATOM   1757  C CB   . ILE A 1 303  ? 116.553 108.757 128.891 1.00 2.39  ?  303  ILE A CB   1 
ATOM   1758  C CG1  . ILE A 1 303  ? 115.074 108.544 129.228 1.00 3.85  ?  303  ILE A CG1  1 
ATOM   1759  C CG2  . ILE A 1 303  ? 117.276 107.418 128.816 1.00 5.66  ?  303  ILE A CG2  1 
ATOM   1760  C CD1  . ILE A 1 303  ? 114.811 108.206 130.680 1.00 6.14  ?  303  ILE A CD1  1 
ATOM   1761  N N    . THR A 1 304  ? 119.426 110.166 128.976 1.00 0.00  ?  304  THR A N    1 
ATOM   1762  C CA   . THR A 1 304  ? 120.884 110.086 128.945 1.00 0.00  ?  304  THR A CA   1 
ATOM   1763  C C    . THR A 1 304  ? 121.507 110.721 130.184 1.00 6.70  ?  304  THR A C    1 
ATOM   1764  O O    . THR A 1 304  ? 122.416 110.143 130.798 1.00 8.78  ?  304  THR A O    1 
ATOM   1765  C CB   . THR A 1 304  ? 121.416 110.760 127.681 1.00 0.00  ?  304  THR A CB   1 
ATOM   1766  O OG1  . THR A 1 304  ? 120.549 110.467 126.579 1.00 0.54  ?  304  THR A OG1  1 
ATOM   1767  C CG2  . THR A 1 304  ? 122.813 110.261 127.363 1.00 0.16  ?  304  THR A CG2  1 
ATOM   1768  N N    . LEU A 1 305  ? 121.020 111.900 130.580 1.00 0.00  ?  305  LEU A N    1 
ATOM   1769  C CA   . LEU A 1 305  ? 121.600 112.583 131.733 1.00 0.00  ?  305  LEU A CA   1 
ATOM   1770  C C    . LEU A 1 305  ? 121.310 111.837 133.033 1.00 0.00  ?  305  LEU A C    1 
ATOM   1771  O O    . LEU A 1 305  ? 122.180 111.742 133.910 1.00 0.09  ?  305  LEU A O    1 
ATOM   1772  C CB   . LEU A 1 305  ? 121.080 114.017 131.799 1.00 0.00  ?  305  LEU A CB   1 
ATOM   1773  C CG   . LEU A 1 305  ? 121.640 114.979 130.747 1.00 2.51  ?  305  LEU A CG   1 
ATOM   1774  C CD1  . LEU A 1 305  ? 121.121 116.391 130.967 1.00 0.00  ?  305  LEU A CD1  1 
ATOM   1775  C CD2  . LEU A 1 305  ? 123.158 114.954 130.743 1.00 0.00  ?  305  LEU A CD2  1 
ATOM   1776  N N    . ALA A 1 306  ? 120.099 111.289 133.171 1.00 3.45  ?  306  ALA A N    1 
ATOM   1777  C CA   . ALA A 1 306  ? 119.765 110.518 134.363 1.00 0.00  ?  306  ALA A CA   1 
ATOM   1778  C C    . ALA A 1 306  ? 120.558 109.220 134.425 1.00 0.89  ?  306  ALA A C    1 
ATOM   1779  O O    . ALA A 1 306  ? 120.952 108.783 135.511 1.00 9.42  ?  306  ALA A O    1 
ATOM   1780  C CB   . ALA A 1 306  ? 118.265 110.236 134.397 1.00 0.00  ?  306  ALA A CB   1 
ATOM   1781  N N    . ALA A 1 307  ? 120.802 108.590 133.271 1.00 3.62  ?  307  ALA A N    1 
ATOM   1782  C CA   . ALA A 1 307  ? 121.653 107.406 133.238 1.00 0.00  ?  307  ALA A CA   1 
ATOM   1783  C C    . ALA A 1 307  ? 123.075 107.740 133.664 1.00 0.03  ?  307  ALA A C    1 
ATOM   1784  O O    . ALA A 1 307  ? 123.701 106.976 134.409 1.00 11.66 ?  307  ALA A O    1 
ATOM   1785  C CB   . ALA A 1 307  ? 121.643 106.794 131.839 1.00 0.00  ?  307  ALA A CB   1 
ATOM   1786  N N    . THR A 1 308  ? 123.594 108.885 133.208 1.00 3.06  ?  308  THR A N    1 
ATOM   1787  C CA   . THR A 1 308  ? 124.921 109.326 133.631 1.00 0.00  ?  308  THR A CA   1 
ATOM   1788  C C    . THR A 1 308  ? 124.984 109.524 135.142 1.00 0.00  ?  308  THR A C    1 
ATOM   1789  O O    . THR A 1 308  ? 125.909 109.035 135.807 1.00 2.04  ?  308  THR A O    1 
ATOM   1790  C CB   . THR A 1 308  ? 125.298 110.622 132.914 1.00 0.00  ?  308  THR A CB   1 
ATOM   1791  O OG1  . THR A 1 308  ? 125.114 110.464 131.502 1.00 4.53  ?  308  THR A OG1  1 
ATOM   1792  C CG2  . THR A 1 308  ? 126.742 110.984 133.197 1.00 0.00  ?  308  THR A CG2  1 
ATOM   1793  N N    . TYR A 1 309  ? 123.993 110.225 135.705 1.00 6.68  ?  309  TYR A N    1 
ATOM   1794  C CA   . TYR A 1 309  ? 123.998 110.451 137.149 1.00 0.00  ?  309  TYR A CA   1 
ATOM   1795  C C    . TYR A 1 309  ? 123.863 109.152 137.931 1.00 1.54  ?  309  TYR A C    1 
ATOM   1796  O O    . TYR A 1 309  ? 124.521 108.981 138.959 1.00 7.59  ?  309  TYR A O    1 
ATOM   1797  C CB   . TYR A 1 309  ? 122.892 111.413 137.581 1.00 0.00  ?  309  TYR A CB   1 
ATOM   1798  C CG   . TYR A 1 309  ? 122.860 111.551 139.092 1.00 0.00  ?  309  TYR A CG   1 
ATOM   1799  C CD1  . TYR A 1 309  ? 123.856 112.245 139.765 1.00 0.00  ?  309  TYR A CD1  1 
ATOM   1800  C CD2  . TYR A 1 309  ? 121.858 110.949 139.848 1.00 0.00  ?  309  TYR A CD2  1 
ATOM   1801  C CE1  . TYR A 1 309  ? 123.845 112.354 141.143 1.00 0.00  ?  309  TYR A CE1  1 
ATOM   1802  C CE2  . TYR A 1 309  ? 121.842 111.052 141.226 1.00 0.00  ?  309  TYR A CE2  1 
ATOM   1803  C CZ   . TYR A 1 309  ? 122.837 111.758 141.867 1.00 0.00  ?  309  TYR A CZ   1 
ATOM   1804  O OH   . TYR A 1 309  ? 122.827 111.869 143.238 1.00 0.00  ?  309  TYR A OH   1 
ATOM   1805  N N    . LEU A 1 310  ? 123.000 108.239 137.488 1.00 0.00  ?  310  LEU A N    1 
ATOM   1806  C CA   . LEU A 1 310  ? 122.787 107.023 138.265 1.00 0.00  ?  310  LEU A CA   1 
ATOM   1807  C C    . LEU A 1 310  ? 123.995 106.100 138.188 1.00 0.00  ?  310  LEU A C    1 
ATOM   1808  O O    . LEU A 1 310  ? 124.355 105.458 139.185 1.00 1.94  ?  310  LEU A O    1 
ATOM   1809  C CB   . LEU A 1 310  ? 121.518 106.316 137.798 1.00 0.00  ?  310  LEU A CB   1 
ATOM   1810  C CG   . LEU A 1 310  ? 120.244 107.022 138.269 1.00 0.00  ?  310  LEU A CG   1 
ATOM   1811  C CD1  . LEU A 1 310  ? 119.021 106.531 137.510 1.00 0.00  ?  310  LEU A CD1  1 
ATOM   1812  C CD2  . LEU A 1 310  ? 120.063 106.854 139.769 1.00 0.00  ?  310  LEU A CD2  1 
ATOM   1813  N N    . THR A 1 311  ? 124.650 106.043 137.024 1.00 3.43  ?  311  THR A N    1 
ATOM   1814  C CA   . THR A 1 311  ? 125.916 105.327 136.918 1.00 0.00  ?  311  THR A CA   1 
ATOM   1815  C C    . THR A 1 311  ? 126.946 105.907 137.874 1.00 2.08  ?  311  THR A C    1 
ATOM   1816  O O    . THR A 1 311  ? 127.597 105.167 138.625 1.00 10.89 ?  311  THR A O    1 
ATOM   1817  C CB   . THR A 1 311  ? 126.429 105.394 135.483 1.00 0.00  ?  311  THR A CB   1 
ATOM   1818  O OG1  . THR A 1 311  ? 125.323 105.284 134.584 1.00 4.50  ?  311  THR A OG1  1 
ATOM   1819  C CG2  . THR A 1 311  ? 127.406 104.266 135.215 1.00 3.81  ?  311  THR A CG2  1 
ATOM   1820  N N    . TYR A 1 312  ? 127.081 107.239 137.882 1.00 4.87  ?  312  TYR A N    1 
ATOM   1821  C CA   . TYR A 1 312  ? 128.039 107.878 138.777 1.00 0.61  ?  312  TYR A CA   1 
ATOM   1822  C C    . TYR A 1 312  ? 127.708 107.604 140.238 1.00 1.07  ?  312  TYR A C    1 
ATOM   1823  O O    . TYR A 1 312  ? 128.606 107.338 141.036 1.00 0.00  ?  312  TYR A O    1 
ATOM   1824  C CB   . TYR A 1 312  ? 128.088 109.384 138.522 1.00 2.48  ?  312  TYR A CB   1 
ATOM   1825  C CG   . TYR A 1 312  ? 128.561 110.175 139.723 1.00 1.02  ?  312  TYR A CG   1 
ATOM   1826  C CD1  . TYR A 1 312  ? 129.903 110.190 140.084 1.00 1.71  ?  312  TYR A CD1  1 
ATOM   1827  C CD2  . TYR A 1 312  ? 127.665 110.904 140.498 1.00 0.00  ?  312  TYR A CD2  1 
ATOM   1828  C CE1  . TYR A 1 312  ? 130.338 110.904 141.183 1.00 2.52  ?  312  TYR A CE1  1 
ATOM   1829  C CE2  . TYR A 1 312  ? 128.091 111.618 141.598 1.00 0.00  ?  312  TYR A CE2  1 
ATOM   1830  C CZ   . TYR A 1 312  ? 129.427 111.616 141.934 1.00 0.55  ?  312  TYR A CZ   1 
ATOM   1831  O OH   . TYR A 1 312  ? 129.854 112.331 143.027 1.00 2.28  ?  312  TYR A OH   1 
ATOM   1832  N N    . TYR A 1 313  ? 126.427 107.654 140.603 1.00 0.00  ?  313  TYR A N    1 
ATOM   1833  C CA   . TYR A 1 313  ? 126.035 107.510 142.002 1.00 0.00  ?  313  TYR A CA   1 
ATOM   1834  C C    . TYR A 1 313  ? 126.266 106.090 142.504 1.00 0.00  ?  313  TYR A C    1 
ATOM   1835  O O    . TYR A 1 313  ? 126.806 105.887 143.602 1.00 8.15  ?  313  TYR A O    1 
ATOM   1836  C CB   . TYR A 1 313  ? 124.568 107.907 142.168 1.00 0.00  ?  313  TYR A CB   1 
ATOM   1837  C CG   . TYR A 1 313  ? 124.021 107.729 143.566 1.00 1.73  ?  313  TYR A CG   1 
ATOM   1838  C CD1  . TYR A 1 313  ? 124.386 108.592 144.589 1.00 0.00  ?  313  TYR A CD1  1 
ATOM   1839  C CD2  . TYR A 1 313  ? 123.135 106.702 143.861 1.00 1.12  ?  313  TYR A CD2  1 
ATOM   1840  C CE1  . TYR A 1 313  ? 123.885 108.437 145.867 1.00 0.07  ?  313  TYR A CE1  1 
ATOM   1841  C CE2  . TYR A 1 313  ? 122.632 106.537 145.137 1.00 0.00  ?  313  TYR A CE2  1 
ATOM   1842  C CZ   . TYR A 1 313  ? 123.011 107.408 146.135 1.00 0.99  ?  313  TYR A CZ   1 
ATOM   1843  O OH   . TYR A 1 313  ? 122.512 107.250 147.407 1.00 3.98  ?  313  TYR A OH   1 
ATOM   1844  N N    . ILE A 1 314  ? 125.854 105.090 141.717 1.00 6.64  ?  314  ILE A N    1 
ATOM   1845  C CA   . ILE A 1 314  ? 126.034 103.705 142.139 1.00 0.34  ?  314  ILE A CA   1 
ATOM   1846  C C    . ILE A 1 314  ? 127.512 103.334 142.151 1.00 0.00  ?  314  ILE A C    1 
ATOM   1847  O O    . ILE A 1 314  ? 127.973 102.608 143.039 1.00 0.00  ?  314  ILE A O    1 
ATOM   1848  C CB   . ILE A 1 314  ? 125.208 102.758 141.250 1.00 0.00  ?  314  ILE A CB   1 
ATOM   1849  C CG1  . ILE A 1 314  ? 123.727 103.128 141.317 1.00 2.00  ?  314  ILE A CG1  1 
ATOM   1850  C CG2  . ILE A 1 314  ? 125.397 101.310 141.678 1.00 2.31  ?  314  ILE A CG2  1 
ATOM   1851  C CD1  . ILE A 1 314  ? 123.090 102.859 142.661 1.00 0.76  ?  314  ILE A CD1  1 
ATOM   1852  N N    . GLY A 1 315  ? 128.286 103.834 141.184 1.00 7.76  ?  315  GLY A N    1 
ATOM   1853  C CA   . GLY A 1 315  ? 129.723 103.630 141.242 1.00 0.52  ?  315  GLY A CA   1 
ATOM   1854  C C    . GLY A 1 315  ? 130.365 104.351 142.411 1.00 1.14  ?  315  GLY A C    1 
ATOM   1855  O O    . GLY A 1 315  ? 131.312 103.846 143.016 1.00 4.98  ?  315  GLY A O    1 
ATOM   1856  N N    . ASP A 1 316  ? 129.844 105.529 142.759 1.00 4.73  ?  316  ASP A N    1 
ATOM   1857  C CA   . ASP A 1 316  ? 130.446 106.352 143.799 1.00 1.48  ?  316  ASP A CA   1 
ATOM   1858  C C    . ASP A 1 316  ? 130.263 105.721 145.169 1.00 4.50  ?  316  ASP A C    1 
ATOM   1859  O O    . ASP A 1 316  ? 131.245 105.415 145.851 1.00 9.04  ?  316  ASP A O    1 
ATOM   1860  C CB   . ASP A 1 316  ? 129.840 107.757 143.760 1.00 1.36  ?  316  ASP A CB   1 
ATOM   1861  C CG   . ASP A 1 316  ? 130.093 108.537 145.034 1.00 6.32  ?  316  ASP A CG   1 
ATOM   1862  O OD1  . ASP A 1 316  ? 131.264 108.883 145.295 1.00 11.44 ?  316  ASP A OD1  1 
ATOM   1863  O OD2  . ASP A 1 316  ? 129.124 108.805 145.774 1.00 4.99  ?  316  ASP A OD2  1 
ATOM   1864  N N    . ILE A 1 317  ? 129.014 105.447 145.557 1.00 6.49  ?  317  ILE A N    1 
ATOM   1865  C CA   . ILE A 1 317  ? 128.731 104.940 146.898 1.00 2.21  ?  317  ILE A CA   1 
ATOM   1866  C C    . ILE A 1 317  ? 129.350 103.574 147.170 1.00 6.35  ?  317  ILE A C    1 
ATOM   1867  O O    . ILE A 1 317  ? 129.305 103.098 148.307 1.00 10.77 ?  317  ILE A O    1 
ATOM   1868  C CB   . ILE A 1 317  ? 127.209 104.871 147.152 1.00 0.00  ?  317  ILE A CB   1 
ATOM   1869  C CG1  . ILE A 1 317  ? 126.583 103.737 146.338 1.00 0.00  ?  317  ILE A CG1  1 
ATOM   1870  C CG2  . ILE A 1 317  ? 126.554 106.207 146.848 1.00 6.91  ?  317  ILE A CG2  1 
ATOM   1871  C CD1  . ILE A 1 317  ? 125.249 103.275 146.869 1.00 0.00  ?  317  ILE A CD1  1 
ATOM   1872  N N    . TRP A 1 318  ? 129.937 102.941 146.159 1.00 6.91  ?  318  TRP A N    1 
ATOM   1873  C CA   . TRP A 1 318  ? 130.534 101.618 146.261 1.00 3.49  ?  318  TRP A CA   1 
ATOM   1874  C C    . TRP A 1 318  ? 132.047 101.634 146.093 1.00 5.53  ?  318  TRP A C    1 
ATOM   1875  O O    . TRP A 1 318  ? 132.742 100.883 146.779 1.00 9.86  ?  318  TRP A O    1 
ATOM   1876  C CB   . TRP A 1 318  ? 129.879 100.700 145.216 1.00 1.82  ?  318  TRP A CB   1 
ATOM   1877  C CG   . TRP A 1 318  ? 130.574 99.416  144.845 1.00 3.19  ?  318  TRP A CG   1 
ATOM   1878  C CD1  . TRP A 1 318  ? 131.247 98.560  145.670 1.00 6.03  ?  318  TRP A CD1  1 
ATOM   1879  C CD2  . TRP A 1 318  ? 130.619 98.830  143.541 1.00 6.97  ?  318  TRP A CD2  1 
ATOM   1880  N NE1  . TRP A 1 318  ? 131.724 97.490  144.954 1.00 6.20  ?  318  TRP A NE1  1 
ATOM   1881  C CE2  . TRP A 1 318  ? 131.349 97.632  143.644 1.00 3.14  ?  318  TRP A CE2  1 
ATOM   1882  C CE3  . TRP A 1 318  ? 130.118 99.209  142.292 1.00 9.24  ?  318  TRP A CE3  1 
ATOM   1883  C CZ2  . TRP A 1 318  ? 131.590 96.810  142.548 1.00 5.37  ?  318  TRP A CZ2  1 
ATOM   1884  C CZ3  . TRP A 1 318  ? 130.358 98.394  141.207 1.00 7.12  ?  318  TRP A CZ3  1 
ATOM   1885  C CH2  . TRP A 1 318  ? 131.087 97.208  141.341 1.00 6.13  ?  318  TRP A CH2  1 
ATOM   1886  N N    . LEU A 1 319  ? 132.592 102.495 145.229 1.00 6.56  ?  319  LEU A N    1 
ATOM   1887  C CA   . LEU A 1 319  ? 134.020 102.495 144.949 1.00 6.02  ?  319  LEU A CA   1 
ATOM   1888  C C    . LEU A 1 319  ? 134.724 103.808 145.265 1.00 9.63  ?  319  LEU A C    1 
ATOM   1889  O O    . LEU A 1 319  ? 135.912 103.931 144.946 1.00 10.46 ?  319  LEU A O    1 
ATOM   1890  C CB   . LEU A 1 319  ? 134.267 102.146 143.473 1.00 7.86  ?  319  LEU A CB   1 
ATOM   1891  C CG   . LEU A 1 319  ? 133.724 100.820 142.941 1.00 7.29  ?  319  LEU A CG   1 
ATOM   1892  C CD1  . LEU A 1 319  ? 133.330 100.961 141.480 1.00 3.51  ?  319  LEU A CD1  1 
ATOM   1893  C CD2  . LEU A 1 319  ? 134.741 99.705  143.120 1.00 13.05 ?  319  LEU A CD2  1 
ATOM   1894  N N    . GLU A 1 320  ? 134.044 104.779 145.882 1.00 12.00 ?  320  GLU A N    1 
ATOM   1895  C CA   . GLU A 1 320  ? 134.574 106.126 146.151 1.00 10.16 ?  320  GLU A CA   1 
ATOM   1896  C C    . GLU A 1 320  ? 134.983 106.742 144.814 1.00 9.08  ?  320  GLU A C    1 
ATOM   1897  O O    . GLU A 1 320  ? 134.166 106.754 143.880 1.00 8.59  ?  320  GLU A O    1 
ATOM   1898  C CB   . GLU A 1 320  ? 135.657 106.066 147.224 1.00 13.21 ?  320  GLU A CB   1 
ATOM   1899  C CG   . GLU A 1 320  ? 135.214 105.340 148.485 1.00 11.30 ?  320  GLU A CG   1 
ATOM   1900  C CD   . GLU A 1 320  ? 134.043 106.022 149.175 1.00 14.86 ?  320  GLU A CD   1 
ATOM   1901  O OE1  . GLU A 1 320  ? 133.941 107.266 149.106 1.00 14.23 ?  320  GLU A OE1  1 
ATOM   1902  O OE2  . GLU A 1 320  ? 133.215 105.309 149.782 1.00 15.79 ?  320  GLU A OE2  1 
ATOM   1903  N N    . VAL A 1 321  ? 136.211 107.249 144.665 1.00 8.88  ?  321  VAL A N    1 
ATOM   1904  C CA   . VAL A 1 321  ? 136.582 107.991 143.461 1.00 10.49 ?  321  VAL A CA   1 
ATOM   1905  C C    . VAL A 1 321  ? 136.988 107.065 142.321 1.00 13.58 ?  321  VAL A C    1 
ATOM   1906  O O    . VAL A 1 321  ? 137.290 107.537 141.217 1.00 15.30 ?  321  VAL A O    1 
ATOM   1907  C CB   . VAL A 1 321  ? 137.668 109.006 143.884 1.00 7.35  ?  321  VAL A CB   1 
ATOM   1908  C CG1  . VAL A 1 321  ? 137.947 110.060 142.806 1.00 12.35 ?  321  VAL A CG1  1 
ATOM   1909  C CG2  . VAL A 1 321  ? 137.278 109.676 145.192 1.00 6.71  ?  321  VAL A CG2  1 
ATOM   1910  N N    . SER A 1 322  ? 136.956 105.751 142.532 1.00 10.75 ?  322  SER A N    1 
ATOM   1911  C CA   . SER A 1 322  ? 137.286 104.789 141.489 1.00 6.45  ?  322  SER A CA   1 
ATOM   1912  C C    . SER A 1 322  ? 136.080 104.381 140.646 1.00 10.18 ?  322  SER A C    1 
ATOM   1913  O O    . SER A 1 322  ? 136.147 103.365 139.947 1.00 12.48 ?  322  SER A O    1 
ATOM   1914  C CB   . SER A 1 322  ? 137.937 103.548 142.103 1.00 12.31 ?  322  SER A CB   1 
ATOM   1915  O OG   . SER A 1 322  ? 139.071 103.898 142.877 1.00 9.95  ?  322  SER A OG   1 
ATOM   1916  N N    . GLY A 1 323  ? 134.980 105.132 140.707 1.00 10.13 ?  323  GLY A N    1 
ATOM   1917  C CA   . GLY A 1 323  ? 133.885 104.983 139.766 1.00 9.45  ?  323  GLY A CA   1 
ATOM   1918  C C    . GLY A 1 323  ? 134.067 105.760 138.484 1.00 7.17  ?  323  GLY A C    1 
ATOM   1919  O O    . GLY A 1 323  ? 133.223 105.710 137.577 1.00 14.99 ?  323  GLY A O    1 
ATOM   1920  N N    . VAL A 1 324  ? 135.178 106.496 138.398 1.00 4.34  ?  324  VAL A N    1 
ATOM   1921  C CA   . VAL A 1 324  ? 135.511 107.220 137.181 1.00 6.56  ?  324  VAL A CA   1 
ATOM   1922  C C    . VAL A 1 324  ? 135.751 106.253 136.033 1.00 10.98 ?  324  VAL A C    1 
ATOM   1923  O O    . VAL A 1 324  ? 135.484 106.586 134.876 1.00 15.46 ?  324  VAL A O    1 
ATOM   1924  C CB   . VAL A 1 324  ? 136.722 108.142 137.421 1.00 6.26  ?  324  VAL A CB   1 
ATOM   1925  C CG1  . VAL A 1 324  ? 136.356 109.244 138.400 1.00 6.94  ?  324  VAL A CG1  1 
ATOM   1926  C CG2  . VAL A 1 324  ? 137.911 107.347 137.944 1.00 5.45  ?  324  VAL A CG2  1 
ATOM   1927  N N    . LEU A 1 325  ? 136.230 105.041 136.325 1.00 6.88  ?  325  LEU A N    1 
ATOM   1928  C CA   . LEU A 1 325  ? 136.377 104.031 135.282 1.00 0.00  ?  325  LEU A CA   1 
ATOM   1929  C C    . LEU A 1 325  ? 135.021 103.623 134.718 1.00 0.00  ?  325  LEU A C    1 
ATOM   1930  O O    . LEU A 1 325  ? 134.859 103.488 133.498 1.00 4.24  ?  325  LEU A O    1 
ATOM   1931  C CB   . LEU A 1 325  ? 137.117 102.816 135.838 1.00 1.94  ?  325  LEU A CB   1 
ATOM   1932  C CG   . LEU A 1 325  ? 138.630 102.947 136.020 1.00 0.00  ?  325  LEU A CG   1 
ATOM   1933  C CD1  . LEU A 1 325  ? 139.277 101.574 136.118 1.00 4.30  ?  325  LEU A CD1  1 
ATOM   1934  C CD2  . LEU A 1 325  ? 139.259 103.764 134.901 1.00 1.82  ?  325  LEU A CD2  1 
ATOM   1935  N N    . ALA A 1 326  ? 134.031 103.441 135.597 1.00 0.00  ?  326  ALA A N    1 
ATOM   1936  C CA   . ALA A 1 326  ? 132.682 103.109 135.152 1.00 0.00  ?  326  ALA A CA   1 
ATOM   1937  C C    . ALA A 1 326  ? 132.092 104.222 134.302 1.00 0.00  ?  326  ALA A C    1 
ATOM   1938  O O    . ALA A 1 326  ? 131.487 103.964 133.252 1.00 1.05  ?  326  ALA A O    1 
ATOM   1939  C CB   . ALA A 1 326  ? 131.787 102.841 136.361 1.00 3.85  ?  326  ALA A CB   1 
ATOM   1940  N N    . VAL A 1 327  ? 132.273 105.473 134.729 1.00 6.06  ?  327  VAL A N    1 
ATOM   1941  C CA   . VAL A 1 327  ? 131.662 106.563 133.975 1.00 5.17  ?  327  VAL A CA   1 
ATOM   1942  C C    . VAL A 1 327  ? 132.419 106.808 132.666 1.00 2.62  ?  327  VAL A C    1 
ATOM   1943  O O    . VAL A 1 327  ? 131.819 107.218 131.664 1.00 4.68  ?  327  VAL A O    1 
ATOM   1944  C CB   . VAL A 1 327  ? 131.548 107.829 134.850 1.00 1.63  ?  327  VAL A CB   1 
ATOM   1945  C CG1  . VAL A 1 327  ? 132.863 108.595 134.928 1.00 4.48  ?  327  VAL A CG1  1 
ATOM   1946  C CG2  . VAL A 1 327  ? 130.409 108.707 134.368 1.00 0.00  ?  327  VAL A CG2  1 
ATOM   1947  N N    . VAL A 1 328  ? 133.723 106.508 132.629 1.00 0.00  ?  328  VAL A N    1 
ATOM   1948  C CA   . VAL A 1 328  ? 134.485 106.572 131.385 1.00 0.00  ?  328  VAL A CA   1 
ATOM   1949  C C    . VAL A 1 328  ? 133.990 105.524 130.400 1.00 0.81  ?  328  VAL A C    1 
ATOM   1950  O O    . VAL A 1 328  ? 133.816 105.806 129.207 1.00 3.03  ?  328  VAL A O    1 
ATOM   1951  C CB   . VAL A 1 328  ? 135.988 106.407 131.680 1.00 0.00  ?  328  VAL A CB   1 
ATOM   1952  C CG1  . VAL A 1 328  ? 136.730 105.836 130.480 1.00 0.00  ?  328  VAL A CG1  1 
ATOM   1953  C CG2  . VAL A 1 328  ? 136.581 107.728 132.056 1.00 2.72  ?  328  VAL A CG2  1 
ATOM   1954  N N    . VAL A 1 329  ? 133.765 104.299 130.882 1.00 4.05  ?  329  VAL A N    1 
ATOM   1955  C CA   . VAL A 1 329  ? 133.254 103.239 130.020 1.00 0.00  ?  329  VAL A CA   1 
ATOM   1956  C C    . VAL A 1 329  ? 131.875 103.607 129.489 1.00 5.03  ?  329  VAL A C    1 
ATOM   1957  O O    . VAL A 1 329  ? 131.575 103.399 128.306 1.00 0.00  ?  329  VAL A O    1 
ATOM   1958  C CB   . VAL A 1 329  ? 133.240 101.900 130.780 1.00 0.00  ?  329  VAL A CB   1 
ATOM   1959  C CG1  . VAL A 1 329  ? 132.407 100.867 130.045 1.00 1.29  ?  329  VAL A CG1  1 
ATOM   1960  C CG2  . VAL A 1 329  ? 134.657 101.397 130.980 1.00 0.00  ?  329  VAL A CG2  1 
ATOM   1961  N N    . LEU A 1 330  ? 131.024 104.181 130.346 1.00 0.00  ?  330  LEU A N    1 
ATOM   1962  C CA   . LEU A 1 330  ? 129.707 104.620 129.890 1.00 2.62  ?  330  LEU A CA   1 
ATOM   1963  C C    . LEU A 1 330  ? 129.819 105.693 128.816 1.00 0.00  ?  330  LEU A C    1 
ATOM   1964  O O    . LEU A 1 330  ? 129.113 105.637 127.801 1.00 0.00  ?  330  LEU A O    1 
ATOM   1965  C CB   . LEU A 1 330  ? 128.875 105.128 131.067 1.00 0.00  ?  330  LEU A CB   1 
ATOM   1966  C CG   . LEU A 1 330  ? 127.485 105.653 130.692 1.00 0.00  ?  330  LEU A CG   1 
ATOM   1967  C CD1  . LEU A 1 330  ? 126.427 105.016 131.557 1.00 0.00  ?  330  LEU A CD1  1 
ATOM   1968  C CD2  . LEU A 1 330  ? 127.416 107.170 130.820 1.00 2.11  ?  330  LEU A CD2  1 
ATOM   1969  N N    . GLY A 1 331  ? 130.709 106.670 129.014 1.00 0.00  ?  331  GLY A N    1 
ATOM   1970  C CA   . GLY A 1 331  ? 130.882 107.713 128.017 1.00 1.58  ?  331  GLY A CA   1 
ATOM   1971  C C    . GLY A 1 331  ? 131.369 107.178 126.685 1.00 0.00  ?  331  GLY A C    1 
ATOM   1972  O O    . GLY A 1 331  ? 130.834 107.534 125.632 1.00 1.79  ?  331  GLY A O    1 
ATOM   1973  N N    . LEU A 1 332  ? 132.367 106.289 126.716 1.00 3.42  ?  332  LEU A N    1 
ATOM   1974  C CA   . LEU A 1 332  ? 132.900 105.721 125.479 1.00 0.00  ?  332  LEU A CA   1 
ATOM   1975  C C    . LEU A 1 332  ? 131.860 104.873 124.753 1.00 0.34  ?  332  LEU A C    1 
ATOM   1976  O O    . LEU A 1 332  ? 131.711 104.982 123.529 1.00 5.83  ?  332  LEU A O    1 
ATOM   1977  C CB   . LEU A 1 332  ? 134.150 104.889 125.770 1.00 0.00  ?  332  LEU A CB   1 
ATOM   1978  C CG   . LEU A 1 332  ? 135.366 105.595 126.375 1.00 0.00  ?  332  LEU A CG   1 
ATOM   1979  C CD1  . LEU A 1 332  ? 136.390 104.578 126.857 1.00 0.00  ?  332  LEU A CD1  1 
ATOM   1980  C CD2  . LEU A 1 332  ? 135.988 106.565 125.391 1.00 0.91  ?  332  LEU A CD2  1 
ATOM   1981  N N    . ILE A 1 333  ? 131.123 104.032 125.486 1.00 2.60  ?  333  ILE A N    1 
ATOM   1982  C CA   . ILE A 1 333  ? 130.157 103.146 124.843 1.00 0.00  ?  333  ILE A CA   1 
ATOM   1983  C C    . ILE A 1 333  ? 128.982 103.942 124.285 1.00 0.00  ?  333  ILE A C    1 
ATOM   1984  O O    . ILE A 1 333  ? 128.487 103.651 123.190 1.00 8.11  ?  333  ILE A O    1 
ATOM   1985  C CB   . ILE A 1 333  ? 129.698 102.050 125.823 1.00 0.00  ?  333  ILE A CB   1 
ATOM   1986  C CG1  . ILE A 1 333  ? 130.870 101.137 126.188 1.00 0.00  ?  333  ILE A CG1  1 
ATOM   1987  C CG2  . ILE A 1 333  ? 128.586 101.210 125.218 1.00 2.30  ?  333  ILE A CG2  1 
ATOM   1988  C CD1  . ILE A 1 333  ? 131.426 100.352 125.025 1.00 3.87  ?  333  ILE A CD1  1 
ATOM   1989  N N    . VAL A 1 334  ? 128.527 104.968 125.010 1.00 1.78  ?  334  VAL A N    1 
ATOM   1990  C CA   . VAL A 1 334  ? 127.435 105.797 124.508 1.00 1.01  ?  334  VAL A CA   1 
ATOM   1991  C C    . VAL A 1 334  ? 127.887 106.599 123.292 1.00 6.81  ?  334  VAL A C    1 
ATOM   1992  O O    . VAL A 1 334  ? 127.133 106.758 122.323 1.00 7.79  ?  334  VAL A O    1 
ATOM   1993  C CB   . VAL A 1 334  ? 126.900 106.698 125.639 1.00 2.03  ?  334  VAL A CB   1 
ATOM   1994  C CG1  . VAL A 1 334  ? 126.144 107.901 125.088 1.00 0.00  ?  334  VAL A CG1  1 
ATOM   1995  C CG2  . VAL A 1 334  ? 126.007 105.892 126.567 1.00 1.77  ?  334  VAL A CG2  1 
ATOM   1996  N N    . ASN A 1 335  ? 129.131 107.090 123.303 1.00 10.08 ?  335  ASN A N    1 
ATOM   1997  C CA   . ASN A 1 335  ? 129.648 107.825 122.154 1.00 8.40  ?  335  ASN A CA   1 
ATOM   1998  C C    . ASN A 1 335  ? 129.782 106.929 120.929 1.00 12.41 ?  335  ASN A C    1 
ATOM   1999  O O    . ASN A 1 335  ? 129.565 107.380 119.798 1.00 13.36 ?  335  ASN A O    1 
ATOM   2000  C CB   . ASN A 1 335  ? 130.995 108.457 122.498 1.00 7.61  ?  335  ASN A CB   1 
ATOM   2001  C CG   . ASN A 1 335  ? 131.325 109.637 121.614 1.00 8.26  ?  335  ASN A CG   1 
ATOM   2002  O OD1  . ASN A 1 335  ? 132.245 109.579 120.802 1.00 16.04 ?  335  ASN A OD1  1 
ATOM   2003  N ND2  . ASN A 1 335  ? 130.577 110.721 121.771 1.00 7.30  ?  335  ASN A ND2  1 
ATOM   2004  N N    . ALA A 1 336  ? 130.161 105.663 121.130 1.00 14.34 ?  336  ALA A N    1 
ATOM   2005  C CA   . ALA A 1 336  ? 130.283 104.740 120.005 1.00 10.74 ?  336  ALA A CA   1 
ATOM   2006  C C    . ALA A 1 336  ? 128.934 104.480 119.345 1.00 14.49 ?  336  ALA A C    1 
ATOM   2007  O O    . ALA A 1 336  ? 128.834 104.441 118.113 1.00 14.51 ?  336  ALA A O    1 
ATOM   2008  C CB   . ALA A 1 336  ? 130.915 103.428 120.467 1.00 8.76  ?  336  ALA A CB   1 
ATOM   2009  N N    . GLU A 1 337  ? 127.884 104.301 120.146 1.00 18.69 ?  337  GLU A N    1 
ATOM   2010  C CA   . GLU A 1 337  ? 126.547 104.023 119.622 1.00 14.82 ?  337  GLU A CA   1 
ATOM   2011  C C    . GLU A 1 337  ? 125.777 105.334 119.455 1.00 13.26 ?  337  GLU A C    1 
ATOM   2012  O O    . GLU A 1 337  ? 124.820 105.639 120.169 1.00 14.48 ?  337  GLU A O    1 
ATOM   2013  C CB   . GLU A 1 337  ? 125.815 103.046 120.533 1.00 12.52 ?  337  GLU A CB   1 
ATOM   2014  C CG   . GLU A 1 337  ? 125.988 101.584 120.141 1.00 16.46 ?  337  GLU A CG   1 
ATOM   2015  C CD   . GLU A 1 337  ? 127.194 100.929 120.792 1.00 19.68 ?  337  GLU A CD   1 
ATOM   2016  O OE1  . GLU A 1 337  ? 128.166 101.640 121.120 1.00 19.20 ?  337  GLU A OE1  1 
ATOM   2017  O OE2  . GLU A 1 337  ? 127.173 99.693  120.970 1.00 20.38 ?  337  GLU A OE2  1 
ATOM   2018  N N    . LYS A 1 338  ? 126.222 106.117 118.474 1.00 12.65 ?  338  LYS A N    1 
ATOM   2019  C CA   . LYS A 1 338  ? 125.627 107.414 118.188 1.00 11.63 ?  338  LYS A CA   1 
ATOM   2020  C C    . LYS A 1 338  ? 124.461 107.341 117.211 1.00 13.12 ?  338  LYS A C    1 
ATOM   2021  O O    . LYS A 1 338  ? 123.767 108.346 117.027 1.00 10.82 ?  338  LYS A O    1 
ATOM   2022  C CB   . LYS A 1 338  ? 126.690 108.369 117.633 1.00 11.27 ?  338  LYS A CB   1 
ATOM   2023  C CG   . LYS A 1 338  ? 127.081 109.496 118.576 1.00 13.86 ?  338  LYS A CG   1 
ATOM   2024  C CD   . LYS A 1 338  ? 128.074 110.441 117.916 1.00 12.88 ?  338  LYS A CD   1 
ATOM   2025  C CE   . LYS A 1 338  ? 128.528 111.528 118.876 1.00 15.17 ?  338  LYS A CE   1 
ATOM   2026  N NZ   . LYS A 1 338  ? 128.310 112.890 118.316 1.00 13.58 ?  338  LYS A NZ   1 
ATOM   2027  N N    . THR A 1 339  ? 124.226 106.187 116.581 1.00 16.49 ?  339  THR A N    1 
ATOM   2028  C CA   . THR A 1 339  ? 123.139 106.071 115.617 1.00 11.63 ?  339  THR A CA   1 
ATOM   2029  C C    . THR A 1 339  ? 121.773 105.943 116.277 1.00 13.10 ?  339  THR A C    1 
ATOM   2030  O O    . THR A 1 339  ? 120.757 106.186 115.617 1.00 14.31 ?  339  THR A O    1 
ATOM   2031  C CB   . THR A 1 339  ? 123.377 104.881 114.682 1.00 9.75  ?  339  THR A CB   1 
ATOM   2032  O OG1  . THR A 1 339  ? 122.398 104.890 113.635 1.00 12.41 ?  339  THR A OG1  1 
ATOM   2033  C CG2  . THR A 1 339  ? 123.295 103.563 115.442 1.00 13.74 ?  339  THR A CG2  1 
ATOM   2034  N N    . SER A 1 340  ? 121.720 105.576 117.555 1.00 13.94 ?  340  SER A N    1 
ATOM   2035  C CA   . SER A 1 340  ? 120.471 105.556 118.302 1.00 13.34 ?  340  SER A CA   1 
ATOM   2036  C C    . SER A 1 340  ? 120.146 106.907 118.918 1.00 8.86  ?  340  SER A C    1 
ATOM   2037  O O    . SER A 1 340  ? 119.124 107.036 119.599 1.00 10.52 ?  340  SER A O    1 
ATOM   2038  C CB   . SER A 1 340  ? 120.528 104.501 119.407 1.00 11.74 ?  340  SER A CB   1 
ATOM   2039  O OG   . SER A 1 340  ? 121.006 105.078 120.608 1.00 8.72  ?  340  SER A OG   1 
ATOM   2040  N N    . ILE A 1 341  ? 120.994 107.907 118.700 1.00 9.74  ?  341  ILE A N    1 
ATOM   2041  C CA   . ILE A 1 341  ? 120.842 109.233 119.279 1.00 11.91 ?  341  ILE A CA   1 
ATOM   2042  C C    . ILE A 1 341  ? 120.717 110.230 118.135 1.00 16.11 ?  341  ILE A C    1 
ATOM   2043  O O    . ILE A 1 341  ? 121.538 110.223 117.211 1.00 21.53 ?  341  ILE A O    1 
ATOM   2044  C CB   . ILE A 1 341  ? 122.032 109.579 120.195 1.00 12.73 ?  341  ILE A CB   1 
ATOM   2045  C CG1  . ILE A 1 341  ? 121.997 108.723 121.462 1.00 17.16 ?  341  ILE A CG1  1 
ATOM   2046  C CG2  . ILE A 1 341  ? 122.027 111.039 120.563 1.00 8.11  ?  341  ILE A CG2  1 
ATOM   2047  C CD1  . ILE A 1 341  ? 123.283 108.760 122.258 1.00 10.60 ?  341  ILE A CD1  1 
ATOM   2048  N N    . SER A 1 342  ? 119.680 111.063 118.187 1.00 10.70 ?  342  SER A N    1 
ATOM   2049  C CA   . SER A 1 342  ? 119.464 112.058 117.149 1.00 7.87  ?  342  SER A CA   1 
ATOM   2050  C C    . SER A 1 342  ? 120.603 113.078 117.153 1.00 14.69 ?  342  SER A C    1 
ATOM   2051  O O    . SER A 1 342  ? 121.158 113.388 118.210 1.00 20.62 ?  342  SER A O    1 
ATOM   2052  C CB   . SER A 1 342  ? 118.125 112.761 117.364 1.00 11.16 ?  342  SER A CB   1 
ATOM   2053  O OG   . SER A 1 342  ? 117.131 111.841 117.781 1.00 7.85  ?  342  SER A OG   1 
ATOM   2054  N N    . PRO A 1 343  ? 120.977 113.607 115.980 1.00 16.32 ?  343  PRO A N    1 
ATOM   2055  C CA   . PRO A 1 343  ? 122.127 114.533 115.917 1.00 12.06 ?  343  PRO A CA   1 
ATOM   2056  C C    . PRO A 1 343  ? 121.957 115.790 116.756 1.00 15.30 ?  343  PRO A C    1 
ATOM   2057  O O    . PRO A 1 343  ? 122.947 116.304 117.301 1.00 17.91 ?  343  PRO A O    1 
ATOM   2058  C CB   . PRO A 1 343  ? 122.224 114.863 114.421 1.00 16.93 ?  343  PRO A CB   1 
ATOM   2059  C CG   . PRO A 1 343  ? 121.541 113.724 113.732 1.00 17.52 ?  343  PRO A CG   1 
ATOM   2060  C CD   . PRO A 1 343  ? 120.429 113.316 114.644 1.00 17.09 ?  343  PRO A CD   1 
ATOM   2061  N N    . GLU A 1 344  ? 120.725 116.293 116.879 1.00 17.31 ?  344  GLU A N    1 
ATOM   2062  C CA   . GLU A 1 344  ? 120.463 117.416 117.772 1.00 13.85 ?  344  GLU A CA   1 
ATOM   2063  C C    . GLU A 1 344  ? 120.770 117.048 119.219 1.00 12.03 ?  344  GLU A C    1 
ATOM   2064  O O    . GLU A 1 344  ? 121.320 117.860 119.976 1.00 13.01 ?  344  GLU A O    1 
ATOM   2065  C CB   . GLU A 1 344  ? 119.010 117.870 117.619 1.00 16.60 ?  344  GLU A CB   1 
ATOM   2066  C CG   . GLU A 1 344  ? 118.009 116.727 117.486 1.00 14.62 ?  344  GLU A CG   1 
ATOM   2067  C CD   . GLU A 1 344  ? 116.604 117.206 117.168 1.00 17.85 ?  344  GLU A CD   1 
ATOM   2068  O OE1  . GLU A 1 344  ? 116.336 118.416 117.318 1.00 16.01 ?  344  GLU A OE1  1 
ATOM   2069  O OE2  . GLU A 1 344  ? 115.766 116.371 116.766 1.00 21.09 ?  344  GLU A OE2  1 
ATOM   2070  N N    . VAL A 1 345  ? 120.446 115.816 119.612 1.00 9.03  ?  345  VAL A N    1 
ATOM   2071  C CA   . VAL A 1 345  ? 120.767 115.358 120.958 1.00 4.85  ?  345  VAL A CA   1 
ATOM   2072  C C    . VAL A 1 345  ? 122.277 115.266 121.147 1.00 2.43  ?  345  VAL A C    1 
ATOM   2073  O O    . VAL A 1 345  ? 122.801 115.616 122.211 1.00 11.57 ?  345  VAL A O    1 
ATOM   2074  C CB   . VAL A 1 345  ? 120.067 114.017 121.241 1.00 5.24  ?  345  VAL A CB   1 
ATOM   2075  C CG1  . VAL A 1 345  ? 120.268 113.599 122.685 1.00 6.49  ?  345  VAL A CG1  1 
ATOM   2076  C CG2  . VAL A 1 345  ? 118.591 114.111 120.904 1.00 5.81  ?  345  VAL A CG2  1 
ATOM   2077  N N    . GLU A 1 346  ? 123.002 114.816 120.115 1.00 1.32  ?  346  GLU A N    1 
ATOM   2078  C CA   . GLU A 1 346  ? 124.460 114.741 120.209 1.00 5.85  ?  346  GLU A CA   1 
ATOM   2079  C C    . GLU A 1 346  ? 125.077 116.121 120.402 1.00 2.95  ?  346  GLU A C    1 
ATOM   2080  O O    . GLU A 1 346  ? 125.941 116.307 121.271 1.00 8.58  ?  346  GLU A O    1 
ATOM   2081  C CB   . GLU A 1 346  ? 125.055 114.073 118.966 1.00 10.57 ?  346  GLU A CB   1 
ATOM   2082  C CG   . GLU A 1 346  ? 124.292 112.885 118.417 1.00 15.17 ?  346  GLU A CG   1 
ATOM   2083  C CD   . GLU A 1 346  ? 124.800 112.441 117.055 1.00 21.59 ?  346  GLU A CD   1 
ATOM   2084  O OE1  . GLU A 1 346  ? 125.682 113.125 116.494 1.00 19.89 ?  346  GLU A OE1  1 
ATOM   2085  O OE2  . GLU A 1 346  ? 124.321 111.404 116.546 1.00 19.55 ?  346  GLU A OE2  1 
ATOM   2086  N N    . VAL A 1 347  ? 124.647 117.106 119.605 1.00 3.67  ?  347  VAL A N    1 
ATOM   2087  C CA   . VAL A 1 347  ? 125.265 118.425 119.715 1.00 1.14  ?  347  VAL A CA   1 
ATOM   2088  C C    . VAL A 1 347  ? 124.893 119.085 121.042 1.00 3.73  ?  347  VAL A C    1 
ATOM   2089  O O    . VAL A 1 347  ? 125.734 119.743 121.674 1.00 8.68  ?  347  VAL A O    1 
ATOM   2090  C CB   . VAL A 1 347  ? 124.922 119.315 118.501 1.00 1.10  ?  347  VAL A CB   1 
ATOM   2091  C CG1  . VAL A 1 347  ? 125.548 118.749 117.233 1.00 10.42 ?  347  VAL A CG1  1 
ATOM   2092  C CG2  . VAL A 1 347  ? 123.434 119.506 118.324 1.00 2.16  ?  347  VAL A CG2  1 
ATOM   2093  N N    . PHE A 1 348  ? 123.652 118.885 121.512 1.00 2.14  ?  348  PHE A N    1 
ATOM   2094  C CA   . PHE A 1 348  ? 123.272 119.424 122.815 1.00 0.00  ?  348  PHE A CA   1 
ATOM   2095  C C    . PHE A 1 348  ? 124.094 118.811 123.940 1.00 3.35  ?  348  PHE A C    1 
ATOM   2096  O O    . PHE A 1 348  ? 124.577 119.529 124.822 1.00 7.29  ?  348  PHE A O    1 
ATOM   2097  C CB   . PHE A 1 348  ? 121.784 119.212 123.088 1.00 0.00  ?  348  PHE A CB   1 
ATOM   2098  C CG   . PHE A 1 348  ? 121.342 119.758 124.422 1.00 0.00  ?  348  PHE A CG   1 
ATOM   2099  C CD1  . PHE A 1 348  ? 121.148 121.115 124.606 1.00 0.21  ?  348  PHE A CD1  1 
ATOM   2100  C CD2  . PHE A 1 348  ? 121.144 118.909 125.500 1.00 0.00  ?  348  PHE A CD2  1 
ATOM   2101  C CE1  . PHE A 1 348  ? 120.757 121.610 125.835 1.00 0.00  ?  348  PHE A CE1  1 
ATOM   2102  C CE2  . PHE A 1 348  ? 120.753 119.402 126.727 1.00 0.00  ?  348  PHE A CE2  1 
ATOM   2103  C CZ   . PHE A 1 348  ? 120.559 120.752 126.894 1.00 0.00  ?  348  PHE A CZ   1 
ATOM   2104  N N    . LEU A 1 349  ? 124.259 117.485 123.936 1.00 6.01  ?  349  LEU A N    1 
ATOM   2105  C CA   . LEU A 1 349  ? 124.990 116.846 125.027 1.00 0.00  ?  349  LEU A CA   1 
ATOM   2106  C C    . LEU A 1 349  ? 126.463 117.229 125.006 1.00 0.00  ?  349  LEU A C    1 
ATOM   2107  O O    . LEU A 1 349  ? 127.069 117.448 126.066 1.00 8.33  ?  349  LEU A O    1 
ATOM   2108  C CB   . LEU A 1 349  ? 124.821 115.330 124.959 1.00 1.74  ?  349  LEU A CB   1 
ATOM   2109  C CG   . LEU A 1 349  ? 123.427 114.812 125.316 1.00 2.47  ?  349  LEU A CG   1 
ATOM   2110  C CD1  . LEU A 1 349  ? 123.277 113.357 124.911 1.00 2.54  ?  349  LEU A CD1  1 
ATOM   2111  C CD2  . LEU A 1 349  ? 123.141 115.000 126.796 1.00 0.00  ?  349  LEU A CD2  1 
ATOM   2112  N N    . HIS A 1 350  ? 127.050 117.345 123.811 1.00 1.10  ?  350  HIS A N    1 
ATOM   2113  C CA   . HIS A 1 350  ? 128.449 117.749 123.721 1.00 3.41  ?  350  HIS A CA   1 
ATOM   2114  C C    . HIS A 1 350  ? 128.654 119.173 124.226 1.00 5.85  ?  350  HIS A C    1 
ATOM   2115  O O    . HIS A 1 350  ? 129.586 119.431 125.000 1.00 8.73  ?  350  HIS A O    1 
ATOM   2116  C CB   . HIS A 1 350  ? 128.945 117.597 122.284 1.00 0.97  ?  350  HIS A CB   1 
ATOM   2117  C CG   . HIS A 1 350  ? 129.396 116.209 121.950 1.00 7.58  ?  350  HIS A CG   1 
ATOM   2118  N ND1  . HIS A 1 350  ? 128.579 115.286 121.334 1.00 13.88 ?  350  HIS A ND1  1 
ATOM   2119  C CD2  . HIS A 1 350  ? 130.580 115.584 122.153 1.00 6.32  ?  350  HIS A CD2  1 
ATOM   2120  C CE1  . HIS A 1 350  ? 129.240 114.154 121.170 1.00 7.55  ?  350  HIS A CE1  1 
ATOM   2121  N NE2  . HIS A 1 350  ? 130.457 114.309 121.658 1.00 7.35  ?  350  HIS A NE2  1 
ATOM   2122  N N    . ARG A 1 351  ? 127.778 120.106 123.832 1.00 8.07  ?  351  ARG A N    1 
ATOM   2123  C CA   . ARG A 1 351  ? 127.904 121.478 124.323 1.00 0.00  ?  351  ARG A CA   1 
ATOM   2124  C C    . ARG A 1 351  ? 127.650 121.565 125.827 1.00 0.00  ?  351  ARG A C    1 
ATOM   2125  O O    . ARG A 1 351  ? 128.322 122.330 126.532 1.00 2.87  ?  351  ARG A O    1 
ATOM   2126  C CB   . ARG A 1 351  ? 126.952 122.392 123.555 1.00 0.54  ?  351  ARG A CB   1 
ATOM   2127  C CG   . ARG A 1 351  ? 127.147 123.870 123.843 1.00 5.29  ?  351  ARG A CG   1 
ATOM   2128  C CD   . ARG A 1 351  ? 128.544 124.332 123.493 1.00 2.40  ?  351  ARG A CD   1 
ATOM   2129  N NE   . ARG A 1 351  ? 128.713 124.517 122.058 1.00 2.13  ?  351  ARG A NE   1 
ATOM   2130  C CZ   . ARG A 1 351  ? 129.887 124.562 121.445 1.00 4.65  ?  351  ARG A CZ   1 
ATOM   2131  N NH1  . ARG A 1 351  ? 131.021 124.427 122.113 1.00 4.72  ?  351  ARG A NH1  1 
ATOM   2132  N NH2  . ARG A 1 351  ? 129.924 124.748 120.129 1.00 6.83  ?  351  ARG A NH2  1 
ATOM   2133  N N    . PHE A 1 352  ? 126.698 120.774 126.332 1.00 0.00  ?  352  PHE A N    1 
ATOM   2134  C CA   . PHE A 1 352  ? 126.394 120.740 127.760 1.00 0.00  ?  352  PHE A CA   1 
ATOM   2135  C C    . PHE A 1 352  ? 127.607 120.313 128.579 1.00 0.00  ?  352  PHE A C    1 
ATOM   2136  O O    . PHE A 1 352  ? 128.008 120.997 129.536 1.00 6.35  ?  352  PHE A O    1 
ATOM   2137  C CB   . PHE A 1 352  ? 125.218 119.784 127.983 1.00 0.00  ?  352  PHE A CB   1 
ATOM   2138  C CG   . PHE A 1 352  ? 124.738 119.706 129.403 1.00 0.00  ?  352  PHE A CG   1 
ATOM   2139  C CD1  . PHE A 1 352  ? 123.826 120.623 129.891 1.00 0.00  ?  352  PHE A CD1  1 
ATOM   2140  C CD2  . PHE A 1 352  ? 125.169 118.688 130.238 1.00 0.00  ?  352  PHE A CD2  1 
ATOM   2141  C CE1  . PHE A 1 352  ? 123.376 120.543 131.191 1.00 0.00  ?  352  PHE A CE1  1 
ATOM   2142  C CE2  . PHE A 1 352  ? 124.723 118.605 131.538 1.00 1.15  ?  352  PHE A CE2  1 
ATOM   2143  C CZ   . PHE A 1 352  ? 123.825 119.532 132.014 1.00 0.00  ?  352  PHE A CZ   1 
ATOM   2144  N N    . TRP A 1 353  ? 128.220 119.188 128.204 1.00 2.32  ?  353  TRP A N    1 
ATOM   2145  C CA   . TRP A 1 353  ? 129.357 118.703 128.976 1.00 0.00  ?  353  TRP A CA   1 
ATOM   2146  C C    . TRP A 1 353  ? 130.588 119.578 128.775 1.00 2.27  ?  353  TRP A C    1 
ATOM   2147  O O    . TRP A 1 353  ? 131.399 119.719 129.700 1.00 12.68 ?  353  TRP A O    1 
ATOM   2148  C CB   . TRP A 1 353  ? 129.644 117.245 128.627 1.00 0.00  ?  353  TRP A CB   1 
ATOM   2149  C CG   . TRP A 1 353  ? 128.614 116.321 129.201 1.00 2.33  ?  353  TRP A CG   1 
ATOM   2150  C CD1  . TRP A 1 353  ? 127.638 115.656 128.523 1.00 0.00  ?  353  TRP A CD1  1 
ATOM   2151  C CD2  . TRP A 1 353  ? 128.427 116.006 130.584 1.00 0.00  ?  353  TRP A CD2  1 
ATOM   2152  N NE1  . TRP A 1 353  ? 126.871 114.924 129.395 1.00 1.17  ?  353  TRP A NE1  1 
ATOM   2153  C CE2  . TRP A 1 353  ? 127.334 115.125 130.668 1.00 0.00  ?  353  TRP A CE2  1 
ATOM   2154  C CE3  . TRP A 1 353  ? 129.087 116.376 131.760 1.00 0.12  ?  353  TRP A CE3  1 
ATOM   2155  C CZ2  . TRP A 1 353  ? 126.885 114.607 131.880 1.00 0.67  ?  353  TRP A CZ2  1 
ATOM   2156  C CZ3  . TRP A 1 353  ? 128.641 115.861 132.960 1.00 0.00  ?  353  TRP A CZ3  1 
ATOM   2157  C CH2  . TRP A 1 353  ? 127.551 114.987 133.012 1.00 0.00  ?  353  TRP A CH2  1 
ATOM   2158  N N    . GLU A 1 354  ? 130.723 120.205 127.601 1.00 4.38  ?  354  GLU A N    1 
ATOM   2159  C CA   . GLU A 1 354  ? 131.802 121.165 127.393 1.00 0.00  ?  354  GLU A CA   1 
ATOM   2160  C C    . GLU A 1 354  ? 131.672 122.357 128.334 1.00 5.90  ?  354  GLU A C    1 
ATOM   2161  O O    . GLU A 1 354  ? 132.663 122.799 128.926 1.00 14.70 ?  354  GLU A O    1 
ATOM   2162  C CB   . GLU A 1 354  ? 131.809 121.626 125.936 1.00 1.13  ?  354  GLU A CB   1 
ATOM   2163  C CG   . GLU A 1 354  ? 133.100 122.289 125.491 1.00 6.98  ?  354  GLU A CG   1 
ATOM   2164  C CD   . GLU A 1 354  ? 133.143 122.540 123.994 1.00 6.18  ?  354  GLU A CD   1 
ATOM   2165  O OE1  . GLU A 1 354  ? 132.142 122.243 123.309 1.00 1.61  ?  354  GLU A OE1  1 
ATOM   2166  O OE2  . GLU A 1 354  ? 134.179 123.036 123.503 1.00 7.66  ?  354  GLU A OE2  1 
ATOM   2167  N N    . MET A 1 355  ? 130.452 122.880 128.498 1.00 0.00  ?  355  MET A N    1 
ATOM   2168  C CA   . MET A 1 355  ? 130.249 124.019 129.391 1.00 0.00  ?  355  MET A CA   1 
ATOM   2169  C C    . MET A 1 355  ? 130.489 123.640 130.851 1.00 0.00  ?  355  MET A C    1 
ATOM   2170  O O    . MET A 1 355  ? 131.108 124.410 131.602 1.00 14.65 ?  355  MET A O    1 
ATOM   2171  C CB   . MET A 1 355  ? 128.849 124.602 129.170 1.00 8.75  ?  355  MET A CB   1 
ATOM   2172  C CG   . MET A 1 355  ? 128.152 125.177 130.394 1.00 16.65 ?  355  MET A CG   1 
ATOM   2173  S SD   . MET A 1 355  ? 126.360 124.938 130.337 1.00 7.86  ?  355  MET A SD   1 
ATOM   2174  C CE   . MET A 1 355  ? 126.177 123.347 131.129 1.00 11.33 ?  355  MET A CE   1 
ATOM   2175  N N    . LEU A 1 356  ? 130.043 122.447 131.265 1.00 2.82  ?  356  LEU A N    1 
ATOM   2176  C CA   . LEU A 1 356  ? 130.313 121.994 132.633 1.00 2.81  ?  356  LEU A CA   1 
ATOM   2177  C C    . LEU A 1 356  ? 131.812 121.868 132.902 1.00 0.00  ?  356  LEU A C    1 
ATOM   2178  O O    . LEU A 1 356  ? 132.317 122.341 133.934 1.00 5.52  ?  356  LEU A O    1 
ATOM   2179  C CB   . LEU A 1 356  ? 129.612 120.661 132.897 1.00 8.58  ?  356  LEU A CB   1 
ATOM   2180  C CG   . LEU A 1 356  ? 128.109 120.669 133.171 1.00 3.25  ?  356  LEU A CG   1 
ATOM   2181  C CD1  . LEU A 1 356  ? 127.686 119.350 133.786 1.00 6.30  ?  356  LEU A CD1  1 
ATOM   2182  C CD2  . LEU A 1 356  ? 127.760 121.812 134.104 1.00 9.10  ?  356  LEU A CD2  1 
ATOM   2183  N N    . ALA A 1 357  ? 132.546 121.246 131.971 1.00 0.70  ?  357  ALA A N    1 
ATOM   2184  C CA   . ALA A 1 357  ? 133.983 121.077 132.158 1.00 0.00  ?  357  ALA A CA   1 
ATOM   2185  C C    . ALA A 1 357  ? 134.714 122.414 132.134 1.00 0.00  ?  357  ALA A C    1 
ATOM   2186  O O    . ALA A 1 357  ? 135.698 122.600 132.860 1.00 1.59  ?  357  ALA A O    1 
ATOM   2187  C CB   . ALA A 1 357  ? 134.541 120.142 131.090 1.00 2.64  ?  357  ALA A CB   1 
ATOM   2188  N N    . TYR A 1 358  ? 134.246 123.357 131.310 1.00 11.80 ?  358  TYR A N    1 
ATOM   2189  C CA   . TYR A 1 358  ? 134.840 124.691 131.266 1.00 0.66  ?  358  TYR A CA   1 
ATOM   2190  C C    . TYR A 1 358  ? 134.695 125.411 132.601 1.00 0.00  ?  358  TYR A C    1 
ATOM   2191  O O    . TYR A 1 358  ? 135.660 126.011 133.106 1.00 2.10  ?  358  TYR A O    1 
ATOM   2192  C CB   . TYR A 1 358  ? 134.181 125.486 130.138 1.00 2.19  ?  358  TYR A CB   1 
ATOM   2193  C CG   . TYR A 1 358  ? 134.344 126.987 130.203 1.00 2.29  ?  358  TYR A CG   1 
ATOM   2194  C CD1  . TYR A 1 358  ? 135.557 127.591 129.905 1.00 1.75  ?  358  TYR A CD1  1 
ATOM   2195  C CD2  . TYR A 1 358  ? 133.272 127.802 130.540 1.00 0.00  ?  358  TYR A CD2  1 
ATOM   2196  C CE1  . TYR A 1 358  ? 135.700 128.965 129.954 1.00 0.26  ?  358  TYR A CE1  1 
ATOM   2197  C CE2  . TYR A 1 358  ? 133.407 129.173 130.593 1.00 2.21  ?  358  TYR A CE2  1 
ATOM   2198  C CZ   . TYR A 1 358  ? 134.621 129.749 130.299 1.00 2.89  ?  358  TYR A CZ   1 
ATOM   2199  O OH   . TYR A 1 358  ? 134.754 131.117 130.350 1.00 10.89 ?  358  TYR A OH   1 
ATOM   2200  N N    . LEU A 1 359  ? 133.498 125.348 133.195 1.00 0.81  ?  359  LEU A N    1 
ATOM   2201  C CA   . LEU A 1 359  ? 133.290 125.961 134.505 1.00 2.19  ?  359  LEU A CA   1 
ATOM   2202  C C    . LEU A 1 359  ? 134.184 125.329 135.563 1.00 0.00  ?  359  LEU A C    1 
ATOM   2203  O O    . LEU A 1 359  ? 134.806 126.041 136.368 1.00 6.25  ?  359  LEU A O    1 
ATOM   2204  C CB   . LEU A 1 359  ? 131.823 125.843 134.910 1.00 8.67  ?  359  LEU A CB   1 
ATOM   2205  C CG   . LEU A 1 359  ? 130.806 126.515 133.993 1.00 7.07  ?  359  LEU A CG   1 
ATOM   2206  C CD1  . LEU A 1 359  ? 129.408 126.076 134.367 1.00 7.74  ?  359  LEU A CD1  1 
ATOM   2207  C CD2  . LEU A 1 359  ? 130.939 128.023 134.082 1.00 7.38  ?  359  LEU A CD2  1 
ATOM   2208  N N    . ALA A 1 360  ? 134.275 123.993 135.564 1.00 5.35  ?  360  ALA A N    1 
ATOM   2209  C CA   . ALA A 1 360  ? 135.120 123.312 136.544 1.00 0.00  ?  360  ALA A CA   1 
ATOM   2210  C C    . ALA A 1 360  ? 136.588 123.695 136.382 1.00 0.00  ?  360  ALA A C    1 
ATOM   2211  O O    . ALA A 1 360  ? 137.291 123.925 137.375 1.00 2.90  ?  360  ALA A O    1 
ATOM   2212  C CB   . ALA A 1 360  ? 134.944 121.800 136.425 1.00 3.10  ?  360  ALA A CB   1 
ATOM   2213  N N    . ASN A 1 361  ? 137.059 123.786 135.134 1.00 11.05 ?  361  ASN A N    1 
ATOM   2214  C CA   . ASN A 1 361  ? 138.449 124.138 134.856 1.00 0.00  ?  361  ASN A CA   1 
ATOM   2215  C C    . ASN A 1 361  ? 138.788 125.528 135.385 1.00 1.59  ?  361  ASN A C    1 
ATOM   2216  O O    . ASN A 1 361  ? 139.792 125.714 136.094 1.00 8.99  ?  361  ASN A O    1 
ATOM   2217  C CB   . ASN A 1 361  ? 138.692 124.077 133.347 1.00 0.14  ?  361  ASN A CB   1 
ATOM   2218  C CG   . ASN A 1 361  ? 139.590 122.933 132.941 1.00 3.74  ?  361  ASN A CG   1 
ATOM   2219  O OD1  . ASN A 1 361  ? 140.295 122.359 133.763 1.00 7.22  ?  361  ASN A OD1  1 
ATOM   2220  N ND2  . ASN A 1 361  ? 139.566 122.594 131.658 1.00 5.09  ?  361  ASN A ND2  1 
ATOM   2221  N N    . THR A 1 362  ? 137.959 126.522 135.041 1.00 18.88 ?  362  THR A N    1 
ATOM   2222  C CA   . THR A 1 362  ? 138.236 127.889 135.476 1.00 3.14  ?  362  THR A CA   1 
ATOM   2223  C C    . THR A 1 362  ? 138.174 128.014 136.994 1.00 3.71  ?  362  THR A C    1 
ATOM   2224  O O    . THR A 1 362  ? 139.011 128.701 137.603 1.00 11.10 ?  362  THR A O    1 
ATOM   2225  C CB   . THR A 1 362  ? 137.263 128.870 134.821 1.00 6.57  ?  362  THR A CB   1 
ATOM   2226  O OG1  . THR A 1 362  ? 135.929 128.592 135.259 1.00 15.79 ?  362  THR A OG1  1 
ATOM   2227  C CG2  . THR A 1 362  ? 137.335 128.770 133.306 1.00 9.47  ?  362  THR A CG2  1 
ATOM   2228  N N    . LEU A 1 363  ? 137.202 127.344 137.627 1.00 0.00  ?  363  LEU A N    1 
ATOM   2229  C CA   . LEU A 1 363  ? 137.111 127.396 139.083 1.00 0.81  ?  363  LEU A CA   1 
ATOM   2230  C C    . LEU A 1 363  ? 138.344 126.794 139.742 1.00 1.49  ?  363  LEU A C    1 
ATOM   2231  O O    . LEU A 1 363  ? 138.881 127.367 140.700 1.00 8.36  ?  363  LEU A O    1 
ATOM   2232  C CB   . LEU A 1 363  ? 135.852 126.677 139.562 1.00 1.41  ?  363  LEU A CB   1 
ATOM   2233  C CG   . LEU A 1 363  ? 134.629 127.561 139.784 1.00 0.53  ?  363  LEU A CG   1 
ATOM   2234  C CD1  . LEU A 1 363  ? 133.386 126.712 139.979 1.00 0.00  ?  363  LEU A CD1  1 
ATOM   2235  C CD2  . LEU A 1 363  ? 134.865 128.467 140.976 1.00 4.05  ?  363  LEU A CD2  1 
ATOM   2236  N N    . ILE A 1 364  ? 138.815 125.651 139.230 1.00 6.51  ?  364  ILE A N    1 
ATOM   2237  C CA   . ILE A 1 364  ? 139.984 124.990 139.805 1.00 0.95  ?  364  ILE A CA   1 
ATOM   2238  C C    . ILE A 1 364  ? 141.213 125.881 139.702 1.00 0.00  ?  364  ILE A C    1 
ATOM   2239  O O    . ILE A 1 364  ? 141.975 126.022 140.670 1.00 3.73  ?  364  ILE A O    1 
ATOM   2240  C CB   . ILE A 1 364  ? 140.212 123.625 139.125 1.00 2.97  ?  364  ILE A CB   1 
ATOM   2241  C CG1  . ILE A 1 364  ? 139.237 122.586 139.675 1.00 8.51  ?  364  ILE A CG1  1 
ATOM   2242  C CG2  . ILE A 1 364  ? 141.649 123.154 139.295 1.00 6.81  ?  364  ILE A CG2  1 
ATOM   2243  C CD1  . ILE A 1 364  ? 139.225 121.297 138.898 1.00 7.39  ?  364  ILE A CD1  1 
ATOM   2244  N N    . PHE A 1 365  ? 141.422 126.506 138.537 1.00 5.71  ?  365  PHE A N    1 
ATOM   2245  C CA   . PHE A 1 365  ? 142.593 127.370 138.378 1.00 0.00  ?  365  PHE A CA   1 
ATOM   2246  C C    . PHE A 1 365  ? 142.533 128.582 139.309 1.00 3.97  ?  365  PHE A C    1 
ATOM   2247  O O    . PHE A 1 365  ? 143.543 128.941 139.935 1.00 0.22  ?  365  PHE A O    1 
ATOM   2248  C CB   . PHE A 1 365  ? 142.745 127.795 136.918 1.00 0.00  ?  365  PHE A CB   1 
ATOM   2249  C CG   . PHE A 1 365  ? 143.498 126.797 136.072 1.00 1.61  ?  365  PHE A CG   1 
ATOM   2250  C CD1  . PHE A 1 365  ? 144.879 126.733 136.120 1.00 0.00  ?  365  PHE A CD1  1 
ATOM   2251  C CD2  . PHE A 1 365  ? 142.826 125.920 135.239 1.00 0.00  ?  365  PHE A CD2  1 
ATOM   2252  C CE1  . PHE A 1 365  ? 145.576 125.820 135.349 1.00 0.00  ?  365  PHE A CE1  1 
ATOM   2253  C CE2  . PHE A 1 365  ? 143.520 125.003 134.468 1.00 0.00  ?  365  PHE A CE2  1 
ATOM   2254  C CZ   . PHE A 1 365  ? 144.895 124.955 134.525 1.00 0.00  ?  365  PHE A CZ   1 
ATOM   2255  N N    . MET A 1 366  ? 141.353 129.198 139.455 1.00 0.00  ?  366  MET A N    1 
ATOM   2256  C CA   . MET A 1 366  ? 141.223 130.312 140.396 1.00 0.51  ?  366  MET A CA   1 
ATOM   2257  C C    . MET A 1 366  ? 141.550 129.902 141.829 1.00 0.00  ?  366  MET A C    1 
ATOM   2258  O O    . MET A 1 366  ? 142.313 130.595 142.525 1.00 9.79  ?  366  MET A O    1 
ATOM   2259  C CB   . MET A 1 366  ? 139.822 130.916 140.330 1.00 1.10  ?  366  MET A CB   1 
ATOM   2260  C CG   . MET A 1 366  ? 139.608 131.850 139.172 1.00 3.65  ?  366  MET A CG   1 
ATOM   2261  S SD   . MET A 1 366  ? 140.202 133.474 139.684 1.00 14.03 ?  366  MET A SD   1 
ATOM   2262  C CE   . MET A 1 366  ? 139.944 134.423 138.196 1.00 8.97  ?  366  MET A CE   1 
ATOM   2263  N N    . MET A 1 367  ? 140.981 128.787 142.304 1.00 0.00  ?  367  MET A N    1 
ATOM   2264  C CA   . MET A 1 367  ? 141.195 128.506 143.721 1.00 0.32  ?  367  MET A CA   1 
ATOM   2265  C C    . MET A 1 367  ? 142.595 127.978 143.986 1.00 5.17  ?  367  MET A C    1 
ATOM   2266  O O    . MET A 1 367  ? 143.141 128.227 145.067 1.00 0.00  ?  367  MET A O    1 
ATOM   2267  C CB   . MET A 1 367  ? 140.161 127.552 144.313 1.00 0.00  ?  367  MET A CB   1 
ATOM   2268  C CG   . MET A 1 367  ? 139.712 126.405 143.488 1.00 0.69  ?  367  MET A CG   1 
ATOM   2269  S SD   . MET A 1 367  ? 138.670 125.372 144.520 1.00 0.00  ?  367  MET A SD   1 
ATOM   2270  C CE   . MET A 1 367  ? 138.144 124.173 143.322 1.00 2.70  ?  367  MET A CE   1 
ATOM   2271  N N    . VAL A 1 368  ? 143.213 127.285 143.023 1.00 1.51  ?  368  VAL A N    1 
ATOM   2272  C CA   . VAL A 1 368  ? 144.599 126.893 143.254 1.00 0.00  ?  368  VAL A CA   1 
ATOM   2273  C C    . VAL A 1 368  ? 145.494 128.127 143.278 1.00 0.00  ?  368  VAL A C    1 
ATOM   2274  O O    . VAL A 1 368  ? 146.441 128.186 144.071 1.00 6.71  ?  368  VAL A O    1 
ATOM   2275  C CB   . VAL A 1 368  ? 145.079 125.834 142.238 1.00 0.00  ?  368  VAL A CB   1 
ATOM   2276  C CG1  . VAL A 1 368  ? 145.167 126.378 140.843 1.00 0.00  ?  368  VAL A CG1  1 
ATOM   2277  C CG2  . VAL A 1 368  ? 146.422 125.277 142.655 1.00 0.95  ?  368  VAL A CG2  1 
ATOM   2278  N N    . GLY A 1 369  ? 145.178 129.153 142.477 1.00 10.90 ?  369  GLY A N    1 
ATOM   2279  C CA   . GLY A 1 369  ? 145.938 130.393 142.561 1.00 0.38  ?  369  GLY A CA   1 
ATOM   2280  C C    . GLY A 1 369  ? 145.844 131.059 143.923 1.00 0.00  ?  369  GLY A C    1 
ATOM   2281  O O    . GLY A 1 369  ? 146.868 131.383 144.541 1.00 0.16  ?  369  GLY A O    1 
ATOM   2282  N N    . VAL A 1 370  ? 144.617 131.242 144.428 1.00 1.21  ?  370  VAL A N    1 
ATOM   2283  C CA   . VAL A 1 370  ? 144.475 131.958 145.701 1.00 0.00  ?  370  VAL A CA   1 
ATOM   2284  C C    . VAL A 1 370  ? 145.058 131.138 146.851 1.00 0.21  ?  370  VAL A C    1 
ATOM   2285  O O    . VAL A 1 370  ? 145.714 131.686 147.748 1.00 2.57  ?  370  VAL A O    1 
ATOM   2286  C CB   . VAL A 1 370  ? 143.010 132.367 145.969 1.00 0.00  ?  370  VAL A CB   1 
ATOM   2287  C CG1  . VAL A 1 370  ? 142.074 131.249 145.710 1.00 0.00  ?  370  VAL A CG1  1 
ATOM   2288  C CG2  . VAL A 1 370  ? 142.821 132.837 147.405 1.00 1.80  ?  370  VAL A CG2  1 
ATOM   2289  N N    . VAL A 1 371  ? 144.878 129.814 146.825 1.00 5.83  ?  371  VAL A N    1 
ATOM   2290  C CA   . VAL A 1 371  ? 145.374 128.987 147.920 1.00 2.18  ?  371  VAL A CA   1 
ATOM   2291  C C    . VAL A 1 371  ? 146.899 128.924 147.906 1.00 1.44  ?  371  VAL A C    1 
ATOM   2292  O O    . VAL A 1 371  ? 147.541 128.992 148.962 1.00 5.61  ?  371  VAL A O    1 
ATOM   2293  C CB   . VAL A 1 371  ? 144.733 127.588 147.856 1.00 0.51  ?  371  VAL A CB   1 
ATOM   2294  C CG1  . VAL A 1 371  ? 145.466 126.618 148.753 1.00 2.61  ?  371  VAL A CG1  1 
ATOM   2295  C CG2  . VAL A 1 371  ? 143.271 127.664 148.254 1.00 1.06  ?  371  VAL A CG2  1 
ATOM   2296  N N    . VAL A 1 372  ? 147.510 128.816 146.720 1.00 4.43  ?  372  VAL A N    1 
ATOM   2297  C CA   . VAL A 1 372  ? 148.967 128.753 146.667 1.00 3.66  ?  372  VAL A CA   1 
ATOM   2298  C C    . VAL A 1 372  ? 149.584 130.100 147.029 1.00 4.85  ?  372  VAL A C    1 
ATOM   2299  O O    . VAL A 1 372  ? 150.707 130.150 147.545 1.00 6.95  ?  372  VAL A O    1 
ATOM   2300  C CB   . VAL A 1 372  ? 149.443 128.242 145.290 1.00 2.21  ?  372  VAL A CB   1 
ATOM   2301  C CG1  . VAL A 1 372  ? 149.488 129.355 144.251 1.00 2.04  ?  372  VAL A CG1  1 
ATOM   2302  C CG2  . VAL A 1 372  ? 150.803 127.579 145.416 1.00 5.17  ?  372  VAL A CG2  1 
ATOM   2303  N N    . THR A 1 373  ? 148.878 131.210 146.782 1.00 9.65  ?  373  THR A N    1 
ATOM   2304  C CA   . THR A 1 373  ? 149.418 132.494 147.219 1.00 6.24  ?  373  THR A CA   1 
ATOM   2305  C C    . THR A 1 373  ? 149.270 132.685 148.726 1.00 8.75  ?  373  THR A C    1 
ATOM   2306  O O    . THR A 1 373  ? 150.201 133.159 149.387 1.00 9.49  ?  373  THR A O    1 
ATOM   2307  C CB   . THR A 1 373  ? 148.743 133.632 146.456 1.00 9.25  ?  373  THR A CB   1 
ATOM   2308  O OG1  . THR A 1 373  ? 149.094 133.531 145.073 1.00 7.37  ?  373  THR A OG1  1 
ATOM   2309  C CG2  . THR A 1 373  ? 149.199 134.985 146.979 1.00 13.71 ?  373  THR A CG2  1 
ATOM   2310  N N    . GLN A 1 374  ? 148.120 132.303 149.288 1.00 12.26 ?  374  GLN A N    1 
ATOM   2311  C CA   . GLN A 1 374  ? 147.865 132.555 150.704 1.00 9.74  ?  374  GLN A CA   1 
ATOM   2312  C C    . GLN A 1 374  ? 148.725 131.670 151.601 1.00 13.40 ?  374  GLN A C    1 
ATOM   2313  O O    . GLN A 1 374  ? 149.320 132.149 152.573 1.00 13.70 ?  374  GLN A O    1 
ATOM   2314  C CB   . GLN A 1 374  ? 146.383 132.345 151.013 1.00 10.39 ?  374  GLN A CB   1 
ATOM   2315  C CG   . GLN A 1 374  ? 145.545 133.609 150.952 1.00 11.98 ?  374  GLN A CG   1 
ATOM   2316  C CD   . GLN A 1 374  ? 144.251 133.487 151.732 1.00 15.79 ?  374  GLN A CD   1 
ATOM   2317  O OE1  . GLN A 1 374  ? 144.221 132.917 152.822 1.00 19.72 ?  374  GLN A OE1  1 
ATOM   2318  N NE2  . GLN A 1 374  ? 143.172 134.026 151.177 1.00 16.04 ?  374  GLN A NE2  1 
ATOM   2319  N N    . LYS A 1 375  ? 148.805 130.376 151.294 1.00 17.15 ?  375  LYS A N    1 
ATOM   2320  C CA   . LYS A 1 375  ? 149.387 129.392 152.199 1.00 14.48 ?  375  LYS A CA   1 
ATOM   2321  C C    . LYS A 1 375  ? 150.769 128.912 151.783 1.00 14.66 ?  375  LYS A C    1 
ATOM   2322  O O    . LYS A 1 375  ? 151.708 128.972 152.580 1.00 15.73 ?  375  LYS A O    1 
ATOM   2323  C CB   . LYS A 1 375  ? 148.450 128.182 152.324 1.00 14.54 ?  375  LYS A CB   1 
ATOM   2324  C CG   . LYS A 1 375  ? 147.110 128.489 152.964 1.00 16.40 ?  375  LYS A CG   1 
ATOM   2325  C CD   . LYS A 1 375  ? 146.524 127.244 153.605 1.00 16.35 ?  375  LYS A CD   1 
ATOM   2326  C CE   . LYS A 1 375  ? 145.034 127.138 153.349 1.00 13.11 ?  375  LYS A CE   1 
ATOM   2327  N NZ   . LYS A 1 375  ? 144.601 125.725 153.160 1.00 11.66 ?  375  LYS A NZ   1 
ATOM   2328  N N    . ALA A 1 376  ? 150.920 128.429 150.550 1.00 14.64 ?  376  ALA A N    1 
ATOM   2329  C CA   . ALA A 1 376  ? 152.127 127.716 150.152 1.00 14.66 ?  376  ALA A CA   1 
ATOM   2330  C C    . ALA A 1 376  ? 153.318 128.625 149.880 1.00 17.99 ?  376  ALA A C    1 
ATOM   2331  O O    . ALA A 1 376  ? 154.422 128.114 149.664 1.00 23.08 ?  376  ALA A O    1 
ATOM   2332  C CB   . ALA A 1 376  ? 151.847 126.865 148.912 1.00 7.04  ?  376  ALA A CB   1 
ATOM   2333  N N    . LEU A 1 377  ? 153.136 129.943 149.879 1.00 16.98 ?  377  LEU A N    1 
ATOM   2334  C CA   . LEU A 1 377  ? 154.221 130.869 149.589 1.00 15.48 ?  377  LEU A CA   1 
ATOM   2335  C C    . LEU A 1 377  ? 154.823 131.489 150.843 1.00 20.06 ?  377  LEU A C    1 
ATOM   2336  O O    . LEU A 1 377  ? 155.576 132.463 150.740 1.00 20.85 ?  377  LEU A O    1 
ATOM   2337  C CB   . LEU A 1 377  ? 153.741 131.967 148.636 1.00 18.92 ?  377  LEU A CB   1 
ATOM   2338  C CG   . LEU A 1 377  ? 153.860 131.661 147.139 1.00 18.38 ?  377  LEU A CG   1 
ATOM   2339  C CD1  . LEU A 1 377  ? 153.814 132.941 146.320 1.00 16.04 ?  377  LEU A CD1  1 
ATOM   2340  C CD2  . LEU A 1 377  ? 155.132 130.881 146.835 1.00 15.74 ?  377  LEU A CD2  1 
ATOM   2341  N N    . VAL A 1 378  ? 154.509 130.953 152.022 1.00 24.45 ?  378  VAL A N    1 
ATOM   2342  C CA   . VAL A 1 378  ? 155.105 131.408 153.272 1.00 25.80 ?  378  VAL A CA   1 
ATOM   2343  C C    . VAL A 1 378  ? 156.063 130.387 153.861 1.00 23.51 ?  378  VAL A C    1 
ATOM   2344  O O    . VAL A 1 378  ? 156.672 130.656 154.906 1.00 22.30 ?  378  VAL A O    1 
ATOM   2345  C CB   . VAL A 1 378  ? 154.025 131.786 154.304 1.00 21.61 ?  378  VAL A CB   1 
ATOM   2346  C CG1  . VAL A 1 378  ? 152.950 132.643 153.654 1.00 20.50 ?  378  VAL A CG1  1 
ATOM   2347  C CG2  . VAL A 1 378  ? 153.415 130.539 154.927 1.00 21.22 ?  378  VAL A CG2  1 
ATOM   2348  N N    . ALA A 1 379  ? 156.226 129.231 153.223 1.00 20.35 ?  379  ALA A N    1 
ATOM   2349  C CA   . ALA A 1 379  ? 157.075 128.153 153.722 1.00 20.58 ?  379  ALA A CA   1 
ATOM   2350  C C    . ALA A 1 379  ? 157.953 127.602 152.606 1.00 19.12 ?  379  ALA A C    1 
ATOM   2351  O O    . ALA A 1 379  ? 158.045 126.392 152.391 1.00 17.51 ?  379  ALA A O    1 
ATOM   2352  C CB   . ALA A 1 379  ? 156.233 127.045 154.346 1.00 21.53 ?  379  ALA A CB   1 
ATOM   2353  N N    . VAL A 1 380  ? 158.613 128.494 151.871 1.00 21.55 ?  380  VAL A N    1 
ATOM   2354  C CA   . VAL A 1 380  ? 159.474 128.116 150.757 1.00 20.20 ?  380  VAL A CA   1 
ATOM   2355  C C    . VAL A 1 380  ? 160.855 128.723 150.962 1.00 21.09 ?  380  VAL A C    1 
ATOM   2356  O O    . VAL A 1 380  ? 160.987 129.840 151.476 1.00 20.88 ?  380  VAL A O    1 
ATOM   2357  C CB   . VAL A 1 380  ? 158.882 128.552 149.400 1.00 21.09 ?  380  VAL A CB   1 
ATOM   2358  C CG1  . VAL A 1 380  ? 157.709 127.662 149.027 1.00 18.62 ?  380  VAL A CG1  1 
ATOM   2359  C CG2  . VAL A 1 380  ? 158.453 130.010 149.447 1.00 19.66 ?  380  VAL A CG2  1 
ATOM   2360  N N    . ASP A 1 381  ? 161.880 127.976 150.572 1.00 22.59 ?  381  ASP A N    1 
ATOM   2361  C CA   . ASP A 1 381  ? 163.269 128.411 150.599 1.00 24.58 ?  381  ASP A CA   1 
ATOM   2362  C C    . ASP A 1 381  ? 163.827 128.377 149.178 1.00 22.80 ?  381  ASP A C    1 
ATOM   2363  O O    . ASP A 1 381  ? 163.137 128.003 148.227 1.00 22.03 ?  381  ASP A O    1 
ATOM   2364  C CB   . ASP A 1 381  ? 164.094 127.529 151.543 1.00 21.25 ?  381  ASP A CB   1 
ATOM   2365  C CG   . ASP A 1 381  ? 165.274 128.263 152.154 1.00 23.57 ?  381  ASP A CG   1 
ATOM   2366  O OD1  . ASP A 1 381  ? 165.903 129.079 151.449 1.00 24.73 ?  381  ASP A OD1  1 
ATOM   2367  O OD2  . ASP A 1 381  ? 165.576 128.018 153.341 1.00 25.77 ?  381  ASP A OD2  1 
ATOM   2368  N N    . LYS A 1 382  ? 165.093 128.782 149.038 1.00 21.07 ?  382  LYS A N    1 
ATOM   2369  C CA   . LYS A 1 382  ? 165.764 128.706 147.743 1.00 21.52 ?  382  LYS A CA   1 
ATOM   2370  C C    . LYS A 1 382  ? 165.927 127.260 147.284 1.00 23.35 ?  382  LYS A C    1 
ATOM   2371  O O    . LYS A 1 382  ? 165.823 126.969 146.082 1.00 24.64 ?  382  LYS A O    1 
ATOM   2372  C CB   . LYS A 1 382  ? 167.120 129.414 147.827 1.00 20.01 ?  382  LYS A CB   1 
ATOM   2373  C CG   . LYS A 1 382  ? 168.104 129.082 146.714 1.00 20.89 ?  382  LYS A CG   1 
ATOM   2374  C CD   . LYS A 1 382  ? 167.663 129.666 145.383 1.00 19.90 ?  382  LYS A CD   1 
ATOM   2375  C CE   . LYS A 1 382  ? 168.536 129.154 144.251 1.00 17.84 ?  382  LYS A CE   1 
ATOM   2376  N NZ   . LYS A 1 382  ? 167.906 129.380 142.923 1.00 18.21 ?  382  LYS A NZ   1 
ATOM   2377  N N    . MET A 1 383  ? 166.159 126.346 148.231 1.00 17.72 ?  383  MET A N    1 
ATOM   2378  C CA   . MET A 1 383  ? 166.265 124.930 147.903 1.00 17.65 ?  383  MET A CA   1 
ATOM   2379  C C    . MET A 1 383  ? 164.978 124.397 147.288 1.00 20.63 ?  383  MET A C    1 
ATOM   2380  O O    . MET A 1 383  ? 165.026 123.489 146.454 1.00 24.40 ?  383  MET A O    1 
ATOM   2381  C CB   . MET A 1 383  ? 166.625 124.130 149.155 1.00 18.37 ?  383  MET A CB   1 
ATOM   2382  C CG   . MET A 1 383  ? 168.008 124.433 149.708 1.00 21.29 ?  383  MET A CG   1 
ATOM   2383  S SD   . MET A 1 383  ? 169.317 124.200 148.490 1.00 36.38 ?  383  MET A SD   1 
ATOM   2384  C CE   . MET A 1 383  ? 169.098 122.469 148.088 1.00 18.86 ?  383  MET A CE   1 
ATOM   2385  N N    . ASP A 1 384  ? 163.827 124.953 147.673 1.00 19.56 ?  384  ASP A N    1 
ATOM   2386  C CA   . ASP A 1 384  ? 162.567 124.545 147.057 1.00 15.24 ?  384  ASP A CA   1 
ATOM   2387  C C    . ASP A 1 384  ? 162.527 124.911 145.578 1.00 17.06 ?  384  ASP A C    1 
ATOM   2388  O O    . ASP A 1 384  ? 162.079 124.110 144.749 1.00 23.96 ?  384  ASP A O    1 
ATOM   2389  C CB   . ASP A 1 384  ? 161.392 125.176 147.802 1.00 16.07 ?  384  ASP A CB   1 
ATOM   2390  C CG   . ASP A 1 384  ? 161.123 124.508 149.134 1.00 21.73 ?  384  ASP A CG   1 
ATOM   2391  O OD1  . ASP A 1 384  ? 161.817 123.522 149.457 1.00 25.36 ?  384  ASP A OD1  1 
ATOM   2392  O OD2  . ASP A 1 384  ? 160.215 124.966 149.857 1.00 19.24 ?  384  ASP A OD2  1 
ATOM   2393  N N    . TRP A 1 385  ? 163.000 126.108 145.223 1.00 9.45  ?  385  TRP A N    1 
ATOM   2394  C CA   . TRP A 1 385  ? 163.044 126.500 143.816 1.00 10.55 ?  385  TRP A CA   1 
ATOM   2395  C C    . TRP A 1 385  ? 164.052 125.659 143.039 1.00 15.75 ?  385  TRP A C    1 
ATOM   2396  O O    . TRP A 1 385  ? 163.799 125.275 141.887 1.00 19.21 ?  385  TRP A O    1 
ATOM   2397  C CB   . TRP A 1 385  ? 163.378 127.986 143.698 1.00 11.03 ?  385  TRP A CB   1 
ATOM   2398  C CG   . TRP A 1 385  ? 162.342 128.881 144.303 1.00 11.41 ?  385  TRP A CG   1 
ATOM   2399  C CD1  . TRP A 1 385  ? 162.307 129.341 145.585 1.00 11.25 ?  385  TRP A CD1  1 
ATOM   2400  C CD2  . TRP A 1 385  ? 161.187 129.422 143.651 1.00 12.56 ?  385  TRP A CD2  1 
ATOM   2401  N NE1  . TRP A 1 385  ? 161.205 130.137 145.774 1.00 9.44  ?  385  TRP A NE1  1 
ATOM   2402  C CE2  . TRP A 1 385  ? 160.500 130.202 144.601 1.00 10.95 ?  385  TRP A CE2  1 
ATOM   2403  C CE3  . TRP A 1 385  ? 160.668 129.322 142.357 1.00 14.04 ?  385  TRP A CE3  1 
ATOM   2404  C CZ2  . TRP A 1 385  ? 159.322 130.879 144.298 1.00 12.80 ?  385  TRP A CZ2  1 
ATOM   2405  C CZ3  . TRP A 1 385  ? 159.499 129.995 142.059 1.00 9.30  ?  385  TRP A CZ3  1 
ATOM   2406  C CH2  . TRP A 1 385  ? 158.839 130.764 143.025 1.00 10.64 ?  385  TRP A CH2  1 
ATOM   2407  N N    . PHE A 1 386  ? 165.201 125.364 143.657 1.00 12.57 ?  386  PHE A N    1 
ATOM   2408  C CA   . PHE A 1 386  ? 166.186 124.492 143.022 1.00 13.11 ?  386  PHE A CA   1 
ATOM   2409  C C    . PHE A 1 386  ? 165.607 123.103 142.767 1.00 18.74 ?  386  PHE A C    1 
ATOM   2410  O O    . PHE A 1 386  ? 165.795 122.527 141.686 1.00 17.24 ?  386  PHE A O    1 
ATOM   2411  C CB   . PHE A 1 386  ? 167.439 124.413 143.897 1.00 12.83 ?  386  PHE A CB   1 
ATOM   2412  C CG   . PHE A 1 386  ? 168.474 123.441 143.405 1.00 15.72 ?  386  PHE A CG   1 
ATOM   2413  C CD1  . PHE A 1 386  ? 169.307 123.770 142.349 1.00 18.22 ?  386  PHE A CD1  1 
ATOM   2414  C CD2  . PHE A 1 386  ? 168.629 122.206 144.015 1.00 15.10 ?  386  PHE A CD2  1 
ATOM   2415  C CE1  . PHE A 1 386  ? 170.265 122.880 141.900 1.00 17.76 ?  386  PHE A CE1  1 
ATOM   2416  C CE2  . PHE A 1 386  ? 169.585 121.312 143.570 1.00 16.87 ?  386  PHE A CE2  1 
ATOM   2417  C CZ   . PHE A 1 386  ? 170.404 121.649 142.512 1.00 16.48 ?  386  PHE A CZ   1 
ATOM   2418  N N    . TYR A 1 387  ? 164.877 122.564 143.746 1.00 15.19 ?  387  TYR A N    1 
ATOM   2419  C CA   . TYR A 1 387  ? 164.248 121.259 143.590 1.00 12.33 ?  387  TYR A CA   1 
ATOM   2420  C C    . TYR A 1 387  ? 163.156 121.296 142.531 1.00 9.29  ?  387  TYR A C    1 
ATOM   2421  O O    . TYR A 1 387  ? 162.964 120.318 141.803 1.00 16.33 ?  387  TYR A O    1 
ATOM   2422  C CB   . TYR A 1 387  ? 163.682 120.793 144.930 1.00 12.84 ?  387  TYR A CB   1 
ATOM   2423  C CG   . TYR A 1 387  ? 164.739 120.401 145.935 1.00 17.10 ?  387  TYR A CG   1 
ATOM   2424  C CD1  . TYR A 1 387  ? 166.001 119.997 145.523 1.00 17.91 ?  387  TYR A CD1  1 
ATOM   2425  C CD2  . TYR A 1 387  ? 164.476 120.441 147.298 1.00 19.19 ?  387  TYR A CD2  1 
ATOM   2426  C CE1  . TYR A 1 387  ? 166.971 119.641 146.440 1.00 20.83 ?  387  TYR A CE1  1 
ATOM   2427  C CE2  . TYR A 1 387  ? 165.439 120.088 148.221 1.00 17.60 ?  387  TYR A CE2  1 
ATOM   2428  C CZ   . TYR A 1 387  ? 166.685 119.688 147.787 1.00 21.13 ?  387  TYR A CZ   1 
ATOM   2429  O OH   . TYR A 1 387  ? 167.648 119.334 148.703 1.00 20.47 ?  387  TYR A OH   1 
ATOM   2430  N N    . LEU A 1 388  ? 162.430 122.413 142.433 1.00 2.88  ?  388  LEU A N    1 
ATOM   2431  C CA   . LEU A 1 388  ? 161.423 122.557 141.385 1.00 8.04  ?  388  LEU A CA   1 
ATOM   2432  C C    . LEU A 1 388  ? 162.060 122.520 140.001 1.00 11.83 ?  388  LEU A C    1 
ATOM   2433  O O    . LEU A 1 388  ? 161.539 121.870 139.087 1.00 13.24 ?  388  LEU A O    1 
ATOM   2434  C CB   . LEU A 1 388  ? 160.644 123.859 141.586 1.00 6.56  ?  388  LEU A CB   1 
ATOM   2435  C CG   . LEU A 1 388  ? 159.728 124.347 140.460 1.00 6.15  ?  388  LEU A CG   1 
ATOM   2436  C CD1  . LEU A 1 388  ? 158.652 123.321 140.136 1.00 6.82  ?  388  LEU A CD1  1 
ATOM   2437  C CD2  . LEU A 1 388  ? 159.106 125.690 140.813 1.00 7.06  ?  388  LEU A CD2  1 
ATOM   2438  N N    . ILE A 1 389  ? 163.199 123.199 139.835 1.00 15.22 ?  389  ILE A N    1 
ATOM   2439  C CA   . ILE A 1 389  ? 163.897 123.182 138.548 1.00 12.99 ?  389  ILE A CA   1 
ATOM   2440  C C    . ILE A 1 389  ? 164.396 121.775 138.220 1.00 14.52 ?  389  ILE A C    1 
ATOM   2441  O O    . ILE A 1 389  ? 164.236 121.286 137.088 1.00 14.53 ?  389  ILE A O    1 
ATOM   2442  C CB   . ILE A 1 389  ? 165.042 124.213 138.553 1.00 12.30 ?  389  ILE A CB   1 
ATOM   2443  C CG1  . ILE A 1 389  ? 164.496 125.616 138.283 1.00 13.94 ?  389  ILE A CG1  1 
ATOM   2444  C CG2  . ILE A 1 389  ? 166.111 123.859 137.528 1.00 12.86 ?  389  ILE A CG2  1 
ATOM   2445  C CD1  . ILE A 1 389  ? 165.240 126.711 139.012 1.00 13.37 ?  389  ILE A CD1  1 
ATOM   2446  N N    . ILE A 1 390  ? 164.996 121.098 139.206 1.00 14.69 ?  390  ILE A N    1 
ATOM   2447  C CA   . ILE A 1 390  ? 165.505 119.745 138.980 1.00 13.63 ?  390  ILE A CA   1 
ATOM   2448  C C    . ILE A 1 390  ? 164.366 118.792 138.630 1.00 12.65 ?  390  ILE A C    1 
ATOM   2449  O O    . ILE A 1 390  ? 164.494 117.950 137.732 1.00 8.89  ?  390  ILE A O    1 
ATOM   2450  C CB   . ILE A 1 390  ? 166.299 119.256 140.207 1.00 11.28 ?  390  ILE A CB   1 
ATOM   2451  C CG1  . ILE A 1 390  ? 167.528 120.136 140.442 1.00 11.71 ?  390  ILE A CG1  1 
ATOM   2452  C CG2  . ILE A 1 390  ? 166.733 117.813 140.025 1.00 8.95  ?  390  ILE A CG2  1 
ATOM   2453  C CD1  . ILE A 1 390  ? 168.555 120.067 139.335 1.00 15.11 ?  390  ILE A CD1  1 
ATOM   2454  N N    . LEU A 1 391  ? 163.229 118.923 139.318 1.00 10.20 ?  391  LEU A N    1 
ATOM   2455  C CA   . LEU A 1 391  ? 162.068 118.089 139.027 1.00 10.10 ?  391  LEU A CA   1 
ATOM   2456  C C    . LEU A 1 391  ? 161.508 118.378 137.639 1.00 9.96  ?  391  LEU A C    1 
ATOM   2457  O O    . LEU A 1 391  ? 161.038 117.462 136.953 1.00 12.04 ?  391  LEU A O    1 
ATOM   2458  C CB   . LEU A 1 391  ? 161.004 118.302 140.105 1.00 10.91 ?  391  LEU A CB   1 
ATOM   2459  C CG   . LEU A 1 391  ? 159.561 117.869 139.847 1.00 10.43 ?  391  LEU A CG   1 
ATOM   2460  C CD1  . LEU A 1 391  ? 159.442 116.356 139.868 1.00 9.50  ?  391  LEU A CD1  1 
ATOM   2461  C CD2  . LEU A 1 391  ? 158.631 118.496 140.872 1.00 7.35  ?  391  LEU A CD2  1 
ATOM   2462  N N    . TYR A 1 392  ? 161.549 119.643 137.207 1.00 9.16  ?  392  TYR A N    1 
ATOM   2463  C CA   . TYR A 1 392  ? 161.088 119.976 135.862 1.00 9.61  ?  392  TYR A CA   1 
ATOM   2464  C C    . TYR A 1 392  ? 161.963 119.328 134.798 1.00 13.63 ?  392  TYR A C    1 
ATOM   2465  O O    . TYR A 1 392  ? 161.459 118.869 133.766 1.00 16.65 ?  392  TYR A O    1 
ATOM   2466  C CB   . TYR A 1 392  ? 161.054 121.490 135.661 1.00 8.47  ?  392  TYR A CB   1 
ATOM   2467  C CG   . TYR A 1 392  ? 160.690 121.878 134.245 1.00 10.71 ?  392  TYR A CG   1 
ATOM   2468  C CD1  . TYR A 1 392  ? 159.451 121.546 133.714 1.00 9.55  ?  392  TYR A CD1  1 
ATOM   2469  C CD2  . TYR A 1 392  ? 161.593 122.550 133.432 1.00 11.89 ?  392  TYR A CD2  1 
ATOM   2470  C CE1  . TYR A 1 392  ? 159.113 121.888 132.420 1.00 10.71 ?  392  TYR A CE1  1 
ATOM   2471  C CE2  . TYR A 1 392  ? 161.264 122.895 132.133 1.00 8.61  ?  392  TYR A CE2  1 
ATOM   2472  C CZ   . TYR A 1 392  ? 160.023 122.562 131.634 1.00 8.39  ?  392  TYR A CZ   1 
ATOM   2473  O OH   . TYR A 1 392  ? 159.690 122.902 130.344 1.00 7.95  ?  392  TYR A OH   1 
ATOM   2474  N N    . LEU A 1 393  ? 163.281 119.307 135.012 1.00 16.01 ?  393  LEU A N    1 
ATOM   2475  C CA   . LEU A 1 393  ? 164.142 118.563 134.090 1.00 15.50 ?  393  LEU A CA   1 
ATOM   2476  C C    . LEU A 1 393  ? 163.858 117.061 134.144 1.00 13.20 ?  393  LEU A C    1 
ATOM   2477  O O    . LEU A 1 393  ? 163.819 116.388 133.101 1.00 13.91 ?  393  LEU A O    1 
ATOM   2478  C CB   . LEU A 1 393  ? 165.618 118.841 134.379 1.00 12.76 ?  393  LEU A CB   1 
ATOM   2479  C CG   . LEU A 1 393  ? 166.285 120.057 133.721 1.00 7.81  ?  393  LEU A CG   1 
ATOM   2480  C CD1  . LEU A 1 393  ? 166.001 120.066 132.225 1.00 14.25 ?  393  LEU A CD1  1 
ATOM   2481  C CD2  . LEU A 1 393  ? 165.879 121.378 134.348 1.00 8.00  ?  393  LEU A CD2  1 
ATOM   2482  N N    . ALA A 1 394  ? 163.644 116.525 135.348 1.00 13.52 ?  394  ALA A N    1 
ATOM   2483  C CA   . ALA A 1 394  ? 163.513 115.080 135.512 1.00 13.43 ?  394  ALA A CA   1 
ATOM   2484  C C    . ALA A 1 394  ? 162.230 114.546 134.887 1.00 12.99 ?  394  ALA A C    1 
ATOM   2485  O O    . ALA A 1 394  ? 162.226 113.448 134.318 1.00 17.06 ?  394  ALA A O    1 
ATOM   2486  C CB   . ALA A 1 394  ? 163.579 114.714 136.992 1.00 11.23 ?  394  ALA A CB   1 
ATOM   2487  N N    . ILE A 1 395  ? 161.127 115.294 134.992 1.00 9.88  ?  395  ILE A N    1 
ATOM   2488  C CA   . ILE A 1 395  ? 159.870 114.811 134.423 1.00 10.38 ?  395  ILE A CA   1 
ATOM   2489  C C    . ILE A 1 395  ? 159.960 114.746 132.901 1.00 12.08 ?  395  ILE A C    1 
ATOM   2490  O O    . ILE A 1 395  ? 159.473 113.792 132.283 1.00 15.71 ?  395  ILE A O    1 
ATOM   2491  C CB   . ILE A 1 395  ? 158.676 115.662 134.901 1.00 12.19 ?  395  ILE A CB   1 
ATOM   2492  C CG1  . ILE A 1 395  ? 158.846 117.139 134.542 1.00 14.64 ?  395  ILE A CG1  1 
ATOM   2493  C CG2  . ILE A 1 395  ? 158.454 115.481 136.395 1.00 10.49 ?  395  ILE A CG2  1 
ATOM   2494  C CD1  . ILE A 1 395  ? 157.550 117.842 134.218 1.00 8.41  ?  395  ILE A CD1  1 
ATOM   2495  N N    . THR A 1 396  ? 160.621 115.725 132.277 1.00 13.92 ?  396  THR A N    1 
ATOM   2496  C CA   . THR A 1 396  ? 160.833 115.677 130.833 1.00 17.46 ?  396  THR A CA   1 
ATOM   2497  C C    . THR A 1 396  ? 161.745 114.519 130.446 1.00 20.26 ?  396  THR A C    1 
ATOM   2498  O O    . THR A 1 396  ? 161.501 113.837 129.439 1.00 17.32 ?  396  THR A O    1 
ATOM   2499  C CB   . THR A 1 396  ? 161.415 117.002 130.341 1.00 13.40 ?  396  THR A CB   1 
ATOM   2500  O OG1  . THR A 1 396  ? 160.878 118.080 131.118 1.00 14.72 ?  396  THR A OG1  1 
ATOM   2501  C CG2  . THR A 1 396  ? 161.080 117.222 128.875 1.00 11.58 ?  396  THR A CG2  1 
ATOM   2502  N N    . ILE A 1 397  ? 162.795 114.276 131.239 1.00 18.01 ?  397  ILE A N    1 
ATOM   2503  C CA   . ILE A 1 397  ? 163.721 113.186 130.932 1.00 8.47  ?  397  ILE A CA   1 
ATOM   2504  C C    . ILE A 1 397  ? 163.004 111.838 130.986 1.00 9.78  ?  397  ILE A C    1 
ATOM   2505  O O    . ILE A 1 397  ? 163.129 111.013 130.073 1.00 14.20 ?  397  ILE A O    1 
ATOM   2506  C CB   . ILE A 1 397  ? 164.931 113.228 131.882 1.00 10.67 ?  397  ILE A CB   1 
ATOM   2507  C CG1  . ILE A 1 397  ? 165.919 114.303 131.426 1.00 16.92 ?  397  ILE A CG1  1 
ATOM   2508  C CG2  . ILE A 1 397  ? 165.621 111.874 131.949 1.00 14.04 ?  397  ILE A CG2  1 
ATOM   2509  C CD1  . ILE A 1 397  ? 167.118 114.454 132.333 1.00 16.12 ?  397  ILE A CD1  1 
ATOM   2510  N N    . ILE A 1 398  ? 162.215 111.605 132.039 1.00 12.68 ?  398  ILE A N    1 
ATOM   2511  C CA   . ILE A 1 398  ? 161.529 110.318 132.142 1.00 14.66 ?  398  ILE A CA   1 
ATOM   2512  C C    . ILE A 1 398  ? 160.368 110.220 131.153 1.00 14.03 ?  398  ILE A C    1 
ATOM   2513  O O    . ILE A 1 398  ? 160.015 109.115 130.718 1.00 16.74 ?  398  ILE A O    1 
ATOM   2514  C CB   . ILE A 1 398  ? 161.081 110.042 133.592 1.00 10.12 ?  398  ILE A CB   1 
ATOM   2515  C CG1  . ILE A 1 398  ? 159.840 110.859 133.961 1.00 10.62 ?  398  ILE A CG1  1 
ATOM   2516  C CG2  . ILE A 1 398  ? 162.240 110.244 134.564 1.00 12.26 ?  398  ILE A CG2  1 
ATOM   2517  C CD1  . ILE A 1 398  ? 159.534 110.870 135.441 1.00 12.06 ?  398  ILE A CD1  1 
ATOM   2518  N N    . ALA A 1 399  ? 159.776 111.353 130.754 1.00 12.98 ?  399  ALA A N    1 
ATOM   2519  C CA   . ALA A 1 399  ? 158.751 111.320 129.716 1.00 14.36 ?  399  ALA A CA   1 
ATOM   2520  C C    . ALA A 1 399  ? 159.347 110.920 128.374 1.00 18.59 ?  399  ALA A C    1 
ATOM   2521  O O    . ALA A 1 399  ? 158.699 110.228 127.581 1.00 25.35 ?  399  ALA A O    1 
ATOM   2522  C CB   . ALA A 1 399  ? 158.057 112.670 129.611 1.00 30.00 ?  399  ALA A CB   1 
ATOM   2523  N N    . GLY A 1 400  ? 160.572 111.365 128.094 1.00 17.08 ?  400  GLY A N    1 
ATOM   2524  C CA   . GLY A 1 400  ? 161.276 110.855 126.929 1.00 15.81 ?  400  GLY A CA   1 
ATOM   2525  C C    . GLY A 1 400  ? 161.655 109.392 127.076 1.00 13.68 ?  400  GLY A C    1 
ATOM   2526  O O    . GLY A 1 400  ? 161.593 108.623 126.111 1.00 13.76 ?  400  GLY A O    1 
ATOM   2527  N N    . MET A 1 401  ? 162.053 108.989 128.285 1.00 18.00 ?  401  MET A N    1 
ATOM   2528  C CA   . MET A 1 401  ? 162.523 107.624 128.511 1.00 21.63 ?  401  MET A CA   1 
ATOM   2529  C C    . MET A 1 401  ? 161.413 106.596 128.306 1.00 23.82 ?  401  MET A C    1 
ATOM   2530  O O    . MET A 1 401  ? 161.643 105.545 127.691 1.00 25.19 ?  401  MET A O    1 
ATOM   2531  C CB   . MET A 1 401  ? 163.117 107.511 129.916 1.00 17.44 ?  401  MET A CB   1 
ATOM   2532  C CG   . MET A 1 401  ? 163.158 106.100 130.480 1.00 16.47 ?  401  MET A CG   1 
ATOM   2533  S SD   . MET A 1 401  ? 163.871 106.002 132.135 1.00 35.85 ?  401  MET A SD   1 
ATOM   2534  C CE   . MET A 1 401  ? 164.969 107.419 132.138 1.00 18.22 ?  401  MET A CE   1 
ATOM   2535  N N    . VAL A 1 402  ? 160.207 106.878 128.810 1.00 20.18 ?  402  VAL A N    1 
ATOM   2536  C CA   . VAL A 1 402  ? 159.122 105.901 128.706 1.00 21.24 ?  402  VAL A CA   1 
ATOM   2537  C C    . VAL A 1 402  ? 158.719 105.690 127.247 1.00 22.04 ?  402  VAL A C    1 
ATOM   2538  O O    . VAL A 1 402  ? 158.516 104.551 126.805 1.00 23.38 ?  402  VAL A O    1 
ATOM   2539  C CB   . VAL A 1 402  ? 157.923 106.311 129.588 1.00 20.80 ?  402  VAL A CB   1 
ATOM   2540  C CG1  . VAL A 1 402  ? 157.475 107.741 129.315 1.00 18.50 ?  402  VAL A CG1  1 
ATOM   2541  C CG2  . VAL A 1 402  ? 156.764 105.341 129.403 1.00 21.85 ?  402  VAL A CG2  1 
ATOM   2542  N N    . ILE A 1 403  ? 158.622 106.772 126.469 1.00 19.81 ?  403  ILE A N    1 
ATOM   2543  C CA   . ILE A 1 403  ? 158.250 106.629 125.065 1.00 21.29 ?  403  ILE A CA   1 
ATOM   2544  C C    . ILE A 1 403  ? 159.397 106.025 124.261 1.00 21.70 ?  403  ILE A C    1 
ATOM   2545  O O    . ILE A 1 403  ? 159.163 105.333 123.262 1.00 21.85 ?  403  ILE A O    1 
ATOM   2546  C CB   . ILE A 1 403  ? 157.778 107.980 124.486 1.00 20.40 ?  403  ILE A CB   1 
ATOM   2547  C CG1  . ILE A 1 403  ? 157.223 107.796 123.073 1.00 19.15 ?  403  ILE A CG1  1 
ATOM   2548  C CG2  . ILE A 1 403  ? 158.890 109.014 124.494 1.00 19.85 ?  403  ILE A CG2  1 
ATOM   2549  C CD1  . ILE A 1 403  ? 156.897 109.077 122.376 1.00 19.82 ?  403  ILE A CD1  1 
ATOM   2550  N N    . SER A 1 404  ? 160.647 106.251 124.678 1.00 20.29 ?  404  SER A N    1 
ATOM   2551  C CA   . SER A 1 404  ? 161.765 105.608 123.997 1.00 24.23 ?  404  SER A CA   1 
ATOM   2552  C C    . SER A 1 404  ? 161.764 104.103 124.230 1.00 25.00 ?  404  SER A C    1 
ATOM   2553  O O    . SER A 1 404  ? 162.052 103.327 123.311 1.00 23.75 ?  404  SER A O    1 
ATOM   2554  C CB   . SER A 1 404  ? 163.086 106.222 124.463 1.00 20.87 ?  404  SER A CB   1 
ATOM   2555  O OG   . SER A 1 404  ? 163.465 105.711 125.729 1.00 19.89 ?  404  SER A OG   1 
ATOM   2556  N N    . LEU A 1 405  ? 161.443 103.671 125.448 1.00 23.51 ?  405  LEU A N    1 
ATOM   2557  C CA   . LEU A 1 405  ? 161.508 102.256 125.789 1.00 23.98 ?  405  LEU A CA   1 
ATOM   2558  C C    . LEU A 1 405  ? 160.217 101.493 125.514 1.00 23.91 ?  405  LEU A C    1 
ATOM   2559  O O    . LEU A 1 405  ? 160.229 100.259 125.576 1.00 25.09 ?  405  LEU A O    1 
ATOM   2560  C CB   . LEU A 1 405  ? 161.884 102.085 127.265 1.00 19.24 ?  405  LEU A CB   1 
ATOM   2561  C CG   . LEU A 1 405  ? 163.346 102.348 127.628 1.00 20.38 ?  405  LEU A CG   1 
ATOM   2562  C CD1  . LEU A 1 405  ? 163.574 102.135 129.116 1.00 23.27 ?  405  LEU A CD1  1 
ATOM   2563  C CD2  . LEU A 1 405  ? 164.270 101.460 126.809 1.00 22.61 ?  405  LEU A CD2  1 
ATOM   2564  N N    . PHE A 1 406  ? 159.111 102.173 125.212 1.00 24.23 ?  406  PHE A N    1 
ATOM   2565  C CA   . PHE A 1 406  ? 157.835 101.482 125.067 1.00 25.42 ?  406  PHE A CA   1 
ATOM   2566  C C    . PHE A 1 406  ? 157.227 101.616 123.679 1.00 25.31 ?  406  PHE A C    1 
ATOM   2567  O O    . PHE A 1 406  ? 156.777 100.615 123.109 1.00 25.34 ?  406  PHE A O    1 
ATOM   2568  C CB   . PHE A 1 406  ? 156.844 101.993 126.126 1.00 28.60 ?  406  PHE A CB   1 
ATOM   2569  C CG   . PHE A 1 406  ? 156.988 101.321 127.462 1.00 30.24 ?  406  PHE A CG   1 
ATOM   2570  C CD1  . PHE A 1 406  ? 158.107 101.547 128.248 1.00 25.72 ?  406  PHE A CD1  1 
ATOM   2571  C CD2  . PHE A 1 406  ? 156.011 100.459 127.930 1.00 29.65 ?  406  PHE A CD2  1 
ATOM   2572  C CE1  . PHE A 1 406  ? 158.245 100.931 129.477 1.00 23.81 ?  406  PHE A CE1  1 
ATOM   2573  C CE2  . PHE A 1 406  ? 156.144 99.839  129.159 1.00 27.81 ?  406  PHE A CE2  1 
ATOM   2574  C CZ   . PHE A 1 406  ? 157.262 100.075 129.933 1.00 25.83 ?  406  PHE A CZ   1 
ATOM   2575  N N    . SER A 1 407  ? 157.185 102.828 123.126 1.00 23.35 ?  407  SER A N    1 
ATOM   2576  C CA   . SER A 1 407  ? 156.512 103.044 121.846 1.00 26.89 ?  407  SER A CA   1 
ATOM   2577  C C    . SER A 1 407  ? 157.119 102.300 120.653 1.00 26.22 ?  407  SER A C    1 
ATOM   2578  O O    . SER A 1 407  ? 156.334 101.772 119.845 1.00 24.24 ?  407  SER A O    1 
ATOM   2579  C CB   . SER A 1 407  ? 156.422 104.548 121.558 1.00 27.08 ?  407  SER A CB   1 
ATOM   2580  O OG   . SER A 1 407  ? 155.426 105.157 122.361 1.00 31.53 ?  407  SER A OG   1 
ATOM   2581  N N    . PRO A 1 408  ? 158.448 102.246 120.444 1.00 27.58 ?  408  PRO A N    1 
ATOM   2582  C CA   . PRO A 1 408  ? 158.954 101.479 119.288 1.00 27.24 ?  408  PRO A CA   1 
ATOM   2583  C C    . PRO A 1 408  ? 158.610 100.000 119.324 1.00 23.00 ?  408  PRO A C    1 
ATOM   2584  O O    . PRO A 1 408  ? 158.495 99.378  118.260 1.00 25.65 ?  408  PRO A O    1 
ATOM   2585  C CB   . PRO A 1 408  ? 160.471 101.703 119.355 1.00 26.59 ?  408  PRO A CB   1 
ATOM   2586  C CG   . PRO A 1 408  ? 160.626 102.979 120.070 1.00 27.11 ?  408  PRO A CG   1 
ATOM   2587  C CD   . PRO A 1 408  ? 159.551 102.969 121.106 1.00 24.47 ?  408  PRO A CD   1 
ATOM   2588  N N    . ILE A 1 409  ? 158.458 99.414  120.513 1.00 17.81 ?  409  ILE A N    1 
ATOM   2589  C CA   . ILE A 1 409  ? 158.018 98.025  120.604 1.00 21.72 ?  409  ILE A CA   1 
ATOM   2590  C C    . ILE A 1 409  ? 156.591 97.883  120.088 1.00 23.58 ?  409  ILE A C    1 
ATOM   2591  O O    . ILE A 1 409  ? 156.277 96.951  119.337 1.00 21.72 ?  409  ILE A O    1 
ATOM   2592  C CB   . ILE A 1 409  ? 158.154 97.518  122.052 1.00 22.09 ?  409  ILE A CB   1 
ATOM   2593  C CG1  . ILE A 1 409  ? 159.620 97.553  122.491 1.00 23.89 ?  409  ILE A CG1  1 
ATOM   2594  C CG2  . ILE A 1 409  ? 157.588 96.110  122.186 1.00 19.19 ?  409  ILE A CG2  1 
ATOM   2595  C CD1  . ILE A 1 409  ? 159.864 96.954  123.860 1.00 21.39 ?  409  ILE A CD1  1 
ATOM   2596  N N    . LEU A 1 410  ? 155.711 98.810  120.464 1.00 24.62 ?  410  LEU A N    1 
ATOM   2597  C CA   . LEU A 1 410  ? 154.305 98.756  120.060 1.00 24.74 ?  410  LEU A CA   1 
ATOM   2598  C C    . LEU A 1 410  ? 154.119 99.486  118.729 1.00 21.83 ?  410  LEU A C    1 
ATOM   2599  O O    . LEU A 1 410  ? 153.487 100.539 118.630 1.00 17.09 ?  410  LEU A O    1 
ATOM   2600  C CB   . LEU A 1 410  ? 153.413 99.336  121.150 1.00 20.03 ?  410  LEU A CB   1 
ATOM   2601  C CG   . LEU A 1 410  ? 152.896 98.363  122.215 1.00 21.50 ?  410  LEU A CG   1 
ATOM   2602  C CD1  . LEU A 1 410  ? 152.262 97.143  121.561 1.00 21.68 ?  410  LEU A CD1  1 
ATOM   2603  C CD2  . LEU A 1 410  ? 153.993 97.951  123.187 1.00 19.73 ?  410  LEU A CD2  1 
ATOM   2604  N N    . SER A 1 411  ? 154.697 98.893  117.686 1.00 23.49 ?  411  SER A N    1 
ATOM   2605  C CA   . SER A 1 411  ? 154.544 99.374  116.321 1.00 23.37 ?  411  SER A CA   1 
ATOM   2606  C C    . SER A 1 411  ? 153.534 98.556  115.527 1.00 23.07 ?  411  SER A C    1 
ATOM   2607  O O    . SER A 1 411  ? 153.459 98.697  114.302 1.00 22.28 ?  411  SER A O    1 
ATOM   2608  C CB   . SER A 1 411  ? 155.897 99.374  115.606 1.00 23.82 ?  411  SER A CB   1 
ATOM   2609  O OG   . SER A 1 411  ? 155.773 99.861  114.282 1.00 27.60 ?  411  SER A OG   1 
ATOM   2610  N N    . ARG A 1 412  ? 152.759 97.704  116.197 1.00 25.71 ?  412  ARG A N    1 
ATOM   2611  C CA   . ARG A 1 412  ? 151.803 96.821  115.543 1.00 26.08 ?  412  ARG A CA   1 
ATOM   2612  C C    . ARG A 1 412  ? 150.461 97.488  115.272 1.00 25.76 ?  412  ARG A C    1 
ATOM   2613  O O    . ARG A 1 412  ? 149.576 96.847  114.695 1.00 27.63 ?  412  ARG A O    1 
ATOM   2614  C CB   . ARG A 1 412  ? 151.589 95.564  116.390 1.00 26.16 ?  412  ARG A CB   1 
ATOM   2615  C CG   . ARG A 1 412  ? 152.811 94.659  116.488 1.00 28.22 ?  412  ARG A CG   1 
ATOM   2616  C CD   . ARG A 1 412  ? 153.566 94.874  117.791 1.00 26.42 ?  412  ARG A CD   1 
ATOM   2617  N NE   . ARG A 1 412  ? 154.749 94.026  117.883 1.00 27.25 ?  412  ARG A NE   1 
ATOM   2618  C CZ   . ARG A 1 412  ? 155.970 94.400  117.526 1.00 26.16 ?  412  ARG A CZ   1 
ATOM   2619  N NH1  . ARG A 1 412  ? 156.210 95.609  117.046 1.00 26.04 ?  412  ARG A NH1  1 
ATOM   2620  N NH2  . ARG A 1 412  ? 156.975 93.539  117.655 1.00 23.87 ?  412  ARG A NH2  1 
ATOM   2621  N N    . ILE A 1 413  ? 150.286 98.750  115.671 1.00 22.50 ?  413  ILE A N    1 
ATOM   2622  C CA   . ILE A 1 413  ? 149.020 99.446  115.464 1.00 25.07 ?  413  ILE A CA   1 
ATOM   2623  C C    . ILE A 1 413  ? 148.801 99.869  114.022 1.00 25.01 ?  413  ILE A C    1 
ATOM   2624  O O    . ILE A 1 413  ? 147.675 100.226 113.657 1.00 20.85 ?  413  ILE A O    1 
ATOM   2625  C CB   . ILE A 1 413  ? 148.933 100.689 116.371 1.00 22.59 ?  413  ILE A CB   1 
ATOM   2626  C CG1  . ILE A 1 413  ? 150.092 101.645 116.078 1.00 24.17 ?  413  ILE A CG1  1 
ATOM   2627  C CG2  . ILE A 1 413  ? 148.957 100.279 117.822 1.00 19.01 ?  413  ILE A CG2  1 
ATOM   2628  C CD1  . ILE A 1 413  ? 150.137 102.854 116.991 1.00 19.86 ?  413  ILE A CD1  1 
ATOM   2629  N N    . GLY A 1 414  ? 149.841 99.839  113.194 1.00 23.50 ?  414  GLY A N    1 
ATOM   2630  C CA   . GLY A 1 414  ? 149.751 100.336 111.839 1.00 24.64 ?  414  GLY A CA   1 
ATOM   2631  C C    . GLY A 1 414  ? 150.059 101.808 111.680 1.00 24.30 ?  414  GLY A C    1 
ATOM   2632  O O    . GLY A 1 414  ? 150.009 102.315 110.553 1.00 19.07 ?  414  GLY A O    1 
ATOM   2633  N N    . TYR A 1 415  ? 150.370 102.509 112.767 1.00 26.97 ?  415  TYR A N    1 
ATOM   2634  C CA   . TYR A 1 415  ? 150.753 103.919 112.734 1.00 28.73 ?  415  TYR A CA   1 
ATOM   2635  C C    . TYR A 1 415  ? 152.103 104.033 113.438 1.00 29.56 ?  415  TYR A C    1 
ATOM   2636  O O    . TYR A 1 415  ? 152.169 104.296 114.641 1.00 29.54 ?  415  TYR A O    1 
ATOM   2637  C CB   . TYR A 1 415  ? 149.692 104.805 113.394 1.00 27.64 ?  415  TYR A CB   1 
ATOM   2638  C CG   . TYR A 1 415  ? 148.290 104.235 113.344 1.00 30.34 ?  415  TYR A CG   1 
ATOM   2639  C CD1  . TYR A 1 415  ? 147.594 104.154 112.144 1.00 29.21 ?  415  TYR A CD1  1 
ATOM   2640  C CD2  . TYR A 1 415  ? 147.661 103.785 114.498 1.00 27.69 ?  415  TYR A CD2  1 
ATOM   2641  C CE1  . TYR A 1 415  ? 146.313 103.634 112.094 1.00 30.29 ?  415  TYR A CE1  1 
ATOM   2642  C CE2  . TYR A 1 415  ? 146.381 103.265 114.458 1.00 28.25 ?  415  TYR A CE2  1 
ATOM   2643  C CZ   . TYR A 1 415  ? 145.712 103.192 113.254 1.00 30.85 ?  415  TYR A CZ   1 
ATOM   2644  O OH   . TYR A 1 415  ? 144.438 102.676 113.209 1.00 29.72 ?  415  TYR A OH   1 
ATOM   2645  N N    . GLY A 1 416  ? 153.178 103.830 112.680 1.00 25.01 ?  416  GLY A N    1 
ATOM   2646  C CA   . GLY A 1 416  ? 154.505 103.898 113.253 1.00 24.17 ?  416  GLY A CA   1 
ATOM   2647  C C    . GLY A 1 416  ? 154.926 105.317 113.577 1.00 23.86 ?  416  GLY A C    1 
ATOM   2648  O O    . GLY A 1 416  ? 154.445 106.294 113.002 1.00 24.82 ?  416  GLY A O    1 
ATOM   2649  N N    . LEU A 1 417  ? 155.850 105.426 114.527 1.00 21.50 ?  417  LEU A N    1 
ATOM   2650  C CA   . LEU A 1 417  ? 156.357 106.718 114.961 1.00 21.07 ?  417  LEU A CA   1 
ATOM   2651  C C    . LEU A 1 417  ? 157.501 107.169 114.063 1.00 19.60 ?  417  LEU A C    1 
ATOM   2652  O O    . LEU A 1 417  ? 158.360 106.372 113.677 1.00 20.38 ?  417  LEU A O    1 
ATOM   2653  C CB   . LEU A 1 417  ? 156.820 106.658 116.419 1.00 19.25 ?  417  LEU A CB   1 
ATOM   2654  C CG   . LEU A 1 417  ? 157.900 105.641 116.798 1.00 24.55 ?  417  LEU A CG   1 
ATOM   2655  C CD1  . LEU A 1 417  ? 159.238 106.331 117.030 1.00 21.41 ?  417  LEU A CD1  1 
ATOM   2656  C CD2  . LEU A 1 417  ? 157.486 104.846 118.024 1.00 23.69 ?  417  LEU A CD2  1 
ATOM   2657  N N    . THR A 1 418  ? 157.494 108.450 113.720 1.00 19.17 ?  418  THR A N    1 
ATOM   2658  C CA   . THR A 1 418  ? 158.576 109.065 112.976 1.00 21.28 ?  418  THR A CA   1 
ATOM   2659  C C    . THR A 1 418  ? 159.516 109.764 113.954 1.00 21.65 ?  418  THR A C    1 
ATOM   2660  O O    . THR A 1 418  ? 159.359 109.674 115.175 1.00 24.08 ?  418  THR A O    1 
ATOM   2661  C CB   . THR A 1 418  ? 158.018 110.033 111.931 1.00 22.79 ?  418  THR A CB   1 
ATOM   2662  O OG1  . THR A 1 418  ? 157.705 111.284 112.556 1.00 21.95 ?  418  THR A OG1  1 
ATOM   2663  C CG2  . THR A 1 418  ? 156.761 109.462 111.293 1.00 21.48 ?  418  THR A CG2  1 
ATOM   2664  N N    . TRP A 1 419  ? 160.513 110.468 113.419 1.00 24.12 ?  419  TRP A N    1 
ATOM   2665  C CA   . TRP A 1 419  ? 161.393 111.248 114.278 1.00 26.53 ?  419  TRP A CA   1 
ATOM   2666  C C    . TRP A 1 419  ? 160.711 112.507 114.796 1.00 25.35 ?  419  TRP A C    1 
ATOM   2667  O O    . TRP A 1 419  ? 160.952 112.911 115.938 1.00 25.69 ?  419  TRP A O    1 
ATOM   2668  C CB   . TRP A 1 419  ? 162.674 111.619 113.531 1.00 26.44 ?  419  TRP A CB   1 
ATOM   2669  C CG   . TRP A 1 419  ? 163.896 111.506 114.379 1.00 27.25 ?  419  TRP A CG   1 
ATOM   2670  C CD1  . TRP A 1 419  ? 164.411 112.459 115.208 1.00 25.95 ?  419  TRP A CD1  1 
ATOM   2671  C CD2  . TRP A 1 419  ? 164.751 110.366 114.497 1.00 28.35 ?  419  TRP A CD2  1 
ATOM   2672  N NE1  . TRP A 1 419  ? 165.541 111.985 115.828 1.00 27.61 ?  419  TRP A NE1  1 
ATOM   2673  C CE2  . TRP A 1 419  ? 165.770 110.701 115.409 1.00 29.03 ?  419  TRP A CE2  1 
ATOM   2674  C CE3  . TRP A 1 419  ? 164.756 109.094 113.916 1.00 24.51 ?  419  TRP A CE3  1 
ATOM   2675  C CZ2  . TRP A 1 419  ? 166.785 109.811 115.754 1.00 26.87 ?  419  TRP A CZ2  1 
ATOM   2676  C CZ3  . TRP A 1 419  ? 165.763 108.213 114.259 1.00 25.42 ?  419  TRP A CZ3  1 
ATOM   2677  C CH2  . TRP A 1 419  ? 166.764 108.575 115.170 1.00 27.41 ?  419  TRP A CH2  1 
ATOM   2678  N N    . ARG A 1 420  ? 159.866 113.134 113.977 1.00 21.97 ?  420  ARG A N    1 
ATOM   2679  C CA   . ARG A 1 420  ? 159.209 114.371 114.389 1.00 26.12 ?  420  ARG A CA   1 
ATOM   2680  C C    . ARG A 1 420  ? 158.104 114.105 115.407 1.00 28.07 ?  420  ARG A C    1 
ATOM   2681  O O    . ARG A 1 420  ? 157.969 114.842 116.395 1.00 25.34 ?  420  ARG A O    1 
ATOM   2682  C CB   . ARG A 1 420  ? 158.648 115.090 113.159 1.00 26.80 ?  420  ARG A CB   1 
ATOM   2683  C CG   . ARG A 1 420  ? 157.794 116.307 113.473 1.00 26.66 ?  420  ARG A CG   1 
ATOM   2684  C CD   . ARG A 1 420  ? 156.545 116.372 112.597 1.00 24.64 ?  420  ARG A CD   1 
ATOM   2685  N NE   . ARG A 1 420  ? 156.793 116.947 111.279 1.00 22.96 ?  420  ARG A NE   1 
ATOM   2686  C CZ   . ARG A 1 420  ? 155.857 117.125 110.355 1.00 27.17 ?  420  ARG A CZ   1 
ATOM   2687  N NH1  . ARG A 1 420  ? 154.599 116.775 110.569 1.00 23.61 ?  420  ARG A NH1  1 
ATOM   2688  N NH2  . ARG A 1 420  ? 156.190 117.673 109.190 1.00 28.52 ?  420  ARG A NH2  1 
ATOM   2689  N N    . ASN A 1 421  ? 157.310 113.053 115.182 1.00 24.97 ?  421  ASN A N    1 
ATOM   2690  C CA   . ASN A 1 421  ? 156.129 112.802 116.002 1.00 21.90 ?  421  ASN A CA   1 
ATOM   2691  C C    . ASN A 1 421  ? 156.499 112.431 117.432 1.00 21.35 ?  421  ASN A C    1 
ATOM   2692  O O    . ASN A 1 421  ? 155.828 112.858 118.380 1.00 24.91 ?  421  ASN A O    1 
ATOM   2693  C CB   . ASN A 1 421  ? 155.280 111.701 115.371 1.00 21.76 ?  421  ASN A CB   1 
ATOM   2694  C CG   . ASN A 1 421  ? 154.632 112.138 114.075 1.00 23.85 ?  421  ASN A CG   1 
ATOM   2695  O OD1  . ASN A 1 421  ? 154.673 113.314 113.715 1.00 22.90 ?  421  ASN A OD1  1 
ATOM   2696  N ND2  . ASN A 1 421  ? 154.025 111.193 113.368 1.00 20.33 ?  421  ASN A ND2  1 
ATOM   2697  N N    . ALA A 1 422  ? 157.549 111.623 117.607 1.00 18.11 ?  422  ALA A N    1 
ATOM   2698  C CA   . ALA A 1 422  ? 157.954 111.218 118.949 1.00 20.52 ?  422  ALA A CA   1 
ATOM   2699  C C    . ALA A 1 422  ? 158.388 112.419 119.779 1.00 23.28 ?  422  ALA A C    1 
ATOM   2700  O O    . ALA A 1 422  ? 157.995 112.552 120.945 1.00 22.81 ?  422  ALA A O    1 
ATOM   2701  C CB   . ALA A 1 422  ? 159.078 110.185 118.870 1.00 20.20 ?  422  ALA A CB   1 
ATOM   2702  N N    . VAL A 1 423  ? 159.172 113.319 119.185 1.00 23.69 ?  423  VAL A N    1 
ATOM   2703  C CA   . VAL A 1 423  ? 159.627 114.500 119.909 1.00 22.15 ?  423  VAL A CA   1 
ATOM   2704  C C    . VAL A 1 423  ? 158.465 115.452 120.174 1.00 20.86 ?  423  VAL A C    1 
ATOM   2705  O O    . VAL A 1 423  ? 158.394 116.076 121.241 1.00 25.18 ?  423  VAL A O    1 
ATOM   2706  C CB   . VAL A 1 423  ? 160.775 115.185 119.148 1.00 23.90 ?  423  VAL A CB   1 
ATOM   2707  C CG1  . VAL A 1 423  ? 161.360 116.319 119.970 1.00 20.94 ?  423  VAL A CG1  1 
ATOM   2708  C CG2  . VAL A 1 423  ? 161.855 114.172 118.819 1.00 21.05 ?  423  VAL A CG2  1 
ATOM   2709  N N    . ILE A 1 424  ? 157.531 115.573 119.222 1.00 16.72 ?  424  ILE A N    1 
ATOM   2710  C CA   . ILE A 1 424  ? 156.362 116.425 119.445 1.00 19.51 ?  424  ILE A CA   1 
ATOM   2711  C C    . ILE A 1 424  ? 155.531 115.910 120.614 1.00 18.34 ?  424  ILE A C    1 
ATOM   2712  O O    . ILE A 1 424  ? 155.152 116.675 121.509 1.00 19.82 ?  424  ILE A O    1 
ATOM   2713  C CB   . ILE A 1 424  ? 155.518 116.542 118.161 1.00 21.57 ?  424  ILE A CB   1 
ATOM   2714  C CG1  . ILE A 1 424  ? 156.100 117.603 117.230 1.00 23.34 ?  424  ILE A CG1  1 
ATOM   2715  C CG2  . ILE A 1 424  ? 154.067 116.873 118.483 1.00 15.48 ?  424  ILE A CG2  1 
ATOM   2716  C CD1  . ILE A 1 424  ? 155.398 117.675 115.898 1.00 20.84 ?  424  ILE A CD1  1 
ATOM   2717  N N    . MET A 1 425  ? 155.260 114.607 120.648 1.00 15.87 ?  425  MET A N    1 
ATOM   2718  C CA   . MET A 1 425  ? 154.393 114.076 121.689 1.00 14.72 ?  425  MET A CA   1 
ATOM   2719  C C    . MET A 1 425  ? 155.119 113.822 123.005 1.00 17.23 ?  425  MET A C    1 
ATOM   2720  O O    . MET A 1 425  ? 154.455 113.559 124.014 1.00 24.94 ?  425  MET A O    1 
ATOM   2721  C CB   . MET A 1 425  ? 153.702 112.795 121.205 1.00 17.61 ?  425  MET A CB   1 
ATOM   2722  C CG   . MET A 1 425  ? 154.461 111.518 121.470 1.00 19.46 ?  425  MET A CG   1 
ATOM   2723  S SD   . MET A 1 425  ? 153.759 110.089 120.619 1.00 24.56 ?  425  MET A SD   1 
ATOM   2724  C CE   . MET A 1 425  ? 153.223 110.827 119.078 1.00 19.50 ?  425  MET A CE   1 
ATOM   2725  N N    . THR A 1 426  ? 156.452 113.905 123.034 1.00 9.90  ?  426  THR A N    1 
ATOM   2726  C CA   . THR A 1 426  ? 157.155 113.904 124.310 1.00 17.38 ?  426  THR A CA   1 
ATOM   2727  C C    . THR A 1 426  ? 157.482 115.303 124.818 1.00 15.02 ?  426  THR A C    1 
ATOM   2728  O O    . THR A 1 426  ? 157.822 115.449 125.997 1.00 11.94 ?  426  THR A O    1 
ATOM   2729  C CB   . THR A 1 426  ? 158.455 113.090 124.224 1.00 19.57 ?  426  THR A CB   1 
ATOM   2730  O OG1  . THR A 1 426  ? 158.921 112.802 125.548 1.00 13.87 ?  426  THR A OG1  1 
ATOM   2731  C CG2  . THR A 1 426  ? 159.535 113.867 123.500 1.00 15.08 ?  426  THR A CG2  1 
ATOM   2732  N N    . TRP A 1 427  ? 157.388 116.330 123.970 1.00 19.33 ?  427  TRP A N    1 
ATOM   2733  C CA   . TRP A 1 427  ? 157.641 117.697 124.410 1.00 11.83 ?  427  TRP A CA   1 
ATOM   2734  C C    . TRP A 1 427  ? 156.363 118.424 124.802 1.00 14.05 ?  427  TRP A C    1 
ATOM   2735  O O    . TRP A 1 427  ? 156.367 119.210 125.755 1.00 16.36 ?  427  TRP A O    1 
ATOM   2736  C CB   . TRP A 1 427  ? 158.364 118.484 123.314 1.00 7.08  ?  427  TRP A CB   1 
ATOM   2737  C CG   . TRP A 1 427  ? 158.629 119.920 123.673 1.00 8.89  ?  427  TRP A CG   1 
ATOM   2738  C CD1  . TRP A 1 427  ? 158.070 121.024 123.097 1.00 11.56 ?  427  TRP A CD1  1 
ATOM   2739  C CD2  . TRP A 1 427  ? 159.524 120.405 124.682 1.00 11.26 ?  427  TRP A CD2  1 
ATOM   2740  N NE1  . TRP A 1 427  ? 158.558 122.164 123.686 1.00 10.66 ?  427  TRP A NE1  1 
ATOM   2741  C CE2  . TRP A 1 427  ? 159.453 121.812 124.662 1.00 9.61  ?  427  TRP A CE2  1 
ATOM   2742  C CE3  . TRP A 1 427  ? 160.378 119.787 125.600 1.00 13.38 ?  427  TRP A CE3  1 
ATOM   2743  C CZ2  . TRP A 1 427  ? 160.201 122.609 125.524 1.00 9.79  ?  427  TRP A CZ2  1 
ATOM   2744  C CZ3  . TRP A 1 427  ? 161.119 120.580 126.455 1.00 8.20  ?  427  TRP A CZ3  1 
ATOM   2745  C CH2  . TRP A 1 427  ? 161.026 121.976 126.411 1.00 8.05  ?  427  TRP A CH2  1 
ATOM   2746  N N    . GLY A 1 428  ? 155.267 118.178 124.090 1.00 12.59 ?  428  GLY A N    1 
ATOM   2747  C CA   . GLY A 1 428  ? 154.010 118.829 124.401 1.00 8.50  ?  428  GLY A CA   1 
ATOM   2748  C C    . GLY A 1 428  ? 153.214 118.125 125.479 1.00 13.15 ?  428  GLY A C    1 
ATOM   2749  O O    . GLY A 1 428  ? 152.002 117.937 125.343 1.00 16.76 ?  428  GLY A O    1 
ATOM   2750  N N    . GLY A 1 429  ? 153.887 117.722 126.553 1.00 15.90 ?  429  GLY A N    1 
ATOM   2751  C CA   . GLY A 1 429  ? 153.220 117.113 127.685 1.00 12.64 ?  429  GLY A CA   1 
ATOM   2752  C C    . GLY A 1 429  ? 152.762 118.138 128.701 1.00 12.48 ?  429  GLY A C    1 
ATOM   2753  O O    . GLY A 1 429  ? 153.336 118.241 129.789 1.00 11.59 ?  429  GLY A O    1 
ATOM   2754  N N    . LEU A 1 430  ? 151.738 118.910 128.351 1.00 12.43 ?  430  LEU A N    1 
ATOM   2755  C CA   . LEU A 1 430  ? 151.219 119.923 129.256 1.00 9.44  ?  430  LEU A CA   1 
ATOM   2756  C C    . LEU A 1 430  ? 150.517 119.276 130.443 1.00 11.06 ?  430  LEU A C    1 
ATOM   2757  O O    . LEU A 1 430  ? 149.929 118.198 130.335 1.00 22.66 ?  430  LEU A O    1 
ATOM   2758  C CB   . LEU A 1 430  ? 150.248 120.850 128.525 1.00 10.27 ?  430  LEU A CB   1 
ATOM   2759  C CG   . LEU A 1 430  ? 150.845 121.891 127.580 1.00 11.15 ?  430  LEU A CG   1 
ATOM   2760  C CD1  . LEU A 1 430  ? 149.746 122.750 126.975 1.00 12.31 ?  430  LEU A CD1  1 
ATOM   2761  C CD2  . LEU A 1 430  ? 151.861 122.750 128.308 1.00 13.86 ?  430  LEU A CD2  1 
ATOM   2762  N N    . ARG A 1 431  ? 150.597 119.941 131.588 1.00 2.13  ?  431  ARG A N    1 
ATOM   2763  C CA   . ARG A 1 431  ? 149.840 119.534 132.759 1.00 3.48  ?  431  ARG A CA   1 
ATOM   2764  C C    . ARG A 1 431  ? 148.549 120.343 132.842 1.00 6.92  ?  431  ARG A C    1 
ATOM   2765  O O    . ARG A 1 431  ? 148.456 121.463 132.335 1.00 11.98 ?  431  ARG A O    1 
ATOM   2766  C CB   . ARG A 1 431  ? 150.673 119.712 134.027 1.00 7.65  ?  431  ARG A CB   1 
ATOM   2767  C CG   . ARG A 1 431  ? 152.040 119.046 133.964 1.00 3.02  ?  431  ARG A CG   1 
ATOM   2768  C CD   . ARG A 1 431  ? 151.992 117.629 134.501 1.00 0.00  ?  431  ARG A CD   1 
ATOM   2769  N NE   . ARG A 1 431  ? 153.301 116.988 134.493 1.00 9.15  ?  431  ARG A NE   1 
ATOM   2770  C CZ   . ARG A 1 431  ? 153.725 116.162 133.547 1.00 9.68  ?  431  ARG A CZ   1 
ATOM   2771  N NH1  . ARG A 1 431  ? 152.971 115.864 132.503 1.00 8.48  ?  431  ARG A NH1  1 
ATOM   2772  N NH2  . ARG A 1 431  ? 154.935 115.621 133.652 1.00 8.13  ?  431  ARG A NH2  1 
ATOM   2773  N N    . GLY A 1 432  ? 147.545 119.760 133.492 1.00 8.83  ?  432  GLY A N    1 
ATOM   2774  C CA   . GLY A 1 432  ? 146.211 120.315 133.499 1.00 12.84 ?  432  GLY A CA   1 
ATOM   2775  C C    . GLY A 1 432  ? 145.681 120.507 134.908 1.00 5.32  ?  432  GLY A C    1 
ATOM   2776  O O    . GLY A 1 432  ? 146.429 120.759 135.853 1.00 1.70  ?  432  GLY A O    1 
ATOM   2777  N N    . ALA A 1 433  ? 144.359 120.391 135.030 1.00 1.85  ?  433  ALA A N    1 
ATOM   2778  C CA   . ALA A 1 433  ? 143.672 120.642 136.288 1.00 0.00  ?  433  ALA A CA   1 
ATOM   2779  C C    . ALA A 1 433  ? 143.426 119.386 137.109 1.00 4.48  ?  433  ALA A C    1 
ATOM   2780  O O    . ALA A 1 433  ? 143.004 119.501 138.262 1.00 10.99 ?  433  ALA A O    1 
ATOM   2781  C CB   . ALA A 1 433  ? 142.335 121.340 136.032 1.00 0.00  ?  433  ALA A CB   1 
ATOM   2782  N N    . VAL A 1 434  ? 143.668 118.198 136.553 1.00 3.56  ?  434  VAL A N    1 
ATOM   2783  C CA   . VAL A 1 434  ? 143.520 116.974 137.336 1.00 0.00  ?  434  VAL A CA   1 
ATOM   2784  C C    . VAL A 1 434  ? 144.570 116.924 138.439 1.00 6.56  ?  434  VAL A C    1 
ATOM   2785  O O    . VAL A 1 434  ? 144.255 116.685 139.612 1.00 15.12 ?  434  VAL A O    1 
ATOM   2786  C CB   . VAL A 1 434  ? 143.601 115.740 136.419 1.00 0.00  ?  434  VAL A CB   1 
ATOM   2787  C CG1  . VAL A 1 434  ? 143.828 114.481 137.236 1.00 1.75  ?  434  VAL A CG1  1 
ATOM   2788  C CG2  . VAL A 1 434  ? 142.339 115.619 135.582 1.00 0.00  ?  434  VAL A CG2  1 
ATOM   2789  N N    . GLY A 1 435  ? 145.830 117.181 138.083 1.00 0.00  ?  435  GLY A N    1 
ATOM   2790  C CA   . GLY A 1 435  ? 146.884 117.208 139.082 1.00 0.00  ?  435  GLY A CA   1 
ATOM   2791  C C    . GLY A 1 435  ? 146.727 118.349 140.068 1.00 1.09  ?  435  GLY A C    1 
ATOM   2792  O O    . GLY A 1 435  ? 147.024 118.198 141.255 1.00 0.55  ?  435  GLY A O    1 
ATOM   2793  N N    . LEU A 1 436  ? 146.251 119.503 139.592 1.00 0.67  ?  436  LEU A N    1 
ATOM   2794  C CA   . LEU A 1 436  ? 145.989 120.627 140.486 1.00 0.00  ?  436  LEU A CA   1 
ATOM   2795  C C    . LEU A 1 436  ? 144.882 120.295 141.479 1.00 3.59  ?  436  LEU A C    1 
ATOM   2796  O O    . LEU A 1 436  ? 144.971 120.650 142.660 1.00 8.96  ?  436  LEU A O    1 
ATOM   2797  C CB   . LEU A 1 436  ? 145.624 121.869 139.675 1.00 0.00  ?  436  LEU A CB   1 
ATOM   2798  C CG   . LEU A 1 436  ? 146.763 122.609 138.973 1.00 0.00  ?  436  LEU A CG   1 
ATOM   2799  C CD1  . LEU A 1 436  ? 146.238 123.859 138.296 1.00 0.57  ?  436  LEU A CD1  1 
ATOM   2800  C CD2  . LEU A 1 436  ? 147.865 122.953 139.958 1.00 0.00  ?  436  LEU A CD2  1 
ATOM   2801  N N    . ALA A 1 437  ? 143.834 119.608 141.017 1.00 0.00  ?  437  ALA A N    1 
ATOM   2802  C CA   . ALA A 1 437  ? 142.755 119.193 141.907 1.00 0.00  ?  437  ALA A CA   1 
ATOM   2803  C C    . ALA A 1 437  ? 143.242 118.184 142.939 1.00 0.00  ?  437  ALA A C    1 
ATOM   2804  O O    . ALA A 1 437  ? 142.866 118.260 144.114 1.00 13.76 ?  437  ALA A O    1 
ATOM   2805  C CB   . ALA A 1 437  ? 141.600 118.614 141.093 1.00 0.00  ?  437  ALA A CB   1 
ATOM   2806  N N    . LEU A 1 438  ? 144.076 117.229 142.519 1.00 3.43  ?  438  LEU A N    1 
ATOM   2807  C CA   . LEU A 1 438  ? 144.621 116.265 143.474 1.00 0.00  ?  438  LEU A CA   1 
ATOM   2808  C C    . LEU A 1 438  ? 145.524 116.946 144.498 1.00 0.61  ?  438  LEU A C    1 
ATOM   2809  O O    . LEU A 1 438  ? 145.506 116.591 145.684 1.00 3.36  ?  438  LEU A O    1 
ATOM   2810  C CB   . LEU A 1 438  ? 145.380 115.162 142.742 1.00 0.00  ?  438  LEU A CB   1 
ATOM   2811  C CG   . LEU A 1 438  ? 144.577 114.325 141.746 1.00 0.00  ?  438  LEU A CG   1 
ATOM   2812  C CD1  . LEU A 1 438  ? 145.442 113.238 141.125 1.00 1.31  ?  438  LEU A CD1  1 
ATOM   2813  C CD2  . LEU A 1 438  ? 143.342 113.743 142.396 1.00 0.00  ?  438  LEU A CD2  1 
ATOM   2814  N N    . ALA A 1 439  ? 146.317 117.927 144.061 1.00 0.00  ?  439  ALA A N    1 
ATOM   2815  C CA   . ALA A 1 439  ? 147.160 118.673 144.989 1.00 0.00  ?  439  ALA A CA   1 
ATOM   2816  C C    . ALA A 1 439  ? 146.325 119.489 145.968 1.00 0.00  ?  439  ALA A C    1 
ATOM   2817  O O    . ALA A 1 439  ? 146.677 119.600 147.148 1.00 3.87  ?  439  ALA A O    1 
ATOM   2818  C CB   . ALA A 1 439  ? 148.114 119.577 144.214 1.00 0.00  ?  439  ALA A CB   1 
ATOM   2819  N N    . LEU A 1 440  ? 145.215 120.066 145.497 1.00 0.83  ?  440  LEU A N    1 
ATOM   2820  C CA   . LEU A 1 440  ? 144.301 120.774 146.389 1.00 0.00  ?  440  LEU A CA   1 
ATOM   2821  C C    . LEU A 1 440  ? 143.682 119.828 147.411 1.00 0.38  ?  440  LEU A C    1 
ATOM   2822  O O    . LEU A 1 440  ? 143.517 120.187 148.583 1.00 7.65  ?  440  LEU A O    1 
ATOM   2823  C CB   . LEU A 1 440  ? 143.207 121.467 145.576 1.00 1.66  ?  440  LEU A CB   1 
ATOM   2824  C CG   . LEU A 1 440  ? 143.543 122.788 144.882 1.00 0.00  ?  440  LEU A CG   1 
ATOM   2825  C CD1  . LEU A 1 440  ? 142.325 123.334 144.157 1.00 0.00  ?  440  LEU A CD1  1 
ATOM   2826  C CD2  . LEU A 1 440  ? 144.066 123.798 145.882 1.00 2.39  ?  440  LEU A CD2  1 
ATOM   2827  N N    . VAL A 1 441  ? 143.330 118.614 146.979 1.00 9.68  ?  441  VAL A N    1 
ATOM   2828  C CA   . VAL A 1 441  ? 142.778 117.614 147.893 1.00 0.00  ?  441  VAL A CA   1 
ATOM   2829  C C    . VAL A 1 441  ? 143.800 117.241 148.962 1.00 0.00  ?  441  VAL A C    1 
ATOM   2830  O O    . VAL A 1 441  ? 143.470 117.146 150.152 1.00 10.81 ?  441  VAL A O    1 
ATOM   2831  C CB   . VAL A 1 441  ? 142.304 116.380 147.101 1.00 0.00  ?  441  VAL A CB   1 
ATOM   2832  C CG1  . VAL A 1 441  ? 142.097 115.190 148.019 1.00 0.00  ?  441  VAL A CG1  1 
ATOM   2833  C CG2  . VAL A 1 441  ? 141.028 116.697 146.343 1.00 0.47  ?  441  VAL A CG2  1 
ATOM   2834  N N    . VAL A 1 442  ? 145.056 117.035 148.556 1.00 7.13  ?  442  VAL A N    1 
ATOM   2835  C CA   . VAL A 1 442  ? 146.115 116.712 149.512 1.00 3.30  ?  442  VAL A CA   1 
ATOM   2836  C C    . VAL A 1 442  ? 146.326 117.860 150.492 1.00 1.56  ?  442  VAL A C    1 
ATOM   2837  O O    . VAL A 1 442  ? 146.486 117.644 151.700 1.00 6.87  ?  442  VAL A O    1 
ATOM   2838  C CB   . VAL A 1 442  ? 147.417 116.358 148.769 1.00 0.00  ?  442  VAL A CB   1 
ATOM   2839  C CG1  . VAL A 1 442  ? 148.586 116.283 149.735 1.00 3.56  ?  442  VAL A CG1  1 
ATOM   2840  C CG2  . VAL A 1 442  ? 147.262 115.048 148.047 1.00 1.20  ?  442  VAL A CG2  1 
ATOM   2841  N N    . GLU A 1 443  ? 146.328 119.097 149.988 1.00 8.74  ?  443  GLU A N    1 
ATOM   2842  C CA   . GLU A 1 443  ? 146.525 120.256 150.853 1.00 3.69  ?  443  GLU A CA   1 
ATOM   2843  C C    . GLU A 1 443  ? 145.388 120.401 151.857 1.00 4.63  ?  443  GLU A C    1 
ATOM   2844  O O    . GLU A 1 443  ? 145.616 120.776 153.013 1.00 8.58  ?  443  GLU A O    1 
ATOM   2845  C CB   . GLU A 1 443  ? 146.654 121.521 150.008 1.00 3.86  ?  443  GLU A CB   1 
ATOM   2846  C CG   . GLU A 1 443  ? 147.539 122.586 150.624 1.00 9.10  ?  443  GLU A CG   1 
ATOM   2847  C CD   . GLU A 1 443  ? 146.756 123.791 151.097 1.00 14.31 ?  443  GLU A CD   1 
ATOM   2848  O OE1  . GLU A 1 443  ? 145.592 123.949 150.675 1.00 11.96 ?  443  GLU A OE1  1 
ATOM   2849  O OE2  . GLU A 1 443  ? 147.308 124.581 151.891 1.00 16.45 ?  443  GLU A OE2  1 
ATOM   2850  N N    . ASN A 1 444  ? 144.154 120.126 151.429 1.00 5.75  ?  444  ASN A N    1 
ATOM   2851  C CA   . ASN A 1 444  ? 143.028 120.162 152.357 1.00 1.92  ?  444  ASN A CA   1 
ATOM   2852  C C    . ASN A 1 444  ? 143.131 119.060 153.406 1.00 2.27  ?  444  ASN A C    1 
ATOM   2853  O O    . ASN A 1 444  ? 142.856 119.296 154.587 1.00 3.06  ?  444  ASN A O    1 
ATOM   2854  C CB   . ASN A 1 444  ? 141.711 120.050 151.592 1.00 3.42  ?  444  ASN A CB   1 
ATOM   2855  C CG   . ASN A 1 444  ? 141.104 121.403 151.278 1.00 10.43 ?  444  ASN A CG   1 
ATOM   2856  O OD1  . ASN A 1 444  ? 141.155 121.871 150.141 1.00 7.43  ?  444  ASN A OD1  1 
ATOM   2857  N ND2  . ASN A 1 444  ? 140.522 122.038 152.289 1.00 10.00 ?  444  ASN A ND2  1 
ATOM   2858  N N    . LEU A 1 445  ? 143.525 117.850 152.997 1.00 1.82  ?  445  LEU A N    1 
ATOM   2859  C CA   . LEU A 1 445  ? 143.565 116.737 153.942 1.00 0.00  ?  445  LEU A CA   1 
ATOM   2860  C C    . LEU A 1 445  ? 144.732 116.846 154.918 1.00 5.48  ?  445  LEU A C    1 
ATOM   2861  O O    . LEU A 1 445  ? 144.650 116.316 156.032 1.00 13.94 ?  445  LEU A O    1 
ATOM   2862  C CB   . LEU A 1 445  ? 143.637 115.406 153.193 1.00 0.97  ?  445  LEU A CB   1 
ATOM   2863  C CG   . LEU A 1 445  ? 142.392 114.958 152.428 1.00 0.21  ?  445  LEU A CG   1 
ATOM   2864  C CD1  . LEU A 1 445  ? 142.616 113.592 151.802 1.00 3.81  ?  445  LEU A CD1  1 
ATOM   2865  C CD2  . LEU A 1 445  ? 141.183 114.936 153.343 1.00 0.00  ?  445  LEU A CD2  1 
ATOM   2866  N N    . ALA A 1 446  ? 145.819 117.514 154.524 1.00 8.40  ?  446  ALA A N    1 
ATOM   2867  C CA   . ALA A 1 446  ? 147.023 117.538 155.351 1.00 6.29  ?  446  ALA A CA   1 
ATOM   2868  C C    . ALA A 1 446  ? 146.802 118.308 156.649 1.00 8.27  ?  446  ALA A C    1 
ATOM   2869  O O    . ALA A 1 446  ? 147.207 117.855 157.726 1.00 8.27  ?  446  ALA A O    1 
ATOM   2870  C CB   . ALA A 1 446  ? 148.187 118.137 154.563 1.00 10.82 ?  446  ALA A CB   1 
ATOM   2871  N N    . GLY A 1 447  ? 146.169 119.461 156.570 1.00 20.00 ?  447  GLY A N    1 
ATOM   2872  C CA   . GLY A 1 447  ? 145.942 120.289 157.751 1.00 21.89 ?  447  GLY A CA   1 
ATOM   2873  C C    . GLY A 1 447  ? 147.036 121.338 157.911 1.00 24.66 ?  447  GLY A C    1 
ATOM   2874  O O    . GLY A 1 447  ? 147.262 122.136 157.005 1.00 22.23 ?  447  GLY A O    1 
ATOM   2875  N N    . ASN A 1 448  ? 147.704 121.327 159.062 1.00 26.08 ?  448  ASN A N    1 
ATOM   2876  C CA   . ASN A 1 448  ? 148.786 122.260 159.342 1.00 24.19 ?  448  ASN A CA   1 
ATOM   2877  C C    . ASN A 1 448  ? 150.159 121.709 158.981 1.00 26.93 ?  448  ASN A C    1 
ATOM   2878  O O    . ASN A 1 448  ? 151.159 122.407 159.172 1.00 28.56 ?  448  ASN A O    1 
ATOM   2879  C CB   . ASN A 1 448  ? 148.770 122.661 160.820 1.00 22.65 ?  448  ASN A CB   1 
ATOM   2880  C CG   . ASN A 1 448  ? 147.931 123.897 161.079 1.00 25.85 ?  448  ASN A CG   1 
ATOM   2881  O OD1  . ASN A 1 448  ? 148.286 125.000 160.663 1.00 28.63 ?  448  ASN A OD1  1 
ATOM   2882  N ND2  . ASN A 1 448  ? 146.811 123.718 161.769 1.00 25.70 ?  448  ASN A ND2  1 
ATOM   2883  N N    . ASP A 1 449  ? 150.234 120.482 158.471 1.00 23.12 ?  449  ASP A N    1 
ATOM   2884  C CA   . ASP A 1 449  ? 151.516 119.902 158.100 1.00 17.34 ?  449  ASP A CA   1 
ATOM   2885  C C    . ASP A 1 449  ? 152.044 120.533 156.816 1.00 20.11 ?  449  ASP A C    1 
ATOM   2886  O O    . ASP A 1 449  ? 151.284 121.020 155.975 1.00 21.14 ?  449  ASP A O    1 
ATOM   2887  C CB   . ASP A 1 449  ? 151.386 118.389 157.927 1.00 19.15 ?  449  ASP A CB   1 
ATOM   2888  C CG   . ASP A 1 449  ? 150.549 117.750 159.015 1.00 23.46 ?  449  ASP A CG   1 
ATOM   2889  O OD1  . ASP A 1 449  ? 150.540 118.280 160.146 1.00 23.71 ?  449  ASP A OD1  1 
ATOM   2890  O OD2  . ASP A 1 449  ? 149.901 116.718 158.742 1.00 22.56 ?  449  ASP A OD2  1 
ATOM   2891  N N    . VAL A 1 450  ? 153.373 120.515 156.669 1.00 23.37 ?  450  VAL A N    1 
ATOM   2892  C CA   . VAL A 1 450  ? 154.015 121.139 155.513 1.00 21.43 ?  450  VAL A CA   1 
ATOM   2893  C C    . VAL A 1 450  ? 153.936 120.293 154.253 1.00 16.91 ?  450  VAL A C    1 
ATOM   2894  O O    . VAL A 1 450  ? 154.322 120.773 153.177 1.00 18.88 ?  450  VAL A O    1 
ATOM   2895  C CB   . VAL A 1 450  ? 155.493 121.453 155.812 1.00 19.87 ?  450  VAL A CB   1 
ATOM   2896  C CG1  . VAL A 1 450  ? 155.612 122.305 157.065 1.00 21.28 ?  450  VAL A CG1  1 
ATOM   2897  C CG2  . VAL A 1 450  ? 156.290 120.167 155.962 1.00 18.27 ?  450  VAL A CG2  1 
ATOM   2898  N N    . ILE A 1 451  ? 153.448 119.052 154.354 1.00 11.70 ?  451  ILE A N    1 
ATOM   2899  C CA   . ILE A 1 451  ? 153.360 118.178 153.185 1.00 11.05 ?  451  ILE A CA   1 
ATOM   2900  C C    . ILE A 1 451  ? 152.413 118.755 152.137 1.00 11.77 ?  451  ILE A C    1 
ATOM   2901  O O    . ILE A 1 451  ? 152.721 118.749 150.939 1.00 16.83 ?  451  ILE A O    1 
ATOM   2902  C CB   . ILE A 1 451  ? 152.954 116.750 153.606 1.00 9.16  ?  451  ILE A CB   1 
ATOM   2903  C CG1  . ILE A 1 451  ? 152.797 115.853 152.369 1.00 10.92 ?  451  ILE A CG1  1 
ATOM   2904  C CG2  . ILE A 1 451  ? 151.738 116.754 154.538 1.00 12.75 ?  451  ILE A CG2  1 
ATOM   2905  C CD1  . ILE A 1 451  ? 152.529 114.397 152.672 1.00 14.61 ?  451  ILE A CD1  1 
ATOM   2906  N N    . GLY A 1 452  ? 151.257 119.267 152.565 1.00 10.26 ?  452  GLY A N    1 
ATOM   2907  C CA   . GLY A 1 452  ? 150.326 119.851 151.614 1.00 8.60  ?  452  GLY A CA   1 
ATOM   2908  C C    . GLY A 1 452  ? 150.886 121.088 150.942 1.00 9.26  ?  452  GLY A C    1 
ATOM   2909  O O    . GLY A 1 452  ? 150.682 121.303 149.743 1.00 17.16 ?  452  GLY A O    1 
ATOM   2910  N N    . SER A 1 453  ? 151.613 121.910 151.703 1.00 6.29  ?  453  SER A N    1 
ATOM   2911  C CA   . SER A 1 453  ? 152.240 123.097 151.134 1.00 3.07  ?  453  SER A CA   1 
ATOM   2912  C C    . SER A 1 453  ? 153.292 122.726 150.095 1.00 9.86  ?  453  SER A C    1 
ATOM   2913  O O    . SER A 1 453  ? 153.342 123.328 149.016 1.00 11.99 ?  453  SER A O    1 
ATOM   2914  C CB   . SER A 1 453  ? 152.861 123.943 152.244 1.00 5.59  ?  453  SER A CB   1 
ATOM   2915  O OG   . SER A 1 453  ? 154.200 123.553 152.485 1.00 9.00  ?  453  SER A OG   1 
ATOM   2916  N N    . LYS A 1 454  ? 154.131 121.728 150.396 1.00 13.39 ?  454  LYS A N    1 
ATOM   2917  C CA   . LYS A 1 454  ? 155.134 121.292 149.427 1.00 5.84  ?  454  LYS A CA   1 
ATOM   2918  C C    . LYS A 1 454  ? 154.487 120.700 148.180 1.00 4.28  ?  454  LYS A C    1 
ATOM   2919  O O    . LYS A 1 454  ? 154.917 120.985 147.053 1.00 11.35 ?  454  LYS A O    1 
ATOM   2920  C CB   . LYS A 1 454  ? 156.084 120.280 150.067 1.00 6.97  ?  454  LYS A CB   1 
ATOM   2921  C CG   . LYS A 1 454  ? 156.892 120.833 151.226 1.00 10.73 ?  454  LYS A CG   1 
ATOM   2922  C CD   . LYS A 1 454  ? 157.827 121.938 150.771 1.00 12.32 ?  454  LYS A CD   1 
ATOM   2923  C CE   . LYS A 1 454  ? 157.924 123.034 151.818 1.00 12.08 ?  454  LYS A CE   1 
ATOM   2924  N NZ   . LYS A 1 454  ? 159.002 122.769 152.808 1.00 14.08 ?  454  LYS A NZ   1 
ATOM   2925  N N    . PHE A 1 455  ? 153.444 119.882 148.365 1.00 1.98  ?  455  PHE A N    1 
ATOM   2926  C CA   . PHE A 1 455  ? 152.731 119.292 147.236 1.00 0.00  ?  455  PHE A CA   1 
ATOM   2927  C C    . PHE A 1 455  ? 152.150 120.365 146.328 1.00 0.80  ?  455  PHE A C    1 
ATOM   2928  O O    . PHE A 1 455  ? 152.337 120.329 145.105 1.00 12.01 ?  455  PHE A O    1 
ATOM   2929  C CB   . PHE A 1 455  ? 151.618 118.374 147.742 1.00 3.44  ?  455  PHE A CB   1 
ATOM   2930  C CG   . PHE A 1 455  ? 152.007 116.929 147.836 1.00 7.19  ?  455  PHE A CG   1 
ATOM   2931  C CD1  . PHE A 1 455  ? 153.006 116.516 148.700 1.00 7.10  ?  455  PHE A CD1  1 
ATOM   2932  C CD2  . PHE A 1 455  ? 151.358 115.980 147.068 1.00 1.31  ?  455  PHE A CD2  1 
ATOM   2933  C CE1  . PHE A 1 455  ? 153.355 115.184 148.787 1.00 3.72  ?  455  PHE A CE1  1 
ATOM   2934  C CE2  . PHE A 1 455  ? 151.702 114.650 147.151 1.00 3.42  ?  455  PHE A CE2  1 
ATOM   2935  C CZ   . PHE A 1 455  ? 152.703 114.251 148.010 1.00 5.52  ?  455  PHE A CZ   1 
ATOM   2936  N N    . LEU A 1 456  ? 151.452 121.341 146.914 1.00 2.02  ?  456  LEU A N    1 
ATOM   2937  C CA   . LEU A 1 456  ? 150.816 122.372 146.104 1.00 1.00  ?  456  LEU A CA   1 
ATOM   2938  C C    . LEU A 1 456  ? 151.846 123.270 145.436 1.00 5.13  ?  456  LEU A C    1 
ATOM   2939  O O    . LEU A 1 456  ? 151.679 123.641 144.269 1.00 11.82 ?  456  LEU A O    1 
ATOM   2940  C CB   . LEU A 1 456  ? 149.853 123.198 146.952 1.00 2.31  ?  456  LEU A CB   1 
ATOM   2941  C CG   . LEU A 1 456  ? 148.786 123.969 146.171 1.00 0.00  ?  456  LEU A CG   1 
ATOM   2942  C CD1  . LEU A 1 456  ? 148.362 123.218 144.919 1.00 0.00  ?  456  LEU A CD1  1 
ATOM   2943  C CD2  . LEU A 1 456  ? 147.591 124.234 147.050 1.00 4.05  ?  456  LEU A CD2  1 
ATOM   2944  N N    . PHE A 1 457  ? 152.925 123.614 146.148 1.00 0.95  ?  457  PHE A N    1 
ATOM   2945  C CA   . PHE A 1 457  ? 153.957 124.466 145.568 1.00 0.00  ?  457  PHE A CA   1 
ATOM   2946  C C    . PHE A 1 457  ? 154.607 123.798 144.364 1.00 0.00  ?  457  PHE A C    1 
ATOM   2947  O O    . PHE A 1 457  ? 154.724 124.405 143.293 1.00 5.46  ?  457  PHE A O    1 
ATOM   2948  C CB   . PHE A 1 457  ? 155.008 124.806 146.625 1.00 6.67  ?  457  PHE A CB   1 
ATOM   2949  C CG   . PHE A 1 457  ? 156.268 125.394 146.059 1.00 7.00  ?  457  PHE A CG   1 
ATOM   2950  C CD1  . PHE A 1 457  ? 156.267 126.657 145.492 1.00 10.45 ?  457  PHE A CD1  1 
ATOM   2951  C CD2  . PHE A 1 457  ? 157.454 124.679 146.085 1.00 8.21  ?  457  PHE A CD2  1 
ATOM   2952  C CE1  . PHE A 1 457  ? 157.425 127.199 144.969 1.00 7.42  ?  457  PHE A CE1  1 
ATOM   2953  C CE2  . PHE A 1 457  ? 158.613 125.216 145.561 1.00 12.15 ?  457  PHE A CE2  1 
ATOM   2954  C CZ   . PHE A 1 457  ? 158.599 126.477 145.003 1.00 10.51 ?  457  PHE A CZ   1 
ATOM   2955  N N    . HIS A 1 458  ? 155.002 122.529 144.508 1.00 2.20  ?  458  HIS A N    1 
ATOM   2956  C CA   . HIS A 1 458  ? 155.673 121.852 143.403 1.00 0.00  ?  458  HIS A CA   1 
ATOM   2957  C C    . HIS A 1 458  ? 154.722 121.584 142.243 1.00 0.00  ?  458  HIS A C    1 
ATOM   2958  O O    . HIS A 1 458  ? 155.108 121.740 141.077 1.00 8.76  ?  458  HIS A O    1 
ATOM   2959  C CB   . HIS A 1 458  ? 156.320 120.560 143.895 1.00 1.14  ?  458  HIS A CB   1 
ATOM   2960  C CG   . HIS A 1 458  ? 157.583 120.782 144.666 1.00 6.07  ?  458  HIS A CG   1 
ATOM   2961  N ND1  . HIS A 1 458  ? 157.622 120.807 146.043 1.00 10.30 ?  458  HIS A ND1  1 
ATOM   2962  C CD2  . HIS A 1 458  ? 158.853 121.000 144.251 1.00 9.10  ?  458  HIS A CD2  1 
ATOM   2963  C CE1  . HIS A 1 458  ? 158.861 121.026 146.443 1.00 9.61  ?  458  HIS A CE1  1 
ATOM   2964  N NE2  . HIS A 1 458  ? 159.628 121.146 145.375 1.00 15.39 ?  458  HIS A NE2  1 
ATOM   2965  N N    . THR A 1 459  ? 153.471 121.204 142.532 1.00 1.13  ?  459  THR A N    1 
ATOM   2966  C CA   . THR A 1 459  ? 152.513 120.966 141.456 1.00 1.60  ?  459  THR A CA   1 
ATOM   2967  C C    . THR A 1 459  ? 152.206 122.245 140.685 1.00 8.28  ?  459  THR A C    1 
ATOM   2968  O O    . THR A 1 459  ? 152.194 122.239 139.447 1.00 18.17 ?  459  THR A O    1 
ATOM   2969  C CB   . THR A 1 459  ? 151.228 120.362 142.021 1.00 0.33  ?  459  THR A CB   1 
ATOM   2970  O OG1  . THR A 1 459  ? 151.553 119.266 142.884 1.00 4.63  ?  459  THR A OG1  1 
ATOM   2971  C CG2  . THR A 1 459  ? 150.336 119.864 140.896 1.00 0.00  ?  459  THR A CG2  1 
ATOM   2972  N N    . ALA A 1 460  ? 151.977 123.355 141.395 1.00 7.40  ?  460  ALA A N    1 
ATOM   2973  C CA   . ALA A 1 460  ? 151.694 124.619 140.725 1.00 1.39  ?  460  ALA A CA   1 
ATOM   2974  C C    . ALA A 1 460  ? 152.900 125.110 139.936 1.00 2.15  ?  460  ALA A C    1 
ATOM   2975  O O    . ALA A 1 460  ? 152.745 125.629 138.824 1.00 7.03  ?  460  ALA A O    1 
ATOM   2976  C CB   . ALA A 1 460  ? 151.254 125.666 141.745 1.00 0.00  ?  460  ALA A CB   1 
ATOM   2977  N N    . GLY A 1 461  ? 154.107 124.950 140.487 1.00 0.00  ?  461  GLY A N    1 
ATOM   2978  C CA   . GLY A 1 461  ? 155.299 125.345 139.756 1.00 0.00  ?  461  GLY A CA   1 
ATOM   2979  C C    . GLY A 1 461  ? 155.501 124.543 138.485 1.00 0.00  ?  461  GLY A C    1 
ATOM   2980  O O    . GLY A 1 461  ? 155.852 125.099 137.441 1.00 9.56  ?  461  GLY A O    1 
ATOM   2981  N N    . ILE A 1 462  ? 155.269 123.229 138.550 1.00 0.00  ?  462  ILE A N    1 
ATOM   2982  C CA   . ILE A 1 462  ? 155.418 122.387 137.367 1.00 0.00  ?  462  ILE A CA   1 
ATOM   2983  C C    . ILE A 1 462  ? 154.373 122.748 136.318 1.00 0.00  ?  462  ILE A C    1 
ATOM   2984  O O    . ILE A 1 462  ? 154.673 122.814 135.118 1.00 9.11  ?  462  ILE A O    1 
ATOM   2985  C CB   . ILE A 1 462  ? 155.345 120.900 137.764 1.00 1.58  ?  462  ILE A CB   1 
ATOM   2986  C CG1  . ILE A 1 462  ? 156.640 120.482 138.456 1.00 2.93  ?  462  ILE A CG1  1 
ATOM   2987  C CG2  . ILE A 1 462  ? 155.094 120.016 136.553 1.00 3.88  ?  462  ILE A CG2  1 
ATOM   2988  C CD1  . ILE A 1 462  ? 157.860 120.603 137.585 1.00 5.77  ?  462  ILE A CD1  1 
ATOM   2989  N N    . VAL A 1 463  ? 153.136 123.010 136.755 1.00 1.91  ?  463  VAL A N    1 
ATOM   2990  C CA   . VAL A 1 463  ? 152.081 123.396 135.818 1.00 0.00  ?  463  VAL A CA   1 
ATOM   2991  C C    . VAL A 1 463  ? 152.421 124.720 135.142 1.00 1.56  ?  463  VAL A C    1 
ATOM   2992  O O    . VAL A 1 463  ? 152.263 124.868 133.923 1.00 4.37  ?  463  VAL A O    1 
ATOM   2993  C CB   . VAL A 1 463  ? 150.722 123.453 136.540 1.00 3.79  ?  463  VAL A CB   1 
ATOM   2994  C CG1  . VAL A 1 463  ? 149.688 124.170 135.691 1.00 5.08  ?  463  VAL A CG1  1 
ATOM   2995  C CG2  . VAL A 1 463  ? 150.242 122.052 136.865 1.00 5.87  ?  463  VAL A CG2  1 
ATOM   2996  N N    . VAL A 1 464  ? 152.916 125.691 135.917 1.00 1.01  ?  464  VAL A N    1 
ATOM   2997  C CA   . VAL A 1 464  ? 153.290 126.993 135.362 1.00 0.00  ?  464  VAL A CA   1 
ATOM   2998  C C    . VAL A 1 464  ? 154.422 126.841 134.353 1.00 2.15  ?  464  VAL A C    1 
ATOM   2999  O O    . VAL A 1 464  ? 154.373 127.396 133.245 1.00 6.40  ?  464  VAL A O    1 
ATOM   3000  C CB   . VAL A 1 464  ? 153.677 127.959 136.498 1.00 2.69  ?  464  VAL A CB   1 
ATOM   3001  C CG1  . VAL A 1 464  ? 154.554 129.090 135.982 1.00 5.51  ?  464  VAL A CG1  1 
ATOM   3002  C CG2  . VAL A 1 464  ? 152.442 128.511 137.172 1.00 1.90  ?  464  VAL A CG2  1 
ATOM   3003  N N    . LEU A 1 465  ? 155.456 126.075 134.720 1.00 4.13  ?  465  LEU A N    1 
ATOM   3004  C CA   . LEU A 1 465  ? 156.611 125.907 133.844 1.00 0.00  ?  465  LEU A CA   1 
ATOM   3005  C C    . LEU A 1 465  ? 156.225 125.217 132.543 1.00 0.09  ?  465  LEU A C    1 
ATOM   3006  O O    . LEU A 1 465  ? 156.666 125.629 131.464 1.00 12.62 ?  465  LEU A O    1 
ATOM   3007  C CB   . LEU A 1 465  ? 157.704 125.120 134.564 1.00 0.00  ?  465  LEU A CB   1 
ATOM   3008  C CG   . LEU A 1 465  ? 158.516 125.882 135.612 1.00 0.00  ?  465  LEU A CG   1 
ATOM   3009  C CD1  . LEU A 1 465  ? 159.635 125.011 136.157 1.00 2.80  ?  465  LEU A CD1  1 
ATOM   3010  C CD2  . LEU A 1 465  ? 159.067 127.176 135.040 1.00 5.98  ?  465  LEU A CD2  1 
ATOM   3011  N N    . THR A 1 466  ? 155.395 124.173 132.620 1.00 0.38  ?  466  THR A N    1 
ATOM   3012  C CA   . THR A 1 466  ? 154.934 123.513 131.403 1.00 2.27  ?  466  THR A CA   1 
ATOM   3013  C C    . THR A 1 466  ? 154.117 124.467 130.544 1.00 2.59  ?  466  THR A C    1 
ATOM   3014  O O    . THR A 1 466  ? 154.440 124.685 129.370 1.00 7.76  ?  466  THR A O    1 
ATOM   3015  C CB   . THR A 1 466  ? 154.116 122.269 131.749 1.00 3.08  ?  466  THR A CB   1 
ATOM   3016  O OG1  . THR A 1 466  ? 153.140 122.598 132.744 1.00 2.92  ?  466  THR A OG1  1 
ATOM   3017  C CG2  . THR A 1 466  ? 155.020 121.167 132.273 1.00 5.47  ?  466  THR A CG2  1 
ATOM   3018  N N    . LEU A 1 467  ? 153.102 125.105 131.143 1.00 8.29  ?  467  LEU A N    1 
ATOM   3019  C CA   . LEU A 1 467  ? 152.184 125.971 130.412 1.00 8.83  ?  467  LEU A CA   1 
ATOM   3020  C C    . LEU A 1 467  ? 152.877 127.169 129.784 1.00 6.10  ?  467  LEU A C    1 
ATOM   3021  O O    . LEU A 1 467  ? 152.357 127.732 128.816 1.00 7.87  ?  467  LEU A O    1 
ATOM   3022  C CB   . LEU A 1 467  ? 151.075 126.459 131.344 1.00 5.50  ?  467  LEU A CB   1 
ATOM   3023  C CG   . LEU A 1 467  ? 149.798 125.626 131.451 1.00 4.64  ?  467  LEU A CG   1 
ATOM   3024  C CD1  . LEU A 1 467  ? 148.699 126.451 132.088 1.00 5.25  ?  467  LEU A CD1  1 
ATOM   3025  C CD2  . LEU A 1 467  ? 149.362 125.112 130.091 1.00 4.07  ?  467  LEU A CD2  1 
ATOM   3026  N N    . VAL A 1 468  ? 154.025 127.586 130.311 1.00 8.13  ?  468  VAL A N    1 
ATOM   3027  C CA   . VAL A 1 468  ? 154.769 128.646 129.643 1.00 9.37  ?  468  VAL A CA   1 
ATOM   3028  C C    . VAL A 1 468  ? 155.672 128.030 128.580 1.00 11.46 ?  468  VAL A C    1 
ATOM   3029  O O    . VAL A 1 468  ? 155.446 128.218 127.376 1.00 17.26 ?  468  VAL A O    1 
ATOM   3030  C CB   . VAL A 1 468  ? 155.584 129.483 130.645 1.00 4.30  ?  468  VAL A CB   1 
ATOM   3031  C CG1  . VAL A 1 468  ? 156.505 130.440 129.909 1.00 10.13 ?  468  VAL A CG1  1 
ATOM   3032  C CG2  . VAL A 1 468  ? 154.657 130.243 131.574 1.00 3.61  ?  468  VAL A CG2  1 
ATOM   3033  N N    . ILE A 1 469  ? 156.653 127.234 129.018 1.00 7.32  ?  469  ILE A N    1 
ATOM   3034  C CA   . ILE A 1 469  ? 157.755 126.841 128.143 1.00 6.04  ?  469  ILE A CA   1 
ATOM   3035  C C    . ILE A 1 469  ? 157.267 125.927 127.026 1.00 6.89  ?  469  ILE A C    1 
ATOM   3036  O O    . ILE A 1 469  ? 157.480 126.210 125.840 1.00 14.42 ?  469  ILE A O    1 
ATOM   3037  C CB   . ILE A 1 469  ? 158.879 126.175 128.956 1.00 5.50  ?  469  ILE A CB   1 
ATOM   3038  C CG1  . ILE A 1 469  ? 159.271 127.047 130.151 1.00 6.47  ?  469  ILE A CG1  1 
ATOM   3039  C CG2  . ILE A 1 469  ? 160.080 125.894 128.071 1.00 6.94  ?  469  ILE A CG2  1 
ATOM   3040  C CD1  . ILE A 1 469  ? 159.764 128.420 129.769 1.00 11.58 ?  469  ILE A CD1  1 
ATOM   3041  N N    . ASN A 1 470  ? 156.621 124.811 127.383 1.00 2.08  ?  470  ASN A N    1 
ATOM   3042  C CA   . ASN A 1 470  ? 156.254 123.834 126.365 1.00 2.79  ?  470  ASN A CA   1 
ATOM   3043  C C    . ASN A 1 470  ? 155.182 124.385 125.437 1.00 11.73 ?  470  ASN A C    1 
ATOM   3044  O O    . ASN A 1 470  ? 155.277 124.241 124.211 1.00 19.27 ?  470  ASN A O    1 
ATOM   3045  C CB   . ASN A 1 470  ? 155.781 122.542 127.028 1.00 4.99  ?  470  ASN A CB   1 
ATOM   3046  C CG   . ASN A 1 470  ? 156.806 121.969 127.981 1.00 7.92  ?  470  ASN A CG   1 
ATOM   3047  O OD1  . ASN A 1 470  ? 157.644 122.692 128.518 1.00 9.55  ?  470  ASN A OD1  1 
ATOM   3048  N ND2  . ASN A 1 470  ? 156.741 120.664 128.203 1.00 4.50  ?  470  ASN A ND2  1 
ATOM   3049  N N    . ALA A 1 471  ? 154.176 125.054 126.003 1.00 11.21 ?  471  ALA A N    1 
ATOM   3050  C CA   . ALA A 1 471  ? 153.074 125.572 125.206 1.00 12.24 ?  471  ALA A CA   1 
ATOM   3051  C C    . ALA A 1 471  ? 153.487 126.737 124.317 1.00 13.69 ?  471  ALA A C    1 
ATOM   3052  O O    . ALA A 1 471  ? 152.801 127.009 123.327 1.00 17.65 ?  471  ALA A O    1 
ATOM   3053  C CB   . ALA A 1 471  ? 151.919 125.993 126.112 1.00 12.45 ?  471  ALA A CB   1 
ATOM   3054  N N    . THR A 1 472  ? 154.584 127.433 124.633 1.00 12.41 ?  472  THR A N    1 
ATOM   3055  C CA   . THR A 1 472  ? 155.062 128.469 123.730 1.00 14.68 ?  472  THR A CA   1 
ATOM   3056  C C    . THR A 1 472  ? 156.138 127.992 122.763 1.00 15.24 ?  472  THR A C    1 
ATOM   3057  O O    . THR A 1 472  ? 156.309 128.611 121.708 1.00 17.48 ?  472  THR A O    1 
ATOM   3058  C CB   . THR A 1 472  ? 155.600 129.666 124.524 1.00 9.92  ?  472  THR A CB   1 
ATOM   3059  O OG1  . THR A 1 472  ? 156.459 129.202 125.573 1.00 11.36 ?  472  THR A OG1  1 
ATOM   3060  C CG2  . THR A 1 472  ? 154.454 130.469 125.120 1.00 7.09  ?  472  THR A CG2  1 
ATOM   3061  N N    . THR A 1 473  ? 156.859 126.916 123.077 1.00 12.10 ?  473  THR A N    1 
ATOM   3062  C CA   . THR A 1 473  ? 157.985 126.494 122.256 1.00 11.60 ?  473  THR A CA   1 
ATOM   3063  C C    . THR A 1 473  ? 157.706 125.218 121.464 1.00 14.46 ?  473  THR A C    1 
ATOM   3064  O O    . THR A 1 473  ? 158.591 124.748 120.738 1.00 16.35 ?  473  THR A O    1 
ATOM   3065  C CB   . THR A 1 473  ? 159.223 126.316 123.148 1.00 12.14 ?  473  THR A CB   1 
ATOM   3066  O OG1  . THR A 1 473  ? 159.190 127.300 124.187 1.00 13.93 ?  473  THR A OG1  1 
ATOM   3067  C CG2  . THR A 1 473  ? 160.509 126.547 122.359 1.00 12.70 ?  473  THR A CG2  1 
ATOM   3068  N N    . ILE A 1 474  ? 156.500 124.648 121.566 1.00 16.19 ?  474  ILE A N    1 
ATOM   3069  C CA   . ILE A 1 474  ? 156.176 123.463 120.772 1.00 17.83 ?  474  ILE A CA   1 
ATOM   3070  C C    . ILE A 1 474  ? 156.207 123.775 119.276 1.00 19.55 ?  474  ILE A C    1 
ATOM   3071  O O    . ILE A 1 474  ? 156.717 122.980 118.474 1.00 17.10 ?  474  ILE A O    1 
ATOM   3072  C CB   . ILE A 1 474  ? 154.821 122.877 121.220 1.00 15.09 ?  474  ILE A CB   1 
ATOM   3073  C CG1  . ILE A 1 474  ? 154.432 121.676 120.353 1.00 13.95 ?  474  ILE A CG1  1 
ATOM   3074  C CG2  . ILE A 1 474  ? 153.732 123.950 121.273 1.00 17.09 ?  474  ILE A CG2  1 
ATOM   3075  C CD1  . ILE A 1 474  ? 153.683 120.599 121.100 1.00 15.93 ?  474  ILE A CD1  1 
ATOM   3076  N N    . GLN A 1 475  ? 155.683 124.939 118.878 1.00 21.14 ?  475  GLN A N    1 
ATOM   3077  C CA   . GLN A 1 475  ? 155.708 125.322 117.468 1.00 23.50 ?  475  GLN A CA   1 
ATOM   3078  C C    . GLN A 1 475  ? 157.134 125.529 116.971 1.00 19.78 ?  475  GLN A C    1 
ATOM   3079  O O    . GLN A 1 475  ? 157.474 125.126 115.853 1.00 13.56 ?  475  GLN A O    1 
ATOM   3080  C CB   . GLN A 1 475  ? 154.878 126.588 117.254 1.00 22.48 ?  475  GLN A CB   1 
ATOM   3081  C CG   . GLN A 1 475  ? 153.381 126.349 117.225 1.00 17.25 ?  475  GLN A CG   1 
ATOM   3082  C CD   . GLN A 1 475  ? 152.599 127.459 117.896 1.00 22.30 ?  475  GLN A CD   1 
ATOM   3083  O OE1  . GLN A 1 475  ? 153.003 127.977 118.937 1.00 22.17 ?  475  GLN A OE1  1 
ATOM   3084  N NE2  . GLN A 1 475  ? 151.469 127.830 117.303 1.00 20.25 ?  475  GLN A NE2  1 
ATOM   3085  N N    . THR A 1 476  ? 157.980 126.158 117.791 1.00 19.88 ?  476  THR A N    1 
ATOM   3086  C CA   . THR A 1 476  ? 159.372 126.371 117.406 1.00 17.34 ?  476  THR A CA   1 
ATOM   3087  C C    . THR A 1 476  ? 160.119 125.047 117.285 1.00 19.75 ?  476  THR A C    1 
ATOM   3088  O O    . THR A 1 476  ? 160.924 124.859 116.365 1.00 16.43 ?  476  THR A O    1 
ATOM   3089  C CB   . THR A 1 476  ? 160.053 127.294 118.418 1.00 13.76 ?  476  THR A CB   1 
ATOM   3090  O OG1  . THR A 1 476  ? 159.403 128.571 118.408 1.00 16.29 ?  476  THR A OG1  1 
ATOM   3091  C CG2  . THR A 1 476  ? 161.520 127.492 118.073 1.00 14.36 ?  476  THR A CG2  1 
ATOM   3092  N N    . LEU A 1 477  ? 159.852 124.107 118.197 1.00 21.90 ?  477  LEU A N    1 
ATOM   3093  C CA   . LEU A 1 477  ? 160.478 122.791 118.108 1.00 21.86 ?  477  LEU A CA   1 
ATOM   3094  C C    . LEU A 1 477  ? 160.022 122.042 116.860 1.00 24.34 ?  477  LEU A C    1 
ATOM   3095  O O    . LEU A 1 477  ? 160.829 121.374 116.201 1.00 23.25 ?  477  LEU A O    1 
ATOM   3096  C CB   . LEU A 1 477  ? 160.172 121.978 119.365 1.00 18.26 ?  477  LEU A CB   1 
ATOM   3097  C CG   . LEU A 1 477  ? 161.223 120.942 119.763 1.00 20.87 ?  477  LEU A CG   1 
ATOM   3098  C CD1  . LEU A 1 477  ? 162.430 121.619 120.393 1.00 17.73 ?  477  LEU A CD1  1 
ATOM   3099  C CD2  . LEU A 1 477  ? 160.625 119.917 120.708 1.00 20.52 ?  477  LEU A CD2  1 
ATOM   3100  N N    . LEU A 1 478  ? 158.733 122.140 116.520 1.00 23.85 ?  478  LEU A N    1 
ATOM   3101  C CA   . LEU A 1 478  ? 158.241 121.507 115.300 1.00 23.12 ?  478  LEU A CA   1 
ATOM   3102  C C    . LEU A 1 478  ? 158.867 122.138 114.059 1.00 26.00 ?  478  LEU A C    1 
ATOM   3103  O O    . LEU A 1 478  ? 159.190 121.438 113.093 1.00 25.85 ?  478  LEU A O    1 
ATOM   3104  C CB   . LEU A 1 478  ? 156.714 121.588 115.248 1.00 20.46 ?  478  LEU A CB   1 
ATOM   3105  C CG   . LEU A 1 478  ? 156.009 121.498 113.892 1.00 24.29 ?  478  LEU A CG   1 
ATOM   3106  C CD1  . LEU A 1 478  ? 156.163 120.120 113.257 1.00 21.11 ?  478  LEU A CD1  1 
ATOM   3107  C CD2  . LEU A 1 478  ? 154.538 121.863 114.032 1.00 25.89 ?  478  LEU A CD2  1 
ATOM   3108  N N    . ARG A 1 479  ? 159.046 123.463 114.067 1.00 27.06 ?  479  ARG A N    1 
ATOM   3109  C CA   . ARG A 1 479  ? 159.690 124.131 112.940 1.00 27.21 ?  479  ARG A CA   1 
ATOM   3110  C C    . ARG A 1 479  ? 161.174 123.790 112.855 1.00 27.91 ?  479  ARG A C    1 
ATOM   3111  O O    . ARG A 1 479  ? 161.764 123.849 111.771 1.00 27.38 ?  479  ARG A O    1 
ATOM   3112  C CB   . ARG A 1 479  ? 159.498 125.644 113.048 1.00 25.87 ?  479  ARG A CB   1 
ATOM   3113  C CG   . ARG A 1 479  ? 159.730 126.399 111.750 1.00 24.58 ?  479  ARG A CG   1 
ATOM   3114  C CD   . ARG A 1 479  ? 159.937 127.880 112.009 1.00 27.48 ?  479  ARG A CD   1 
ATOM   3115  N NE   . ARG A 1 479  ? 160.991 128.111 112.989 1.00 28.11 ?  479  ARG A NE   1 
ATOM   3116  C CZ   . ARG A 1 479  ? 161.450 129.307 113.330 1.00 28.02 ?  479  ARG A CZ   1 
ATOM   3117  N NH1  . ARG A 1 479  ? 160.968 130.413 112.786 1.00 28.05 ?  479  ARG A NH1  1 
ATOM   3118  N NH2  . ARG A 1 479  ? 162.416 129.397 114.239 1.00 25.51 ?  479  ARG A NH2  1 
ATOM   3119  N N    . ILE A 1 480  ? 161.802 123.466 113.984 1.00 24.69 ?  480  ILE A N    1 
ATOM   3120  C CA   . ILE A 1 480  ? 163.175 122.975 113.943 1.00 23.45 ?  480  ILE A CA   1 
ATOM   3121  C C    . ILE A 1 480  ? 163.218 121.568 113.355 1.00 21.76 ?  480  ILE A C    1 
ATOM   3122  O O    . ILE A 1 480  ? 164.081 121.250 112.526 1.00 24.72 ?  480  ILE A O    1 
ATOM   3123  C CB   . ILE A 1 480  ? 163.803 123.034 115.348 1.00 25.17 ?  480  ILE A CB   1 
ATOM   3124  C CG1  . ILE A 1 480  ? 164.189 124.475 115.695 1.00 24.65 ?  480  ILE A CG1  1 
ATOM   3125  C CG2  . ILE A 1 480  ? 165.010 122.108 115.457 1.00 23.83 ?  480  ILE A CG2  1 
ATOM   3126  C CD1  . ILE A 1 480  ? 165.419 124.975 114.965 1.00 22.83 ?  480  ILE A CD1  1 
ATOM   3127  N N    . LEU A 1 481  ? 162.272 120.715 113.752 1.00 19.39 ?  481  LEU A N    1 
ATOM   3128  C CA   . LEU A 1 481  ? 162.300 119.316 113.331 1.00 24.87 ?  481  LEU A CA   1 
ATOM   3129  C C    . LEU A 1 481  ? 161.920 119.165 111.861 1.00 26.06 ?  481  LEU A C    1 
ATOM   3130  O O    . LEU A 1 481  ? 162.728 118.717 111.040 1.00 25.45 ?  481  LEU A O    1 
ATOM   3131  C CB   . LEU A 1 481  ? 161.364 118.490 114.214 1.00 23.73 ?  481  LEU A CB   1 
ATOM   3132  C CG   . LEU A 1 481  ? 161.807 118.258 115.657 1.00 27.04 ?  481  LEU A CG   1 
ATOM   3133  C CD1  . LEU A 1 481  ? 160.661 117.674 116.458 1.00 25.92 ?  481  LEU A CD1  1 
ATOM   3134  C CD2  . LEU A 1 481  ? 163.020 117.343 115.707 1.00 26.04 ?  481  LEU A CD2  1 
ATOM   3135  N N    . GLY A 1 482  ? 160.691 119.536 111.509 1.00 27.88 ?  482  GLY A N    1 
ATOM   3136  C CA   . GLY A 1 482  ? 160.206 119.332 110.158 1.00 25.06 ?  482  GLY A CA   1 
ATOM   3137  C C    . GLY A 1 482  ? 159.681 120.587 109.493 1.00 26.47 ?  482  GLY A C    1 
ATOM   3138  O O    . GLY A 1 482  ? 158.766 120.519 108.666 1.00 25.92 ?  482  GLY A O    1 
ATOM   3139  N N    . MET A 1 483  ? 160.231 121.741 109.887 1.00 26.43 ?  483  MET A N    1 
ATOM   3140  C CA   . MET A 1 483  ? 159.957 123.055 109.303 1.00 28.83 ?  483  MET A CA   1 
ATOM   3141  C C    . MET A 1 483  ? 158.516 123.524 109.490 1.00 30.01 ?  483  MET A C    1 
ATOM   3142  O O    . MET A 1 483  ? 158.152 124.595 108.992 1.00 34.55 ?  483  MET A O    1 
ATOM   3143  C CB   . MET A 1 483  ? 160.322 123.073 107.814 1.00 27.69 ?  483  MET A CB   1 
ATOM   3144  C CG   . MET A 1 483  ? 161.682 123.683 107.519 1.00 30.39 ?  483  MET A CG   1 
ATOM   3145  S SD   . MET A 1 483  ? 161.800 124.341 105.845 1.00 43.58 ?  483  MET A SD   1 
ATOM   3146  C CE   . MET A 1 483  ? 160.333 125.367 105.783 1.00 31.01 ?  483  MET A CE   1 
ATOM   3147  N N    . SER A 1 484  ? 157.710 122.733 110.192 1.00 23.64 ?  484  SER A N    1 
ATOM   3148  C CA   . SER A 1 484  ? 156.310 123.086 110.405 1.00 26.27 ?  484  SER A CA   1 
ATOM   3149  C C    . SER A 1 484  ? 155.667 123.534 109.102 1.00 26.24 ?  484  SER A C    1 
ATOM   3150  O O    . SER A 1 484  ? 154.676 124.263 109.111 1.00 26.66 ?  484  SER A O    1 
ATOM   3151  C CB   . SER A 1 484  ? 156.188 124.182 111.465 1.00 26.28 ?  484  SER A CB   1 
ATOM   3152  O OG   . SER A 1 484  ? 154.830 124.455 111.762 1.00 25.26 ?  484  SER A OG   1 
ATOM   3153  N N    . ASP A 1 485  ? 156.228 123.100 107.979 1.00 25.95 ?  485  ASP A N    1 
ATOM   3154  C CA   . ASP A 1 485  ? 155.700 123.500 106.677 1.00 27.79 ?  485  ASP A CA   1 
ATOM   3155  C C    . ASP A 1 485  ? 154.329 122.896 106.397 1.00 30.13 ?  485  ASP A C    1 
ATOM   3156  O O    . ASP A 1 485  ? 154.091 121.723 106.684 1.00 28.11 ?  485  ASP A O    1 
ATOM   3157  C CB   . ASP A 1 485  ? 156.681 123.123 105.562 1.00 27.64 ?  485  ASP A CB   1 
ATOM   3158  C CG   . ASP A 1 485  ? 157.125 121.673 105.634 1.00 31.38 ?  485  ASP A CG   1 
ATOM   3159  O OD1  . ASP A 1 485  ? 156.777 120.981 106.614 1.00 30.52 ?  485  ASP A OD1  1 
ATOM   3160  O OD2  . ASP A 1 485  ? 157.828 121.223 104.706 1.00 28.86 ?  485  ASP A OD2  1 
ATOM   3161  N N    . ILE A 1 486  ? 153.440 123.633 105.774 1.00 27.20 ?  486  ILE A N    1 
ATOM   3162  C CA   . ILE A 1 486  ? 152.090 123.125 105.570 1.00 25.32 ?  486  ILE A CA   1 
ATOM   3163  C C    . ILE A 1 486  ? 151.995 122.065 104.477 1.00 26.90 ?  486  ILE A C    1 
ATOM   3164  O O    . ILE A 1 486  ? 150.931 121.485 104.292 1.00 23.37 ?  486  ILE A O    1 
ATOM   3165  C CB   . ILE A 1 486  ? 151.176 124.310 105.245 1.00 22.67 ?  486  ILE A CB   1 
ATOM   3166  C CG1  . ILE A 1 486  ? 151.656 124.994 103.960 1.00 23.96 ?  486  ILE A CG1  1 
ATOM   3167  C CG2  . ILE A 1 486  ? 151.065 125.234 106.455 1.00 23.04 ?  486  ILE A CG2  1 
ATOM   3168  C CD1  . ILE A 1 486  ? 150.704 126.042 103.429 1.00 23.91 ?  486  ILE A CD1  1 
ATOM   3169  N N    . SER A 1 487  ? 153.091 121.820 103.759 1.00 25.65 ?  487  SER A N    1 
ATOM   3170  C CA   . SER A 1 487  ? 153.130 120.820 102.682 1.00 24.73 ?  487  SER A CA   1 
ATOM   3171  C C    . SER A 1 487  ? 152.270 121.183 101.499 1.00 22.61 ?  487  SER A C    1 
ATOM   3172  O O    . SER A 1 487  ? 151.960 122.346 101.295 1.00 20.36 ?  487  SER A O    1 
ATOM   3173  C CB   . SER A 1 487  ? 152.737 119.434 103.194 1.00 22.84 ?  487  SER A CB   1 
ATOM   3174  O OG   . SER A 1 487  ? 151.373 119.358 103.559 1.00 25.56 ?  487  SER A OG   1 
ATOM   3175  N N    . ILE A 1 488  ? 151.914 120.200 100.680 1.00 22.10 ?  488  ILE A N    1 
ATOM   3176  C CA   . ILE A 1 488  ? 151.159 120.486 99.454  1.00 27.49 ?  488  ILE A CA   1 
ATOM   3177  C C    . ILE A 1 488  ? 149.656 120.706 99.651  1.00 27.21 ?  488  ILE A C    1 
ATOM   3178  O O    . ILE A 1 488  ? 149.080 121.606 99.038  1.00 25.60 ?  488  ILE A O    1 
ATOM   3179  C CB   . ILE A 1 488  ? 151.360 119.369 98.410  1.00 26.80 ?  488  ILE A CB   1 
ATOM   3180  C CG1  . ILE A 1 488  ? 152.842 119.232 98.068  1.00 25.06 ?  488  ILE A CG1  1 
ATOM   3181  C CG2  . ILE A 1 488  ? 150.546 119.654 97.158  1.00 25.70 ?  488  ILE A CG2  1 
ATOM   3182  C CD1  . ILE A 1 488  ? 153.468 120.515 97.568  1.00 22.23 ?  488  ILE A CD1  1 
ATOM   3183  N N    . PRO A 1 489  ? 149.013 119.891 100.504 1.00 26.09 ?  489  PRO A N    1 
ATOM   3184  C CA   . PRO A 1 489  ? 147.563 120.028 100.651 1.00 27.13 ?  489  PRO A CA   1 
ATOM   3185  C C    . PRO A 1 489  ? 147.146 121.483 100.795 1.00 25.20 ?  489  PRO A C    1 
ATOM   3186  O O    . PRO A 1 489  ? 146.053 121.848 100.372 1.00 28.48 ?  489  PRO A O    1 
ATOM   3187  C CB   . PRO A 1 489  ? 147.284 119.283 101.953 1.00 26.01 ?  489  PRO A CB   1 
ATOM   3188  C CG   . PRO A 1 489  ? 148.332 118.224 102.004 1.00 28.01 ?  489  PRO A CG   1 
ATOM   3189  C CD   . PRO A 1 489  ? 149.526 118.714 101.228 1.00 24.24 ?  489  PRO A CD   1 
ATOM   3190  N N    . LYS A 1 490  ? 148.002 122.303 101.390 1.00 20.14 ?  490  LYS A N    1 
ATOM   3191  C CA   . LYS A 1 490  ? 147.685 123.711 101.562 1.00 24.01 ?  490  LYS A CA   1 
ATOM   3192  C C    . LYS A 1 490  ? 148.337 124.553 100.472 1.00 27.43 ?  490  LYS A C    1 
ATOM   3193  O O    . LYS A 1 490  ? 147.750 125.530 100.007 1.00 27.20 ?  490  LYS A O    1 
ATOM   3194  C CB   . LYS A 1 490  ? 148.139 124.182 102.940 1.00 25.17 ?  490  LYS A CB   1 
ATOM   3195  C CG   . LYS A 1 490  ? 147.891 123.175 104.051 1.00 26.42 ?  490  LYS A CG   1 
ATOM   3196  C CD   . LYS A 1 490  ? 146.433 122.751 104.105 1.00 24.74 ?  490  LYS A CD   1 
ATOM   3197  C CE   . LYS A 1 490  ? 146.186 121.790 105.256 1.00 29.45 ?  490  LYS A CE   1 
ATOM   3198  N NZ   . LYS A 1 490  ? 146.562 122.393 106.564 1.00 29.83 ?  490  LYS A NZ   1 
ATOM   3199  N N    . ARG A 1 491  ? 149.543 124.177 100.058 1.00 27.20 ?  491  ARG A N    1 
ATOM   3200  C CA   . ARG A 1 491  ? 150.254 124.929 99.032  1.00 26.06 ?  491  ARG A CA   1 
ATOM   3201  C C    . ARG A 1 491  ? 149.414 125.144 97.782  1.00 22.46 ?  491  ARG A C    1 
ATOM   3202  O O    . ARG A 1 491  ? 149.414 126.236 97.216  1.00 24.30 ?  491  ARG A O    1 
ATOM   3203  C CB   . ARG A 1 491  ? 151.546 124.204 98.656  1.00 27.09 ?  491  ARG A CB   1 
ATOM   3204  C CG   . ARG A 1 491  ? 152.690 125.133 98.297  1.00 25.90 ?  491  ARG A CG   1 
ATOM   3205  C CD   . ARG A 1 491  ? 153.069 125.994 99.490  1.00 26.57 ?  491  ARG A CD   1 
ATOM   3206  N NE   . ARG A 1 491  ? 154.168 126.904 99.184  1.00 28.36 ?  491  ARG A NE   1 
ATOM   3207  C CZ   . ARG A 1 491  ? 154.694 127.757 100.055 1.00 28.81 ?  491  ARG A CZ   1 
ATOM   3208  N NH1  . ARG A 1 491  ? 154.222 127.820 101.293 1.00 23.88 ?  491  ARG A NH1  1 
ATOM   3209  N NH2  . ARG A 1 491  ? 155.693 128.549 99.690  1.00 28.66 ?  491  ARG A NH2  1 
ATOM   3210  N N    . LEU A 1 492  ? 148.698 124.114 97.346  1.00 21.71 ?  492  LEU A N    1 
ATOM   3211  C CA   . LEU A 1 492  ? 147.931 124.225 96.106  1.00 24.99 ?  492  LEU A CA   1 
ATOM   3212  C C    . LEU A 1 492  ? 146.430 124.313 96.338  1.00 26.30 ?  492  LEU A C    1 
ATOM   3213  O O    . LEU A 1 492  ? 145.787 125.260 95.890  1.00 27.95 ?  492  LEU A O    1 
ATOM   3214  C CB   . LEU A 1 492  ? 148.248 123.035 95.192  1.00 25.37 ?  492  LEU A CB   1 
ATOM   3215  C CG   . LEU A 1 492  ? 149.669 122.891 94.637  1.00 25.78 ?  492  LEU A CG   1 
ATOM   3216  C CD1  . LEU A 1 492  ? 149.814 121.579 93.882  1.00 23.90 ?  492  LEU A CD1  1 
ATOM   3217  C CD2  . LEU A 1 492  ? 150.071 124.067 93.758  1.00 24.32 ?  492  LEU A CD2  1 
ATOM   3218  N N    . ALA A 1 493  ? 145.866 123.327 97.026  1.00 19.07 ?  493  ALA A N    1 
ATOM   3219  C CA   . ALA A 1 493  ? 144.421 123.305 97.239  1.00 17.81 ?  493  ALA A CA   1 
ATOM   3220  C C    . ALA A 1 493  ? 143.906 124.645 97.733  1.00 20.67 ?  493  ALA A C    1 
ATOM   3221  O O    . ALA A 1 493  ? 143.100 125.290 97.061  1.00 21.16 ?  493  ALA A O    1 
ATOM   3222  C CB   . ALA A 1 493  ? 144.049 122.202 98.219  1.00 18.94 ?  493  ALA A CB   1 
ATOM   3223  N N    . MET A 1 494  ? 144.365 125.070 98.903  1.00 20.89 ?  494  MET A N    1 
ATOM   3224  C CA   . MET A 1 494  ? 143.898 126.307 99.462  1.00 19.20 ?  494  MET A CA   1 
ATOM   3225  C C    . MET A 1 494  ? 144.188 127.461 98.529  1.00 20.18 ?  494  MET A C    1 
ATOM   3226  O O    . MET A 1 494  ? 143.649 128.532 98.719  1.00 21.87 ?  494  MET A O    1 
ATOM   3227  C CB   . MET A 1 494  ? 144.548 126.562 100.795 1.00 19.04 ?  494  MET A CB   1 
ATOM   3228  C CG   . MET A 1 494  ? 143.689 127.356 101.758 1.00 20.98 ?  494  MET A CG   1 
ATOM   3229  S SD   . MET A 1 494  ? 142.151 126.500 102.131 1.00 29.48 ?  494  MET A SD   1 
ATOM   3230  C CE   . MET A 1 494  ? 141.737 127.231 103.710 1.00 23.73 ?  494  MET A CE   1 
ATOM   3231  N N    . ALA A 1 495  ? 145.051 127.291 97.537  1.00 17.49 ?  495  ALA A N    1 
ATOM   3232  C CA   . ALA A 1 495  ? 145.203 128.402 96.599  1.00 16.06 ?  495  ALA A CA   1 
ATOM   3233  C C    . ALA A 1 495  ? 144.122 128.438 95.552  1.00 20.40 ?  495  ALA A C    1 
ATOM   3234  O O    . ALA A 1 495  ? 143.696 129.510 95.150  1.00 23.93 ?  495  ALA A O    1 
ATOM   3235  C CB   . ALA A 1 495  ? 146.526 128.318 95.907  1.00 17.97 ?  495  ALA A CB   1 
ATOM   3236  N N    . GLY A 1 496  ? 143.703 127.289 95.058  1.00 21.99 ?  496  GLY A N    1 
ATOM   3237  C CA   . GLY A 1 496  ? 142.625 127.197 94.087  1.00 19.45 ?  496  GLY A CA   1 
ATOM   3238  C C    . GLY A 1 496  ? 141.361 127.780 94.636  1.00 18.50 ?  496  GLY A C    1 
ATOM   3239  O O    . GLY A 1 496  ? 140.771 128.635 94.015  1.00 22.30 ?  496  GLY A O    1 
ATOM   3240  N N    . ALA A 1 497  ? 140.974 127.370 95.823  1.00 15.57 ?  497  ALA A N    1 
ATOM   3241  C CA   . ALA A 1 497  ? 139.760 127.835 96.427  1.00 15.99 ?  497  ALA A CA   1 
ATOM   3242  C C    . ALA A 1 497  ? 139.751 129.296 96.626  1.00 11.99 ?  497  ALA A C    1 
ATOM   3243  O O    . ALA A 1 497  ? 138.712 129.898 96.518  1.00 13.20 ?  497  ALA A O    1 
ATOM   3244  C CB   . ALA A 1 497  ? 139.587 127.183 97.762  1.00 19.74 ?  497  ALA A CB   1 
ATOM   3245  N N    . VAL A 1 498  ? 140.864 129.899 96.964  1.00 11.64 ?  498  VAL A N    1 
ATOM   3246  C CA   . VAL A 1 498  ? 140.815 131.304 97.252  1.00 12.25 ?  498  VAL A CA   1 
ATOM   3247  C C    . VAL A 1 498  ? 140.848 132.065 95.970  1.00 15.54 ?  498  VAL A C    1 
ATOM   3248  O O    . VAL A 1 498  ? 140.231 133.091 95.861  1.00 20.50 ?  498  VAL A O    1 
ATOM   3249  C CB   . VAL A 1 498  ? 141.964 131.727 98.132  1.00 13.61 ?  498  VAL A CB   1 
ATOM   3250  C CG1  . VAL A 1 498  ? 142.176 133.226 98.057  1.00 17.21 ?  498  VAL A CG1  1 
ATOM   3251  C CG2  . VAL A 1 498  ? 141.702 131.285 99.559  1.00 17.41 ?  498  VAL A CG2  1 
ATOM   3252  N N    . ARG A 1 499  ? 141.552 131.584 94.975  1.00 17.55 ?  499  ARG A N    1 
ATOM   3253  C CA   . ARG A 1 499  ? 141.494 132.261 93.681  1.00 17.03 ?  499  ARG A CA   1 
ATOM   3254  C C    . ARG A 1 499  ? 140.100 132.184 93.068  1.00 15.98 ?  499  ARG A C    1 
ATOM   3255  O O    . ARG A 1 499  ? 139.572 133.192 92.575  1.00 21.47 ?  499  ARG A O    1 
ATOM   3256  C CB   . ARG A 1 499  ? 142.525 131.657 92.727  1.00 20.47 ?  499  ARG A CB   1 
ATOM   3257  C CG   . ARG A 1 499  ? 142.970 132.596 91.616  1.00 22.99 ?  499  ARG A CG   1 
ATOM   3258  C CD   . ARG A 1 499  ? 144.246 132.110 90.942  1.00 25.58 ?  499  ARG A CD   1 
ATOM   3259  N NE   . ARG A 1 499  ? 144.027 130.900 90.158  1.00 21.77 ?  499  ARG A NE   1 
ATOM   3260  C CZ   . ARG A 1 499  ? 143.590 130.887 88.906  1.00 22.68 ?  499  ARG A CZ   1 
ATOM   3261  N NH1  . ARG A 1 499  ? 143.311 132.007 88.260  1.00 23.06 ?  499  ARG A NH1  1 
ATOM   3262  N NH2  . ARG A 1 499  ? 143.429 129.721 88.286  1.00 20.71 ?  499  ARG A NH2  1 
ATOM   3263  N N    . ARG A 1 500  ? 139.502 131.002 93.090  1.00 9.48  ?  500  ARG A N    1 
ATOM   3264  C CA   . ARG A 1 500  ? 138.164 130.840 92.544  1.00 13.94 ?  500  ARG A CA   1 
ATOM   3265  C C    . ARG A 1 500  ? 137.174 131.690 93.318  1.00 19.53 ?  500  ARG A C    1 
ATOM   3266  O O    . ARG A 1 500  ? 136.351 132.389 92.726  1.00 22.38 ?  500  ARG A O    1 
ATOM   3267  C CB   . ARG A 1 500  ? 137.771 129.370 92.602  1.00 9.10  ?  500  ARG A CB   1 
ATOM   3268  C CG   . ARG A 1 500  ? 138.566 128.448 91.699  1.00 12.45 ?  500  ARG A CG   1 
ATOM   3269  C CD   . ARG A 1 500  ? 138.043 127.025 91.815  1.00 13.40 ?  500  ARG A CD   1 
ATOM   3270  N NE   . ARG A 1 500  ? 138.828 126.089 91.013  1.00 15.77 ?  500  ARG A NE   1 
ATOM   3271  C CZ   . ARG A 1 500  ? 138.661 124.769 91.020  1.00 17.16 ?  500  ARG A CZ   1 
ATOM   3272  N NH1  . ARG A 1 500  ? 137.735 124.220 91.793  1.00 16.35 ?  500  ARG A NH1  1 
ATOM   3273  N NH2  . ARG A 1 500  ? 139.420 123.998 90.254  1.00 15.21 ?  500  ARG A NH2  1 
ATOM   3274  N N    . ILE A 1 501  ? 137.254 131.639 94.641  1.00 14.90 ?  501  ILE A N    1 
ATOM   3275  C CA   . ILE A 1 501  ? 136.349 132.418 95.484  1.00 5.23  ?  501  ILE A CA   1 
ATOM   3276  C C    . ILE A 1 501  ? 136.458 133.899 95.147  1.00 5.85  ?  501  ILE A C    1 
ATOM   3277  O O    . ILE A 1 501  ? 135.446 134.607 95.057  1.00 14.69 ?  501  ILE A O    1 
ATOM   3278  C CB   . ILE A 1 501  ? 136.644 132.146 96.971  1.00 7.14  ?  501  ILE A CB   1 
ATOM   3279  C CG1  . ILE A 1 501  ? 136.081 130.788 97.386  1.00 10.80 ?  501  ILE A CG1  1 
ATOM   3280  C CG2  . ILE A 1 501  ? 136.068 133.240 97.858  1.00 6.70  ?  501  ILE A CG2  1 
ATOM   3281  C CD1  . ILE A 1 501  ? 136.455 130.393 98.787  1.00 6.06  ?  501  ILE A CD1  1 
ATOM   3282  N N    . HIS A 1 502  ? 137.686 134.387 94.945  1.00 6.47  ?  502  HIS A N    1 
ATOM   3283  C CA   . HIS A 1 502  ? 137.886 135.780 94.557  1.00 4.91  ?  502  HIS A CA   1 
ATOM   3284  C C    . HIS A 1 502  ? 137.238 136.078 93.213  1.00 11.70 ?  502  HIS A C    1 
ATOM   3285  O O    . HIS A 1 502  ? 136.623 137.136 93.034  1.00 18.75 ?  502  HIS A O    1 
ATOM   3286  C CB   . HIS A 1 502  ? 139.377 136.098 94.495  1.00 8.14  ?  502  HIS A CB   1 
ATOM   3287  C CG   . HIS A 1 502  ? 139.946 136.596 95.785  1.00 13.61 ?  502  HIS A CG   1 
ATOM   3288  N ND1  . HIS A 1 502  ? 140.025 135.808 96.913  1.00 15.99 ?  502  HIS A ND1  1 
ATOM   3289  C CD2  . HIS A 1 502  ? 140.476 137.794 96.124  1.00 18.34 ?  502  HIS A CD2  1 
ATOM   3290  C CE1  . HIS A 1 502  ? 140.575 136.501 97.893  1.00 14.43 ?  502  HIS A CE1  1 
ATOM   3291  N NE2  . HIS A 1 502  ? 140.858 137.710 97.441  1.00 19.52 ?  502  HIS A NE2  1 
ATOM   3292  N N    . GLU A 1 503  ? 137.373 135.161 92.252  1.00 11.88 ?  503  GLU A N    1 
ATOM   3293  C CA   . GLU A 1 503  ? 136.768 135.384 90.941  1.00 14.36 ?  503  GLU A CA   1 
ATOM   3294  C C    . GLU A 1 503  ? 135.242 135.390 91.026  1.00 13.69 ?  503  GLU A C    1 
ATOM   3295  O O    . GLU A 1 503  ? 134.580 136.212 90.378  1.00 16.63 ?  503  GLU A O    1 
ATOM   3296  C CB   . GLU A 1 503  ? 137.247 134.323 89.947  1.00 12.27 ?  503  GLU A CB   1 
ATOM   3297  C CG   . GLU A 1 503  ? 138.743 134.344 89.500  1.00 19.53 ?  503  GLU A CG   1 
ATOM   3298  C CD   . GLU A 1 503  ? 139.369 135.703 89.126  1.00 19.46 ?  503  GLU A CD   1 
ATOM   3299  O OE1  . GLU A 1 503  ? 138.680 136.737 88.986  1.00 18.49 ?  503  GLU A OE1  1 
ATOM   3300  O OE2  . GLU A 1 503  ? 140.607 135.720 88.949  1.00 15.66 ?  503  GLU A OE2  1 
ATOM   3301  N N    . GLY A 1 504  ? 134.665 134.482 91.820  1.00 13.26 ?  504  GLY A N    1 
ATOM   3302  C CA   . GLY A 1 504  ? 133.220 134.487 92.005  1.00 9.30  ?  504  GLY A CA   1 
ATOM   3303  C C    . GLY A 1 504  ? 132.720 135.744 92.693  1.00 9.93  ?  504  GLY A C    1 
ATOM   3304  O O    . GLY A 1 504  ? 131.666 136.283 92.339  1.00 16.65 ?  504  GLY A O    1 
ATOM   3305  N N    . GLN A 1 505  ? 133.473 136.233 93.682  1.00 9.21  ?  505  GLN A N    1 
ATOM   3306  C CA   . GLN A 1 505  ? 133.113 137.478 94.353  1.00 9.00  ?  505  GLN A CA   1 
ATOM   3307  C C    . GLN A 1 505  ? 133.198 138.668 93.404  1.00 11.09 ?  505  GLN A C    1 
ATOM   3308  O O    . GLN A 1 505  ? 132.346 139.562 93.447  1.00 14.72 ?  505  GLN A O    1 
ATOM   3309  C CB   . GLN A 1 505  ? 134.012 137.693 95.569  1.00 5.12  ?  505  GLN A CB   1 
ATOM   3310  C CG   . GLN A 1 505  ? 133.488 137.058 96.844  1.00 7.81  ?  505  GLN A CG   1 
ATOM   3311  C CD   . GLN A 1 505  ? 134.376 137.334 98.039  1.00 12.00 ?  505  GLN A CD   1 
ATOM   3312  O OE1  . GLN A 1 505  ? 135.477 137.865 97.900  1.00 8.26  ?  505  GLN A OE1  1 
ATOM   3313  N NE2  . GLN A 1 505  ? 133.899 136.975 99.225  1.00 12.96 ?  505  GLN A NE2  1 
ATOM   3314  N N    . ASN A 1 506  ? 134.222 138.698 92.545  1.00 11.90 ?  506  ASN A N    1 
ATOM   3315  C CA   . ASN A 1 506  ? 134.333 139.769 91.557  1.00 6.96  ?  506  ASN A CA   1 
ATOM   3316  C C    . ASN A 1 506  ? 133.176 139.728 90.567  1.00 7.32  ?  506  ASN A C    1 
ATOM   3317  O O    . ASN A 1 506  ? 132.649 140.776 90.172  1.00 11.35 ?  506  ASN A O    1 
ATOM   3318  C CB   . ASN A 1 506  ? 135.668 139.669 90.820  1.00 10.15 ?  506  ASN A CB   1 
ATOM   3319  C CG   . ASN A 1 506  ? 136.299 141.025 90.569  1.00 10.32 ?  506  ASN A CG   1 
ATOM   3320  O OD1  . ASN A 1 506  ? 135.678 141.913 89.986  1.00 9.30  ?  506  ASN A OD1  1 
ATOM   3321  N ND2  . ASN A 1 506  ? 137.545 141.186 90.999  1.00 11.52 ?  506  ASN A ND2  1 
ATOM   3322  N N    . ARG A 1 507  ? 132.770 138.524 90.154  1.00 10.27 ?  507  ARG A N    1 
ATOM   3323  C CA   . ARG A 1 507  ? 131.621 138.387 89.264  1.00 10.33 ?  507  ARG A CA   1 
ATOM   3324  C C    . ARG A 1 507  ? 130.339 138.882 89.926  1.00 13.26 ?  507  ARG A C    1 
ATOM   3325  O O    . ARG A 1 507  ? 129.539 139.591 89.299  1.00 20.28 ?  507  ARG A O    1 
ATOM   3326  C CB   . ARG A 1 507  ? 131.476 136.928 88.835  1.00 12.54 ?  507  ARG A CB   1 
ATOM   3327  C CG   . ARG A 1 507  ? 130.265 136.636 87.968  1.00 14.79 ?  507  ARG A CG   1 
ATOM   3328  C CD   . ARG A 1 507  ? 130.590 135.636 86.865  1.00 19.33 ?  507  ARG A CD   1 
ATOM   3329  N NE   . ARG A 1 507  ? 131.677 134.731 87.224  1.00 15.28 ?  507  ARG A NE   1 
ATOM   3330  C CZ   . ARG A 1 507  ? 131.527 133.613 87.922  1.00 16.05 ?  507  ARG A CZ   1 
ATOM   3331  N NH1  . ARG A 1 507  ? 130.339 133.220 88.351  1.00 19.97 ?  507  ARG A NH1  1 
ATOM   3332  N NH2  . ARG A 1 507  ? 132.596 132.872 88.197  1.00 16.68 ?  507  ARG A NH2  1 
ATOM   3333  N N    . THR A 1 508  ? 130.130 138.527 91.197  1.00 11.48 ?  508  THR A N    1 
ATOM   3334  C CA   . THR A 1 508  ? 128.944 138.996 91.912  1.00 6.85  ?  508  THR A CA   1 
ATOM   3335  C C    . THR A 1 508  ? 128.958 140.513 92.083  1.00 1.57  ?  508  THR A C    1 
ATOM   3336  O O    . THR A 1 508  ? 127.919 141.170 91.948  1.00 3.79  ?  508  THR A O    1 
ATOM   3337  C CB   . THR A 1 508  ? 128.837 138.303 93.269  1.00 3.85  ?  508  THR A CB   1 
ATOM   3338  O OG1  . THR A 1 508  ? 128.961 136.887 93.092  1.00 11.86 ?  508  THR A OG1  1 
ATOM   3339  C CG2  . THR A 1 508  ? 127.496 138.603 93.913  1.00 2.93  ?  508  THR A CG2  1 
ATOM   3340  N N    . LEU A 1 509  ? 130.127 141.088 92.378  1.00 4.58  ?  509  LEU A N    1 
ATOM   3341  C CA   . LEU A 1 509  ? 130.227 142.538 92.527  1.00 3.33  ?  509  LEU A CA   1 
ATOM   3342  C C    . LEU A 1 509  ? 129.965 143.251 91.205  1.00 4.56  ?  509  LEU A C    1 
ATOM   3343  O O    . LEU A 1 509  ? 129.326 144.311 91.183  1.00 11.23 ?  509  LEU A O    1 
ATOM   3344  C CB   . LEU A 1 509  ? 131.602 142.911 93.082  1.00 4.17  ?  509  LEU A CB   1 
ATOM   3345  C CG   . LEU A 1 509  ? 131.734 144.182 93.925  1.00 0.93  ?  509  LEU A CG   1 
ATOM   3346  C CD1  . LEU A 1 509  ? 132.885 144.037 94.906  1.00 8.22  ?  509  LEU A CD1  1 
ATOM   3347  C CD2  . LEU A 1 509  ? 131.936 145.410 93.054  1.00 2.12  ?  509  LEU A CD2  1 
ATOM   3348  N N    . ASN A 1 510  ? 130.453 142.691 90.093  1.00 7.91  ?  510  ASN A N    1 
ATOM   3349  C CA   . ASN A 1 510  ? 130.178 143.282 88.787  1.00 10.47 ?  510  ASN A CA   1 
ATOM   3350  C C    . ASN A 1 510  ? 128.707 143.162 88.411  1.00 10.30 ?  510  ASN A C    1 
ATOM   3351  O O    . ASN A 1 510  ? 128.174 144.039 87.722  1.00 14.23 ?  510  ASN A O    1 
ATOM   3352  C CB   . ASN A 1 510  ? 131.055 142.632 87.718  1.00 10.70 ?  510  ASN A CB   1 
ATOM   3353  C CG   . ASN A 1 510  ? 131.663 143.645 86.770  1.00 14.32 ?  510  ASN A CG   1 
ATOM   3354  O OD1  . ASN A 1 510  ? 131.260 144.808 86.742  1.00 10.94 ?  510  ASN A OD1  1 
ATOM   3355  N ND2  . ASN A 1 510  ? 132.640 143.208 85.984  1.00 14.63 ?  510  ASN A ND2  1 
ATOM   3356  N N    . MET A 1 511  ? 128.044 142.082 88.833  1.00 10.47 ?  511  MET A N    1 
ATOM   3357  C CA   . MET A 1 511  ? 126.596 142.000 88.665  1.00 6.41  ?  511  MET A CA   1 
ATOM   3358  C C    . MET A 1 511  ? 125.887 143.070 89.486  1.00 5.57  ?  511  MET A C    1 
ATOM   3359  O O    . MET A 1 511  ? 124.927 143.691 89.016  1.00 6.67  ?  511  MET A O    1 
ATOM   3360  C CB   . MET A 1 511  ? 126.092 140.613 89.063  1.00 11.19 ?  511  MET A CB   1 
ATOM   3361  C CG   . MET A 1 511  ? 124.594 140.417 88.867  1.00 10.74 ?  511  MET A CG   1 
ATOM   3362  S SD   . MET A 1 511  ? 123.625 140.630 90.375  1.00 13.16 ?  511  MET A SD   1 
ATOM   3363  C CE   . MET A 1 511  ? 123.878 139.056 91.184  1.00 6.58  ?  511  MET A CE   1 
ATOM   3364  N N    . LEU A 1 512  ? 126.347 143.293 90.720  1.00 9.16  ?  512  LEU A N    1 
ATOM   3365  C CA   . LEU A 1 512  ? 125.681 144.244 91.607  1.00 5.19  ?  512  LEU A CA   1 
ATOM   3366  C C    . LEU A 1 512  ? 125.880 145.686 91.160  1.00 5.88  ?  512  LEU A C    1 
ATOM   3367  O O    . LEU A 1 512  ? 124.994 146.521 91.369  1.00 6.66  ?  512  LEU A O    1 
ATOM   3368  C CB   . LEU A 1 512  ? 126.183 144.075 93.040  1.00 2.39  ?  512  LEU A CB   1 
ATOM   3369  C CG   . LEU A 1 512  ? 125.666 142.878 93.833  1.00 3.04  ?  512  LEU A CG   1 
ATOM   3370  C CD1  . LEU A 1 512  ? 126.357 142.813 95.177  1.00 1.62  ?  512  LEU A CD1  1 
ATOM   3371  C CD2  . LEU A 1 512  ? 124.161 142.951 94.007  1.00 1.62  ?  512  LEU A CD2  1 
ATOM   3372  N N    . LYS A 1 513  ? 127.033 146.007 90.567  1.00 7.35  ?  513  LYS A N    1 
ATOM   3373  C CA   . LYS A 1 513  ? 127.289 147.388 90.165  1.00 4.49  ?  513  LYS A CA   1 
ATOM   3374  C C    . LYS A 1 513  ? 126.377 147.830 89.027  1.00 11.90 ?  513  LYS A C    1 
ATOM   3375  O O    . LYS A 1 513  ? 126.077 149.023 88.905  1.00 17.01 ?  513  LYS A O    1 
ATOM   3376  C CB   . LYS A 1 513  ? 128.755 147.565 89.770  1.00 5.37  ?  513  LYS A CB   1 
ATOM   3377  C CG   . LYS A 1 513  ? 129.705 147.635 90.953  1.00 6.28  ?  513  LYS A CG   1 
ATOM   3378  C CD   . LYS A 1 513  ? 131.120 147.977 90.517  1.00 8.01  ?  513  LYS A CD   1 
ATOM   3379  C CE   . LYS A 1 513  ? 131.541 149.340 91.038  1.00 9.29  ?  513  LYS A CE   1 
ATOM   3380  N NZ   . LYS A 1 513  ? 132.930 149.324 91.571  1.00 13.39 ?  513  LYS A NZ   1 
ATOM   3381  N N    . SER A 1 514  ? 125.922 146.894 88.192  1.00 17.32 ?  514  SER A N    1 
ATOM   3382  C CA   . SER A 1 514  ? 125.007 147.196 87.100  1.00 11.89 ?  514  SER A CA   1 
ATOM   3383  C C    . SER A 1 514  ? 123.543 147.052 87.501  1.00 9.35  ?  514  SER A C    1 
ATOM   3384  O O    . SER A 1 514  ? 122.690 146.842 86.632  1.00 13.75 ?  514  SER A O    1 
ATOM   3385  C CB   . SER A 1 514  ? 125.310 146.303 85.895  1.00 12.04 ?  514  SER A CB   1 
ATOM   3386  O OG   . SER A 1 514  ? 126.634 146.499 85.432  1.00 11.70 ?  514  SER A OG   1 
ATOM   3387  N N    . ASP A 1 515  ? 123.234 147.162 88.790  1.00 11.48 ?  515  ASP A N    1 
ATOM   3388  C CA   . ASP A 1 515  ? 121.864 147.065 89.266  1.00 12.30 ?  515  ASP A CA   1 
ATOM   3389  C C    . ASP A 1 515  ? 121.128 148.382 89.028  1.00 16.41 ?  515  ASP A C    1 
ATOM   3390  O O    . ASP A 1 515  ? 121.646 149.319 88.415  1.00 21.50 ?  515  ASP A O    1 
ATOM   3391  C CB   . ASP A 1 515  ? 121.843 146.691 90.747  1.00 10.58 ?  515  ASP A CB   1 
ATOM   3392  C CG   . ASP A 1 515  ? 120.695 145.770 91.101  1.00 12.57 ?  515  ASP A CG   1 
ATOM   3393  O OD1  . ASP A 1 515  ? 119.550 146.073 90.710  1.00 14.11 ?  515  ASP A OD1  1 
ATOM   3394  O OD2  . ASP A 1 515  ? 120.936 144.752 91.783  1.00 14.91 ?  515  ASP A OD2  1 
ATOM   3395  N N    . ARG A 1 516  ? 119.891 148.453 89.522  1.00 9.40  ?  516  ARG A N    1 
ATOM   3396  C CA   . ARG A 1 516  ? 119.093 149.667 89.453  1.00 13.78 ?  516  ARG A CA   1 
ATOM   3397  C C    . ARG A 1 516  ? 118.740 150.241 90.815  1.00 15.18 ?  516  ARG A C    1 
ATOM   3398  O O    . ARG A 1 516  ? 118.335 151.406 90.887  1.00 15.63 ?  516  ARG A O    1 
ATOM   3399  C CB   . ARG A 1 516  ? 117.793 149.412 88.670  1.00 16.85 ?  516  ARG A CB   1 
ATOM   3400  C CG   . ARG A 1 516  ? 117.340 150.578 87.805  1.00 17.49 ?  516  ARG A CG   1 
ATOM   3401  C CD   . ARG A 1 516  ? 116.038 150.268 87.072  1.00 18.66 ?  516  ARG A CD   1 
ATOM   3402  N NE   . ARG A 1 516  ? 114.855 150.372 87.920  1.00 19.22 ?  516  ARG A NE   1 
ATOM   3403  C CZ   . ARG A 1 516  ? 114.239 149.340 88.481  1.00 16.47 ?  516  ARG A CZ   1 
ATOM   3404  N NH1  . ARG A 1 516  ? 114.692 148.105 88.342  1.00 12.92 ?  516  ARG A NH1  1 
ATOM   3405  N NH2  . ARG A 1 516  ? 113.136 149.551 89.194  1.00 15.90 ?  516  ARG A NH2  1 
ATOM   3406  N N    . PHE A 1 517  ? 118.884 149.467 91.889  1.00 15.88 ?  517  PHE A N    1 
ATOM   3407  C CA   . PHE A 1 517  ? 118.570 149.916 93.238  1.00 10.65 ?  517  PHE A CA   1 
ATOM   3408  C C    . PHE A 1 517  ? 119.790 150.079 94.129  1.00 10.11 ?  517  PHE A C    1 
ATOM   3409  O O    . PHE A 1 517  ? 119.814 150.993 94.953  1.00 14.69 ?  517  PHE A O    1 
ATOM   3410  C CB   . PHE A 1 517  ? 117.587 148.944 93.903  1.00 8.93  ?  517  PHE A CB   1 
ATOM   3411  C CG   . PHE A 1 517  ? 116.161 149.092 93.431  1.00 12.93 ?  517  PHE A CG   1 
ATOM   3412  C CD1  . PHE A 1 517  ? 115.805 150.075 92.520  1.00 14.35 ?  517  PHE A CD1  1 
ATOM   3413  C CD2  . PHE A 1 517  ? 115.167 148.278 93.945  1.00 13.25 ?  517  PHE A CD2  1 
ATOM   3414  C CE1  . PHE A 1 517  ? 114.493 150.215 92.107  1.00 14.23 ?  517  PHE A CE1  1 
ATOM   3415  C CE2  . PHE A 1 517  ? 113.856 148.409 93.533  1.00 12.19 ?  517  PHE A CE2  1 
ATOM   3416  C CZ   . PHE A 1 517  ? 113.518 149.381 92.615  1.00 12.06 ?  517  PHE A CZ   1 
ATOM   3417  N N    . LEU A 1 518  ? 120.810 149.231 93.979  1.00 5.62  ?  518  LEU A N    1 
ATOM   3418  C CA   . LEU A 1 518  ? 122.045 149.357 94.742  1.00 0.00  ?  518  LEU A CA   1 
ATOM   3419  C C    . LEU A 1 518  ? 123.097 150.184 94.017  1.00 4.47  ?  518  LEU A C    1 
ATOM   3420  O O    . LEU A 1 518  ? 124.298 149.985 94.236  1.00 13.96 ?  518  LEU A O    1 
ATOM   3421  C CB   . LEU A 1 518  ? 122.604 147.975 95.085  1.00 0.00  ?  518  LEU A CB   1 
ATOM   3422  C CG   . LEU A 1 518  ? 121.631 146.931 95.633  1.00 0.84  ?  518  LEU A CG   1 
ATOM   3423  C CD1  . LEU A 1 518  ? 122.371 145.650 95.973  1.00 7.78  ?  518  LEU A CD1  1 
ATOM   3424  C CD2  . LEU A 1 518  ? 120.908 147.466 96.857  1.00 0.00  ?  518  LEU A CD2  1 
ATOM   3425  N N    . ALA A 1 519  ? 122.677 151.117 93.164  1.00 3.80  ?  519  ALA A N    1 
ATOM   3426  C CA   . ALA A 1 519  ? 123.614 151.916 92.387  1.00 8.65  ?  519  ALA A CA   1 
ATOM   3427  C C    . ALA A 1 519  ? 124.228 153.063 93.175  1.00 11.07 ?  519  ALA A C    1 
ATOM   3428  O O    . ALA A 1 519  ? 125.119 153.738 92.651  1.00 7.91  ?  519  ALA A O    1 
ATOM   3429  C CB   . ALA A 1 519  ? 122.923 152.474 91.140  1.00 11.03 ?  519  ALA A CB   1 
ATOM   3430  N N    . ASP A 1 520  ? 123.779 153.313 94.405  1.00 9.65  ?  520  ASP A N    1 
ATOM   3431  C CA   . ASP A 1 520  ? 124.333 154.391 95.214  1.00 7.38  ?  520  ASP A CA   1 
ATOM   3432  C C    . ASP A 1 520  ? 125.093 153.882 96.431  1.00 7.72  ?  520  ASP A C    1 
ATOM   3433  O O    . ASP A 1 520  ? 125.496 154.686 97.278  1.00 11.98 ?  520  ASP A O    1 
ATOM   3434  C CB   . ASP A 1 520  ? 123.224 155.391 95.591  1.00 9.51  ?  520  ASP A CB   1 
ATOM   3435  C CG   . ASP A 1 520  ? 122.240 154.887 96.664  1.00 15.84 ?  520  ASP A CG   1 
ATOM   3436  O OD1  . ASP A 1 520  ? 122.617 154.252 97.670  1.00 19.72 ?  520  ASP A OD1  1 
ATOM   3437  O OD2  . ASP A 1 520  ? 121.047 155.231 96.534  1.00 13.34 ?  520  ASP A OD2  1 
ATOM   3438  N N    . ALA A 1 521  ? 125.300 152.573 96.530  1.00 4.38  ?  521  ALA A N    1 
ATOM   3439  C CA   . ALA A 1 521  ? 125.981 151.986 97.672  1.00 3.13  ?  521  ALA A CA   1 
ATOM   3440  C C    . ALA A 1 521  ? 127.447 152.398 97.702  1.00 8.11  ?  521  ALA A C    1 
ATOM   3441  O O    . ALA A 1 521  ? 128.049 152.720 96.674  1.00 13.61 ?  521  ALA A O    1 
ATOM   3442  C CB   . ALA A 1 521  ? 125.873 150.463 97.629  1.00 2.01  ?  521  ALA A CB   1 
ATOM   3443  N N    . ASP A 1 522  ? 128.023 152.383 98.900  1.00 6.78  ?  522  ASP A N    1 
ATOM   3444  C CA   . ASP A 1 522  ? 129.432 152.718 99.076  1.00 10.20 ?  522  ASP A CA   1 
ATOM   3445  C C    . ASP A 1 522  ? 130.251 151.502 98.672  1.00 12.27 ?  522  ASP A C    1 
ATOM   3446  O O    . ASP A 1 522  ? 130.411 150.555 99.446  1.00 16.77 ?  522  ASP A O    1 
ATOM   3447  C CB   . ASP A 1 522  ? 129.712 153.137 100.514 1.00 12.14 ?  522  ASP A CB   1 
ATOM   3448  C CG   . ASP A 1 522  ? 129.943 154.626 100.646 1.00 16.34 ?  522  ASP A CG   1 
ATOM   3449  O OD1  . ASP A 1 522  ? 129.456 155.380 99.778  1.00 15.44 ?  522  ASP A OD1  1 
ATOM   3450  O OD2  . ASP A 1 522  ? 130.607 155.047 101.615 1.00 18.13 ?  522  ASP A OD2  1 
ATOM   3451  N N    . TRP A 1 523  ? 130.770 151.524 97.446  1.00 11.01 ?  523  TRP A N    1 
ATOM   3452  C CA   . TRP A 1 523  ? 131.432 150.352 96.892  1.00 10.24 ?  523  TRP A CA   1 
ATOM   3453  C C    . TRP A 1 523  ? 132.825 150.134 97.458  1.00 15.26 ?  523  TRP A C    1 
ATOM   3454  O O    . TRP A 1 523  ? 133.324 149.004 97.409  1.00 17.44 ?  523  TRP A O    1 
ATOM   3455  C CB   . TRP A 1 523  ? 131.489 150.464 95.369  1.00 10.53 ?  523  TRP A CB   1 
ATOM   3456  C CG   . TRP A 1 523  ? 130.141 150.327 94.741  1.00 9.74  ?  523  TRP A CG   1 
ATOM   3457  C CD1  . TRP A 1 523  ? 129.459 151.281 94.045  1.00 10.36 ?  523  TRP A CD1  1 
ATOM   3458  C CD2  . TRP A 1 523  ? 129.297 149.171 94.771  1.00 8.82  ?  523  TRP A CD2  1 
ATOM   3459  N NE1  . TRP A 1 523  ? 128.247 150.786 93.630  1.00 9.15  ?  523  TRP A NE1  1 
ATOM   3460  C CE2  . TRP A 1 523  ? 128.124 149.493 94.064  1.00 8.53  ?  523  TRP A CE2  1 
ATOM   3461  C CE3  . TRP A 1 523  ? 129.422 147.892 95.322  1.00 6.54  ?  523  TRP A CE3  1 
ATOM   3462  C CZ2  . TRP A 1 523  ? 127.086 148.585 93.894  1.00 8.99  ?  523  TRP A CZ2  1 
ATOM   3463  C CZ3  . TRP A 1 523  ? 128.390 146.994 95.153  1.00 4.16  ?  523  TRP A CZ3  1 
ATOM   3464  C CH2  . TRP A 1 523  ? 127.237 147.343 94.446  1.00 9.21  ?  523  TRP A CH2  1 
ATOM   3465  N N    . ASP A 1 524  ? 133.458 151.178 97.998  1.00 16.83 ?  524  ASP A N    1 
ATOM   3466  C CA   . ASP A 1 524  ? 134.730 150.993 98.686  1.00 13.76 ?  524  ASP A CA   1 
ATOM   3467  C C    . ASP A 1 524  ? 134.556 150.109 99.913  1.00 15.18 ?  524  ASP A C    1 
ATOM   3468  O O    . ASP A 1 524  ? 135.350 149.190 100.149 1.00 16.93 ?  524  ASP A O    1 
ATOM   3469  C CB   . ASP A 1 524  ? 135.317 152.349 99.079  1.00 16.65 ?  524  ASP A CB   1 
ATOM   3470  C CG   . ASP A 1 524  ? 135.258 153.360 97.952  1.00 21.19 ?  524  ASP A CG   1 
ATOM   3471  O OD1  . ASP A 1 524  ? 136.156 153.336 97.084  1.00 22.32 ?  524  ASP A OD1  1 
ATOM   3472  O OD2  . ASP A 1 524  ? 134.318 154.182 97.936  1.00 22.60 ?  524  ASP A OD2  1 
ATOM   3473  N N    . ILE A 1 525  ? 133.500 150.360 100.693 1.00 12.93 ?  525  ILE A N    1 
ATOM   3474  C CA   . ILE A 1 525  ? 133.248 149.580 101.903 1.00 9.94  ?  525  ILE A CA   1 
ATOM   3475  C C    . ILE A 1 525  ? 132.962 148.126 101.549 1.00 9.43  ?  525  ILE A C    1 
ATOM   3476  O O    . ILE A 1 525  ? 133.512 147.203 102.159 1.00 11.42 ?  525  ILE A O    1 
ATOM   3477  C CB   . ILE A 1 525  ? 132.100 150.205 102.722 1.00 11.79 ?  525  ILE A CB   1 
ATOM   3478  C CG1  . ILE A 1 525  ? 132.589 151.409 103.534 1.00 14.66 ?  525  ILE A CG1  1 
ATOM   3479  C CG2  . ILE A 1 525  ? 131.477 149.183 103.661 1.00 9.97  ?  525  ILE A CG2  1 
ATOM   3480  C CD1  . ILE A 1 525  ? 132.654 152.714 102.772 1.00 14.47 ?  525  ILE A CD1  1 
ATOM   3481  N N    . ALA A 1 526  ? 132.109 147.901 100.545 1.00 12.19 ?  526  ALA A N    1 
ATOM   3482  C CA   . ALA A 1 526  ? 131.766 146.536 100.155 1.00 10.80 ?  526  ALA A CA   1 
ATOM   3483  C C    . ALA A 1 526  ? 132.974 145.793 99.596  1.00 13.40 ?  526  ALA A C    1 
ATOM   3484  O O    . ALA A 1 526  ? 133.217 144.632 99.950  1.00 15.74 ?  526  ALA A O    1 
ATOM   3485  C CB   . ALA A 1 526  ? 130.628 146.553 99.134  1.00 8.36  ?  526  ALA A CB   1 
ATOM   3486  N N    . THR A 1 527  ? 133.754 146.454 98.736  1.00 13.34 ?  527  THR A N    1 
ATOM   3487  C CA   . THR A 1 527  ? 134.925 145.812 98.147  1.00 14.04 ?  527  THR A CA   1 
ATOM   3488  C C    . THR A 1 527  ? 135.980 145.495 99.201  1.00 15.92 ?  527  THR A C    1 
ATOM   3489  O O    . THR A 1 527  ? 136.614 144.435 99.149  1.00 14.83 ?  527  THR A O    1 
ATOM   3490  C CB   . THR A 1 527  ? 135.511 146.698 97.049  1.00 10.92 ?  527  THR A CB   1 
ATOM   3491  O OG1  . THR A 1 527  ? 134.448 147.287 96.291  1.00 9.81  ?  527  THR A OG1  1 
ATOM   3492  C CG2  . THR A 1 527  ? 136.390 145.879 96.120  1.00 15.13 ?  527  THR A CG2  1 
ATOM   3493  N N    . ALA A 1 528  ? 136.186 146.397 100.164 1.00 17.40 ?  528  ALA A N    1 
ATOM   3494  C CA   . ALA A 1 528  ? 137.187 146.157 101.195 1.00 15.47 ?  528  ALA A CA   1 
ATOM   3495  C C    . ALA A 1 528  ? 136.724 145.148 102.237 1.00 15.65 ?  528  ALA A C    1 
ATOM   3496  O O    . ALA A 1 528  ? 137.553 144.421 102.794 1.00 20.94 ?  528  ALA A O    1 
ATOM   3497  C CB   . ALA A 1 528  ? 137.565 147.473 101.876 1.00 12.13 ?  528  ALA A CB   1 
ATOM   3498  N N    . ALA A 1 529  ? 135.423 145.082 102.518 1.00 12.58 ?  529  ALA A N    1 
ATOM   3499  C CA   . ALA A 1 529  ? 134.898 144.220 103.566 1.00 10.66 ?  529  ALA A CA   1 
ATOM   3500  C C    . ALA A 1 529  ? 134.330 142.911 103.042 1.00 15.30 ?  529  ALA A C    1 
ATOM   3501  O O    . ALA A 1 529  ? 133.781 142.136 103.830 1.00 16.73 ?  529  ALA A O    1 
ATOM   3502  C CB   . ALA A 1 529  ? 133.822 144.961 104.365 1.00 10.54 ?  529  ALA A CB   1 
ATOM   3503  N N    . CYS A 1 530  ? 134.432 142.646 101.738 1.00 19.35 ?  530  CYS A N    1 
ATOM   3504  C CA   . CYS A 1 530  ? 133.966 141.380 101.194 1.00 17.23 ?  530  CYS A CA   1 
ATOM   3505  C C    . CYS A 1 530  ? 135.082 140.448 100.745 1.00 19.06 ?  530  CYS A C    1 
ATOM   3506  O O    . CYS A 1 530  ? 134.827 139.252 100.574 1.00 18.73 ?  530  CYS A O    1 
ATOM   3507  C CB   . CYS A 1 530  ? 133.015 141.628 100.016 1.00 16.38 ?  530  CYS A CB   1 
ATOM   3508  S SG   . CYS A 1 530  ? 131.349 142.104 100.528 1.00 32.16 ?  530  CYS A SG   1 
ATOM   3509  N N    . GLU A 1 531  ? 136.298 140.951 100.555 1.00 21.90 ?  531  GLU A N    1 
ATOM   3510  C CA   . GLU A 1 531  ? 137.409 140.101 100.157 1.00 23.87 ?  531  GLU A CA   1 
ATOM   3511  C C    . GLU A 1 531  ? 137.914 139.280 101.339 1.00 24.32 ?  531  GLU A C    1 
ATOM   3512  O O    . GLU A 1 531  ? 137.814 139.691 102.499 1.00 23.01 ?  531  GLU A O    1 
ATOM   3513  C CB   . GLU A 1 531  ? 138.548 140.937 99.567  1.00 23.21 ?  531  GLU A CB   1 
ATOM   3514  C CG   . GLU A 1 531  ? 139.332 141.757 100.582 1.00 22.30 ?  531  GLU A CG   1 
ATOM   3515  C CD   . GLU A 1 531  ? 140.603 142.345 100.000 1.00 26.23 ?  531  GLU A CD   1 
ATOM   3516  O OE1  . GLU A 1 531  ? 141.484 141.564 99.585  1.00 28.74 ?  531  GLU A OE1  1 
ATOM   3517  O OE2  . GLU A 1 531  ? 140.721 143.588 99.957  1.00 22.63 ?  531  GLU A OE2  1 
ATOM   3518  N N    . ILE A 1 532  ? 138.454 138.102 101.032 1.00 25.43 ?  532  ILE A N    1 
ATOM   3519  C CA   . ILE A 1 532  ? 138.969 137.181 102.035 1.00 24.57 ?  532  ILE A CA   1 
ATOM   3520  C C    . ILE A 1 532  ? 140.471 137.010 101.820 1.00 27.31 ?  532  ILE A C    1 
ATOM   3521  O O    . ILE A 1 532  ? 141.025 137.404 100.795 1.00 26.25 ?  532  ILE A O    1 
ATOM   3522  C CB   . ILE A 1 532  ? 138.239 135.820 102.011 1.00 23.53 ?  532  ILE A CB   1 
ATOM   3523  C CG1  . ILE A 1 532  ? 138.895 134.856 101.019 1.00 20.97 ?  532  ILE A CG1  1 
ATOM   3524  C CG2  . ILE A 1 532  ? 136.762 136.001 101.685 1.00 24.04 ?  532  ILE A CG2  1 
ATOM   3525  C CD1  . ILE A 1 532  ? 138.499 133.413 101.228 1.00 22.75 ?  532  ILE A CD1  1 
ATOM   3526  N N    . SER A 1 533  ? 141.131 136.427 102.820 1.00 23.74 ?  533  SER A N    1 
ATOM   3527  C CA   . SER A 1 533  ? 142.568 136.204 102.786 1.00 22.94 ?  533  SER A CA   1 
ATOM   3528  C C    . SER A 1 533  ? 142.875 134.719 102.919 1.00 21.78 ?  533  SER A C    1 
ATOM   3529  O O    . SER A 1 533  ? 142.110 133.959 103.521 1.00 19.84 ?  533  SER A O    1 
ATOM   3530  C CB   . SER A 1 533  ? 143.281 136.981 103.901 1.00 22.27 ?  533  SER A CB   1 
ATOM   3531  O OG   . SER A 1 533  ? 143.619 138.289 103.476 1.00 24.76 ?  533  SER A OG   1 
ATOM   3532  N N    . ASP A 1 534  ? 144.002 134.316 102.342 1.00 23.47 ?  534  ASP A N    1 
ATOM   3533  C CA   . ASP A 1 534  ? 144.451 132.933 102.454 1.00 24.44 ?  534  ASP A CA   1 
ATOM   3534  C C    . ASP A 1 534  ? 144.892 132.652 103.886 1.00 25.62 ?  534  ASP A C    1 
ATOM   3535  O O    . ASP A 1 534  ? 145.733 133.385 104.422 1.00 22.11 ?  534  ASP A O    1 
ATOM   3536  C CB   . ASP A 1 534  ? 145.603 132.676 101.483 1.00 22.76 ?  534  ASP A CB   1 
ATOM   3537  C CG   . ASP A 1 534  ? 145.615 131.257 100.946 1.00 23.39 ?  534  ASP A CG   1 
ATOM   3538  O OD1  . ASP A 1 534  ? 145.026 130.365 101.589 1.00 20.50 ?  534  ASP A OD1  1 
ATOM   3539  O OD2  . ASP A 1 534  ? 146.222 131.034 99.877  1.00 23.55 ?  534  ASP A OD2  1 
ATOM   3540  N N    . PRO A 1 535  ? 144.334 131.632 104.547 1.00 27.08 ?  535  PRO A N    1 
ATOM   3541  C CA   . PRO A 1 535  ? 144.805 131.293 105.902 1.00 29.06 ?  535  PRO A CA   1 
ATOM   3542  C C    . PRO A 1 535  ? 146.270 130.894 105.962 1.00 30.65 ?  535  PRO A C    1 
ATOM   3543  O O    . PRO A 1 535  ? 146.934 131.168 106.970 1.00 29.83 ?  535  PRO A O    1 
ATOM   3544  C CB   . PRO A 1 535  ? 143.885 130.134 106.309 1.00 27.11 ?  535  PRO A CB   1 
ATOM   3545  C CG   . PRO A 1 535  ? 142.659 130.321 105.487 1.00 25.23 ?  535  PRO A CG   1 
ATOM   3546  C CD   . PRO A 1 535  ? 143.130 130.872 104.174 1.00 25.28 ?  535  PRO A CD   1 
ATOM   3547  N N    . TYR A 1 536  ? 146.797 130.257 104.921 1.00 30.26 ?  536  TYR A N    1 
ATOM   3548  C CA   . TYR A 1 536  ? 148.211 129.903 104.883 1.00 29.68 ?  536  TYR A CA   1 
ATOM   3549  C C    . TYR A 1 536  ? 148.996 130.882 104.017 1.00 26.24 ?  536  TYR A C    1 
ATOM   3550  O O    . TYR A 1 536  ? 148.448 131.869 103.528 1.00 26.79 ?  536  TYR A O    1 
ATOM   3551  C CB   . TYR A 1 536  ? 148.400 128.476 104.364 1.00 28.38 ?  536  TYR A CB   1 
ATOM   3552  C CG   . TYR A 1 536  ? 147.479 127.464 105.004 1.00 30.04 ?  536  TYR A CG   1 
ATOM   3553  C CD1  . TYR A 1 536  ? 147.558 127.189 106.363 1.00 27.97 ?  536  TYR A CD1  1 
ATOM   3554  C CD2  . TYR A 1 536  ? 146.533 126.783 104.251 1.00 27.86 ?  536  TYR A CD2  1 
ATOM   3555  C CE1  . TYR A 1 536  ? 146.718 126.264 106.955 1.00 29.38 ?  536  TYR A CE1  1 
ATOM   3556  C CE2  . TYR A 1 536  ? 145.689 125.856 104.833 1.00 26.51 ?  536  TYR A CE2  1 
ATOM   3557  C CZ   . TYR A 1 536  ? 145.786 125.601 106.185 1.00 28.89 ?  536  TYR A CZ   1 
ATOM   3558  O OH   . TYR A 1 536  ? 144.949 124.679 106.769 1.00 26.53 ?  536  TYR A OH   1 
ATOM   3559  N N    . PRO A 1 570  ? 161.801 110.647 76.301  1.00 24.88 ?  570  PRO A N    1 
ATOM   3560  C CA   . PRO A 1 570  ? 162.891 109.789 75.827  1.00 25.67 ?  570  PRO A CA   1 
ATOM   3561  C C    . PRO A 1 570  ? 163.904 109.466 76.922  1.00 26.74 ?  570  PRO A C    1 
ATOM   3562  O O    . PRO A 1 570  ? 164.315 108.313 77.057  1.00 29.51 ?  570  PRO A O    1 
ATOM   3563  C CB   . PRO A 1 570  ? 163.534 110.627 74.720  1.00 25.28 ?  570  PRO A CB   1 
ATOM   3564  C CG   . PRO A 1 570  ? 162.417 111.459 74.197  1.00 27.31 ?  570  PRO A CG   1 
ATOM   3565  C CD   . PRO A 1 570  ? 161.529 111.761 75.375  1.00 26.22 ?  570  PRO A CD   1 
ATOM   3566  N N    . SER A 1 571  ? 164.302 110.480 77.684  1.00 21.89 ?  571  SER A N    1 
ATOM   3567  C CA   . SER A 1 571  ? 165.258 110.270 78.761  1.00 24.29 ?  571  SER A CA   1 
ATOM   3568  C C    . SER A 1 571  ? 164.613 109.472 79.893  1.00 26.59 ?  571  SER A C    1 
ATOM   3569  O O    . SER A 1 571  ? 163.422 109.643 80.173  1.00 23.24 ?  571  SER A O    1 
ATOM   3570  C CB   . SER A 1 571  ? 165.769 111.609 79.292  1.00 20.85 ?  571  SER A CB   1 
ATOM   3571  O OG   . SER A 1 571  ? 166.494 111.438 80.497  1.00 21.61 ?  571  SER A OG   1 
ATOM   3572  N N    . PRO A 1 572  ? 165.364 108.574 80.541  1.00 24.05 ?  572  PRO A N    1 
ATOM   3573  C CA   . PRO A 1 572  ? 164.801 107.845 81.693  1.00 23.59 ?  572  PRO A CA   1 
ATOM   3574  C C    . PRO A 1 572  ? 164.395 108.749 82.846  1.00 23.62 ?  572  PRO A C    1 
ATOM   3575  O O    . PRO A 1 572  ? 163.401 108.467 83.527  1.00 22.90 ?  572  PRO A O    1 
ATOM   3576  C CB   . PRO A 1 572  ? 165.937 106.890 82.089  1.00 22.63 ?  572  PRO A CB   1 
ATOM   3577  C CG   . PRO A 1 572  ? 166.784 106.767 80.862  1.00 23.36 ?  572  PRO A CG   1 
ATOM   3578  C CD   . PRO A 1 572  ? 166.715 108.104 80.192  1.00 20.66 ?  572  PRO A CD   1 
ATOM   3579  N N    . ARG A 1 573  ? 165.142 109.831 83.085  1.00 22.62 ?  573  ARG A N    1 
ATOM   3580  C CA   . ARG A 1 573  ? 164.780 110.762 84.151  1.00 24.21 ?  573  ARG A CA   1 
ATOM   3581  C C    . ARG A 1 573  ? 163.480 111.490 83.832  1.00 24.57 ?  573  ARG A C    1 
ATOM   3582  O O    . ARG A 1 573  ? 162.631 111.673 84.713  1.00 20.02 ?  573  ARG A O    1 
ATOM   3583  C CB   . ARG A 1 573  ? 165.917 111.756 84.386  1.00 24.00 ?  573  ARG A CB   1 
ATOM   3584  C CG   . ARG A 1 573  ? 167.302 111.185 84.118  1.00 23.10 ?  573  ARG A CG   1 
ATOM   3585  C CD   . ARG A 1 573  ? 167.895 110.551 85.369  1.00 23.20 ?  573  ARG A CD   1 
ATOM   3586  N NE   . ARG A 1 573  ? 167.387 109.203 85.595  1.00 24.15 ?  573  ARG A NE   1 
ATOM   3587  C CZ   . ARG A 1 573  ? 167.852 108.114 84.997  1.00 26.38 ?  573  ARG A CZ   1 
ATOM   3588  N NH1  . ARG A 1 573  ? 168.847 108.175 84.128  1.00 27.10 ?  573  ARG A NH1  1 
ATOM   3589  N NH2  . ARG A 1 573  ? 167.304 106.935 85.278  1.00 22.63 ?  573  ARG A NH2  1 
ATOM   3590  N N    . GLU A 1 574  ? 163.303 111.903 82.573  1.00 30.53 ?  574  GLU A N    1 
ATOM   3591  C CA   . GLU A 1 574  ? 162.041 112.508 82.162  1.00 30.19 ?  574  GLU A CA   1 
ATOM   3592  C C    . GLU A 1 574  ? 160.890 111.519 82.288  1.00 30.57 ?  574  GLU A C    1 
ATOM   3593  O O    . GLU A 1 574  ? 159.792 111.885 82.725  1.00 25.06 ?  574  GLU A O    1 
ATOM   3594  C CB   . GLU A 1 574  ? 162.148 113.025 80.727  1.00 26.53 ?  574  GLU A CB   1 
ATOM   3595  C CG   . GLU A 1 574  ? 163.228 114.070 80.519  1.00 26.14 ?  574  GLU A CG   1 
ATOM   3596  C CD   . GLU A 1 574  ? 162.715 115.482 80.721  1.00 30.59 ?  574  GLU A CD   1 
ATOM   3597  O OE1  . GLU A 1 574  ? 161.513 115.719 80.475  1.00 32.06 ?  574  GLU A OE1  1 
ATOM   3598  O OE2  . GLU A 1 574  ? 163.512 116.354 81.124  1.00 32.60 ?  574  GLU A OE2  1 
ATOM   3599  N N    . PHE A 1 575  ? 161.126 110.259 81.908  1.00 30.25 ?  575  PHE A N    1 
ATOM   3600  C CA   . PHE A 1 575  ? 160.097 109.231 82.039  1.00 28.78 ?  575  PHE A CA   1 
ATOM   3601  C C    . PHE A 1 575  ? 159.703 109.030 83.496  1.00 28.45 ?  575  PHE A C    1 
ATOM   3602  O O    . PHE A 1 575  ? 158.515 108.899 83.811  1.00 27.17 ?  575  PHE A O    1 
ATOM   3603  C CB   . PHE A 1 575  ? 160.591 107.918 81.430  1.00 26.63 ?  575  PHE A CB   1 
ATOM   3604  C CG   . PHE A 1 575  ? 159.503 106.910 81.191  1.00 29.56 ?  575  PHE A CG   1 
ATOM   3605  C CD1  . PHE A 1 575  ? 158.721 106.969 80.049  1.00 30.09 ?  575  PHE A CD1  1 
ATOM   3606  C CD2  . PHE A 1 575  ? 159.268 105.898 82.108  1.00 29.09 ?  575  PHE A CD2  1 
ATOM   3607  C CE1  . PHE A 1 575  ? 157.721 106.040 79.828  1.00 28.38 ?  575  PHE A CE1  1 
ATOM   3608  C CE2  . PHE A 1 575  ? 158.269 104.965 81.892  1.00 28.75 ?  575  PHE A CE2  1 
ATOM   3609  C CZ   . PHE A 1 575  ? 157.495 105.037 80.751  1.00 26.47 ?  575  PHE A CZ   1 
ATOM   3610  N N    . ALA A 1 576  ? 160.687 109.024 84.400  1.00 25.80 ?  576  ALA A N    1 
ATOM   3611  C CA   . ALA A 1 576  ? 160.388 108.922 85.825  1.00 28.87 ?  576  ALA A CA   1 
ATOM   3612  C C    . ALA A 1 576  ? 159.619 110.142 86.318  1.00 28.07 ?  576  ALA A C    1 
ATOM   3613  O O    . ALA A 1 576  ? 158.738 110.023 87.179  1.00 24.49 ?  576  ALA A O    1 
ATOM   3614  C CB   . ALA A 1 576  ? 161.680 108.743 86.621  1.00 26.65 ?  576  ALA A CB   1 
ATOM   3615  N N    . ASP A 1 577  ? 159.938 111.324 85.783  1.00 24.76 ?  577  ASP A N    1 
ATOM   3616  C CA   . ASP A 1 577  ? 159.235 112.539 86.188  1.00 27.01 ?  577  ASP A CA   1 
ATOM   3617  C C    . ASP A 1 577  ? 157.759 112.483 85.803  1.00 27.65 ?  577  ASP A C    1 
ATOM   3618  O O    . ASP A 1 577  ? 156.878 112.751 86.632  1.00 28.32 ?  577  ASP A O    1 
ATOM   3619  C CB   . ASP A 1 577  ? 159.911 113.763 85.570  1.00 24.85 ?  577  ASP A CB   1 
ATOM   3620  C CG   . ASP A 1 577  ? 161.203 114.131 86.272  1.00 25.53 ?  577  ASP A CG   1 
ATOM   3621  O OD1  . ASP A 1 577  ? 161.428 113.644 87.400  1.00 23.51 ?  577  ASP A OD1  1 
ATOM   3622  O OD2  . ASP A 1 577  ? 161.995 114.907 85.697  1.00 29.47 ?  577  ASP A OD2  1 
ATOM   3623  N N    . MET A 1 578  ? 157.465 112.124 84.547  1.00 28.41 ?  578  MET A N    1 
ATOM   3624  C CA   . MET A 1 578  ? 156.057 112.003 84.159  1.00 28.47 ?  578  MET A CA   1 
ATOM   3625  C C    . MET A 1 578  ? 155.374 110.828 84.849  1.00 28.63 ?  578  MET A C    1 
ATOM   3626  O O    . MET A 1 578  ? 154.168 110.893 85.108  1.00 26.55 ?  578  MET A O    1 
ATOM   3627  C CB   . MET A 1 578  ? 155.878 111.896 82.640  1.00 26.46 ?  578  MET A CB   1 
ATOM   3628  C CG   . MET A 1 578  ? 156.962 112.520 81.795  1.00 28.95 ?  578  MET A CG   1 
ATOM   3629  S SD   . MET A 1 578  ? 156.460 112.854 80.095  1.00 37.42 ?  578  MET A SD   1 
ATOM   3630  C CE   . MET A 1 578  ? 155.561 111.358 79.705  1.00 28.17 ?  578  MET A CE   1 
ATOM   3631  N N    . MET A 1 579  ? 156.113 109.761 85.170  1.00 30.78 ?  579  MET A N    1 
ATOM   3632  C CA   . MET A 1 579  ? 155.528 108.660 85.930  1.00 29.98 ?  579  MET A CA   1 
ATOM   3633  C C    . MET A 1 579  ? 155.098 109.113 87.321  1.00 30.08 ?  579  MET A C    1 
ATOM   3634  O O    . MET A 1 579  ? 153.993 108.790 87.774  1.00 33.42 ?  579  MET A O    1 
ATOM   3635  C CB   . MET A 1 579  ? 156.526 107.505 86.024  1.00 28.45 ?  579  MET A CB   1 
ATOM   3636  C CG   . MET A 1 579  ? 156.102 106.385 86.959  1.00 31.30 ?  579  MET A CG   1 
ATOM   3637  S SD   . MET A 1 579  ? 154.631 105.515 86.386  1.00 38.79 ?  579  MET A SD   1 
ATOM   3638  C CE   . MET A 1 579  ? 154.121 104.690 87.891  1.00 29.51 ?  579  MET A CE   1 
ATOM   3639  N N    . GLU A 1 580  ? 155.956 109.876 88.005  1.00 23.24 ?  580  GLU A N    1 
ATOM   3640  C CA   . GLU A 1 580  ? 155.607 110.395 89.324  1.00 26.83 ?  580  GLU A CA   1 
ATOM   3641  C C    . GLU A 1 580  ? 154.444 111.376 89.245  1.00 25.45 ?  580  GLU A C    1 
ATOM   3642  O O    . GLU A 1 580  ? 153.553 111.363 90.106  1.00 24.04 ?  580  GLU A O    1 
ATOM   3643  C CB   . GLU A 1 580  ? 156.827 111.057 89.964  1.00 25.34 ?  580  GLU A CB   1 
ATOM   3644  C CG   . GLU A 1 580  ? 157.832 110.074 90.535  1.00 25.73 ?  580  GLU A CG   1 
ATOM   3645  C CD   . GLU A 1 580  ? 157.247 109.224 91.645  1.00 28.72 ?  580  GLU A CD   1 
ATOM   3646  O OE1  . GLU A 1 580  ? 156.535 109.779 92.508  1.00 21.76 ?  580  GLU A OE1  1 
ATOM   3647  O OE2  . GLU A 1 580  ? 157.496 108.000 91.651  1.00 33.68 ?  580  GLU A OE2  1 
ATOM   3648  N N    . GLU A 1 581  ? 154.436 112.233 88.218  1.00 23.71 ?  581  GLU A N    1 
ATOM   3649  C CA   . GLU A 1 581  ? 153.331 113.173 88.048  1.00 26.16 ?  581  GLU A CA   1 
ATOM   3650  C C    . GLU A 1 581  ? 152.013 112.443 87.812  1.00 28.83 ?  581  GLU A C    1 
ATOM   3651  O O    . GLU A 1 581  ? 150.984 112.802 88.398  1.00 29.86 ?  581  GLU A O    1 
ATOM   3652  C CB   . GLU A 1 581  ? 153.633 114.132 86.895  1.00 24.45 ?  581  GLU A CB   1 
ATOM   3653  C CG   . GLU A 1 581  ? 153.057 115.529 87.074  1.00 26.61 ?  581  GLU A CG   1 
ATOM   3654  C CD   . GLU A 1 581  ? 151.573 115.594 86.770  1.00 28.19 ?  581  GLU A CD   1 
ATOM   3655  O OE1  . GLU A 1 581  ? 151.103 114.802 85.926  1.00 24.72 ?  581  GLU A OE1  1 
ATOM   3656  O OE2  . GLU A 1 581  ? 150.877 116.437 87.374  1.00 28.27 ?  581  GLU A OE2  1 
ATOM   3657  N N    . ALA A 1 582  ? 152.029 111.405 86.970  1.00 25.70 ?  582  ALA A N    1 
ATOM   3658  C CA   . ALA A 1 582  ? 150.817 110.634 86.708  1.00 23.88 ?  582  ALA A CA   1 
ATOM   3659  C C    . ALA A 1 582  ? 150.350 109.886 87.950  1.00 21.52 ?  582  ALA A C    1 
ATOM   3660  O O    . ALA A 1 582  ? 149.144 109.787 88.202  1.00 24.00 ?  582  ALA A O    1 
ATOM   3661  C CB   . ALA A 1 582  ? 151.055 109.662 85.552  1.00 18.94 ?  582  ALA A CB   1 
ATOM   3662  N N    . ARG A 1 583  ? 151.289 109.348 88.736  1.00 15.87 ?  583  ARG A N    1 
ATOM   3663  C CA   . ARG A 1 583  ? 150.917 108.651 89.964  1.00 21.24 ?  583  ARG A CA   1 
ATOM   3664  C C    . ARG A 1 583  ? 150.267 109.598 90.968  1.00 22.99 ?  583  ARG A C    1 
ATOM   3665  O O    . ARG A 1 583  ? 149.235 109.266 91.573  1.00 27.32 ?  583  ARG A O    1 
ATOM   3666  C CB   . ARG A 1 583  ? 152.150 107.984 90.572  1.00 21.72 ?  583  ARG A CB   1 
ATOM   3667  C CG   . ARG A 1 583  ? 151.920 107.377 91.942  1.00 21.05 ?  583  ARG A CG   1 
ATOM   3668  C CD   . ARG A 1 583  ? 153.204 107.363 92.748  1.00 20.03 ?  583  ARG A CD   1 
ATOM   3669  N NE   . ARG A 1 583  ? 152.948 107.244 94.177  1.00 24.71 ?  583  ARG A NE   1 
ATOM   3670  C CZ   . ARG A 1 583  ? 153.776 107.666 95.122  1.00 24.23 ?  583  ARG A CZ   1 
ATOM   3671  N NH1  . ARG A 1 583  ? 154.925 108.250 94.824  1.00 22.08 ?  583  ARG A NH1  1 
ATOM   3672  N NH2  . ARG A 1 583  ? 153.445 107.497 96.399  1.00 24.09 ?  583  ARG A NH2  1 
ATOM   3673  N N    . LEU A 1 584  ? 150.850 110.787 91.151  1.00 18.63 ?  584  LEU A N    1 
ATOM   3674  C CA   . LEU A 1 584  ? 150.256 111.765 92.058  1.00 17.12 ?  584  LEU A CA   1 
ATOM   3675  C C    . LEU A 1 584  ? 148.897 112.236 91.551  1.00 18.10 ?  584  LEU A C    1 
ATOM   3676  O O    . LEU A 1 584  ? 147.970 112.443 92.345  1.00 21.82 ?  584  LEU A O    1 
ATOM   3677  C CB   . LEU A 1 584  ? 151.204 112.949 92.250  1.00 21.12 ?  584  LEU A CB   1 
ATOM   3678  C CG   . LEU A 1 584  ? 152.511 112.663 92.994  1.00 22.95 ?  584  LEU A CG   1 
ATOM   3679  C CD1  . LEU A 1 584  ? 153.209 113.959 93.377  1.00 19.34 ?  584  LEU A CD1  1 
ATOM   3680  C CD2  . LEU A 1 584  ? 152.261 111.803 94.225  1.00 20.53 ?  584  LEU A CD2  1 
ATOM   3681  N N    . ARG A 1 585  ? 148.757 112.397 90.231  1.00 18.81 ?  585  ARG A N    1 
ATOM   3682  C CA   . ARG A 1 585  ? 147.473 112.788 89.658  1.00 22.37 ?  585  ARG A CA   1 
ATOM   3683  C C    . ARG A 1 585  ? 146.410 111.720 89.892  1.00 22.31 ?  585  ARG A C    1 
ATOM   3684  O O    . ARG A 1 585  ? 145.262 112.041 90.222  1.00 22.61 ?  585  ARG A O    1 
ATOM   3685  C CB   . ARG A 1 585  ? 147.637 113.068 88.164  1.00 20.58 ?  585  ARG A CB   1 
ATOM   3686  C CG   . ARG A 1 585  ? 146.532 113.919 87.562  1.00 21.17 ?  585  ARG A CG   1 
ATOM   3687  C CD   . ARG A 1 585  ? 146.953 114.502 86.222  1.00 23.06 ?  585  ARG A CD   1 
ATOM   3688  N NE   . ARG A 1 585  ? 148.041 115.464 86.360  1.00 25.00 ?  585  ARG A NE   1 
ATOM   3689  C CZ   . ARG A 1 585  ? 147.958 116.742 86.015  1.00 25.27 ?  585  ARG A CZ   1 
ATOM   3690  N NH1  . ARG A 1 585  ? 146.849 117.249 85.501  1.00 21.94 ?  585  ARG A NH1  1 
ATOM   3691  N NH2  . ARG A 1 585  ? 149.014 117.531 86.192  1.00 22.27 ?  585  ARG A NH2  1 
ATOM   3692  N N    . MET A 1 586  ? 146.775 110.443 89.731  1.00 17.38 ?  586  MET A N    1 
ATOM   3693  C CA   . MET A 1 586  ? 145.825 109.365 89.992  1.00 15.68 ?  586  MET A CA   1 
ATOM   3694  C C    . MET A 1 586  ? 145.417 109.321 91.457  1.00 17.28 ?  586  MET A C    1 
ATOM   3695  O O    . MET A 1 586  ? 144.239 109.113 91.769  1.00 24.13 ?  586  MET A O    1 
ATOM   3696  C CB   . MET A 1 586  ? 146.403 108.013 89.578  1.00 14.67 ?  586  MET A CB   1 
ATOM   3697  C CG   . MET A 1 586  ? 146.139 107.623 88.139  1.00 17.70 ?  586  MET A CG   1 
ATOM   3698  S SD   . MET A 1 586  ? 146.715 105.950 87.795  1.00 20.73 ?  586  MET A SD   1 
ATOM   3699  C CE   . MET A 1 586  ? 146.297 105.122 89.329  1.00 19.86 ?  586  MET A CE   1 
ATOM   3700  N N    . LEU A 1 587  ? 146.376 109.494 92.371  1.00 13.25 ?  587  LEU A N    1 
ATOM   3701  C CA   . LEU A 1 587  ? 146.034 109.484 93.792  1.00 10.98 ?  587  LEU A CA   1 
ATOM   3702  C C    . LEU A 1 587  ? 145.111 110.646 94.148  1.00 9.76  ?  587  LEU A C    1 
ATOM   3703  O O    . LEU A 1 587  ? 144.142 110.475 94.904  1.00 19.75 ?  587  LEU A O    1 
ATOM   3704  C CB   . LEU A 1 587  ? 147.302 109.517 94.643  1.00 10.69 ?  587  LEU A CB   1 
ATOM   3705  C CG   . LEU A 1 587  ? 147.954 108.153 94.881  1.00 13.60 ?  587  LEU A CG   1 
ATOM   3706  C CD1  . LEU A 1 587  ? 149.470 108.270 94.908  1.00 14.82 ?  587  LEU A CD1  1 
ATOM   3707  C CD2  . LEU A 1 587  ? 147.434 107.515 96.160  1.00 14.96 ?  587  LEU A CD2  1 
ATOM   3708  N N    . LYS A 1 588  ? 145.383 111.831 93.592  1.00 4.37  ?  588  LYS A N    1 
ATOM   3709  C CA   . LYS A 1 588  ? 144.519 112.982 93.833  1.00 7.81  ?  588  LYS A CA   1 
ATOM   3710  C C    . LYS A 1 588  ? 143.116 112.750 93.285  1.00 11.24 ?  588  LYS A C    1 
ATOM   3711  O O    . LYS A 1 588  ? 142.122 113.055 93.956  1.00 13.38 ?  588  LYS A O    1 
ATOM   3712  C CB   . LYS A 1 588  ? 145.137 114.233 93.209  1.00 12.74 ?  588  LYS A CB   1 
ATOM   3713  C CG   . LYS A 1 588  ? 144.341 115.506 93.436  1.00 14.67 ?  588  LYS A CG   1 
ATOM   3714  C CD   . LYS A 1 588  ? 144.273 115.857 94.911  1.00 16.40 ?  588  LYS A CD   1 
ATOM   3715  C CE   . LYS A 1 588  ? 145.529 116.587 95.356  1.00 17.54 ?  588  LYS A CE   1 
ATOM   3716  N NZ   . LYS A 1 588  ? 145.571 117.984 94.844  1.00 19.79 ?  588  LYS A NZ   1 
ATOM   3717  N N    . ALA A 1 589  ? 143.015 112.195 92.073  1.00 12.38 ?  589  ALA A N    1 
ATOM   3718  C CA   . ALA A 1 589  ? 141.707 111.933 91.478  1.00 9.72  ?  589  ALA A CA   1 
ATOM   3719  C C    . ALA A 1 589  ? 140.934 110.884 92.269  1.00 14.35 ?  589  ALA A C    1 
ATOM   3720  O O    . ALA A 1 589  ? 139.712 110.995 92.426  1.00 16.55 ?  589  ALA A O    1 
ATOM   3721  C CB   . ALA A 1 589  ? 141.873 111.500 90.023  1.00 9.88  ?  589  ALA A CB   1 
ATOM   3722  N N    . GLU A 1 590  ? 141.627 109.860 92.774  1.00 14.13 ?  590  GLU A N    1 
ATOM   3723  C CA   . GLU A 1 590  ? 140.978 108.859 93.615  1.00 3.03  ?  590  GLU A CA   1 
ATOM   3724  C C    . GLU A 1 590  ? 140.445 109.475 94.902  1.00 1.29  ?  590  GLU A C    1 
ATOM   3725  O O    . GLU A 1 590  ? 139.336 109.147 95.343  1.00 6.35  ?  590  GLU A O    1 
ATOM   3726  C CB   . GLU A 1 590  ? 141.954 107.725 93.926  1.00 1.61  ?  590  GLU A CB   1 
ATOM   3727  C CG   . GLU A 1 590  ? 142.084 106.698 92.816  1.00 7.75  ?  590  GLU A CG   1 
ATOM   3728  C CD   . GLU A 1 590  ? 143.278 105.791 92.997  1.00 10.69 ?  590  GLU A CD   1 
ATOM   3729  O OE1  . GLU A 1 590  ? 143.874 105.813 94.091  1.00 15.61 ?  590  GLU A OE1  1 
ATOM   3730  O OE2  . GLU A 1 590  ? 143.620 105.054 92.048  1.00 9.40  ?  590  GLU A OE2  1 
ATOM   3731  N N    . LYS A 1 591  ? 141.224 110.367 95.524  1.00 2.46  ?  591  LYS A N    1 
ATOM   3732  C CA   . LYS A 1 591  ? 140.751 111.041 96.732  1.00 0.00  ?  591  LYS A CA   1 
ATOM   3733  C C    . LYS A 1 591  ? 139.530 111.911 96.442  1.00 2.72  ?  591  LYS A C    1 
ATOM   3734  O O    . LYS A 1 591  ? 138.577 111.946 97.237  1.00 8.17  ?  591  LYS A O    1 
ATOM   3735  C CB   . LYS A 1 591  ? 141.879 111.874 97.339  1.00 6.28  ?  591  LYS A CB   1 
ATOM   3736  C CG   . LYS A 1 591  ? 141.659 112.257 98.792  1.00 12.08 ?  591  LYS A CG   1 
ATOM   3737  C CD   . LYS A 1 591  ? 142.396 113.538 99.142  1.00 11.68 ?  591  LYS A CD   1 
ATOM   3738  C CE   . LYS A 1 591  ? 143.129 113.403 100.466 1.00 10.87 ?  591  LYS A CE   1 
ATOM   3739  N NZ   . LYS A 1 591  ? 144.309 112.503 100.347 1.00 8.95  ?  591  LYS A NZ   1 
ATOM   3740  N N    . ILE A 1 592  ? 139.541 112.615 95.304  1.00 4.60  ?  592  ILE A N    1 
ATOM   3741  C CA   . ILE A 1 592  ? 138.386 113.418 94.901  1.00 6.36  ?  592  ILE A CA   1 
ATOM   3742  C C    . ILE A 1 592  ? 137.163 112.530 94.704  1.00 7.69  ?  592  ILE A C    1 
ATOM   3743  O O    . ILE A 1 592  ? 136.048 112.882 95.111  1.00 9.65  ?  592  ILE A O    1 
ATOM   3744  C CB   . ILE A 1 592  ? 138.703 114.226 93.625  1.00 6.10  ?  592  ILE A CB   1 
ATOM   3745  C CG1  . ILE A 1 592  ? 139.857 115.212 93.842  1.00 12.11 ?  592  ILE A CG1  1 
ATOM   3746  C CG2  . ILE A 1 592  ? 137.470 114.971 93.132  1.00 4.70  ?  592  ILE A CG2  1 
ATOM   3747  C CD1  . ILE A 1 592  ? 139.868 115.907 95.182  1.00 11.96 ?  592  ILE A CD1  1 
ATOM   3748  N N    . SER A 1 593  ? 137.356 111.365 94.079  1.00 8.21  ?  593  SER A N    1 
ATOM   3749  C CA   . SER A 1 593  ? 136.248 110.441 93.851  1.00 4.74  ?  593  SER A CA   1 
ATOM   3750  C C    . SER A 1 593  ? 135.673 109.920 95.162  1.00 2.55  ?  593  SER A C    1 
ATOM   3751  O O    . SER A 1 593  ? 134.450 109.823 95.313  1.00 5.54  ?  593  SER A O    1 
ATOM   3752  C CB   . SER A 1 593  ? 136.709 109.279 92.974  1.00 4.14  ?  593  SER A CB   1 
ATOM   3753  O OG   . SER A 1 593  ? 135.658 108.354 92.769  1.00 6.12  ?  593  SER A OG   1 
ATOM   3754  N N    . TYR A 1 594  ? 136.538 109.576 96.121  1.00 5.83  ?  594  TYR A N    1 
ATOM   3755  C CA   . TYR A 1 594  ? 136.051 109.097 97.414  1.00 2.71  ?  594  TYR A CA   1 
ATOM   3756  C C    . TYR A 1 594  ? 135.272 110.181 98.152  1.00 5.40  ?  594  TYR A C    1 
ATOM   3757  O O    . TYR A 1 594  ? 134.211 109.910 98.734  1.00 3.92  ?  594  TYR A O    1 
ATOM   3758  C CB   . TYR A 1 594  ? 137.212 108.595 98.276  1.00 0.13  ?  594  TYR A CB   1 
ATOM   3759  C CG   . TYR A 1 594  ? 138.048 107.505 97.643  1.00 0.00  ?  594  TYR A CG   1 
ATOM   3760  C CD1  . TYR A 1 594  ? 137.493 106.611 96.738  1.00 1.22  ?  594  TYR A CD1  1 
ATOM   3761  C CD2  . TYR A 1 594  ? 139.392 107.367 97.956  1.00 3.16  ?  594  TYR A CD2  1 
ATOM   3762  C CE1  . TYR A 1 594  ? 138.253 105.617 96.159  1.00 0.78  ?  594  TYR A CE1  1 
ATOM   3763  C CE2  . TYR A 1 594  ? 140.161 106.375 97.381  1.00 2.98  ?  594  TYR A CE2  1 
ATOM   3764  C CZ   . TYR A 1 594  ? 139.585 105.503 96.484  1.00 0.00  ?  594  TYR A CZ   1 
ATOM   3765  O OH   . TYR A 1 594  ? 140.345 104.512 95.909  1.00 0.00  ?  594  TYR A OH   1 
ATOM   3766  N N    . TRP A 1 595  ? 135.772 111.421 98.128  1.00 10.88 ?  595  TRP A N    1 
ATOM   3767  C CA   . TRP A 1 595  ? 135.043 112.505 98.781  1.00 7.92  ?  595  TRP A CA   1 
ATOM   3768  C C    . TRP A 1 595  ? 133.700 112.763 98.106  1.00 4.29  ?  595  TRP A C    1 
ATOM   3769  O O    . TRP A 1 595  ? 132.683 112.946 98.787  1.00 9.99  ?  595  TRP A O    1 
ATOM   3770  C CB   . TRP A 1 595  ? 135.892 113.775 98.810  1.00 8.76  ?  595  TRP A CB   1 
ATOM   3771  C CG   . TRP A 1 595  ? 136.780 113.841 100.010 1.00 11.25 ?  595  TRP A CG   1 
ATOM   3772  C CD1  . TRP A 1 595  ? 138.136 113.706 100.037 1.00 8.76  ?  595  TRP A CD1  1 
ATOM   3773  C CD2  . TRP A 1 595  ? 136.369 114.042 101.367 1.00 12.25 ?  595  TRP A CD2  1 
ATOM   3774  N NE1  . TRP A 1 595  ? 138.597 113.817 101.326 1.00 9.56  ?  595  TRP A NE1  1 
ATOM   3775  C CE2  . TRP A 1 595  ? 137.531 114.023 102.162 1.00 11.97 ?  595  TRP A CE2  1 
ATOM   3776  C CE3  . TRP A 1 595  ? 135.131 114.239 101.987 1.00 12.08 ?  595  TRP A CE3  1 
ATOM   3777  C CZ2  . TRP A 1 595  ? 137.493 114.194 103.544 1.00 10.76 ?  595  TRP A CZ2  1 
ATOM   3778  C CZ3  . TRP A 1 595  ? 135.094 114.408 103.358 1.00 10.27 ?  595  TRP A CZ3  1 
ATOM   3779  C CH2  . TRP A 1 595  ? 136.268 114.385 104.122 1.00 10.92 ?  595  TRP A CH2  1 
ATOM   3780  N N    . LYS A 1 596  ? 133.672 112.749 96.770  1.00 2.79  ?  596  LYS A N    1 
ATOM   3781  C CA   . LYS A 1 596  ? 132.421 112.944 96.044  1.00 4.23  ?  596  LYS A CA   1 
ATOM   3782  C C    . LYS A 1 596  ? 131.427 111.824 96.322  1.00 5.51  ?  596  LYS A C    1 
ATOM   3783  O O    . LYS A 1 596  ? 130.216 112.069 96.360  1.00 9.18  ?  596  LYS A O    1 
ATOM   3784  C CB   . LYS A 1 596  ? 132.697 113.042 94.545  1.00 7.87  ?  596  LYS A CB   1 
ATOM   3785  C CG   . LYS A 1 596  ? 131.886 114.105 93.825  1.00 8.68  ?  596  LYS A CG   1 
ATOM   3786  C CD   . LYS A 1 596  ? 132.258 114.189 92.350  1.00 8.44  ?  596  LYS A CD   1 
ATOM   3787  C CE   . LYS A 1 596  ? 133.763 114.206 92.142  1.00 7.42  ?  596  LYS A CE   1 
ATOM   3788  N NZ   . LYS A 1 596  ? 134.121 114.037 90.707  1.00 13.38 ?  596  LYS A NZ   1 
ATOM   3789  N N    . GLN A 1 597  ? 131.915 110.595 96.510  1.00 11.51 ?  597  GLN A N    1 
ATOM   3790  C CA   . GLN A 1 597  ? 131.033 109.508 96.923  1.00 4.19  ?  597  GLN A CA   1 
ATOM   3791  C C    . GLN A 1 597  ? 130.487 109.746 98.325  1.00 3.38  ?  597  GLN A C    1 
ATOM   3792  O O    . GLN A 1 597  ? 129.338 109.393 98.613  1.00 4.49  ?  597  GLN A O    1 
ATOM   3793  C CB   . GLN A 1 597  ? 131.768 108.169 96.856  1.00 4.29  ?  597  GLN A CB   1 
ATOM   3794  C CG   . GLN A 1 597  ? 131.963 107.629 95.451  1.00 7.27  ?  597  GLN A CG   1 
ATOM   3795  C CD   . GLN A 1 597  ? 132.525 106.222 95.441  1.00 2.10  ?  597  GLN A CD   1 
ATOM   3796  O OE1  . GLN A 1 597  ? 131.871 105.279 95.883  1.00 6.32  ?  597  GLN A OE1  1 
ATOM   3797  N NE2  . GLN A 1 597  ? 133.742 106.074 94.935  1.00 2.83  ?  597  GLN A NE2  1 
ATOM   3798  N N    . PHE A 1 598  ? 131.301 110.325 99.215  1.00 8.28  ?  598  PHE A N    1 
ATOM   3799  C CA   . PHE A 1 598  ? 130.815 110.624 100.561 1.00 5.08  ?  598  PHE A CA   1 
ATOM   3800  C C    . PHE A 1 598  ? 129.699 111.664 100.534 1.00 12.35 ?  598  PHE A C    1 
ATOM   3801  O O    . PHE A 1 598  ? 128.665 111.492 101.189 1.00 14.26 ?  598  PHE A O    1 
ATOM   3802  C CB   . PHE A 1 598  ? 131.948 111.117 101.459 1.00 5.12  ?  598  PHE A CB   1 
ATOM   3803  C CG   . PHE A 1 598  ? 131.492 111.497 102.849 1.00 12.70 ?  598  PHE A CG   1 
ATOM   3804  C CD1  . PHE A 1 598  ? 130.621 110.677 103.555 1.00 16.80 ?  598  PHE A CD1  1 
ATOM   3805  C CD2  . PHE A 1 598  ? 131.890 112.692 103.427 1.00 18.02 ?  598  PHE A CD2  1 
ATOM   3806  C CE1  . PHE A 1 598  ? 130.189 111.022 104.821 1.00 15.13 ?  598  PHE A CE1  1 
ATOM   3807  C CE2  . PHE A 1 598  ? 131.458 113.043 104.696 1.00 17.05 ?  598  PHE A CE2  1 
ATOM   3808  C CZ   . PHE A 1 598  ? 130.606 112.207 105.391 1.00 12.68 ?  598  PHE A CZ   1 
ATOM   3809  N N    . GLU A 1 599  ? 129.899 112.765 99.795  1.00 17.76 ?  599  GLU A N    1 
ATOM   3810  C CA   . GLU A 1 599  ? 128.914 113.849 99.812  1.00 11.39 ?  599  GLU A CA   1 
ATOM   3811  C C    . GLU A 1 599  ? 127.563 113.435 99.241  1.00 11.55 ?  599  GLU A C    1 
ATOM   3812  O O    . GLU A 1 599  ? 126.546 114.046 99.588  1.00 19.91 ?  599  GLU A O    1 
ATOM   3813  C CB   . GLU A 1 599  ? 129.422 115.079 99.051  1.00 11.17 ?  599  GLU A CB   1 
ATOM   3814  C CG   . GLU A 1 599  ? 130.880 115.426 99.269  1.00 15.85 ?  599  GLU A CG   1 
ATOM   3815  C CD   . GLU A 1 599  ? 131.140 116.064 100.618 1.00 17.98 ?  599  GLU A CD   1 
ATOM   3816  O OE1  . GLU A 1 599  ? 132.306 116.053 101.067 1.00 11.70 ?  599  GLU A OE1  1 
ATOM   3817  O OE2  . GLU A 1 599  ? 130.183 116.586 101.226 1.00 21.19 ?  599  GLU A OE2  1 
ATOM   3818  N N    . HIS A 1 600  ? 127.522 112.421 98.384  1.00 6.42  ?  600  HIS A N    1 
ATOM   3819  C CA   . HIS A 1 600  ? 126.267 111.924 97.839  1.00 7.63  ?  600  HIS A CA   1 
ATOM   3820  C C    . HIS A 1 600  ? 125.593 110.897 98.738  1.00 14.86 ?  600  HIS A C    1 
ATOM   3821  O O    . HIS A 1 600  ? 124.505 110.420 98.399  1.00 17.65 ?  600  HIS A O    1 
ATOM   3822  C CB   . HIS A 1 600  ? 126.496 111.317 96.452  1.00 14.06 ?  600  HIS A CB   1 
ATOM   3823  C CG   . HIS A 1 600  ? 125.441 111.678 95.454  1.00 17.86 ?  600  HIS A CG   1 
ATOM   3824  N ND1  . HIS A 1 600  ? 125.242 112.969 95.013  1.00 18.63 ?  600  HIS A ND1  1 
ATOM   3825  C CD2  . HIS A 1 600  ? 124.525 110.916 94.811  1.00 17.38 ?  600  HIS A CD2  1 
ATOM   3826  C CE1  . HIS A 1 600  ? 124.249 112.986 94.142  1.00 17.82 ?  600  HIS A CE1  1 
ATOM   3827  N NE2  . HIS A 1 600  ? 123.797 111.754 94.002  1.00 18.48 ?  600  HIS A NE2  1 
ATOM   3828  N N    . GLY A 1 601  ? 126.203 110.546 99.866  1.00 18.36 ?  601  GLY A N    1 
ATOM   3829  C CA   . GLY A 1 601  ? 125.636 109.557 100.757 1.00 15.04 ?  601  GLY A CA   1 
ATOM   3830  C C    . GLY A 1 601  ? 125.841 108.120 100.340 1.00 15.39 ?  601  GLY A C    1 
ATOM   3831  O O    . GLY A 1 601  ? 125.191 107.231 100.901 1.00 22.07 ?  601  GLY A O    1 
ATOM   3832  N N    . MET A 1 602  ? 126.720 107.860 99.374  1.00 12.01 ?  602  MET A N    1 
ATOM   3833  C CA   . MET A 1 602  ? 127.011 106.503 98.933  1.00 11.92 ?  602  MET A CA   1 
ATOM   3834  C C    . MET A 1 602  ? 128.110 105.836 99.747  1.00 14.81 ?  602  MET A C    1 
ATOM   3835  O O    . MET A 1 602  ? 128.357 104.640 99.563  1.00 17.40 ?  602  MET A O    1 
ATOM   3836  C CB   . MET A 1 602  ? 127.407 106.504 97.453  1.00 13.77 ?  602  MET A CB   1 
ATOM   3837  C CG   . MET A 1 602  ? 126.308 106.049 96.510  1.00 16.78 ?  602  MET A CG   1 
ATOM   3838  S SD   . MET A 1 602  ? 126.958 105.569 94.899  1.00 31.81 ?  602  MET A SD   1 
ATOM   3839  C CE   . MET A 1 602  ? 127.992 106.982 94.520  1.00 18.69 ?  602  MET A CE   1 
ATOM   3840  N N    . LEU A 1 603  ? 128.764 106.572 100.640 1.00 12.63 ?  603  LEU A N    1 
ATOM   3841  C CA   . LEU A 1 603  ? 129.810 106.035 101.494 1.00 10.74 ?  603  LEU A CA   1 
ATOM   3842  C C    . LEU A 1 603  ? 129.554 106.463 102.929 1.00 14.88 ?  603  LEU A C    1 
ATOM   3843  O O    . LEU A 1 603  ? 129.042 107.556 103.186 1.00 14.23 ?  603  LEU A O    1 
ATOM   3844  C CB   . LEU A 1 603  ? 131.204 106.514 101.060 1.00 4.95  ?  603  LEU A CB   1 
ATOM   3845  C CG   . LEU A 1 603  ? 132.059 105.575 100.211 1.00 0.10  ?  603  LEU A CG   1 
ATOM   3846  C CD1  . LEU A 1 603  ? 133.452 106.154 100.015 1.00 1.20  ?  603  LEU A CD1  1 
ATOM   3847  C CD2  . LEU A 1 603  ? 132.132 104.202 100.847 1.00 7.16  ?  603  LEU A CD2  1 
ATOM   3848  N N    . ALA A 1 604  ? 129.907 105.586 103.863 1.00 15.52 ?  604  ALA A N    1 
ATOM   3849  C CA   . ALA A 1 604  ? 129.873 105.935 105.271 1.00 9.62  ?  604  ALA A CA   1 
ATOM   3850  C C    . ALA A 1 604  ? 131.185 106.606 105.671 1.00 13.87 ?  604  ALA A C    1 
ATOM   3851  O O    . ALA A 1 604  ? 132.187 106.550 104.954 1.00 13.29 ?  604  ALA A O    1 
ATOM   3852  C CB   . ALA A 1 604  ? 129.610 104.698 106.125 1.00 12.51 ?  604  ALA A CB   1 
ATOM   3853  N N    . ARG A 1 605  ? 131.167 107.258 106.837 1.00 17.04 ?  605  ARG A N    1 
ATOM   3854  C CA   . ARG A 1 605  ? 132.321 108.044 107.264 1.00 16.19 ?  605  ARG A CA   1 
ATOM   3855  C C    . ARG A 1 605  ? 133.538 107.167 107.539 1.00 18.06 ?  605  ARG A C    1 
ATOM   3856  O O    . ARG A 1 605  ? 134.664 107.542 107.195 1.00 22.37 ?  605  ARG A O    1 
ATOM   3857  C CB   . ARG A 1 605  ? 131.963 108.875 108.496 1.00 20.33 ?  605  ARG A CB   1 
ATOM   3858  C CG   . ARG A 1 605  ? 133.037 109.876 108.892 1.00 19.13 ?  605  ARG A CG   1 
ATOM   3859  C CD   . ARG A 1 605  ? 132.555 110.811 109.988 1.00 20.04 ?  605  ARG A CD   1 
ATOM   3860  N NE   . ARG A 1 605  ? 131.307 111.475 109.628 1.00 20.21 ?  605  ARG A NE   1 
ATOM   3861  C CZ   . ARG A 1 605  ? 131.228 112.681 109.083 1.00 22.33 ?  605  ARG A CZ   1 
ATOM   3862  N NH1  . ARG A 1 605  ? 132.312 113.395 108.823 1.00 21.23 ?  605  ARG A NH1  1 
ATOM   3863  N NH2  . ARG A 1 605  ? 130.032 113.185 108.793 1.00 20.64 ?  605  ARG A NH2  1 
ATOM   3864  N N    . GLU A 1 606  ? 133.336 105.998 108.155 1.00 16.57 ?  606  GLU A N    1 
ATOM   3865  C CA   . GLU A 1 606  ? 134.468 105.134 108.481 1.00 17.28 ?  606  GLU A CA   1 
ATOM   3866  C C    . GLU A 1 606  ? 135.129 104.574 107.226 1.00 17.20 ?  606  GLU A C    1 
ATOM   3867  O O    . GLU A 1 606  ? 136.362 104.512 107.143 1.00 15.53 ?  606  GLU A O    1 
ATOM   3868  C CB   . GLU A 1 606  ? 134.032 103.998 109.412 1.00 17.52 ?  606  GLU A CB   1 
ATOM   3869  C CG   . GLU A 1 606  ? 133.017 104.374 110.492 1.00 23.23 ?  606  GLU A CG   1 
ATOM   3870  C CD   . GLU A 1 606  ? 131.574 104.304 110.024 1.00 23.66 ?  606  GLU A CD   1 
ATOM   3871  O OE1  . GLU A 1 606  ? 131.344 104.151 108.808 1.00 19.26 ?  606  GLU A OE1  1 
ATOM   3872  O OE2  . GLU A 1 606  ? 130.669 104.400 110.879 1.00 23.22 ?  606  GLU A OE2  1 
ATOM   3873  N N    . ALA A 1 607  ? 134.328 104.163 106.239 1.00 14.85 ?  607  ALA A N    1 
ATOM   3874  C CA   . ALA A 1 607  ? 134.884 103.650 104.990 1.00 10.22 ?  607  ALA A CA   1 
ATOM   3875  C C    . ALA A 1 607  ? 135.639 104.732 104.229 1.00 15.99 ?  607  ALA A C    1 
ATOM   3876  O O    . ALA A 1 607  ? 136.719 104.474 103.681 1.00 17.79 ?  607  ALA A O    1 
ATOM   3877  C CB   . ALA A 1 607  ? 133.771 103.068 104.123 1.00 7.41  ?  607  ALA A CB   1 
ATOM   3878  N N    . LEU A 1 608  ? 135.083 105.947 104.180 1.00 17.92 ?  608  LEU A N    1 
ATOM   3879  C CA   . LEU A 1 608  ? 135.771 107.056 103.526 1.00 13.93 ?  608  LEU A CA   1 
ATOM   3880  C C    . LEU A 1 608  ? 137.080 107.377 104.232 1.00 11.22 ?  608  LEU A C    1 
ATOM   3881  O O    . LEU A 1 608  ? 138.100 107.630 103.579 1.00 8.34  ?  608  LEU A O    1 
ATOM   3882  C CB   . LEU A 1 608  ? 134.871 108.291 103.496 1.00 10.90 ?  608  LEU A CB   1 
ATOM   3883  C CG   . LEU A 1 608  ? 135.591 109.636 103.350 1.00 10.84 ?  608  LEU A CG   1 
ATOM   3884  C CD1  . LEU A 1 608  ? 135.944 109.910 101.893 1.00 13.10 ?  608  LEU A CD1  1 
ATOM   3885  C CD2  . LEU A 1 608  ? 134.789 110.774 103.947 1.00 9.05  ?  608  LEU A CD2  1 
ATOM   3886  N N    . ARG A 1 609  ? 137.066 107.366 105.569 1.00 15.04 ?  609  ARG A N    1 
ATOM   3887  C CA   . ARG A 1 609  ? 138.282 107.618 106.334 1.00 15.44 ?  609  ARG A CA   1 
ATOM   3888  C C    . ARG A 1 609  ? 139.337 106.555 106.062 1.00 13.58 ?  609  ARG A C    1 
ATOM   3889  O O    . ARG A 1 609  ? 140.518 106.876 105.898 1.00 15.68 ?  609  ARG A O    1 
ATOM   3890  C CB   . ARG A 1 609  ? 137.957 107.681 107.826 1.00 16.32 ?  609  ARG A CB   1 
ATOM   3891  C CG   . ARG A 1 609  ? 137.403 109.018 108.287 1.00 16.52 ?  609  ARG A CG   1 
ATOM   3892  C CD   . ARG A 1 609  ? 137.488 109.161 109.799 1.00 17.71 ?  609  ARG A CD   1 
ATOM   3893  N NE   . ARG A 1 609  ? 137.087 107.941 110.488 1.00 20.96 ?  609  ARG A NE   1 
ATOM   3894  C CZ   . ARG A 1 609  ? 136.261 107.902 111.525 1.00 24.85 ?  609  ARG A CZ   1 
ATOM   3895  N NH1  . ARG A 1 609  ? 135.730 109.005 112.027 1.00 22.85 ?  609  ARG A NH1  1 
ATOM   3896  N NH2  . ARG A 1 609  ? 135.960 106.728 112.071 1.00 23.63 ?  609  ARG A NH2  1 
ATOM   3897  N N    . LEU A 1 610  ? 138.926 105.285 105.990 1.00 11.06 ?  610  LEU A N    1 
ATOM   3898  C CA   . LEU A 1 610  ? 139.865 104.213 105.665 1.00 13.05 ?  610  LEU A CA   1 
ATOM   3899  C C    . LEU A 1 610  ? 140.454 104.395 104.270 1.00 15.44 ?  610  LEU A C    1 
ATOM   3900  O O    . LEU A 1 610  ? 141.667 104.234 104.071 1.00 13.94 ?  610  LEU A O    1 
ATOM   3901  C CB   . LEU A 1 610  ? 139.166 102.857 105.770 1.00 12.56 ?  610  LEU A CB   1 
ATOM   3902  C CG   . LEU A 1 610  ? 139.440 101.979 106.992 1.00 14.67 ?  610  LEU A CG   1 
ATOM   3903  C CD1  . LEU A 1 610  ? 138.749 102.533 108.224 1.00 15.15 ?  610  LEU A CD1  1 
ATOM   3904  C CD2  . LEU A 1 610  ? 138.993 100.552 106.723 1.00 14.39 ?  610  LEU A CD2  1 
ATOM   3905  N N    . LEU A 1 611  ? 139.611 104.746 103.295 1.00 15.18 ?  611  LEU A N    1 
ATOM   3906  C CA   . LEU A 1 611  ? 140.087 104.890 101.923 1.00 10.65 ?  611  LEU A CA   1 
ATOM   3907  C C    . LEU A 1 611  ? 141.044 106.069 101.783 1.00 13.82 ?  611  LEU A C    1 
ATOM   3908  O O    . LEU A 1 611  ? 142.089 105.950 101.131 1.00 18.29 ?  611  LEU A O    1 
ATOM   3909  C CB   . LEU A 1 611  ? 138.901 105.038 100.971 1.00 8.93  ?  611  LEU A CB   1 
ATOM   3910  C CG   . LEU A 1 611  ? 138.087 103.769 100.707 1.00 0.79  ?  611  LEU A CG   1 
ATOM   3911  C CD1  . LEU A 1 611  ? 136.656 104.117 100.343 1.00 2.00  ?  611  LEU A CD1  1 
ATOM   3912  C CD2  . LEU A 1 611  ? 138.733 102.930 99.619  1.00 1.51  ?  611  LEU A CD2  1 
ATOM   3913  N N    . VAL A 1 612  ? 140.726 107.206 102.408 1.00 14.39 ?  612  VAL A N    1 
ATOM   3914  C CA   . VAL A 1 612  ? 141.614 108.359 102.290 1.00 12.58 ?  612  VAL A CA   1 
ATOM   3915  C C    . VAL A 1 612  ? 142.871 108.165 103.131 1.00 14.64 ?  612  VAL A C    1 
ATOM   3916  O O    . VAL A 1 612  ? 143.930 108.706 102.797 1.00 17.44 ?  612  VAL A O    1 
ATOM   3917  C CB   . VAL A 1 612  ? 140.883 109.669 102.647 1.00 9.77  ?  612  VAL A CB   1 
ATOM   3918  C CG1  . VAL A 1 612  ? 139.661 109.851 101.760 1.00 14.09 ?  612  VAL A CG1  1 
ATOM   3919  C CG2  . VAL A 1 612  ? 140.505 109.713 104.119 1.00 14.30 ?  612  VAL A CG2  1 
ATOM   3920  N N    . GLN A 1 613  ? 142.794 107.381 104.211 1.00 15.02 ?  613  GLN A N    1 
ATOM   3921  C CA   . GLN A 1 613  ? 143.997 107.038 104.960 1.00 11.90 ?  613  GLN A CA   1 
ATOM   3922  C C    . GLN A 1 613  ? 144.935 106.181 104.120 1.00 15.35 ?  613  GLN A C    1 
ATOM   3923  O O    . GLN A 1 613  ? 146.149 106.415 104.104 1.00 16.09 ?  613  GLN A O    1 
ATOM   3924  C CB   . GLN A 1 613  ? 143.614 106.325 106.258 1.00 12.37 ?  613  GLN A CB   1 
ATOM   3925  C CG   . GLN A 1 613  ? 144.666 105.375 106.805 1.00 14.62 ?  613  GLN A CG   1 
ATOM   3926  C CD   . GLN A 1 613  ? 144.086 104.356 107.768 1.00 19.08 ?  613  GLN A CD   1 
ATOM   3927  O OE1  . GLN A 1 613  ? 143.025 104.572 108.355 1.00 18.34 ?  613  GLN A OE1  1 
ATOM   3928  N NE2  . GLN A 1 613  ? 144.784 103.239 107.938 1.00 17.89 ?  613  GLN A NE2  1 
ATOM   3929  N N    . HIS A 1 614  ? 144.385 105.200 103.397 1.00 17.92 ?  614  HIS A N    1 
ATOM   3930  C CA   . HIS A 1 614  ? 145.209 104.406 102.489 1.00 20.19 ?  614  HIS A CA   1 
ATOM   3931  C C    . HIS A 1 614  ? 145.785 105.266 101.369 1.00 15.55 ?  614  HIS A C    1 
ATOM   3932  O O    . HIS A 1 614  ? 146.943 105.086 100.972 1.00 19.11 ?  614  HIS A O    1 
ATOM   3933  C CB   . HIS A 1 614  ? 144.395 103.249 101.912 1.00 18.21 ?  614  HIS A CB   1 
ATOM   3934  C CG   . HIS A 1 614  ? 143.985 102.234 102.931 1.00 18.06 ?  614  HIS A CG   1 
ATOM   3935  N ND1  . HIS A 1 614  ? 142.697 102.139 103.410 1.00 18.15 ?  614  HIS A ND1  1 
ATOM   3936  C CD2  . HIS A 1 614  ? 144.694 101.269 103.562 1.00 16.71 ?  614  HIS A CD2  1 
ATOM   3937  C CE1  . HIS A 1 614  ? 142.630 101.159 104.294 1.00 18.99 ?  614  HIS A CE1  1 
ATOM   3938  N NE2  . HIS A 1 614  ? 143.828 100.615 104.404 1.00 19.54 ?  614  HIS A NE2  1 
ATOM   3939  N N    . ALA A 1 615  ? 144.991 106.209 100.851 1.00 8.89  ?  615  ALA A N    1 
ATOM   3940  C CA   . ALA A 1 615  ? 145.479 107.093 99.796  1.00 18.17 ?  615  ALA A CA   1 
ATOM   3941  C C    . ALA A 1 615  ? 146.624 107.974 100.286 1.00 24.44 ?  615  ALA A C    1 
ATOM   3942  O O    . ALA A 1 615  ? 147.639 108.126 99.596  1.00 19.02 ?  615  ALA A O    1 
ATOM   3943  C CB   . ALA A 1 615  ? 144.334 107.950 99.258  1.00 15.67 ?  615  ALA A CB   1 
ATOM   3944  N N    . GLU A 1 616  ? 146.488 108.547 101.485 1.00 20.28 ?  616  GLU A N    1 
ATOM   3945  C CA   . GLU A 1 616  ? 147.553 109.375 102.041 1.00 14.67 ?  616  GLU A CA   1 
ATOM   3946  C C    . GLU A 1 616  ? 148.790 108.552 102.381 1.00 14.49 ?  616  GLU A C    1 
ATOM   3947  O O    . GLU A 1 616  ? 149.915 109.046 102.242 1.00 16.88 ?  616  GLU A O    1 
ATOM   3948  C CB   . GLU A 1 616  ? 147.051 110.115 103.281 1.00 13.76 ?  616  GLU A CB   1 
ATOM   3949  C CG   . GLU A 1 616  ? 146.115 111.271 102.976 1.00 14.99 ?  616  GLU A CG   1 
ATOM   3950  C CD   . GLU A 1 616  ? 145.228 111.628 104.153 1.00 16.03 ?  616  GLU A CD   1 
ATOM   3951  O OE1  . GLU A 1 616  ? 145.343 110.968 105.206 1.00 16.37 ?  616  GLU A OE1  1 
ATOM   3952  O OE2  . GLU A 1 616  ? 144.417 112.569 104.025 1.00 16.17 ?  616  GLU A OE2  1 
ATOM   3953  N N    . VAL A 1 617  ? 148.604 107.310 102.835 1.00 13.71 ?  617  VAL A N    1 
ATOM   3954  C CA   . VAL A 1 617  ? 149.738 106.432 103.109 1.00 18.48 ?  617  VAL A CA   1 
ATOM   3955  C C    . VAL A 1 617  ? 150.489 106.115 101.821 1.00 20.15 ?  617  VAL A C    1 
ATOM   3956  O O    . VAL A 1 617  ? 151.726 106.120 101.787 1.00 21.31 ?  617  VAL A O    1 
ATOM   3957  C CB   . VAL A 1 617  ? 149.256 105.157 103.829 1.00 22.43 ?  617  VAL A CB   1 
ATOM   3958  C CG1  . VAL A 1 617  ? 150.223 103.998 103.619 1.00 17.28 ?  617  VAL A CG1  1 
ATOM   3959  C CG2  . VAL A 1 617  ? 149.063 105.430 105.313 1.00 20.84 ?  617  VAL A CG2  1 
ATOM   3960  N N    . ALA A 1 618  ? 149.758 105.847 100.739 1.00 24.06 ?  618  ALA A N    1 
ATOM   3961  C CA   . ALA A 1 618  ? 150.402 105.551 99.466  1.00 22.95 ?  618  ALA A CA   1 
ATOM   3962  C C    . ALA A 1 618  ? 150.982 106.787 98.788  1.00 18.27 ?  618  ALA A C    1 
ATOM   3963  O O    . ALA A 1 618  ? 151.866 106.647 97.936  1.00 19.89 ?  618  ALA A O    1 
ATOM   3964  C CB   . ALA A 1 618  ? 149.411 104.869 98.522  1.00 20.36 ?  618  ALA A CB   1 
ATOM   3965  N N    . ALA A 1 619  ? 150.503 107.985 99.136  1.00 15.00 ?  619  ALA A N    1 
ATOM   3966  C CA   . ALA A 1 619  ? 150.934 109.191 98.433  1.00 23.06 ?  619  ALA A CA   1 
ATOM   3967  C C    . ALA A 1 619  ? 152.383 109.552 98.747  1.00 22.44 ?  619  ALA A C    1 
ATOM   3968  O O    . ALA A 1 619  ? 153.176 109.814 97.835  1.00 18.21 ?  619  ALA A O    1 
ATOM   3969  C CB   . ALA A 1 619  ? 150.005 110.355 98.779  1.00 21.18 ?  619  ALA A CB   1 
ATOM   3970  N N    . ASP A 1 620  ? 152.753 109.574 100.030 1.00 22.10 ?  620  ASP A N    1 
ATOM   3971  C CA   . ASP A 1 620  ? 154.073 110.072 100.405 1.00 22.34 ?  620  ASP A CA   1 
ATOM   3972  C C    . ASP A 1 620  ? 155.192 109.077 100.122 1.00 22.78 ?  620  ASP A C    1 
ATOM   3973  O O    . ASP A 1 620  ? 156.367 109.457 100.174 1.00 25.60 ?  620  ASP A O    1 
ATOM   3974  C CB   . ASP A 1 620  ? 154.092 110.482 101.884 1.00 21.10 ?  620  ASP A CB   1 
ATOM   3975  C CG   . ASP A 1 620  ? 153.870 109.314 102.833 1.00 23.78 ?  620  ASP A CG   1 
ATOM   3976  O OD1  . ASP A 1 620  ? 153.478 108.220 102.381 1.00 25.02 ?  620  ASP A OD1  1 
ATOM   3977  O OD2  . ASP A 1 620  ? 154.093 109.495 104.048 1.00 23.31 ?  620  ASP A OD2  1 
ATOM   3978  N N    . GLU A 1 621  ? 154.859 107.824 99.826  1.00 24.01 ?  621  GLU A N    1 
ATOM   3979  C CA   . GLU A 1 621  ? 155.854 106.825 99.476  1.00 26.25 ?  621  GLU A CA   1 
ATOM   3980  C C    . GLU A 1 621  ? 156.447 107.157 98.106  1.00 27.11 ?  621  GLU A C    1 
ATOM   3981  O O    . GLU A 1 621  ? 155.878 107.927 97.329  1.00 27.01 ?  621  GLU A O    1 
ATOM   3982  C CB   . GLU A 1 621  ? 155.218 105.430 99.490  1.00 26.21 ?  621  GLU A CB   1 
ATOM   3983  C CG   . GLU A 1 621  ? 156.120 104.275 99.940  1.00 25.56 ?  621  GLU A CG   1 
ATOM   3984  C CD   . GLU A 1 621  ? 157.087 103.800 98.876  1.00 29.65 ?  621  GLU A CD   1 
ATOM   3985  O OE1  . GLU A 1 621  ? 156.684 103.723 97.698  1.00 28.10 ?  621  GLU A OE1  1 
ATOM   3986  O OE2  . GLU A 1 621  ? 158.250 103.501 99.218  1.00 29.81 ?  621  GLU A OE2  1 
ATOM   3987  N N    . LYS A 1 622  ? 157.627 106.592 97.833  1.00 26.23 ?  622  LYS A N    1 
ATOM   3988  C CA   . LYS A 1 622  ? 158.313 106.866 96.572  1.00 29.20 ?  622  LYS A CA   1 
ATOM   3989  C C    . LYS A 1 622  ? 157.499 106.381 95.376  1.00 29.93 ?  622  LYS A C    1 
ATOM   3990  O O    . LYS A 1 622  ? 157.247 107.141 94.434  1.00 25.94 ?  622  LYS A O    1 
ATOM   3991  C CB   . LYS A 1 622  ? 159.700 106.221 96.579  1.00 26.70 ?  622  LYS A CB   1 
ATOM   3992  C CG   . LYS A 1 622  ? 160.425 106.271 95.240  1.00 24.77 ?  622  LYS A CG   1 
ATOM   3993  C CD   . LYS A 1 622  ? 160.655 107.702 94.768  1.00 25.23 ?  622  LYS A CD   1 
ATOM   3994  C CE   . LYS A 1 622  ? 161.588 108.457 95.700  1.00 30.60 ?  622  LYS A CE   1 
ATOM   3995  N NZ   . LYS A 1 622  ? 161.735 109.882 95.291  1.00 31.57 ?  622  LYS A NZ   1 
ATOM   3996  N N    . ASP A 1 623  ? 157.074 105.117 95.396  1.00 26.10 ?  623  ASP A N    1 
ATOM   3997  C CA   . ASP A 1 623  ? 156.265 104.572 94.306  1.00 26.32 ?  623  ASP A CA   1 
ATOM   3998  C C    . ASP A 1 623  ? 155.406 103.449 94.881  1.00 27.18 ?  623  ASP A C    1 
ATOM   3999  O O    . ASP A 1 623  ? 155.883 102.321 95.042  1.00 26.14 ?  623  ASP A O    1 
ATOM   4000  C CB   . ASP A 1 623  ? 157.142 104.077 93.163  1.00 25.03 ?  623  ASP A CB   1 
ATOM   4001  C CG   . ASP A 1 623  ? 156.380 103.947 91.859  1.00 26.52 ?  623  ASP A CG   1 
ATOM   4002  O OD1  . ASP A 1 623  ? 155.214 104.391 91.802  1.00 28.02 ?  623  ASP A OD1  1 
ATOM   4003  O OD2  . ASP A 1 623  ? 156.949 103.403 90.889  1.00 25.24 ?  623  ASP A OD2  1 
ATOM   4004  N N    . GLN A 1 624  ? 154.148 103.763 95.180  1.00 27.38 ?  624  GLN A N    1 
ATOM   4005  C CA   . GLN A 1 624  ? 153.219 102.775 95.725  1.00 27.15 ?  624  GLN A CA   1 
ATOM   4006  C C    . GLN A 1 624  ? 151.802 103.262 95.481  1.00 27.88 ?  624  GLN A C    1 
ATOM   4007  O O    . GLN A 1 624  ? 151.440 104.356 95.925  1.00 28.97 ?  624  GLN A O    1 
ATOM   4008  C CB   . GLN A 1 624  ? 153.464 102.553 97.219  1.00 23.76 ?  624  GLN A CB   1 
ATOM   4009  C CG   . GLN A 1 624  ? 152.363 101.769 97.916  1.00 22.82 ?  624  GLN A CG   1 
ATOM   4010  C CD   . GLN A 1 624  ? 152.354 101.978 99.418  1.00 26.37 ?  624  GLN A CD   1 
ATOM   4011  O OE1  . GLN A 1 624  ? 153.185 102.707 99.960  1.00 25.74 ?  624  GLN A OE1  1 
ATOM   4012  N NE2  . GLN A 1 624  ? 151.411 101.338 100.099 1.00 28.55 ?  624  GLN A NE2  1 
ATOM   4013  N N    . PHE A 1 625  ? 151.007 102.461 94.778  1.00 25.74 ?  625  PHE A N    1 
ATOM   4014  C CA   . PHE A 1 625  ? 149.609 102.775 94.533  1.00 23.78 ?  625  PHE A CA   1 
ATOM   4015  C C    . PHE A 1 625  ? 148.758 102.214 95.671  1.00 27.00 ?  625  PHE A C    1 
ATOM   4016  O O    . PHE A 1 625  ? 149.270 101.793 96.712  1.00 27.60 ?  625  PHE A O    1 
ATOM   4017  C CB   . PHE A 1 625  ? 149.171 102.227 93.177  1.00 22.36 ?  625  PHE A CB   1 
ATOM   4018  C CG   . PHE A 1 625  ? 149.868 102.864 92.012  1.00 23.96 ?  625  PHE A CG   1 
ATOM   4019  C CD1  . PHE A 1 625  ? 149.366 104.019 91.436  1.00 23.82 ?  625  PHE A CD1  1 
ATOM   4020  C CD2  . PHE A 1 625  ? 151.021 102.304 91.487  1.00 26.21 ?  625  PHE A CD2  1 
ATOM   4021  C CE1  . PHE A 1 625  ? 150.004 104.607 90.362  1.00 25.88 ?  625  PHE A CE1  1 
ATOM   4022  C CE2  . PHE A 1 625  ? 151.664 102.888 90.412  1.00 27.42 ?  625  PHE A CE2  1 
ATOM   4023  C CZ   . PHE A 1 625  ? 151.155 104.040 89.850  1.00 27.55 ?  625  PHE A CZ   1 
ATOM   4024  N N    . ILE A 1 626  ? 147.441 102.209 95.486  1.00 23.03 ?  626  ILE A N    1 
ATOM   4025  C CA   . ILE A 1 626  ? 146.531 101.612 96.458  1.00 19.92 ?  626  ILE A CA   1 
ATOM   4026  C C    . ILE A 1 626  ? 146.646 100.098 96.336  1.00 20.36 ?  626  ILE A C    1 
ATOM   4027  O O    . ILE A 1 626  ? 146.143 99.503  95.380  1.00 21.42 ?  626  ILE A O    1 
ATOM   4028  C CB   . ILE A 1 626  ? 145.088 102.077 96.241  1.00 15.43 ?  626  ILE A CB   1 
ATOM   4029  C CG1  . ILE A 1 626  ? 145.038 103.595 96.078  1.00 14.56 ?  626  ILE A CG1  1 
ATOM   4030  C CG2  . ILE A 1 626  ? 144.203 101.616 97.389  1.00 17.02 ?  626  ILE A CG2  1 
ATOM   4031  C CD1  . ILE A 1 626  ? 145.098 104.354 97.378  1.00 17.03 ?  626  ILE A CD1  1 
ATOM   4032  N N    . LEU A 1 627  ? 147.309 99.472  97.302  1.00 23.07 ?  627  LEU A N    1 
ATOM   4033  C CA   . LEU A 1 627  ? 147.479 98.028  97.283  1.00 24.41 ?  627  LEU A CA   1 
ATOM   4034  C C    . LEU A 1 627  ? 146.257 97.345  97.883  1.00 19.69 ?  627  LEU A C    1 
ATOM   4035  O O    . LEU A 1 627  ? 145.687 97.813  98.873  1.00 19.39 ?  627  LEU A O    1 
ATOM   4036  C CB   . LEU A 1 627  ? 148.741 97.626  98.046  1.00 24.50 ?  627  LEU A CB   1 
ATOM   4037  C CG   . LEU A 1 627  ? 149.209 96.177  97.898  1.00 24.74 ?  627  LEU A CG   1 
ATOM   4038  C CD1  . LEU A 1 627  ? 149.775 95.936  96.507  1.00 22.49 ?  627  LEU A CD1  1 
ATOM   4039  C CD2  . LEU A 1 627  ? 150.235 95.835  98.965  1.00 22.06 ?  627  LEU A CD2  1 
ATOM   4040  N N    . VAL A 1 628  ? 145.854 96.232  97.264  1.00 15.01 ?  628  VAL A N    1 
ATOM   4041  C CA   . VAL A 1 628  ? 144.686 95.489  97.718  1.00 16.31 ?  628  VAL A CA   1 
ATOM   4042  C C    . VAL A 1 628  ? 144.917 94.864  99.089  1.00 17.69 ?  628  VAL A C    1 
ATOM   4043  O O    . VAL A 1 628  ? 143.958 94.649  99.839  1.00 18.06 ?  628  VAL A O    1 
ATOM   4044  C CB   . VAL A 1 628  ? 144.319 94.425  96.663  1.00 20.43 ?  628  VAL A CB   1 
ATOM   4045  C CG1  . VAL A 1 628  ? 142.993 93.746  96.989  1.00 20.06 ?  628  VAL A CG1  1 
ATOM   4046  C CG2  . VAL A 1 628  ? 144.276 95.050  95.278  1.00 19.33 ?  628  VAL A CG2  1 
ATOM   4047  N N    . ASP A 1 629  ? 146.174 94.585  99.446  1.00 19.40 ?  629  ASP A N    1 
ATOM   4048  C CA   . ASP A 1 629  ? 146.464 93.926  100.716 1.00 21.19 ?  629  ASP A CA   1 
ATOM   4049  C C    . ASP A 1 629  ? 146.134 94.811  101.913 1.00 22.98 ?  629  ASP A C    1 
ATOM   4050  O O    . ASP A 1 629  ? 145.720 94.298  102.959 1.00 24.90 ?  629  ASP A O    1 
ATOM   4051  C CB   . ASP A 1 629  ? 147.930 93.499  100.759 1.00 23.69 ?  629  ASP A CB   1 
ATOM   4052  C CG   . ASP A 1 629  ? 148.227 92.346  99.820  1.00 24.70 ?  629  ASP A CG   1 
ATOM   4053  O OD1  . ASP A 1 629  ? 148.157 92.545  98.589  1.00 24.57 ?  629  ASP A OD1  1 
ATOM   4054  O OD2  . ASP A 1 629  ? 148.529 91.239  100.313 1.00 26.39 ?  629  ASP A OD2  1 
ATOM   4055  N N    . ASP A 1 630  ? 146.320 96.128  101.793 1.00 20.22 ?  630  ASP A N    1 
ATOM   4056  C CA   . ASP A 1 630  ? 145.924 97.019  102.879 1.00 18.65 ?  630  ASP A CA   1 
ATOM   4057  C C    . ASP A 1 630  ? 144.408 97.081  103.015 1.00 15.48 ?  630  ASP A C    1 
ATOM   4058  O O    . ASP A 1 630  ? 143.879 97.113  104.132 1.00 19.96 ?  630  ASP A O    1 
ATOM   4059  C CB   . ASP A 1 630  ? 146.495 98.420  102.662 1.00 21.64 ?  630  ASP A CB   1 
ATOM   4060  C CG   . ASP A 1 630  ? 147.885 98.402  102.061 1.00 24.23 ?  630  ASP A CG   1 
ATOM   4061  O OD1  . ASP A 1 630  ? 148.826 97.936  102.737 1.00 26.08 ?  630  ASP A OD1  1 
ATOM   4062  O OD2  . ASP A 1 630  ? 148.039 98.879  100.919 1.00 17.79 ?  630  ASP A OD2  1 
ATOM   4063  N N    . LEU A 1 631  ? 143.692 97.100  101.887 1.00 15.61 ?  631  LEU A N    1 
ATOM   4064  C CA   . LEU A 1 631  ? 142.236 97.164  101.919 1.00 16.16 ?  631  LEU A CA   1 
ATOM   4065  C C    . LEU A 1 631  ? 141.609 95.851  102.365 1.00 15.70 ?  631  LEU A C    1 
ATOM   4066  O O    . LEU A 1 631  ? 140.471 95.855  102.846 1.00 17.67 ?  631  LEU A O    1 
ATOM   4067  C CB   . LEU A 1 631  ? 141.695 97.541  100.540 1.00 15.17 ?  631  LEU A CB   1 
ATOM   4068  C CG   . LEU A 1 631  ? 142.070 98.907  99.969  1.00 8.95  ?  631  LEU A CG   1 
ATOM   4069  C CD1  . LEU A 1 631  ? 141.965 98.871  98.457  1.00 12.69 ?  631  LEU A CD1  1 
ATOM   4070  C CD2  . LEU A 1 631  ? 141.190 100.001 100.545 1.00 7.61  ?  631  LEU A CD2  1 
ATOM   4071  N N    . LYS A 1 632  ? 142.327 94.735  102.216 1.00 14.56 ?  632  LYS A N    1 
ATOM   4072  C CA   . LYS A 1 632  ? 141.777 93.419  102.519 1.00 11.79 ?  632  LYS A CA   1 
ATOM   4073  C C    . LYS A 1 632  ? 141.463 93.241  103.998 1.00 9.59  ?  632  LYS A C    1 
ATOM   4074  O O    . LYS A 1 632  ? 140.703 92.336  104.353 1.00 10.96 ?  632  LYS A O    1 
ATOM   4075  C CB   . LYS A 1 632  ? 142.753 92.339  102.050 1.00 13.78 ?  632  LYS A CB   1 
ATOM   4076  C CG   . LYS A 1 632  ? 142.103 91.018  101.683 1.00 11.64 ?  632  LYS A CG   1 
ATOM   4077  C CD   . LYS A 1 632  ? 143.125 89.892  101.658 1.00 14.43 ?  632  LYS A CD   1 
ATOM   4078  C CE   . LYS A 1 632  ? 144.273 90.202  100.708 1.00 18.13 ?  632  LYS A CE   1 
ATOM   4079  N NZ   . LYS A 1 632  ? 143.793 90.535  99.337  1.00 17.96 ?  632  LYS A NZ   1 
ATOM   4080  N N    . LYS A 1 633  ? 142.011 94.093  104.863 1.00 19.29 ?  633  LYS A N    1 
ATOM   4081  C CA   . LYS A 1 633  ? 141.755 94.046  106.296 1.00 21.79 ?  633  LYS A CA   1 
ATOM   4082  C C    . LYS A 1 633  ? 140.462 94.755  106.688 1.00 19.31 ?  633  LYS A C    1 
ATOM   4083  O O    . LYS A 1 633  ? 140.315 95.161  107.847 1.00 18.23 ?  633  LYS A O    1 
ATOM   4084  C CB   . LYS A 1 633  ? 142.939 94.644  107.059 1.00 15.27 ?  633  LYS A CB   1 
ATOM   4085  C CG   . LYS A 1 633  ? 144.301 94.215  106.526 1.00 16.51 ?  633  LYS A CG   1 
ATOM   4086  C CD   . LYS A 1 633  ? 144.503 92.711  106.641 1.00 18.38 ?  633  LYS A CD   1 
ATOM   4087  C CE   . LYS A 1 633  ? 145.407 92.187  105.534 1.00 18.99 ?  633  LYS A CE   1 
ATOM   4088  N NZ   . LYS A 1 633  ? 146.670 92.968  105.420 1.00 18.63 ?  633  LYS A NZ   1 
ATOM   4089  N N    . SER A 1 634  ? 139.539 94.942  105.745 1.00 16.31 ?  634  SER A N    1 
ATOM   4090  C CA   . SER A 1 634  ? 138.229 95.509  106.029 1.00 12.93 ?  634  SER A CA   1 
ATOM   4091  C C    . SER A 1 634  ? 137.103 94.490  105.972 1.00 15.44 ?  634  SER A C    1 
ATOM   4092  O O    . SER A 1 634  ? 136.133 94.623  106.720 1.00 23.86 ?  634  SER A O    1 
ATOM   4093  C CB   . SER A 1 634  ? 137.917 96.647  105.049 1.00 15.83 ?  634  SER A CB   1 
ATOM   4094  O OG   . SER A 1 634  ? 139.088 97.375  104.727 1.00 14.74 ?  634  SER A OG   1 
ATOM   4095  N N    . TRP A 1 635  ? 137.203 93.481  105.108 1.00 12.90 ?  635  TRP A N    1 
ATOM   4096  C CA   . TRP A 1 635  ? 136.191 92.439  105.021 1.00 9.08  ?  635  TRP A CA   1 
ATOM   4097  C C    . TRP A 1 635  ? 136.704 91.065  105.429 1.00 14.10 ?  635  TRP A C    1 
ATOM   4098  O O    . TRP A 1 635  ? 135.917 90.112  105.456 1.00 23.08 ?  635  TRP A O    1 
ATOM   4099  C CB   . TRP A 1 635  ? 135.609 92.372  103.601 1.00 10.37 ?  635  TRP A CB   1 
ATOM   4100  C CG   . TRP A 1 635  ? 136.618 92.124  102.520 1.00 13.24 ?  635  TRP A CG   1 
ATOM   4101  C CD1  . TRP A 1 635  ? 137.168 90.926  102.168 1.00 11.10 ?  635  TRP A CD1  1 
ATOM   4102  C CD2  . TRP A 1 635  ? 137.179 93.099  101.635 1.00 12.71 ?  635  TRP A CD2  1 
ATOM   4103  N NE1  . TRP A 1 635  ? 138.045 91.097  101.125 1.00 7.86  ?  635  TRP A NE1  1 
ATOM   4104  C CE2  . TRP A 1 635  ? 138.069 92.422  100.778 1.00 9.73  ?  635  TRP A CE2  1 
ATOM   4105  C CE3  . TRP A 1 635  ? 137.019 94.479  101.486 1.00 7.61  ?  635  TRP A CE3  1 
ATOM   4106  C CZ2  . TRP A 1 635  ? 138.796 93.079  99.789  1.00 11.01 ?  635  TRP A CZ2  1 
ATOM   4107  C CZ3  . TRP A 1 635  ? 137.741 95.129  100.505 1.00 4.93  ?  635  TRP A CZ3  1 
ATOM   4108  C CH2  . TRP A 1 635  ? 138.619 94.429  99.669  1.00 6.27  ?  635  TRP A CH2  1 
ATOM   4109  N N    . GLN A 1 636  ? 137.992 90.932  105.745 1.00 13.80 ?  636  GLN A N    1 
ATOM   4110  C CA   . GLN A 1 636  ? 138.546 89.675  106.230 1.00 17.21 ?  636  GLN A CA   1 
ATOM   4111  C C    . GLN A 1 636  ? 138.388 89.500  107.733 1.00 19.96 ?  636  GLN A C    1 
ATOM   4112  O O    . GLN A 1 636  ? 138.703 88.425  108.254 1.00 19.19 ?  636  GLN A O    1 
ATOM   4113  C CB   . GLN A 1 636  ? 140.032 89.574  105.869 1.00 14.49 ?  636  GLN A CB   1 
ATOM   4114  C CG   . GLN A 1 636  ? 140.484 88.187  105.449 1.00 12.36 ?  636  GLN A CG   1 
ATOM   4115  C CD   . GLN A 1 636  ? 140.035 87.828  104.047 1.00 16.36 ?  636  GLN A CD   1 
ATOM   4116  O OE1  . GLN A 1 636  ? 140.622 88.276  103.063 1.00 16.60 ?  636  GLN A OE1  1 
ATOM   4117  N NE2  . GLN A 1 636  ? 138.989 87.016  103.949 1.00 17.04 ?  636  GLN A NE2  1 
ATOM   4118  N N    . ILE A 1 637  ? 137.903 90.527  108.439 1.00 20.18 ?  637  ILE A N    1 
ATOM   4119  C CA   . ILE A 1 637  ? 137.786 90.481  109.896 1.00 23.76 ?  637  ILE A CA   1 
ATOM   4120  C C    . ILE A 1 637  ? 136.598 89.653  110.361 1.00 22.59 ?  637  ILE A C    1 
ATOM   4121  O O    . ILE A 1 637  ? 136.375 89.523  111.571 1.00 22.92 ?  637  ILE A O    1 
ATOM   4122  C CB   . ILE A 1 637  ? 137.744 91.931  110.425 1.00 20.84 ?  637  ILE A CB   1 
ATOM   4123  C CG1  . ILE A 1 637  ? 138.634 92.827  109.562 1.00 17.95 ?  637  ILE A CG1  1 
ATOM   4124  C CG2  . ILE A 1 637  ? 138.223 92.026  111.868 1.00 15.91 ?  637  ILE A CG2  1 
ATOM   4125  C CD1  . ILE A 1 637  ? 140.126 92.600  109.785 1.00 20.00 ?  637  ILE A CD1  1 
ATOM   4126  N N    . LYS A 1 638  ? 135.821 89.082  109.438 1.00 16.40 ?  638  LYS A N    1 
ATOM   4127  C CA   . LYS A 1 638  ? 134.811 88.110  109.844 1.00 19.49 ?  638  LYS A CA   1 
ATOM   4128  C C    . LYS A 1 638  ? 135.458 86.839  110.382 1.00 24.43 ?  638  LYS A C    1 
ATOM   4129  O O    . LYS A 1 638  ? 134.988 86.267  111.374 1.00 29.69 ?  638  LYS A O    1 
ATOM   4130  C CB   . LYS A 1 638  ? 133.880 87.791  108.674 1.00 19.30 ?  638  LYS A CB   1 
ATOM   4131  C CG   . LYS A 1 638  ? 132.754 86.838  109.037 1.00 22.52 ?  638  LYS A CG   1 
ATOM   4132  C CD   . LYS A 1 638  ? 131.855 86.546  107.858 1.00 22.85 ?  638  LYS A CD   1 
ATOM   4133  C CE   . LYS A 1 638  ? 132.593 85.735  106.803 1.00 22.54 ?  638  LYS A CE   1 
ATOM   4134  N NZ   . LYS A 1 638  ? 132.961 84.384  107.305 1.00 17.97 ?  638  LYS A NZ   1 
ATOM   4135  N N    . GLY A 1 639  ? 136.559 86.405  109.771 1.00 18.08 ?  639  GLY A N    1 
ATOM   4136  C CA   . GLY A 1 639  ? 137.182 85.142  110.121 1.00 18.60 ?  639  GLY A CA   1 
ATOM   4137  C C    . GLY A 1 639  ? 137.888 85.122  111.462 1.00 21.15 ?  639  GLY A C    1 
ATOM   4138  O O    . GLY A 1 639  ? 139.085 84.832  111.541 1.00 22.35 ?  639  GLY A O    1 
ATOM   4139  N N    . ILE A 1 640  ? 137.150 85.442  112.526 1.00 23.73 ?  640  ILE A N    1 
ATOM   4140  C CA   . ILE A 1 640  ? 137.632 85.349  113.900 1.00 21.43 ?  640  ILE A CA   1 
ATOM   4141  C C    . ILE A 1 640  ? 136.572 84.552  114.655 1.00 22.74 ?  640  ILE A C    1 
ATOM   4142  O O    . ILE A 1 640  ? 135.667 83.976  114.041 1.00 24.17 ?  640  ILE A O    1 
ATOM   4143  C CB   . ILE A 1 640  ? 137.885 86.729  114.545 1.00 21.18 ?  640  ILE A CB   1 
ATOM   4144  C CG1  . ILE A 1 640  ? 138.435 87.732  113.540 1.00 19.38 ?  640  ILE A CG1  1 
ATOM   4145  C CG2  . ILE A 1 640  ? 138.981 86.645  115.602 1.00 19.18 ?  640  ILE A CG2  1 
ATOM   4146  C CD1  . ILE A 1 640  ? 138.401 89.147  114.060 1.00 20.61 ?  640  ILE A CD1  1 
ATOM   4147  N N    . TYR A 1 641  ? 136.691 84.496  115.982 1.00 21.95 ?  641  TYR A N    1 
ATOM   4148  C CA   . TYR A 1 641  ? 135.772 83.728  116.823 1.00 23.69 ?  641  TYR A CA   1 
ATOM   4149  C C    . TYR A 1 641  ? 134.267 83.985  116.657 1.00 26.56 ?  641  TYR A C    1 
ATOM   4150  O O    . TYR A 1 641  ? 133.496 83.092  117.045 1.00 23.01 ?  641  TYR A O    1 
ATOM   4151  C CB   . TYR A 1 641  ? 136.136 83.904  118.311 1.00 20.96 ?  641  TYR A CB   1 
ATOM   4152  C CG   . TYR A 1 641  ? 136.041 85.308  118.890 1.00 22.53 ?  641  TYR A CG   1 
ATOM   4153  C CD1  . TYR A 1 641  ? 136.858 86.342  118.443 1.00 22.26 ?  641  TYR A CD1  1 
ATOM   4154  C CD2  . TYR A 1 641  ? 135.104 85.602  119.873 1.00 22.23 ?  641  TYR A CD2  1 
ATOM   4155  C CE1  . TYR A 1 641  ? 136.757 87.616  118.969 1.00 22.97 ?  641  TYR A CE1  1 
ATOM   4156  C CE2  . TYR A 1 641  ? 134.994 86.874  120.405 1.00 23.68 ?  641  TYR A CE2  1 
ATOM   4157  C CZ   . TYR A 1 641  ? 135.823 87.876  119.949 1.00 25.05 ?  641  TYR A CZ   1 
ATOM   4158  O OH   . TYR A 1 641  ? 135.716 89.143  120.477 1.00 27.38 ?  641  TYR A OH   1 
ATOM   4159  N N    . PRO A 1 642  ? 133.751 85.168  116.167 1.00 25.32 ?  642  PRO A N    1 
ATOM   4160  C CA   . PRO A 1 642  ? 132.292 85.264  115.965 1.00 21.32 ?  642  PRO A CA   1 
ATOM   4161  C C    . PRO A 1 642  ? 131.691 84.217  115.035 1.00 24.30 ?  642  PRO A C    1 
ATOM   4162  O O    . PRO A 1 642  ? 130.603 83.702  115.314 1.00 25.23 ?  642  PRO A O    1 
ATOM   4163  C CB   . PRO A 1 642  ? 132.104 86.676  115.386 1.00 18.36 ?  642  PRO A CB   1 
ATOM   4164  C CG   . PRO A 1 642  ? 133.467 87.197  115.109 1.00 19.14 ?  642  PRO A CG   1 
ATOM   4165  C CD   . PRO A 1 642  ? 134.340 86.518  116.094 1.00 21.44 ?  642  PRO A CD   1 
ATOM   4166  N N    . TRP A 1 643  ? 132.384 83.884  113.943 1.00 19.52 ?  643  TRP A N    1 
ATOM   4167  C CA   . TRP A 1 643  ? 131.869 82.871  113.025 1.00 18.64 ?  643  TRP A CA   1 
ATOM   4168  C C    . TRP A 1 643  ? 131.800 81.503  113.692 1.00 21.02 ?  643  TRP A C    1 
ATOM   4169  O O    . TRP A 1 643  ? 130.802 80.784  113.554 1.00 18.92 ?  643  TRP A O    1 
ATOM   4170  C CB   . TRP A 1 643  ? 132.738 82.808  111.770 1.00 21.00 ?  643  TRP A CB   1 
ATOM   4171  C CG   . TRP A 1 643  ? 132.615 81.511  111.027 1.00 25.44 ?  643  TRP A CG   1 
ATOM   4172  C CD1  . TRP A 1 643  ? 131.508 81.032  110.388 1.00 22.85 ?  643  TRP A CD1  1 
ATOM   4173  C CD2  . TRP A 1 643  ? 133.637 80.521  110.855 1.00 27.06 ?  643  TRP A CD2  1 
ATOM   4174  N NE1  . TRP A 1 643  ? 131.779 79.809  109.825 1.00 23.03 ?  643  TRP A NE1  1 
ATOM   4175  C CE2  . TRP A 1 643  ? 133.079 79.472  110.097 1.00 24.11 ?  643  TRP A CE2  1 
ATOM   4176  C CE3  . TRP A 1 643  ? 134.970 80.421  111.267 1.00 24.19 ?  643  TRP A CE3  1 
ATOM   4177  C CZ2  . TRP A 1 643  ? 133.807 78.338  109.743 1.00 21.72 ?  643  TRP A CZ2  1 
ATOM   4178  C CZ3  . TRP A 1 643  ? 135.691 79.294  110.914 1.00 23.43 ?  643  TRP A CZ3  1 
ATOM   4179  C CH2  . TRP A 1 643  ? 135.108 78.269  110.159 1.00 21.58 ?  643  TRP A CH2  1 
ATOM   4180  N N    . LEU A 1 644  ? 132.852 81.134  114.428 1.00 23.59 ?  644  LEU A N    1 
ATOM   4181  C CA   . LEU A 1 644  ? 132.861 79.856  115.133 1.00 24.26 ?  644  LEU A CA   1 
ATOM   4182  C C    . LEU A 1 644  ? 131.794 79.818  116.220 1.00 22.28 ?  644  LEU A C    1 
ATOM   4183  O O    . LEU A 1 644  ? 131.145 78.787  116.422 1.00 20.11 ?  644  LEU A O    1 
ATOM   4184  C CB   . LEU A 1 644  ? 134.246 79.599  115.724 1.00 22.82 ?  644  LEU A CB   1 
ATOM   4185  C CG   . LEU A 1 644  ? 134.382 78.420  116.690 1.00 20.65 ?  644  LEU A CG   1 
ATOM   4186  C CD1  . LEU A 1 644  ? 134.875 77.183  115.956 1.00 19.70 ?  644  LEU A CD1  1 
ATOM   4187  C CD2  . LEU A 1 644  ? 135.308 78.772  117.843 1.00 19.75 ?  644  LEU A CD2  1 
ATOM   4188  N N    . LYS A 1 645  ? 131.601 80.934  116.927 1.00 20.62 ?  645  LYS A N    1 
ATOM   4189  C CA   . LYS A 1 645  ? 130.579 81.001  117.967 1.00 18.69 ?  645  LYS A CA   1 
ATOM   4190  C C    . LYS A 1 645  ? 129.181 80.849  117.380 1.00 21.92 ?  645  LYS A C    1 
ATOM   4191  O O    . LYS A 1 645  ? 128.338 80.133  117.938 1.00 23.11 ?  645  LYS A O    1 
ATOM   4192  C CB   . LYS A 1 645  ? 130.715 82.319  118.730 1.00 19.08 ?  645  LYS A CB   1 
ATOM   4193  C CG   . LYS A 1 645  ? 129.746 82.511  119.883 1.00 20.31 ?  645  LYS A CG   1 
ATOM   4194  C CD   . LYS A 1 645  ? 129.671 83.982  120.275 1.00 23.05 ?  645  LYS A CD   1 
ATOM   4195  C CE   . LYS A 1 645  ? 128.433 84.290  121.101 1.00 21.74 ?  645  LYS A CE   1 
ATOM   4196  N NZ   . LYS A 1 645  ? 128.552 85.581  121.834 1.00 23.39 ?  645  LYS A NZ   1 
ATOM   4197  N N    . ARG A 1 646  ? 128.922 81.503  116.244 1.00 21.92 ?  646  ARG A N    1 
ATOM   4198  C CA   . ARG A 1 646  ? 127.634 81.353  115.574 1.00 21.30 ?  646  ARG A CA   1 
ATOM   4199  C C    . ARG A 1 646  ? 127.428 79.924  115.085 1.00 21.83 ?  646  ARG A C    1 
ATOM   4200  O O    . ARG A 1 646  ? 126.327 79.373  115.201 1.00 21.22 ?  646  ARG A O    1 
ATOM   4201  C CB   . ARG A 1 646  ? 127.532 82.339  114.410 1.00 20.04 ?  646  ARG A CB   1 
ATOM   4202  C CG   . ARG A 1 646  ? 126.237 82.243  113.624 1.00 19.43 ?  646  ARG A CG   1 
ATOM   4203  C CD   . ARG A 1 646  ? 126.082 83.424  112.685 1.00 18.28 ?  646  ARG A CD   1 
ATOM   4204  N NE   . ARG A 1 646  ? 127.064 83.406  111.608 1.00 22.41 ?  646  ARG A NE   1 
ATOM   4205  C CZ   . ARG A 1 646  ? 126.852 82.883  110.409 1.00 20.54 ?  646  ARG A CZ   1 
ATOM   4206  N NH1  . ARG A 1 646  ? 125.692 82.332  110.091 1.00 20.68 ?  646  ARG A NH1  1 
ATOM   4207  N NH2  . ARG A 1 646  ? 127.827 82.916  109.505 1.00 18.98 ?  646  ARG A NH2  1 
ATOM   4208  N N    . LYS A 1 647  ? 128.482 79.306  114.543 1.00 19.04 ?  647  LYS A N    1 
ATOM   4209  C CA   . LYS A 1 647  ? 128.384 77.918  114.096 1.00 20.87 ?  647  LYS A CA   1 
ATOM   4210  C C    . LYS A 1 647  ? 128.093 76.977  115.261 1.00 23.75 ?  647  LYS A C    1 
ATOM   4211  O O    . LYS A 1 647  ? 127.275 76.058  115.136 1.00 21.68 ?  647  LYS A O    1 
ATOM   4212  C CB   . LYS A 1 647  ? 129.674 77.512  113.381 1.00 21.77 ?  647  LYS A CB   1 
ATOM   4213  C CG   . LYS A 1 647  ? 129.784 76.029  113.059 1.00 20.14 ?  647  LYS A CG   1 
ATOM   4214  C CD   . LYS A 1 647  ? 128.671 75.572  112.129 1.00 20.94 ?  647  LYS A CD   1 
ATOM   4215  C CE   . LYS A 1 647  ? 128.361 74.097  112.332 1.00 21.46 ?  647  LYS A CE   1 
ATOM   4216  N NZ   . LYS A 1 647  ? 127.044 73.717  111.751 1.00 26.23 ?  647  LYS A NZ   1 
ATOM   4217  N N    . LEU A 1 648  ? 128.752 77.192  116.402 1.00 22.80 ?  648  LEU A N    1 
ATOM   4218  C CA   . LEU A 1 648  ? 128.521 76.346  117.569 1.00 21.05 ?  648  LEU A CA   1 
ATOM   4219  C C    . LEU A 1 648  ? 127.116 76.534  118.129 1.00 21.29 ?  648  LEU A C    1 
ATOM   4220  O O    . LEU A 1 648  ? 126.484 75.566  118.565 1.00 20.87 ?  648  LEU A O    1 
ATOM   4221  C CB   . LEU A 1 648  ? 129.570 76.628  118.644 1.00 20.01 ?  648  LEU A CB   1 
ATOM   4222  C CG   . LEU A 1 648  ? 131.001 76.169  118.351 1.00 22.06 ?  648  LEU A CG   1 
ATOM   4223  C CD1  . LEU A 1 648  ? 131.913 76.459  119.534 1.00 22.14 ?  648  LEU A CD1  1 
ATOM   4224  C CD2  . LEU A 1 648  ? 131.034 74.691  117.994 1.00 20.53 ?  648  LEU A CD2  1 
ATOM   4225  N N    . GLU A 1 649  ? 126.611 77.769  118.137 1.00 21.39 ?  649  GLU A N    1 
ATOM   4226  C CA   . GLU A 1 649  ? 125.256 77.999  118.623 1.00 22.17 ?  649  GLU A CA   1 
ATOM   4227  C C    . GLU A 1 649  ? 124.183 77.563  117.633 1.00 23.22 ?  649  GLU A C    1 
ATOM   4228  O O    . GLU A 1 649  ? 123.029 77.382  118.038 1.00 20.02 ?  649  GLU A O    1 
ATOM   4229  C CB   . GLU A 1 649  ? 125.060 79.473  118.979 1.00 16.14 ?  649  GLU A CB   1 
ATOM   4230  C CG   . GLU A 1 649  ? 125.394 79.796  120.423 1.00 19.96 ?  649  GLU A CG   1 
ATOM   4231  C CD   . GLU A 1 649  ? 125.796 81.240  120.624 1.00 21.29 ?  649  GLU A CD   1 
ATOM   4232  O OE1  . GLU A 1 649  ? 125.027 82.138  120.222 1.00 20.68 ?  649  GLU A OE1  1 
ATOM   4233  O OE2  . GLU A 1 649  ? 126.878 81.474  121.199 1.00 20.06 ?  649  GLU A OE2  1 
ATOM   4234  N N    . ASP A 1 650  ? 124.527 77.405  116.352 1.00 21.28 ?  650  ASP A N    1 
ATOM   4235  C CA   . ASP A 1 650  ? 123.541 76.951  115.375 1.00 21.72 ?  650  ASP A CA   1 
ATOM   4236  C C    . ASP A 1 650  ? 123.084 75.523  115.656 1.00 25.18 ?  650  ASP A C    1 
ATOM   4237  O O    . ASP A 1 650  ? 121.887 75.224  115.580 1.00 23.10 ?  650  ASP A O    1 
ATOM   4238  C CB   . ASP A 1 650  ? 124.117 77.060  113.963 1.00 23.06 ?  650  ASP A CB   1 
ATOM   4239  C CG   . ASP A 1 650  ? 123.268 76.343  112.929 1.00 25.93 ?  650  ASP A CG   1 
ATOM   4240  O OD1  . ASP A 1 650  ? 122.041 76.580  112.895 1.00 25.68 ?  650  ASP A OD1  1 
ATOM   4241  O OD2  . ASP A 1 650  ? 123.827 75.543  112.150 1.00 21.27 ?  650  ASP A OD2  1 
ATOM   4242  N N    . LEU A 1 651  ? 124.019 74.627  115.981 1.00 23.63 ?  651  LEU A N    1 
ATOM   4243  C CA   . LEU A 1 651  ? 123.667 73.230  116.205 1.00 22.26 ?  651  LEU A CA   1 
ATOM   4244  C C    . LEU A 1 651  ? 122.976 72.998  117.543 1.00 22.49 ?  651  LEU A C    1 
ATOM   4245  O O    . LEU A 1 651  ? 122.275 71.991  117.693 1.00 26.25 ?  651  LEU A O    1 
ATOM   4246  C CB   . LEU A 1 651  ? 124.915 72.346  116.107 1.00 21.37 ?  651  LEU A CB   1 
ATOM   4247  C CG   . LEU A 1 651  ? 126.140 72.726  116.942 1.00 21.87 ?  651  LEU A CG   1 
ATOM   4248  C CD1  . LEU A 1 651  ? 126.236 71.867  118.196 1.00 23.28 ?  651  LEU A CD1  1 
ATOM   4249  C CD2  . LEU A 1 651  ? 127.411 72.613  116.113 1.00 23.50 ?  651  LEU A CD2  1 
ATOM   4250  N N    . ILE A 1 652  ? 123.165 73.893  118.514 1.00 20.76 ?  652  ILE A N    1 
ATOM   4251  C CA   . ILE A 1 652  ? 122.494 73.747  119.803 1.00 21.44 ?  652  ILE A CA   1 
ATOM   4252  C C    . ILE A 1 652  ? 120.991 73.950  119.646 1.00 23.85 ?  652  ILE A C    1 
ATOM   4253  O O    . ILE A 1 652  ? 120.183 73.166  120.159 1.00 20.88 ?  652  ILE A O    1 
ATOM   4254  C CB   . ILE A 1 652  ? 123.099 74.720  120.833 1.00 22.73 ?  652  ILE A CB   1 
ATOM   4255  C CG1  . ILE A 1 652  ? 124.414 74.161  121.380 1.00 21.56 ?  652  ILE A CG1  1 
ATOM   4256  C CG2  . ILE A 1 652  ? 122.125 74.991  121.972 1.00 21.60 ?  652  ILE A CG2  1 
ATOM   4257  C CD1  . ILE A 1 652  ? 125.058 75.034  122.434 1.00 19.92 ?  652  ILE A CD1  1 
ATOM   4258  N N    . SER A 1 653  ? 120.596 74.988  118.917 1.00 25.97 ?  653  SER A N    1 
ATOM   4259  C CA   . SER A 1 653  ? 119.185 75.274  118.689 1.00 26.61 ?  653  SER A CA   1 
ATOM   4260  C C    . SER A 1 653  ? 118.615 74.390  117.584 1.00 23.88 ?  653  SER A C    1 
ATOM   4261  O O    . SER A 1 653  ? 118.604 73.165  117.697 1.00 21.53 ?  653  SER A O    1 
ATOM   4262  C CB   . SER A 1 653  ? 118.988 76.749  118.336 1.00 25.11 ?  653  SER A CB   1 
ATOM   4263  O OG   . SER A 1 653  ? 117.730 76.962  117.720 1.00 25.62 ?  653  SER A OG   1 
ATOM   4264  N N    . LEU A 1 670  ? 99.264  70.521  120.166 1.00 22.93 ?  670  LEU A N    1 
ATOM   4265  C CA   . LEU A 1 670  ? 98.088  71.206  120.690 1.00 23.57 ?  670  LEU A CA   1 
ATOM   4266  C C    . LEU A 1 670  ? 98.487  72.414  121.530 1.00 24.28 ?  670  LEU A C    1 
ATOM   4267  O O    . LEU A 1 670  ? 97.634  73.176  121.986 1.00 23.85 ?  670  LEU A O    1 
ATOM   4268  C CB   . LEU A 1 670  ? 97.234  70.246  121.521 1.00 22.42 ?  670  LEU A CB   1 
ATOM   4269  C CG   . LEU A 1 670  ? 96.699  69.010  120.795 1.00 23.16 ?  670  LEU A CG   1 
ATOM   4270  C CD1  . LEU A 1 670  ? 95.913  68.125  121.751 1.00 20.26 ?  670  LEU A CD1  1 
ATOM   4271  C CD2  . LEU A 1 670  ? 95.844  69.411  119.602 1.00 22.71 ?  670  LEU A CD2  1 
ATOM   4272  N N    . MET A 1 671  ? 99.793  72.580  121.735 1.00 25.33 ?  671  MET A N    1 
ATOM   4273  C CA   . MET A 1 671  ? 100.309 73.692  122.523 1.00 24.27 ?  671  MET A CA   1 
ATOM   4274  C C    . MET A 1 671  ? 101.388 74.440  121.752 1.00 29.17 ?  671  MET A C    1 
ATOM   4275  O O    . MET A 1 671  ? 101.580 75.645  121.948 1.00 29.02 ?  671  MET A O    1 
ATOM   4276  C CB   . MET A 1 671  ? 100.862 73.186  123.857 1.00 24.94 ?  671  MET A CB   1 
ATOM   4277  C CG   . MET A 1 671  ? 101.887 72.081  123.699 1.00 27.21 ?  671  MET A CG   1 
ATOM   4278  S SD   . MET A 1 671  ? 102.746 71.643  125.216 1.00 39.62 ?  671  MET A SD   1 
ATOM   4279  C CE   . MET A 1 671  ? 103.371 70.033  124.751 1.00 24.29 ?  671  MET A CE   1 
ATOM   4280  N N    . TYR A 1 672  ? 102.101 73.731  120.873 1.00 32.63 ?  672  TYR A N    1 
ATOM   4281  C CA   . TYR A 1 672  ? 103.163 74.355  120.096 1.00 33.54 ?  672  TYR A CA   1 
ATOM   4282  C C    . TYR A 1 672  ? 102.622 75.256  118.996 1.00 34.61 ?  672  TYR A C    1 
ATOM   4283  O O    . TYR A 1 672  ? 103.345 76.141  118.527 1.00 32.80 ?  672  TYR A O    1 
ATOM   4284  C CB   . TYR A 1 672  ? 104.077 73.284  119.494 1.00 32.59 ?  672  TYR A CB   1 
ATOM   4285  C CG   . TYR A 1 672  ? 103.477 72.534  118.324 1.00 31.06 ?  672  TYR A CG   1 
ATOM   4286  C CD1  . TYR A 1 672  ? 102.500 71.565  118.521 1.00 30.50 ?  672  TYR A CD1  1 
ATOM   4287  C CD2  . TYR A 1 672  ? 103.893 72.789  117.023 1.00 30.91 ?  672  TYR A CD2  1 
ATOM   4288  C CE1  . TYR A 1 672  ? 101.950 70.877  117.455 1.00 32.78 ?  672  TYR A CE1  1 
ATOM   4289  C CE2  . TYR A 1 672  ? 103.349 72.106  115.951 1.00 33.46 ?  672  TYR A CE2  1 
ATOM   4290  C CZ   . TYR A 1 672  ? 102.379 71.151  116.173 1.00 35.92 ?  672  TYR A CZ   1 
ATOM   4291  O OH   . TYR A 1 672  ? 101.835 70.468  115.110 1.00 33.34 ?  672  TYR A OH   1 
ATOM   4292  N N    . LYS A 1 673  ? 101.382 75.043  118.565 1.00 28.52 ?  673  LYS A N    1 
ATOM   4293  C CA   . LYS A 1 673  ? 100.746 75.884  117.558 1.00 28.75 ?  673  LYS A CA   1 
ATOM   4294  C C    . LYS A 1 673  ? 99.446  76.512  118.032 1.00 28.88 ?  673  LYS A C    1 
ATOM   4295  O O    . LYS A 1 673  ? 99.211  77.696  117.774 1.00 31.59 ?  673  LYS A O    1 
ATOM   4296  C CB   . LYS A 1 673  ? 100.484 75.070  116.283 1.00 26.81 ?  673  LYS A CB   1 
ATOM   4297  C CG   . LYS A 1 673  ? 100.010 75.901  115.102 1.00 28.03 ?  673  LYS A CG   1 
ATOM   4298  C CD   . LYS A 1 673  ? 99.720  75.026  113.895 1.00 27.33 ?  673  LYS A CD   1 
ATOM   4299  C CE   . LYS A 1 673  ? 99.274  75.858  112.704 1.00 27.13 ?  673  LYS A CE   1 
ATOM   4300  N NZ   . LYS A 1 673  ? 99.012  75.012  111.507 1.00 25.26 ?  673  LYS A NZ   1 
ATOM   4301  N N    . ILE A 1 674  ? 98.590  75.749  118.717 1.00 22.13 ?  674  ILE A N    1 
ATOM   4302  C CA   . ILE A 1 674  ? 97.309  76.285  119.171 1.00 21.54 ?  674  ILE A CA   1 
ATOM   4303  C C    . ILE A 1 674  ? 97.519  77.292  120.295 1.00 25.11 ?  674  ILE A C    1 
ATOM   4304  O O    . ILE A 1 674  ? 96.922  78.375  120.300 1.00 25.55 ?  674  ILE A O    1 
ATOM   4305  C CB   . ILE A 1 674  ? 96.373  75.142  119.601 1.00 24.30 ?  674  ILE A CB   1 
ATOM   4306  C CG1  . ILE A 1 674  ? 96.241  74.109  118.480 1.00 24.01 ?  674  ILE A CG1  1 
ATOM   4307  C CG2  . ILE A 1 674  ? 95.007  75.687  119.989 1.00 24.37 ?  674  ILE A CG2  1 
ATOM   4308  C CD1  . ILE A 1 674  ? 95.722  74.682  117.178 1.00 21.66 ?  674  ILE A CD1  1 
ATOM   4309  N N    . CYS A 1 675  ? 98.370  76.955  121.259 1.00 26.89 ?  675  CYS A N    1 
ATOM   4310  C CA   . CYS A 1 675  ? 98.711  77.866  122.342 1.00 27.65 ?  675  CYS A CA   1 
ATOM   4311  C C    . CYS A 1 675  ? 99.834  78.823  121.970 1.00 28.20 ?  675  CYS A C    1 
ATOM   4312  O O    . CYS A 1 675  ? 100.207 79.668  122.790 1.00 29.23 ?  675  CYS A O    1 
ATOM   4313  C CB   . CYS A 1 675  ? 99.100  77.077  123.598 1.00 27.60 ?  675  CYS A CB   1 
ATOM   4314  S SG   . CYS A 1 675  ? 97.813  75.967  124.215 1.00 39.17 ?  675  CYS A SG   1 
ATOM   4315  N N    . HIS A 1 676  ? 100.379 78.706  120.761 1.00 26.64 ?  676  HIS A N    1 
ATOM   4316  C CA   . HIS A 1 676  ? 101.457 79.583  120.329 1.00 25.06 ?  676  HIS A CA   1 
ATOM   4317  C C    . HIS A 1 676  ? 100.955 81.008  120.140 1.00 27.19 ?  676  HIS A C    1 
ATOM   4318  O O    . HIS A 1 676  ? 99.876  81.239  119.586 1.00 25.81 ?  676  HIS A O    1 
ATOM   4319  C CB   . HIS A 1 676  ? 102.069 79.072  119.027 1.00 25.71 ?  676  HIS A CB   1 
ATOM   4320  C CG   . HIS A 1 676  ? 103.300 79.812  118.607 1.00 29.71 ?  676  HIS A CG   1 
ATOM   4321  N ND1  . HIS A 1 676  ? 104.567 79.430  118.994 1.00 30.37 ?  676  HIS A ND1  1 
ATOM   4322  C CD2  . HIS A 1 676  ? 103.459 80.911  117.833 1.00 26.30 ?  676  HIS A CD2  1 
ATOM   4323  C CE1  . HIS A 1 676  ? 105.453 80.262  118.476 1.00 28.26 ?  676  HIS A CE1  1 
ATOM   4324  N NE2  . HIS A 1 676  ? 104.807 81.170  117.768 1.00 26.55 ?  676  HIS A NE2  1 
ATOM   4325  N N    . HIS A 1 677  ? 101.755 81.964  120.600 1.00 29.10 ?  677  HIS A N    1 
ATOM   4326  C CA   . HIS A 1 677  ? 101.439 83.381  120.495 1.00 28.61 ?  677  HIS A CA   1 
ATOM   4327  C C    . HIS A 1 677  ? 102.730 84.160  120.706 1.00 28.56 ?  677  HIS A C    1 
ATOM   4328  O O    . HIS A 1 677  ? 103.814 83.581  120.824 1.00 29.36 ?  677  HIS A O    1 
ATOM   4329  C CB   . HIS A 1 677  ? 100.361 83.785  121.508 1.00 25.76 ?  677  HIS A CB   1 
ATOM   4330  C CG   . HIS A 1 677  ? 99.524  84.948  121.075 1.00 29.27 ?  677  HIS A CG   1 
ATOM   4331  N ND1  . HIS A 1 677  ? 99.767  86.238  121.495 1.00 29.48 ?  677  HIS A ND1  1 
ATOM   4332  C CD2  . HIS A 1 677  ? 98.447  85.016  120.257 1.00 31.66 ?  677  HIS A CD2  1 
ATOM   4333  C CE1  . HIS A 1 677  ? 98.876  87.050  120.955 1.00 28.94 ?  677  HIS A CE1  1 
ATOM   4334  N NE2  . HIS A 1 677  ? 98.063  86.333  120.200 1.00 32.67 ?  677  HIS A NE2  1 
ATOM   4335  N N    . MET A 1 678  ? 102.608 85.487  120.752 1.00 24.14 ?  678  MET A N    1 
ATOM   4336  C CA   . MET A 1 678  ? 103.741 86.324  121.124 1.00 25.39 ?  678  MET A CA   1 
ATOM   4337  C C    . MET A 1 678  ? 104.060 86.241  122.610 1.00 29.19 ?  678  MET A C    1 
ATOM   4338  O O    . MET A 1 678  ? 105.105 86.750  123.029 1.00 29.49 ?  678  MET A O    1 
ATOM   4339  C CB   . MET A 1 678  ? 103.474 87.778  120.731 1.00 28.00 ?  678  MET A CB   1 
ATOM   4340  C CG   . MET A 1 678  ? 103.774 88.092  119.275 1.00 28.15 ?  678  MET A CG   1 
ATOM   4341  S SD   . MET A 1 678  ? 104.489 89.732  119.054 1.00 33.17 ?  678  MET A SD   1 
ATOM   4342  C CE   . MET A 1 678  ? 104.730 89.762  117.280 1.00 27.88 ?  678  MET A CE   1 
ATOM   4343  N N    . ALA A 1 679  ? 103.190 85.619  123.409 1.00 29.29 ?  679  ALA A N    1 
ATOM   4344  C CA   . ALA A 1 679  ? 103.396 85.472  124.844 1.00 27.24 ?  679  ALA A CA   1 
ATOM   4345  C C    . ALA A 1 679  ? 103.161 84.035  125.297 1.00 26.88 ?  679  ALA A C    1 
ATOM   4346  O O    . ALA A 1 679  ? 102.635 83.802  126.387 1.00 25.73 ?  679  ALA A O    1 
ATOM   4347  C CB   . ALA A 1 679  ? 102.499 86.431  125.626 1.00 27.38 ?  679  ALA A CB   1 
ATOM   4348  N N    . PHE A 1 680  ? 103.537 83.056  124.470 1.00 27.78 ?  680  PHE A N    1 
ATOM   4349  C CA   . PHE A 1 680  ? 103.369 81.658  124.856 1.00 30.00 ?  680  PHE A CA   1 
ATOM   4350  C C    . PHE A 1 680  ? 104.430 81.240  125.868 1.00 30.05 ?  680  PHE A C    1 
ATOM   4351  O O    . PHE A 1 680  ? 104.113 80.877  127.007 1.00 29.09 ?  680  PHE A O    1 
ATOM   4352  C CB   . PHE A 1 680  ? 103.418 80.761  123.617 1.00 27.51 ?  680  PHE A CB   1 
ATOM   4353  C CG   . PHE A 1 680  ? 103.540 79.296  123.933 1.00 28.63 ?  680  PHE A CG   1 
ATOM   4354  C CD1  . PHE A 1 680  ? 102.568 78.650  124.681 1.00 26.87 ?  680  PHE A CD1  1 
ATOM   4355  C CD2  . PHE A 1 680  ? 104.627 78.566  123.482 1.00 28.49 ?  680  PHE A CD2  1 
ATOM   4356  C CE1  . PHE A 1 680  ? 102.678 77.302  124.973 1.00 27.14 ?  680  PHE A CE1  1 
ATOM   4357  C CE2  . PHE A 1 680  ? 104.744 77.218  123.770 1.00 28.97 ?  680  PHE A CE2  1 
ATOM   4358  C CZ   . PHE A 1 680  ? 103.768 76.586  124.517 1.00 29.88 ?  680  PHE A CZ   1 
ATOM   4359  N N    . GLU A 1 681  ? 105.702 81.282  125.467 1.00 28.60 ?  681  GLU A N    1 
ATOM   4360  C CA   . GLU A 1 681  ? 106.794 81.018  126.394 1.00 29.43 ?  681  GLU A CA   1 
ATOM   4361  C C    . GLU A 1 681  ? 107.106 82.225  127.268 1.00 26.46 ?  681  GLU A C    1 
ATOM   4362  O O    . GLU A 1 681  ? 107.771 82.079  128.303 1.00 24.52 ?  681  GLU A O    1 
ATOM   4363  C CB   . GLU A 1 681  ? 108.044 80.591  125.621 1.00 29.83 ?  681  GLU A CB   1 
ATOM   4364  C CG   . GLU A 1 681  ? 109.033 79.768  126.429 1.00 29.16 ?  681  GLU A CG   1 
ATOM   4365  C CD   . GLU A 1 681  ? 110.419 79.763  125.819 1.00 32.53 ?  681  GLU A CD   1 
ATOM   4366  O OE1  . GLU A 1 681  ? 110.555 80.174  124.647 1.00 32.45 ?  681  GLU A OE1  1 
ATOM   4367  O OE2  . GLU A 1 681  ? 111.373 79.354  126.512 1.00 33.04 ?  681  GLU A OE2  1 
ATOM   4368  N N    . VAL A 1 682  ? 106.631 83.410  126.877 1.00 28.02 ?  682  VAL A N    1 
ATOM   4369  C CA   . VAL A 1 682  ? 106.821 84.597  127.699 1.00 31.33 ?  682  VAL A CA   1 
ATOM   4370  C C    . VAL A 1 682  ? 106.039 84.479  129.002 1.00 30.53 ?  682  VAL A C    1 
ATOM   4371  O O    . VAL A 1 682  ? 106.429 85.062  130.016 1.00 28.11 ?  682  VAL A O    1 
ATOM   4372  C CB   . VAL A 1 682  ? 106.439 85.860  126.903 1.00 30.83 ?  682  VAL A CB   1 
ATOM   4373  C CG1  . VAL A 1 682  ? 106.899 87.120  127.624 1.00 28.80 ?  682  VAL A CG1  1 
ATOM   4374  C CG2  . VAL A 1 682  ? 107.045 85.800  125.511 1.00 26.54 ?  682  VAL A CG2  1 
ATOM   4375  N N    . THR A 1 683  ? 104.943 83.713  129.010 1.00 26.02 ?  683  THR A N    1 
ATOM   4376  C CA   . THR A 1 683  ? 104.246 83.443  130.266 1.00 28.74 ?  683  THR A CA   1 
ATOM   4377  C C    . THR A 1 683  ? 105.127 82.657  131.233 1.00 29.89 ?  683  THR A C    1 
ATOM   4378  O O    . THR A 1 683  ? 105.185 82.971  132.428 1.00 26.23 ?  683  THR A O    1 
ATOM   4379  C CB   . THR A 1 683  ? 102.941 82.690  130.001 1.00 28.22 ?  683  THR A CB   1 
ATOM   4380  O OG1  . THR A 1 683  ? 103.153 81.694  128.993 1.00 27.73 ?  683  THR A OG1  1 
ATOM   4381  C CG2  . THR A 1 683  ? 101.849 83.651  129.553 1.00 26.86 ?  683  THR A CG2  1 
ATOM   4382  N N    . ILE A 1 684  ? 105.837 81.643  130.732 1.00 27.65 ?  684  ILE A N    1 
ATOM   4383  C CA   . ILE A 1 684  ? 106.739 80.875  131.586 1.00 26.88 ?  684  ILE A CA   1 
ATOM   4384  C C    . ILE A 1 684  ? 107.923 81.731  132.022 1.00 26.76 ?  684  ILE A C    1 
ATOM   4385  O O    . ILE A 1 684  ? 108.403 81.622  133.158 1.00 24.02 ?  684  ILE A O    1 
ATOM   4386  C CB   . ILE A 1 684  ? 107.198 79.594  130.867 1.00 28.17 ?  684  ILE A CB   1 
ATOM   4387  C CG1  . ILE A 1 684  ? 106.041 78.977  130.076 1.00 26.91 ?  684  ILE A CG1  1 
ATOM   4388  C CG2  . ILE A 1 684  ? 107.751 78.594  131.870 1.00 26.72 ?  684  ILE A CG2  1 
ATOM   4389  C CD1  . ILE A 1 684  ? 104.945 78.386  130.940 1.00 25.07 ?  684  ILE A CD1  1 
ATOM   4390  N N    . ASN A 1 685  ? 108.415 82.591  131.126 1.00 27.12 ?  685  ASN A N    1 
ATOM   4391  C CA   . ASN A 1 685  ? 109.493 83.509  131.492 1.00 26.59 ?  685  ASN A CA   1 
ATOM   4392  C C    . ASN A 1 685  ? 109.049 84.482  132.582 1.00 27.67 ?  685  ASN A C    1 
ATOM   4393  O O    . ASN A 1 685  ? 109.809 84.773  133.513 1.00 28.97 ?  685  ASN A O    1 
ATOM   4394  C CB   . ASN A 1 685  ? 109.982 84.267  130.257 1.00 27.81 ?  685  ASN A CB   1 
ATOM   4395  C CG   . ASN A 1 685  ? 110.465 83.342  129.156 1.00 31.32 ?  685  ASN A CG   1 
ATOM   4396  O OD1  . ASN A 1 685  ? 110.837 82.196  129.410 1.00 29.92 ?  685  ASN A OD1  1 
ATOM   4397  N ND2  . ASN A 1 685  ? 110.462 83.836  127.923 1.00 28.76 ?  685  ASN A ND2  1 
ATOM   4398  N N    . ILE A 1 686  ? 107.818 84.989  132.482 1.00 23.87 ?  686  ILE A N    1 
ATOM   4399  C CA   . ILE A 1 686  ? 107.265 85.867  133.508 1.00 27.53 ?  686  ILE A CA   1 
ATOM   4400  C C    . ILE A 1 686  ? 107.094 85.112  134.820 1.00 25.12 ?  686  ILE A C    1 
ATOM   4401  O O    . ILE A 1 686  ? 107.322 85.663  135.902 1.00 21.48 ?  686  ILE A O    1 
ATOM   4402  C CB   . ILE A 1 686  ? 105.939 86.480  133.010 1.00 27.47 ?  686  ILE A CB   1 
ATOM   4403  C CG1  . ILE A 1 686  ? 106.213 87.615  132.022 1.00 25.47 ?  686  ILE A CG1  1 
ATOM   4404  C CG2  . ILE A 1 686  ? 105.073 86.983  134.162 1.00 23.49 ?  686  ILE A CG2  1 
ATOM   4405  C CD1  . ILE A 1 686  ? 105.039 87.930  131.121 1.00 22.36 ?  686  ILE A CD1  1 
ATOM   4406  N N    . ALA A 1 687  ? 106.706 83.836  134.746 1.00 22.80 ?  687  ALA A N    1 
ATOM   4407  C CA   . ALA A 1 687  ? 106.615 83.017  135.951 1.00 26.16 ?  687  ALA A CA   1 
ATOM   4408  C C    . ALA A 1 687  ? 107.978 82.857  136.615 1.00 28.30 ?  687  ALA A C    1 
ATOM   4409  O O    . ALA A 1 687  ? 108.089 82.920  137.844 1.00 28.55 ?  687  ALA A O    1 
ATOM   4410  C CB   . ALA A 1 687  ? 106.018 81.651  135.616 1.00 25.65 ?  687  ALA A CB   1 
ATOM   4411  N N    . ILE A 1 688  ? 109.028 82.660  135.815 1.00 23.98 ?  688  ILE A N    1 
ATOM   4412  C CA   . ILE A 1 688  ? 110.381 82.555  136.361 1.00 25.63 ?  688  ILE A CA   1 
ATOM   4413  C C    . ILE A 1 688  ? 110.818 83.878  136.990 1.00 25.03 ?  688  ILE A C    1 
ATOM   4414  O O    . ILE A 1 688  ? 111.432 83.899  138.067 1.00 25.27 ?  688  ILE A O    1 
ATOM   4415  C CB   . ILE A 1 688  ? 111.355 82.090  135.260 1.00 22.46 ?  688  ILE A CB   1 
ATOM   4416  C CG1  . ILE A 1 688  ? 111.043 80.649  134.848 1.00 22.90 ?  688  ILE A CG1  1 
ATOM   4417  C CG2  . ILE A 1 688  ? 112.801 82.204  135.718 1.00 22.27 ?  688  ILE A CG2  1 
ATOM   4418  C CD1  . ILE A 1 688  ? 111.322 79.624  135.929 1.00 23.49 ?  688  ILE A CD1  1 
ATOM   4419  N N    . VAL A 1 689  ? 110.507 84.998  136.332 1.00 20.08 ?  689  VAL A N    1 
ATOM   4420  C CA   . VAL A 1 689  ? 110.869 86.313  136.862 1.00 27.76 ?  689  VAL A CA   1 
ATOM   4421  C C    . VAL A 1 689  ? 110.116 86.599  138.161 1.00 30.46 ?  689  VAL A C    1 
ATOM   4422  O O    . VAL A 1 689  ? 110.662 87.199  139.094 1.00 28.93 ?  689  VAL A O    1 
ATOM   4423  C CB   . VAL A 1 689  ? 110.620 87.396  135.793 1.00 28.00 ?  689  VAL A CB   1 
ATOM   4424  C CG1  . VAL A 1 689  ? 110.737 88.796  136.381 1.00 22.67 ?  689  VAL A CG1  1 
ATOM   4425  C CG2  . VAL A 1 689  ? 111.600 87.235  134.641 1.00 25.74 ?  689  VAL A CG2  1 
ATOM   4426  N N    . LEU A 1 690  ? 108.859 86.162  138.252 1.00 27.88 ?  690  LEU A N    1 
ATOM   4427  C CA   . LEU A 1 690  ? 108.106 86.326  139.492 1.00 28.64 ?  690  LEU A CA   1 
ATOM   4428  C C    . LEU A 1 690  ? 108.583 85.374  140.583 1.00 28.73 ?  690  LEU A C    1 
ATOM   4429  O O    . LEU A 1 690  ? 108.470 85.697  141.771 1.00 31.67 ?  690  LEU A O    1 
ATOM   4430  C CB   . LEU A 1 690  ? 106.607 86.128  139.243 1.00 26.40 ?  690  LEU A CB   1 
ATOM   4431  C CG   . LEU A 1 690  ? 105.706 87.306  138.844 1.00 27.79 ?  690  LEU A CG   1 
ATOM   4432  C CD1  . LEU A 1 690  ? 105.394 88.164  140.061 1.00 28.23 ?  690  LEU A CD1  1 
ATOM   4433  C CD2  . LEU A 1 690  ? 106.290 88.166  137.732 1.00 26.47 ?  690  LEU A CD2  1 
ATOM   4434  N N    . ASN A 1 691  ? 109.098 84.201  140.212 1.00 23.58 ?  691  ASN A N    1 
ATOM   4435  C CA   . ASN A 1 691  ? 109.537 83.214  141.190 1.00 27.56 ?  691  ASN A CA   1 
ATOM   4436  C C    . ASN A 1 691  ? 110.974 83.405  141.657 1.00 27.09 ?  691  ASN A C    1 
ATOM   4437  O O    . ASN A 1 691  ? 111.362 82.787  142.654 1.00 22.55 ?  691  ASN A O    1 
ATOM   4438  C CB   . ASN A 1 691  ? 109.384 81.797  140.621 1.00 26.64 ?  691  ASN A CB   1 
ATOM   4439  C CG   . ASN A 1 691  ? 108.793 80.824  141.627 1.00 25.71 ?  691  ASN A CG   1 
ATOM   4440  O OD1  . ASN A 1 691  ? 108.180 81.230  142.615 1.00 26.27 ?  691  ASN A OD1  1 
ATOM   4441  N ND2  . ASN A 1 691  ? 108.981 79.532  141.382 1.00 22.75 ?  691  ASN A ND2  1 
ATOM   4442  N N    . ILE A 1 692  ? 111.778 84.218  140.965 1.00 26.42 ?  692  ILE A N    1 
ATOM   4443  C CA   . ILE A 1 692  ? 113.151 84.419  141.430 1.00 29.68 ?  692  ILE A CA   1 
ATOM   4444  C C    . ILE A 1 692  ? 113.178 85.186  142.753 1.00 29.33 ?  692  ILE A C    1 
ATOM   4445  O O    . ILE A 1 692  ? 114.053 84.944  143.595 1.00 24.47 ?  692  ILE A O    1 
ATOM   4446  C CB   . ILE A 1 692  ? 114.017 85.105  140.349 1.00 28.81 ?  692  ILE A CB   1 
ATOM   4447  C CG1  . ILE A 1 692  ? 115.496 85.090  140.753 1.00 28.76 ?  692  ILE A CG1  1 
ATOM   4448  C CG2  . ILE A 1 692  ? 113.577 86.532  140.085 1.00 23.50 ?  692  ILE A CG2  1 
ATOM   4449  C CD1  . ILE A 1 692  ? 116.402 85.872  139.818 1.00 25.70 ?  692  ILE A CD1  1 
ATOM   4450  N N    . VAL A 1 693  ? 112.236 86.102  142.968 1.00 28.07 ?  693  VAL A N    1 
ATOM   4451  C CA   . VAL A 1 693  ? 112.206 86.925  144.178 1.00 29.68 ?  693  VAL A CA   1 
ATOM   4452  C C    . VAL A 1 693  ? 111.969 86.073  145.427 1.00 24.92 ?  693  VAL A C    1 
ATOM   4453  O O    . VAL A 1 693  ? 112.690 86.265  146.417 1.00 23.50 ?  693  VAL A O    1 
ATOM   4454  C CB   . VAL A 1 693  ? 111.178 88.066  144.052 1.00 29.36 ?  693  VAL A CB   1 
ATOM   4455  C CG1  . VAL A 1 693  ? 111.261 88.996  145.253 1.00 28.69 ?  693  VAL A CG1  1 
ATOM   4456  C CG2  . VAL A 1 693  ? 111.396 88.836  142.758 1.00 26.78 ?  693  VAL A CG2  1 
ATOM   4457  N N    . PRO A 1 694  ? 111.007 85.133  145.468 1.00 24.41 ?  694  PRO A N    1 
ATOM   4458  C CA   . PRO A 1 694  ? 110.982 84.204  146.612 1.00 27.58 ?  694  PRO A CA   1 
ATOM   4459  C C    . PRO A 1 694  ? 112.132 83.211  146.612 1.00 28.77 ?  694  PRO A C    1 
ATOM   4460  O O    . PRO A 1 694  ? 112.456 82.668  147.674 1.00 27.42 ?  694  PRO A O    1 
ATOM   4461  C CB   . PRO A 1 694  ? 109.630 83.491  146.468 1.00 25.57 ?  694  PRO A CB   1 
ATOM   4462  C CG   . PRO A 1 694  ? 109.287 83.619  145.047 1.00 23.91 ?  694  PRO A CG   1 
ATOM   4463  C CD   . PRO A 1 694  ? 109.800 84.954  144.634 1.00 22.87 ?  694  PRO A CD   1 
ATOM   4464  N N    . ILE A 1 695  ? 112.741 82.937  145.457 1.00 26.79 ?  695  ILE A N    1 
ATOM   4465  C CA   . ILE A 1 695  ? 113.906 82.059  145.423 1.00 28.62 ?  695  ILE A CA   1 
ATOM   4466  C C    . ILE A 1 695  ? 115.122 82.758  146.021 1.00 29.38 ?  695  ILE A C    1 
ATOM   4467  O O    . ILE A 1 695  ? 115.878 82.164  146.801 1.00 27.33 ?  695  ILE A O    1 
ATOM   4468  C CB   . ILE A 1 695  ? 114.162 81.579  143.980 1.00 27.68 ?  695  ILE A CB   1 
ATOM   4469  C CG1  . ILE A 1 695  ? 113.318 80.339  143.676 1.00 26.16 ?  695  ILE A CG1  1 
ATOM   4470  C CG2  . ILE A 1 695  ? 115.638 81.276  143.743 1.00 26.98 ?  695  ILE A CG2  1 
ATOM   4471  C CD1  . ILE A 1 695  ? 113.301 79.952  142.213 1.00 26.56 ?  695  ILE A CD1  1 
ATOM   4472  N N    . ILE A 1 696  ? 115.314 84.038  145.694 1.00 25.04 ?  696  ILE A N    1 
ATOM   4473  C CA   . ILE A 1 696  ? 116.553 84.721  146.056 1.00 28.29 ?  696  ILE A CA   1 
ATOM   4474  C C    . ILE A 1 696  ? 116.570 85.196  147.506 1.00 25.47 ?  696  ILE A C    1 
ATOM   4475  O O    . ILE A 1 696  ? 117.648 85.507  148.030 1.00 19.80 ?  696  ILE A O    1 
ATOM   4476  C CB   . ILE A 1 696  ? 116.808 85.899  145.096 1.00 26.29 ?  696  ILE A CB   1 
ATOM   4477  C CG1  . ILE A 1 696  ? 118.310 86.161  144.938 1.00 24.96 ?  696  ILE A CG1  1 
ATOM   4478  C CG2  . ILE A 1 696  ? 116.083 87.157  145.561 1.00 22.83 ?  696  ILE A CG2  1 
ATOM   4479  C CD1  . ILE A 1 696  ? 119.114 84.931  144.573 1.00 22.56 ?  696  ILE A CD1  1 
ATOM   4480  N N    . MET A 1 697  ? 115.420 85.253  148.183 1.00 26.53 ?  697  MET A N    1 
ATOM   4481  C CA   . MET A 1 697  ? 115.411 85.743  149.557 1.00 25.91 ?  697  MET A CA   1 
ATOM   4482  C C    . MET A 1 697  ? 115.916 84.714  150.559 1.00 27.72 ?  697  MET A C    1 
ATOM   4483  O O    . MET A 1 697  ? 116.222 85.085  151.698 1.00 28.92 ?  697  MET A O    1 
ATOM   4484  C CB   . MET A 1 697  ? 114.004 86.226  149.949 1.00 25.92 ?  697  MET A CB   1 
ATOM   4485  C CG   . MET A 1 697  ? 112.827 85.267  149.702 1.00 27.43 ?  697  MET A CG   1 
ATOM   4486  S SD   . MET A 1 697  ? 112.774 83.729  150.654 1.00 39.03 ?  697  MET A SD   1 
ATOM   4487  C CE   . MET A 1 697  ? 112.179 84.322  152.237 1.00 28.59 ?  697  MET A CE   1 
ATOM   4488  N N    . GLU A 1 698  ? 116.001 83.440  150.167 1.00 26.10 ?  698  GLU A N    1 
ATOM   4489  C CA   . GLU A 1 698  ? 116.480 82.406  151.080 1.00 28.89 ?  698  GLU A CA   1 
ATOM   4490  C C    . GLU A 1 698  ? 117.944 82.621  151.446 1.00 30.76 ?  698  GLU A C    1 
ATOM   4491  O O    . GLU A 1 698  ? 118.327 82.470  152.611 1.00 29.84 ?  698  GLU A O    1 
ATOM   4492  C CB   . GLU A 1 698  ? 116.282 81.026  150.453 1.00 29.88 ?  698  GLU A CB   1 
ATOM   4493  C CG   . GLU A 1 698  ? 114.955 80.854  149.732 1.00 30.33 ?  698  GLU A CG   1 
ATOM   4494  C CD   . GLU A 1 698  ? 113.886 80.236  150.610 1.00 32.04 ?  698  GLU A CD   1 
ATOM   4495  O OE1  . GLU A 1 698  ? 114.242 79.599  151.623 1.00 31.90 ?  698  GLU A OE1  1 
ATOM   4496  O OE2  . GLU A 1 698  ? 112.689 80.384  150.286 1.00 28.42 ?  698  GLU A OE2  1 
ATOM   4497  N N    . PHE A 1 699  ? 118.776 82.974  150.465 1.00 25.28 ?  699  PHE A N    1 
ATOM   4498  C CA   . PHE A 1 699  ? 120.189 83.216  150.717 1.00 22.36 ?  699  PHE A CA   1 
ATOM   4499  C C    . PHE A 1 699  ? 120.467 84.619  151.241 1.00 21.07 ?  699  PHE A C    1 
ATOM   4500  O O    . PHE A 1 699  ? 121.578 84.875  151.718 1.00 23.17 ?  699  PHE A O    1 
ATOM   4501  C CB   . PHE A 1 699  ? 120.998 82.974  149.440 1.00 23.55 ?  699  PHE A CB   1 
ATOM   4502  C CG   . PHE A 1 699  ? 122.439 82.631  149.691 1.00 26.03 ?  699  PHE A CG   1 
ATOM   4503  C CD1  . PHE A 1 699  ? 122.784 81.435  150.299 1.00 25.41 ?  699  PHE A CD1  1 
ATOM   4504  C CD2  . PHE A 1 699  ? 123.448 83.504  149.318 1.00 23.30 ?  699  PHE A CD2  1 
ATOM   4505  C CE1  . PHE A 1 699  ? 124.110 81.116  150.531 1.00 26.28 ?  699  PHE A CE1  1 
ATOM   4506  C CE2  . PHE A 1 699  ? 124.776 83.191  149.548 1.00 24.83 ?  699  PHE A CE2  1 
ATOM   4507  C CZ   . PHE A 1 699  ? 125.106 81.995  150.155 1.00 27.25 ?  699  PHE A CZ   1 
ATOM   4508  N N    . VAL A 1 700  ? 119.497 85.525  151.166 1.00 21.17 ?  700  VAL A N    1 
ATOM   4509  C CA   . VAL A 1 700  ? 119.674 86.883  151.666 1.00 24.51 ?  700  VAL A CA   1 
ATOM   4510  C C    . VAL A 1 700  ? 118.802 87.108  152.895 1.00 21.38 ?  700  VAL A C    1 
ATOM   4511  O O    . VAL A 1 700  ? 117.623 87.441  152.779 1.00 15.97 ?  700  VAL A O    1 
ATOM   4512  C CB   . VAL A 1 700  ? 119.359 87.926  150.578 1.00 23.99 ?  700  VAL A CB   1 
ATOM   4513  C CG1  . VAL A 1 700  ? 119.807 89.309  151.024 1.00 19.70 ?  700  VAL A CG1  1 
ATOM   4514  C CG2  . VAL A 1 700  ? 120.025 87.543  149.265 1.00 23.58 ?  700  VAL A CG2  1 
ATOM   4515  N N    . ASP A 1 730  ? 107.397 83.951  159.758 1.00 32.47 ?  730  ASP A N    1 
ATOM   4516  C CA   . ASP A 1 730  ? 106.918 85.272  159.371 1.00 33.66 ?  730  ASP A CA   1 
ATOM   4517  C C    . ASP A 1 730  ? 106.311 85.248  157.971 1.00 36.55 ?  730  ASP A C    1 
ATOM   4518  O O    . ASP A 1 730  ? 105.113 85.017  157.807 1.00 37.52 ?  730  ASP A O    1 
ATOM   4519  C CB   . ASP A 1 730  ? 108.055 86.295  159.435 1.00 28.56 ?  730  ASP A CB   1 
ATOM   4520  C CG   . ASP A 1 730  ? 108.320 86.784  160.845 1.00 33.57 ?  730  ASP A CG   1 
ATOM   4521  O OD1  . ASP A 1 730  ? 107.530 86.446  161.752 1.00 35.90 ?  730  ASP A OD1  1 
ATOM   4522  O OD2  . ASP A 1 730  ? 109.319 87.506  161.047 1.00 34.82 ?  730  ASP A OD2  1 
ATOM   4523  N N    . ALA A 1 731  ? 107.149 85.489  156.964 1.00 31.44 ?  731  ALA A N    1 
ATOM   4524  C CA   . ALA A 1 731  ? 106.722 85.513  155.573 1.00 31.42 ?  731  ALA A CA   1 
ATOM   4525  C C    . ALA A 1 731  ? 107.053 84.223  154.834 1.00 28.76 ?  731  ALA A C    1 
ATOM   4526  O O    . ALA A 1 731  ? 106.960 84.183  153.603 1.00 29.93 ?  731  ALA A O    1 
ATOM   4527  C CB   . ALA A 1 731  ? 107.352 86.705  154.849 1.00 26.41 ?  731  ALA A CB   1 
ATOM   4528  N N    . LEU A 1 732  ? 107.445 83.170  155.556 1.00 26.00 ?  732  LEU A N    1 
ATOM   4529  C CA   . LEU A 1 732  ? 107.794 81.914  154.902 1.00 30.03 ?  732  LEU A CA   1 
ATOM   4530  C C    . LEU A 1 732  ? 106.559 81.165  154.415 1.00 30.35 ?  732  LEU A C    1 
ATOM   4531  O O    . LEU A 1 732  ? 106.636 80.427  153.426 1.00 29.91 ?  732  LEU A O    1 
ATOM   4532  C CB   . LEU A 1 732  ? 108.607 81.038  155.857 1.00 28.29 ?  732  LEU A CB   1 
ATOM   4533  C CG   . LEU A 1 732  ? 109.245 79.766  155.291 1.00 28.52 ?  732  LEU A CG   1 
ATOM   4534  C CD1  . LEU A 1 732  ? 109.976 80.058  153.989 1.00 27.43 ?  732  LEU A CD1  1 
ATOM   4535  C CD2  . LEU A 1 732  ? 110.185 79.135  156.308 1.00 26.99 ?  732  LEU A CD2  1 
ATOM   4536  N N    . ARG A 1 733  ? 105.418 81.345  155.085 1.00 28.81 ?  733  ARG A N    1 
ATOM   4537  C CA   . ARG A 1 733  ? 104.224 80.575  154.745 1.00 30.84 ?  733  ARG A CA   1 
ATOM   4538  C C    . ARG A 1 733  ? 103.656 80.980  153.389 1.00 27.41 ?  733  ARG A C    1 
ATOM   4539  O O    . ARG A 1 733  ? 103.296 80.116  152.581 1.00 22.47 ?  733  ARG A O    1 
ATOM   4540  C CB   . ARG A 1 733  ? 103.170 80.735  155.840 1.00 32.39 ?  733  ARG A CB   1 
ATOM   4541  C CG   . ARG A 1 733  ? 103.539 80.066  157.157 1.00 30.15 ?  733  ARG A CG   1 
ATOM   4542  C CD   . ARG A 1 733  ? 103.308 78.562  157.105 1.00 28.99 ?  733  ARG A CD   1 
ATOM   4543  N NE   . ARG A 1 733  ? 104.500 77.835  156.682 1.00 34.27 ?  733  ARG A NE   1 
ATOM   4544  C CZ   . ARG A 1 733  ? 105.482 77.466  157.494 1.00 33.30 ?  733  ARG A CZ   1 
ATOM   4545  N NH1  . ARG A 1 733  ? 105.446 77.737  158.789 1.00 30.72 ?  733  ARG A NH1  1 
ATOM   4546  N NH2  . ARG A 1 733  ? 106.525 76.810  156.995 1.00 29.43 ?  733  ARG A NH2  1 
ATOM   4547  N N    . ILE A 1 734  ? 103.568 82.285  153.119 1.00 26.71 ?  734  ILE A N    1 
ATOM   4548  C CA   . ILE A 1 734  ? 103.039 82.746  151.838 1.00 28.46 ?  734  ILE A CA   1 
ATOM   4549  C C    . ILE A 1 734  ? 103.983 82.364  150.701 1.00 26.86 ?  734  ILE A C    1 
ATOM   4550  O O    . ILE A 1 734  ? 103.541 81.972  149.611 1.00 22.80 ?  734  ILE A O    1 
ATOM   4551  C CB   . ILE A 1 734  ? 102.771 84.265  151.891 1.00 27.59 ?  734  ILE A CB   1 
ATOM   4552  C CG1  . ILE A 1 734  ? 102.517 84.835  150.493 1.00 24.14 ?  734  ILE A CG1  1 
ATOM   4553  C CG2  . ILE A 1 734  ? 103.914 84.996  152.585 1.00 26.70 ?  734  ILE A CG2  1 
ATOM   4554  C CD1  . ILE A 1 734  ? 102.164 86.306  150.487 1.00 25.50 ?  734  ILE A CD1  1 
ATOM   4555  N N    . SER A 1 735  ? 105.295 82.455  150.942 1.00 25.75 ?  735  SER A N    1 
ATOM   4556  C CA   . SER A 1 735  ? 106.270 82.033  149.941 1.00 28.14 ?  735  SER A CA   1 
ATOM   4557  C C    . SER A 1 735  ? 106.159 80.541  149.657 1.00 30.24 ?  735  SER A C    1 
ATOM   4558  O O    . SER A 1 735  ? 106.231 80.117  148.499 1.00 27.10 ?  735  SER A O    1 
ATOM   4559  C CB   . SER A 1 735  ? 107.683 82.389  150.402 1.00 28.21 ?  735  SER A CB   1 
ATOM   4560  O OG   . SER A 1 735  ? 108.061 81.620  151.531 1.00 25.45 ?  735  SER A OG   1 
ATOM   4561  N N    . ASN A 1 736  ? 105.968 79.729  150.700 1.00 27.34 ?  736  ASN A N    1 
ATOM   4562  C CA   . ASN A 1 736  ? 105.789 78.294  150.501 1.00 25.76 ?  736  ASN A CA   1 
ATOM   4563  C C    . ASN A 1 736  ? 104.499 77.994  149.744 1.00 28.22 ?  736  ASN A C    1 
ATOM   4564  O O    . ASN A 1 736  ? 104.468 77.098  148.892 1.00 25.41 ?  736  ASN A O    1 
ATOM   4565  C CB   . ASN A 1 736  ? 105.802 77.573  151.849 1.00 26.31 ?  736  ASN A CB   1 
ATOM   4566  C CG   . ASN A 1 736  ? 106.816 76.447  151.897 1.00 29.65 ?  736  ASN A CG   1 
ATOM   4567  O OD1  . ASN A 1 736  ? 107.697 76.353  151.043 1.00 31.64 ?  736  ASN A OD1  1 
ATOM   4568  N ND2  . ASN A 1 736  ? 106.698 75.587  152.902 1.00 27.11 ?  736  ASN A ND2  1 
ATOM   4569  N N    . TYR A 1 737  ? 103.427 78.733  150.040 1.00 27.96 ?  737  TYR A N    1 
ATOM   4570  C CA   . TYR A 1 737  ? 102.156 78.513  149.356 1.00 29.66 ?  737  TYR A CA   1 
ATOM   4571  C C    . TYR A 1 737  ? 102.254 78.856  147.873 1.00 28.95 ?  737  TYR A C    1 
ATOM   4572  O O    . TYR A 1 737  ? 101.780 78.097  147.017 1.00 27.40 ?  737  TYR A O    1 
ATOM   4573  C CB   . TYR A 1 737  ? 101.051 79.330  150.028 1.00 29.29 ?  737  TYR A CB   1 
ATOM   4574  C CG   . TYR A 1 737  ? 100.688 78.850  151.416 1.00 30.38 ?  737  TYR A CG   1 
ATOM   4575  C CD1  . TYR A 1 737  ? 100.913 77.533  151.798 1.00 29.28 ?  737  TYR A CD1  1 
ATOM   4576  C CD2  . TYR A 1 737  ? 100.121 79.715  152.344 1.00 28.90 ?  737  TYR A CD2  1 
ATOM   4577  C CE1  . TYR A 1 737  ? 100.584 77.091  153.067 1.00 29.16 ?  737  TYR A CE1  1 
ATOM   4578  C CE2  . TYR A 1 737  ? 99.788  79.282  153.615 1.00 26.68 ?  737  TYR A CE2  1 
ATOM   4579  C CZ   . TYR A 1 737  ? 100.022 77.969  153.970 1.00 29.20 ?  737  TYR A CZ   1 
ATOM   4580  O OH   . TYR A 1 737  ? 99.692  77.534  155.233 1.00 30.91 ?  737  TYR A OH   1 
ATOM   4581  N N    . VAL A 1 738  ? 102.873 79.995  147.545 1.00 25.17 ?  738  VAL A N    1 
ATOM   4582  C CA   . VAL A 1 738  ? 103.014 80.346  146.134 1.00 28.94 ?  738  VAL A CA   1 
ATOM   4583  C C    . VAL A 1 738  ? 104.014 79.421  145.446 1.00 26.86 ?  738  VAL A C    1 
ATOM   4584  O O    . VAL A 1 738  ? 103.880 79.138  144.249 1.00 21.10 ?  738  VAL A O    1 
ATOM   4585  C CB   . VAL A 1 738  ? 103.379 81.835  145.958 1.00 30.83 ?  738  VAL A CB   1 
ATOM   4586  C CG1  . VAL A 1 738  ? 102.320 82.720  146.603 1.00 28.26 ?  738  VAL A CG1  1 
ATOM   4587  C CG2  . VAL A 1 738  ? 104.756 82.151  146.515 1.00 24.26 ?  738  VAL A CG2  1 
ATOM   4588  N N    . PHE A 1 739  ? 105.005 78.908  146.186 1.00 24.12 ?  739  PHE A N    1 
ATOM   4589  C CA   . PHE A 1 739  ? 105.899 77.894  145.638 1.00 25.63 ?  739  PHE A CA   1 
ATOM   4590  C C    . PHE A 1 739  ? 105.134 76.631  145.270 1.00 26.53 ?  739  PHE A C    1 
ATOM   4591  O O    . PHE A 1 739  ? 105.344 76.062  144.195 1.00 22.12 ?  739  PHE A O    1 
ATOM   4592  C CB   . PHE A 1 739  ? 107.001 77.568  146.647 1.00 24.47 ?  739  PHE A CB   1 
ATOM   4593  C CG   . PHE A 1 739  ? 108.279 78.327  146.425 1.00 28.10 ?  739  PHE A CG   1 
ATOM   4594  C CD1  . PHE A 1 739  ? 108.346 79.349  145.492 1.00 27.91 ?  739  PHE A CD1  1 
ATOM   4595  C CD2  . PHE A 1 739  ? 109.413 78.020  147.159 1.00 28.16 ?  739  PHE A CD2  1 
ATOM   4596  C CE1  . PHE A 1 739  ? 109.523 80.045  145.292 1.00 26.87 ?  739  PHE A CE1  1 
ATOM   4597  C CE2  . PHE A 1 739  ? 110.592 78.714  146.965 1.00 26.61 ?  739  PHE A CE2  1 
ATOM   4598  C CZ   . PHE A 1 739  ? 110.646 79.728  146.030 1.00 22.80 ?  739  PHE A CZ   1 
ATOM   4599  N N    . PHE A 1 740  ? 104.234 76.186  146.151 1.00 26.38 ?  740  PHE A N    1 
ATOM   4600  C CA   . PHE A 1 740  ? 103.423 75.007  145.863 1.00 28.87 ?  740  PHE A CA   1 
ATOM   4601  C C    . PHE A 1 740  ? 102.489 75.250  144.682 1.00 26.74 ?  740  PHE A C    1 
ATOM   4602  O O    . PHE A 1 740  ? 102.285 74.355  143.853 1.00 22.80 ?  740  PHE A O    1 
ATOM   4603  C CB   . PHE A 1 740  ? 102.627 74.599  147.102 1.00 26.22 ?  740  PHE A CB   1 
ATOM   4604  C CG   . PHE A 1 740  ? 103.477 74.079  148.227 1.00 26.43 ?  740  PHE A CG   1 
ATOM   4605  C CD1  . PHE A 1 740  ? 104.648 73.386  147.965 1.00 24.20 ?  740  PHE A CD1  1 
ATOM   4606  C CD2  . PHE A 1 740  ? 103.103 74.279  149.546 1.00 27.52 ?  740  PHE A CD2  1 
ATOM   4607  C CE1  . PHE A 1 740  ? 105.432 72.905  148.997 1.00 22.71 ?  740  PHE A CE1  1 
ATOM   4608  C CE2  . PHE A 1 740  ? 103.882 73.801  150.583 1.00 26.14 ?  740  PHE A CE2  1 
ATOM   4609  C CZ   . PHE A 1 740  ? 105.048 73.113  150.308 1.00 23.69 ?  740  PHE A CZ   1 
ATOM   4610  N N    . VAL A 1 741  ? 101.918 76.454  144.590 1.00 26.45 ?  741  VAL A N    1 
ATOM   4611  C CA   . VAL A 1 741  ? 101.018 76.774  143.481 1.00 27.81 ?  741  VAL A CA   1 
ATOM   4612  C C    . VAL A 1 741  ? 101.773 76.749  142.154 1.00 29.82 ?  741  VAL A C    1 
ATOM   4613  O O    . VAL A 1 741  ? 101.314 76.159  141.166 1.00 27.54 ?  741  VAL A O    1 
ATOM   4614  C CB   . VAL A 1 741  ? 100.336 78.133  143.722 1.00 28.10 ?  741  VAL A CB   1 
ATOM   4615  C CG1  . VAL A 1 741  ? 99.700  78.656  142.441 1.00 24.78 ?  741  VAL A CG1  1 
ATOM   4616  C CG2  . VAL A 1 741  ? 99.295  78.014  144.824 1.00 28.33 ?  741  VAL A CG2  1 
ATOM   4617  N N    . ILE A 1 742  ? 102.955 77.373  142.118 1.00 28.83 ?  742  ILE A N    1 
ATOM   4618  C CA   . ILE A 1 742  ? 103.750 77.399  140.893 1.00 28.60 ?  742  ILE A CA   1 
ATOM   4619  C C    . ILE A 1 742  ? 104.254 76.000  140.548 1.00 26.02 ?  742  ILE A C    1 
ATOM   4620  O O    . ILE A 1 742  ? 104.327 75.624  139.371 1.00 21.10 ?  742  ILE A O    1 
ATOM   4621  C CB   . ILE A 1 742  ? 104.897 78.419  141.036 1.00 28.19 ?  742  ILE A CB   1 
ATOM   4622  C CG1  . ILE A 1 742  ? 104.324 79.839  141.105 1.00 26.59 ?  742  ILE A CG1  1 
ATOM   4623  C CG2  . ILE A 1 742  ? 105.892 78.303  139.887 1.00 26.68 ?  742  ILE A CG2  1 
ATOM   4624  C CD1  . ILE A 1 742  ? 105.339 80.942  140.883 1.00 25.47 ?  742  ILE A CD1  1 
ATOM   4625  N N    . TYR A 1 743  ? 104.587 75.199  141.566 1.00 24.44 ?  743  TYR A N    1 
ATOM   4626  C CA   . TYR A 1 743  ? 105.017 73.827  141.322 1.00 25.96 ?  743  TYR A CA   1 
ATOM   4627  C C    . TYR A 1 743  ? 103.886 72.987  140.742 1.00 27.59 ?  743  TYR A C    1 
ATOM   4628  O O    . TYR A 1 743  ? 104.115 72.174  139.843 1.00 26.85 ?  743  TYR A O    1 
ATOM   4629  C CB   . TYR A 1 743  ? 105.549 73.203  142.612 1.00 26.93 ?  743  TYR A CB   1 
ATOM   4630  C CG   . TYR A 1 743  ? 106.929 73.688  143.005 1.00 27.73 ?  743  TYR A CG   1 
ATOM   4631  C CD1  . TYR A 1 743  ? 107.686 74.471  142.141 1.00 25.12 ?  743  TYR A CD1  1 
ATOM   4632  C CD2  . TYR A 1 743  ? 107.473 73.366  144.242 1.00 28.60 ?  743  TYR A CD2  1 
ATOM   4633  C CE1  . TYR A 1 743  ? 108.944 74.919  142.497 1.00 27.19 ?  743  TYR A CE1  1 
ATOM   4634  C CE2  . TYR A 1 743  ? 108.732 73.808  144.607 1.00 27.62 ?  743  TYR A CE2  1 
ATOM   4635  C CZ   . TYR A 1 743  ? 109.463 74.584  143.730 1.00 27.77 ?  743  TYR A CZ   1 
ATOM   4636  O OH   . TYR A 1 743  ? 110.716 75.027  144.086 1.00 27.04 ?  743  TYR A OH   1 
ATOM   4637  N N    . ALA A 1 744  ? 102.658 73.177  141.231 1.00 27.46 ?  744  ALA A N    1 
ATOM   4638  C CA   . ALA A 1 744  ? 101.513 72.484  140.646 1.00 25.30 ?  744  ALA A CA   1 
ATOM   4639  C C    . ALA A 1 744  ? 101.257 72.944  139.214 1.00 24.59 ?  744  ALA A C    1 
ATOM   4640  O O    . ALA A 1 744  ? 100.906 72.131  138.347 1.00 20.83 ?  744  ALA A O    1 
ATOM   4641  C CB   . ALA A 1 744  ? 100.271 72.700  141.511 1.00 22.71 ?  744  ALA A CB   1 
ATOM   4642  N N    . ILE A 1 745  ? 101.426 74.244  138.952 1.00 24.27 ?  745  ILE A N    1 
ATOM   4643  C CA   . ILE A 1 745  ? 101.219 74.773  137.604 1.00 25.82 ?  745  ILE A CA   1 
ATOM   4644  C C    . ILE A 1 745  ? 102.224 74.163  136.631 1.00 27.18 ?  745  ILE A C    1 
ATOM   4645  O O    . ILE A 1 745  ? 101.859 73.680  135.551 1.00 25.98 ?  745  ILE A O    1 
ATOM   4646  C CB   . ILE A 1 745  ? 101.301 76.311  137.615 1.00 25.89 ?  745  ILE A CB   1 
ATOM   4647  C CG1  . ILE A 1 745  ? 100.021 76.910  138.200 1.00 24.44 ?  745  ILE A CG1  1 
ATOM   4648  C CG2  . ILE A 1 745  ? 101.546 76.855  136.214 1.00 23.33 ?  745  ILE A CG2  1 
ATOM   4649  C CD1  . ILE A 1 745  ? 98.764  76.514  137.456 1.00 24.20 ?  745  ILE A CD1  1 
ATOM   4650  N N    . GLU A 1 746  ? 103.504 74.146  137.009 1.00 27.35 ?  746  GLU A N    1 
ATOM   4651  C CA   . GLU A 1 746  ? 104.506 73.549  136.134 1.00 23.74 ?  746  GLU A CA   1 
ATOM   4652  C C    . GLU A 1 746  ? 104.393 72.029  136.082 1.00 23.64 ?  746  GLU A C    1 
ATOM   4653  O O    . GLU A 1 746  ? 104.786 71.427  135.079 1.00 24.59 ?  746  GLU A O    1 
ATOM   4654  C CB   . GLU A 1 746  ? 105.915 73.973  136.558 1.00 25.35 ?  746  GLU A CB   1 
ATOM   4655  C CG   . GLU A 1 746  ? 106.375 73.446  137.902 1.00 27.63 ?  746  GLU A CG   1 
ATOM   4656  C CD   . GLU A 1 746  ? 107.791 73.872  138.235 1.00 30.36 ?  746  GLU A CD   1 
ATOM   4657  O OE1  . GLU A 1 746  ? 108.287 74.831  137.607 1.00 27.73 ?  746  GLU A OE1  1 
ATOM   4658  O OE2  . GLU A 1 746  ? 108.409 73.249  139.123 1.00 28.79 ?  746  GLU A OE2  1 
ATOM   4659  N N    . ALA A 1 747  ? 103.833 71.398  137.119 1.00 23.02 ?  747  ALA A N    1 
ATOM   4660  C CA   . ALA A 1 747  ? 103.568 69.966  137.060 1.00 27.53 ?  747  ALA A CA   1 
ATOM   4661  C C    . ALA A 1 747  ? 102.490 69.646  136.034 1.00 28.20 ?  747  ALA A C    1 
ATOM   4662  O O    . ALA A 1 747  ? 102.626 68.690  135.264 1.00 30.58 ?  747  ALA A O    1 
ATOM   4663  C CB   . ALA A 1 747  ? 103.169 69.447  138.441 1.00 24.24 ?  747  ALA A CB   1 
ATOM   4664  N N    . ILE A 1 748  ? 101.414 70.437  135.999 1.00 23.28 ?  748  ILE A N    1 
ATOM   4665  C CA   . ILE A 1 748  ? 100.396 70.203  134.977 1.00 24.44 ?  748  ILE A CA   1 
ATOM   4666  C C    . ILE A 1 748  ? 100.920 70.605  133.599 1.00 22.34 ?  748  ILE A C    1 
ATOM   4667  O O    . ILE A 1 748  ? 100.513 70.031  132.580 1.00 24.09 ?  748  ILE A O    1 
ATOM   4668  C CB   . ILE A 1 748  ? 99.072  70.911  135.341 1.00 26.89 ?  748  ILE A CB   1 
ATOM   4669  C CG1  . ILE A 1 748  ? 97.883  70.118  134.796 1.00 23.67 ?  748  ILE A CG1  1 
ATOM   4670  C CG2  . ILE A 1 748  ? 99.017  72.339  134.815 1.00 23.90 ?  748  ILE A CG2  1 
ATOM   4671  C CD1  . ILE A 1 748  ? 96.629  70.245  135.632 1.00 19.63 ?  748  ILE A CD1  1 
ATOM   4672  N N    . VAL A 1 749  ? 101.860 71.557  133.544 1.00 19.87 ?  749  VAL A N    1 
ATOM   4673  C CA   . VAL A 1 749  ? 102.508 71.896  132.278 1.00 24.11 ?  749  VAL A CA   1 
ATOM   4674  C C    . VAL A 1 749  ? 103.317 70.711  131.761 1.00 25.24 ?  749  VAL A C    1 
ATOM   4675  O O    . VAL A 1 749  ? 103.255 70.366  130.576 1.00 24.26 ?  749  VAL A O    1 
ATOM   4676  C CB   . VAL A 1 749  ? 103.376 73.159  132.449 1.00 26.12 ?  749  VAL A CB   1 
ATOM   4677  C CG1  . VAL A 1 749  ? 104.484 73.212  131.404 1.00 22.88 ?  749  VAL A CG1  1 
ATOM   4678  C CG2  . VAL A 1 749  ? 102.511 74.408  132.374 1.00 26.76 ?  749  VAL A CG2  1 
ATOM   4679  N N    . LYS A 1 750  ? 104.071 70.055  132.648 1.00 26.79 ?  750  LYS A N    1 
ATOM   4680  C CA   . LYS A 1 750  ? 104.822 68.866  132.253 1.00 29.15 ?  750  LYS A CA   1 
ATOM   4681  C C    . LYS A 1 750  ? 103.901 67.694  131.932 1.00 28.33 ?  750  LYS A C    1 
ATOM   4682  O O    . LYS A 1 750  ? 104.233 66.865  131.079 1.00 28.06 ?  750  LYS A O    1 
ATOM   4683  C CB   . LYS A 1 750  ? 105.811 68.480  133.352 1.00 26.50 ?  750  LYS A CB   1 
ATOM   4684  C CG   . LYS A 1 750  ? 107.018 69.398  133.449 1.00 24.91 ?  750  LYS A CG   1 
ATOM   4685  C CD   . LYS A 1 750  ? 108.067 69.039  132.411 1.00 26.63 ?  750  LYS A CD   1 
ATOM   4686  C CE   . LYS A 1 750  ? 108.666 67.669  132.685 1.00 30.34 ?  750  LYS A CE   1 
ATOM   4687  N NZ   . LYS A 1 750  ? 109.692 67.297  131.672 1.00 29.65 ?  750  LYS A NZ   1 
ATOM   4688  N N    . ILE A 1 751  ? 102.749 67.607  132.602 1.00 24.15 ?  751  ILE A N    1 
ATOM   4689  C CA   . ILE A 1 751  ? 101.764 66.582  132.267 1.00 25.65 ?  751  ILE A CA   1 
ATOM   4690  C C    . ILE A 1 751  ? 101.248 66.788  130.847 1.00 27.94 ?  751  ILE A C    1 
ATOM   4691  O O    . ILE A 1 751  ? 101.115 65.833  130.072 1.00 24.98 ?  751  ILE A O    1 
ATOM   4692  C CB   . ILE A 1 751  ? 100.622 66.584  133.303 1.00 25.19 ?  751  ILE A CB   1 
ATOM   4693  C CG1  . ILE A 1 751  ? 101.071 65.890  134.591 1.00 26.26 ?  751  ILE A CG1  1 
ATOM   4694  C CG2  . ILE A 1 751  ? 99.372  65.911  132.752 1.00 24.97 ?  751  ILE A CG2  1 
ATOM   4695  C CD1  . ILE A 1 751  ? 101.540 64.465  134.388 1.00 25.72 ?  751  ILE A CD1  1 
ATOM   4696  N N    . LEU A 1 752  ? 100.963 68.042  130.482 1.00 24.49 ?  752  LEU A N    1 
ATOM   4697  C CA   . LEU A 1 752  ? 100.589 68.350  129.104 1.00 24.51 ?  752  LEU A CA   1 
ATOM   4698  C C    . LEU A 1 752  ? 101.735 68.055  128.140 1.00 28.82 ?  752  LEU A C    1 
ATOM   4699  O O    . LEU A 1 752  ? 101.512 67.555  127.031 1.00 26.57 ?  752  LEU A O    1 
ATOM   4700  C CB   . LEU A 1 752  ? 100.156 69.812  128.993 1.00 23.52 ?  752  LEU A CB   1 
ATOM   4701  C CG   . LEU A 1 752  ? 99.699  70.299  127.616 1.00 23.64 ?  752  LEU A CG   1 
ATOM   4702  C CD1  . LEU A 1 752  ? 98.614  69.393  127.052 1.00 22.88 ?  752  LEU A CD1  1 
ATOM   4703  C CD2  . LEU A 1 752  ? 99.217  71.740  127.687 1.00 22.61 ?  752  LEU A CD2  1 
ATOM   4704  N N    . GLY A 1 753  ? 102.969 68.353  128.549 1.00 25.69 ?  753  GLY A N    1 
ATOM   4705  C CA   . GLY A 1 753  ? 104.138 68.121  127.716 1.00 24.61 ?  753  GLY A CA   1 
ATOM   4706  C C    . GLY A 1 753  ? 104.539 66.667  127.578 1.00 26.32 ?  753  GLY A C    1 
ATOM   4707  O O    . GLY A 1 753  ? 105.375 66.354  126.724 1.00 24.72 ?  753  GLY A O    1 
ATOM   4708  N N    . LEU A 1 754  ? 103.985 65.785  128.414 1.00 24.14 ?  754  LEU A N    1 
ATOM   4709  C CA   . LEU A 1 754  ? 104.211 64.352  128.240 1.00 26.10 ?  754  LEU A CA   1 
ATOM   4710  C C    . LEU A 1 754  ? 103.686 63.859  126.896 1.00 30.32 ?  754  LEU A C    1 
ATOM   4711  O O    . LEU A 1 754  ? 104.188 62.863  126.362 1.00 30.91 ?  754  LEU A O    1 
ATOM   4712  C CB   . LEU A 1 754  ? 103.558 63.569  129.380 1.00 24.40 ?  754  LEU A CB   1 
ATOM   4713  C CG   . LEU A 1 754  ? 104.251 63.605  130.743 1.00 27.61 ?  754  LEU A CG   1 
ATOM   4714  C CD1  . LEU A 1 754  ? 103.577 62.646  131.713 1.00 25.09 ?  754  LEU A CD1  1 
ATOM   4715  C CD2  . LEU A 1 754  ? 105.731 63.280  130.605 1.00 28.38 ?  754  LEU A CD2  1 
ATOM   4716  N N    . GLY A 1 755  ? 102.684 64.536  126.338 1.00 25.87 ?  755  GLY A N    1 
ATOM   4717  C CA   . GLY A 1 755  ? 102.165 64.226  125.024 1.00 24.84 ?  755  GLY A CA   1 
ATOM   4718  C C    . GLY A 1 755  ? 102.950 64.795  123.866 1.00 22.72 ?  755  GLY A C    1 
ATOM   4719  O O    . GLY A 1 755  ? 102.564 64.593  122.711 1.00 21.05 ?  755  GLY A O    1 
ATOM   4720  N N    . ARG A 1 756  ? 104.046 65.505  124.135 1.00 20.76 ?  756  ARG A N    1 
ATOM   4721  C CA   . ARG A 1 756  ? 104.895 66.067  123.091 1.00 24.40 ?  756  ARG A CA   1 
ATOM   4722  C C    . ARG A 1 756  ? 105.902 65.064  122.540 1.00 28.71 ?  756  ARG A C    1 
ATOM   4723  O O    . ARG A 1 756  ? 106.846 65.475  121.854 1.00 28.36 ?  756  ARG A O    1 
ATOM   4724  C CB   . ARG A 1 756  ? 105.631 67.303  123.615 1.00 23.46 ?  756  ARG A CB   1 
ATOM   4725  N N    . HIS A 1 757  ? 105.731 63.776  122.851 1.00 32.43 ?  757  HIS A N    1 
ATOM   4726  C CA   . HIS A 1 757  ? 106.504 62.664  122.295 1.00 33.47 ?  757  HIS A CA   1 
ATOM   4727  C C    . HIS A 1 757  ? 107.989 62.729  122.646 1.00 31.02 ?  757  HIS A C    1 
ATOM   4728  O O    . HIS A 1 757  ? 108.803 62.073  121.985 1.00 27.94 ?  757  HIS A O    1 
ATOM   4729  C CB   . HIS A 1 757  ? 106.326 62.566  120.773 1.00 30.32 ?  757  HIS A CB   1 
ATOM   4730  C CG   . HIS A 1 757  ? 104.930 62.846  120.309 1.00 32.20 ?  757  HIS A CG   1 
ATOM   4731  N ND1  . HIS A 1 757  ? 103.878 61.990  120.554 1.00 34.78 ?  757  HIS A ND1  1 
ATOM   4732  C CD2  . HIS A 1 757  ? 104.413 63.889  119.617 1.00 29.75 ?  757  HIS A CD2  1 
ATOM   4733  C CE1  . HIS A 1 757  ? 102.773 62.492  120.031 1.00 36.22 ?  757  HIS A CE1  1 
ATOM   4734  N NE2  . HIS A 1 757  ? 103.071 63.644  119.457 1.00 34.63 ?  757  HIS A NE2  1 
ATOM   4735  N N    . TYR A 1 758  ? 108.347 63.499  123.683 1.00 29.69 ?  758  TYR A N    1 
ATOM   4736  C CA   . TYR A 1 758  ? 109.717 63.575  124.207 1.00 29.10 ?  758  TYR A CA   1 
ATOM   4737  C C    . TYR A 1 758  ? 110.717 63.969  123.119 1.00 30.21 ?  758  TYR A C    1 
ATOM   4738  O O    . TYR A 1 758  ? 111.811 63.409  123.023 1.00 29.26 ?  758  TYR A O    1 
ATOM   4739  C CB   . TYR A 1 758  ? 110.119 62.254  124.870 1.00 29.33 ?  758  TYR A CB   1 
ATOM   4740  C CG   . TYR A 1 758  ? 111.234 62.365  125.885 1.00 30.12 ?  758  TYR A CG   1 
ATOM   4741  C CD1  . TYR A 1 758  ? 111.131 63.230  126.967 1.00 28.42 ?  758  TYR A CD1  1 
ATOM   4742  C CD2  . TYR A 1 758  ? 112.384 61.594  125.769 1.00 31.08 ?  758  TYR A CD2  1 
ATOM   4743  C CE1  . TYR A 1 758  ? 112.146 63.330  127.901 1.00 29.69 ?  758  TYR A CE1  1 
ATOM   4744  C CE2  . TYR A 1 758  ? 113.403 61.687  126.697 1.00 30.71 ?  758  TYR A CE2  1 
ATOM   4745  C CZ   . TYR A 1 758  ? 113.279 62.556  127.760 1.00 31.27 ?  758  TYR A CZ   1 
ATOM   4746  O OH   . TYR A 1 758  ? 114.291 62.650  128.686 1.00 28.28 ?  758  TYR A OH   1 
ATOM   4747  N N    . ILE A 1 759  ? 110.328 64.937  122.283 1.00 29.14 ?  759  ILE A N    1 
ATOM   4748  C CA   . ILE A 1 759  ? 111.125 65.271  121.105 1.00 30.94 ?  759  ILE A CA   1 
ATOM   4749  C C    . ILE A 1 759  ? 112.435 65.956  121.478 1.00 29.89 ?  759  ILE A C    1 
ATOM   4750  O O    . ILE A 1 759  ? 113.503 65.570  120.988 1.00 25.78 ?  759  ILE A O    1 
ATOM   4751  C CB   . ILE A 1 759  ? 110.317 66.171  120.150 1.00 30.00 ?  759  ILE A CB   1 
ATOM   4752  N N    . VAL A 1 760  ? 112.380 66.971  122.342 1.00 26.12 ?  760  VAL A N    1 
ATOM   4753  C CA   . VAL A 1 760  ? 113.586 67.713  122.692 1.00 24.55 ?  760  VAL A CA   1 
ATOM   4754  C C    . VAL A 1 760  ? 114.404 66.923  123.705 1.00 25.63 ?  760  VAL A C    1 
ATOM   4755  O O    . VAL A 1 760  ? 113.858 66.267  124.604 1.00 23.95 ?  760  VAL A O    1 
ATOM   4756  C CB   . VAL A 1 760  ? 113.227 69.115  123.214 1.00 26.00 ?  760  VAL A CB   1 
ATOM   4757  C CG1  . VAL A 1 760  ? 112.727 69.985  122.073 1.00 26.49 ?  760  VAL A CG1  1 
ATOM   4758  C CG2  . VAL A 1 760  ? 112.167 69.028  124.294 1.00 24.42 ?  760  VAL A CG2  1 
ATOM   4759  N N    . SER A 1 761  ? 115.727 66.972  123.554 1.00 26.41 ?  761  SER A N    1 
ATOM   4760  C CA   . SER A 1 761  ? 116.644 66.165  124.350 1.00 23.46 ?  761  SER A CA   1 
ATOM   4761  C C    . SER A 1 761  ? 117.122 66.872  125.612 1.00 23.66 ?  761  SER A C    1 
ATOM   4762  O O    . SER A 1 761  ? 117.057 66.301  126.703 1.00 24.97 ?  761  SER A O    1 
ATOM   4763  C CB   . SER A 1 761  ? 117.853 65.756  123.498 1.00 21.63 ?  761  SER A CB   1 
ATOM   4764  O OG   . SER A 1 761  ? 117.468 64.888  122.447 1.00 25.39 ?  761  SER A OG   1 
ATOM   4765  N N    . HIS A 1 762  ? 117.601 68.108  125.488 1.00 28.87 ?  762  HIS A N    1 
ATOM   4766  C CA   . HIS A 1 762  ? 118.193 68.825  126.613 1.00 32.66 ?  762  HIS A CA   1 
ATOM   4767  C C    . HIS A 1 762  ? 117.142 69.479  127.505 1.00 32.45 ?  762  HIS A C    1 
ATOM   4768  O O    . HIS A 1 762  ? 117.153 69.289  128.728 1.00 30.43 ?  762  HIS A O    1 
ATOM   4769  C CB   . HIS A 1 762  ? 119.175 69.880  126.091 1.00 30.25 ?  762  HIS A CB   1 
ATOM   4770  C CG   . HIS A 1 762  ? 120.022 70.503  127.156 1.00 31.65 ?  762  HIS A CG   1 
ATOM   4771  N ND1  . HIS A 1 762  ? 119.557 71.496  127.991 1.00 29.38 ?  762  HIS A ND1  1 
ATOM   4772  C CD2  . HIS A 1 762  ? 121.307 70.277  127.520 1.00 30.22 ?  762  HIS A CD2  1 
ATOM   4773  C CE1  . HIS A 1 762  ? 120.518 71.854  128.824 1.00 29.77 ?  762  HIS A CE1  1 
ATOM   4774  N NE2  . HIS A 1 762  ? 121.590 71.129  128.560 1.00 31.47 ?  762  HIS A NE2  1 
ATOM   4775  N N    . TRP A 1 763  ? 116.231 70.248  126.906 1.00 29.82 ?  763  TRP A N    1 
ATOM   4776  C CA   . TRP A 1 763  ? 115.302 71.050  127.695 1.00 30.57 ?  763  TRP A CA   1 
ATOM   4777  C C    . TRP A 1 763  ? 114.267 70.183  128.401 1.00 29.37 ?  763  TRP A C    1 
ATOM   4778  O O    . TRP A 1 763  ? 113.887 70.474  129.540 1.00 27.85 ?  763  TRP A O    1 
ATOM   4779  C CB   . TRP A 1 763  ? 114.634 72.097  126.804 1.00 29.64 ?  763  TRP A CB   1 
ATOM   4780  C CG   . TRP A 1 763  ? 115.611 72.815  125.912 1.00 31.05 ?  763  TRP A CG   1 
ATOM   4781  C CD1  . TRP A 1 763  ? 115.620 72.822  124.548 1.00 28.05 ?  763  TRP A CD1  1 
ATOM   4782  C CD2  . TRP A 1 763  ? 116.726 73.620  126.325 1.00 30.85 ?  763  TRP A CD2  1 
ATOM   4783  N NE1  . TRP A 1 763  ? 116.666 73.583  124.085 1.00 28.02 ?  763  TRP A NE1  1 
ATOM   4784  C CE2  . TRP A 1 763  ? 117.360 74.084  125.155 1.00 27.45 ?  763  TRP A CE2  1 
ATOM   4785  C CE3  . TRP A 1 763  ? 117.246 73.996  127.568 1.00 29.33 ?  763  TRP A CE3  1 
ATOM   4786  C CZ2  . TRP A 1 763  ? 118.487 74.902  125.192 1.00 25.71 ?  763  TRP A CZ2  1 
ATOM   4787  C CZ3  . TRP A 1 763  ? 118.366 74.808  127.601 1.00 26.99 ?  763  TRP A CZ3  1 
ATOM   4788  C CH2  . TRP A 1 763  ? 118.974 75.252  126.421 1.00 25.99 ?  763  TRP A CH2  1 
ATOM   4789  N N    . ASN A 1 764  ? 113.806 69.110  127.751 1.00 25.64 ?  764  ASN A N    1 
ATOM   4790  C CA   . ASN A 1 764  ? 112.878 68.195  128.413 1.00 27.07 ?  764  ASN A CA   1 
ATOM   4791  C C    . ASN A 1 764  ? 113.539 67.495  129.593 1.00 24.49 ?  764  ASN A C    1 
ATOM   4792  O O    . ASN A 1 764  ? 112.921 67.339  130.652 1.00 25.22 ?  764  ASN A O    1 
ATOM   4793  C CB   . ASN A 1 764  ? 112.338 67.169  127.419 1.00 28.75 ?  764  ASN A CB   1 
ATOM   4794  C CG   . ASN A 1 764  ? 110.858 67.352  127.142 1.00 28.22 ?  764  ASN A CG   1 
ATOM   4795  O OD1  . ASN A 1 764  ? 110.248 68.324  127.586 1.00 25.77 ?  764  ASN A OD1  1 
ATOM   4796  N ND2  . ASN A 1 764  ? 110.273 66.414  126.406 1.00 25.28 ?  764  ASN A ND2  1 
ATOM   4797  N N    . LYS A 1 765  ? 114.796 67.072  129.431 1.00 21.77 ?  765  LYS A N    1 
ATOM   4798  C CA   . LYS A 1 765  ? 115.520 66.443  130.533 1.00 27.99 ?  765  LYS A CA   1 
ATOM   4799  C C    . LYS A 1 765  ? 115.708 67.410  131.694 1.00 29.15 ?  765  LYS A C    1 
ATOM   4800  O O    . LYS A 1 765  ? 115.512 67.042  132.860 1.00 29.01 ?  765  LYS A O    1 
ATOM   4801  C CB   . LYS A 1 765  ? 116.877 65.933  130.047 1.00 25.46 ?  765  LYS A CB   1 
ATOM   4802  C CG   . LYS A 1 765  ? 116.852 64.548  129.426 1.00 24.96 ?  765  LYS A CG   1 
ATOM   4803  C CD   . LYS A 1 765  ? 118.234 64.156  128.925 1.00 25.49 ?  765  LYS A CD   1 
ATOM   4804  C CE   . LYS A 1 765  ? 118.148 63.181  127.762 1.00 26.14 ?  765  LYS A CE   1 
ATOM   4805  N NZ   . LYS A 1 765  ? 119.486 62.911  127.164 1.00 23.39 ?  765  LYS A NZ   1 
ATOM   4806  N N    . PHE A 1 766  ? 116.080 68.658  131.394 1.00 26.48 ?  766  PHE A N    1 
ATOM   4807  C CA   . PHE A 1 766  ? 116.296 69.635  132.457 1.00 25.38 ?  766  PHE A CA   1 
ATOM   4808  C C    . PHE A 1 766  ? 114.989 69.998  133.154 1.00 28.26 ?  766  PHE A C    1 
ATOM   4809  O O    . PHE A 1 766  ? 114.959 70.159  134.379 1.00 27.77 ?  766  PHE A O    1 
ATOM   4810  C CB   . PHE A 1 766  ? 116.985 70.877  131.893 1.00 26.67 ?  766  PHE A CB   1 
ATOM   4811  C CG   . PHE A 1 766  ? 118.489 70.801  131.924 1.00 28.46 ?  766  PHE A CG   1 
ATOM   4812  C CD1  . PHE A 1 766  ? 119.142 69.607  131.663 1.00 26.15 ?  766  PHE A CD1  1 
ATOM   4813  C CD2  . PHE A 1 766  ? 119.248 71.922  132.216 1.00 26.51 ?  766  PHE A CD2  1 
ATOM   4814  C CE1  . PHE A 1 766  ? 120.523 69.532  131.692 1.00 26.46 ?  766  PHE A CE1  1 
ATOM   4815  C CE2  . PHE A 1 766  ? 120.629 71.854  132.247 1.00 26.69 ?  766  PHE A CE2  1 
ATOM   4816  C CZ   . PHE A 1 766  ? 121.267 70.658  131.984 1.00 28.92 ?  766  PHE A CZ   1 
ATOM   4817  N N    . ASP A 1 767  ? 113.894 70.113  132.396 1.00 28.63 ?  767  ASP A N    1 
ATOM   4818  C CA   . ASP A 1 767  ? 112.596 70.396  133.001 1.00 29.05 ?  767  ASP A CA   1 
ATOM   4819  C C    . ASP A 1 767  ? 112.113 69.228  133.852 1.00 28.67 ?  767  ASP A C    1 
ATOM   4820  O O    . ASP A 1 767  ? 111.507 69.435  134.910 1.00 28.30 ?  767  ASP A O    1 
ATOM   4821  C CB   . ASP A 1 767  ? 111.574 70.732  131.915 1.00 27.17 ?  767  ASP A CB   1 
ATOM   4822  C CG   . ASP A 1 767  ? 110.608 71.821  132.340 1.00 30.73 ?  767  ASP A CG   1 
ATOM   4823  O OD1  . ASP A 1 767  ? 110.118 71.770  133.488 1.00 31.50 ?  767  ASP A OD1  1 
ATOM   4824  O OD2  . ASP A 1 767  ? 110.338 72.728  131.526 1.00 30.48 ?  767  ASP A OD2  1 
ATOM   4825  N N    . ALA A 1 768  ? 112.366 67.993  133.408 1.00 23.25 ?  768  ALA A N    1 
ATOM   4826  C CA   . ALA A 1 768  ? 112.006 66.827  134.208 1.00 25.45 ?  768  ALA A CA   1 
ATOM   4827  C C    . ALA A 1 768  ? 112.809 66.775  135.501 1.00 30.40 ?  768  ALA A C    1 
ATOM   4828  O O    . ALA A 1 768  ? 112.267 66.446  136.562 1.00 29.86 ?  768  ALA A O    1 
ATOM   4829  C CB   . ALA A 1 768  ? 112.209 65.549  133.395 1.00 22.72 ?  768  ALA A CB   1 
ATOM   4830  N N    . PHE A 1 769  ? 114.104 67.097  135.431 1.00 28.08 ?  769  PHE A N    1 
ATOM   4831  C CA   . PHE A 1 769  ? 114.920 67.158  136.641 1.00 27.52 ?  769  PHE A CA   1 
ATOM   4832  C C    . PHE A 1 769  ? 114.431 68.255  137.581 1.00 27.00 ?  769  PHE A C    1 
ATOM   4833  O O    . PHE A 1 769  ? 114.400 68.070  138.805 1.00 22.53 ?  769  PHE A O    1 
ATOM   4834  C CB   . PHE A 1 769  ? 116.387 67.375  136.268 1.00 27.34 ?  769  PHE A CB   1 
ATOM   4835  C CG   . PHE A 1 769  ? 117.270 67.718  137.434 1.00 31.27 ?  769  PHE A CG   1 
ATOM   4836  C CD1  . PHE A 1 769  ? 117.644 66.744  138.345 1.00 30.06 ?  769  PHE A CD1  1 
ATOM   4837  C CD2  . PHE A 1 769  ? 117.736 69.011  137.612 1.00 28.37 ?  769  PHE A CD2  1 
ATOM   4838  C CE1  . PHE A 1 769  ? 118.459 67.054  139.418 1.00 29.18 ?  769  PHE A CE1  1 
ATOM   4839  C CE2  . PHE A 1 769  ? 118.552 69.328  138.683 1.00 27.10 ?  769  PHE A CE2  1 
ATOM   4840  C CZ   . PHE A 1 769  ? 118.914 68.348  139.587 1.00 26.59 ?  769  PHE A CZ   1 
ATOM   4841  N N    . ILE A 1 770  ? 114.037 69.403  137.020 1.00 24.80 ?  770  ILE A N    1 
ATOM   4842  C CA   . ILE A 1 770  ? 113.504 70.500  137.824 1.00 26.87 ?  770  ILE A CA   1 
ATOM   4843  C C    . ILE A 1 770  ? 112.213 70.077  138.516 1.00 27.58 ?  770  ILE A C    1 
ATOM   4844  O O    . ILE A 1 770  ? 112.006 70.361  139.702 1.00 25.50 ?  770  ILE A O    1 
ATOM   4845  C CB   . ILE A 1 770  ? 113.305 71.748  136.939 1.00 27.85 ?  770  ILE A CB   1 
ATOM   4846  C CG1  . ILE A 1 770  ? 114.605 72.549  136.850 1.00 26.84 ?  770  ILE A CG1  1 
ATOM   4847  C CG2  . ILE A 1 770  ? 112.173 72.629  137.458 1.00 29.42 ?  770  ILE A CG2  1 
ATOM   4848  C CD1  . ILE A 1 770  ? 114.506 73.777  135.972 1.00 27.87 ?  770  ILE A CD1  1 
ATOM   4849  N N    . LEU A 1 771  ? 111.333 69.380  137.791 1.00 25.18 ?  771  LEU A N    1 
ATOM   4850  C CA   . LEU A 1 771  ? 110.086 68.900  138.382 1.00 26.08 ?  771  LEU A CA   1 
ATOM   4851  C C    . LEU A 1 771  ? 110.344 67.859  139.465 1.00 26.57 ?  771  LEU A C    1 
ATOM   4852  O O    . LEU A 1 771  ? 109.651 67.837  140.489 1.00 26.59 ?  771  LEU A O    1 
ATOM   4853  C CB   . LEU A 1 771  ? 109.178 68.326  137.296 1.00 27.00 ?  771  LEU A CB   1 
ATOM   4854  C CG   . LEU A 1 771  ? 107.680 68.531  137.526 1.00 30.29 ?  771  LEU A CG   1 
ATOM   4855  C CD1  . LEU A 1 771  ? 107.277 69.940  137.127 1.00 26.18 ?  771  LEU A CD1  1 
ATOM   4856  C CD2  . LEU A 1 771  ? 106.866 67.495  136.767 1.00 26.81 ?  771  LEU A CD2  1 
ATOM   4857  N N    . VAL A 1 772  ? 111.327 66.980  139.248 1.00 25.07 ?  772  VAL A N    1 
ATOM   4858  C CA   . VAL A 1 772  ? 111.677 65.975  140.250 1.00 27.06 ?  772  VAL A CA   1 
ATOM   4859  C C    . VAL A 1 772  ? 112.185 66.645  141.521 1.00 26.19 ?  772  VAL A C    1 
ATOM   4860  O O    . VAL A 1 772  ? 111.808 66.262  142.637 1.00 25.43 ?  772  VAL A O    1 
ATOM   4861  C CB   . VAL A 1 772  ? 112.707 64.986  139.668 1.00 26.48 ?  772  VAL A CB   1 
ATOM   4862  C CG1  . VAL A 1 772  ? 113.472 64.270  140.774 1.00 22.81 ?  772  VAL A CG1  1 
ATOM   4863  C CG2  . VAL A 1 772  ? 112.018 63.980  138.759 1.00 24.24 ?  772  VAL A CG2  1 
ATOM   4864  N N    . VAL A 1 773  ? 113.036 67.664  141.373 1.00 21.27 ?  773  VAL A N    1 
ATOM   4865  C CA   . VAL A 1 773  ? 113.535 68.396  142.535 1.00 20.87 ?  773  VAL A CA   1 
ATOM   4866  C C    . VAL A 1 773  ? 112.400 69.133  143.241 1.00 22.24 ?  773  VAL A C    1 
ATOM   4867  O O    . VAL A 1 773  ? 112.301 69.114  144.474 1.00 24.94 ?  773  VAL A O    1 
ATOM   4868  C CB   . VAL A 1 773  ? 114.665 69.354  142.110 1.00 20.71 ?  773  VAL A CB   1 
ATOM   4869  C CG1  . VAL A 1 773  ? 114.988 70.343  143.221 1.00 19.01 ?  773  VAL A CG1  1 
ATOM   4870  C CG2  . VAL A 1 773  ? 115.906 68.566  141.721 1.00 22.24 ?  773  VAL A CG2  1 
ATOM   4871  N N    . ALA A 1 774  ? 111.513 69.772  142.472 1.00 21.48 ?  774  ALA A N    1 
ATOM   4872  C CA   . ALA A 1 774  ? 110.450 70.579  143.064 1.00 26.67 ?  774  ALA A CA   1 
ATOM   4873  C C    . ALA A 1 774  ? 109.384 69.725  143.738 1.00 25.54 ?  774  ALA A C    1 
ATOM   4874  O O    . ALA A 1 774  ? 108.726 70.189  144.676 1.00 20.86 ?  774  ALA A O    1 
ATOM   4875  C CB   . ALA A 1 774  ? 109.815 71.467  141.995 1.00 24.60 ?  774  ALA A CB   1 
ATOM   4876  N N    . LEU A 1 775  ? 109.192 68.485  143.280 1.00 26.47 ?  775  LEU A N    1 
ATOM   4877  C CA   . LEU A 1 775  ? 108.184 67.622  143.884 1.00 27.13 ?  775  LEU A CA   1 
ATOM   4878  C C    . LEU A 1 775  ? 108.601 67.113  145.259 1.00 25.71 ?  775  LEU A C    1 
ATOM   4879  O O    . LEU A 1 775  ? 107.750 66.617  146.005 1.00 21.55 ?  775  LEU A O    1 
ATOM   4880  C CB   . LEU A 1 775  ? 107.879 66.440  142.962 1.00 23.57 ?  775  LEU A CB   1 
ATOM   4881  C CG   . LEU A 1 775  ? 106.543 66.489  142.216 1.00 24.57 ?  775  LEU A CG   1 
ATOM   4882  C CD1  . LEU A 1 775  ? 105.382 66.306  143.182 1.00 21.04 ?  775  LEU A CD1  1 
ATOM   4883  C CD2  . LEU A 1 775  ? 106.398 67.789  141.439 1.00 25.69 ?  775  LEU A CD2  1 
ATOM   4884  N N    . VAL A 1 776  ? 109.878 67.222  145.608 1.00 24.89 ?  776  VAL A N    1 
ATOM   4885  C CA   . VAL A 1 776  ? 110.355 66.789  146.915 1.00 25.07 ?  776  VAL A CA   1 
ATOM   4886  C C    . VAL A 1 776  ? 110.408 67.974  147.872 1.00 26.34 ?  776  VAL A C    1 
ATOM   4887  O O    . VAL A 1 776  ? 110.151 69.113  147.481 1.00 22.93 ?  776  VAL A O    1 
ATOM   4888  C CB   . VAL A 1 776  ? 111.731 66.111  146.810 1.00 22.62 ?  776  VAL A CB   1 
ATOM   4889  C CG1  . VAL A 1 776  ? 112.320 65.887  148.194 1.00 18.60 ?  776  VAL A CG1  1 
ATOM   4890  C CG2  . VAL A 1 776  ? 111.618 64.797  146.053 1.00 23.61 ?  776  VAL A CG2  1 
ATOM   4891  N N    . LYS A 1 797  ? 121.914 68.119  158.350 1.00 23.79 ?  797  LYS A N    1 
ATOM   4892  C CA   . LYS A 1 797  ? 121.447 69.450  157.981 1.00 28.19 ?  797  LYS A CA   1 
ATOM   4893  C C    . LYS A 1 797  ? 121.151 69.535  156.487 1.00 28.80 ?  797  LYS A C    1 
ATOM   4894  O O    . LYS A 1 797  ? 121.501 70.517  155.833 1.00 29.95 ?  797  LYS A O    1 
ATOM   4895  C CB   . LYS A 1 797  ? 122.479 70.509  158.372 1.00 29.43 ?  797  LYS A CB   1 
ATOM   4896  C CG   . LYS A 1 797  ? 122.873 70.487  159.840 1.00 30.79 ?  797  LYS A CG   1 
ATOM   4897  C CD   . LYS A 1 797  ? 123.983 71.486  160.126 1.00 27.65 ?  797  LYS A CD   1 
ATOM   4898  C CE   . LYS A 1 797  ? 124.289 71.564  161.613 1.00 27.67 ?  797  LYS A CE   1 
ATOM   4899  N NZ   . LYS A 1 797  ? 125.276 72.637  161.919 1.00 26.53 ?  797  LYS A NZ   1 
ATOM   4900  N N    . VAL A 1 798  ? 120.502 68.498  155.950 1.00 27.85 ?  798  VAL A N    1 
ATOM   4901  C CA   . VAL A 1 798  ? 120.165 68.478  154.528 1.00 27.29 ?  798  VAL A CA   1 
ATOM   4902  C C    . VAL A 1 798  ? 118.975 69.363  154.192 1.00 28.38 ?  798  VAL A C    1 
ATOM   4903  O O    . VAL A 1 798  ? 118.753 69.659  153.011 1.00 22.47 ?  798  VAL A O    1 
ATOM   4904  C CB   . VAL A 1 798  ? 119.896 67.038  154.050 1.00 25.05 ?  798  VAL A CB   1 
ATOM   4905  C CG1  . VAL A 1 798  ? 120.963 66.096  154.586 1.00 24.14 ?  798  VAL A CG1  1 
ATOM   4906  C CG2  . VAL A 1 798  ? 118.509 66.574  154.477 1.00 22.07 ?  798  VAL A CG2  1 
ATOM   4907  N N    . VAL A 1 799  ? 118.207 69.797  155.194 1.00 28.65 ?  799  VAL A N    1 
ATOM   4908  C CA   . VAL A 1 799  ? 117.077 70.685  154.936 1.00 27.87 ?  799  VAL A CA   1 
ATOM   4909  C C    . VAL A 1 799  ? 117.567 72.056  154.489 1.00 27.10 ?  799  VAL A C    1 
ATOM   4910  O O    . VAL A 1 799  ? 116.976 72.683  153.602 1.00 24.74 ?  799  VAL A O    1 
ATOM   4911  C CB   . VAL A 1 799  ? 116.177 70.782  156.180 1.00 25.44 ?  799  VAL A CB   1 
ATOM   4912  C CG1  . VAL A 1 799  ? 114.796 71.289  155.797 1.00 26.17 ?  799  VAL A CG1  1 
ATOM   4913  C CG2  . VAL A 1 799  ? 116.081 69.430  156.871 1.00 21.52 ?  799  VAL A CG2  1 
ATOM   4914  N N    . LYS A 1 800  ? 118.656 72.541  155.091 1.00 27.48 ?  800  LYS A N    1 
ATOM   4915  C CA   . LYS A 1 800  ? 119.229 73.818  154.678 1.00 30.34 ?  800  LYS A CA   1 
ATOM   4916  C C    . LYS A 1 800  ? 119.760 73.750  153.251 1.00 30.15 ?  800  LYS A C    1 
ATOM   4917  O O    . LYS A 1 800  ? 119.651 74.723  152.495 1.00 26.39 ?  800  LYS A O    1 
ATOM   4918  C CB   . LYS A 1 800  ? 120.335 74.233  155.649 1.00 28.08 ?  800  LYS A CB   1 
ATOM   4919  C CG   . LYS A 1 800  ? 119.916 74.195  157.111 1.00 27.89 ?  800  LYS A CG   1 
ATOM   4920  C CD   . LYS A 1 800  ? 120.384 75.434  157.856 1.00 27.31 ?  800  LYS A CD   1 
ATOM   4921  C CE   . LYS A 1 800  ? 121.891 75.426  158.052 1.00 25.80 ?  800  LYS A CE   1 
ATOM   4922  N NZ   . LYS A 1 800  ? 122.315 74.399  159.043 1.00 25.96 ?  800  LYS A NZ   1 
ATOM   4923  N N    . LEU A 1 801  ? 120.348 72.613  152.869 1.00 26.79 ?  801  LEU A N    1 
ATOM   4924  C CA   . LEU A 1 801  ? 120.795 72.435  151.491 1.00 28.14 ?  801  LEU A CA   1 
ATOM   4925  C C    . LEU A 1 801  ? 119.614 72.364  150.529 1.00 27.27 ?  801  LEU A C    1 
ATOM   4926  O O    . LEU A 1 801  ? 119.662 72.942  149.437 1.00 27.49 ?  801  LEU A O    1 
ATOM   4927  C CB   . LEU A 1 801  ? 121.657 71.178  151.378 1.00 27.22 ?  801  LEU A CB   1 
ATOM   4928  C CG   . LEU A 1 801  ? 123.167 71.377  151.520 1.00 26.04 ?  801  LEU A CG   1 
ATOM   4929  C CD1  . LEU A 1 801  ? 123.571 71.407  152.986 1.00 23.13 ?  801  LEU A CD1  1 
ATOM   4930  C CD2  . LEU A 1 801  ? 123.925 70.291  150.773 1.00 23.74 ?  801  LEU A CD2  1 
ATOM   4931  N N    . PHE A 1 802  ? 118.544 71.663  150.916 1.00 25.32 ?  802  PHE A N    1 
ATOM   4932  C CA   . PHE A 1 802  ? 117.367 71.563  150.060 1.00 27.31 ?  802  PHE A CA   1 
ATOM   4933  C C    . PHE A 1 802  ? 116.600 72.876  149.966 1.00 26.90 ?  802  PHE A C    1 
ATOM   4934  O O    . PHE A 1 802  ? 115.818 73.054  149.026 1.00 24.39 ?  802  PHE A O    1 
ATOM   4935  C CB   . PHE A 1 802  ? 116.439 70.456  150.564 1.00 26.64 ?  802  PHE A CB   1 
ATOM   4936  C CG   . PHE A 1 802  ? 116.588 69.157  149.824 1.00 28.44 ?  802  PHE A CG   1 
ATOM   4937  C CD1  . PHE A 1 802  ? 116.131 69.032  148.521 1.00 27.42 ?  802  PHE A CD1  1 
ATOM   4938  C CD2  . PHE A 1 802  ? 117.184 68.062  150.428 1.00 26.22 ?  802  PHE A CD2  1 
ATOM   4939  C CE1  . PHE A 1 802  ? 116.265 67.838  147.835 1.00 27.33 ?  802  PHE A CE1  1 
ATOM   4940  C CE2  . PHE A 1 802  ? 117.321 66.865  149.748 1.00 27.10 ?  802  PHE A CE2  1 
ATOM   4941  C CZ   . PHE A 1 802  ? 116.861 66.754  148.450 1.00 25.80 ?  802  PHE A CZ   1 
ATOM   4942  N N    . ARG A 1 803  ? 116.794 73.786  150.925 1.00 26.87 ?  803  ARG A N    1 
ATOM   4943  C CA   . ARG A 1 803  ? 116.174 75.105  150.836 1.00 28.94 ?  803  ARG A CA   1 
ATOM   4944  C C    . ARG A 1 803  ? 116.681 75.886  149.629 1.00 27.50 ?  803  ARG A C    1 
ATOM   4945  O O    . ARG A 1 803  ? 115.938 76.688  149.053 1.00 26.90 ?  803  ARG A O    1 
ATOM   4946  C CB   . ARG A 1 803  ? 116.428 75.892  152.123 1.00 25.98 ?  803  ARG A CB   1 
ATOM   4947  C CG   . ARG A 1 803  ? 115.469 75.561  153.255 1.00 26.39 ?  803  ARG A CG   1 
ATOM   4948  C CD   . ARG A 1 803  ? 115.719 76.437  154.473 1.00 28.88 ?  803  ARG A CD   1 
ATOM   4949  N NE   . ARG A 1 803  ? 117.137 76.711  154.669 1.00 25.26 ?  803  ARG A NE   1 
ATOM   4950  C CZ   . ARG A 1 803  ? 117.627 77.467  155.643 1.00 26.01 ?  803  ARG A CZ   1 
ATOM   4951  N NH1  . ARG A 1 803  ? 116.839 78.036  156.540 1.00 24.92 ?  803  ARG A NH1  1 
ATOM   4952  N NH2  . ARG A 1 803  ? 118.942 77.655  155.718 1.00 25.25 ?  803  ARG A NH2  1 
ATOM   4953  N N    . LEU A 1 804  ? 117.936 75.668  149.234 1.00 21.69 ?  804  LEU A N    1 
ATOM   4954  C CA   . LEU A 1 804  ? 118.502 76.305  148.053 1.00 21.40 ?  804  LEU A CA   1 
ATOM   4955  C C    . LEU A 1 804  ? 118.586 75.373  146.851 1.00 24.15 ?  804  LEU A C    1 
ATOM   4956  O O    . LEU A 1 804  ? 118.792 75.854  145.731 1.00 20.61 ?  804  LEU A O    1 
ATOM   4957  C CB   . LEU A 1 804  ? 119.900 76.855  148.365 1.00 20.47 ?  804  LEU A CB   1 
ATOM   4958  C CG   . LEU A 1 804  ? 120.029 77.714  149.623 1.00 22.79 ?  804  LEU A CG   1 
ATOM   4959  C CD1  . LEU A 1 804  ? 121.491 77.994  149.934 1.00 23.06 ?  804  LEU A CD1  1 
ATOM   4960  C CD2  . LEU A 1 804  ? 119.256 79.013  149.463 1.00 21.92 ?  804  LEU A CD2  1 
ATOM   4961  N N    . LEU A 1 805  ? 118.445 74.060  147.056 1.00 25.31 ?  805  LEU A N    1 
ATOM   4962  C CA   . LEU A 1 805  ? 118.472 73.123  145.936 1.00 24.42 ?  805  LEU A CA   1 
ATOM   4963  C C    . LEU A 1 805  ? 117.276 73.326  145.014 1.00 26.18 ?  805  LEU A C    1 
ATOM   4964  O O    . LEU A 1 805  ? 117.405 73.223  143.789 1.00 26.32 ?  805  LEU A O    1 
ATOM   4965  C CB   . LEU A 1 805  ? 118.516 71.686  146.454 1.00 21.93 ?  805  LEU A CB   1 
ATOM   4966  C CG   . LEU A 1 805  ? 119.910 71.089  146.657 1.00 23.14 ?  805  LEU A CG   1 
ATOM   4967  C CD1  . LEU A 1 805  ? 119.819 69.710  147.292 1.00 23.39 ?  805  LEU A CD1  1 
ATOM   4968  C CD2  . LEU A 1 805  ? 120.665 71.028  145.337 1.00 23.33 ?  805  LEU A CD2  1 
ATOM   4969  N N    . ARG A 1 806  ? 116.102 73.609  145.585 1.00 28.32 ?  806  ARG A N    1 
ATOM   4970  C CA   . ARG A 1 806  ? 114.930 73.913  144.773 1.00 28.51 ?  806  ARG A CA   1 
ATOM   4971  C C    . ARG A 1 806  ? 115.051 75.254  144.062 1.00 28.27 ?  806  ARG A C    1 
ATOM   4972  O O    . ARG A 1 806  ? 114.309 75.505  143.107 1.00 27.26 ?  806  ARG A O    1 
ATOM   4973  C CB   . ARG A 1 806  ? 113.669 73.898  145.640 1.00 27.11 ?  806  ARG A CB   1 
ATOM   4974  C CG   . ARG A 1 806  ? 113.229 72.510  146.073 1.00 26.18 ?  806  ARG A CG   1 
ATOM   4975  C CD   . ARG A 1 806  ? 111.829 72.536  146.665 1.00 27.08 ?  806  ARG A CD   1 
ATOM   4976  N NE   . ARG A 1 806  ? 111.760 73.358  147.867 1.00 30.62 ?  806  ARG A NE   1 
ATOM   4977  C CZ   . ARG A 1 806  ? 112.060 72.930  149.086 1.00 27.94 ?  806  ARG A CZ   1 
ATOM   4978  N NH1  . ARG A 1 806  ? 112.452 71.686  149.305 1.00 23.24 ?  806  ARG A NH1  1 
ATOM   4979  N NH2  . ARG A 1 806  ? 111.963 73.772  150.111 1.00 25.91 ?  806  ARG A NH2  1 
ATOM   4980  N N    . GLY A 1 807  ? 115.966 76.118  144.504 1.00 26.24 ?  807  GLY A N    1 
ATOM   4981  C CA   . GLY A 1 807  ? 116.185 77.393  143.851 1.00 25.98 ?  807  GLY A CA   1 
ATOM   4982  C C    . GLY A 1 807  ? 116.950 77.324  142.550 1.00 26.67 ?  807  GLY A C    1 
ATOM   4983  O O    . GLY A 1 807  ? 117.036 78.333  141.844 1.00 26.12 ?  807  GLY A O    1 
ATOM   4984  N N    . LEU A 1 808  ? 117.510 76.160  142.214 1.00 24.91 ?  808  LEU A N    1 
ATOM   4985  C CA   . LEU A 1 808  ? 118.215 75.980  140.946 1.00 26.01 ?  808  LEU A CA   1 
ATOM   4986  C C    . LEU A 1 808  ? 117.168 75.682  139.871 1.00 27.39 ?  808  LEU A C    1 
ATOM   4987  O O    . LEU A 1 808  ? 116.937 74.543  139.458 1.00 30.97 ?  808  LEU A O    1 
ATOM   4988  C CB   . LEU A 1 808  ? 119.266 74.881  141.071 1.00 25.28 ?  808  LEU A CB   1 
ATOM   4989  C CG   . LEU A 1 808  ? 120.410 74.730  140.052 1.00 24.21 ?  808  LEU A CG   1 
ATOM   4990  C CD1  . LEU A 1 808  ? 121.533 73.913  140.676 1.00 22.96 ?  808  LEU A CD1  1 
ATOM   4991  C CD2  . LEU A 1 808  ? 119.998 74.102  138.726 1.00 24.55 ?  808  LEU A CD2  1 
ATOM   4992  N N    . ARG A 1 809  ? 116.487 76.748  139.451 1.00 25.54 ?  809  ARG A N    1 
ATOM   4993  C CA   . ARG A 1 809  ? 115.486 76.675  138.395 1.00 25.17 ?  809  ARG A CA   1 
ATOM   4994  C C    . ARG A 1 809  ? 115.830 77.579  137.220 1.00 26.27 ?  809  ARG A C    1 
ATOM   4995  O O    . ARG A 1 809  ? 114.966 77.835  136.373 1.00 24.42 ?  809  ARG A O    1 
ATOM   4996  C CB   . ARG A 1 809  ? 114.100 77.029  138.943 1.00 27.53 ?  809  ARG A CB   1 
ATOM   4997  C CG   . ARG A 1 809  ? 113.001 76.086  138.482 1.00 25.43 ?  809  ARG A CG   1 
ATOM   4998  C CD   . ARG A 1 809  ? 111.690 76.336  139.209 1.00 26.08 ?  809  ARG A CD   1 
ATOM   4999  N NE   . ARG A 1 809  ? 110.834 77.267  138.485 1.00 23.54 ?  809  ARG A NE   1 
ATOM   5000  C CZ   . ARG A 1 809  ? 109.560 77.493  138.775 1.00 25.44 ?  809  ARG A CZ   1 
ATOM   5001  N NH1  . ARG A 1 809  ? 108.955 76.862  139.768 1.00 26.08 ?  809  ARG A NH1  1 
ATOM   5002  N NH2  . ARG A 1 809  ? 108.875 78.372  138.049 1.00 25.07 ?  809  ARG A NH2  1 
ATOM   5003  N N    . MET A 1 810  ? 117.064 78.070  137.149 1.00 32.31 ?  810  MET A N    1 
ATOM   5004  C CA   . MET A 1 810  ? 117.501 78.929  136.050 1.00 32.55 ?  810  MET A CA   1 
ATOM   5005  C C    . MET A 1 810  ? 118.113 78.114  134.916 1.00 31.59 ?  810  MET A C    1 
ATOM   5006  O O    . MET A 1 810  ? 119.223 78.372  134.451 1.00 29.05 ?  810  MET A O    1 
ATOM   5007  C CB   . MET A 1 810  ? 118.476 79.979  136.568 1.00 28.10 ?  810  MET A CB   1 
ATOM   5008  C CG   . MET A 1 810  ? 117.840 80.951  137.542 1.00 30.34 ?  810  MET A CG   1 
ATOM   5009  S SD   . MET A 1 810  ? 116.077 81.139  137.209 1.00 40.14 ?  810  MET A SD   1 
ATOM   5010  C CE   . MET A 1 810  ? 115.737 82.689  138.026 1.00 28.55 ?  810  MET A CE   1 
ATOM   5011  N N    . LEU A 1 811  ? 117.368 77.107  134.471 1.00 28.47 ?  811  LEU A N    1 
ATOM   5012  C CA   . LEU A 1 811  ? 117.720 76.317  133.303 1.00 29.55 ?  811  LEU A CA   1 
ATOM   5013  C C    . LEU A 1 811  ? 116.746 76.527  132.155 1.00 30.21 ?  811  LEU A C    1 
ATOM   5014  O O    . LEU A 1 811  ? 116.951 75.969  131.072 1.00 26.31 ?  811  LEU A O    1 
ATOM   5015  C CB   . LEU A 1 811  ? 117.786 74.830  133.669 1.00 27.29 ?  811  LEU A CB   1 
ATOM   5016  C CG   . LEU A 1 811  ? 118.585 74.488  134.930 1.00 29.72 ?  811  LEU A CG   1 
ATOM   5017  C CD1  . LEU A 1 811  ? 118.183 73.125  135.474 1.00 30.88 ?  811  LEU A CD1  1 
ATOM   5018  C CD2  . LEU A 1 811  ? 120.080 74.542  134.654 1.00 26.73 ?  811  LEU A CD2  1 
ATOM   5019  N N    . ARG A 1 812  ? 115.688 77.309  132.366 1.00 33.07 ?  812  ARG A N    1 
ATOM   5020  C CA   . ARG A 1 812  ? 114.735 77.629  131.314 1.00 33.60 ?  812  ARG A CA   1 
ATOM   5021  C C    . ARG A 1 812  ? 114.994 78.984  130.670 1.00 33.38 ?  812  ARG A C    1 
ATOM   5022  O O    . ARG A 1 812  ? 114.448 79.254  129.594 1.00 33.72 ?  812  ARG A O    1 
ATOM   5023  C CB   . ARG A 1 812  ? 113.305 77.595  131.867 1.00 30.70 ?  812  ARG A CB   1 
ATOM   5024  C CG   . ARG A 1 812  ? 112.909 76.251  132.459 1.00 28.05 ?  812  ARG A CG   1 
ATOM   5025  C CD   . ARG A 1 812  ? 111.424 76.203  132.777 1.00 31.74 ?  812  ARG A CD   1 
ATOM   5026  N NE   . ARG A 1 812  ? 110.622 76.761  131.696 1.00 33.70 ?  812  ARG A NE   1 
ATOM   5027  C CZ   . ARG A 1 812  ? 110.280 76.100  130.598 1.00 33.00 ?  812  ARG A CZ   1 
ATOM   5028  N NH1  . ARG A 1 812  ? 110.647 74.844  130.404 1.00 32.44 ?  812  ARG A NH1  1 
ATOM   5029  N NH2  . ARG A 1 812  ? 109.551 76.715  129.671 1.00 31.00 ?  812  ARG A NH2  1 
ATOM   5030  N N    . LEU A 1 813  ? 115.803 79.838  131.302 1.00 25.53 ?  813  LEU A N    1 
ATOM   5031  C CA   . LEU A 1 813  ? 116.174 81.105  130.682 1.00 27.77 ?  813  LEU A CA   1 
ATOM   5032  C C    . LEU A 1 813  ? 117.210 80.909  129.583 1.00 30.24 ?  813  LEU A C    1 
ATOM   5033  O O    . LEU A 1 813  ? 117.197 81.637  128.583 1.00 31.30 ?  813  LEU A O    1 
ATOM   5034  C CB   . LEU A 1 813  ? 116.697 82.077  131.739 1.00 25.04 ?  813  LEU A CB   1 
ATOM   5035  C CG   . LEU A 1 813  ? 115.737 82.441  132.873 1.00 30.80 ?  813  LEU A CG   1 
ATOM   5036  C CD1  . LEU A 1 813  ? 116.457 83.241  133.948 1.00 30.54 ?  813  LEU A CD1  1 
ATOM   5037  C CD2  . LEU A 1 813  ? 114.542 83.214  132.337 1.00 26.06 ?  813  LEU A CD2  1 
ATOM   5038  N N    . THR A 1 814  ? 118.114 79.940  129.748 1.00 25.68 ?  814  THR A N    1 
ATOM   5039  C CA   . THR A 1 814  ? 119.121 79.678  128.727 1.00 24.66 ?  814  THR A CA   1 
ATOM   5040  C C    . THR A 1 814  ? 118.524 79.068  127.465 1.00 24.21 ?  814  THR A C    1 
ATOM   5041  O O    . THR A 1 814  ? 119.179 79.084  126.418 1.00 24.98 ?  814  THR A O    1 
ATOM   5042  C CB   . THR A 1 814  ? 120.215 78.762  129.280 1.00 24.13 ?  814  THR A CB   1 
ATOM   5043  O OG1  . THR A 1 814  ? 121.102 78.381  128.221 1.00 22.81 ?  814  THR A OG1  1 
ATOM   5044  C CG2  . THR A 1 814  ? 119.606 77.516  129.897 1.00 22.48 ?  814  THR A CG2  1 
ATOM   5045  N N    . LYS A 1 815  ? 117.308 78.523  127.541 1.00 21.68 ?  815  LYS A N    1 
ATOM   5046  C CA   . LYS A 1 815  ? 116.640 78.043  126.336 1.00 21.87 ?  815  LYS A CA   1 
ATOM   5047  C C    . LYS A 1 815  ? 116.226 79.204  125.440 1.00 22.52 ?  815  LYS A C    1 
ATOM   5048  O O    . LYS A 1 815  ? 116.334 79.117  124.211 1.00 24.43 ?  815  LYS A O    1 
ATOM   5049  C CB   . LYS A 1 815  ? 115.428 77.190  126.710 1.00 23.19 ?  815  LYS A CB   1 
ATOM   5050  C CG   . LYS A 1 815  ? 114.772 76.487  125.530 1.00 23.64 ?  815  LYS A CG   1 
ATOM   5051  C CD   . LYS A 1 815  ? 113.337 76.948  125.331 1.00 24.74 ?  815  LYS A CD   1 
ATOM   5052  C CE   . LYS A 1 815  ? 112.385 76.207  126.258 1.00 23.98 ?  815  LYS A CE   1 
ATOM   5053  N NZ   . LYS A 1 815  ? 110.962 76.540  125.973 1.00 23.70 ?  815  LYS A NZ   1 
ATOM   5054  N N    . ALA A 1 816  ? 115.756 80.296  126.036 1.00 22.02 ?  816  ALA A N    1 
ATOM   5055  C CA   . ALA A 1 816  ? 115.368 81.487  125.293 1.00 26.01 ?  816  ALA A CA   1 
ATOM   5056  C C    . ALA A 1 816  ? 116.497 82.501  125.161 1.00 24.06 ?  816  ALA A C    1 
ATOM   5057  O O    . ALA A 1 816  ? 116.312 83.528  124.501 1.00 21.45 ?  816  ALA A O    1 
ATOM   5058  C CB   . ALA A 1 816  ? 114.156 82.150  125.955 1.00 23.99 ?  816  ALA A CB   1 
ATOM   5059  N N    . LEU A 1 817  ? 117.654 82.246  125.773 1.00 21.27 ?  817  LEU A N    1 
ATOM   5060  C CA   . LEU A 1 817  ? 118.791 83.150  125.656 1.00 19.30 ?  817  LEU A CA   1 
ATOM   5061  C C    . LEU A 1 817  ? 119.679 82.836  124.458 1.00 22.74 ?  817  LEU A C    1 
ATOM   5062  O O    . LEU A 1 817  ? 120.427 83.715  124.014 1.00 25.81 ?  817  LEU A O    1 
ATOM   5063  C CB   . LEU A 1 817  ? 119.629 83.109  126.939 1.00 18.90 ?  817  LEU A CB   1 
ATOM   5064  C CG   . LEU A 1 817  ? 120.540 84.304  127.231 1.00 18.52 ?  817  LEU A CG   1 
ATOM   5065  C CD1  . LEU A 1 817  ? 119.717 85.507  127.665 1.00 20.52 ?  817  LEU A CD1  1 
ATOM   5066  C CD2  . LEU A 1 817  ? 121.576 83.948  128.285 1.00 19.19 ?  817  LEU A CD2  1 
ATOM   5067  N N    . ILE A 1 818  ? 119.618 81.605  123.936 1.00 20.29 ?  818  ILE A N    1 
ATOM   5068  C CA   . ILE A 1 818  ? 120.398 81.264  122.739 1.00 18.99 ?  818  ILE A CA   1 
ATOM   5069  C C    . ILE A 1 818  ? 120.024 82.113  121.530 1.00 21.10 ?  818  ILE A C    1 
ATOM   5070  O O    . ILE A 1 818  ? 120.939 82.575  120.825 1.00 20.42 ?  818  ILE A O    1 
ATOM   5071  C CB   . ILE A 1 818  ? 120.318 79.754  122.469 1.00 18.47 ?  818  ILE A CB   1 
ATOM   5072  C CG1  . ILE A 1 818  ? 120.897 78.960  123.643 1.00 18.83 ?  818  ILE A CG1  1 
ATOM   5073  C CG2  . ILE A 1 818  ? 121.043 79.390  121.182 1.00 18.32 ?  818  ILE A CG2  1 
ATOM   5074  C CD1  . ILE A 1 818  ? 122.255 79.441  124.108 1.00 18.94 ?  818  ILE A CD1  1 
ATOM   5075  N N    . PRO A 1 819  ? 118.739 82.353  121.205 1.00 17.29 ?  819  PRO A N    1 
ATOM   5076  C CA   . PRO A 1 819  ? 118.447 83.266  120.085 1.00 15.66 ?  819  PRO A CA   1 
ATOM   5077  C C    . PRO A 1 819  ? 118.994 84.670  120.268 1.00 16.60 ?  819  PRO A C    1 
ATOM   5078  O O    . PRO A 1 819  ? 119.396 85.292  119.280 1.00 26.21 ?  819  PRO A O    1 
ATOM   5079  C CB   . PRO A 1 819  ? 116.914 83.267  120.028 1.00 17.87 ?  819  PRO A CB   1 
ATOM   5080  C CG   . PRO A 1 819  ? 116.534 81.951  120.547 1.00 20.99 ?  819  PRO A CG   1 
ATOM   5081  C CD   . PRO A 1 819  ? 117.497 81.694  121.664 1.00 16.94 ?  819  PRO A CD   1 
ATOM   5082  N N    . LYS A 1 820  ? 119.038 85.188  121.498 1.00 11.11 ?  820  LYS A N    1 
ATOM   5083  C CA   . LYS A 1 820  ? 119.573 86.530  121.709 1.00 11.55 ?  820  LYS A CA   1 
ATOM   5084  C C    . LYS A 1 820  ? 121.075 86.581  121.448 1.00 10.57 ?  820  LYS A C    1 
ATOM   5085  O O    . LYS A 1 820  ? 121.579 87.549  120.866 1.00 16.80 ?  820  LYS A O    1 
ATOM   5086  C CB   . LYS A 1 820  ? 119.250 87.006  123.125 1.00 13.91 ?  820  LYS A CB   1 
ATOM   5087  C CG   . LYS A 1 820  ? 117.763 86.988  123.462 1.00 15.64 ?  820  LYS A CG   1 
ATOM   5088  C CD   . LYS A 1 820  ? 116.940 87.673  122.381 1.00 14.54 ?  820  LYS A CD   1 
ATOM   5089  C CE   . LYS A 1 820  ? 115.449 87.521  122.634 1.00 14.35 ?  820  LYS A CE   1 
ATOM   5090  N NZ   . LYS A 1 820  ? 114.648 88.464  121.804 1.00 15.94 ?  820  LYS A NZ   1 
ATOM   5091  N N    . LEU A 1 821  ? 121.807 85.544  121.862 1.00 13.51 ?  821  LEU A N    1 
ATOM   5092  C CA   . LEU A 1 821  ? 123.240 85.496  121.586 1.00 18.20 ?  821  LEU A CA   1 
ATOM   5093  C C    . LEU A 1 821  ? 123.508 85.307  120.096 1.00 18.84 ?  821  LEU A C    1 
ATOM   5094  O O    . LEU A 1 821  ? 124.459 85.885  119.549 1.00 17.65 ?  821  LEU A O    1 
ATOM   5095  C CB   . LEU A 1 821  ? 123.891 84.381  122.404 1.00 17.48 ?  821  LEU A CB   1 
ATOM   5096  C CG   . LEU A 1 821  ? 123.978 84.602  123.917 1.00 17.73 ?  821  LEU A CG   1 
ATOM   5097  C CD1  . LEU A 1 821  ? 125.017 83.682  124.538 1.00 22.30 ?  821  LEU A CD1  1 
ATOM   5098  C CD2  . LEU A 1 821  ? 124.282 86.056  124.251 1.00 16.87 ?  821  LEU A CD2  1 
ATOM   5099  N N    . ILE A 1 822  ? 122.674 84.509  119.424 1.00 18.15 ?  822  ILE A N    1 
ATOM   5100  C CA   . ILE A 1 822  ? 122.782 84.376  117.972 1.00 10.73 ?  822  ILE A CA   1 
ATOM   5101  C C    . ILE A 1 822  ? 122.530 85.720  117.297 1.00 10.82 ?  822  ILE A C    1 
ATOM   5102  O O    . ILE A 1 822  ? 123.235 86.102  116.355 1.00 17.52 ?  822  ILE A O    1 
ATOM   5103  C CB   . ILE A 1 822  ? 121.818 83.283  117.468 1.00 12.99 ?  822  ILE A CB   1 
ATOM   5104  C CG1  . ILE A 1 822  ? 122.415 81.896  117.716 1.00 15.59 ?  822  ILE A CG1  1 
ATOM   5105  C CG2  . ILE A 1 822  ? 121.497 83.463  115.992 1.00 14.51 ?  822  ILE A CG2  1 
ATOM   5106  C CD1  . ILE A 1 822  ? 121.536 80.761  117.248 1.00 18.12 ?  822  ILE A CD1  1 
ATOM   5107  N N    . LEU A 1 823  ? 121.545 86.473  117.793 1.00 6.51  ?  823  LEU A N    1 
ATOM   5108  C CA   . LEU A 1 823  ? 121.257 87.795  117.247 1.00 5.41  ?  823  LEU A CA   1 
ATOM   5109  C C    . LEU A 1 823  ? 122.422 88.758  117.456 1.00 9.72  ?  823  LEU A C    1 
ATOM   5110  O O    . LEU A 1 823  ? 122.751 89.545  116.561 1.00 13.65 ?  823  LEU A O    1 
ATOM   5111  C CB   . LEU A 1 823  ? 119.983 88.353  117.880 1.00 5.29  ?  823  LEU A CB   1 
ATOM   5112  C CG   . LEU A 1 823  ? 118.715 88.359  117.025 1.00 9.95  ?  823  LEU A CG   1 
ATOM   5113  C CD1  . LEU A 1 823  ? 118.315 86.946  116.635 1.00 11.63 ?  823  LEU A CD1  1 
ATOM   5114  C CD2  . LEU A 1 823  ? 117.582 89.055  117.762 1.00 11.58 ?  823  LEU A CD2  1 
ATOM   5115  N N    . VAL A 1 824  ? 123.056 88.721  118.631 1.00 10.80 ?  824  VAL A N    1 
ATOM   5116  C CA   . VAL A 1 824  ? 124.148 89.662  118.877 1.00 8.38  ?  824  VAL A CA   1 
ATOM   5117  C C    . VAL A 1 824  ? 125.385 89.299  118.050 1.00 8.50  ?  824  VAL A C    1 
ATOM   5118  O O    . VAL A 1 824  ? 126.094 90.192  117.560 1.00 13.46 ?  824  VAL A O    1 
ATOM   5119  C CB   . VAL A 1 824  ? 124.444 89.780  120.391 1.00 10.09 ?  824  VAL A CB   1 
ATOM   5120  C CG1  . VAL A 1 824  ? 125.326 88.654  120.915 1.00 12.77 ?  824  VAL A CG1  1 
ATOM   5121  C CG2  . VAL A 1 824  ? 125.070 91.132  120.701 1.00 14.39 ?  824  VAL A CG2  1 
ATOM   5122  N N    . VAL A 1 825  ? 125.646 88.004  117.833 1.00 9.25  ?  825  VAL A N    1 
ATOM   5123  C CA   . VAL A 1 825  ? 126.779 87.650  116.981 1.00 7.08  ?  825  VAL A CA   1 
ATOM   5124  C C    . VAL A 1 825  ? 126.466 87.963  115.517 1.00 11.32 ?  825  VAL A C    1 
ATOM   5125  O O    . VAL A 1 825  ? 127.364 88.348  114.751 1.00 15.07 ?  825  VAL A O    1 
ATOM   5126  C CB   . VAL A 1 825  ? 127.200 86.181  117.213 1.00 9.47  ?  825  VAL A CB   1 
ATOM   5127  C CG1  . VAL A 1 825  ? 126.336 85.199  116.441 1.00 15.51 ?  825  VAL A CG1  1 
ATOM   5128  C CG2  . VAL A 1 825  ? 128.665 85.992  116.860 1.00 12.27 ?  825  VAL A CG2  1 
ATOM   5129  N N    . ASN A 1 826  ? 125.191 87.860  115.118 1.00 11.91 ?  826  ASN A N    1 
ATOM   5130  C CA   . ASN A 1 826  ? 124.780 88.312  113.793 1.00 6.19  ?  826  ASN A CA   1 
ATOM   5131  C C    . ASN A 1 826  ? 124.999 89.808  113.636 1.00 7.21  ?  826  ASN A C    1 
ATOM   5132  O O    . ASN A 1 826  ? 125.433 90.272  112.577 1.00 11.21 ?  826  ASN A O    1 
ATOM   5133  C CB   . ASN A 1 826  ? 123.310 87.969  113.556 1.00 4.71  ?  826  ASN A CB   1 
ATOM   5134  C CG   . ASN A 1 826  ? 123.124 86.616  112.915 1.00 5.67  ?  826  ASN A CG   1 
ATOM   5135  O OD1  . ASN A 1 826  ? 124.090 85.962  112.533 1.00 6.46  ?  826  ASN A OD1  1 
ATOM   5136  N ND2  . ASN A 1 826  ? 121.874 86.186  112.794 1.00 10.89 ?  826  ASN A ND2  1 
ATOM   5137  N N    . GLY A 1 827  ? 124.694 90.576  114.682 1.00 10.91 ?  827  GLY A N    1 
ATOM   5138  C CA   . GLY A 1 827  ? 124.927 92.009  114.636 1.00 8.76  ?  827  GLY A CA   1 
ATOM   5139  C C    . GLY A 1 827  ? 126.395 92.364  114.499 1.00 11.38 ?  827  GLY A C    1 
ATOM   5140  O O    . GLY A 1 827  ? 126.752 93.272  113.747 1.00 16.32 ?  827  GLY A O    1 
ATOM   5141  N N    . LYS A 1 828  ? 127.266 91.651  115.222 1.00 10.02 ?  828  LYS A N    1 
ATOM   5142  C CA   . LYS A 1 828  ? 128.703 91.901  115.095 1.00 9.28  ?  828  LYS A CA   1 
ATOM   5143  C C    . LYS A 1 828  ? 129.210 91.566  113.692 1.00 10.81 ?  828  LYS A C    1 
ATOM   5144  O O    . LYS A 1 828  ? 129.979 92.338  113.091 1.00 15.22 ?  828  LYS A O    1 
ATOM   5145  C CB   . LYS A 1 828  ? 129.471 91.098  116.144 1.00 7.49  ?  828  LYS A CB   1 
ATOM   5146  C CG   . LYS A 1 828  ? 129.091 91.418  117.582 1.00 13.80 ?  828  LYS A CG   1 
ATOM   5147  C CD   . LYS A 1 828  ? 129.975 92.498  118.182 1.00 16.35 ?  828  LYS A CD   1 
ATOM   5148  C CE   . LYS A 1 828  ? 131.411 92.024  118.324 1.00 16.16 ?  828  LYS A CE   1 
ATOM   5149  N NZ   . LYS A 1 828  ? 132.305 93.104  118.826 1.00 14.88 ?  828  LYS A NZ   1 
ATOM   5150  N N    . ILE A 1 829  ? 128.776 90.423  113.148 1.00 7.96  ?  829  ILE A N    1 
ATOM   5151  C CA   . ILE A 1 829  ? 129.185 90.030  111.800 1.00 7.72  ?  829  ILE A CA   1 
ATOM   5152  C C    . ILE A 1 829  ? 128.689 91.040  110.770 1.00 6.64  ?  829  ILE A C    1 
ATOM   5153  O O    . ILE A 1 829  ? 129.423 91.419  109.848 1.00 10.29 ?  829  ILE A O    1 
ATOM   5154  C CB   . ILE A 1 829  ? 128.694 88.602  111.494 1.00 6.64  ?  829  ILE A CB   1 
ATOM   5155  C CG1  . ILE A 1 829  ? 129.460 87.586  112.342 1.00 9.00  ?  829  ILE A CG1  1 
ATOM   5156  C CG2  . ILE A 1 829  ? 128.834 88.276  110.017 1.00 9.19  ?  829  ILE A CG2  1 
ATOM   5157  C CD1  . ILE A 1 829  ? 128.929 86.181  112.230 1.00 12.96 ?  829  ILE A CD1  1 
ATOM   5158  N N    . ASN A 1 830  ? 127.446 91.505  110.920 1.00 7.42  ?  830  ASN A N    1 
ATOM   5159  C CA   . ASN A 1 830  ? 126.900 92.504  110.007 1.00 1.68  ?  830  ASN A CA   1 
ATOM   5160  C C    . ASN A 1 830  ? 127.642 93.830  110.114 1.00 7.92  ?  830  ASN A C    1 
ATOM   5161  O O    . ASN A 1 830  ? 127.874 94.498  109.099 1.00 21.38 ?  830  ASN A O    1 
ATOM   5162  C CB   . ASN A 1 830  ? 125.410 92.701  110.284 1.00 4.36  ?  830  ASN A CB   1 
ATOM   5163  C CG   . ASN A 1 830  ? 124.699 93.426  109.161 1.00 5.96  ?  830  ASN A CG   1 
ATOM   5164  O OD1  . ASN A 1 830  ? 123.814 94.245  109.401 1.00 7.87  ?  830  ASN A OD1  1 
ATOM   5165  N ND2  . ASN A 1 830  ? 125.083 93.129  107.927 1.00 12.52 ?  830  ASN A ND2  1 
ATOM   5166  N N    . ASN A 1 831  ? 128.015 94.232  111.332 1.00 9.84  ?  831  ASN A N    1 
ATOM   5167  C CA   . ASN A 1 831  ? 128.751 95.478  111.509 1.00 10.57 ?  831  ASN A CA   1 
ATOM   5168  C C    . ASN A 1 831  ? 130.123 95.418  110.855 1.00 8.93  ?  831  ASN A C    1 
ATOM   5169  O O    . ASN A 1 831  ? 130.615 96.439  110.361 1.00 10.48 ?  831  ASN A O    1 
ATOM   5170  C CB   . ASN A 1 831  ? 128.886 95.805  112.996 1.00 12.11 ?  831  ASN A CB   1 
ATOM   5171  C CG   . ASN A 1 831  ? 127.595 96.320  113.596 1.00 17.68 ?  831  ASN A CG   1 
ATOM   5172  O OD1  . ASN A 1 831  ? 126.800 96.972  112.919 1.00 20.45 ?  831  ASN A OD1  1 
ATOM   5173  N ND2  . ASN A 1 831  ? 127.375 96.025  114.870 1.00 18.95 ?  831  ASN A ND2  1 
ATOM   5174  N N    . GLN A 1 832  ? 130.761 94.246  110.847 1.00 5.00  ?  832  GLN A N    1 
ATOM   5175  C CA   . GLN A 1 832  ? 132.022 94.132  110.116 1.00 7.34  ?  832  GLN A CA   1 
ATOM   5176  C C    . GLN A 1 832  ? 131.794 94.107  108.604 1.00 11.10 ?  832  GLN A C    1 
ATOM   5177  O O    . GLN A 1 832  ? 132.521 94.765  107.838 1.00 20.37 ?  832  GLN A O    1 
ATOM   5178  C CB   . GLN A 1 832  ? 132.777 92.881  110.560 1.00 10.31 ?  832  GLN A CB   1 
ATOM   5179  C CG   . GLN A 1 832  ? 134.145 92.743  109.924 1.00 11.87 ?  832  GLN A CG   1 
ATOM   5180  C CD   . GLN A 1 832  ? 134.955 94.020  110.027 1.00 16.09 ?  832  GLN A CD   1 
ATOM   5181  O OE1  . GLN A 1 832  ? 135.348 94.430  111.119 1.00 18.72 ?  832  GLN A OE1  1 
ATOM   5182  N NE2  . GLN A 1 832  ? 135.208 94.656  108.891 1.00 17.27 ?  832  GLN A NE2  1 
ATOM   5183  N N    . LEU A 1 833  ? 130.780 93.357  108.158 1.00 11.32 ?  833  LEU A N    1 
ATOM   5184  C CA   . LEU A 1 833  ? 130.573 93.153  106.729 1.00 2.13  ?  833  LEU A CA   1 
ATOM   5185  C C    . LEU A 1 833  ? 130.124 94.427  106.029 1.00 0.90  ?  833  LEU A C    1 
ATOM   5186  O O    . LEU A 1 833  ? 130.444 94.624  104.853 1.00 9.74  ?  833  LEU A O    1 
ATOM   5187  C CB   . LEU A 1 833  ? 129.550 92.046  106.492 1.00 5.53  ?  833  LEU A CB   1 
ATOM   5188  C CG   . LEU A 1 833  ? 129.963 90.985  105.473 1.00 8.20  ?  833  LEU A CG   1 
ATOM   5189  C CD1  . LEU A 1 833  ? 131.354 90.448  105.787 1.00 12.06 ?  833  LEU A CD1  1 
ATOM   5190  C CD2  . LEU A 1 833  ? 128.942 89.873  105.408 1.00 8.69  ?  833  LEU A CD2  1 
ATOM   5191  N N    . SER A 1 834  ? 129.373 95.290  106.720 1.00 0.86  ?  834  SER A N    1 
ATOM   5192  C CA   . SER A 1 834  ? 128.952 96.547  106.109 1.00 0.00  ?  834  SER A CA   1 
ATOM   5193  C C    . SER A 1 834  ? 130.147 97.436  105.793 1.00 2.81  ?  834  SER A C    1 
ATOM   5194  O O    . SER A 1 834  ? 130.226 98.020  104.705 1.00 11.05 ?  834  SER A O    1 
ATOM   5195  C CB   . SER A 1 834  ? 127.973 97.276  107.026 1.00 0.50  ?  834  SER A CB   1 
ATOM   5196  O OG   . SER A 1 834  ? 128.648 98.223  107.832 1.00 7.65  ?  834  SER A OG   1 
ATOM   5197  N N    . LEU A 1 835  ? 131.092 97.540  106.732 1.00 7.29  ?  835  LEU A N    1 
ATOM   5198  C CA   . LEU A 1 835  ? 132.306 98.312  106.489 1.00 4.07  ?  835  LEU A CA   1 
ATOM   5199  C C    . LEU A 1 835  ? 133.128 97.706  105.361 1.00 0.00  ?  835  LEU A C    1 
ATOM   5200  O O    . LEU A 1 835  ? 133.650 98.434  104.503 1.00 2.69  ?  835  LEU A O    1 
ATOM   5201  C CB   . LEU A 1 835  ? 133.133 98.400  107.771 1.00 5.04  ?  835  LEU A CB   1 
ATOM   5202  C CG   . LEU A 1 835  ? 134.514 99.046  107.655 1.00 13.00 ?  835  LEU A CG   1 
ATOM   5203  C CD1  . LEU A 1 835  ? 134.468 100.496 108.105 1.00 11.16 ?  835  LEU A CD1  1 
ATOM   5204  C CD2  . LEU A 1 835  ? 135.538 98.263  108.459 1.00 12.66 ?  835  LEU A CD2  1 
ATOM   5205  N N    . GLY A 1 836  ? 133.249 96.374  105.339 1.00 1.61  ?  836  GLY A N    1 
ATOM   5206  C CA   . GLY A 1 836  ? 133.990 95.736  104.258 1.00 3.59  ?  836  GLY A CA   1 
ATOM   5207  C C    . GLY A 1 836  ? 133.376 95.987  102.891 1.00 2.94  ?  836  GLY A C    1 
ATOM   5208  O O    . GLY A 1 836  ? 134.084 96.312  101.929 1.00 13.50 ?  836  GLY A O    1 
ATOM   5209  N N    . TYR A 1 837  ? 132.049 95.864  102.794 1.00 6.41  ?  837  TYR A N    1 
ATOM   5210  C CA   . TYR A 1 837  ? 131.357 96.111  101.533 1.00 0.00  ?  837  TYR A CA   1 
ATOM   5211  C C    . TYR A 1 837  ? 131.478 97.564  101.099 1.00 0.99  ?  837  TYR A C    1 
ATOM   5212  O O    . TYR A 1 837  ? 131.663 97.844  99.910  1.00 10.79 ?  837  TYR A O    1 
ATOM   5213  C CB   . TYR A 1 837  ? 129.887 95.717  101.656 1.00 0.00  ?  837  TYR A CB   1 
ATOM   5214  C CG   . TYR A 1 837  ? 129.559 94.408  100.991 1.00 3.08  ?  837  TYR A CG   1 
ATOM   5215  C CD1  . TYR A 1 837  ? 129.632 94.277  99.613  1.00 7.15  ?  837  TYR A CD1  1 
ATOM   5216  C CD2  . TYR A 1 837  ? 129.179 93.302  101.738 1.00 3.83  ?  837  TYR A CD2  1 
ATOM   5217  C CE1  . TYR A 1 837  ? 129.335 93.086  98.996  1.00 6.50  ?  837  TYR A CE1  1 
ATOM   5218  C CE2  . TYR A 1 837  ? 128.880 92.104  101.129 1.00 3.80  ?  837  TYR A CE2  1 
ATOM   5219  C CZ   . TYR A 1 837  ? 128.961 92.003  99.759  1.00 8.75  ?  837  TYR A CZ   1 
ATOM   5220  O OH   . TYR A 1 837  ? 128.665 90.816  99.143  1.00 13.29 ?  837  TYR A OH   1 
ATOM   5221  N N    . ASP A 1 838  ? 131.361 98.503  102.044 1.00 0.80  ?  838  ASP A N    1 
ATOM   5222  C CA   . ASP A 1 838  ? 131.500 99.914  101.699 1.00 0.18  ?  838  ASP A CA   1 
ATOM   5223  C C    . ASP A 1 838  ? 132.897 100.223 101.174 1.00 2.28  ?  838  ASP A C    1 
ATOM   5224  O O    . ASP A 1 838  ? 133.045 100.944 100.179 1.00 3.47  ?  838  ASP A O    1 
ATOM   5225  C CB   . ASP A 1 838  ? 131.180 100.788 102.909 1.00 4.92  ?  838  ASP A CB   1 
ATOM   5226  C CG   . ASP A 1 838  ? 129.694 100.896 103.175 1.00 9.23  ?  838  ASP A CG   1 
ATOM   5227  O OD1  . ASP A 1 838  ? 128.965 99.922  102.891 1.00 7.90  ?  838  ASP A OD1  1 
ATOM   5228  O OD2  . ASP A 1 838  ? 129.254 101.955 103.670 1.00 14.97 ?  838  ASP A OD2  1 
ATOM   5229  N N    . VAL A 1 839  ? 133.931 99.671  101.817 1.00 0.88  ?  839  VAL A N    1 
ATOM   5230  C CA   . VAL A 1 839  ? 135.302 99.915  101.369 1.00 1.03  ?  839  VAL A CA   1 
ATOM   5231  C C    . VAL A 1 839  ? 135.516 99.347  99.969  1.00 0.34  ?  839  VAL A C    1 
ATOM   5232  O O    . VAL A 1 839  ? 136.070 100.018 99.085  1.00 12.09 ?  839  VAL A O    1 
ATOM   5233  C CB   . VAL A 1 839  ? 136.308 99.332  102.377 1.00 3.33  ?  839  VAL A CB   1 
ATOM   5234  C CG1  . VAL A 1 839  ? 137.699 99.261  101.770 1.00 4.72  ?  839  VAL A CG1  1 
ATOM   5235  C CG2  . VAL A 1 839  ? 136.326 100.163 103.646 1.00 5.12  ?  839  VAL A CG2  1 
ATOM   5236  N N    . GLY A 1 840  ? 135.057 98.112  99.740  1.00 0.36  ?  840  GLY A N    1 
ATOM   5237  C CA   . GLY A 1 840  ? 135.230 97.506  98.427  1.00 0.00  ?  840  GLY A CA   1 
ATOM   5238  C C    . GLY A 1 840  ? 134.488 98.245  97.328  1.00 4.15  ?  840  GLY A C    1 
ATOM   5239  O O    . GLY A 1 840  ? 135.043 98.499  96.253  1.00 9.34  ?  840  GLY A O    1 
ATOM   5240  N N    . LYS A 1 841  ? 133.230 98.615  97.589  1.00 4.02  ?  841  LYS A N    1 
ATOM   5241  C CA   . LYS A 1 841  ? 132.434 99.333  96.599  1.00 0.00  ?  841  LYS A CA   1 
ATOM   5242  C C    . LYS A 1 841  ? 133.033 100.697 96.287  1.00 0.00  ?  841  LYS A C    1 
ATOM   5243  O O    . LYS A 1 841  ? 133.104 101.099 95.117  1.00 8.09  ?  841  LYS A O    1 
ATOM   5244  C CB   . LYS A 1 841  ? 131.001 99.484  97.106  1.00 0.00  ?  841  LYS A CB   1 
ATOM   5245  C CG   . LYS A 1 841  ? 129.937 99.365  96.037  1.00 8.04  ?  841  LYS A CG   1 
ATOM   5246  C CD   . LYS A 1 841  ? 128.639 98.831  96.622  1.00 11.28 ?  841  LYS A CD   1 
ATOM   5247  C CE   . LYS A 1 841  ? 128.845 97.472  97.274  1.00 7.65  ?  841  LYS A CE   1 
ATOM   5248  N NZ   . LYS A 1 841  ? 127.702 97.080  98.141  1.00 6.39  ?  841  LYS A NZ   1 
ATOM   5249  N N    . GLY A 1 842  ? 133.470 101.425 97.321  1.00 0.00  ?  842  GLY A N    1 
ATOM   5250  C CA   . GLY A 1 842  ? 134.085 102.720 97.095  1.00 0.00  ?  842  GLY A CA   1 
ATOM   5251  C C    . GLY A 1 842  ? 135.366 102.628 96.292  1.00 0.00  ?  842  GLY A C    1 
ATOM   5252  O O    . GLY A 1 842  ? 135.606 103.445 95.400  1.00 6.06  ?  842  GLY A O    1 
ATOM   5253  N N    . TYR A 1 843  ? 136.200 101.623 96.584  1.00 0.00  ?  843  TYR A N    1 
ATOM   5254  C CA   . TYR A 1 843  ? 137.419 101.441 95.802  1.00 0.00  ?  843  TYR A CA   1 
ATOM   5255  C C    . TYR A 1 843  ? 137.105 101.121 94.346  1.00 1.06  ?  843  TYR A C    1 
ATOM   5256  O O    . TYR A 1 843  ? 137.743 101.664 93.435  1.00 9.09  ?  843  TYR A O    1 
ATOM   5257  C CB   . TYR A 1 843  ? 138.285 100.342 96.416  1.00 0.00  ?  843  TYR A CB   1 
ATOM   5258  C CG   . TYR A 1 843  ? 139.517 100.017 95.601  1.00 1.12  ?  843  TYR A CG   1 
ATOM   5259  C CD1  . TYR A 1 843  ? 140.643 100.825 95.661  1.00 7.22  ?  843  TYR A CD1  1 
ATOM   5260  C CD2  . TYR A 1 843  ? 139.558 98.898  94.779  1.00 6.01  ?  843  TYR A CD2  1 
ATOM   5261  C CE1  . TYR A 1 843  ? 141.771 100.534 94.919  1.00 10.82 ?  843  TYR A CE1  1 
ATOM   5262  C CE2  . TYR A 1 843  ? 140.681 98.599  94.034  1.00 9.89  ?  843  TYR A CE2  1 
ATOM   5263  C CZ   . TYR A 1 843  ? 141.785 99.419  94.109  1.00 13.45 ?  843  TYR A CZ   1 
ATOM   5264  O OH   . TYR A 1 843  ? 142.907 99.124  93.370  1.00 13.46 ?  843  TYR A OH   1 
ATOM   5265  N N    . ILE A 1 844  ? 136.122 100.245 94.107  1.00 5.23  ?  844  ILE A N    1 
ATOM   5266  C CA   . ILE A 1 844  ? 135.771 99.867  92.737  1.00 1.52  ?  844  ILE A CA   1 
ATOM   5267  C C    . ILE A 1 844  ? 135.283 101.082 91.955  1.00 3.56  ?  844  ILE A C    1 
ATOM   5268  O O    . ILE A 1 844  ? 135.714 101.328 90.819  1.00 11.26 ?  844  ILE A O    1 
ATOM   5269  C CB   . ILE A 1 844  ? 134.718 98.743  92.746  1.00 4.39  ?  844  ILE A CB   1 
ATOM   5270  C CG1  . ILE A 1 844  ? 135.333 97.431  93.244  1.00 5.51  ?  844  ILE A CG1  1 
ATOM   5271  C CG2  . ILE A 1 844  ? 134.078 98.587  91.370  1.00 5.75  ?  844  ILE A CG2  1 
ATOM   5272  C CD1  . ILE A 1 844  ? 135.836 96.513  92.159  1.00 4.13  ?  844  ILE A CD1  1 
ATOM   5273  N N    . ILE A 1 845  ? 134.393 101.871 92.563  1.00 6.91  ?  845  ILE A N    1 
ATOM   5274  C CA   . ILE A 1 845  ? 133.848 103.046 91.887  1.00 5.03  ?  845  ILE A CA   1 
ATOM   5275  C C    . ILE A 1 845  ? 134.940 104.084 91.639  1.00 8.21  ?  845  ILE A C    1 
ATOM   5276  O O    . ILE A 1 845  ? 134.996 104.702 90.565  1.00 9.36  ?  845  ILE A O    1 
ATOM   5277  C CB   . ILE A 1 845  ? 132.675 103.625 92.699  1.00 4.06  ?  845  ILE A CB   1 
ATOM   5278  C CG1  . ILE A 1 845  ? 131.515 102.631 92.732  1.00 4.23  ?  845  ILE A CG1  1 
ATOM   5279  C CG2  . ILE A 1 845  ? 132.201 104.941 92.112  1.00 7.87  ?  845  ILE A CG2  1 
ATOM   5280  C CD1  . ILE A 1 845  ? 130.430 102.999 93.714  1.00 5.01  ?  845  ILE A CD1  1 
ATOM   5281  N N    . GLY A 1 846  ? 135.832 104.283 92.616  1.00 6.50  ?  846  GLY A N    1 
ATOM   5282  C CA   . GLY A 1 846  ? 136.916 105.234 92.436  1.00 3.80  ?  846  GLY A CA   1 
ATOM   5283  C C    . GLY A 1 846  ? 137.861 104.851 91.313  1.00 6.29  ?  846  GLY A C    1 
ATOM   5284  O O    . GLY A 1 846  ? 138.248 105.698 90.506  1.00 15.35 ?  846  GLY A O    1 
ATOM   5285  N N    . GLU A 1 847  ? 138.236 103.568 91.238  1.00 6.30  ?  847  GLU A N    1 
ATOM   5286  C CA   . GLU A 1 847  ? 139.086 103.119 90.137  1.00 5.75  ?  847  GLU A CA   1 
ATOM   5287  C C    . GLU A 1 847  ? 138.379 103.253 88.795  1.00 8.95  ?  847  GLU A C    1 
ATOM   5288  O O    . GLU A 1 847  ? 138.996 103.656 87.801  1.00 17.22 ?  847  GLU A O    1 
ATOM   5289  C CB   . GLU A 1 847  ? 139.539 101.675 90.357  1.00 6.90  ?  847  GLU A CB   1 
ATOM   5290  C CG   . GLU A 1 847  ? 140.330 101.437 91.633  1.00 11.60 ?  847  GLU A CG   1 
ATOM   5291  C CD   . GLU A 1 847  ? 141.365 102.513 91.895  1.00 18.49 ?  847  GLU A CD   1 
ATOM   5292  O OE1  . GLU A 1 847  ? 142.452 102.452 91.284  1.00 21.82 ?  847  GLU A OE1  1 
ATOM   5293  O OE2  . GLU A 1 847  ? 141.095 103.416 92.715  1.00 15.99 ?  847  GLU A OE2  1 
ATOM   5294  N N    . GLU A 1 848  ? 137.083 102.926 88.746  1.00 12.16 ?  848  GLU A N    1 
ATOM   5295  C CA   . GLU A 1 848  ? 136.352 103.010 87.484  1.00 11.80 ?  848  GLU A CA   1 
ATOM   5296  C C    . GLU A 1 848  ? 136.241 104.450 86.993  1.00 10.80 ?  848  GLU A C    1 
ATOM   5297  O O    . GLU A 1 848  ? 136.294 104.701 85.783  1.00 13.86 ?  848  GLU A O    1 
ATOM   5298  C CB   . GLU A 1 848  ? 134.967 102.382 87.637  1.00 12.95 ?  848  GLU A CB   1 
ATOM   5299  C CG   . GLU A 1 848  ? 134.884 100.956 87.114  1.00 13.97 ?  848  GLU A CG   1 
ATOM   5300  C CD   . GLU A 1 848  ? 133.727 100.179 87.708  1.00 17.90 ?  848  GLU A CD   1 
ATOM   5301  O OE1  . GLU A 1 848  ? 132.887 100.792 88.399  1.00 16.08 ?  848  GLU A OE1  1 
ATOM   5302  O OE2  . GLU A 1 848  ? 133.658 98.952  87.484  1.00 16.99 ?  848  GLU A OE2  1 
ATOM   5303  N N    . GLU A 1 849  ? 136.082 105.408 87.910  1.00 9.66  ?  849  GLU A N    1 
ATOM   5304  C CA   . GLU A 1 849  ? 136.029 106.810 87.496  1.00 13.34 ?  849  GLU A CA   1 
ATOM   5305  C C    . GLU A 1 849  ? 137.413 107.343 87.129  1.00 15.20 ?  849  GLU A C    1 
ATOM   5306  O O    . GLU A 1 849  ? 137.557 108.105 86.164  1.00 12.48 ?  849  GLU A O    1 
ATOM   5307  C CB   . GLU A 1 849  ? 135.401 107.661 88.598  1.00 10.75 ?  849  GLU A CB   1 
ATOM   5308  C CG   . GLU A 1 849  ? 133.886 107.573 88.659  1.00 12.07 ?  849  GLU A CG   1 
ATOM   5309  C CD   . GLU A 1 849  ? 133.323 108.074 89.975  1.00 17.27 ?  849  GLU A CD   1 
ATOM   5310  O OE1  . GLU A 1 849  ? 134.062 108.751 90.720  1.00 18.68 ?  849  GLU A OE1  1 
ATOM   5311  O OE2  . GLU A 1 849  ? 132.141 107.792 90.263  1.00 16.61 ?  849  GLU A OE2  1 
ATOM   5312  N N    . VAL A 1 850  ? 138.440 106.961 87.894  1.00 15.24 ?  850  VAL A N    1 
ATOM   5313  C CA   . VAL A 1 850  ? 139.787 107.472 87.663  1.00 12.94 ?  850  VAL A CA   1 
ATOM   5314  C C    . VAL A 1 850  ? 140.358 106.947 86.351  1.00 10.83 ?  850  VAL A C    1 
ATOM   5315  O O    . VAL A 1 850  ? 141.095 107.662 85.659  1.00 11.75 ?  850  VAL A O    1 
ATOM   5316  C CB   . VAL A 1 850  ? 140.667 107.133 88.882  1.00 11.66 ?  850  VAL A CB   1 
ATOM   5317  C CG1  . VAL A 1 850  ? 142.150 107.117 88.534  1.00 11.16 ?  850  VAL A CG1  1 
ATOM   5318  C CG2  . VAL A 1 850  ? 140.392 108.128 89.989  1.00 10.55 ?  850  VAL A CG2  1 
ATOM   5319  N N    . GLY A 1 851  ? 140.027 105.708 85.976  1.00 15.00 ?  851  GLY A N    1 
ATOM   5320  C CA   . GLY A 1 851  ? 140.471 105.190 84.692  1.00 12.21 ?  851  GLY A CA   1 
ATOM   5321  C C    . GLY A 1 851  ? 139.947 105.986 83.513  1.00 14.99 ?  851  GLY A C    1 
ATOM   5322  O O    . GLY A 1 851  ? 140.632 106.121 82.496  1.00 22.51 ?  851  GLY A O    1 
ATOM   5323  N N    . LYS A 1 852  ? 138.726 106.512 83.622  1.00 12.08 ?  852  LYS A N    1 
ATOM   5324  C CA   . LYS A 1 852  ? 138.195 107.368 82.567  1.00 18.91 ?  852  LYS A CA   1 
ATOM   5325  C C    . LYS A 1 852  ? 138.752 108.786 82.659  1.00 20.25 ?  852  LYS A C    1 
ATOM   5326  O O    . LYS A 1 852  ? 138.933 109.447 81.630  1.00 13.94 ?  852  LYS A O    1 
ATOM   5327  C CB   . LYS A 1 852  ? 136.663 107.395 82.618  1.00 16.03 ?  852  LYS A CB   1 
ATOM   5328  C CG   . LYS A 1 852  ? 135.937 106.106 82.188  1.00 13.76 ?  852  LYS A CG   1 
ATOM   5329  C CD   . LYS A 1 852  ? 136.830 105.085 81.482  1.00 15.48 ?  852  LYS A CD   1 
ATOM   5330  C CE   . LYS A 1 852  ? 136.020 104.155 80.590  1.00 17.05 ?  852  LYS A CE   1 
ATOM   5331  N NZ   . LYS A 1 852  ? 136.885 103.215 79.820  1.00 12.69 ?  852  LYS A NZ   1 
ATOM   5332  N N    . ILE A 1 853  ? 139.004 109.279 83.875  1.00 21.84 ?  853  ILE A N    1 
ATOM   5333  C CA   . ILE A 1 853  ? 139.521 110.639 84.032  1.00 16.76 ?  853  ILE A CA   1 
ATOM   5334  C C    . ILE A 1 853  ? 140.943 110.745 83.484  1.00 15.73 ?  853  ILE A C    1 
ATOM   5335  O O    . ILE A 1 853  ? 141.272 111.677 82.741  1.00 19.02 ?  853  ILE A O    1 
ATOM   5336  C CB   . ILE A 1 853  ? 139.447 111.084 85.505  1.00 11.11 ?  853  ILE A CB   1 
ATOM   5337  C CG1  . ILE A 1 853  ? 138.039 111.574 85.852  1.00 16.25 ?  853  ILE A CG1  1 
ATOM   5338  C CG2  . ILE A 1 853  ? 140.468 112.174 85.805  1.00 10.16 ?  853  ILE A CG2  1 
ATOM   5339  C CD1  . ILE A 1 853  ? 137.884 112.005 87.297  1.00 15.93 ?  853  ILE A CD1  1 
ATOM   5340  N N    . ILE A 1 854  ? 141.802 109.782 83.830  1.00 17.80 ?  854  ILE A N    1 
ATOM   5341  C CA   . ILE A 1 854  ? 143.222 109.848 83.479  1.00 16.97 ?  854  ILE A CA   1 
ATOM   5342  C C    . ILE A 1 854  ? 143.505 109.543 82.016  1.00 17.32 ?  854  ILE A C    1 
ATOM   5343  O O    . ILE A 1 854  ? 144.656 109.683 81.579  1.00 19.53 ?  854  ILE A O    1 
ATOM   5344  C CB   . ILE A 1 854  ? 144.005 108.896 84.406  1.00 17.55 ?  854  ILE A CB   1 
ATOM   5345  C CG1  . ILE A 1 854  ? 145.367 109.492 84.776  1.00 19.62 ?  854  ILE A CG1  1 
ATOM   5346  C CG2  . ILE A 1 854  ? 144.118 107.492 83.806  1.00 14.56 ?  854  ILE A CG2  1 
ATOM   5347  C CD1  . ILE A 1 854  ? 145.302 110.525 85.875  1.00 19.35 ?  854  ILE A CD1  1 
ATOM   5348  N N    . ASP A 1 855  ? 142.488 109.150 81.243  1.00 17.65 ?  855  ASP A N    1 
ATOM   5349  C CA   . ASP A 1 855  ? 142.702 108.774 79.847  1.00 22.54 ?  855  ASP A CA   1 
ATOM   5350  C C    . ASP A 1 855  ? 143.202 109.949 79.014  1.00 22.46 ?  855  ASP A C    1 
ATOM   5351  O O    . ASP A 1 855  ? 144.077 109.783 78.156  1.00 24.53 ?  855  ASP A O    1 
ATOM   5352  C CB   . ASP A 1 855  ? 141.408 108.214 79.256  1.00 22.40 ?  855  ASP A CB   1 
ATOM   5353  C CG   . ASP A 1 855  ? 141.658 107.219 78.140  1.00 24.80 ?  855  ASP A CG   1 
ATOM   5354  O OD1  . ASP A 1 855  ? 142.837 106.991 77.794  1.00 24.19 ?  855  ASP A OD1  1 
ATOM   5355  O OD2  . ASP A 1 855  ? 140.673 106.665 77.607  1.00 22.30 ?  855  ASP A OD2  1 
ATOM   5356  N N    . ARG A 1 856  ? 142.659 111.144 79.247  1.00 20.56 ?  856  ARG A N    1 
ATOM   5357  C CA   . ARG A 1 856  ? 143.022 112.330 78.484  1.00 23.89 ?  856  ARG A CA   1 
ATOM   5358  C C    . ARG A 1 856  ? 143.977 113.249 79.239  1.00 25.93 ?  856  ARG A C    1 
ATOM   5359  O O    . ARG A 1 856  ? 144.200 114.386 78.810  1.00 25.56 ?  856  ARG A O    1 
ATOM   5360  C CB   . ARG A 1 856  ? 141.762 113.093 78.072  1.00 22.89 ?  856  ARG A CB   1 
ATOM   5361  C CG   . ARG A 1 856  ? 140.917 113.576 79.237  1.00 20.85 ?  856  ARG A CG   1 
ATOM   5362  C CD   . ARG A 1 856  ? 139.529 113.988 78.772  1.00 24.53 ?  856  ARG A CD   1 
ATOM   5363  N NE   . ARG A 1 856  ? 139.145 115.299 79.282  1.00 25.19 ?  856  ARG A NE   1 
ATOM   5364  C CZ   . ARG A 1 856  ? 138.567 115.504 80.458  1.00 26.03 ?  856  ARG A CZ   1 
ATOM   5365  N NH1  . ARG A 1 856  ? 138.289 114.502 81.276  1.00 23.06 ?  856  ARG A NH1  1 
ATOM   5366  N NH2  . ARG A 1 856  ? 138.261 116.746 80.822  1.00 26.57 ?  856  ARG A NH2  1 
ATOM   5367  N N    . MET A 1 857  ? 144.553 112.780 80.348  1.00 22.96 ?  857  MET A N    1 
ATOM   5368  C CA   . MET A 1 857  ? 145.469 113.581 81.154  1.00 20.80 ?  857  MET A CA   1 
ATOM   5369  C C    . MET A 1 857  ? 146.870 112.979 81.210  1.00 23.83 ?  857  MET A C    1 
ATOM   5370  O O    . MET A 1 857  ? 147.679 113.380 82.053  1.00 24.85 ?  857  MET A O    1 
ATOM   5371  C CB   . MET A 1 857  ? 144.918 113.763 82.570  1.00 21.30 ?  857  MET A CB   1 
ATOM   5372  C CG   . MET A 1 857  ? 143.605 114.529 82.646  1.00 26.10 ?  857  MET A CG   1 
ATOM   5373  S SD   . MET A 1 857  ? 143.560 115.969 81.561  1.00 32.31 ?  857  MET A SD   1 
ATOM   5374  C CE   . MET A 1 857  ? 142.222 116.908 82.294  1.00 22.55 ?  857  MET A CE   1 
ATOM   5375  N N    . VAL A 1 858  ? 147.176 112.024 80.333  1.00 27.86 ?  858  VAL A N    1 
ATOM   5376  C CA   . VAL A 1 858  ? 148.479 111.370 80.291  1.00 27.09 ?  858  VAL A CA   1 
ATOM   5377  C C    . VAL A 1 858  ? 149.004 111.448 78.865  1.00 25.98 ?  858  VAL A C    1 
ATOM   5378  O O    . VAL A 1 858  ? 148.286 111.112 77.917  1.00 27.06 ?  858  VAL A O    1 
ATOM   5379  C CB   . VAL A 1 858  ? 148.398 109.905 80.767  1.00 26.06 ?  858  VAL A CB   1 
ATOM   5380  C CG1  . VAL A 1 858  ? 149.690 109.163 80.461  1.00 23.54 ?  858  VAL A CG1  1 
ATOM   5381  C CG2  . VAL A 1 858  ? 148.091 109.847 82.255  1.00 24.09 ?  858  VAL A CG2  1 
ATOM   5382  N N    . ASP A 1 859  ? 150.255 111.890 78.713  1.00 25.36 ?  859  ASP A N    1 
ATOM   5383  C CA   . ASP A 1 859  ? 150.869 112.087 77.405  1.00 26.37 ?  859  ASP A CA   1 
ATOM   5384  C C    . ASP A 1 859  ? 151.908 111.016 77.079  1.00 25.80 ?  859  ASP A C    1 
ATOM   5385  O O    . ASP A 1 859  ? 152.896 111.293 76.397  1.00 28.95 ?  859  ASP A O    1 
ATOM   5386  C CB   . ASP A 1 859  ? 151.499 113.476 77.319  1.00 27.32 ?  859  ASP A CB   1 
ATOM   5387  C CG   . ASP A 1 859  ? 150.465 114.584 77.285  1.00 29.24 ?  859  ASP A CG   1 
ATOM   5388  O OD1  . ASP A 1 859  ? 149.310 114.308 76.899  1.00 27.15 ?  859  ASP A OD1  1 
ATOM   5389  O OD2  . ASP A 1 859  ? 150.808 115.731 77.641  1.00 28.82 ?  859  ASP A OD2  1 
ATOM   5390  N N    . ASN A 1 860  ? 151.700 109.790 77.557  1.00 23.16 ?  860  ASN A N    1 
ATOM   5391  C CA   . ASN A 1 860  ? 152.592 108.684 77.230  1.00 27.10 ?  860  ASN A CA   1 
ATOM   5392  C C    . ASN A 1 860  ? 151.781 107.400 77.165  1.00 27.82 ?  860  ASN A C    1 
ATOM   5393  O O    . ASN A 1 860  ? 151.056 107.078 78.111  1.00 27.56 ?  860  ASN A O    1 
ATOM   5394  C CB   . ASN A 1 860  ? 153.717 108.544 78.260  1.00 26.68 ?  860  ASN A CB   1 
ATOM   5395  C CG   . ASN A 1 860  ? 154.621 107.360 77.976  1.00 28.70 ?  860  ASN A CG   1 
ATOM   5396  O OD1  . ASN A 1 860  ? 154.678 106.406 78.752  1.00 24.87 ?  860  ASN A OD1  1 
ATOM   5397  N ND2  . ASN A 1 860  ? 155.337 107.417 76.859  1.00 27.28 ?  860  ASN A ND2  1 
ATOM   5398  N N    . LYS A 1 861  ? 151.912 106.674 76.051  1.00 23.27 ?  861  LYS A N    1 
ATOM   5399  C CA   . LYS A 1 861  ? 151.143 105.446 75.865  1.00 24.73 ?  861  LYS A CA   1 
ATOM   5400  C C    . LYS A 1 861  ? 151.555 104.369 76.861  1.00 24.41 ?  861  LYS A C    1 
ATOM   5401  O O    . LYS A 1 861  ? 150.698 103.663 77.407  1.00 24.56 ?  861  LYS A O    1 
ATOM   5402  C CB   . LYS A 1 861  ? 151.305 104.940 74.432  1.00 24.74 ?  861  LYS A CB   1 
ATOM   5403  C CG   . LYS A 1 861  ? 150.414 105.641 73.418  1.00 24.24 ?  861  LYS A CG   1 
ATOM   5404  C CD   . LYS A 1 861  ? 151.128 106.813 72.760  1.00 24.11 ?  861  LYS A CD   1 
ATOM   5405  C CE   . LYS A 1 861  ? 152.403 106.368 72.060  1.00 23.97 ?  861  LYS A CE   1 
ATOM   5406  N NZ   . LYS A 1 861  ? 153.096 107.505 71.393  1.00 26.19 ?  861  LYS A NZ   1 
ATOM   5407  N N    . LYS A 1 862  ? 152.861 104.226 77.108  1.00 20.75 ?  862  LYS A N    1 
ATOM   5408  C CA   . LYS A 1 862  ? 153.343 103.194 78.022  1.00 27.11 ?  862  LYS A CA   1 
ATOM   5409  C C    . LYS A 1 862  ? 152.873 103.447 79.449  1.00 27.43 ?  862  LYS A C    1 
ATOM   5410  O O    . LYS A 1 862  ? 152.444 102.516 80.144  1.00 28.05 ?  862  LYS A O    1 
ATOM   5411  C CB   . LYS A 1 862  ? 154.869 103.120 77.969  1.00 24.74 ?  862  LYS A CB   1 
ATOM   5412  C CG   . LYS A 1 862  ? 155.419 102.168 76.917  1.00 24.16 ?  862  LYS A CG   1 
ATOM   5413  C CD   . LYS A 1 862  ? 155.465 102.814 75.539  1.00 25.53 ?  862  LYS A CD   1 
ATOM   5414  C CE   . LYS A 1 862  ? 156.229 104.131 75.564  1.00 24.89 ?  862  LYS A CE   1 
ATOM   5415  N NZ   . LYS A 1 862  ? 156.116 104.867 74.274  1.00 21.09 ?  862  LYS A NZ   1 
ATOM   5416  N N    . ILE A 1 863  ? 152.941 104.703 79.898  1.00 20.66 ?  863  ILE A N    1 
ATOM   5417  C CA   . ILE A 1 863  ? 152.543 105.034 81.263  1.00 24.19 ?  863  ILE A CA   1 
ATOM   5418  C C    . ILE A 1 863  ? 151.051 104.787 81.458  1.00 24.72 ?  863  ILE A C    1 
ATOM   5419  O O    . ILE A 1 863  ? 150.637 104.159 82.440  1.00 23.23 ?  863  ILE A O    1 
ATOM   5420  C CB   . ILE A 1 863  ? 152.937 106.485 81.596  1.00 24.93 ?  863  ILE A CB   1 
ATOM   5421  C CG1  . ILE A 1 863  ? 154.403 106.547 82.031  1.00 25.41 ?  863  ILE A CG1  1 
ATOM   5422  C CG2  . ILE A 1 863  ? 152.046 107.063 82.689  1.00 22.54 ?  863  ILE A CG2  1 
ATOM   5423  C CD1  . ILE A 1 863  ? 154.928 107.952 82.221  1.00 26.34 ?  863  ILE A CD1  1 
ATOM   5424  N N    . LEU A 1 864  ? 150.226 105.246 80.510  1.00 24.65 ?  864  LEU A N    1 
ATOM   5425  C CA   . LEU A 1 864  ? 148.784 105.049 80.637  1.00 26.62 ?  864  LEU A CA   1 
ATOM   5426  C C    . LEU A 1 864  ? 148.418 103.573 80.538  1.00 27.87 ?  864  LEU A C    1 
ATOM   5427  O O    . LEU A 1 864  ? 147.495 103.114 81.221  1.00 30.80 ?  864  LEU A O    1 
ATOM   5428  C CB   . LEU A 1 864  ? 148.033 105.882 79.590  1.00 24.96 ?  864  LEU A CB   1 
ATOM   5429  C CG   . LEU A 1 864  ? 147.947 105.504 78.106  1.00 22.70 ?  864  LEU A CG   1 
ATOM   5430  C CD1  . LEU A 1 864  ? 146.703 104.678 77.803  1.00 19.97 ?  864  LEU A CD1  1 
ATOM   5431  C CD2  . LEU A 1 864  ? 147.950 106.759 77.248  1.00 24.75 ?  864  LEU A CD2  1 
ATOM   5432  N N    . ARG A 1 865  ? 149.139 102.812 79.708  1.00 23.98 ?  865  ARG A N    1 
ATOM   5433  C CA   . ARG A 1 865  ? 148.903 101.373 79.625  1.00 24.85 ?  865  ARG A CA   1 
ATOM   5434  C C    . ARG A 1 865  ? 149.215 100.684 80.948  1.00 22.55 ?  865  ARG A C    1 
ATOM   5435  O O    . ARG A 1 865  ? 148.444 99.833  81.410  1.00 20.91 ?  865  ARG A O    1 
ATOM   5436  C CB   . ARG A 1 865  ? 149.739 100.774 78.495  1.00 20.80 ?  865  ARG A CB   1 
ATOM   5437  C CG   . ARG A 1 865  ? 149.254 99.420  78.009  1.00 20.13 ?  865  ARG A CG   1 
ATOM   5438  C CD   . ARG A 1 865  ? 150.367 98.654  77.310  1.00 21.21 ?  865  ARG A CD   1 
ATOM   5439  N NE   . ARG A 1 865  ? 151.646 98.787  77.998  1.00 22.29 ?  865  ARG A NE   1 
ATOM   5440  C CZ   . ARG A 1 865  ? 152.043 98.013  78.999  1.00 25.28 ?  865  ARG A CZ   1 
ATOM   5441  N NH1  . ARG A 1 865  ? 151.283 97.034  79.459  1.00 22.93 ?  865  ARG A NH1  1 
ATOM   5442  N NH2  . ARG A 1 865  ? 153.235 98.226  79.550  1.00 27.15 ?  865  ARG A NH2  1 
ATOM   5443  N N    . GLU A 1 866  ? 150.334 101.053 81.580  1.00 20.05 ?  866  GLU A N    1 
ATOM   5444  C CA   . GLU A 1 866  ? 150.687 100.472 82.873  1.00 23.26 ?  866  GLU A CA   1 
ATOM   5445  C C    . GLU A 1 866  ? 149.660 100.829 83.943  1.00 26.30 ?  866  GLU A C    1 
ATOM   5446  O O    . GLU A 1 866  ? 149.271 99.977  84.757  1.00 24.78 ?  866  GLU A O    1 
ATOM   5447  C CB   . GLU A 1 866  ? 152.079 100.945 83.292  1.00 22.30 ?  866  GLU A CB   1 
ATOM   5448  C CG   . GLU A 1 866  ? 152.774 100.038 84.291  1.00 25.66 ?  866  GLU A CG   1 
ATOM   5449  C CD   . GLU A 1 866  ? 152.571 98.570  83.979  1.00 28.52 ?  866  GLU A CD   1 
ATOM   5450  O OE1  . GLU A 1 866  ? 153.097 98.105  82.946  1.00 25.69 ?  866  GLU A OE1  1 
ATOM   5451  O OE2  . GLU A 1 866  ? 151.889 97.881  84.765  1.00 29.81 ?  866  GLU A OE2  1 
ATOM   5452  N N    . LEU A 1 867  ? 149.213 102.089 83.956  1.00 24.31 ?  867  LEU A N    1 
ATOM   5453  C CA   . LEU A 1 867  ? 148.229 102.522 84.945  1.00 22.59 ?  867  LEU A CA   1 
ATOM   5454  C C    . LEU A 1 867  ? 146.899 101.799 84.753  1.00 22.83 ?  867  LEU A C    1 
ATOM   5455  O O    . LEU A 1 867  ? 146.272 101.360 85.728  1.00 23.03 ?  867  LEU A O    1 
ATOM   5456  C CB   . LEU A 1 867  ? 148.044 104.039 84.863  1.00 20.12 ?  867  LEU A CB   1 
ATOM   5457  C CG   . LEU A 1 867  ? 149.290 104.873 85.190  1.00 22.80 ?  867  LEU A CG   1 
ATOM   5458  C CD1  . LEU A 1 867  ? 149.027 106.368 85.041  1.00 23.34 ?  867  LEU A CD1  1 
ATOM   5459  C CD2  . LEU A 1 867  ? 149.847 104.546 86.567  1.00 20.89 ?  867  LEU A CD2  1 
ATOM   5460  N N    . LYS A 1 868  ? 146.466 101.644 83.499  1.00 21.91 ?  868  LYS A N    1 
ATOM   5461  C CA   . LYS A 1 868  ? 145.241 100.903 83.219  1.00 22.27 ?  868  LYS A CA   1 
ATOM   5462  C C    . LYS A 1 868  ? 145.373 99.444  83.638  1.00 26.68 ?  868  LYS A C    1 
ATOM   5463  O O    . LYS A 1 868  ? 144.430 98.863  84.189  1.00 30.44 ?  868  LYS A O    1 
ATOM   5464  C CB   . LYS A 1 868  ? 144.897 101.010 81.733  1.00 20.66 ?  868  LYS A CB   1 
ATOM   5465  C CG   . LYS A 1 868  ? 144.251 102.330 81.339  1.00 23.77 ?  868  LYS A CG   1 
ATOM   5466  C CD   . LYS A 1 868  ? 143.878 102.349 79.865  1.00 26.15 ?  868  LYS A CD   1 
ATOM   5467  C CE   . LYS A 1 868  ? 143.210 103.662 79.480  1.00 27.48 ?  868  LYS A CE   1 
ATOM   5468  N NZ   . LYS A 1 868  ? 142.885 103.724 78.028  1.00 26.61 ?  868  LYS A NZ   1 
ATOM   5469  N N    . HIS A 1 869  ? 146.544 98.842  83.401  1.00 20.74 ?  869  HIS A N    1 
ATOM   5470  C CA   . HIS A 1 869  ? 146.758 97.446  83.772  1.00 19.63 ?  869  HIS A CA   1 
ATOM   5471  C C    . HIS A 1 869  ? 146.667 97.247  85.282  1.00 21.06 ?  869  HIS A C    1 
ATOM   5472  O O    . HIS A 1 869  ? 145.980 96.331  85.758  1.00 24.71 ?  869  HIS A O    1 
ATOM   5473  C CB   . HIS A 1 869  ? 148.114 96.974  83.244  1.00 21.09 ?  869  HIS A CB   1 
ATOM   5474  C CG   . HIS A 1 869  ? 148.510 95.611  83.720  1.00 24.51 ?  869  HIS A CG   1 
ATOM   5475  N ND1  . HIS A 1 869  ? 149.301 95.412  84.831  1.00 23.34 ?  869  HIS A ND1  1 
ATOM   5476  C CD2  . HIS A 1 869  ? 148.230 94.379  83.232  1.00 25.91 ?  869  HIS A CD2  1 
ATOM   5477  C CE1  . HIS A 1 869  ? 149.489 94.116  85.009  1.00 24.20 ?  869  HIS A CE1  1 
ATOM   5478  N NE2  . HIS A 1 869  ? 148.849 93.468  84.053  1.00 26.97 ?  869  HIS A NE2  1 
ATOM   5479  N N    . ILE A 1 870  ? 147.345 98.103  86.056  1.00 16.94 ?  870  ILE A N    1 
ATOM   5480  C CA   . ILE A 1 870  ? 147.336 97.915  87.507  1.00 21.23 ?  870  ILE A CA   1 
ATOM   5481  C C    . ILE A 1 870  ? 145.948 98.210  88.077  1.00 21.11 ?  870  ILE A C    1 
ATOM   5482  O O    . ILE A 1 870  ? 145.477 97.512  88.990  1.00 20.91 ?  870  ILE A O    1 
ATOM   5483  C CB   . ILE A 1 870  ? 148.442 98.752  88.186  1.00 23.27 ?  870  ILE A CB   1 
ATOM   5484  C CG1  . ILE A 1 870  ? 148.400 98.580  89.706  1.00 21.39 ?  870  ILE A CG1  1 
ATOM   5485  C CG2  . ILE A 1 870  ? 148.332 100.223 87.851  1.00 22.19 ?  870  ILE A CG2  1 
ATOM   5486  C CD1  . ILE A 1 870  ? 149.212 97.408  90.207  1.00 20.27 ?  870  ILE A CD1  1 
ATOM   5487  N N    . SER A 1 871  ? 145.254 99.216  87.526  1.00 19.45 ?  871  SER A N    1 
ATOM   5488  C CA   . SER A 1 871  ? 143.898 99.514  87.980  1.00 19.25 ?  871  SER A CA   1 
ATOM   5489  C C    . SER A 1 871  ? 142.948 98.355  87.697  1.00 19.84 ?  871  SER A C    1 
ATOM   5490  O O    . SER A 1 871  ? 142.137 97.983  88.557  1.00 20.34 ?  871  SER A O    1 
ATOM   5491  C CB   . SER A 1 871  ? 143.398 100.794 87.312  1.00 18.15 ?  871  SER A CB   1 
ATOM   5492  O OG   . SER A 1 871  ? 142.428 101.445 88.112  1.00 15.88 ?  871  SER A OG   1 
ATOM   5493  N N    . GLU A 1 872  ? 143.043 97.765  86.500  1.00 17.93 ?  872  GLU A N    1 
ATOM   5494  C CA   . GLU A 1 872  ? 142.193 96.630  86.154  1.00 15.69 ?  872  GLU A CA   1 
ATOM   5495  C C    . GLU A 1 872  ? 142.474 95.433  87.053  1.00 16.70 ?  872  GLU A C    1 
ATOM   5496  O O    . GLU A 1 872  ? 141.540 94.752  87.500  1.00 19.78 ?  872  GLU A O    1 
ATOM   5497  C CB   . GLU A 1 872  ? 142.399 96.255  84.687  1.00 12.75 ?  872  GLU A CB   1 
ATOM   5498  C CG   . GLU A 1 872  ? 141.334 95.332  84.122  1.00 18.86 ?  872  GLU A CG   1 
ATOM   5499  C CD   . GLU A 1 872  ? 140.389 96.046  83.176  1.00 23.25 ?  872  GLU A CD   1 
ATOM   5500  O OE1  . GLU A 1 872  ? 140.807 97.052  82.565  1.00 21.07 ?  872  GLU A OE1  1 
ATOM   5501  O OE2  . GLU A 1 872  ? 139.229 95.603  83.045  1.00 24.29 ?  872  GLU A OE2  1 
ATOM   5502  N N    . THR A 1 873  ? 143.754 95.164  87.333  1.00 17.63 ?  873  THR A N    1 
ATOM   5503  C CA   . THR A 1 873  ? 144.109 94.036  88.193  1.00 17.91 ?  873  THR A CA   1 
ATOM   5504  C C    . THR A 1 873  ? 143.548 94.218  89.601  1.00 19.79 ?  873  THR A C    1 
ATOM   5505  O O    . THR A 1 873  ? 142.948 93.292  90.171  1.00 23.60 ?  873  THR A O    1 
ATOM   5506  C CB   . THR A 1 873  ? 145.632 93.874  88.225  1.00 18.93 ?  873  THR A CB   1 
ATOM   5507  O OG1  . THR A 1 873  ? 146.068 93.218  87.029  1.00 21.11 ?  873  THR A OG1  1 
ATOM   5508  C CG2  . THR A 1 873  ? 146.074 93.054  89.431  1.00 16.11 ?  873  THR A CG2  1 
ATOM   5509  N N    . GLY A 1 874  ? 143.707 95.420  90.165  1.00 17.64 ?  874  GLY A N    1 
ATOM   5510  C CA   . GLY A 1 874  ? 143.176 95.676  91.496  1.00 14.99 ?  874  GLY A CA   1 
ATOM   5511  C C    . GLY A 1 874  ? 141.663 95.581  91.557  1.00 15.82 ?  874  GLY A C    1 
ATOM   5512  O O    . GLY A 1 874  ? 141.104 94.995  92.492  1.00 15.40 ?  874  GLY A O    1 
ATOM   5513  N N    . ARG A 1 875  ? 140.980 96.144  90.553  1.00 16.54 ?  875  ARG A N    1 
ATOM   5514  C CA   . ARG A 1 875  ? 139.521 96.088  90.521  1.00 12.44 ?  875  ARG A CA   1 
ATOM   5515  C C    . ARG A 1 875  ? 139.023 94.651  90.412  1.00 13.94 ?  875  ARG A C    1 
ATOM   5516  O O    . ARG A 1 875  ? 138.070 94.264  91.102  1.00 22.52 ?  875  ARG A O    1 
ATOM   5517  C CB   . ARG A 1 875  ? 138.996 96.933  89.359  1.00 11.43 ?  875  ARG A CB   1 
ATOM   5518  C CG   . ARG A 1 875  ? 137.571 96.615  88.942  1.00 13.45 ?  875  ARG A CG   1 
ATOM   5519  C CD   . ARG A 1 875  ? 137.124 97.480  87.776  1.00 12.26 ?  875  ARG A CD   1 
ATOM   5520  N NE   . ARG A 1 875  ? 137.490 96.899  86.490  1.00 17.78 ?  875  ARG A NE   1 
ATOM   5521  C CZ   . ARG A 1 875  ? 136.839 95.905  85.901  1.00 21.59 ?  875  ARG A CZ   1 
ATOM   5522  N NH1  . ARG A 1 875  ? 135.765 95.360  86.448  1.00 18.24 ?  875  ARG A NH1  1 
ATOM   5523  N NH2  . ARG A 1 875  ? 137.274 95.450  84.729  1.00 21.79 ?  875  ARG A NH2  1 
ATOM   5524  N N    . LEU A 1 876  ? 139.664 93.842  89.562  1.00 11.76 ?  876  LEU A N    1 
ATOM   5525  C CA   . LEU A 1 876  ? 139.255 92.449  89.411  1.00 12.64 ?  876  LEU A CA   1 
ATOM   5526  C C    . LEU A 1 876  ? 139.462 91.663  90.700  1.00 17.70 ?  876  LEU A C    1 
ATOM   5527  O O    . LEU A 1 876  ? 138.597 90.868  91.096  1.00 19.22 ?  876  LEU A O    1 
ATOM   5528  C CB   . LEU A 1 876  ? 140.022 91.800  88.260  1.00 13.61 ?  876  LEU A CB   1 
ATOM   5529  C CG   . LEU A 1 876  ? 139.397 91.907  86.867  1.00 19.91 ?  876  LEU A CG   1 
ATOM   5530  C CD1  . LEU A 1 876  ? 140.013 90.882  85.928  1.00 18.80 ?  876  LEU A CD1  1 
ATOM   5531  C CD2  . LEU A 1 876  ? 137.888 91.739  86.934  1.00 18.66 ?  876  LEU A CD2  1 
ATOM   5532  N N    . GLN A 1 877  ? 140.598 91.876  91.374  1.00 16.27 ?  877  GLN A N    1 
ATOM   5533  C CA   . GLN A 1 877  ? 140.839 91.183  92.637  1.00 14.46 ?  877  GLN A CA   1 
ATOM   5534  C C    . GLN A 1 877  ? 139.798 91.564  93.685  1.00 12.53 ?  877  GLN A C    1 
ATOM   5535  O O    . GLN A 1 877  ? 139.260 90.692  94.386  1.00 21.42 ?  877  GLN A O    1 
ATOM   5536  C CB   . GLN A 1 877  ? 142.246 91.492  93.146  1.00 19.84 ?  877  GLN A CB   1 
ATOM   5537  C CG   . GLN A 1 877  ? 142.660 90.692  94.373  1.00 20.93 ?  877  GLN A CG   1 
ATOM   5538  C CD   . GLN A 1 877  ? 142.735 89.202  94.101  1.00 22.65 ?  877  GLN A CD   1 
ATOM   5539  O OE1  . GLN A 1 877  ? 142.288 88.387  94.909  1.00 25.14 ?  877  GLN A OE1  1 
ATOM   5540  N NE2  . GLN A 1 877  ? 143.310 88.837  92.961  1.00 19.22 ?  877  GLN A NE2  1 
ATOM   5541  N N    . VAL A 1 878  ? 139.482 92.860  93.785  1.00 4.20  ?  878  VAL A N    1 
ATOM   5542  C CA   . VAL A 1 878  ? 138.518 93.314  94.785  1.00 2.74  ?  878  VAL A CA   1 
ATOM   5543  C C    . VAL A 1 878  ? 137.133 92.746  94.498  1.00 6.40  ?  878  VAL A C    1 
ATOM   5544  O O    . VAL A 1 878  ? 136.432 92.291  95.413  1.00 8.63  ?  878  VAL A O    1 
ATOM   5545  C CB   . VAL A 1 878  ? 138.505 94.853  94.851  1.00 10.75 ?  878  VAL A CB   1 
ATOM   5546  C CG1  . VAL A 1 878  ? 137.297 95.354  95.625  1.00 5.42  ?  878  VAL A CG1  1 
ATOM   5547  C CG2  . VAL A 1 878  ? 139.785 95.359  95.488  1.00 17.89 ?  878  VAL A CG2  1 
ATOM   5548  N N    . VAL A 1 879  ? 136.721 92.742  93.227  1.00 11.67 ?  879  VAL A N    1 
ATOM   5549  C CA   . VAL A 1 879  ? 135.381 92.257  92.909  1.00 8.03  ?  879  VAL A CA   1 
ATOM   5550  C C    . VAL A 1 879  ? 135.278 90.743  93.105  1.00 11.80 ?  879  VAL A C    1 
ATOM   5551  O O    . VAL A 1 879  ? 134.235 90.245  93.552  1.00 13.96 ?  879  VAL A O    1 
ATOM   5552  C CB   . VAL A 1 879  ? 134.957 92.714  91.495  1.00 3.70  ?  879  VAL A CB   1 
ATOM   5553  C CG1  . VAL A 1 879  ? 135.593 91.880  90.395  1.00 7.51  ?  879  VAL A CG1  1 
ATOM   5554  C CG2  . VAL A 1 879  ? 133.445 92.692  91.367  1.00 9.22  ?  879  VAL A CG2  1 
ATOM   5555  N N    . LYS A 1 880  ? 136.353 89.990  92.830  1.00 14.54 ?  880  LYS A N    1 
ATOM   5556  C CA   . LYS A 1 880  ? 136.320 88.552  93.092  1.00 9.75  ?  880  LYS A CA   1 
ATOM   5557  C C    . LYS A 1 880  ? 136.230 88.264  94.586  1.00 6.57  ?  880  LYS A C    1 
ATOM   5558  O O    . LYS A 1 880  ? 135.466 87.383  95.012  1.00 16.17 ?  880  LYS A O    1 
ATOM   5559  C CB   . LYS A 1 880  ? 137.552 87.875  92.494  1.00 13.71 ?  880  LYS A CB   1 
ATOM   5560  C CG   . LYS A 1 880  ? 137.562 86.365  92.666  1.00 14.56 ?  880  LYS A CG   1 
ATOM   5561  C CD   . LYS A 1 880  ? 138.706 85.719  91.904  1.00 14.59 ?  880  LYS A CD   1 
ATOM   5562  C CE   . LYS A 1 880  ? 139.227 84.491  92.634  1.00 14.51 ?  880  LYS A CE   1 
ATOM   5563  N NZ   . LYS A 1 880  ? 139.421 84.743  94.088  1.00 18.44 ?  880  LYS A NZ   1 
ATOM   5564  N N    . GLU A 1 881  ? 137.001 88.999  95.395  1.00 9.13  ?  881  GLU A N    1 
ATOM   5565  C CA   . GLU A 1 881  ? 136.940 88.805  96.841  1.00 11.18 ?  881  GLU A CA   1 
ATOM   5566  C C    . GLU A 1 881  ? 135.563 89.159  97.392  1.00 11.81 ?  881  GLU A C    1 
ATOM   5567  O O    . GLU A 1 881  ? 135.043 88.464  98.273  1.00 18.61 ?  881  GLU A O    1 
ATOM   5568  C CB   . GLU A 1 881  ? 138.029 89.629  97.526  1.00 14.30 ?  881  GLU A CB   1 
ATOM   5569  C CG   . GLU A 1 881  ? 139.438 89.138  97.235  1.00 15.65 ?  881  GLU A CG   1 
ATOM   5570  C CD   . GLU A 1 881  ? 140.394 89.380  98.385  1.00 20.45 ?  881  GLU A CD   1 
ATOM   5571  O OE1  . GLU A 1 881  ? 140.865 90.527  98.536  1.00 17.86 ?  881  GLU A OE1  1 
ATOM   5572  O OE2  . GLU A 1 881  ? 140.683 88.422  99.132  1.00 23.77 ?  881  GLU A OE2  1 
ATOM   5573  N N    . LEU A 1 882  ? 134.950 90.229  96.875  1.00 8.55  ?  882  LEU A N    1 
ATOM   5574  C CA   . LEU A 1 882  ? 133.610 90.603  97.324  1.00 5.88  ?  882  LEU A CA   1 
ATOM   5575  C C    . LEU A 1 882  ? 132.574 89.554  96.931  1.00 6.50  ?  882  LEU A C    1 
ATOM   5576  O O    . LEU A 1 882  ? 131.660 89.254  97.711  1.00 11.15 ?  882  LEU A O    1 
ATOM   5577  C CB   . LEU A 1 882  ? 133.230 91.970  96.760  1.00 8.47  ?  882  LEU A CB   1 
ATOM   5578  C CG   . LEU A 1 882  ? 133.159 93.118  97.768  1.00 5.13  ?  882  LEU A CG   1 
ATOM   5579  C CD1  . LEU A 1 882  ? 134.446 93.208  98.570  1.00 7.61  ?  882  LEU A CD1  1 
ATOM   5580  C CD2  . LEU A 1 882  ? 132.866 94.434  97.066  1.00 6.19  ?  882  LEU A CD2  1 
ATOM   5581  N N    . GLY A 1 883  ? 132.697 88.987  95.727  1.00 8.55  ?  883  GLY A N    1 
ATOM   5582  C CA   . GLY A 1 883  ? 131.786 87.924  95.327  1.00 12.05 ?  883  GLY A CA   1 
ATOM   5583  C C    . GLY A 1 883  ? 131.902 86.690  96.202  1.00 9.96  ?  883  GLY A C    1 
ATOM   5584  O O    . GLY A 1 883  ? 130.892 86.097  96.596  1.00 11.83 ?  883  GLY A O    1 
ATOM   5585  N N    . LEU A 1 884  ? 133.134 86.293  96.533  1.00 6.75  ?  884  LEU A N    1 
ATOM   5586  C CA   . LEU A 1 884  ? 133.312 85.147  97.423  1.00 6.51  ?  884  LEU A CA   1 
ATOM   5587  C C    . LEU A 1 884  ? 132.792 85.445  98.828  1.00 10.97 ?  884  LEU A C    1 
ATOM   5588  O O    . LEU A 1 884  ? 132.218 84.565  99.485  1.00 16.83 ?  884  LEU A O    1 
ATOM   5589  C CB   . LEU A 1 884  ? 134.783 84.736  97.464  1.00 11.42 ?  884  LEU A CB   1 
ATOM   5590  C CG   . LEU A 1 884  ? 135.311 84.041  96.206  1.00 13.51 ?  884  LEU A CG   1 
ATOM   5591  C CD1  . LEU A 1 884  ? 136.666 83.408  96.474  1.00 12.04 ?  884  LEU A CD1  1 
ATOM   5592  C CD2  . LEU A 1 884  ? 134.321 83.001  95.703  1.00 10.40 ?  884  LEU A CD2  1 
ATOM   5593  N N    . LEU A 1 885  ? 132.981 86.683  99.300  1.00 12.59 ?  885  LEU A N    1 
ATOM   5594  C CA   . LEU A 1 885  ? 132.454 87.080  100.603 1.00 10.67 ?  885  LEU A CA   1 
ATOM   5595  C C    . LEU A 1 885  ? 130.932 87.014  100.628 1.00 15.81 ?  885  LEU A C    1 
ATOM   5596  O O    . LEU A 1 885  ? 130.337 86.638  101.645 1.00 16.29 ?  885  LEU A O    1 
ATOM   5597  C CB   . LEU A 1 885  ? 132.938 88.487  100.949 1.00 9.91  ?  885  LEU A CB   1 
ATOM   5598  C CG   . LEU A 1 885  ? 132.653 89.030  102.348 1.00 9.22  ?  885  LEU A CG   1 
ATOM   5599  C CD1  . LEU A 1 885  ? 133.709 88.561  103.334 1.00 10.79 ?  885  LEU A CD1  1 
ATOM   5600  C CD2  . LEU A 1 885  ? 132.588 90.548  102.309 1.00 9.87  ?  885  LEU A CD2  1 
ATOM   5601  N N    . GLN A 1 886  ? 130.285 87.392  99.523  1.00 17.44 ?  886  GLN A N    1 
ATOM   5602  C CA   . GLN A 1 886  ? 128.840 87.202  99.416  1.00 11.82 ?  886  GLN A CA   1 
ATOM   5603  C C    . GLN A 1 886  ? 128.477 85.724  99.430  1.00 8.60  ?  886  GLN A C    1 
ATOM   5604  O O    . GLN A 1 886  ? 127.483 85.325  100.048 1.00 8.65  ?  886  GLN A O    1 
ATOM   5605  C CB   . GLN A 1 886  ? 128.305 87.849  98.142  1.00 11.82 ?  886  GLN A CB   1 
ATOM   5606  C CG   . GLN A 1 886  ? 126.798 88.047  98.155  1.00 10.56 ?  886  GLN A CG   1 
ATOM   5607  C CD   . GLN A 1 886  ? 126.074 87.121  97.199  1.00 15.88 ?  886  GLN A CD   1 
ATOM   5608  O OE1  . GLN A 1 886  ? 126.662 86.610  96.247  1.00 17.88 ?  886  GLN A OE1  1 
ATOM   5609  N NE2  . GLN A 1 886  ? 124.790 86.899  97.450  1.00 12.38 ?  886  GLN A NE2  1 
ATOM   5610  N N    . ARG A 1 887  ? 129.266 84.901  98.735  1.00 10.93 ?  887  ARG A N    1 
ATOM   5611  C CA   . ARG A 1 887  ? 128.966 83.475  98.632  1.00 16.42 ?  887  ARG A CA   1 
ATOM   5612  C C    . ARG A 1 887  ? 129.056 82.771  99.983  1.00 18.52 ?  887  ARG A C    1 
ATOM   5613  O O    . ARG A 1 887  ? 128.290 81.835  100.242 1.00 15.30 ?  887  ARG A O    1 
ATOM   5614  C CB   . ARG A 1 887  ? 129.910 82.827  97.615  1.00 16.48 ?  887  ARG A CB   1 
ATOM   5615  C CG   . ARG A 1 887  ? 129.876 81.306  97.562  1.00 16.02 ?  887  ARG A CG   1 
ATOM   5616  C CD   . ARG A 1 887  ? 128.585 80.794  96.944  1.00 15.51 ?  887  ARG A CD   1 
ATOM   5617  N NE   . ARG A 1 887  ? 128.773 79.516  96.268  1.00 19.16 ?  887  ARG A NE   1 
ATOM   5618  C CZ   . ARG A 1 887  ? 127.786 78.758  95.810  1.00 19.74 ?  887  ARG A CZ   1 
ATOM   5619  N NH1  . ARG A 1 887  ? 126.520 79.121  95.936  1.00 18.82 ?  887  ARG A NH1  1 
ATOM   5620  N NH2  . ARG A 1 887  ? 128.076 77.605  95.213  1.00 20.76 ?  887  ARG A NH2  1 
ATOM   5621  N N    . GLU A 1 888  ? 129.961 83.221  100.859 1.00 22.93 ?  888  GLU A N    1 
ATOM   5622  C CA   . GLU A 1 888  ? 130.223 82.492  102.100 1.00 18.39 ?  888  GLU A CA   1 
ATOM   5623  C C    . GLU A 1 888  ? 129.011 82.477  103.035 1.00 18.93 ?  888  GLU A C    1 
ATOM   5624  O O    . GLU A 1 888  ? 128.716 81.445  103.650 1.00 20.86 ?  888  GLU A O    1 
ATOM   5625  C CB   . GLU A 1 888  ? 131.444 83.086  102.802 1.00 17.29 ?  888  GLU A CB   1 
ATOM   5626  C CG   . GLU A 1 888  ? 131.956 82.255  103.966 1.00 21.49 ?  888  GLU A CG   1 
ATOM   5627  C CD   . GLU A 1 888  ? 133.324 82.703  104.445 1.00 24.85 ?  888  GLU A CD   1 
ATOM   5628  O OE1  . GLU A 1 888  ? 134.187 81.831  104.681 1.00 24.10 ?  888  GLU A OE1  1 
ATOM   5629  O OE2  . GLU A 1 888  ? 133.534 83.925  104.592 1.00 21.04 ?  888  GLU A OE2  1 
ATOM   5630  N N    . HIS A 1 889  ? 128.289 83.600  103.155 1.00 21.37 ?  889  HIS A N    1 
ATOM   5631  C CA   . HIS A 1 889  ? 127.134 83.672  104.051 1.00 15.64 ?  889  HIS A CA   1 
ATOM   5632  C C    . HIS A 1 889  ? 126.057 84.581  103.468 1.00 13.07 ?  889  HIS A C    1 
ATOM   5633  O O    . HIS A 1 889  ? 126.210 85.809  103.476 1.00 14.71 ?  889  HIS A O    1 
ATOM   5634  C CB   . HIS A 1 889  ? 127.551 84.176  105.433 1.00 13.26 ?  889  HIS A CB   1 
ATOM   5635  C CG   . HIS A 1 889  ? 128.741 85.080  105.407 1.00 15.35 ?  889  HIS A CG   1 
ATOM   5636  N ND1  . HIS A 1 889  ? 130.034 84.607  105.381 1.00 12.55 ?  889  HIS A ND1  1 
ATOM   5637  C CD2  . HIS A 1 889  ? 128.834 86.430  105.403 1.00 17.35 ?  889  HIS A CD2  1 
ATOM   5638  C CE1  . HIS A 1 889  ? 130.873 85.626  105.347 1.00 18.66 ?  889  HIS A CE1  1 
ATOM   5639  N NE2  . HIS A 1 889  ? 130.171 86.744  105.370 1.00 17.77 ?  889  HIS A NE2  1 
ATOM   5640  N N    . PRO A 1 890  ? 124.948 84.022  102.971 1.00 10.64 ?  890  PRO A N    1 
ATOM   5641  C CA   . PRO A 1 890  ? 123.990 84.831  102.202 1.00 14.93 ?  890  PRO A CA   1 
ATOM   5642  C C    . PRO A 1 890  ? 123.118 85.774  103.021 1.00 12.84 ?  890  PRO A C    1 
ATOM   5643  O O    . PRO A 1 890  ? 122.758 86.846  102.527 1.00 14.38 ?  890  PRO A O    1 
ATOM   5644  C CB   . PRO A 1 890  ? 123.129 83.772  101.501 1.00 13.89 ?  890  PRO A CB   1 
ATOM   5645  C CG   . PRO A 1 890  ? 123.241 82.561  102.353 1.00 12.47 ?  890  PRO A CG   1 
ATOM   5646  C CD   . PRO A 1 890  ? 124.607 82.589  102.966 1.00 10.21 ?  890  PRO A CD   1 
ATOM   5647  N N    . GLY A 1 891  ? 122.753 85.391  104.247 1.00 8.48  ?  891  GLY A N    1 
ATOM   5648  C CA   . GLY A 1 891  ? 121.803 86.192  105.009 1.00 4.24  ?  891  GLY A CA   1 
ATOM   5649  C C    . GLY A 1 891  ? 122.336 87.567  105.371 1.00 6.69  ?  891  GLY A C    1 
ATOM   5650  O O    . GLY A 1 891  ? 121.656 88.584  105.186 1.00 13.99 ?  891  GLY A O    1 
ATOM   5651  N N    . ILE A 1 892  ? 123.571 87.614  105.873 1.00 10.92 ?  892  ILE A N    1 
ATOM   5652  C CA   . ILE A 1 892  ? 124.188 88.883  106.244 1.00 9.85  ?  892  ILE A CA   1 
ATOM   5653  C C    . ILE A 1 892  ? 124.397 89.756  105.013 1.00 8.87  ?  892  ILE A C    1 
ATOM   5654  O O    . ILE A 1 892  ? 124.206 90.979  105.061 1.00 16.36 ?  892  ILE A O    1 
ATOM   5655  C CB   . ILE A 1 892  ? 125.510 88.620  106.987 1.00 8.77  ?  892  ILE A CB   1 
ATOM   5656  C CG1  . ILE A 1 892  ? 125.335 87.494  108.011 1.00 8.58  ?  892  ILE A CG1  1 
ATOM   5657  C CG2  . ILE A 1 892  ? 126.006 89.884  107.646 1.00 8.46  ?  892  ILE A CG2  1 
ATOM   5658  C CD1  . ILE A 1 892  ? 124.671 87.921  109.299 1.00 10.67 ?  892  ILE A CD1  1 
ATOM   5659  N N    . ALA A 1 893  ? 124.790 89.142  103.892 1.00 0.19  ?  893  ALA A N    1 
ATOM   5660  C CA   . ALA A 1 893  ? 124.996 89.890  102.657 1.00 0.00  ?  893  ALA A CA   1 
ATOM   5661  C C    . ALA A 1 893  ? 123.695 90.495  102.145 1.00 0.51  ?  893  ALA A C    1 
ATOM   5662  O O    . ALA A 1 893  ? 123.668 91.654  101.712 1.00 10.99 ?  893  ALA A O    1 
ATOM   5663  C CB   . ALA A 1 893  ? 125.619 88.983  101.597 1.00 6.61  ?  893  ALA A CB   1 
ATOM   5664  N N    . VAL A 1 894  ? 122.604 89.726  102.192 1.00 4.84  ?  894  VAL A N    1 
ATOM   5665  C CA   . VAL A 1 894  ? 121.308 90.246  101.762 1.00 1.81  ?  894  VAL A CA   1 
ATOM   5666  C C    . VAL A 1 894  ? 120.871 91.391  102.665 1.00 0.17  ?  894  VAL A C    1 
ATOM   5667  O O    . VAL A 1 894  ? 120.364 92.416  102.190 1.00 6.65  ?  894  VAL A O    1 
ATOM   5668  C CB   . VAL A 1 894  ? 120.264 89.113  101.724 1.00 0.31  ?  894  VAL A CB   1 
ATOM   5669  C CG1  . VAL A 1 894  ? 118.859 89.675  101.622 1.00 3.29  ?  894  VAL A CG1  1 
ATOM   5670  C CG2  . VAL A 1 894  ? 120.538 88.189  100.556 1.00 4.78  ?  894  VAL A CG2  1 
ATOM   5671  N N    . SER A 1 895  ? 121.096 91.251  103.975 1.00 1.45  ?  895  SER A N    1 
ATOM   5672  C CA   . SER A 1 895  ? 120.723 92.307  104.911 1.00 1.24  ?  895  SER A CA   1 
ATOM   5673  C C    . SER A 1 895  ? 121.486 93.601  104.636 1.00 1.61  ?  895  SER A C    1 
ATOM   5674  O O    . SER A 1 895  ? 120.891 94.688  104.579 1.00 7.47  ?  895  SER A O    1 
ATOM   5675  C CB   . SER A 1 895  ? 120.966 91.837  106.343 1.00 5.37  ?  895  SER A CB   1 
ATOM   5676  O OG   . SER A 1 895  ? 120.856 92.916  107.252 1.00 8.29  ?  895  SER A OG   1 
ATOM   5677  N N    . VAL A 1 896  ? 122.805 93.505  104.442 1.00 0.61  ?  896  VAL A N    1 
ATOM   5678  C CA   . VAL A 1 896  ? 123.593 94.721  104.253 1.00 0.43  ?  896  VAL A CA   1 
ATOM   5679  C C    . VAL A 1 896  ? 123.289 95.362  102.899 1.00 3.30  ?  896  VAL A C    1 
ATOM   5680  O O    . VAL A 1 896  ? 123.231 96.594  102.782 1.00 8.02  ?  896  VAL A O    1 
ATOM   5681  C CB   . VAL A 1 896  ? 125.099 94.446  104.447 1.00 0.00  ?  896  VAL A CB   1 
ATOM   5682  C CG1  . VAL A 1 896  ? 125.625 93.420  103.473 1.00 0.58  ?  896  VAL A CG1  1 
ATOM   5683  C CG2  . VAL A 1 896  ? 125.887 95.730  104.319 1.00 7.33  ?  896  VAL A CG2  1 
ATOM   5684  N N    . LYS A 1 897  ? 123.055 94.548  101.861 1.00 1.82  ?  897  LYS A N    1 
ATOM   5685  C CA   . LYS A 1 897  ? 122.729 95.113  100.556 1.00 0.00  ?  897  LYS A CA   1 
ATOM   5686  C C    . LYS A 1 897  ? 121.362 95.794  100.571 1.00 0.00  ?  897  LYS A C    1 
ATOM   5687  O O    . LYS A 1 897  ? 121.180 96.855  99.955  1.00 7.84  ?  897  LYS A O    1 
ATOM   5688  C CB   . LYS A 1 897  ? 122.796 94.021  99.490  1.00 0.00  ?  897  LYS A CB   1 
ATOM   5689  C CG   . LYS A 1 897  ? 124.131 93.974  98.758  1.00 0.00  ?  897  LYS A CG   1 
ATOM   5690  C CD   . LYS A 1 897  ? 124.578 92.548  98.486  1.00 0.00  ?  897  LYS A CD   1 
ATOM   5691  C CE   . LYS A 1 897  ? 125.913 92.509  97.764  1.00 3.80  ?  897  LYS A CE   1 
ATOM   5692  N NZ   . LYS A 1 897  ? 126.192 91.165  97.195  1.00 12.46 ?  897  LYS A NZ   1 
ATOM   5693  N N    . THR A 1 898  ? 120.393 95.208  101.285 1.00 1.43  ?  898  THR A N    1 
ATOM   5694  C CA   . THR A 1 898  ? 119.089 95.847  101.435 1.00 0.00  ?  898  THR A CA   1 
ATOM   5695  C C    . THR A 1 898  ? 119.207 97.174  102.174 1.00 0.00  ?  898  THR A C    1 
ATOM   5696  O O    . THR A 1 898  ? 118.569 98.165  101.791 1.00 5.11  ?  898  THR A O    1 
ATOM   5697  C CB   . THR A 1 898  ? 118.131 94.909  102.168 1.00 0.00  ?  898  THR A CB   1 
ATOM   5698  O OG1  . THR A 1 898  ? 118.023 93.675  101.449 1.00 0.47  ?  898  THR A OG1  1 
ATOM   5699  C CG2  . THR A 1 898  ? 116.756 95.533  102.284 1.00 4.93  ?  898  THR A CG2  1 
ATOM   5700  N N    . ARG A 1 899  ? 120.025 97.215  103.231 1.00 0.00  ?  899  ARG A N    1 
ATOM   5701  C CA   . ARG A 1 899  ? 120.236 98.468  103.952 1.00 4.21  ?  899  ARG A CA   1 
ATOM   5702  C C    . ARG A 1 899  ? 120.874 99.526  103.058 1.00 2.81  ?  899  ARG A C    1 
ATOM   5703  O O    . ARG A 1 899  ? 120.495 100.704 103.114 1.00 5.08  ?  899  ARG A O    1 
ATOM   5704  C CB   . ARG A 1 899  ? 121.095 98.223  105.191 1.00 0.49  ?  899  ARG A CB   1 
ATOM   5705  C CG   . ARG A 1 899  ? 121.173 99.413  106.131 1.00 2.71  ?  899  ARG A CG   1 
ATOM   5706  C CD   . ARG A 1 899  ? 121.615 98.995  107.523 1.00 5.26  ?  899  ARG A CD   1 
ATOM   5707  N NE   . ARG A 1 899  ? 123.013 98.586  107.559 1.00 9.95  ?  899  ARG A NE   1 
ATOM   5708  C CZ   . ARG A 1 899  ? 123.424 97.359  107.848 1.00 9.55  ?  899  ARG A CZ   1 
ATOM   5709  N NH1  . ARG A 1 899  ? 122.567 96.392  108.130 1.00 8.06  ?  899  ARG A NH1  1 
ATOM   5710  N NH2  . ARG A 1 899  ? 124.728 97.097  107.858 1.00 3.09  ?  899  ARG A NH2  1 
ATOM   5711  N N    . GLN A 1 900  ? 121.836 99.122  102.223 1.00 0.00  ?  900  GLN A N    1 
ATOM   5712  C CA   . GLN A 1 900  ? 122.462 100.053 101.285 1.00 0.00  ?  900  GLN A CA   1 
ATOM   5713  C C    . GLN A 1 900  ? 121.439 100.639 100.317 1.00 0.51  ?  900  GLN A C    1 
ATOM   5714  O O    . GLN A 1 900  ? 121.408 101.856 100.083 1.00 4.88  ?  900  GLN A O    1 
ATOM   5715  C CB   . GLN A 1 900  ? 123.573 99.342  100.511 1.00 1.48  ?  900  GLN A CB   1 
ATOM   5716  C CG   . GLN A 1 900  ? 124.952 99.421  101.142 1.00 1.81  ?  900  GLN A CG   1 
ATOM   5717  C CD   . GLN A 1 900  ? 126.055 99.037  100.170 1.00 1.19  ?  900  GLN A CD   1 
ATOM   5718  O OE1  . GLN A 1 900  ? 126.053 97.939  99.615  1.00 0.00  ?  900  GLN A OE1  1 
ATOM   5719  N NE2  . GLN A 1 900  ? 126.998 99.946  99.954  1.00 2.85  ?  900  GLN A NE2  1 
ATOM   5720  N N    . ALA A 1 901  ? 120.587 99.779  99.746  1.00 0.00  ?  901  ALA A N    1 
ATOM   5721  C CA   . ALA A 1 901  ? 119.587 100.249 98.790  1.00 0.00  ?  901  ALA A CA   1 
ATOM   5722  C C    . ALA A 1 901  ? 118.588 101.202 99.441  1.00 0.00  ?  901  ALA A C    1 
ATOM   5723  O O    . ALA A 1 901  ? 118.244 102.246 98.865  1.00 11.41 ?  901  ALA A O    1 
ATOM   5724  C CB   . ALA A 1 901  ? 118.863 99.059  98.165  1.00 0.00  ?  901  ALA A CB   1 
ATOM   5725  N N    . ILE A 1 902  ? 118.117 100.863 100.645 1.00 3.62  ?  902  ILE A N    1 
ATOM   5726  C CA   . ILE A 1 902  ? 117.152 101.719 101.331 1.00 0.00  ?  902  ILE A CA   1 
ATOM   5727  C C    . ILE A 1 902  ? 117.778 103.065 101.682 1.00 2.50  ?  902  ILE A C    1 
ATOM   5728  O O    . ILE A 1 902  ? 117.134 104.115 101.553 1.00 6.57  ?  902  ILE A O    1 
ATOM   5729  C CB   . ILE A 1 902  ? 116.591 101.004 102.573 1.00 0.00  ?  902  ILE A CB   1 
ATOM   5730  C CG1  . ILE A 1 902  ? 115.812 99.758  102.158 1.00 0.00  ?  902  ILE A CG1  1 
ATOM   5731  C CG2  . ILE A 1 902  ? 115.684 101.927 103.367 1.00 2.97  ?  902  ILE A CG2  1 
ATOM   5732  C CD1  . ILE A 1 902  ? 115.287 98.954  103.322 1.00 5.43  ?  902  ILE A CD1  1 
ATOM   5733  N N    . ARG A 1 903  ? 119.042 103.060 102.120 1.00 4.33  ?  903  ARG A N    1 
ATOM   5734  C CA   . ARG A 1 903  ? 119.726 104.313 102.428 1.00 1.38  ?  903  ARG A CA   1 
ATOM   5735  C C    . ARG A 1 903  ? 119.867 105.190 101.189 1.00 0.00  ?  903  ARG A C    1 
ATOM   5736  O O    . ARG A 1 903  ? 119.677 106.412 101.261 1.00 6.90  ?  903  ARG A O    1 
ATOM   5737  C CB   . ARG A 1 903  ? 121.094 104.014 103.041 1.00 0.00  ?  903  ARG A CB   1 
ATOM   5738  C CG   . ARG A 1 903  ? 121.931 105.237 103.357 1.00 3.04  ?  903  ARG A CG   1 
ATOM   5739  C CD   . ARG A 1 903  ? 123.281 104.838 103.937 1.00 3.16  ?  903  ARG A CD   1 
ATOM   5740  N NE   . ARG A 1 903  ? 124.245 104.479 102.904 1.00 5.48  ?  903  ARG A NE   1 
ATOM   5741  C CZ   . ARG A 1 903  ? 125.095 103.464 102.992 1.00 7.62  ?  903  ARG A CZ   1 
ATOM   5742  N NH1  . ARG A 1 903  ? 125.127 102.680 104.057 1.00 6.82  ?  903  ARG A NH1  1 
ATOM   5743  N NH2  . ARG A 1 903  ? 125.933 103.231 101.987 1.00 6.91  ?  903  ARG A NH2  1 
ATOM   5744  N N    . THR A 1 904  ? 120.189 104.582 100.042 1.00 0.00  ?  904  THR A N    1 
ATOM   5745  C CA   . THR A 1 904  ? 120.283 105.341 98.796  1.00 0.00  ?  904  THR A CA   1 
ATOM   5746  C C    . THR A 1 904  ? 118.946 105.987 98.437  1.00 0.00  ?  904  THR A C    1 
ATOM   5747  O O    . THR A 1 904  ? 118.886 107.179 98.096  1.00 6.34  ?  904  THR A O    1 
ATOM   5748  C CB   . THR A 1 904  ? 120.756 104.425 97.666  1.00 0.00  ?  904  THR A CB   1 
ATOM   5749  O OG1  . THR A 1 904  ? 122.120 104.050 97.892  1.00 9.16  ?  904  THR A OG1  1 
ATOM   5750  C CG2  . THR A 1 904  ? 120.645 105.122 96.320  1.00 0.00  ?  904  THR A CG2  1 
ATOM   5751  N N    . ILE A 1 905  ? 117.859 105.213 98.529  1.00 0.00  ?  905  ILE A N    1 
ATOM   5752  C CA   . ILE A 1 905  ? 116.540 105.741 98.177  1.00 0.00  ?  905  ILE A CA   1 
ATOM   5753  C C    . ILE A 1 905  ? 116.143 106.880 99.111  1.00 0.00  ?  905  ILE A C    1 
ATOM   5754  O O    . ILE A 1 905  ? 115.620 107.913 98.666  1.00 3.30  ?  905  ILE A O    1 
ATOM   5755  C CB   . ILE A 1 905  ? 115.489 104.616 98.183  1.00 0.00  ?  905  ILE A CB   1 
ATOM   5756  C CG1  . ILE A 1 905  ? 115.820 103.568 97.127  1.00 0.00  ?  905  ILE A CG1  1 
ATOM   5757  C CG2  . ILE A 1 905  ? 114.105 105.177 97.922  1.00 2.66  ?  905  ILE A CG2  1 
ATOM   5758  C CD1  . ILE A 1 905  ? 114.876 102.396 97.128  1.00 0.00  ?  905  ILE A CD1  1 
ATOM   5759  N N    . LEU A 1 906  ? 116.386 106.716 100.415 1.00 2.85  ?  906  LEU A N    1 
ATOM   5760  C CA   . LEU A 1 906  ? 116.018 107.757 101.371 1.00 0.46  ?  906  LEU A CA   1 
ATOM   5761  C C    . LEU A 1 906  ? 116.830 109.030 101.158 1.00 0.00  ?  906  LEU A C    1 
ATOM   5762  O O    . LEU A 1 906  ? 116.286 110.139 101.253 1.00 7.40  ?  906  LEU A O    1 
ATOM   5763  C CB   . LEU A 1 906  ? 116.184 107.245 102.800 1.00 1.32  ?  906  LEU A CB   1 
ATOM   5764  C CG   . LEU A 1 906  ? 115.206 106.153 103.235 1.00 0.00  ?  906  LEU A CG   1 
ATOM   5765  C CD1  . LEU A 1 906  ? 115.610 105.580 104.580 1.00 4.54  ?  906  LEU A CD1  1 
ATOM   5766  C CD2  . LEU A 1 906  ? 113.789 106.695 103.281 1.00 5.57  ?  906  LEU A CD2  1 
ATOM   5767  N N    . ASN A 1 907  ? 118.127 108.894 100.860 1.00 1.07  ?  907  ASN A N    1 
ATOM   5768  C CA   . ASN A 1 907  ? 118.947 110.070 100.579 1.00 2.08  ?  907  ASN A CA   1 
ATOM   5769  C C    . ASN A 1 907  ? 118.450 110.812 99.344  1.00 3.59  ?  907  ASN A C    1 
ATOM   5770  O O    . ASN A 1 907  ? 118.382 112.050 99.336  1.00 11.11 ?  907  ASN A O    1 
ATOM   5771  C CB   . ASN A 1 907  ? 120.408 109.660 100.399 1.00 7.29  ?  907  ASN A CB   1 
ATOM   5772  C CG   . ASN A 1 907  ? 121.061 109.242 101.699 1.00 12.11 ?  907  ASN A CG   1 
ATOM   5773  O OD1  . ASN A 1 907  ? 120.728 109.752 102.768 1.00 15.61 ?  907  ASN A OD1  1 
ATOM   5774  N ND2  . ASN A 1 907  ? 122.002 108.311 101.614 1.00 7.27  ?  907  ASN A ND2  1 
ATOM   5775  N N    . HIS A 1 908  ? 118.084 110.074 98.294  1.00 5.15  ?  908  HIS A N    1 
ATOM   5776  C CA   . HIS A 1 908  ? 117.611 110.737 97.082  1.00 1.57  ?  908  HIS A CA   1 
ATOM   5777  C C    . HIS A 1 908  ? 116.253 111.402 97.296  1.00 2.99  ?  908  HIS A C    1 
ATOM   5778  O O    . HIS A 1 908  ? 115.987 112.475 96.739  1.00 6.97  ?  908  HIS A O    1 
ATOM   5779  C CB   . HIS A 1 908  ? 117.564 109.740 95.928  1.00 2.28  ?  908  HIS A CB   1 
ATOM   5780  C CG   . HIS A 1 908  ? 118.893 109.527 95.274  1.00 1.81  ?  908  HIS A CG   1 
ATOM   5781  N ND1  . HIS A 1 908  ? 120.055 109.355 95.994  1.00 6.71  ?  908  HIS A ND1  1 
ATOM   5782  C CD2  . HIS A 1 908  ? 119.248 109.472 93.969  1.00 7.68  ?  908  HIS A CD2  1 
ATOM   5783  C CE1  . HIS A 1 908  ? 121.068 109.196 95.161  1.00 7.59  ?  908  HIS A CE1  1 
ATOM   5784  N NE2  . HIS A 1 908  ? 120.605 109.263 93.926  1.00 10.48 ?  908  HIS A NE2  1 
ATOM   5785  N N    . SER A 1 909  ? 115.388 110.796 98.115  1.00 6.29  ?  909  SER A N    1 
ATOM   5786  C CA   . SER A 1 909  ? 114.108 111.432 98.423  1.00 5.11  ?  909  SER A CA   1 
ATOM   5787  C C    . SER A 1 909  ? 114.302 112.701 99.250  1.00 3.01  ?  909  SER A C    1 
ATOM   5788  O O    . SER A 1 909  ? 113.579 113.689 99.063  1.00 8.74  ?  909  SER A O    1 
ATOM   5789  C CB   . SER A 1 909  ? 113.193 110.451 99.151  1.00 3.72  ?  909  SER A CB   1 
ATOM   5790  O OG   . SER A 1 909  ? 113.287 110.616 100.553 1.00 10.23 ?  909  SER A OG   1 
ATOM   5791  N N    . ARG A 1 910  ? 115.274 112.693 100.166 1.00 0.49  ?  910  ARG A N    1 
ATOM   5792  C CA   . ARG A 1 910  ? 115.601 113.906 100.912 1.00 0.00  ?  910  ARG A CA   1 
ATOM   5793  C C    . ARG A 1 910  ? 116.118 115.002 99.985  1.00 7.57  ?  910  ARG A C    1 
ATOM   5794  O O    . ARG A 1 910  ? 115.782 116.184 100.154 1.00 13.56 ?  910  ARG A O    1 
ATOM   5795  C CB   . ARG A 1 910  ? 116.629 113.586 101.994 1.00 3.03  ?  910  ARG A CB   1 
ATOM   5796  C CG   . ARG A 1 910  ? 116.967 114.745 102.910 1.00 8.10  ?  910  ARG A CG   1 
ATOM   5797  C CD   . ARG A 1 910  ? 118.134 114.395 103.819 1.00 12.86 ?  910  ARG A CD   1 
ATOM   5798  N NE   . ARG A 1 910  ? 118.282 112.954 103.988 1.00 18.96 ?  910  ARG A NE   1 
ATOM   5799  C CZ   . ARG A 1 910  ? 118.037 112.302 105.116 1.00 12.78 ?  910  ARG A CZ   1 
ATOM   5800  N NH1  . ARG A 1 910  ? 117.634 112.934 106.206 1.00 14.20 ?  910  ARG A NH1  1 
ATOM   5801  N NH2  . ARG A 1 910  ? 118.203 110.983 105.152 1.00 7.14  ?  910  ARG A NH2  1 
ATOM   5802  N N    . GLU A 1 911  ? 116.940 114.626 99.000  1.00 10.03 ?  911  GLU A N    1 
ATOM   5803  C CA   . GLU A 1 911  ? 117.402 115.594 98.007  1.00 8.66  ?  911  GLU A CA   1 
ATOM   5804  C C    . GLU A 1 911  ? 116.237 116.169 97.208  1.00 5.93  ?  911  GLU A C    1 
ATOM   5805  O O    . GLU A 1 911  ? 116.214 117.367 96.902  1.00 10.66 ?  911  GLU A O    1 
ATOM   5806  C CB   . GLU A 1 911  ? 118.416 114.944 97.067  1.00 10.15 ?  911  GLU A CB   1 
ATOM   5807  C CG   . GLU A 1 911  ? 119.856 115.039 97.534  1.00 12.83 ?  911  GLU A CG   1 
ATOM   5808  C CD   . GLU A 1 911  ? 120.794 114.200 96.688  1.00 15.68 ?  911  GLU A CD   1 
ATOM   5809  O OE1  . GLU A 1 911  ? 120.590 114.138 95.458  1.00 11.72 ?  911  GLU A OE1  1 
ATOM   5810  O OE2  . GLU A 1 911  ? 121.734 113.603 97.253  1.00 15.43 ?  911  GLU A OE2  1 
ATOM   5811  N N    . THR A 1 912  ? 115.267 115.322 96.851  1.00 7.83  ?  912  THR A N    1 
ATOM   5812  C CA   . THR A 1 912  ? 114.081 115.798 96.140  1.00 7.56  ?  912  THR A CA   1 
ATOM   5813  C C    . THR A 1 912  ? 113.282 116.781 96.991  1.00 8.25  ?  912  THR A C    1 
ATOM   5814  O O    . THR A 1 912  ? 112.794 117.800 96.485  1.00 15.47 ?  912  THR A O    1 
ATOM   5815  C CB   . THR A 1 912  ? 113.212 114.608 95.727  1.00 4.73  ?  912  THR A CB   1 
ATOM   5816  O OG1  . THR A 1 912  ? 113.918 113.815 94.766  1.00 5.93  ?  912  THR A OG1  1 
ATOM   5817  C CG2  . THR A 1 912  ? 111.903 115.075 95.111  1.00 2.65  ?  912  THR A CG2  1 
ATOM   5818  N N    . ILE A 1 913  ? 113.147 116.494 98.290  1.00 12.34 ?  913  ILE A N    1 
ATOM   5819  C CA   . ILE A 1 913  ? 112.444 117.405 99.195  1.00 12.93 ?  913  ILE A CA   1 
ATOM   5820  C C    . ILE A 1 913  ? 113.152 118.754 99.256  1.00 8.91  ?  913  ILE A C    1 
ATOM   5821  O O    . ILE A 1 913  ? 112.512 119.813 99.185  1.00 8.51  ?  913  ILE A O    1 
ATOM   5822  C CB   . ILE A 1 913  ? 112.314 116.772 100.595 1.00 13.65 ?  913  ILE A CB   1 
ATOM   5823  C CG1  . ILE A 1 913  ? 111.198 115.730 100.614 1.00 9.29  ?  913  ILE A CG1  1 
ATOM   5824  C CG2  . ILE A 1 913  ? 112.049 117.832 101.654 1.00 11.83 ?  913  ILE A CG2  1 
ATOM   5825  C CD1  . ILE A 1 913  ? 111.392 114.659 101.657 1.00 10.03 ?  913  ILE A CD1  1 
ATOM   5826  N N    . HIS A 1 914  ? 114.482 118.739 99.378  1.00 10.97 ?  914  HIS A N    1 
ATOM   5827  C CA   . HIS A 1 914  ? 115.232 119.993 99.438  1.00 11.78 ?  914  HIS A CA   1 
ATOM   5828  C C    . HIS A 1 914  ? 115.136 120.773 98.131  1.00 8.77  ?  914  HIS A C    1 
ATOM   5829  O O    . HIS A 1 914  ? 115.058 122.008 98.146  1.00 11.97 ?  914  HIS A O    1 
ATOM   5830  C CB   . HIS A 1 914  ? 116.690 119.720 99.798  1.00 18.41 ?  914  HIS A CB   1 
ATOM   5831  C CG   . HIS A 1 914  ? 116.900 119.401 101.245 1.00 14.06 ?  914  HIS A CG   1 
ATOM   5832  N ND1  . HIS A 1 914  ? 116.074 119.883 102.237 1.00 17.01 ?  914  HIS A ND1  1 
ATOM   5833  C CD2  . HIS A 1 914  ? 117.838 118.649 101.868 1.00 17.50 ?  914  HIS A CD2  1 
ATOM   5834  C CE1  . HIS A 1 914  ? 116.496 119.444 103.410 1.00 19.31 ?  914  HIS A CE1  1 
ATOM   5835  N NE2  . HIS A 1 914  ? 117.564 118.692 103.213 1.00 22.07 ?  914  HIS A NE2  1 
ATOM   5836  N N    . GLU A 1 915  ? 115.143 120.077 96.991  1.00 9.67  ?  915  GLU A N    1 
ATOM   5837  C CA   . GLU A 1 915  ? 115.010 120.765 95.710  1.00 8.51  ?  915  GLU A CA   1 
ATOM   5838  C C    . GLU A 1 915  ? 113.618 121.363 95.541  1.00 13.92 ?  915  GLU A C    1 
ATOM   5839  O O    . GLU A 1 915  ? 113.467 122.435 94.944  1.00 19.72 ?  915  GLU A O    1 
ATOM   5840  C CB   . GLU A 1 915  ? 115.330 119.810 94.562  1.00 12.92 ?  915  GLU A CB   1 
ATOM   5841  C CG   . GLU A 1 915  ? 116.794 119.809 94.161  1.00 18.36 ?  915  GLU A CG   1 
ATOM   5842  C CD   . GLU A 1 915  ? 117.267 118.454 93.674  1.00 19.05 ?  915  GLU A CD   1 
ATOM   5843  O OE1  . GLU A 1 915  ? 116.456 117.719 93.073  1.00 17.32 ?  915  GLU A OE1  1 
ATOM   5844  O OE2  . GLU A 1 915  ? 118.451 118.124 93.893  1.00 16.11 ?  915  GLU A OE2  1 
ATOM   5845  N N    . LEU A 1 916  ? 112.588 120.679 96.046  1.00 17.47 ?  916  LEU A N    1 
ATOM   5846  C CA   . LEU A 1 916  ? 111.248 121.257 96.051  1.00 10.17 ?  916  LEU A CA   1 
ATOM   5847  C C    . LEU A 1 916  ? 111.184 122.496 96.935  1.00 9.01  ?  916  LEU A C    1 
ATOM   5848  O O    . LEU A 1 916  ? 110.537 123.488 96.579  1.00 10.78 ?  916  LEU A O    1 
ATOM   5849  C CB   . LEU A 1 916  ? 110.227 120.223 96.522  1.00 9.67  ?  916  LEU A CB   1 
ATOM   5850  C CG   . LEU A 1 916  ? 109.420 119.498 95.450  1.00 7.73  ?  916  LEU A CG   1 
ATOM   5851  C CD1  . LEU A 1 916  ? 108.360 118.628 96.097  1.00 8.91  ?  916  LEU A CD1  1 
ATOM   5852  C CD2  . LEU A 1 916  ? 108.788 120.496 94.497  1.00 11.45 ?  916  LEU A CD2  1 
ATOM   5853  N N    . GLN A 1 917  ? 111.840 122.448 98.097  1.00 14.93 ?  917  GLN A N    1 
ATOM   5854  C CA   . GLN A 1 917  ? 111.838 123.592 99.004  1.00 10.72 ?  917  GLN A CA   1 
ATOM   5855  C C    . GLN A 1 917  ? 112.568 124.785 98.398  1.00 11.18 ?  917  GLN A C    1 
ATOM   5856  O O    . GLN A 1 917  ? 112.141 125.933 98.568  1.00 15.56 ?  917  GLN A O    1 
ATOM   5857  C CB   . GLN A 1 917  ? 112.465 123.198 100.341 1.00 11.64 ?  917  GLN A CB   1 
ATOM   5858  C CG   . GLN A 1 917  ? 112.188 124.167 101.475 1.00 9.64  ?  917  GLN A CG   1 
ATOM   5859  C CD   . GLN A 1 917  ? 112.877 123.763 102.762 1.00 15.49 ?  917  GLN A CD   1 
ATOM   5860  O OE1  . GLN A 1 917  ? 113.558 122.740 102.820 1.00 18.86 ?  917  GLN A OE1  1 
ATOM   5861  N NE2  . GLN A 1 917  ? 112.700 124.565 103.806 1.00 16.35 ?  917  GLN A NE2  1 
ATOM   5862  N N    . GLY A 1 918  ? 113.674 124.534 97.692  1.00 15.80 ?  918  GLY A N    1 
ATOM   5863  C CA   . GLY A 1 918  ? 114.422 125.618 97.077  1.00 11.65 ?  918  GLY A CA   1 
ATOM   5864  C C    . GLY A 1 918  ? 113.675 126.323 95.962  1.00 12.61 ?  918  GLY A C    1 
ATOM   5865  O O    . GLY A 1 918  ? 113.820 127.537 95.786  1.00 16.51 ?  918  GLY A O    1 
ATOM   5866  N N    . ALA A 1 919  ? 112.870 125.586 95.198  1.00 9.85  ?  919  ALA A N    1 
ATOM   5867  C CA   . ALA A 1 919  ? 112.135 126.155 94.075  1.00 9.21  ?  919  ALA A CA   1 
ATOM   5868  C C    . ALA A 1 919  ? 110.878 126.904 94.499  1.00 9.81  ?  919  ALA A C    1 
ATOM   5869  O O    . ALA A 1 919  ? 110.143 127.383 93.631  1.00 11.99 ?  919  ALA A O    1 
ATOM   5870  C CB   . ALA A 1 919  ? 111.763 125.055 93.078  1.00 7.50  ?  919  ALA A CB   1 
ATOM   5871  N N    . GLY A 1 920  ? 110.609 127.006 95.800  1.00 9.27  ?  920  GLY A N    1 
ATOM   5872  C CA   . GLY A 1 920  ? 109.469 127.742 96.300  1.00 8.48  ?  920  GLY A CA   1 
ATOM   5873  C C    . GLY A 1 920  ? 108.164 126.982 96.316  1.00 10.15 ?  920  GLY A C    1 
ATOM   5874  O O    . GLY A 1 920  ? 107.207 127.446 96.947  1.00 8.94  ?  920  GLY A O    1 
ATOM   5875  N N    . LEU A 1 921  ? 108.096 125.817 95.670  1.00 16.36 ?  921  LEU A N    1 
ATOM   5876  C CA   . LEU A 1 921  ? 106.854 125.060 95.573  1.00 15.11 ?  921  LEU A CA   1 
ATOM   5877  C C    . LEU A 1 921  ? 106.449 124.405 96.887  1.00 15.86 ?  921  LEU A C    1 
ATOM   5878  O O    . LEU A 1 921  ? 105.327 123.896 96.982  1.00 10.04 ?  921  LEU A O    1 
ATOM   5879  C CB   . LEU A 1 921  ? 106.983 123.997 94.481  1.00 9.18  ?  921  LEU A CB   1 
ATOM   5880  C CG   . LEU A 1 921  ? 107.433 124.520 93.116  1.00 13.10 ?  921  LEU A CG   1 
ATOM   5881  C CD1  . LEU A 1 921  ? 108.023 123.402 92.272  1.00 16.54 ?  921  LEU A CD1  1 
ATOM   5882  C CD2  . LEU A 1 921  ? 106.280 125.195 92.389  1.00 15.89 ?  921  LEU A CD2  1 
ATOM   5883  N N    . LEU A 1 922  ? 107.319 124.406 97.893  1.00 14.87 ?  922  LEU A N    1 
ATOM   5884  C CA   . LEU A 1 922  ? 107.029 123.803 99.186  1.00 14.02 ?  922  LEU A CA   1 
ATOM   5885  C C    . LEU A 1 922  ? 107.260 124.826 100.287 1.00 19.46 ?  922  LEU A C    1 
ATOM   5886  O O    . LEU A 1 922  ? 108.294 125.501 100.304 1.00 18.73 ?  922  LEU A O    1 
ATOM   5887  C CB   . LEU A 1 922  ? 107.902 122.566 99.424  1.00 15.05 ?  922  LEU A CB   1 
ATOM   5888  C CG   . LEU A 1 922  ? 107.288 121.445 100.260 1.00 15.69 ?  922  LEU A CG   1 
ATOM   5889  C CD1  . LEU A 1 922  ? 106.055 120.892 99.575  1.00 15.37 ?  922  LEU A CD1  1 
ATOM   5890  C CD2  . LEU A 1 922  ? 108.308 120.348 100.492 1.00 13.94 ?  922  LEU A CD2  1 
ATOM   5891  N N    . ASP A 1 923  ? 106.299 124.936 101.201 1.00 19.52 ?  923  ASP A N    1 
ATOM   5892  C CA   . ASP A 1 923  ? 106.466 125.795 102.361 1.00 18.86 ?  923  ASP A CA   1 
ATOM   5893  C C    . ASP A 1 923  ? 107.476 125.180 103.329 1.00 22.16 ?  923  ASP A C    1 
ATOM   5894  O O    . ASP A 1 923  ? 107.867 124.015 103.210 1.00 25.30 ?  923  ASP A O    1 
ATOM   5895  C CB   . ASP A 1 923  ? 105.126 126.024 103.060 1.00 22.41 ?  923  ASP A CB   1 
ATOM   5896  C CG   . ASP A 1 923  ? 103.971 126.139 102.083 1.00 27.69 ?  923  ASP A CG   1 
ATOM   5897  O OD1  . ASP A 1 923  ? 104.113 126.858 101.072 1.00 28.12 ?  923  ASP A OD1  1 
ATOM   5898  O OD2  . ASP A 1 923  ? 102.919 125.513 102.330 1.00 25.74 ?  923  ASP A OD2  1 
ATOM   5899  N N    . GLU A 1 924  ? 107.908 125.988 104.300 1.00 21.94 ?  924  GLU A N    1 
ATOM   5900  C CA   . GLU A 1 924  ? 108.912 125.524 105.252 1.00 20.86 ?  924  GLU A CA   1 
ATOM   5901  C C    . GLU A 1 924  ? 108.352 124.445 106.174 1.00 23.45 ?  924  GLU A C    1 
ATOM   5902  O O    . GLU A 1 924  ? 109.045 123.471 106.486 1.00 26.54 ?  924  GLU A O    1 
ATOM   5903  C CB   . GLU A 1 924  ? 109.448 126.703 106.064 1.00 16.54 ?  924  GLU A CB   1 
ATOM   5904  C CG   . GLU A 1 924  ? 110.789 127.225 105.572 1.00 19.00 ?  924  GLU A CG   1 
ATOM   5905  C CD   . GLU A 1 924  ? 111.668 127.747 106.691 1.00 26.59 ?  924  GLU A CD   1 
ATOM   5906  O OE1  . GLU A 1 924  ? 111.302 127.573 107.872 1.00 28.53 ?  924  GLU A OE1  1 
ATOM   5907  O OE2  . GLU A 1 924  ? 112.728 128.332 106.387 1.00 28.55 ?  924  GLU A OE2  1 
ATOM   5908  N N    . MET A 1 925  ? 107.100 124.598 106.612 1.00 21.64 ?  925  MET A N    1 
ATOM   5909  C CA   . MET A 1 925  ? 106.509 123.627 107.531 1.00 22.30 ?  925  MET A CA   1 
ATOM   5910  C C    . MET A 1 925  ? 106.218 122.300 106.835 1.00 23.50 ?  925  MET A C    1 
ATOM   5911  O O    . MET A 1 925  ? 106.402 121.229 107.427 1.00 29.03 ?  925  MET A O    1 
ATOM   5912  C CB   . MET A 1 925  ? 105.232 124.200 108.148 1.00 22.99 ?  925  MET A CB   1 
ATOM   5913  C CG   . MET A 1 925  ? 105.358 125.387 109.143 1.00 27.09 ?  925  MET A CG   1 
ATOM   5914  S SD   . MET A 1 925  ? 106.601 125.436 110.472 1.00 34.88 ?  925  MET A SD   1 
ATOM   5915  C CE   . MET A 1 925  ? 108.127 125.903 109.647 1.00 24.08 ?  925  MET A CE   1 
ATOM   5916  N N    . GLU A 1 926  ? 105.754 122.351 105.582 1.00 19.22 ?  926  GLU A N    1 
ATOM   5917  C CA   . GLU A 1 926  ? 105.525 121.126 104.820 1.00 20.65 ?  926  GLU A CA   1 
ATOM   5918  C C    . GLU A 1 926  ? 106.831 120.376 104.587 1.00 20.72 ?  926  GLU A C    1 
ATOM   5919  O O    . GLU A 1 926  ? 106.887 119.142 104.704 1.00 25.34 ?  926  GLU A O    1 
ATOM   5920  C CB   . GLU A 1 926  ? 104.858 121.458 103.484 1.00 20.54 ?  926  GLU A CB   1 
ATOM   5921  C CG   . GLU A 1 926  ? 103.340 121.428 103.506 1.00 22.16 ?  926  GLU A CG   1 
ATOM   5922  C CD   . GLU A 1 926  ? 102.753 122.360 104.542 1.00 26.77 ?  926  GLU A CD   1 
ATOM   5923  O OE1  . GLU A 1 926  ? 103.154 123.542 104.571 1.00 26.02 ?  926  GLU A OE1  1 
ATOM   5924  O OE2  . GLU A 1 926  ? 101.891 121.912 105.327 1.00 25.73 ?  926  GLU A OE2  1 
ATOM   5925  N N    . ALA A 1 927  ? 107.893 121.115 104.256 1.00 16.09 ?  927  ALA A N    1 
ATOM   5926  C CA   . ALA A 1 927  ? 109.209 120.512 104.097 1.00 15.70 ?  927  ALA A CA   1 
ATOM   5927  C C    . ALA A 1 927  ? 109.704 119.918 105.407 1.00 17.44 ?  927  ALA A C    1 
ATOM   5928  O O    . ALA A 1 927  ? 110.313 118.845 105.414 1.00 23.65 ?  927  ALA A O    1 
ATOM   5929  C CB   . ALA A 1 927  ? 110.199 121.549 103.570 1.00 13.37 ?  927  ALA A CB   1 
ATOM   5930  N N    . HIS A 1 928  ? 109.452 120.605 106.526 1.00 16.76 ?  928  HIS A N    1 
ATOM   5931  C CA   . HIS A 1 928  ? 109.844 120.075 107.829 1.00 16.83 ?  928  HIS A CA   1 
ATOM   5932  C C    . HIS A 1 928  ? 109.119 118.771 108.137 1.00 13.04 ?  928  HIS A C    1 
ATOM   5933  O O    . HIS A 1 928  ? 109.724 117.827 108.655 1.00 17.12 ?  928  HIS A O    1 
ATOM   5934  C CB   . HIS A 1 928  ? 109.575 121.108 108.925 1.00 16.03 ?  928  HIS A CB   1 
ATOM   5935  C CG   . HIS A 1 928  ? 110.560 122.236 108.954 1.00 15.81 ?  928  HIS A CG   1 
ATOM   5936  N ND1  . HIS A 1 928  ? 110.890 122.969 107.835 1.00 15.70 ?  928  HIS A ND1  1 
ATOM   5937  C CD2  . HIS A 1 928  ? 111.284 122.760 109.972 1.00 19.35 ?  928  HIS A CD2  1 
ATOM   5938  C CE1  . HIS A 1 928  ? 111.776 123.894 108.161 1.00 17.76 ?  928  HIS A CE1  1 
ATOM   5939  N NE2  . HIS A 1 928  ? 112.032 123.788 109.452 1.00 18.91 ?  928  HIS A NE2  1 
ATOM   5940  N N    . LYS A 1 929  ? 107.825 118.696 107.813 1.00 7.69  ?  929  LYS A N    1 
ATOM   5941  C CA   . LYS A 1 929  ? 107.073 117.462 108.039 1.00 9.97  ?  929  LYS A CA   1 
ATOM   5942  C C    . LYS A 1 929  ? 107.602 116.315 107.180 1.00 15.04 ?  929  LYS A C    1 
ATOM   5943  O O    . LYS A 1 929  ? 107.767 115.185 107.667 1.00 18.67 ?  929  LYS A O    1 
ATOM   5944  C CB   . LYS A 1 929  ? 105.589 117.698 107.762 1.00 11.18 ?  929  LYS A CB   1 
ATOM   5945  C CG   . LYS A 1 929  ? 104.874 118.509 108.832 1.00 14.48 ?  929  LYS A CG   1 
ATOM   5946  C CD   . LYS A 1 929  ? 103.373 118.547 108.583 1.00 16.69 ?  929  LYS A CD   1 
ATOM   5947  C CE   . LYS A 1 929  ? 102.913 119.927 108.139 1.00 14.93 ?  929  LYS A CE   1 
ATOM   5948  N NZ   . LYS A 1 929  ? 102.952 120.918 109.251 1.00 15.87 ?  929  LYS A NZ   1 
ATOM   5949  N N    . LEU A 1 930  ? 107.872 116.584 105.897 1.00 14.53 ?  930  LEU A N    1 
ATOM   5950  C CA   . LEU A 1 930  ? 108.390 115.534 105.019 1.00 9.79  ?  930  LEU A CA   1 
ATOM   5951  C C    . LEU A 1 930  ? 109.777 115.070 105.463 1.00 7.56  ?  930  LEU A C    1 
ATOM   5952  O O    . LEU A 1 930  ? 110.070 113.865 105.460 1.00 11.23 ?  930  LEU A O    1 
ATOM   5953  C CB   . LEU A 1 930  ? 108.414 116.029 103.574 1.00 12.35 ?  930  LEU A CB   1 
ATOM   5954  C CG   . LEU A 1 930  ? 107.042 116.259 102.932 1.00 11.05 ?  930  LEU A CG   1 
ATOM   5955  C CD1  . LEU A 1 930  ? 107.180 116.889 101.557 1.00 12.90 ?  930  LEU A CD1  1 
ATOM   5956  C CD2  . LEU A 1 930  ? 106.259 114.959 102.849 1.00 12.75 ?  930  LEU A CD2  1 
ATOM   5957  N N    . GLU A 1 931  ? 110.636 116.012 105.867 1.00 7.59  ?  931  GLU A N    1 
ATOM   5958  C CA   . GLU A 1 931  ? 111.948 115.656 106.395 1.00 10.26 ?  931  GLU A CA   1 
ATOM   5959  C C    . GLU A 1 931  ? 111.826 114.852 107.682 1.00 13.26 ?  931  GLU A C    1 
ATOM   5960  O O    . GLU A 1 931  ? 112.635 113.956 107.937 1.00 15.84 ?  931  GLU A O    1 
ATOM   5961  C CB   . GLU A 1 931  ? 112.778 116.916 106.641 1.00 16.13 ?  931  GLU A CB   1 
ATOM   5962  C CG   . GLU A 1 931  ? 113.259 117.630 105.389 1.00 17.94 ?  931  GLU A CG   1 
ATOM   5963  C CD   . GLU A 1 931  ? 114.407 116.918 104.711 1.00 20.94 ?  931  GLU A CD   1 
ATOM   5964  O OE1  . GLU A 1 931  ? 115.551 117.034 105.199 1.00 20.28 ?  931  GLU A OE1  1 
ATOM   5965  O OE2  . GLU A 1 931  ? 114.168 116.258 103.679 1.00 24.88 ?  931  GLU A OE2  1 
ATOM   5966  N N    . LEU A 1 932  ? 110.830 115.175 108.514 1.00 15.71 ?  932  LEU A N    1 
ATOM   5967  C CA   . LEU A 1 932  ? 110.598 114.417 109.738 1.00 11.41 ?  932  LEU A CA   1 
ATOM   5968  C C    . LEU A 1 932  ? 110.234 112.973 109.428 1.00 12.16 ?  932  LEU A C    1 
ATOM   5969  O O    . LEU A 1 932  ? 110.743 112.044 110.069 1.00 16.14 ?  932  LEU A O    1 
ATOM   5970  C CB   . LEU A 1 932  ? 109.491 115.081 110.554 1.00 7.65  ?  932  LEU A CB   1 
ATOM   5971  C CG   . LEU A 1 932  ? 109.522 114.917 112.071 1.00 8.72  ?  932  LEU A CG   1 
ATOM   5972  C CD1  . LEU A 1 932  ? 110.732 115.623 112.661 1.00 12.54 ?  932  LEU A CD1  1 
ATOM   5973  C CD2  . LEU A 1 932  ? 108.233 115.444 112.674 1.00 14.05 ?  932  LEU A CD2  1 
ATOM   5974  N N    . THR A 1 933  ? 109.360 112.768 108.439 1.00 9.99  ?  933  THR A N    1 
ATOM   5975  C CA   . THR A 1 933  ? 109.026 111.406 108.027 1.00 6.36  ?  933  THR A CA   1 
ATOM   5976  C C    . THR A 1 933  ? 110.257 110.674 107.502 1.00 8.53  ?  933  THR A C    1 
ATOM   5977  O O    . THR A 1 933  ? 110.466 109.491 107.807 1.00 14.12 ?  933  THR A O    1 
ATOM   5978  C CB   . THR A 1 933  ? 107.924 111.421 106.968 1.00 8.96  ?  933  THR A CB   1 
ATOM   5979  O OG1  . THR A 1 933  ? 108.373 112.147 105.817 1.00 14.07 ?  933  THR A OG1  1 
ATOM   5980  C CG2  . THR A 1 933  ? 106.663 112.071 107.514 1.00 11.34 ?  933  THR A CG2  1 
ATOM   5981  N N    . VAL A 1 934  ? 111.098 111.374 106.735 1.00 13.03 ?  934  VAL A N    1 
ATOM   5982  C CA   . VAL A 1 934  ? 112.307 110.752 106.195 1.00 9.29  ?  934  VAL A CA   1 
ATOM   5983  C C    . VAL A 1 934  ? 113.268 110.357 107.319 1.00 8.95  ?  934  VAL A C    1 
ATOM   5984  O O    . VAL A 1 934  ? 113.838 109.258 107.303 1.00 8.95  ?  934  VAL A O    1 
ATOM   5985  C CB   . VAL A 1 934  ? 112.971 111.686 105.162 1.00 10.29 ?  934  VAL A CB   1 
ATOM   5986  C CG1  . VAL A 1 934  ? 114.470 111.441 105.073 1.00 10.42 ?  934  VAL A CG1  1 
ATOM   5987  C CG2  . VAL A 1 934  ? 112.323 111.507 103.793 1.00 4.66  ?  934  VAL A CG2  1 
ATOM   5988  N N    . GLU A 1 935  ? 113.453 111.230 108.320 1.00 9.99  ?  935  GLU A N    1 
ATOM   5989  C CA   . GLU A 1 935  ? 114.356 110.880 109.418 1.00 7.69  ?  935  GLU A CA   1 
ATOM   5990  C C    . GLU A 1 935  ? 113.799 109.752 110.280 1.00 9.86  ?  935  GLU A C    1 
ATOM   5991  O O    . GLU A 1 935  ? 114.572 108.928 110.786 1.00 14.92 ?  935  GLU A O    1 
ATOM   5992  C CB   . GLU A 1 935  ? 114.695 112.079 110.316 1.00 8.64  ?  935  GLU A CB   1 
ATOM   5993  C CG   . GLU A 1 935  ? 115.360 113.284 109.648 1.00 13.44 ?  935  GLU A CG   1 
ATOM   5994  C CD   . GLU A 1 935  ? 114.953 114.613 110.274 1.00 16.70 ?  935  GLU A CD   1 
ATOM   5995  O OE1  . GLU A 1 935  ? 115.811 115.233 110.936 1.00 14.66 ?  935  GLU A OE1  1 
ATOM   5996  O OE2  . GLU A 1 935  ? 113.791 115.037 110.136 1.00 16.01 ?  935  GLU A OE2  1 
ATOM   5997  N N    . ILE A 1 936  ? 112.476 109.697 110.468 1.00 9.64  ?  936  ILE A N    1 
ATOM   5998  C CA   . ILE A 1 936  ? 111.883 108.567 111.182 1.00 4.79  ?  936  ILE A CA   1 
ATOM   5999  C C    . ILE A 1 936  ? 112.141 107.267 110.431 1.00 3.11  ?  936  ILE A C    1 
ATOM   6000  O O    . ILE A 1 936  ? 112.492 106.243 111.034 1.00 11.40 ?  936  ILE A O    1 
ATOM   6001  C CB   . ILE A 1 936  ? 110.377 108.802 111.417 1.00 11.35 ?  936  ILE A CB   1 
ATOM   6002  C CG1  . ILE A 1 936  ? 110.146 109.956 112.398 1.00 9.06  ?  936  ILE A CG1  1 
ATOM   6003  C CG2  . ILE A 1 936  ? 109.696 107.536 111.918 1.00 12.47 ?  936  ILE A CG2  1 
ATOM   6004  C CD1  . ILE A 1 936  ? 111.067 109.947 113.600 1.00 8.38  ?  936  ILE A CD1  1 
ATOM   6005  N N    . LYS A 1 937  ? 111.995 107.292 109.102 1.00 6.17  ?  937  LYS A N    1 
ATOM   6006  C CA   . LYS A 1 937  ? 112.270 106.095 108.310 1.00 10.46 ?  937  LYS A CA   1 
ATOM   6007  C C    . LYS A 1 937  ? 113.740 105.694 108.389 1.00 8.39  ?  937  LYS A C    1 
ATOM   6008  O O    . LYS A 1 937  ? 114.061 104.503 108.447 1.00 4.79  ?  937  LYS A O    1 
ATOM   6009  C CB   . LYS A 1 937  ? 111.850 106.315 106.858 1.00 8.19  ?  937  LYS A CB   1 
ATOM   6010  C CG   . LYS A 1 937  ? 110.352 106.438 106.670 1.00 8.04  ?  937  LYS A CG   1 
ATOM   6011  C CD   . LYS A 1 937  ? 109.996 106.681 105.219 1.00 13.94 ?  937  LYS A CD   1 
ATOM   6012  C CE   . LYS A 1 937  ? 109.447 105.422 104.580 1.00 15.16 ?  937  LYS A CE   1 
ATOM   6013  N NZ   . LYS A 1 937  ? 107.980 105.278 104.789 1.00 13.93 ?  937  LYS A NZ   1 
ATOM   6014  N N    . MET A 1 938  ? 114.647 106.674 108.396 1.00 8.07  ?  938  MET A N    1 
ATOM   6015  C CA   . MET A 1 938  ? 116.072 106.365 108.512 1.00 6.14  ?  938  MET A CA   1 
ATOM   6016  C C    . MET A 1 938  ? 116.404 105.745 109.866 1.00 10.30 ?  938  MET A C    1 
ATOM   6017  O O    . MET A 1 938  ? 117.175 104.777 109.942 1.00 14.83 ?  938  MET A O    1 
ATOM   6018  C CB   . MET A 1 938  ? 116.902 107.627 108.288 1.00 13.17 ?  938  MET A CB   1 
ATOM   6019  C CG   . MET A 1 938  ? 118.400 107.378 108.196 1.00 16.28 ?  938  MET A CG   1 
ATOM   6020  S SD   . MET A 1 938  ? 118.862 106.341 106.795 1.00 26.14 ?  938  MET A SD   1 
ATOM   6021  C CE   . MET A 1 938  ? 118.793 107.531 105.460 1.00 8.50  ?  938  MET A CE   1 
ATOM   6022  N N    . LYS A 1 939  ? 115.836 106.293 110.945 1.00 10.54 ?  939  LYS A N    1 
ATOM   6023  C CA   . LYS A 1 939  ? 116.078 105.737 112.273 1.00 5.27  ?  939  LYS A CA   1 
ATOM   6024  C C    . LYS A 1 939  ? 115.502 104.332 112.400 1.00 9.28  ?  939  LYS A C    1 
ATOM   6025  O O    . LYS A 1 939  ? 116.102 103.467 113.048 1.00 17.93 ?  939  LYS A O    1 
ATOM   6026  C CB   . LYS A 1 939  ? 115.497 106.658 113.346 1.00 7.12  ?  939  LYS A CB   1 
ATOM   6027  C CG   . LYS A 1 939  ? 115.910 106.287 114.763 1.00 12.57 ?  939  LYS A CG   1 
ATOM   6028  C CD   . LYS A 1 939  ? 115.673 107.428 115.740 1.00 10.59 ?  939  LYS A CD   1 
ATOM   6029  C CE   . LYS A 1 939  ? 116.537 107.277 116.983 1.00 6.22  ?  939  LYS A CE   1 
ATOM   6030  N NZ   . LYS A 1 939  ? 115.742 106.852 118.166 1.00 5.19  ?  939  LYS A NZ   1 
ATOM   6031  N N    . ARG A 1 940  ? 114.338 104.084 111.792 1.00 4.30  ?  940  ARG A N    1 
ATOM   6032  C CA   . ARG A 1 940  ? 113.786 102.733 111.798 1.00 4.41  ?  940  ARG A CA   1 
ATOM   6033  C C    . ARG A 1 940  ? 114.619 101.775 110.953 1.00 9.30  ?  940  ARG A C    1 
ATOM   6034  O O    . ARG A 1 940  ? 114.728 100.591 111.292 1.00 12.88 ?  940  ARG A O    1 
ATOM   6035  C CB   . ARG A 1 940  ? 112.339 102.753 111.308 1.00 6.64  ?  940  ARG A CB   1 
ATOM   6036  C CG   . ARG A 1 940  ? 111.371 103.422 112.268 1.00 10.08 ?  940  ARG A CG   1 
ATOM   6037  C CD   . ARG A 1 940  ? 109.933 103.242 111.819 1.00 10.22 ?  940  ARG A CD   1 
ATOM   6038  N NE   . ARG A 1 940  ? 109.006 104.031 112.623 1.00 10.55 ?  940  ARG A NE   1 
ATOM   6039  C CZ   . ARG A 1 940  ? 108.506 103.644 113.789 1.00 14.47 ?  940  ARG A CZ   1 
ATOM   6040  N NH1  . ARG A 1 940  ? 108.820 102.475 114.322 1.00 13.59 ?  940  ARG A NH1  1 
ATOM   6041  N NH2  . ARG A 1 940  ? 107.668 104.450 114.434 1.00 15.83 ?  940  ARG A NH2  1 
ATOM   6042  N N    . LEU A 1 941  ? 115.201 102.259 109.851 1.00 13.45 ?  941  LEU A N    1 
ATOM   6043  C CA   . LEU A 1 941  ? 116.065 101.416 109.028 1.00 11.49 ?  941  LEU A CA   1 
ATOM   6044  C C    . LEU A 1 941  ? 117.338 101.031 109.768 1.00 11.34 ?  941  LEU A C    1 
ATOM   6045  O O    . LEU A 1 941  ? 117.805 99.891  109.657 1.00 5.20  ?  941  LEU A O    1 
ATOM   6046  C CB   . LEU A 1 941  ? 116.405 102.129 107.718 1.00 11.64 ?  941  LEU A CB   1 
ATOM   6047  C CG   . LEU A 1 941  ? 117.675 101.664 106.996 1.00 6.57  ?  941  LEU A CG   1 
ATOM   6048  C CD1  . LEU A 1 941  ? 117.415 100.396 106.205 1.00 9.56  ?  941  LEU A CD1  1 
ATOM   6049  C CD2  . LEU A 1 941  ? 118.217 102.759 106.094 1.00 1.57  ?  941  LEU A CD2  1 
ATOM   6050  N N    . MET A 1 942  ? 117.908 101.963 110.534 1.00 14.45 ?  942  MET A N    1 
ATOM   6051  C CA   . MET A 1 942  ? 119.159 101.684 111.235 1.00 11.79 ?  942  MET A CA   1 
ATOM   6052  C C    . MET A 1 942  ? 119.024 100.611 112.313 1.00 13.21 ?  942  MET A C    1 
ATOM   6053  O O    . MET A 1 942  ? 120.049 100.111 112.788 1.00 12.44 ?  942  MET A O    1 
ATOM   6054  C CB   . MET A 1 942  ? 119.715 102.968 111.852 1.00 11.83 ?  942  MET A CB   1 
ATOM   6055  C CG   . MET A 1 942  ? 120.273 103.947 110.833 1.00 15.80 ?  942  MET A CG   1 
ATOM   6056  S SD   . MET A 1 942  ? 121.641 103.250 109.888 1.00 19.46 ?  942  MET A SD   1 
ATOM   6057  C CE   . MET A 1 942  ? 121.405 104.048 108.302 1.00 12.74 ?  942  MET A CE   1 
ATOM   6058  N N    . ASN A 1 943  ? 117.806 100.242 112.703 1.00 11.09 ?  943  ASN A N    1 
ATOM   6059  C CA   . ASN A 1 943  ? 117.562 99.185  113.677 1.00 12.01 ?  943  ASN A CA   1 
ATOM   6060  C C    . ASN A 1 943  ? 116.813 98.018  113.040 1.00 17.20 ?  943  ASN A C    1 
ATOM   6061  O O    . ASN A 1 943  ? 115.872 97.467  113.614 1.00 15.58 ?  943  ASN A O    1 
ATOM   6062  C CB   . ASN A 1 943  ? 116.803 99.725  114.887 1.00 13.51 ?  943  ASN A CB   1 
ATOM   6063  C CG   . ASN A 1 943  ? 117.623 100.717 115.691 1.00 18.55 ?  943  ASN A CG   1 
ATOM   6064  O OD1  . ASN A 1 943  ? 117.490 101.929 115.526 1.00 11.11 ?  943  ASN A OD1  1 
ATOM   6065  N ND2  . ASN A 1 943  ? 118.479 100.203 116.568 1.00 18.51 ?  943  ASN A ND2  1 
ATOM   6066  N N    . ALA A 1 944  ? 117.231 97.635  111.838 1.00 19.22 ?  944  ALA A N    1 
ATOM   6067  C CA   . ALA A 1 944  ? 116.636 96.538  111.092 1.00 15.44 ?  944  ALA A CA   1 
ATOM   6068  C C    . ALA A 1 944  ? 117.232 95.201  111.533 1.00 15.43 ?  944  ALA A C    1 
ATOM   6069  O O    . ALA A 1 944  ? 118.244 95.170  112.238 1.00 12.26 ?  944  ALA A O    1 
ATOM   6070  C CB   . ALA A 1 944  ? 116.860 96.755  109.597 1.00 16.28 ?  944  ALA A CB   1 
ATOM   6071  N N    . PRO A 1 945  ? 116.601 94.080  111.166 1.00 19.41 ?  945  PRO A N    1 
ATOM   6072  C CA   . PRO A 1 945  ? 117.232 92.774  111.399 1.00 16.62 ?  945  PRO A CA   1 
ATOM   6073  C C    . PRO A 1 945  ? 118.578 92.660  110.698 1.00 17.74 ?  945  PRO A C    1 
ATOM   6074  O O    . PRO A 1 945  ? 118.781 93.193  109.605 1.00 16.98 ?  945  PRO A O    1 
ATOM   6075  C CB   . PRO A 1 945  ? 116.217 91.784  110.821 1.00 12.60 ?  945  PRO A CB   1 
ATOM   6076  C CG   . PRO A 1 945  ? 114.915 92.460  110.981 1.00 14.07 ?  945  PRO A CG   1 
ATOM   6077  C CD   . PRO A 1 945  ? 115.172 93.936  110.825 1.00 17.33 ?  945  PRO A CD   1 
ATOM   6078  N N    . SER A 1 946  ? 119.503 91.952  111.343 1.00 13.64 ?  946  SER A N    1 
ATOM   6079  C CA   . SER A 1 946  ? 120.872 91.825  110.866 1.00 7.93  ?  946  SER A CA   1 
ATOM   6080  C C    . SER A 1 946  ? 121.108 90.555  110.059 1.00 8.90  ?  946  SER A C    1 
ATOM   6081  O O    . SER A 1 946  ? 122.260 90.252  109.732 1.00 8.63  ?  946  SER A O    1 
ATOM   6082  C CB   . SER A 1 946  ? 121.845 91.878  112.045 1.00 8.79  ?  946  SER A CB   1 
ATOM   6083  O OG   . SER A 1 946  ? 121.991 93.204  112.522 1.00 15.11 ?  946  SER A OG   1 
ATOM   6084  N N    . SER A 1 947  ? 120.055 89.804  109.738 1.00 9.81  ?  947  SER A N    1 
ATOM   6085  C CA   . SER A 1 947  ? 120.191 88.621  108.890 1.00 12.33 ?  947  SER A CA   1 
ATOM   6086  C C    . SER A 1 947  ? 118.851 88.391  108.198 1.00 16.45 ?  947  SER A C    1 
ATOM   6087  O O    . SER A 1 947  ? 117.929 87.832  108.798 1.00 19.85 ?  947  SER A O    1 
ATOM   6088  C CB   . SER A 1 947  ? 120.618 87.405  109.700 1.00 11.70 ?  947  SER A CB   1 
ATOM   6089  O OG   . SER A 1 947  ? 120.339 86.204  109.002 1.00 14.35 ?  947  SER A OG   1 
ATOM   6090  N N    . ILE A 1 948  ? 118.753 88.824  106.945 1.00 13.15 ?  948  ILE A N    1 
ATOM   6091  C CA   . ILE A 1 948  ? 117.562 88.603  106.129 1.00 13.28 ?  948  ILE A CA   1 
ATOM   6092  C C    . ILE A 1 948  ? 117.768 87.327  105.322 1.00 13.31 ?  948  ILE A C    1 
ATOM   6093  O O    . ILE A 1 948  ? 118.785 87.204  104.626 1.00 13.13 ?  948  ILE A O    1 
ATOM   6094  C CB   . ILE A 1 948  ? 117.280 89.804  105.214 1.00 13.29 ?  948  ILE A CB   1 
ATOM   6095  C CG1  . ILE A 1 948  ? 116.941 91.041  106.048 1.00 10.30 ?  948  ILE A CG1  1 
ATOM   6096  C CG2  . ILE A 1 948  ? 116.153 89.484  104.250 1.00 12.34 ?  948  ILE A CG2  1 
ATOM   6097  C CD1  . ILE A 1 948  ? 116.556 92.247  105.224 1.00 10.15 ?  948  ILE A CD1  1 
ATOM   6098  N N    . PRO A 1 949  ? 116.859 86.356  105.400 1.00 17.88 ?  949  PRO A N    1 
ATOM   6099  C CA   . PRO A 1 949  ? 117.040 85.086  104.674 1.00 16.37 ?  949  PRO A CA   1 
ATOM   6100  C C    . PRO A 1 949  ? 117.107 85.305  103.174 1.00 16.49 ?  949  PRO A C    1 
ATOM   6101  O O    . PRO A 1 949  ? 116.408 86.174  102.632 1.00 16.44 ?  949  PRO A O    1 
ATOM   6102  C CB   . PRO A 1 949  ? 115.793 84.277  105.061 1.00 17.34 ?  949  PRO A CB   1 
ATOM   6103  C CG   . PRO A 1 949  ? 115.318 84.892  106.336 1.00 19.37 ?  949  PRO A CG   1 
ATOM   6104  C CD   . PRO A 1 949  ? 115.645 86.349  106.233 1.00 19.36 ?  949  PRO A CD   1 
ATOM   6105  N N    . PRO A 1 950  ? 117.953 84.545  102.471 1.00 17.53 ?  950  PRO A N    1 
ATOM   6106  C CA   . PRO A 1 950  ? 118.047 84.709  101.021 1.00 16.21 ?  950  PRO A CA   1 
ATOM   6107  C C    . PRO A 1 950  ? 116.772 84.267  100.340 1.00 17.16 ?  950  PRO A C    1 
ATOM   6108  O O    . PRO A 1 950  ? 116.073 83.354  100.819 1.00 15.93 ?  950  PRO A O    1 
ATOM   6109  C CB   . PRO A 1 950  ? 119.235 83.804  100.640 1.00 14.79 ?  950  PRO A CB   1 
ATOM   6110  C CG   . PRO A 1 950  ? 119.339 82.823  101.751 1.00 14.13 ?  950  PRO A CG   1 
ATOM   6111  C CD   . PRO A 1 950  ? 118.907 83.549  102.986 1.00 15.37 ?  950  PRO A CD   1 
ATOM   6112  N N    . PRO A 1 951  ? 116.413 84.878  99.213  1.00 22.50 ?  951  PRO A N    1 
ATOM   6113  C CA   . PRO A 1 951  ? 115.145 84.557  98.557  1.00 21.59 ?  951  PRO A CA   1 
ATOM   6114  C C    . PRO A 1 951  ? 115.253 83.283  97.740  1.00 22.08 ?  951  PRO A C    1 
ATOM   6115  O O    . PRO A 1 951  ? 116.354 82.891  97.325  1.00 22.37 ?  951  PRO A O    1 
ATOM   6116  C CB   . PRO A 1 951  ? 114.889 85.778  97.654  1.00 20.79 ?  951  PRO A CB   1 
ATOM   6117  C CG   . PRO A 1 951  ? 116.030 86.743  97.910  1.00 20.71 ?  951  PRO A CG   1 
ATOM   6118  C CD   . PRO A 1 951  ? 117.137 85.950  98.512  1.00 21.02 ?  951  PRO A CD   1 
ATOM   6119  N N    . PRO A 1 952  ? 114.134 82.608  97.493  1.00 23.22 ?  952  PRO A N    1 
ATOM   6120  C CA   . PRO A 1 952  ? 114.138 81.454  96.586  1.00 23.37 ?  952  PRO A CA   1 
ATOM   6121  C C    . PRO A 1 952  ? 114.381 81.896  95.154  1.00 24.91 ?  952  PRO A C    1 
ATOM   6122  O O    . PRO A 1 952  ? 114.195 83.078  94.827  1.00 21.05 ?  952  PRO A O    1 
ATOM   6123  C CB   . PRO A 1 952  ? 112.729 80.861  96.759  1.00 22.93 ?  952  PRO A CB   1 
ATOM   6124  C CG   . PRO A 1 952  ? 112.210 81.443  98.037  1.00 23.65 ?  952  PRO A CG   1 
ATOM   6125  C CD   . PRO A 1 952  ? 112.824 82.799  98.134  1.00 23.04 ?  952  PRO A CD   1 
ATOM   6126  N N    . PRO A 1 953  ? 114.818 80.985  94.277  1.00 25.00 ?  953  PRO A N    1 
ATOM   6127  C CA   . PRO A 1 953  ? 115.086 81.373  92.879  1.00 23.25 ?  953  PRO A CA   1 
ATOM   6128  C C    . PRO A 1 953  ? 113.872 81.900  92.129  1.00 21.12 ?  953  PRO A C    1 
ATOM   6129  O O    . PRO A 1 953  ? 114.043 82.657  91.163  1.00 19.43 ?  953  PRO A O    1 
ATOM   6130  C CB   . PRO A 1 953  ? 115.606 80.074  92.249  1.00 20.62 ?  953  PRO A CB   1 
ATOM   6131  C CG   . PRO A 1 953  ? 116.136 79.283  93.395  1.00 21.85 ?  953  PRO A CG   1 
ATOM   6132  C CD   . PRO A 1 953  ? 115.242 79.601  94.554  1.00 19.46 ?  953  PRO A CD   1 
ATOM   6133  N N    . GLU A 1 954  ? 112.656 81.517  92.531  1.00 23.03 ?  954  GLU A N    1 
ATOM   6134  C CA   . GLU A 1 954  ? 111.458 82.054  91.892  1.00 25.65 ?  954  GLU A CA   1 
ATOM   6135  C C    . GLU A 1 954  ? 111.347 83.559  92.105  1.00 25.51 ?  954  GLU A C    1 
ATOM   6136  O O    . GLU A 1 954  ? 110.957 84.297  91.192  1.00 24.56 ?  954  GLU A O    1 
ATOM   6137  C CB   . GLU A 1 954  ? 110.216 81.342  92.426  1.00 23.78 ?  954  GLU A CB   1 
ATOM   6138  C CG   . GLU A 1 954  ? 110.395 79.846  92.634  1.00 23.62 ?  954  GLU A CG   1 
ATOM   6139  C CD   . GLU A 1 954  ? 109.884 79.029  91.464  1.00 27.31 ?  954  GLU A CD   1 
ATOM   6140  O OE1  . GLU A 1 954  ? 108.835 79.396  90.894  1.00 25.42 ?  954  GLU A OE1  1 
ATOM   6141  O OE2  . GLU A 1 954  ? 110.530 78.019  91.113  1.00 28.93 ?  954  GLU A OE2  1 
ATOM   6142  N N    . ASN A 1 955  ? 111.684 84.031  93.308  1.00 22.77 ?  955  ASN A N    1 
ATOM   6143  C CA   . ASN A 1 955  ? 111.669 85.465  93.574  1.00 20.51 ?  955  ASN A CA   1 
ATOM   6144  C C    . ASN A 1 955  ? 112.741 86.188  92.766  1.00 21.00 ?  955  ASN A C    1 
ATOM   6145  O O    . ASN A 1 955  ? 112.533 87.326  92.330  1.00 19.73 ?  955  ASN A O    1 
ATOM   6146  C CB   . ASN A 1 955  ? 111.857 85.722  95.069  1.00 19.59 ?  955  ASN A CB   1 
ATOM   6147  C CG   . ASN A 1 955  ? 111.170 86.991  95.535  1.00 22.34 ?  955  ASN A CG   1 
ATOM   6148  O OD1  . ASN A 1 955  ? 111.059 87.962  94.787  1.00 22.68 ?  955  ASN A OD1  1 
ATOM   6149  N ND2  . ASN A 1 955  ? 110.702 86.988  96.778  1.00 22.49 ?  955  ASN A ND2  1 
ATOM   6150  N N    . LEU A 1 956  ? 113.897 85.548  92.568  1.00 19.84 ?  956  LEU A N    1 
ATOM   6151  C CA   . LEU A 1 956  ? 114.938 86.141  91.734  1.00 17.33 ?  956  LEU A CA   1 
ATOM   6152  C C    . LEU A 1 956  ? 114.493 86.243  90.280  1.00 22.78 ?  956  LEU A C    1 
ATOM   6153  O O    . LEU A 1 956  ? 114.780 87.237  89.604  1.00 24.19 ?  956  LEU A O    1 
ATOM   6154  C CB   . LEU A 1 956  ? 116.229 85.330  91.846  1.00 14.41 ?  956  LEU A CB   1 
ATOM   6155  C CG   . LEU A 1 956  ? 117.067 85.555  93.106  1.00 15.20 ?  956  LEU A CG   1 
ATOM   6156  C CD1  . LEU A 1 956  ? 118.262 84.617  93.128  1.00 17.83 ?  956  LEU A CD1  1 
ATOM   6157  C CD2  . LEU A 1 956  ? 117.519 87.004  93.196  1.00 16.10 ?  956  LEU A CD2  1 
ATOM   6158  N N    . LEU A 1 957  ? 113.795 85.219  89.779  1.00 20.43 ?  957  LEU A N    1 
ATOM   6159  C CA   . LEU A 1 957  ? 113.288 85.278  88.411  1.00 18.10 ?  957  LEU A CA   1 
ATOM   6160  C C    . LEU A 1 957  ? 112.167 86.300  88.268  1.00 19.36 ?  957  LEU A C    1 
ATOM   6161  O O    . LEU A 1 957  ? 112.038 86.932  87.215  1.00 21.62 ?  957  LEU A O    1 
ATOM   6162  C CB   . LEU A 1 957  ? 112.810 83.894  87.965  1.00 20.15 ?  957  LEU A CB   1 
ATOM   6163  C CG   . LEU A 1 957  ? 112.875 83.552  86.471  1.00 21.49 ?  957  LEU A CG   1 
ATOM   6164  C CD1  . LEU A 1 957  ? 112.974 82.054  86.279  1.00 21.95 ?  957  LEU A CD1  1 
ATOM   6165  C CD2  . LEU A 1 957  ? 111.664 84.080  85.719  1.00 17.58 ?  957  LEU A CD2  1 
ATOM   6166  N N    . LYS A 1 958  ? 111.347 86.477  89.303  1.00 16.45 ?  958  LYS A N    1 
ATOM   6167  C CA   . LYS A 1 958  ? 110.225 87.401  89.209  1.00 18.74 ?  958  LYS A CA   1 
ATOM   6168  C C    . LYS A 1 958  ? 110.625 88.858  89.411  1.00 19.95 ?  958  LYS A C    1 
ATOM   6169  O O    . LYS A 1 958  ? 109.821 89.748  89.111  1.00 23.60 ?  958  LYS A O    1 
ATOM   6170  C CB   . LYS A 1 958  ? 109.142 87.011  90.222  1.00 18.31 ?  958  LYS A CB   1 
ATOM   6171  C CG   . LYS A 1 958  ? 109.228 87.730  91.559  1.00 18.68 ?  958  LYS A CG   1 
ATOM   6172  C CD   . LYS A 1 958  ? 107.858 87.843  92.208  1.00 21.75 ?  958  LYS A CD   1 
ATOM   6173  C CE   . LYS A 1 958  ? 107.806 88.991  93.202  1.00 19.59 ?  958  LYS A CE   1 
ATOM   6174  N NZ   . LYS A 1 958  ? 106.424 89.224  93.705  1.00 18.37 ?  958  LYS A NZ   1 
ATOM   6175  N N    . ASN A 1 959  ? 111.841 89.128  89.887  1.00 15.20 ?  959  ASN A N    1 
ATOM   6176  C CA   . ASN A 1 959  ? 112.269 90.481  90.217  1.00 17.85 ?  959  ASN A CA   1 
ATOM   6177  C C    . ASN A 1 959  ? 113.255 91.056  89.205  1.00 19.25 ?  959  ASN A C    1 
ATOM   6178  O O    . ASN A 1 959  ? 113.932 92.045  89.507  1.00 19.10 ?  959  ASN A O    1 
ATOM   6179  C CB   . ASN A 1 959  ? 112.875 90.513  91.620  1.00 17.43 ?  959  ASN A CB   1 
ATOM   6180  C CG   . ASN A 1 959  ? 112.193 91.519  92.526  1.00 20.61 ?  959  ASN A CG   1 
ATOM   6181  O OD1  . ASN A 1 959  ? 111.528 92.443  92.058  1.00 15.28 ?  959  ASN A OD1  1 
ATOM   6182  N ND2  . ASN A 1 959  ? 112.354 91.343  93.832  1.00 20.69 ?  959  ASN A ND2  1 
ATOM   6183  N N    . VAL A 1 960  ? 113.360 90.456  88.017  1.00 17.41 ?  960  VAL A N    1 
ATOM   6184  C CA   . VAL A 1 960  ? 114.214 91.011  86.973  1.00 12.55 ?  960  VAL A CA   1 
ATOM   6185  C C    . VAL A 1 960  ? 113.622 92.331  86.486  1.00 17.46 ?  960  VAL A C    1 
ATOM   6186  O O    . VAL A 1 960  ? 112.401 92.537  86.507  1.00 21.25 ?  960  VAL A O    1 
ATOM   6187  C CB   . VAL A 1 960  ? 114.384 90.001  85.821  1.00 13.00 ?  960  VAL A CB   1 
ATOM   6188  C CG1  . VAL A 1 960  ? 115.515 90.412  84.890  1.00 14.90 ?  960  VAL A CG1  1 
ATOM   6189  C CG2  . VAL A 1 960  ? 114.657 88.619  86.377  1.00 16.93 ?  960  VAL A CG2  1 
ATOM   6190  N N    . SER A 1 961  ? 114.502 93.244  86.059  1.00 20.87 ?  961  SER A N    1 
ATOM   6191  C CA   . SER A 1 961  ? 114.078 94.597  85.708  1.00 20.78 ?  961  SER A CA   1 
ATOM   6192  C C    . SER A 1 961  ? 113.142 94.606  84.505  1.00 19.21 ?  961  SER A C    1 
ATOM   6193  O O    . SER A 1 961  ? 112.196 95.401  84.454  1.00 24.29 ?  961  SER A O    1 
ATOM   6194  C CB   . SER A 1 961  ? 115.302 95.473  85.438  1.00 20.10 ?  961  SER A CB   1 
ATOM   6195  O OG   . SER A 1 961  ? 116.336 94.727  84.822  1.00 21.00 ?  961  SER A OG   1 
ATOM   6196  N N    . TRP A 1 962  ? 113.386 93.739  83.526  1.00 11.55 ?  962  TRP A N    1 
ATOM   6197  C CA   . TRP A 1 962  ? 112.549 93.678  82.336  1.00 14.81 ?  962  TRP A CA   1 
ATOM   6198  C C    . TRP A 1 962  ? 111.440 92.637  82.440  1.00 19.17 ?  962  TRP A C    1 
ATOM   6199  O O    . TRP A 1 962  ? 110.742 92.394  81.451  1.00 21.49 ?  962  TRP A O    1 
ATOM   6200  C CB   . TRP A 1 962  ? 113.402 93.413  81.091  1.00 16.42 ?  962  TRP A CB   1 
ATOM   6201  C CG   . TRP A 1 962  ? 114.444 92.350  81.251  1.00 20.25 ?  962  TRP A CG   1 
ATOM   6202  C CD1  . TRP A 1 962  ? 115.707 92.507  81.742  1.00 20.56 ?  962  TRP A CD1  1 
ATOM   6203  C CD2  . TRP A 1 962  ? 114.319 90.967  80.899  1.00 18.01 ?  962  TRP A CD2  1 
ATOM   6204  N NE1  . TRP A 1 962  ? 116.374 91.306  81.724  1.00 15.48 ?  962  TRP A NE1  1 
ATOM   6205  C CE2  . TRP A 1 962  ? 115.543 90.345  81.212  1.00 17.70 ?  962  TRP A CE2  1 
ATOM   6206  C CE3  . TRP A 1 962  ? 113.289 90.194  80.356  1.00 16.28 ?  962  TRP A CE3  1 
ATOM   6207  C CZ2  . TRP A 1 962  ? 115.765 88.987  80.998  1.00 20.83 ?  962  TRP A CZ2  1 
ATOM   6208  C CZ3  . TRP A 1 962  ? 113.512 88.847  80.143  1.00 18.60 ?  962  TRP A CZ3  1 
ATOM   6209  C CH2  . TRP A 1 962  ? 114.740 88.257  80.464  1.00 18.80 ?  962  TRP A CH2  1 
ATOM   6210  N N    . LEU A 1 963  ? 111.261 92.018  83.609  1.00 17.22 ?  963  LEU A N    1 
ATOM   6211  C CA   . LEU A 1 963  ? 110.169 91.082  83.832  1.00 16.85 ?  963  LEU A CA   1 
ATOM   6212  C C    . LEU A 1 963  ? 109.211 91.499  84.936  1.00 22.27 ?  963  LEU A C    1 
ATOM   6213  O O    . LEU A 1 963  ? 108.098 90.966  84.991  1.00 26.66 ?  963  LEU A O    1 
ATOM   6214  C CB   . LEU A 1 963  ? 110.713 89.683  84.166  1.00 18.64 ?  963  LEU A CB   1 
ATOM   6215  C CG   . LEU A 1 963  ? 111.282 88.859  83.010  1.00 21.02 ?  963  LEU A CG   1 
ATOM   6216  C CD1  . LEU A 1 963  ? 111.753 87.497  83.497  1.00 18.61 ?  963  LEU A CD1  1 
ATOM   6217  C CD2  . LEU A 1 963  ? 110.253 88.707  81.903  1.00 21.61 ?  963  LEU A CD2  1 
ATOM   6218  N N    . ALA A 1 964  ? 109.602 92.424  85.809  1.00 21.01 ?  964  ALA A N    1 
ATOM   6219  C CA   . ALA A 1 964  ? 108.749 92.818  86.920  1.00 21.15 ?  964  ALA A CA   1 
ATOM   6220  C C    . ALA A 1 964  ? 107.580 93.668  86.437  1.00 21.53 ?  964  ALA A C    1 
ATOM   6221  O O    . ALA A 1 964  ? 107.700 94.462  85.500  1.00 17.03 ?  964  ALA A O    1 
ATOM   6222  C CB   . ALA A 1 964  ? 109.556 93.586  87.966  1.00 19.17 ?  964  ALA A CB   1 
ATOM   6223  N N    . GLY A 1 965  ? 106.434 93.491  87.094  1.00 24.37 ?  965  GLY A N    1 
ATOM   6224  C CA   . GLY A 1 965  ? 105.239 94.251  86.814  1.00 25.89 ?  965  GLY A CA   1 
ATOM   6225  C C    . GLY A 1 965  ? 104.269 93.585  85.860  1.00 26.82 ?  965  GLY A C    1 
ATOM   6226  O O    . GLY A 1 965  ? 103.099 93.981  85.814  1.00 29.21 ?  965  GLY A O    1 
ATOM   6227  N N    . ASP A 1 966  ? 104.719 92.588  85.103  1.00 22.54 ?  966  ASP A N    1 
ATOM   6228  C CA   . ASP A 1 966  ? 103.879 91.873  84.147  1.00 24.44 ?  966  ASP A CA   1 
ATOM   6229  C C    . ASP A 1 966  ? 103.657 90.459  84.671  1.00 25.45 ?  966  ASP A C    1 
ATOM   6230  O O    . ASP A 1 966  ? 104.571 89.629  84.637  1.00 23.07 ?  966  ASP A O    1 
ATOM   6231  C CB   . ASP A 1 966  ? 104.523 91.851  82.762  1.00 23.88 ?  966  ASP A CB   1 
ATOM   6232  C CG   . ASP A 1 966  ? 104.623 93.231  82.140  1.00 27.40 ?  966  ASP A CG   1 
ATOM   6233  O OD1  . ASP A 1 966  ? 104.371 94.228  82.847  1.00 26.77 ?  966  ASP A OD1  1 
ATOM   6234  O OD2  . ASP A 1 966  ? 104.957 93.317  80.940  1.00 28.92 ?  966  ASP A OD2  1 
ATOM   6235  N N    . MET A 1 967  ? 102.441 90.190  85.154  1.00 23.25 ?  967  MET A N    1 
ATOM   6236  C CA   . MET A 1 967  ? 102.137 88.875  85.710  1.00 21.77 ?  967  MET A CA   1 
ATOM   6237  C C    . MET A 1 967  ? 102.060 87.811  84.621  1.00 20.57 ?  967  MET A C    1 
ATOM   6238  O O    . MET A 1 967  ? 102.533 86.684  84.814  1.00 21.73 ?  967  MET A O    1 
ATOM   6239  C CB   . MET A 1 967  ? 100.830 88.931  86.500  1.00 19.31 ?  967  MET A CB   1 
ATOM   6240  C CG   . MET A 1 967  ? 100.919 89.738  87.785  1.00 18.24 ?  967  MET A CG   1 
ATOM   6241  S SD   . MET A 1 967  ? 101.509 91.420  87.516  1.00 27.53 ?  967  MET A SD   1 
ATOM   6242  C CE   . MET A 1 967  ? 100.088 92.156  86.711  1.00 20.76 ?  967  MET A CE   1 
ATOM   6243  N N    . LYS A 1 968  ? 101.457 88.148  83.477  1.00 20.76 ?  968  LYS A N    1 
ATOM   6244  C CA   . LYS A 1 968  ? 101.364 87.192  82.376  1.00 26.10 ?  968  LYS A CA   1 
ATOM   6245  C C    . LYS A 1 968  ? 102.743 86.840  81.834  1.00 26.34 ?  968  LYS A C    1 
ATOM   6246  O O    . LYS A 1 968  ? 103.035 85.667  81.571  1.00 23.02 ?  968  LYS A O    1 
ATOM   6247  C CB   . LYS A 1 968  ? 100.481 87.757  81.263  1.00 23.57 ?  968  LYS A CB   1 
ATOM   6248  C CG   . LYS A 1 968  ? 98.988  87.668  81.539  1.00 22.03 ?  968  LYS A CG   1 
ATOM   6249  C CD   . LYS A 1 968  ? 98.453  88.975  82.102  1.00 21.38 ?  968  LYS A CD   1 
ATOM   6250  C CE   . LYS A 1 968  ? 98.592  90.107  81.096  1.00 23.08 ?  968  LYS A CE   1 
ATOM   6251  N NZ   . LYS A 1 968  ? 97.932  91.356  81.567  1.00 25.04 ?  968  LYS A NZ   1 
ATOM   6252  N N    . LEU A 1 969  ? 103.607 87.845  81.669  1.00 25.81 ?  969  LEU A N    1 
ATOM   6253  C CA   . LEU A 1 969  ? 104.971 87.592  81.215  1.00 26.39 ?  969  LEU A CA   1 
ATOM   6254  C C    . LEU A 1 969  ? 105.757 86.789  82.242  1.00 22.22 ?  969  LEU A C    1 
ATOM   6255  O O    . LEU A 1 969  ? 106.555 85.918  81.875  1.00 20.82 ?  969  LEU A O    1 
ATOM   6256  C CB   . LEU A 1 969  ? 105.676 88.913  80.914  1.00 23.76 ?  969  LEU A CB   1 
ATOM   6257  C CG   . LEU A 1 969  ? 106.959 88.855  80.081  1.00 21.30 ?  969  LEU A CG   1 
ATOM   6258  C CD1  . LEU A 1 969  ? 106.870 87.796  78.991  1.00 19.36 ?  969  LEU A CD1  1 
ATOM   6259  C CD2  . LEU A 1 969  ? 107.259 90.220  79.488  1.00 21.23 ?  969  LEU A CD2  1 
ATOM   6260  N N    . ILE A 1 970  ? 105.550 87.073  83.531  1.00 18.89 ?  970  ILE A N    1 
ATOM   6261  C CA   . ILE A 1 970  ? 106.231 86.322  84.584  1.00 20.26 ?  970  ILE A CA   1 
ATOM   6262  C C    . ILE A 1 970  ? 105.818 84.857  84.541  1.00 21.72 ?  970  ILE A C    1 
ATOM   6263  O O    . ILE A 1 970  ? 106.662 83.957  84.629  1.00 18.80 ?  970  ILE A O    1 
ATOM   6264  C CB   . ILE A 1 970  ? 105.955 86.963  85.959  1.00 20.96 ?  970  ILE A CB   1 
ATOM   6265  C CG1  . ILE A 1 970  ? 107.016 88.019  86.274  1.00 18.57 ?  970  ILE A CG1  1 
ATOM   6266  C CG2  . ILE A 1 970  ? 105.924 85.919  87.072  1.00 21.21 ?  970  ILE A CG2  1 
ATOM   6267  C CD1  . ILE A 1 970  ? 106.776 88.753  87.574  1.00 20.39 ?  970  ILE A CD1  1 
ATOM   6268  N N    . ASP A 1 971  ? 104.517 84.594  84.379  1.00 27.36 ?  971  ASP A N    1 
ATOM   6269  C CA   . ASP A 1 971  ? 104.041 83.216  84.288  1.00 29.24 ?  971  ASP A CA   1 
ATOM   6270  C C    . ASP A 1 971  ? 104.576 82.525  83.038  1.00 28.49 ?  971  ASP A C    1 
ATOM   6271  O O    . ASP A 1 971  ? 104.972 81.353  83.089  1.00 23.00 ?  971  ASP A O    1 
ATOM   6272  C CB   . ASP A 1 971  ? 102.513 83.189  84.305  1.00 25.29 ?  971  ASP A CB   1 
ATOM   6273  C CG   . ASP A 1 971  ? 101.953 82.781  85.654  1.00 25.62 ?  971  ASP A CG   1 
ATOM   6274  O OD1  . ASP A 1 971  ? 102.640 82.038  86.386  1.00 26.29 ?  971  ASP A OD1  1 
ATOM   6275  O OD2  . ASP A 1 971  ? 100.825 83.205  85.983  1.00 27.28 ?  971  ASP A OD2  1 
ATOM   6276  N N    . PHE A 1 972  ? 104.601 83.240  81.908  1.00 25.87 ?  972  PHE A N    1 
ATOM   6277  C CA   . PHE A 1 972  ? 105.098 82.664  80.661  1.00 27.38 ?  972  PHE A CA   1 
ATOM   6278  C C    . PHE A 1 972  ? 106.575 82.299  80.764  1.00 29.19 ?  972  PHE A C    1 
ATOM   6279  O O    . PHE A 1 972  ? 106.990 81.230  80.302  1.00 24.61 ?  972  PHE A O    1 
ATOM   6280  C CB   . PHE A 1 972  ? 104.866 83.644  79.509  1.00 26.39 ?  972  PHE A CB   1 
ATOM   6281  C CG   . PHE A 1 972  ? 105.071 83.047  78.143  1.00 25.31 ?  972  PHE A CG   1 
ATOM   6282  C CD1  . PHE A 1 972  ? 104.025 82.424  77.482  1.00 23.64 ?  972  PHE A CD1  1 
ATOM   6283  C CD2  . PHE A 1 972  ? 106.305 83.121  77.514  1.00 25.65 ?  972  PHE A CD2  1 
ATOM   6284  C CE1  . PHE A 1 972  ? 104.206 81.880  76.222  1.00 24.94 ?  972  PHE A CE1  1 
ATOM   6285  C CE2  . PHE A 1 972  ? 106.493 82.577  76.257  1.00 26.12 ?  972  PHE A CE2  1 
ATOM   6286  C CZ   . PHE A 1 972  ? 105.442 81.956  75.611  1.00 25.82 ?  972  PHE A CZ   1 
ATOM   6287  N N    . ILE A 1 973  ? 107.384 83.178  81.358  1.00 25.80 ?  973  ILE A N    1 
ATOM   6288  C CA   . ILE A 1 973  ? 108.813 82.904  81.481  1.00 23.86 ?  973  ILE A CA   1 
ATOM   6289  C C    . ILE A 1 973  ? 109.064 81.801  82.504  1.00 25.18 ?  973  ILE A C    1 
ATOM   6290  O O    . ILE A 1 973  ? 109.887 80.904  82.278  1.00 26.01 ?  973  ILE A O    1 
ATOM   6291  C CB   . ILE A 1 973  ? 109.577 84.196  81.825  1.00 22.48 ?  973  ILE A CB   1 
ATOM   6292  C CG1  . ILE A 1 973  ? 109.477 85.198  80.674  1.00 20.44 ?  973  ILE A CG1  1 
ATOM   6293  C CG2  . ILE A 1 973  ? 111.040 83.899  82.098  1.00 23.12 ?  973  ILE A CG2  1 
ATOM   6294  C CD1  . ILE A 1 973  ? 109.828 84.621  79.318  1.00 22.22 ?  973  ILE A CD1  1 
ATOM   6295  N N    . LYS A 1 974  ? 108.355 81.837  83.639  1.00 20.20 ?  974  LYS A N    1 
ATOM   6296  C CA   . LYS A 1 974  ? 108.551 80.837  84.683  1.00 20.44 ?  974  LYS A CA   1 
ATOM   6297  C C    . LYS A 1 974  ? 108.122 79.448  84.227  1.00 21.36 ?  974  LYS A C    1 
ATOM   6298  O O    . LYS A 1 974  ? 108.716 78.449  84.650  1.00 18.44 ?  974  LYS A O    1 
ATOM   6299  C CB   . LYS A 1 974  ? 107.786 81.247  85.942  1.00 21.46 ?  974  LYS A CB   1 
ATOM   6300  C CG   . LYS A 1 974  ? 108.062 80.386  87.165  1.00 22.43 ?  974  LYS A CG   1 
ATOM   6301  C CD   . LYS A 1 974  ? 107.212 80.818  88.352  1.00 18.90 ?  974  LYS A CD   1 
ATOM   6302  C CE   . LYS A 1 974  ? 107.417 82.288  88.683  1.00 19.09 ?  974  LYS A CE   1 
ATOM   6303  N NZ   . LYS A 1 974  ? 108.844 82.598  88.978  1.00 17.15 ?  974  LYS A NZ   1 
ATOM   6304  N N    . ALA A 1 975  ? 107.100 79.361  83.372  1.00 24.28 ?  975  ALA A N    1 
ATOM   6305  C CA   . ALA A 1 975  ? 106.677 78.060  82.865  1.00 25.42 ?  975  ALA A CA   1 
ATOM   6306  C C    . ALA A 1 975  ? 107.726 77.438  81.950  1.00 24.80 ?  975  ALA A C    1 
ATOM   6307  O O    . ALA A 1 975  ? 107.890 76.213  81.944  1.00 24.01 ?  975  ALA A O    1 
ATOM   6308  C CB   . ALA A 1 975  ? 105.343 78.190  82.132  1.00 25.80 ?  975  ALA A CB   1 
ATOM   6309  N N    . ARG A 1 976  ? 108.442 78.254  81.178  1.00 25.12 ?  976  ARG A N    1 
ATOM   6310  C CA   . ARG A 1 976  ? 109.379 77.764  80.176  1.00 25.70 ?  976  ARG A CA   1 
ATOM   6311  C C    . ARG A 1 976  ? 110.837 77.866  80.611  1.00 27.90 ?  976  ARG A C    1 
ATOM   6312  O O    . ARG A 1 976  ? 111.732 77.673  79.782  1.00 27.10 ?  976  ARG A O    1 
ATOM   6313  C CB   . ARG A 1 976  ? 109.176 78.516  78.861  1.00 28.91 ?  976  ARG A CB   1 
ATOM   6314  C CG   . ARG A 1 976  ? 108.027 77.987  78.021  1.00 28.56 ?  976  ARG A CG   1 
ATOM   6315  C CD   . ARG A 1 976  ? 107.269 79.119  77.350  1.00 26.72 ?  976  ARG A CD   1 
ATOM   6316  N NE   . ARG A 1 976  ? 105.887 78.750  77.067  1.00 29.40 ?  976  ARG A NE   1 
ATOM   6317  C CZ   . ARG A 1 976  ? 104.867 78.993  77.879  1.00 29.73 ?  976  ARG A CZ   1 
ATOM   6318  N NH1  . ARG A 1 976  ? 105.037 79.611  79.036  1.00 26.53 ?  976  ARG A NH1  1 
ATOM   6319  N NH2  . ARG A 1 976  ? 103.646 78.609  77.519  1.00 29.08 ?  976  ARG A NH2  1 
ATOM   6320  N N    . ALA A 1 977  ? 111.100 78.163  81.880  1.00 28.15 ?  977  ALA A N    1 
ATOM   6321  C CA   . ALA A 1 977  ? 112.465 78.265  82.375  1.00 24.74 ?  977  ALA A CA   1 
ATOM   6322  C C    . ALA A 1 977  ? 112.914 76.944  82.986  1.00 24.18 ?  977  ALA A C    1 
ATOM   6323  O O    . ALA A 1 977  ? 112.105 76.170  83.504  1.00 22.92 ?  977  ALA A O    1 
ATOM   6324  C CB   . ALA A 1 977  ? 112.586 79.383  83.411  1.00 20.30 ?  977  ALA A CB   1 
ATOM   6325  N N    . SER A 1 978  ? 114.220 76.692  82.922  1.00 21.37 ?  978  SER A N    1 
ATOM   6326  C CA   . SER A 1 978  ? 114.800 75.478  83.475  1.00 22.03 ?  978  SER A CA   1 
ATOM   6327  C C    . SER A 1 978  ? 115.939 75.839  84.420  1.00 23.55 ?  978  SER A C    1 
ATOM   6328  O O    . SER A 1 978  ? 116.533 76.913  84.324  1.00 26.86 ?  978  SER A O    1 
ATOM   6329  C CB   . SER A 1 978  ? 115.307 74.541  82.370  1.00 23.66 ?  978  SER A CB   1 
ATOM   6330  O OG   . SER A 1 978  ? 116.636 74.862  82.001  1.00 24.03 ?  978  SER A OG   1 
ATOM   6331  N N    . LEU A 1 979  ? 116.235 74.930  85.343  1.00 21.06 ?  979  LEU A N    1 
ATOM   6332  C CA   . LEU A 1 979  ? 117.315 75.106  86.306  1.00 19.05 ?  979  LEU A CA   1 
ATOM   6333  C C    . LEU A 1 979  ? 118.495 74.228  85.918  1.00 23.46 ?  979  LEU A C    1 
ATOM   6334  O O    . LEU A 1 979  ? 118.331 73.025  85.691  1.00 28.15 ?  979  LEU A O    1 
ATOM   6335  C CB   . LEU A 1 979  ? 116.852 74.766  87.724  1.00 22.66 ?  979  LEU A CB   1 
ATOM   6336  C CG   . LEU A 1 979  ? 117.407 75.644  88.848  1.00 25.20 ?  979  LEU A CG   1 
ATOM   6337  C CD1  . LEU A 1 979  ? 116.971 77.087  88.682  1.00 23.92 ?  979  LEU A CD1  1 
ATOM   6338  C CD2  . LEU A 1 979  ? 116.985 75.104  90.205  1.00 21.82 ?  979  LEU A CD2  1 
ATOM   6339  N N    . LEU A 1 980  ? 119.680 74.829  85.847  1.00 21.66 ?  980  LEU A N    1 
ATOM   6340  C CA   . LEU A 1 980  ? 120.906 74.117  85.518  1.00 21.88 ?  980  LEU A CA   1 
ATOM   6341  C C    . LEU A 1 980  ? 121.908 74.268  86.652  1.00 21.35 ?  980  LEU A C    1 
ATOM   6342  O O    . LEU A 1 980  ? 122.055 75.352  87.226  1.00 22.22 ?  980  LEU A O    1 
ATOM   6343  C CB   . LEU A 1 980  ? 121.520 74.632  84.210  1.00 22.36 ?  980  LEU A CB   1 
ATOM   6344  C CG   . LEU A 1 980  ? 121.224 73.886  82.906  1.00 20.86 ?  980  LEU A CG   1 
ATOM   6345  C CD1  . LEU A 1 980  ? 121.881 72.515  82.917  1.00 20.15 ?  980  LEU A CD1  1 
ATOM   6346  C CD2  . LEU A 1 980  ? 119.729 73.767  82.647  1.00 19.15 ?  980  LEU A CD2  1 
ATOM   6347  N N    . HIS A 1 981  ? 122.594 73.174  86.972  1.00 24.11 ?  981  HIS A N    1 
ATOM   6348  C CA   . HIS A 1 981  ? 123.619 73.150  88.006  1.00 26.53 ?  981  HIS A CA   1 
ATOM   6349  C C    . HIS A 1 981  ? 124.954 72.804  87.364  1.00 27.16 ?  981  HIS A C    1 
ATOM   6350  O O    . HIS A 1 981  ? 125.044 71.842  86.595  1.00 25.65 ?  981  HIS A O    1 
ATOM   6351  C CB   . HIS A 1 981  ? 123.271 72.136  89.100  1.00 22.89 ?  981  HIS A CB   1 
ATOM   6352  C CG   . HIS A 1 981  ? 124.073 72.295  90.355  1.00 26.27 ?  981  HIS A CG   1 
ATOM   6353  N ND1  . HIS A 1 981  ? 125.433 72.076  90.404  1.00 25.17 ?  981  HIS A ND1  1 
ATOM   6354  C CD2  . HIS A 1 981  ? 123.703 72.641  91.611  1.00 27.03 ?  981  HIS A CD2  1 
ATOM   6355  C CE1  . HIS A 1 981  ? 125.868 72.286  91.634  1.00 26.42 ?  981  HIS A CE1  1 
ATOM   6356  N NE2  . HIS A 1 981  ? 124.838 72.630  92.386  1.00 27.22 ?  981  HIS A NE2  1 
ATOM   6357  N N    . PHE A 1 982  ? 125.985 73.585  87.677  1.00 23.22 ?  982  PHE A N    1 
ATOM   6358  C CA   . PHE A 1 982  ? 127.319 73.362  87.146  1.00 21.91 ?  982  PHE A CA   1 
ATOM   6359  C C    . PHE A 1 982  ? 128.324 73.340  88.288  1.00 23.28 ?  982  PHE A C    1 
ATOM   6360  O O    . PHE A 1 982  ? 128.145 74.010  89.309  1.00 25.43 ?  982  PHE A O    1 
ATOM   6361  C CB   . PHE A 1 982  ? 127.713 74.443  86.130  1.00 18.80 ?  982  PHE A CB   1 
ATOM   6362  C CG   . PHE A 1 982  ? 126.993 74.337  84.817  1.00 22.71 ?  982  PHE A CG   1 
ATOM   6363  C CD1  . PHE A 1 982  ? 125.731 74.885  84.656  1.00 21.08 ?  982  PHE A CD1  1 
ATOM   6364  C CD2  . PHE A 1 982  ? 127.580 73.691  83.742  1.00 25.98 ?  982  PHE A CD2  1 
ATOM   6365  C CE1  . PHE A 1 982  ? 125.069 74.791  83.446  1.00 22.35 ?  982  PHE A CE1  1 
ATOM   6366  C CE2  . PHE A 1 982  ? 126.923 73.592  82.531  1.00 22.42 ?  982  PHE A CE2  1 
ATOM   6367  C CZ   . PHE A 1 982  ? 125.665 74.143  82.383  1.00 21.61 ?  982  PHE A CZ   1 
ATOM   6368  N N    . ASP A 1 983  ? 129.388 72.568  88.100  1.00 21.36 ?  983  ASP A N    1 
ATOM   6369  C CA   . ASP A 1 983  ? 130.427 72.401  89.099  1.00 21.19 ?  983  ASP A CA   1 
ATOM   6370  C C    . ASP A 1 983  ? 131.621 73.293  88.763  1.00 22.97 ?  983  ASP A C    1 
ATOM   6371  O O    . ASP A 1 983  ? 131.583 74.101  87.831  1.00 27.93 ?  983  ASP A O    1 
ATOM   6372  C CB   . ASP A 1 983  ? 130.824 70.926  89.196  1.00 24.01 ?  983  ASP A CB   1 
ATOM   6373  C CG   . ASP A 1 983  ? 129.643 69.991  89.021  1.00 25.21 ?  983  ASP A CG   1 
ATOM   6374  O OD1  . ASP A 1 983  ? 128.623 70.181  89.717  1.00 24.97 ?  983  ASP A OD1  1 
ATOM   6375  O OD2  . ASP A 1 983  ? 129.733 69.066  88.187  1.00 25.19 ?  983  ASP A OD2  1 
ATOM   6376  N N    . TYR A 1 984  ? 132.695 73.152  89.537  1.00 24.00 ?  984  TYR A N    1 
ATOM   6377  C CA   . TYR A 1 984  ? 133.893 73.954  89.330  1.00 25.58 ?  984  TYR A CA   1 
ATOM   6378  C C    . TYR A 1 984  ? 134.605 73.526  88.052  1.00 26.05 ?  984  TYR A C    1 
ATOM   6379  O O    . TYR A 1 984  ? 134.811 72.332  87.813  1.00 25.47 ?  984  TYR A O    1 
ATOM   6380  C CB   . TYR A 1 984  ? 134.826 73.812  90.535  1.00 25.37 ?  984  TYR A CB   1 
ATOM   6381  C CG   . TYR A 1 984  ? 136.030 74.735  90.541  1.00 24.84 ?  984  TYR A CG   1 
ATOM   6382  C CD1  . TYR A 1 984  ? 136.015 75.947  89.861  1.00 22.93 ?  984  TYR A CD1  1 
ATOM   6383  C CD2  . TYR A 1 984  ? 137.186 74.389  91.230  1.00 24.61 ?  984  TYR A CD2  1 
ATOM   6384  C CE1  . TYR A 1 984  ? 137.115 76.785  89.867  1.00 25.31 ?  984  TYR A CE1  1 
ATOM   6385  C CE2  . TYR A 1 984  ? 138.290 75.221  91.243  1.00 24.37 ?  984  TYR A CE2  1 
ATOM   6386  C CZ   . TYR A 1 984  ? 138.248 76.418  90.560  1.00 24.84 ?  984  TYR A CZ   1 
ATOM   6387  O OH   . TYR A 1 984  ? 139.343 77.251  90.569  1.00 22.66 ?  984  TYR A OH   1 
ATOM   6388  N N    . GLY A 1 985  ? 134.981 74.505  87.230  1.00 23.87 ?  985  GLY A N    1 
ATOM   6389  C CA   . GLY A 1 985  ? 135.789 74.269  86.053  1.00 23.47 ?  985  GLY A CA   1 
ATOM   6390  C C    . GLY A 1 985  ? 135.018 74.097  84.762  1.00 24.84 ?  985  GLY A C    1 
ATOM   6391  O O    . GLY A 1 985  ? 135.634 74.125  83.688  1.00 25.08 ?  985  GLY A O    1 
ATOM   6392  N N    . GLU A 1 986  ? 133.702 73.920  84.828  1.00 24.93 ?  986  GLU A N    1 
ATOM   6393  C CA   . GLU A 1 986  ? 132.913 73.737  83.619  1.00 24.76 ?  986  GLU A CA   1 
ATOM   6394  C C    . GLU A 1 986  ? 132.826 75.036  82.826  1.00 23.46 ?  986  GLU A C    1 
ATOM   6395  O O    . GLU A 1 986  ? 132.897 76.137  83.377  1.00 22.95 ?  986  GLU A O    1 
ATOM   6396  C CB   . GLU A 1 986  ? 131.510 73.240  83.966  1.00 27.36 ?  986  GLU A CB   1 
ATOM   6397  C CG   . GLU A 1 986  ? 131.478 72.187  85.062  1.00 27.86 ?  986  GLU A CG   1 
ATOM   6398  C CD   . GLU A 1 986  ? 130.486 71.077  84.774  1.00 29.01 ?  986  GLU A CD   1 
ATOM   6399  O OE1  . GLU A 1 986  ? 129.751 71.179  83.769  1.00 27.65 ?  986  GLU A OE1  1 
ATOM   6400  O OE2  . GLU A 1 986  ? 130.443 70.100  85.551  1.00 26.94 ?  986  GLU A OE2  1 
ATOM   6401  N N    . VAL A 1 987  ? 132.683 74.896  81.511  1.00 22.73 ?  987  VAL A N    1 
ATOM   6402  C CA   . VAL A 1 987  ? 132.510 76.023  80.603  1.00 22.08 ?  987  VAL A CA   1 
ATOM   6403  C C    . VAL A 1 987  ? 131.079 75.976  80.087  1.00 23.21 ?  987  VAL A C    1 
ATOM   6404  O O    . VAL A 1 987  ? 130.632 74.944  79.571  1.00 21.17 ?  987  VAL A O    1 
ATOM   6405  C CB   . VAL A 1 987  ? 133.531 75.986  79.451  1.00 18.99 ?  987  VAL A CB   1 
ATOM   6406  C CG1  . VAL A 1 987  ? 132.980 76.667  78.201  1.00 19.94 ?  987  VAL A CG1  1 
ATOM   6407  C CG2  . VAL A 1 987  ? 134.841 76.626  79.883  1.00 16.96 ?  987  VAL A CG2  1 
ATOM   6408  N N    . ILE A 1 988  ? 130.356 77.079  80.250  1.00 20.00 ?  988  ILE A N    1 
ATOM   6409  C CA   . ILE A 1 988  ? 128.935 77.108  79.920  1.00 19.36 ?  988  ILE A CA   1 
ATOM   6410  C C    . ILE A 1 988  ? 128.711 77.430  78.449  1.00 24.35 ?  988  ILE A C    1 
ATOM   6411  O O    . ILE A 1 988  ? 127.917 76.771  77.773  1.00 23.59 ?  988  ILE A O    1 
ATOM   6412  C CB   . ILE A 1 988  ? 128.205 78.111  80.837  1.00 19.13 ?  988  ILE A CB   1 
ATOM   6413  C CG1  . ILE A 1 988  ? 128.666 77.933  82.284  1.00 18.90 ?  988  ILE A CG1  1 
ATOM   6414  C CG2  . ILE A 1 988  ? 126.709 77.894  80.757  1.00 20.02 ?  988  ILE A CG2  1 
ATOM   6415  C CD1  . ILE A 1 988  ? 127.931 78.811  83.273  1.00 18.89 ?  988  ILE A CD1  1 
ATOM   6416  N N    . VAL A 1 989  ? 129.398 78.445  77.929  1.00 21.67 ?  989  VAL A N    1 
ATOM   6417  C CA   . VAL A 1 989  ? 129.290 78.817  76.522  1.00 22.16 ?  989  VAL A CA   1 
ATOM   6418  C C    . VAL A 1 989  ? 130.606 79.457  76.092  1.00 21.48 ?  989  VAL A C    1 
ATOM   6419  O O    . VAL A 1 989  ? 131.174 80.283  76.812  1.00 26.37 ?  989  VAL A O    1 
ATOM   6420  C CB   . VAL A 1 989  ? 128.078 79.748  76.280  1.00 19.95 ?  989  VAL A CB   1 
ATOM   6421  C CG1  . VAL A 1 989  ? 128.033 80.864  77.310  1.00 21.33 ?  989  VAL A CG1  1 
ATOM   6422  C CG2  . VAL A 1 989  ? 128.093 80.319  74.868  1.00 20.40 ?  989  VAL A CG2  1 
ATOM   6423  N N    . ARG A 1 990  ? 131.096 79.056  74.923  1.00 20.13 ?  990  ARG A N    1 
ATOM   6424  C CA   . ARG A 1 990  ? 132.349 79.557  74.377  1.00 24.52 ?  990  ARG A CA   1 
ATOM   6425  C C    . ARG A 1 990  ? 132.089 80.688  73.385  1.00 27.73 ?  990  ARG A C    1 
ATOM   6426  O O    . ARG A 1 990  ? 130.954 80.954  72.984  1.00 28.45 ?  990  ARG A O    1 
ATOM   6427  C CB   . ARG A 1 990  ? 133.131 78.424  73.705  1.00 24.91 ?  990  ARG A CB   1 
ATOM   6428  C CG   . ARG A 1 990  ? 133.968 77.592  74.662  1.00 24.49 ?  990  ARG A CG   1 
ATOM   6429  C CD   . ARG A 1 990  ? 133.737 76.105  74.444  1.00 23.64 ?  990  ARG A CD   1 
ATOM   6430  N NE   . ARG A 1 990  ? 134.455 75.290  75.416  1.00 26.69 ?  990  ARG A NE   1 
ATOM   6431  C CZ   . ARG A 1 990  ? 134.023 74.126  75.884  1.00 25.87 ?  990  ARG A CZ   1 
ATOM   6432  N NH1  . ARG A 1 990  ? 132.872 73.607  75.490  1.00 28.07 ?  990  ARG A NH1  1 
ATOM   6433  N NH2  . ARG A 1 990  ? 134.765 73.467  76.770  1.00 22.94 ?  990  ARG A NH2  1 
ATOM   6434  N N    . GLU A 1 991  ? 133.170 81.359  72.993  1.00 27.07 ?  991  GLU A N    1 
ATOM   6435  C CA   . GLU A 1 991  ? 133.071 82.455  72.040  1.00 26.08 ?  991  GLU A CA   1 
ATOM   6436  C C    . GLU A 1 991  ? 132.802 81.930  70.634  1.00 27.06 ?  991  GLU A C    1 
ATOM   6437  O O    . GLU A 1 991  ? 133.130 80.790  70.296  1.00 24.41 ?  991  GLU A O    1 
ATOM   6438  C CB   . GLU A 1 991  ? 134.353 83.288  72.041  1.00 25.91 ?  991  GLU A CB   1 
ATOM   6439  C CG   . GLU A 1 991  ? 134.893 83.606  73.421  1.00 27.10 ?  991  GLU A CG   1 
ATOM   6440  C CD   . GLU A 1 991  ? 136.198 84.376  73.376  1.00 31.04 ?  991  GLU A CD   1 
ATOM   6441  O OE1  . GLU A 1 991  ? 136.410 85.133  72.405  1.00 27.22 ?  991  GLU A OE1  1 
ATOM   6442  O OE2  . GLU A 1 991  ? 137.012 84.226  74.311  1.00 30.39 ?  991  GLU A OE2  1 
ATOM   6443  N N    . GLY A 1 992  ? 132.194 82.784  69.809  1.00 27.73 ?  992  GLY A N    1 
ATOM   6444  C CA   . GLY A 1 992  ? 131.918 82.461  68.426  1.00 28.17 ?  992  GLY A CA   1 
ATOM   6445  C C    . GLY A 1 992  ? 130.687 81.618  68.185  1.00 27.84 ?  992  GLY A C    1 
ATOM   6446  O O    . GLY A 1 992  ? 130.143 81.646  67.075  1.00 28.67 ?  992  GLY A O    1 
ATOM   6447  N N    . ASP A 1 993  ? 130.228 80.867  69.182  1.00 23.24 ?  993  ASP A N    1 
ATOM   6448  C CA   . ASP A 1 993  ? 129.056 80.024  69.017  1.00 24.36 ?  993  ASP A CA   1 
ATOM   6449  C C    . ASP A 1 993  ? 127.789 80.872  68.957  1.00 25.22 ?  993  ASP A C    1 
ATOM   6450  O O    . ASP A 1 993  ? 127.736 81.999  69.458  1.00 25.78 ?  993  ASP A O    1 
ATOM   6451  C CB   . ASP A 1 993  ? 128.959 79.017  70.163  1.00 26.43 ?  993  ASP A CB   1 
ATOM   6452  C CG   . ASP A 1 993  ? 130.277 78.322  70.442  1.00 26.66 ?  993  ASP A CG   1 
ATOM   6453  O OD1  . ASP A 1 993  ? 131.055 78.115  69.487  1.00 24.40 ?  993  ASP A OD1  1 
ATOM   6454  O OD2  . ASP A 1 993  ? 130.536 77.988  71.616  1.00 24.44 ?  993  ASP A OD2  1 
ATOM   6455  N N    . GLU A 1 994  ? 126.762 80.316  68.319  1.00 27.67 ?  994  GLU A N    1 
ATOM   6456  C CA   . GLU A 1 994  ? 125.475 80.990  68.243  1.00 27.48 ?  994  GLU A CA   1 
ATOM   6457  C C    . GLU A 1 994  ? 124.826 81.052  69.621  1.00 26.59 ?  994  GLU A C    1 
ATOM   6458  O O    . GLU A 1 994  ? 125.038 80.185  70.473  1.00 30.32 ?  994  GLU A O    1 
ATOM   6459  C CB   . GLU A 1 994  ? 124.554 80.274  67.256  1.00 27.03 ?  994  GLU A CB   1 
ATOM   6460  C CG   . GLU A 1 994  ? 123.787 81.208  66.332  1.00 27.54 ?  994  GLU A CG   1 
ATOM   6461  C CD   . GLU A 1 994  ? 122.564 81.811  66.993  1.00 31.11 ?  994  GLU A CD   1 
ATOM   6462  O OE1  . GLU A 1 994  ? 121.988 81.159  67.889  1.00 30.00 ?  994  GLU A OE1  1 
ATOM   6463  O OE2  . GLU A 1 994  ? 122.179 82.939  66.617  1.00 30.98 ?  994  GLU A OE2  1 
ATOM   6464  N N    . SER A 1 995  ? 124.032 82.098  69.836  1.00 20.49 ?  995  SER A N    1 
ATOM   6465  C CA   . SER A 1 995  ? 123.411 82.337  71.135  1.00 24.23 ?  995  SER A CA   1 
ATOM   6466  C C    . SER A 1 995  ? 122.317 81.305  71.381  1.00 22.92 ?  995  SER A C    1 
ATOM   6467  O O    . SER A 1 995  ? 121.258 81.346  70.747  1.00 21.91 ?  995  SER A O    1 
ATOM   6468  C CB   . SER A 1 995  ? 122.851 83.754  71.191  1.00 22.99 ?  995  SER A CB   1 
ATOM   6469  O OG   . SER A 1 995  ? 123.883 84.706  71.004  1.00 21.57 ?  995  SER A OG   1 
ATOM   6470  N N    . ASP A 1 996  ? 122.576 80.375  72.303  1.00 22.28 ?  996  ASP A N    1 
ATOM   6471  C CA   . ASP A 1 996  ? 121.593 79.343  72.615  1.00 22.80 ?  996  ASP A CA   1 
ATOM   6472  C C    . ASP A 1 996  ? 120.385 79.923  73.342  1.00 27.13 ?  996  ASP A C    1 
ATOM   6473  O O    . ASP A 1 996  ? 119.246 79.517  73.084  1.00 26.20 ?  996  ASP A O    1 
ATOM   6474  C CB   . ASP A 1 996  ? 122.241 78.237  73.448  1.00 22.42 ?  996  ASP A CB   1 
ATOM   6475  C CG   . ASP A 1 996  ? 121.373 76.996  73.547  1.00 27.58 ?  996  ASP A CG   1 
ATOM   6476  O OD1  . ASP A 1 996  ? 120.442 76.849  72.728  1.00 30.26 ?  996  ASP A OD1  1 
ATOM   6477  O OD2  . ASP A 1 996  ? 121.624 76.166  74.446  1.00 27.64 ?  996  ASP A OD2  1 
ATOM   6478  N N    . GLY A 1 997  ? 120.608 80.866  74.248  1.00 25.45 ?  997  GLY A N    1 
ATOM   6479  C CA   . GLY A 1 997  ? 119.508 81.425  75.006  1.00 22.27 ?  997  GLY A CA   1 
ATOM   6480  C C    . GLY A 1 997  ? 119.981 82.470  75.988  1.00 23.18 ?  997  GLY A C    1 
ATOM   6481  O O    . GLY A 1 997  ? 121.068 83.033  75.847  1.00 22.46 ?  997  GLY A O    1 
ATOM   6482  N N    . LEU A 1 998  ? 119.146 82.721  76.993  1.00 28.54 ?  998  LEU A N    1 
ATOM   6483  C CA   . LEU A 1 998  ? 119.387 83.754  77.992  1.00 24.37 ?  998  LEU A CA   1 
ATOM   6484  C C    . LEU A 1 998  ? 119.567 83.109  79.359  1.00 22.78 ?  998  LEU A C    1 
ATOM   6485  O O    . LEU A 1 998  ? 118.777 82.245  79.752  1.00 23.19 ?  998  LEU A O    1 
ATOM   6486  C CB   . LEU A 1 998  ? 118.231 84.757  78.020  1.00 18.20 ?  998  LEU A CB   1 
ATOM   6487  C CG   . LEU A 1 998  ? 118.320 85.931  78.994  1.00 17.91 ?  998  LEU A CG   1 
ATOM   6488  C CD1  . LEU A 1 998  ? 118.030 87.236  78.272  1.00 21.18 ?  998  LEU A CD1  1 
ATOM   6489  C CD2  . LEU A 1 998  ? 117.358 85.738  80.154  1.00 23.21 ?  998  LEU A CD2  1 
ATOM   6490  N N    . PHE A 1 999  ? 120.602 83.532  80.077  1.00 15.96 ?  999  PHE A N    1 
ATOM   6491  C CA   . PHE A 1 999  ? 120.937 82.997  81.388  1.00 12.96 ?  999  PHE A CA   1 
ATOM   6492  C C    . PHE A 1 999  ? 120.461 83.933  82.492  1.00 16.80 ?  999  PHE A C    1 
ATOM   6493  O O    . PHE A 1 999  ? 120.082 85.080  82.247  1.00 22.82 ?  999  PHE A O    1 
ATOM   6494  C CB   . PHE A 1 999  ? 122.449 82.788  81.511  1.00 14.57 ?  999  PHE A CB   1 
ATOM   6495  C CG   . PHE A 1 999  ? 122.978 81.657  80.682  1.00 21.73 ?  999  PHE A CG   1 
ATOM   6496  C CD1  . PHE A 1 999  ? 122.158 80.608  80.303  1.00 21.13 ?  999  PHE A CD1  1 
ATOM   6497  C CD2  . PHE A 1 999  ? 124.299 81.651  80.268  1.00 23.55 ?  999  PHE A CD2  1 
ATOM   6498  C CE1  . PHE A 1 999  ? 122.651 79.568  79.536  1.00 20.16 ?  999  PHE A CE1  1 
ATOM   6499  C CE2  . PHE A 1 999  ? 124.794 80.618  79.500  1.00 21.19 ?  999  PHE A CE2  1 
ATOM   6500  C CZ   . PHE A 1 999  ? 123.969 79.574  79.134  1.00 21.12 ?  999  PHE A CZ   1 
ATOM   6501  N N    . LEU A 1 1000 ? 120.486 83.423  83.721  1.00 10.64 ?  1000 LEU A N    1 
ATOM   6502  C CA   . LEU A 1 1000 ? 120.230 84.243  84.904  1.00 8.66  ?  1000 LEU A CA   1 
ATOM   6503  C C    . LEU A 1 1000 ? 120.885 83.544  86.086  1.00 16.58 ?  1000 LEU A C    1 
ATOM   6504  O O    . LEU A 1 1000 ? 120.408 82.494  86.528  1.00 24.61 ?  1000 LEU A O    1 
ATOM   6505  C CB   . LEU A 1 1000 ? 118.733 84.445  85.135  1.00 10.27 ?  1000 LEU A CB   1 
ATOM   6506  C CG   . LEU A 1 1000 ? 118.301 84.946  86.517  1.00 15.61 ?  1000 LEU A CG   1 
ATOM   6507  C CD1  . LEU A 1 1000 ? 118.760 86.377  86.732  1.00 18.93 ?  1000 LEU A CD1  1 
ATOM   6508  C CD2  . LEU A 1 1000 ? 116.797 84.833  86.696  1.00 20.43 ?  1000 LEU A CD2  1 
ATOM   6509  N N    . ILE A 1 1001 ? 121.978 84.117  86.588  1.00 17.82 ?  1001 ILE A N    1 
ATOM   6510  C CA   . ILE A 1 1001 ? 122.710 83.515  87.697  1.00 17.71 ?  1001 ILE A CA   1 
ATOM   6511  C C    . ILE A 1 1001 ? 121.890 83.665  88.971  1.00 14.99 ?  1001 ILE A C    1 
ATOM   6512  O O    . ILE A 1 1001 ? 121.563 84.782  89.387  1.00 15.97 ?  1001 ILE A O    1 
ATOM   6513  C CB   . ILE A 1 1001 ? 124.092 84.162  87.858  1.00 11.57 ?  1001 ILE A CB   1 
ATOM   6514  C CG1  . ILE A 1 1001 ? 124.771 84.346  86.500  1.00 11.26 ?  1001 ILE A CG1  1 
ATOM   6515  C CG2  . ILE A 1 1001 ? 124.961 83.332  88.784  1.00 12.01 ?  1001 ILE A CG2  1 
ATOM   6516  C CD1  . ILE A 1 1001 ? 125.161 83.053  85.835  1.00 15.39 ?  1001 ILE A CD1  1 
ATOM   6517  N N    . VAL A 1 1002 ? 121.554 82.539  89.599  1.00 11.33 ?  1002 VAL A N    1 
ATOM   6518  C CA   . VAL A 1 1002 ? 120.840 82.558  90.872  1.00 16.73 ?  1002 VAL A CA   1 
ATOM   6519  C C    . VAL A 1 1002 ? 121.667 82.011  92.024  1.00 19.69 ?  1002 VAL A C    1 
ATOM   6520  O O    . VAL A 1 1002 ? 121.295 82.236  93.187  1.00 21.34 ?  1002 VAL A O    1 
ATOM   6521  C CB   . VAL A 1 1002 ? 119.493 81.808  90.786  1.00 20.46 ?  1002 VAL A CB   1 
ATOM   6522  C CG1  . VAL A 1 1002 ? 118.646 82.373  89.664  1.00 20.50 ?  1002 VAL A CG1  1 
ATOM   6523  C CG2  . VAL A 1 1002 ? 119.708 80.318  90.600  1.00 20.00 ?  1002 VAL A CG2  1 
ATOM   6524  N N    . SER A 1 1003 ? 122.769 81.314  91.755  1.00 14.80 ?  1003 SER A N    1 
ATOM   6525  C CA   . SER A 1 1003 ? 123.666 80.912  92.832  1.00 14.46 ?  1003 SER A CA   1 
ATOM   6526  C C    . SER A 1 1003 ? 125.083 80.792  92.297  1.00 20.01 ?  1003 SER A C    1 
ATOM   6527  O O    . SER A 1 1003 ? 125.307 80.098  91.305  1.00 19.63 ?  1003 SER A O    1 
ATOM   6528  C CB   . SER A 1 1003 ? 123.226 79.582  93.456  1.00 22.49 ?  1003 SER A CB   1 
ATOM   6529  O OG   . SER A 1 1003 ? 124.163 79.138  94.423  1.00 24.58 ?  1003 SER A OG   1 
ATOM   6530  N N    . GLY A 1 1004 ? 126.027 81.453  92.956  1.00 19.63 ?  1004 GLY A N    1 
ATOM   6531  C CA   . GLY A 1 1004 ? 127.433 81.246  92.686  1.00 18.53 ?  1004 GLY A CA   1 
ATOM   6532  C C    . GLY A 1 1004 ? 128.048 82.350  91.840  1.00 12.01 ?  1004 GLY A C    1 
ATOM   6533  O O    . GLY A 1 1004 ? 127.371 83.071  91.103  1.00 14.65 ?  1004 GLY A O    1 
ATOM   6534  N N    . LEU A 1 1005 ? 129.368 82.475  91.960  1.00 10.47 ?  1005 LEU A N    1 
ATOM   6535  C CA   . LEU A 1 1005 ? 130.166 83.396  91.165  1.00 11.61 ?  1005 LEU A CA   1 
ATOM   6536  C C    . LEU A 1 1005 ? 130.599 82.728  89.866  1.00 11.86 ?  1005 LEU A C    1 
ATOM   6537  O O    . LEU A 1 1005 ? 130.804 81.513  89.809  1.00 20.48 ?  1005 LEU A O    1 
ATOM   6538  C CB   . LEU A 1 1005 ? 131.398 83.851  91.950  1.00 17.20 ?  1005 LEU A CB   1 
ATOM   6539  C CG   . LEU A 1 1005 ? 132.183 85.068  91.453  1.00 12.52 ?  1005 LEU A CG   1 
ATOM   6540  C CD1  . LEU A 1 1005 ? 131.466 86.361  91.787  1.00 9.36  ?  1005 LEU A CD1  1 
ATOM   6541  C CD2  . LEU A 1 1005 ? 133.589 85.068  92.030  1.00 15.83 ?  1005 LEU A CD2  1 
ATOM   6542  N N    . VAL A 1 1006 ? 130.741 83.535  88.815  1.00 8.33  ?  1006 VAL A N    1 
ATOM   6543  C CA   . VAL A 1 1006 ? 131.096 83.024  87.498  1.00 9.74  ?  1006 VAL A CA   1 
ATOM   6544  C C    . VAL A 1 1006 ? 131.960 84.068  86.796  1.00 14.76 ?  1006 VAL A C    1 
ATOM   6545  O O    . VAL A 1 1006 ? 131.847 85.267  87.062  1.00 21.34 ?  1006 VAL A O    1 
ATOM   6546  C CB   . VAL A 1 1006 ? 129.820 82.672  86.693  1.00 7.70  ?  1006 VAL A CB   1 
ATOM   6547  C CG1  . VAL A 1 1006 ? 129.007 83.920  86.367  1.00 10.72 ?  1006 VAL A CG1  1 
ATOM   6548  C CG2  . VAL A 1 1006 ? 130.140 81.853  85.464  1.00 12.26 ?  1006 VAL A CG2  1 
ATOM   6549  N N    . LYS A 1 1007 ? 132.857 83.611  85.920  1.00 11.92 ?  1007 LYS A N    1 
ATOM   6550  C CA   . LYS A 1 1007 ? 133.830 84.480  85.269  1.00 8.42  ?  1007 LYS A CA   1 
ATOM   6551  C C    . LYS A 1 1007 ? 133.526 84.578  83.781  1.00 14.85 ?  1007 LYS A C    1 
ATOM   6552  O O    . LYS A 1 1007 ? 133.428 83.558  83.092  1.00 17.85 ?  1007 LYS A O    1 
ATOM   6553  C CB   . LYS A 1 1007 ? 135.256 83.964  85.486  1.00 8.89  ?  1007 LYS A CB   1 
ATOM   6554  C CG   . LYS A 1 1007 ? 136.308 84.640  84.621  1.00 13.02 ?  1007 LYS A CG   1 
ATOM   6555  C CD   . LYS A 1 1007 ? 137.714 84.288  85.087  1.00 15.74 ?  1007 LYS A CD   1 
ATOM   6556  C CE   . LYS A 1 1007 ? 138.689 84.233  83.922  1.00 13.69 ?  1007 LYS A CE   1 
ATOM   6557  N NZ   . LYS A 1 1007 ? 138.206 83.329  82.843  1.00 12.40 ?  1007 LYS A NZ   1 
ATOM   6558  N N    . LEU A 1 1008 ? 133.391 85.809  83.290  1.00 16.76 ?  1008 LEU A N    1 
ATOM   6559  C CA   . LEU A 1 1008 ? 133.079 86.100  81.894  1.00 12.07 ?  1008 LEU A CA   1 
ATOM   6560  C C    . LEU A 1 1008 ? 134.309 86.756  81.279  1.00 15.94 ?  1008 LEU A C    1 
ATOM   6561  O O    . LEU A 1 1008 ? 134.613 87.914  81.586  1.00 18.25 ?  1008 LEU A O    1 
ATOM   6562  C CB   . LEU A 1 1008 ? 131.855 87.013  81.803  1.00 12.54 ?  1008 LEU A CB   1 
ATOM   6563  C CG   . LEU A 1 1008 ? 131.454 87.658  80.477  1.00 16.13 ?  1008 LEU A CG   1 
ATOM   6564  C CD1  . LEU A 1 1008 ? 130.584 86.713  79.671  1.00 17.36 ?  1008 LEU A CD1  1 
ATOM   6565  C CD2  . LEU A 1 1008 ? 130.738 88.980  80.714  1.00 14.64 ?  1008 LEU A CD2  1 
ATOM   6566  N N    . TYR A 1 1009 ? 135.026 86.024  80.427  1.00 16.50 ?  1009 TYR A N    1 
ATOM   6567  C CA   . TYR A 1 1009 ? 136.297 86.495  79.891  1.00 22.47 ?  1009 TYR A CA   1 
ATOM   6568  C C    . TYR A 1 1009 ? 136.317 86.328  78.380  1.00 23.68 ?  1009 TYR A C    1 
ATOM   6569  O O    . TYR A 1 1009 ? 135.917 85.285  77.860  1.00 19.16 ?  1009 TYR A O    1 
ATOM   6570  C CB   . TYR A 1 1009 ? 137.475 85.736  80.528  1.00 22.63 ?  1009 TYR A CB   1 
ATOM   6571  C CG   . TYR A 1 1009 ? 138.670 85.529  79.620  1.00 25.03 ?  1009 TYR A CG   1 
ATOM   6572  C CD1  . TYR A 1 1009 ? 139.555 86.566  79.353  1.00 22.79 ?  1009 TYR A CD1  1 
ATOM   6573  C CD2  . TYR A 1 1009 ? 138.922 84.289  79.044  1.00 23.06 ?  1009 TYR A CD2  1 
ATOM   6574  C CE1  . TYR A 1 1009 ? 140.650 86.378  78.528  1.00 24.11 ?  1009 TYR A CE1  1 
ATOM   6575  C CE2  . TYR A 1 1009 ? 140.013 84.092  78.218  1.00 23.59 ?  1009 TYR A CE2  1 
ATOM   6576  C CZ   . TYR A 1 1009 ? 140.874 85.139  77.964  1.00 25.75 ?  1009 TYR A CZ   1 
ATOM   6577  O OH   . TYR A 1 1009 ? 141.961 84.946  77.144  1.00 23.21 ?  1009 TYR A OH   1 
ATOM   6578  N N    . GLY A 1 1010 ? 136.790 87.349  77.679  1.00 25.36 ?  1010 GLY A N    1 
ATOM   6579  C CA   . GLY A 1 1010 ? 136.831 87.276  76.232  1.00 24.93 ?  1010 GLY A CA   1 
ATOM   6580  C C    . GLY A 1 1010 ? 137.428 88.523  75.624  1.00 23.61 ?  1010 GLY A C    1 
ATOM   6581  O O    . GLY A 1 1010 ? 138.194 89.242  76.267  1.00 23.46 ?  1010 GLY A O    1 
ATOM   6582  N N    . LYS A 1 1011 ? 137.076 88.762  74.364  1.00 24.19 ?  1011 LYS A N    1 
ATOM   6583  C CA   . LYS A 1 1011 ? 137.547 89.937  73.641  1.00 25.81 ?  1011 LYS A CA   1 
ATOM   6584  C C    . LYS A 1 1011 ? 136.395 90.889  73.339  1.00 26.18 ?  1011 LYS A C    1 
ATOM   6585  O O    . LYS A 1 1011 ? 135.263 90.459  73.119  1.00 26.22 ?  1011 LYS A O    1 
ATOM   6586  C CB   . LYS A 1 1011 ? 138.244 89.526  72.342  1.00 23.70 ?  1011 LYS A CB   1 
ATOM   6587  C CG   . LYS A 1 1011 ? 138.556 90.688  71.412  1.00 21.16 ?  1011 LYS A CG   1 
ATOM   6588  C CD   . LYS A 1 1011 ? 139.773 91.465  71.887  1.00 24.60 ?  1011 LYS A CD   1 
ATOM   6589  C CE   . LYS A 1 1011 ? 140.135 92.577  70.915  1.00 26.16 ?  1011 LYS A CE   1 
ATOM   6590  N NZ   . LYS A 1 1011 ? 141.565 92.974  71.036  1.00 25.79 ?  1011 LYS A NZ   1 
ATOM   6591  N N    . VAL A 1 1031 ? 140.280 90.273  75.628  1.00 22.46 ?  1031 VAL A N    1 
ATOM   6592  C CA   . VAL A 1 1031 ? 141.256 90.958  76.463  1.00 23.19 ?  1031 VAL A CA   1 
ATOM   6593  C C    . VAL A 1 1031 ? 140.635 91.333  77.803  1.00 26.38 ?  1031 VAL A C    1 
ATOM   6594  O O    . VAL A 1 1031 ? 141.345 91.559  78.783  1.00 25.10 ?  1031 VAL A O    1 
ATOM   6595  C CB   . VAL A 1 1031 ? 141.815 92.207  75.759  1.00 22.16 ?  1031 VAL A CB   1 
ATOM   6596  C CG1  . VAL A 1 1031 ? 142.824 91.810  74.691  1.00 21.80 ?  1031 VAL A CG1  1 
ATOM   6597  C CG2  . VAL A 1 1031 ? 140.685 93.030  75.160  1.00 22.94 ?  1031 VAL A CG2  1 
ATOM   6598  N N    . PHE A 1 1032 ? 139.309 91.396  77.843  1.00 25.74 ?  1032 PHE A N    1 
ATOM   6599  C CA   . PHE A 1 1032 ? 138.587 91.807  79.037  1.00 23.07 ?  1032 PHE A CA   1 
ATOM   6600  C C    . PHE A 1 1032 ? 138.113 90.595  79.832  1.00 22.72 ?  1032 PHE A C    1 
ATOM   6601  O O    . PHE A 1 1032 ? 137.936 89.494  79.301  1.00 19.65 ?  1032 PHE A O    1 
ATOM   6602  C CB   . PHE A 1 1032 ? 137.398 92.705  78.674  1.00 20.78 ?  1032 PHE A CB   1 
ATOM   6603  C CG   . PHE A 1 1032 ? 136.112 91.961  78.443  1.00 21.45 ?  1032 PHE A CG   1 
ATOM   6604  C CD1  . PHE A 1 1032 ? 135.928 91.202  77.299  1.00 23.80 ?  1032 PHE A CD1  1 
ATOM   6605  C CD2  . PHE A 1 1032 ? 135.082 92.031  79.367  1.00 19.50 ?  1032 PHE A CD2  1 
ATOM   6606  C CE1  . PHE A 1 1032 ? 134.744 90.520  77.085  1.00 24.29 ?  1032 PHE A CE1  1 
ATOM   6607  C CE2  . PHE A 1 1032 ? 133.896 91.352  79.159  1.00 21.05 ?  1032 PHE A CE2  1 
ATOM   6608  C CZ   . PHE A 1 1032 ? 133.727 90.596  78.017  1.00 21.99 ?  1032 PHE A CZ   1 
ATOM   6609  N N    . GLU A 1 1033 ? 137.919 90.818  81.130  1.00 26.76 ?  1033 GLU A N    1 
ATOM   6610  C CA   . GLU A 1 1033 ? 137.506 89.774  82.057  1.00 23.21 ?  1033 GLU A CA   1 
ATOM   6611  C C    . GLU A 1 1033 ? 136.721 90.418  83.190  1.00 22.10 ?  1033 GLU A C    1 
ATOM   6612  O O    . GLU A 1 1033 ? 137.144 91.443  83.730  1.00 21.64 ?  1033 GLU A O    1 
ATOM   6613  C CB   . GLU A 1 1033 ? 138.722 89.018  82.604  1.00 21.00 ?  1033 GLU A CB   1 
ATOM   6614  C CG   . GLU A 1 1033 ? 138.439 88.143  83.813  1.00 22.39 ?  1033 GLU A CG   1 
ATOM   6615  C CD   . GLU A 1 1033 ? 139.706 87.591  84.436  1.00 25.31 ?  1033 GLU A CD   1 
ATOM   6616  O OE1  . GLU A 1 1033 ? 140.782 87.721  83.814  1.00 27.35 ?  1033 GLU A OE1  1 
ATOM   6617  O OE2  . GLU A 1 1033 ? 139.629 87.030  85.549  1.00 22.11 ?  1033 GLU A OE2  1 
ATOM   6618  N N    . ASP A 1 1034 ? 135.582 89.822  83.539  1.00 16.40 ?  1034 ASP A N    1 
ATOM   6619  C CA   . ASP A 1 1034 ? 134.740 90.326  84.613  1.00 14.63 ?  1034 ASP A CA   1 
ATOM   6620  C C    . ASP A 1 1034 ? 134.171 89.150  85.392  1.00 13.66 ?  1034 ASP A C    1 
ATOM   6621  O O    . ASP A 1 1034 ? 134.256 87.994  84.970  1.00 18.39 ?  1034 ASP A O    1 
ATOM   6622  C CB   . ASP A 1 1034 ? 133.611 91.215  84.077  1.00 16.31 ?  1034 ASP A CB   1 
ATOM   6623  C CG   . ASP A 1 1034 ? 133.284 92.368  85.008  1.00 21.96 ?  1034 ASP A CG   1 
ATOM   6624  O OD1  . ASP A 1 1034 ? 134.129 92.701  85.865  1.00 19.65 ?  1034 ASP A OD1  1 
ATOM   6625  O OD2  . ASP A 1 1034 ? 132.181 92.941  84.884  1.00 20.67 ?  1034 ASP A OD2  1 
ATOM   6626  N N    . TYR A 1 1035 ? 133.593 89.454  86.549  1.00 9.02  ?  1035 TYR A N    1 
ATOM   6627  C CA   . TYR A 1 1035 ? 132.963 88.458  87.402  1.00 5.95  ?  1035 TYR A CA   1 
ATOM   6628  C C    . TYR A 1 1035 ? 131.499 88.817  87.602  1.00 10.44 ?  1035 TYR A C    1 
ATOM   6629  O O    . TYR A 1 1035 ? 131.178 89.950  87.977  1.00 18.10 ?  1035 TYR A O    1 
ATOM   6630  C CB   . TYR A 1 1035 ? 133.678 88.355  88.751  1.00 9.45  ?  1035 TYR A CB   1 
ATOM   6631  C CG   . TYR A 1 1035 ? 135.088 87.820  88.655  1.00 12.09 ?  1035 TYR A CG   1 
ATOM   6632  C CD1  . TYR A 1 1035 ? 135.329 86.524  88.218  1.00 13.48 ?  1035 TYR A CD1  1 
ATOM   6633  C CD2  . TYR A 1 1035 ? 136.178 88.609  88.994  1.00 14.50 ?  1035 TYR A CD2  1 
ATOM   6634  C CE1  . TYR A 1 1035 ? 136.615 86.028  88.127  1.00 15.12 ?  1035 TYR A CE1  1 
ATOM   6635  C CE2  . TYR A 1 1035 ? 137.469 88.122  88.904  1.00 12.16 ?  1035 TYR A CE2  1 
ATOM   6636  C CZ   . TYR A 1 1035 ? 137.680 86.831  88.470  1.00 14.36 ?  1035 TYR A CZ   1 
ATOM   6637  O OH   . TYR A 1 1035 ? 138.962 86.340  88.379  1.00 16.49 ?  1035 TYR A OH   1 
ATOM   6638  N N    . LEU A 1 1036 ? 130.619 87.854  87.352  1.00 8.84  ?  1036 LEU A N    1 
ATOM   6639  C CA   . LEU A 1 1036 ? 129.190 88.013  87.558  1.00 11.32 ?  1036 LEU A CA   1 
ATOM   6640  C C    . LEU A 1 1036 ? 128.745 87.161  88.738  1.00 13.67 ?  1036 LEU A C    1 
ATOM   6641  O O    . LEU A 1 1036 ? 129.280 86.074  88.981  1.00 14.17 ?  1036 LEU A O    1 
ATOM   6642  C CB   . LEU A 1 1036 ? 128.402 87.626  86.304  1.00 10.23 ?  1036 LEU A CB   1 
ATOM   6643  C CG   . LEU A 1 1036 ? 128.723 88.430  85.045  1.00 9.74  ?  1036 LEU A CG   1 
ATOM   6644  C CD1  . LEU A 1 1036 ? 128.477 87.597  83.801  1.00 11.57 ?  1036 LEU A CD1  1 
ATOM   6645  C CD2  . LEU A 1 1036 ? 127.909 89.710  85.008  1.00 11.07 ?  1036 LEU A CD2  1 
ATOM   6646  N N    . THR A 1 1037 ? 127.757 87.665  89.464  1.00 9.48  ?  1037 THR A N    1 
ATOM   6647  C CA   . THR A 1 1037 ? 127.275 87.058  90.695  1.00 8.22  ?  1037 THR A CA   1 
ATOM   6648  C C    . THR A 1 1037 ? 125.765 86.834  90.531  1.00 11.47 ?  1037 THR A C    1 
ATOM   6649  O O    . THR A 1 1037 ? 125.229 86.925  89.424  1.00 16.43 ?  1037 THR A O    1 
ATOM   6650  C CB   . THR A 1 1037 ? 127.646 87.949  91.888  1.00 14.46 ?  1037 THR A CB   1 
ATOM   6651  O OG1  . THR A 1 1037 ? 128.959 88.477  91.680  1.00 18.56 ?  1037 THR A OG1  1 
ATOM   6652  C CG2  . THR A 1 1037 ? 127.728 87.136  93.181  1.00 15.66 ?  1037 THR A CG2  1 
ATOM   6653  N N    . VAL A 1 1038 ? 125.085 86.516  91.635  1.00 11.12 ?  1038 VAL A N    1 
ATOM   6654  C CA   . VAL A 1 1038 ? 123.665 86.191  91.590  1.00 8.97  ?  1038 VAL A CA   1 
ATOM   6655  C C    . VAL A 1 1038 ? 122.854 87.405  91.149  1.00 12.10 ?  1038 VAL A C    1 
ATOM   6656  O O    . VAL A 1 1038 ? 123.253 88.561  91.345  1.00 12.94 ?  1038 VAL A O    1 
ATOM   6657  C CB   . VAL A 1 1038 ? 123.200 85.671  92.963  1.00 9.44  ?  1038 VAL A CB   1 
ATOM   6658  C CG1  . VAL A 1 1038 ? 124.053 84.502  93.392  1.00 14.58 ?  1038 VAL A CG1  1 
ATOM   6659  C CG2  . VAL A 1 1038 ? 123.300 86.756  94.000  1.00 10.92 ?  1038 VAL A CG2  1 
ATOM   6660  N N    . GLY A 1 1039 ? 121.714 87.139  90.515  1.00 15.82 ?  1039 GLY A N    1 
ATOM   6661  C CA   . GLY A 1 1039 ? 120.840 88.197  90.053  1.00 12.19 ?  1039 GLY A CA   1 
ATOM   6662  C C    . GLY A 1 1039 ? 121.258 88.869  88.765  1.00 10.61 ?  1039 GLY A C    1 
ATOM   6663  O O    . GLY A 1 1039 ? 120.630 89.858  88.373  1.00 15.84 ?  1039 GLY A O    1 
ATOM   6664  N N    . ASN A 1 1040 ? 122.298 88.375  88.101  1.00 10.30 ?  1040 ASN A N    1 
ATOM   6665  C CA   . ASN A 1 1040 ? 122.800 88.972  86.873  1.00 10.67 ?  1040 ASN A CA   1 
ATOM   6666  C C    . ASN A 1 1040 ? 122.346 88.163  85.665  1.00 12.99 ?  1040 ASN A C    1 
ATOM   6667  O O    . ASN A 1 1040 ? 122.130 86.952  85.749  1.00 17.16 ?  1040 ASN A O    1 
ATOM   6668  C CB   . ASN A 1 1040 ? 124.327 89.067  86.894  1.00 12.51 ?  1040 ASN A CB   1 
ATOM   6669  C CG   . ASN A 1 1040 ? 124.828 90.285  87.650  1.00 17.68 ?  1040 ASN A CG   1 
ATOM   6670  O OD1  . ASN A 1 1040 ? 125.774 90.945  87.224  1.00 22.99 ?  1040 ASN A OD1  1 
ATOM   6671  N ND2  . ASN A 1 1040 ? 124.194 90.589  88.775  1.00 16.22 ?  1040 ASN A ND2  1 
ATOM   6672  N N    . VAL A 1 1041 ? 122.205 88.851  84.535  1.00 12.43 ?  1041 VAL A N    1 
ATOM   6673  C CA   . VAL A 1 1041 ? 121.693 88.271  83.299  1.00 10.10 ?  1041 VAL A CA   1 
ATOM   6674  C C    . VAL A 1 1041 ? 122.796 88.315  82.251  1.00 13.70 ?  1041 VAL A C    1 
ATOM   6675  O O    . VAL A 1 1041 ? 123.487 89.331  82.113  1.00 18.94 ?  1041 VAL A O    1 
ATOM   6676  C CB   . VAL A 1 1041 ? 120.440 89.017  82.804  1.00 11.59 ?  1041 VAL A CB   1 
ATOM   6677  C CG1  . VAL A 1 1041 ? 119.796 88.275  81.648  1.00 15.53 ?  1041 VAL A CG1  1 
ATOM   6678  C CG2  . VAL A 1 1041 ? 119.448 89.201  83.942  1.00 11.71 ?  1041 VAL A CG2  1 
ATOM   6679  N N    . ILE A 1 1042 ? 122.963 87.214  81.520  1.00 15.93 ?  1042 ILE A N    1 
ATOM   6680  C CA   . ILE A 1 1042 ? 123.967 87.097  80.470  1.00 15.53 ?  1042 ILE A CA   1 
ATOM   6681  C C    . ILE A 1 1042 ? 123.269 86.760  79.160  1.00 17.62 ?  1042 ILE A C    1 
ATOM   6682  O O    . ILE A 1 1042 ? 122.329 85.959  79.137  1.00 22.15 ?  1042 ILE A O    1 
ATOM   6683  C CB   . ILE A 1 1042 ? 125.027 86.024  80.799  1.00 13.49 ?  1042 ILE A CB   1 
ATOM   6684  C CG1  . ILE A 1 1042 ? 125.439 86.091  82.268  1.00 15.95 ?  1042 ILE A CG1  1 
ATOM   6685  C CG2  . ILE A 1 1042 ? 126.247 86.180  79.904  1.00 17.69 ?  1042 ILE A CG2  1 
ATOM   6686  C CD1  . ILE A 1 1042 ? 126.156 84.852  82.742  1.00 16.38 ?  1042 ILE A CD1  1 
ATOM   6687  N N    . GLY A 1 1043 ? 123.729 87.373  78.073  1.00 20.23 ?  1043 GLY A N    1 
ATOM   6688  C CA   . GLY A 1 1043 ? 123.264 87.013  76.749  1.00 23.58 ?  1043 GLY A CA   1 
ATOM   6689  C C    . GLY A 1 1043 ? 122.076 87.784  76.225  1.00 24.81 ?  1043 GLY A C    1 
ATOM   6690  O O    . GLY A 1 1043 ? 121.423 87.313  75.287  1.00 25.52 ?  1043 GLY A O    1 
ATOM   6691  N N    . GLU A 1 1044 ? 121.761 88.945  76.806  1.00 21.91 ?  1044 GLU A N    1 
ATOM   6692  C CA   . GLU A 1 1044 ? 120.653 89.750  76.299  1.00 22.74 ?  1044 GLU A CA   1 
ATOM   6693  C C    . GLU A 1 1044 ? 120.938 90.264  74.892  1.00 21.88 ?  1044 GLU A C    1 
ATOM   6694  O O    . GLU A 1 1044 ? 120.052 90.261  74.029  1.00 20.00 ?  1044 GLU A O    1 
ATOM   6695  C CB   . GLU A 1 1044 ? 120.373 90.912  77.251  1.00 20.25 ?  1044 GLU A CB   1 
ATOM   6696  C CG   . GLU A 1 1044 ? 120.067 90.479  78.675  1.00 23.30 ?  1044 GLU A CG   1 
ATOM   6697  C CD   . GLU A 1 1044 ? 119.286 91.519  79.453  1.00 26.33 ?  1044 GLU A CD   1 
ATOM   6698  O OE1  . GLU A 1 1044 ? 118.103 91.746  79.124  1.00 22.28 ?  1044 GLU A OE1  1 
ATOM   6699  O OE2  . GLU A 1 1044 ? 119.856 92.108  80.396  1.00 26.81 ?  1044 GLU A OE2  1 
ATOM   6700  N N    . MET A 1 1045 ? 122.174 90.707  74.643  1.00 22.92 ?  1045 MET A N    1 
ATOM   6701  C CA   . MET A 1 1045 ? 122.562 91.142  73.305  1.00 23.37 ?  1045 MET A CA   1 
ATOM   6702  C C    . MET A 1 1045 ? 122.492 90.000  72.300  1.00 25.50 ?  1045 MET A C    1 
ATOM   6703  O O    . MET A 1 1045 ? 122.101 90.214  71.145  1.00 26.69 ?  1045 MET A O    1 
ATOM   6704  C CB   . MET A 1 1045 ? 123.973 91.730  73.335  1.00 24.62 ?  1045 MET A CB   1 
ATOM   6705  C CG   . MET A 1 1045 ? 124.025 93.247  73.421  1.00 24.76 ?  1045 MET A CG   1 
ATOM   6706  S SD   . MET A 1 1045 ? 123.127 94.053  72.083  1.00 39.96 ?  1045 MET A SD   1 
ATOM   6707  C CE   . MET A 1 1045 ? 124.444 94.283  70.891  1.00 24.84 ?  1045 MET A CE   1 
ATOM   6708  N N    . GLY A 1 1046 ? 122.866 88.789  72.719  1.00 23.99 ?  1046 GLY A N    1 
ATOM   6709  C CA   . GLY A 1 1046 ? 122.812 87.650  71.818  1.00 24.85 ?  1046 GLY A CA   1 
ATOM   6710  C C    . GLY A 1 1046 ? 121.397 87.275  71.421  1.00 24.09 ?  1046 GLY A C    1 
ATOM   6711  O O    . GLY A 1 1046 ? 121.152 86.863  70.285  1.00 20.67 ?  1046 GLY A O    1 
ATOM   6712  N N    . VAL A 1 1047 ? 120.446 87.402  72.351  1.00 21.23 ?  1047 VAL A N    1 
ATOM   6713  C CA   . VAL A 1 1047 ? 119.049 87.126  72.020  1.00 20.49 ?  1047 VAL A CA   1 
ATOM   6714  C C    . VAL A 1 1047 ? 118.369 88.312  71.357  1.00 26.62 ?  1047 VAL A C    1 
ATOM   6715  O O    . VAL A 1 1047 ? 117.298 88.146  70.759  1.00 27.02 ?  1047 VAL A O    1 
ATOM   6716  C CB   . VAL A 1 1047 ? 118.271 86.689  73.278  1.00 19.88 ?  1047 VAL A CB   1 
ATOM   6717  C CG1  . VAL A 1 1047 ? 117.767 87.894  74.062  1.00 20.32 ?  1047 VAL A CG1  1 
ATOM   6718  C CG2  . VAL A 1 1047 ? 117.123 85.757  72.909  1.00 22.78 ?  1047 VAL A CG2  1 
ATOM   6719  N N    . LEU A 1 1048 ? 118.964 89.503  71.426  1.00 24.94 ?  1048 LEU A N    1 
ATOM   6720  C CA   . LEU A 1 1048 ? 118.381 90.675  70.780  1.00 22.76 ?  1048 LEU A CA   1 
ATOM   6721  C C    . LEU A 1 1048 ? 118.827 90.802  69.325  1.00 22.69 ?  1048 LEU A C    1 
ATOM   6722  O O    . LEU A 1 1048 ? 117.993 90.838  68.415  1.00 25.80 ?  1048 LEU A O    1 
ATOM   6723  C CB   . LEU A 1 1048 ? 118.737 91.942  71.567  1.00 24.07 ?  1048 LEU A CB   1 
ATOM   6724  C CG   . LEU A 1 1048 ? 117.809 92.286  72.732  1.00 22.97 ?  1048 LEU A CG   1 
ATOM   6725  C CD1  . LEU A 1 1048 ? 118.255 93.571  73.407  1.00 24.57 ?  1048 LEU A CD1  1 
ATOM   6726  C CD2  . LEU A 1 1048 ? 116.372 92.401  72.252  1.00 22.34 ?  1048 LEU A CD2  1 
ATOM   6727  N N    . THR A 1 1049 ? 120.136 90.872  69.090  1.00 21.68 ?  1049 THR A N    1 
ATOM   6728  C CA   . THR A 1 1049 ? 120.663 91.094  67.750  1.00 26.37 ?  1049 THR A CA   1 
ATOM   6729  C C    . THR A 1 1049 ? 121.037 89.810  67.019  1.00 25.55 ?  1049 THR A C    1 
ATOM   6730  O O    . THR A 1 1049 ? 121.475 89.886  65.866  1.00 23.06 ?  1049 THR A O    1 
ATOM   6731  C CB   . THR A 1 1049 ? 121.885 92.016  67.808  1.00 24.49 ?  1049 THR A CB   1 
ATOM   6732  O OG1  . THR A 1 1049 ? 122.713 91.649  68.919  1.00 25.33 ?  1049 THR A OG1  1 
ATOM   6733  C CG2  . THR A 1 1049 ? 121.455 93.463  67.952  1.00 20.80 ?  1049 THR A CG2  1 
ATOM   6734  N N    . LYS A 1 1050 ? 120.868 88.646  67.657  1.00 25.46 ?  1050 LYS A N    1 
ATOM   6735  C CA   . LYS A 1 1050 ? 121.209 87.342  67.075  1.00 30.74 ?  1050 LYS A CA   1 
ATOM   6736  C C    . LYS A 1 1050 ? 122.666 87.287  66.618  1.00 30.35 ?  1050 LYS A C    1 
ATOM   6737  O O    . LYS A 1 1050 ? 122.985 86.736  65.562  1.00 26.59 ?  1050 LYS A O    1 
ATOM   6738  C CB   . LYS A 1 1050 ? 120.262 86.977  65.929  1.00 29.85 ?  1050 LYS A CB   1 
ATOM   6739  C CG   . LYS A 1 1050 ? 119.216 85.940  66.302  1.00 27.29 ?  1050 LYS A CG   1 
ATOM   6740  C CD   . LYS A 1 1050 ? 118.011 86.590  66.957  1.00 26.95 ?  1050 LYS A CD   1 
ATOM   6741  C CE   . LYS A 1 1050 ? 116.903 85.582  67.209  1.00 27.15 ?  1050 LYS A CE   1 
ATOM   6742  N NZ   . LYS A 1 1050 ? 115.724 86.220  67.856  1.00 30.58 ?  1050 LYS A NZ   1 
ATOM   6743  N N    . LYS A 1 1051 ? 123.566 87.866  67.428  1.00 29.33 ?  1051 LYS A N    1 
ATOM   6744  C CA   . LYS A 1 1051 ? 124.992 87.865  67.143  1.00 27.79 ?  1051 LYS A CA   1 
ATOM   6745  C C    . LYS A 1 1051 ? 125.679 86.702  67.855  1.00 30.35 ?  1051 LYS A C    1 
ATOM   6746  O O    . LYS A 1 1051 ? 125.200 86.232  68.892  1.00 31.54 ?  1051 LYS A O    1 
ATOM   6747  C CB   . LYS A 1 1051 ? 125.624 89.183  67.585  1.00 25.16 ?  1051 LYS A CB   1 
ATOM   6748  C CG   . LYS A 1 1051 ? 125.054 90.411  66.896  1.00 25.67 ?  1051 LYS A CG   1 
ATOM   6749  C CD   . LYS A 1 1051 ? 124.990 90.234  65.387  1.00 27.77 ?  1051 LYS A CD   1 
ATOM   6750  C CE   . LYS A 1 1051 ? 126.340 90.493  64.740  1.00 30.86 ?  1051 LYS A CE   1 
ATOM   6751  N NZ   . LYS A 1 1051 ? 126.246 90.507  63.254  1.00 30.10 ?  1051 LYS A NZ   1 
ATOM   6752  N N    . PRO A 1 1052 ? 126.792 86.210  67.310  1.00 27.38 ?  1052 PRO A N    1 
ATOM   6753  C CA   . PRO A 1 1052 ? 127.530 85.138  67.987  1.00 27.12 ?  1052 PRO A CA   1 
ATOM   6754  C C    . PRO A 1 1052 ? 128.119 85.602  69.310  1.00 25.49 ?  1052 PRO A C    1 
ATOM   6755  O O    . PRO A 1 1052 ? 128.396 86.787  69.515  1.00 23.17 ?  1052 PRO A O    1 
ATOM   6756  C CB   . PRO A 1 1052 ? 128.636 84.778  66.987  1.00 24.22 ?  1052 PRO A CB   1 
ATOM   6757  C CG   . PRO A 1 1052 ? 128.138 85.266  65.670  1.00 25.47 ?  1052 PRO A CG   1 
ATOM   6758  C CD   . PRO A 1 1052 ? 127.339 86.493  65.972  1.00 22.61 ?  1052 PRO A CD   1 
ATOM   6759  N N    . ARG A 1 1053 ? 128.295 84.645  70.219  1.00 24.85 ?  1053 ARG A N    1 
ATOM   6760  C CA   . ARG A 1 1053 ? 128.868 84.934  71.525  1.00 26.28 ?  1053 ARG A CA   1 
ATOM   6761  C C    . ARG A 1 1053 ? 130.322 85.373  71.391  1.00 26.71 ?  1053 ARG A C    1 
ATOM   6762  O O    . ARG A 1 1053 ? 131.045 84.944  70.488  1.00 26.59 ?  1053 ARG A O    1 
ATOM   6763  C CB   . ARG A 1 1053 ? 128.772 83.707  72.432  1.00 26.45 ?  1053 ARG A CB   1 
ATOM   6764  C CG   . ARG A 1 1053 ? 127.364 83.152  72.575  1.00 24.74 ?  1053 ARG A CG   1 
ATOM   6765  C CD   . ARG A 1 1053 ? 126.685 83.676  73.830  1.00 26.95 ?  1053 ARG A CD   1 
ATOM   6766  N NE   . ARG A 1 1053 ? 125.279 83.296  73.888  1.00 25.33 ?  1053 ARG A NE   1 
ATOM   6767  C CZ   . ARG A 1 1053 ? 124.548 83.298  74.994  1.00 23.90 ?  1053 ARG A CZ   1 
ATOM   6768  N NH1  . ARG A 1 1053 ? 125.060 83.656  76.161  1.00 23.61 ?  1053 ARG A NH1  1 
ATOM   6769  N NH2  . ARG A 1 1053 ? 123.271 82.932  74.929  1.00 24.17 ?  1053 ARG A NH2  1 
ATOM   6770  N N    . ASN A 1 1054 ? 130.750 86.244  72.309  1.00 25.89 ?  1054 ASN A N    1 
ATOM   6771  C CA   . ASN A 1 1054 ? 132.070 86.858  72.225  1.00 28.29 ?  1054 ASN A CA   1 
ATOM   6772  C C    . ASN A 1 1054 ? 132.850 86.752  73.531  1.00 29.00 ?  1054 ASN A C    1 
ATOM   6773  O O    . ASN A 1 1054 ? 133.880 87.419  73.682  1.00 29.35 ?  1054 ASN A O    1 
ATOM   6774  C CB   . ASN A 1 1054 ? 131.950 88.325  71.804  1.00 26.08 ?  1054 ASN A CB   1 
ATOM   6775  C CG   . ASN A 1 1054 ? 131.070 89.130  72.741  1.00 29.27 ?  1054 ASN A CG   1 
ATOM   6776  O OD1  . ASN A 1 1054 ? 130.280 88.571  73.503  1.00 27.76 ?  1054 ASN A OD1  1 
ATOM   6777  N ND2  . ASN A 1 1054 ? 131.201 90.450  72.688  1.00 27.53 ?  1054 ASN A ND2  1 
ATOM   6778  N N    . ALA A 1 1055 ? 132.395 85.931  74.476  1.00 23.98 ?  1055 ALA A N    1 
ATOM   6779  C CA   . ALA A 1 1055 ? 133.092 85.799  75.749  1.00 21.00 ?  1055 ALA A CA   1 
ATOM   6780  C C    . ALA A 1 1055 ? 132.782 84.441  76.359  1.00 20.91 ?  1055 ALA A C    1 
ATOM   6781  O O    . ALA A 1 1055 ? 131.610 84.081  76.511  1.00 20.97 ?  1055 ALA A O    1 
ATOM   6782  C CB   . ALA A 1 1055 ? 132.697 86.923  76.711  1.00 20.92 ?  1055 ALA A CB   1 
ATOM   6783  N N    . THR A 1 1056 ? 133.829 83.698  76.707  1.00 20.51 ?  1056 THR A N    1 
ATOM   6784  C CA   . THR A 1 1056 ? 133.653 82.417  77.375  1.00 21.11 ?  1056 THR A CA   1 
ATOM   6785  C C    . THR A 1 1056 ? 133.259 82.631  78.832  1.00 19.65 ?  1056 THR A C    1 
ATOM   6786  O O    . THR A 1 1056 ? 133.786 83.514  79.518  1.00 22.03 ?  1056 THR A O    1 
ATOM   6787  C CB   . THR A 1 1056 ? 134.937 81.590  77.297  1.00 19.71 ?  1056 THR A CB   1 
ATOM   6788  O OG1  . THR A 1 1056 ? 135.500 81.698  75.984  1.00 22.50 ?  1056 THR A OG1  1 
ATOM   6789  C CG2  . THR A 1 1056 ? 134.649 80.125  77.592  1.00 17.67 ?  1056 THR A CG2  1 
ATOM   6790  N N    . VAL A 1 1057 ? 132.325 81.809  79.301  1.00 12.12 ?  1057 VAL A N    1 
ATOM   6791  C CA   . VAL A 1 1057 ? 131.779 81.899  80.650  1.00 14.32 ?  1057 VAL A CA   1 
ATOM   6792  C C    . VAL A 1 1057 ? 132.164 80.628  81.395  1.00 17.79 ?  1057 VAL A C    1 
ATOM   6793  O O    . VAL A 1 1057 ? 131.710 79.533  81.043  1.00 18.99 ?  1057 VAL A O    1 
ATOM   6794  C CB   . VAL A 1 1057 ? 130.254 82.089  80.620  1.00 17.81 ?  1057 VAL A CB   1 
ATOM   6795  C CG1  . VAL A 1 1057 ? 129.744 82.521  81.969  1.00 17.11 ?  1057 VAL A CG1  1 
ATOM   6796  C CG2  . VAL A 1 1057 ? 129.870 83.106  79.562  1.00 16.18 ?  1057 VAL A CG2  1 
ATOM   6797  N N    . THR A 1 1058 ? 132.996 80.771  82.426  1.00 16.74 ?  1058 THR A N    1 
ATOM   6798  C CA   . THR A 1 1058 ? 133.519 79.639  83.180  1.00 16.13 ?  1058 THR A CA   1 
ATOM   6799  C C    . THR A 1 1058 ? 133.099 79.736  84.640  1.00 16.93 ?  1058 THR A C    1 
ATOM   6800  O O    . THR A 1 1058 ? 133.173 80.807  85.251  1.00 17.99 ?  1058 THR A O    1 
ATOM   6801  C CB   . THR A 1 1058 ? 135.050 79.559  83.094  1.00 15.21 ?  1058 THR A CB   1 
ATOM   6802  O OG1  . THR A 1 1058 ? 135.633 80.425  84.075  1.00 11.96 ?  1058 THR A OG1  1 
ATOM   6803  C CG2  . THR A 1 1058 ? 135.542 79.957  81.708  1.00 14.82 ?  1058 THR A CG2  1 
ATOM   6804  N N    . CYS A 1 1059 ? 132.682 78.606  85.202  1.00 19.32 ?  1059 CYS A N    1 
ATOM   6805  C CA   . CYS A 1 1059 ? 132.183 78.566  86.571  1.00 19.41 ?  1059 CYS A CA   1 
ATOM   6806  C C    . CYS A 1 1059 ? 133.342 78.659  87.556  1.00 22.26 ?  1059 CYS A C    1 
ATOM   6807  O O    . CYS A 1 1059 ? 134.195 77.766  87.606  1.00 26.74 ?  1059 CYS A O    1 
ATOM   6808  C CB   . CYS A 1 1059 ? 131.389 77.284  86.803  1.00 19.15 ?  1059 CYS A CB   1 
ATOM   6809  S SG   . CYS A 1 1059 ? 130.466 76.714  85.360  1.00 29.62 ?  1059 CYS A SG   1 
ATOM   6810  N N    . GLU A 1 1060 ? 133.374 79.740  88.338  1.00 20.32 ?  1060 GLU A N    1 
ATOM   6811  C CA   . GLU A 1 1060 ? 134.364 79.855  89.403  1.00 22.51 ?  1060 GLU A CA   1 
ATOM   6812  C C    . GLU A 1 1060 ? 133.995 79.006  90.612  1.00 24.22 ?  1060 GLU A C    1 
ATOM   6813  O O    . GLU A 1 1060 ? 134.885 78.509  91.311  1.00 24.71 ?  1060 GLU A O    1 
ATOM   6814  C CB   . GLU A 1 1060 ? 134.528 81.318  89.817  1.00 23.18 ?  1060 GLU A CB   1 
ATOM   6815  C CG   . GLU A 1 1060 ? 135.916 81.664  90.332  1.00 24.54 ?  1060 GLU A CG   1 
ATOM   6816  C CD   . GLU A 1 1060 ? 136.913 81.915  89.215  1.00 26.40 ?  1060 GLU A CD   1 
ATOM   6817  O OE1  . GLU A 1 1060 ? 136.500 81.941  88.037  1.00 25.26 ?  1060 GLU A OE1  1 
ATOM   6818  O OE2  . GLU A 1 1060 ? 138.113 82.086  89.517  1.00 26.86 ?  1060 GLU A OE2  1 
ATOM   6819  N N    . THR A 1 1061 ? 132.700 78.857  90.891  1.00 20.63 ?  1061 THR A N    1 
ATOM   6820  C CA   . THR A 1 1061 ? 132.215 77.949  91.924  1.00 22.57 ?  1061 THR A CA   1 
ATOM   6821  C C    . THR A 1 1061 ? 131.124 77.060  91.343  1.00 19.82 ?  1061 THR A C    1 
ATOM   6822  O O    . THR A 1 1061 ? 130.898 77.063  90.129  1.00 17.66 ?  1061 THR A O    1 
ATOM   6823  C CB   . THR A 1 1061 ? 131.671 78.715  93.137  1.00 22.03 ?  1061 THR A CB   1 
ATOM   6824  O OG1  . THR A 1 1061 ? 130.500 79.448  92.757  1.00 21.04 ?  1061 THR A OG1  1 
ATOM   6825  C CG2  . THR A 1 1061 ? 132.711 79.674  93.703  1.00 18.43 ?  1061 THR A CG2  1 
ATOM   6826  N N    . THR A 1 1062 ? 130.446 76.292  92.192  1.00 19.60 ?  1062 THR A N    1 
ATOM   6827  C CA   . THR A 1 1062 ? 129.257 75.565  91.761  1.00 21.77 ?  1062 THR A CA   1 
ATOM   6828  C C    . THR A 1 1062 ? 128.132 76.569  91.548  1.00 20.87 ?  1062 THR A C    1 
ATOM   6829  O O    . THR A 1 1062 ? 127.686 77.222  92.497  1.00 21.82 ?  1062 THR A O    1 
ATOM   6830  C CB   . THR A 1 1062 ? 128.865 74.514  92.795  1.00 20.73 ?  1062 THR A CB   1 
ATOM   6831  O OG1  . THR A 1 1062 ? 128.685 75.140  94.072  1.00 16.14 ?  1062 THR A OG1  1 
ATOM   6832  C CG2  . THR A 1 1062 ? 129.942 73.446  92.906  1.00 20.06 ?  1062 THR A CG2  1 
ATOM   6833  N N    . VAL A 1 1063 ? 127.669 76.701  90.307  1.00 19.44 ?  1063 VAL A N    1 
ATOM   6834  C CA   . VAL A 1 1063 ? 126.745 77.761  89.922  1.00 18.37 ?  1063 VAL A CA   1 
ATOM   6835  C C    . VAL A 1 1063 ? 125.405 77.147  89.535  1.00 19.06 ?  1063 VAL A C    1 
ATOM   6836  O O    . VAL A 1 1063 ? 125.344 76.197  88.745  1.00 19.52 ?  1063 VAL A O    1 
ATOM   6837  C CB   . VAL A 1 1063 ? 127.320 78.625  88.783  1.00 19.95 ?  1063 VAL A CB   1 
ATOM   6838  C CG1  . VAL A 1 1063 ? 127.894 77.761  87.681  1.00 19.51 ?  1063 VAL A CG1  1 
ATOM   6839  C CG2  . VAL A 1 1063 ? 126.263 79.568  88.223  1.00 19.86 ?  1063 VAL A CG2  1 
ATOM   6840  N N    . GLN A 1 1064 ? 124.338 77.680  90.117  1.00 20.91 ?  1064 GLN A N    1 
ATOM   6841  C CA   . GLN A 1 1064 ? 122.972 77.382  89.717  1.00 22.84 ?  1064 GLN A CA   1 
ATOM   6842  C C    . GLN A 1 1064 ? 122.462 78.536  88.868  1.00 20.29 ?  1064 GLN A C    1 
ATOM   6843  O O    . GLN A 1 1064 ? 122.554 79.700  89.280  1.00 20.74 ?  1064 GLN A O    1 
ATOM   6844  C CB   . GLN A 1 1064 ? 122.074 77.180  90.937  1.00 22.39 ?  1064 GLN A CB   1 
ATOM   6845  C CG   . GLN A 1 1064 ? 122.336 75.887  91.685  1.00 22.37 ?  1064 GLN A CG   1 
ATOM   6846  C CD   . GLN A 1 1064 ? 121.163 75.455  92.542  1.00 25.55 ?  1064 GLN A CD   1 
ATOM   6847  O OE1  . GLN A 1 1064 ? 120.835 74.271  92.609  1.00 28.38 ?  1064 GLN A OE1  1 
ATOM   6848  N NE2  . GLN A 1 1064 ? 120.529 76.413  93.209  1.00 20.80 ?  1064 GLN A NE2  1 
ATOM   6849  N N    . VAL A 1 1065 ? 121.934 78.211  87.686  1.00 18.72 ?  1065 VAL A N    1 
ATOM   6850  C CA   . VAL A 1 1065 ? 121.532 79.198  86.695  1.00 18.07 ?  1065 VAL A CA   1 
ATOM   6851  C C    . VAL A 1 1065 ? 120.133 78.863  86.187  1.00 22.59 ?  1065 VAL A C    1 
ATOM   6852  O O    . VAL A 1 1065 ? 119.666 77.723  86.269  1.00 27.81 ?  1065 VAL A O    1 
ATOM   6853  C CB   . VAL A 1 1065 ? 122.544 79.274  85.523  1.00 19.78 ?  1065 VAL A CB   1 
ATOM   6854  C CG1  . VAL A 1 1065 ? 122.260 78.211  84.476  1.00 17.74 ?  1065 VAL A CG1  1 
ATOM   6855  C CG2  . VAL A 1 1065 ? 122.553 80.656  84.893  1.00 20.62 ?  1065 VAL A CG2  1 
ATOM   6856  N N    . TYR A 1 1066 ? 119.455 79.890  85.681  1.00 18.60 ?  1066 TYR A N    1 
ATOM   6857  C CA   . TYR A 1 1066 ? 118.159 79.760  85.028  1.00 17.04 ?  1066 TYR A CA   1 
ATOM   6858  C C    . TYR A 1 1066 ? 118.346 79.904  83.525  1.00 18.07 ?  1066 TYR A C    1 
ATOM   6859  O O    . TYR A 1 1066 ? 118.941 80.882  83.061  1.00 24.54 ?  1066 TYR A O    1 
ATOM   6860  C CB   . TYR A 1 1066 ? 117.177 80.816  85.542  1.00 18.53 ?  1066 TYR A CB   1 
ATOM   6861  C CG   . TYR A 1 1066 ? 116.136 80.290  86.505  1.00 20.13 ?  1066 TYR A CG   1 
ATOM   6862  C CD1  . TYR A 1 1066 ? 115.268 79.272  86.132  1.00 22.44 ?  1066 TYR A CD1  1 
ATOM   6863  C CD2  . TYR A 1 1066 ? 116.021 80.811  87.787  1.00 19.07 ?  1066 TYR A CD2  1 
ATOM   6864  C CE1  . TYR A 1 1066 ? 114.312 78.790  87.007  1.00 21.62 ?  1066 TYR A CE1  1 
ATOM   6865  C CE2  . TYR A 1 1066 ? 115.069 80.333  88.671  1.00 23.63 ?  1066 TYR A CE2  1 
ATOM   6866  C CZ   . TYR A 1 1066 ? 114.218 79.324  88.275  1.00 23.82 ?  1066 TYR A CZ   1 
ATOM   6867  O OH   . TYR A 1 1066 ? 113.269 78.844  89.148  1.00 25.49 ?  1066 TYR A OH   1 
ATOM   6868  N N    . PHE A 1 1067 ? 117.839 78.935  82.771  1.00 20.79 ?  1067 PHE A N    1 
ATOM   6869  C CA   . PHE A 1 1067 ? 117.988 78.896  81.324  1.00 21.92 ?  1067 PHE A CA   1 
ATOM   6870  C C    . PHE A 1 1067 ? 116.630 79.085  80.663  1.00 21.35 ?  1067 PHE A C    1 
ATOM   6871  O O    . PHE A 1 1067 ? 115.659 78.406  81.019  1.00 21.60 ?  1067 PHE A O    1 
ATOM   6872  C CB   . PHE A 1 1067 ? 118.616 77.575  80.873  1.00 21.14 ?  1067 PHE A CB   1 
ATOM   6873  C CG   . PHE A 1 1067 ? 119.093 77.579  79.445  1.00 23.52 ?  1067 PHE A CG   1 
ATOM   6874  C CD1  . PHE A 1 1067 ? 119.394 78.767  78.798  1.00 22.39 ?  1067 PHE A CD1  1 
ATOM   6875  C CD2  . PHE A 1 1067 ? 119.242 76.390  78.749  1.00 23.96 ?  1067 PHE A CD2  1 
ATOM   6876  C CE1  . PHE A 1 1067 ? 119.834 78.770  77.487  1.00 23.81 ?  1067 PHE A CE1  1 
ATOM   6877  C CE2  . PHE A 1 1067 ? 119.681 76.386  77.438  1.00 24.03 ?  1067 PHE A CE2  1 
ATOM   6878  C CZ   . PHE A 1 1067 ? 119.976 77.578  76.807  1.00 23.76 ?  1067 PHE A CZ   1 
ATOM   6879  N N    . ILE A 1 1068 ? 116.571 80.016  79.714  1.00 18.18 ?  1068 ILE A N    1 
ATOM   6880  C CA   . ILE A 1 1068 ? 115.408 80.240  78.866  1.00 24.07 ?  1068 ILE A CA   1 
ATOM   6881  C C    . ILE A 1 1068 ? 115.856 80.087  77.419  1.00 21.40 ?  1068 ILE A C    1 
ATOM   6882  O O    . ILE A 1 1068 ? 116.828 80.725  76.998  1.00 21.58 ?  1068 ILE A O    1 
ATOM   6883  C CB   . ILE A 1 1068 ? 114.788 81.629  79.104  1.00 23.24 ?  1068 ILE A CB   1 
ATOM   6884  C CG1  . ILE A 1 1068 ? 114.241 81.736  80.528  1.00 22.19 ?  1068 ILE A CG1  1 
ATOM   6885  C CG2  . ILE A 1 1068 ? 113.693 81.911  78.086  1.00 22.39 ?  1068 ILE A CG2  1 
ATOM   6886  C CD1  . ILE A 1 1068 ? 114.970 82.745  81.385  1.00 19.13 ?  1068 ILE A CD1  1 
ATOM   6887  N N    . THR A 1 1069 ? 115.158 79.239  76.668  1.00 23.77 ?  1069 THR A N    1 
ATOM   6888  C CA   . THR A 1 1069 ? 115.523 78.995  75.279  1.00 25.53 ?  1069 THR A CA   1 
ATOM   6889  C C    . THR A 1 1069 ? 115.263 80.232  74.424  1.00 27.26 ?  1069 THR A C    1 
ATOM   6890  O O    . THR A 1 1069 ? 114.363 81.030  74.698  1.00 26.77 ?  1069 THR A O    1 
ATOM   6891  C CB   . THR A 1 1069 ? 114.746 77.803  74.720  1.00 25.98 ?  1069 THR A CB   1 
ATOM   6892  O OG1  . THR A 1 1069 ? 113.344 77.991  74.950  1.00 22.86 ?  1069 THR A OG1  1 
ATOM   6893  C CG2  . THR A 1 1069 ? 115.197 76.513  75.390  1.00 24.96 ?  1069 THR A CG2  1 
ATOM   6894  N N    . ALA A 1 1070 ? 116.080 80.387  73.378  1.00 25.63 ?  1070 ALA A N    1 
ATOM   6895  C CA   . ALA A 1 1070 ? 115.962 81.551  72.505  1.00 21.71 ?  1070 ALA A CA   1 
ATOM   6896  C C    . ALA A 1 1070 ? 114.666 81.535  71.705  1.00 20.19 ?  1070 ALA A C    1 
ATOM   6897  O O    . ALA A 1 1070 ? 114.114 82.600  71.407  1.00 18.92 ?  1070 ALA A O    1 
ATOM   6898  C CB   . ALA A 1 1070 ? 117.164 81.627  71.564  1.00 18.70 ?  1070 ALA A CB   1 
ATOM   6899  N N    . GLU A 1 1071 ? 114.177 80.348  71.338  1.00 20.15 ?  1071 GLU A N    1 
ATOM   6900  C CA   . GLU A 1 1071 ? 112.913 80.257  70.613  1.00 21.17 ?  1071 GLU A CA   1 
ATOM   6901  C C    . GLU A 1 1071 ? 111.748 80.732  71.473  1.00 19.47 ?  1071 GLU A C    1 
ATOM   6902  O O    . GLU A 1 1071 ? 110.846 81.422  70.982  1.00 19.49 ?  1071 GLU A O    1 
ATOM   6903  C CB   . GLU A 1 1071 ? 112.684 78.822  70.138  1.00 20.60 ?  1071 GLU A CB   1 
ATOM   6904  C CG   . GLU A 1 1071 ? 113.230 78.529  68.748  1.00 19.09 ?  1071 GLU A CG   1 
ATOM   6905  C CD   . GLU A 1 1071 ? 114.717 78.811  68.630  1.00 18.99 ?  1071 GLU A CD   1 
ATOM   6906  O OE1  . GLU A 1 1071 ? 115.483 78.342  69.497  1.00 16.67 ?  1071 GLU A OE1  1 
ATOM   6907  O OE2  . GLU A 1 1071 ? 115.118 79.502  67.670  1.00 21.62 ?  1071 GLU A OE2  1 
ATOM   6908  N N    . ASP A 1 1072 ? 111.755 80.378  72.760  1.00 20.00 ?  1072 ASP A N    1 
ATOM   6909  C CA   . ASP A 1 1072 ? 110.728 80.872  73.672  1.00 25.32 ?  1072 ASP A CA   1 
ATOM   6910  C C    . ASP A 1 1072 ? 110.834 82.381  73.854  1.00 23.57 ?  1072 ASP A C    1 
ATOM   6911  O O    . ASP A 1 1072 ? 109.815 83.068  73.993  1.00 20.84 ?  1072 ASP A O    1 
ATOM   6912  C CB   . ASP A 1 1072 ? 110.835 80.154  75.016  1.00 26.39 ?  1072 ASP A CB   1 
ATOM   6913  C CG   . ASP A 1 1072 ? 110.248 78.757  74.976  1.00 30.61 ?  1072 ASP A CG   1 
ATOM   6914  O OD1  . ASP A 1 1072 ? 109.508 78.450  74.018  1.00 31.23 ?  1072 ASP A OD1  1 
ATOM   6915  O OD2  . ASP A 1 1072 ? 110.536 77.963  75.895  1.00 28.48 ?  1072 ASP A OD2  1 
ATOM   6916  N N    . MET A 1 1073 ? 112.059 82.914  73.850  1.00 22.26 ?  1073 MET A N    1 
ATOM   6917  C CA   . MET A 1 1073 ? 112.240 84.361  73.919  1.00 24.38 ?  1073 MET A CA   1 
ATOM   6918  C C    . MET A 1 1073 ? 111.677 85.048  72.681  1.00 25.70 ?  1073 MET A C    1 
ATOM   6919  O O    . MET A 1 1073 ? 111.050 86.108  72.782  1.00 22.29 ?  1073 MET A O    1 
ATOM   6920  C CB   . MET A 1 1073 ? 113.720 84.698  74.097  1.00 24.61 ?  1073 MET A CB   1 
ATOM   6921  C CG   . MET A 1 1073 ? 113.979 85.862  75.038  1.00 24.92 ?  1073 MET A CG   1 
ATOM   6922  S SD   . MET A 1 1073 ? 113.555 85.477  76.747  1.00 30.74 ?  1073 MET A SD   1 
ATOM   6923  C CE   . MET A 1 1073 ? 112.303 86.716  77.071  1.00 22.87 ?  1073 MET A CE   1 
ATOM   6924  N N    . ASN A 1 1074 ? 111.890 84.458  71.501  1.00 27.98 ?  1074 ASN A N    1 
ATOM   6925  C CA   . ASN A 1 1074 ? 111.312 85.008  70.277  1.00 27.01 ?  1074 ASN A CA   1 
ATOM   6926  C C    . ASN A 1 1074 ? 109.790 84.939  70.304  1.00 26.47 ?  1074 ASN A C    1 
ATOM   6927  O O    . ASN A 1 1074 ? 109.111 85.867  69.845  1.00 23.53 ?  1074 ASN A O    1 
ATOM   6928  C CB   . ASN A 1 1074 ? 111.859 84.266  69.058  1.00 24.49 ?  1074 ASN A CB   1 
ATOM   6929  C CG   . ASN A 1 1074 ? 113.367 84.358  68.948  1.00 25.91 ?  1074 ASN A CG   1 
ATOM   6930  O OD1  . ASN A 1 1074 ? 114.015 85.066  69.718  1.00 21.30 ?  1074 ASN A OD1  1 
ATOM   6931  N ND2  . ASN A 1 1074 ? 113.934 83.639  67.986  1.00 22.59 ?  1074 ASN A ND2  1 
ATOM   6932  N N    . ILE A 1 1075 ? 109.240 83.843  70.834  1.00 28.05 ?  1075 ILE A N    1 
ATOM   6933  C CA   . ILE A 1 1075 ? 107.790 83.708  70.957  1.00 27.18 ?  1075 ILE A CA   1 
ATOM   6934  C C    . ILE A 1 1075 ? 107.232 84.779  71.888  1.00 24.54 ?  1075 ILE A C    1 
ATOM   6935  O O    . ILE A 1 1075 ? 106.208 85.408  71.594  1.00 23.78 ?  1075 ILE A O    1 
ATOM   6936  C CB   . ILE A 1 1075 ? 107.431 82.287  71.433  1.00 27.09 ?  1075 ILE A CB   1 
ATOM   6937  C CG1  . ILE A 1 1075 ? 107.582 81.288  70.285  1.00 23.84 ?  1075 ILE A CG1  1 
ATOM   6938  C CG2  . ILE A 1 1075 ? 106.015 82.234  71.992  1.00 25.49 ?  1075 ILE A CG2  1 
ATOM   6939  C CD1  . ILE A 1 1075 ? 107.827 79.868  70.741  1.00 23.35 ?  1075 ILE A CD1  1 
ATOM   6940  N N    . ALA A 1 1076 ? 107.908 85.016  73.016  1.00 24.09 ?  1076 ALA A N    1 
ATOM   6941  C CA   . ALA A 1 1076 ? 107.474 86.056  73.944  1.00 28.59 ?  1076 ALA A CA   1 
ATOM   6942  C C    . ALA A 1 1076 ? 107.614 87.450  73.342  1.00 26.92 ?  1076 ALA A C    1 
ATOM   6943  O O    . ALA A 1 1076 ? 106.802 88.334  73.639  1.00 22.38 ?  1076 ALA A O    1 
ATOM   6944  C CB   . ALA A 1 1076 ? 108.264 85.959  75.248  1.00 23.96 ?  1076 ALA A CB   1 
ATOM   6945  N N    . ILE A 1 1077 ? 108.640 87.669  72.516  1.00 25.42 ?  1077 ILE A N    1 
ATOM   6946  C CA   . ILE A 1 1077 ? 108.797 88.952  71.834  1.00 27.94 ?  1077 ILE A CA   1 
ATOM   6947  C C    . ILE A 1 1077 ? 107.646 89.177  70.861  1.00 31.16 ?  1077 ILE A C    1 
ATOM   6948  O O    . ILE A 1 1077 ? 107.041 90.255  70.821  1.00 30.76 ?  1077 ILE A O    1 
ATOM   6949  C CB   . ILE A 1 1077 ? 110.161 89.014  71.121  1.00 27.10 ?  1077 ILE A CB   1 
ATOM   6950  C CG1  . ILE A 1 1077 ? 111.276 89.326  72.120  1.00 27.88 ?  1077 ILE A CG1  1 
ATOM   6951  C CG2  . ILE A 1 1077 ? 110.153 90.052  70.006  1.00 24.72 ?  1077 ILE A CG2  1 
ATOM   6952  C CD1  . ILE A 1 1077 ? 112.662 89.015  71.602  1.00 27.09 ?  1077 ILE A CD1  1 
ATOM   6953  N N    . ASP A 1 1078 ? 107.310 88.151  70.078  1.00 27.59 ?  1078 ASP A N    1 
ATOM   6954  C CA   . ASP A 1 1078 ? 106.250 88.269  69.085  1.00 26.97 ?  1078 ASP A CA   1 
ATOM   6955  C C    . ASP A 1 1078 ? 104.852 88.172  69.683  1.00 29.13 ?  1078 ASP A C    1 
ATOM   6956  O O    . ASP A 1 1078 ? 103.875 88.426  68.970  1.00 30.77 ?  1078 ASP A O    1 
ATOM   6957  C CB   . ASP A 1 1078 ? 106.422 87.197  68.006  1.00 25.99 ?  1078 ASP A CB   1 
ATOM   6958  C CG   . ASP A 1 1078 ? 107.686 87.391  67.191  1.00 29.36 ?  1078 ASP A CG   1 
ATOM   6959  O OD1  . ASP A 1 1078 ? 108.312 88.465  67.311  1.00 27.28 ?  1078 ASP A OD1  1 
ATOM   6960  O OD2  . ASP A 1 1078 ? 108.053 86.471  66.430  1.00 30.93 ?  1078 ASP A OD2  1 
ATOM   6961  N N    . THR A 1 1079 ? 104.729 87.812  70.960  1.00 22.66 ?  1079 THR A N    1 
ATOM   6962  C CA   . THR A 1 1079 ? 103.425 87.701  71.603  1.00 22.91 ?  1079 THR A CA   1 
ATOM   6963  C C    . THR A 1 1079 ? 102.971 89.022  72.218  1.00 24.58 ?  1079 THR A C    1 
ATOM   6964  O O    . THR A 1 1079 ? 101.861 89.487  71.944  1.00 24.60 ?  1079 THR A O    1 
ATOM   6965  C CB   . THR A 1 1079 ? 103.459 86.609  72.678  1.00 20.98 ?  1079 THR A CB   1 
ATOM   6966  O OG1  . THR A 1 1079 ? 103.937 85.386  72.105  1.00 19.67 ?  1079 THR A OG1  1 
ATOM   6967  C CG2  . THR A 1 1079 ? 102.070 86.385  73.254  1.00 21.99 ?  1079 THR A CG2  1 
ATOM   6968  N N    . PHE A 1 1080 ? 103.813 89.634  73.047  1.00 25.36 ?  1080 PHE A N    1 
ATOM   6969  C CA   . PHE A 1 1080 ? 103.444 90.865  73.731  1.00 25.80 ?  1080 PHE A CA   1 
ATOM   6970  C C    . PHE A 1 1080 ? 103.669 92.062  72.815  1.00 26.39 ?  1080 PHE A C    1 
ATOM   6971  O O    . PHE A 1 1080 ? 104.766 92.247  72.278  1.00 26.94 ?  1080 PHE A O    1 
ATOM   6972  C CB   . PHE A 1 1080 ? 104.251 91.021  75.020  1.00 24.78 ?  1080 PHE A CB   1 
ATOM   6973  C CG   . PHE A 1 1080 ? 103.806 90.109  76.129  1.00 24.29 ?  1080 PHE A CG   1 
ATOM   6974  C CD1  . PHE A 1 1080 ? 104.154 88.767  76.126  1.00 25.14 ?  1080 PHE A CD1  1 
ATOM   6975  C CD2  . PHE A 1 1080 ? 103.037 90.593  77.175  1.00 23.28 ?  1080 PHE A CD2  1 
ATOM   6976  C CE1  . PHE A 1 1080 ? 103.745 87.926  77.143  1.00 25.34 ?  1080 PHE A CE1  1 
ATOM   6977  C CE2  . PHE A 1 1080 ? 102.625 89.756  78.197  1.00 23.26 ?  1080 PHE A CE2  1 
ATOM   6978  C CZ   . PHE A 1 1080 ? 102.980 88.422  78.180  1.00 23.60 ?  1080 PHE A CZ   1 
ATOM   6979  N N    . THR A 1 1081 ? 102.624 92.878  72.639  1.00 23.38 ?  1081 THR A N    1 
ATOM   6980  C CA   . THR A 1 1081 ? 102.677 94.025  71.739  1.00 23.90 ?  1081 THR A CA   1 
ATOM   6981  C C    . THR A 1 1081 ? 102.165 95.301  72.400  1.00 24.81 ?  1081 THR A C    1 
ATOM   6982  O O    . THR A 1 1081 ? 101.748 96.229  71.699  1.00 19.97 ?  1081 THR A O    1 
ATOM   6983  C CB   . THR A 1 1081 ? 101.884 93.749  70.459  1.00 24.80 ?  1081 THR A CB   1 
ATOM   6984  O OG1  . THR A 1 1081 ? 100.649 93.101  70.789  1.00 23.22 ?  1081 THR A OG1  1 
ATOM   6985  C CG2  . THR A 1 1081 ? 102.682 92.862  69.514  1.00 24.10 ?  1081 THR A CG2  1 
ATOM   6986  N N    . LEU A 1 1082 ? 102.185 95.370  73.729  1.00 28.55 ?  1082 LEU A N    1 
ATOM   6987  C CA   . LEU A 1 1082 ? 101.745 96.563  74.436  1.00 29.09 ?  1082 LEU A CA   1 
ATOM   6988  C C    . LEU A 1 1082 ? 102.852 97.618  74.409  1.00 27.78 ?  1082 LEU A C    1 
ATOM   6989  O O    . LEU A 1 1082 ? 103.925 97.415  73.834  1.00 25.74 ?  1082 LEU A O    1 
ATOM   6990  C CB   . LEU A 1 1082 ? 101.340 96.206  75.865  1.00 26.07 ?  1082 LEU A CB   1 
ATOM   6991  C CG   . LEU A 1 1082 ? 100.211 97.013  76.513  1.00 25.42 ?  1082 LEU A CG   1 
ATOM   6992  C CD1  . LEU A 1 1082 ? 98.951  96.955  75.663  1.00 23.64 ?  1082 LEU A CD1  1 
ATOM   6993  C CD2  . LEU A 1 1082 ? 99.936  96.517  77.924  1.00 24.54 ?  1082 LEU A CD2  1 
ATOM   6994  N N    . TYR A 1 1083 ? 102.581 98.771  75.024  1.00 24.62 ?  1083 TYR A N    1 
ATOM   6995  C CA   . TYR A 1 1083 ? 103.604 99.811  75.120  1.00 29.44 ?  1083 TYR A CA   1 
ATOM   6996  C C    . TYR A 1 1083 ? 104.838 99.366  75.901  1.00 27.62 ?  1083 TYR A C    1 
ATOM   6997  O O    . TYR A 1 1083 ? 105.956 99.634  75.427  1.00 24.97 ?  1083 TYR A O    1 
ATOM   6998  C CB   . TYR A 1 1083 ? 102.998 101.094 75.708  1.00 28.76 ?  1083 TYR A CB   1 
ATOM   6999  C CG   . TYR A 1 1083 ? 104.025 102.067 76.245  1.00 29.65 ?  1083 TYR A CG   1 
ATOM   7000  C CD1  . TYR A 1 1083 ? 104.798 102.834 75.382  1.00 27.17 ?  1083 TYR A CD1  1 
ATOM   7001  C CD2  . TYR A 1 1083 ? 104.217 102.224 77.612  1.00 26.33 ?  1083 TYR A CD2  1 
ATOM   7002  C CE1  . TYR A 1 1083 ? 105.738 103.726 75.865  1.00 29.23 ?  1083 TYR A CE1  1 
ATOM   7003  C CE2  . TYR A 1 1083 ? 105.154 103.114 78.105  1.00 26.22 ?  1083 TYR A CE2  1 
ATOM   7004  C CZ   . TYR A 1 1083 ? 105.911 103.862 77.227  1.00 29.55 ?  1083 TYR A CZ   1 
ATOM   7005  O OH   . TYR A 1 1083 ? 106.844 104.749 77.712  1.00 31.03 ?  1083 TYR A OH   1 
ATOM   7006  N N    . PRO A 1 1084 ? 104.736 98.699  77.076  1.00 28.37 ?  1084 PRO A N    1 
ATOM   7007  C CA   . PRO A 1 1084 ? 105.980 98.108  77.620  1.00 26.75 ?  1084 PRO A CA   1 
ATOM   7008  C C    . PRO A 1 1084 ? 106.337 96.813  76.895  1.00 23.77 ?  1084 PRO A C    1 
ATOM   7009  O O    . PRO A 1 1084 ? 106.120 95.698  77.367  1.00 22.30 ?  1084 PRO A O    1 
ATOM   7010  C CB   . PRO A 1 1084 ? 105.631 97.872  79.093  1.00 26.29 ?  1084 PRO A CB   1 
ATOM   7011  C CG   . PRO A 1 1084 ? 104.351 98.615  79.343  1.00 27.18 ?  1084 PRO A CG   1 
ATOM   7012  C CD   . PRO A 1 1084 ? 103.633 98.580  78.045  1.00 27.92 ?  1084 PRO A CD   1 
ATOM   7013  N N    . SER A 1 1085 ? 106.890 96.965  75.695  1.00 26.24 ?  1085 SER A N    1 
ATOM   7014  C CA   . SER A 1 1085 ? 107.260 95.815  74.885  1.00 29.01 ?  1085 SER A CA   1 
ATOM   7015  C C    . SER A 1 1085 ? 108.477 95.110  75.472  1.00 23.20 ?  1085 SER A C    1 
ATOM   7016  O O    . SER A 1 1085 ? 109.349 95.733  76.085  1.00 20.54 ?  1085 SER A O    1 
ATOM   7017  C CB   . SER A 1 1085 ? 107.547 96.247  73.447  1.00 25.12 ?  1085 SER A CB   1 
ATOM   7018  O OG   . SER A 1 1085 ? 108.210 95.222  72.727  1.00 22.94 ?  1085 SER A OG   1 
ATOM   7019  N N    . LEU A 1 1086 ? 108.517 93.787  75.293  1.00 18.43 ?  1086 LEU A N    1 
ATOM   7020  C CA   . LEU A 1 1086 ? 109.689 93.020  75.702  1.00 20.68 ?  1086 LEU A CA   1 
ATOM   7021  C C    . LEU A 1 1086 ? 110.920 93.453  74.916  1.00 24.25 ?  1086 LEU A C    1 
ATOM   7022  O O    . LEU A 1 1086 ? 112.006 93.624  75.487  1.00 29.26 ?  1086 LEU A O    1 
ATOM   7023  C CB   . LEU A 1 1086 ? 109.424 91.525  75.510  1.00 24.50 ?  1086 LEU A CB   1 
ATOM   7024  C CG   . LEU A 1 1086 ? 110.204 90.518  76.359  1.00 25.84 ?  1086 LEU A CG   1 
ATOM   7025  C CD1  . LEU A 1 1086 ? 109.361 89.280  76.597  1.00 24.59 ?  1086 LEU A CD1  1 
ATOM   7026  C CD2  . LEU A 1 1086 ? 111.519 90.135  75.701  1.00 24.89 ?  1086 LEU A CD2  1 
ATOM   7027  N N    . GLU A 1 1087 ? 110.760 93.646  73.604  1.00 21.53 ?  1087 GLU A N    1 
ATOM   7028  C CA   . GLU A 1 1087 ? 111.854 94.136  72.773  1.00 21.98 ?  1087 GLU A CA   1 
ATOM   7029  C C    . GLU A 1 1087 ? 112.286 95.531  73.206  1.00 25.21 ?  1087 GLU A C    1 
ATOM   7030  O O    . GLU A 1 1087 ? 113.486 95.811  73.314  1.00 23.76 ?  1087 GLU A O    1 
ATOM   7031  C CB   . GLU A 1 1087 ? 111.422 94.135  71.306  1.00 19.58 ?  1087 GLU A CB   1 
ATOM   7032  C CG   . GLU A 1 1087 ? 112.405 94.776  70.339  1.00 23.15 ?  1087 GLU A CG   1 
ATOM   7033  C CD   . GLU A 1 1087 ? 113.313 93.759  69.675  1.00 27.01 ?  1087 GLU A CD   1 
ATOM   7034  O OE1  . GLU A 1 1087 ? 114.279 94.170  68.998  1.00 27.94 ?  1087 GLU A OE1  1 
ATOM   7035  O OE2  . GLU A 1 1087 ? 113.057 92.546  69.826  1.00 25.13 ?  1087 GLU A OE2  1 
ATOM   7036  N N    . TYR A 1 1088 ? 111.317 96.409  73.483  1.00 25.70 ?  1088 TYR A N    1 
ATOM   7037  C CA   . TYR A 1 1088 ? 111.632 97.768  73.914  1.00 22.83 ?  1088 TYR A CA   1 
ATOM   7038  C C    . TYR A 1 1088 ? 112.341 97.781  75.262  1.00 22.47 ?  1088 TYR A C    1 
ATOM   7039  O O    . TYR A 1 1088 ? 113.313 98.521  75.446  1.00 23.78 ?  1088 TYR A O    1 
ATOM   7040  C CB   . TYR A 1 1088 ? 110.354 98.603  73.974  1.00 20.81 ?  1088 TYR A CB   1 
ATOM   7041  C CG   . TYR A 1 1088 ? 110.536 99.962  74.609  1.00 24.76 ?  1088 TYR A CG   1 
ATOM   7042  C CD1  . TYR A 1 1088 ? 111.305 100.940 73.994  1.00 22.44 ?  1088 TYR A CD1  1 
ATOM   7043  C CD2  . TYR A 1 1088 ? 109.936 100.268 75.824  1.00 26.63 ?  1088 TYR A CD2  1 
ATOM   7044  C CE1  . TYR A 1 1088 ? 111.474 102.184 74.571  1.00 21.19 ?  1088 TYR A CE1  1 
ATOM   7045  C CE2  . TYR A 1 1088 ? 110.098 101.509 76.408  1.00 23.24 ?  1088 TYR A CE2  1 
ATOM   7046  C CZ   . TYR A 1 1088 ? 110.868 102.462 75.777  1.00 25.39 ?  1088 TYR A CZ   1 
ATOM   7047  O OH   . TYR A 1 1088 ? 111.033 103.699 76.355  1.00 30.83 ?  1088 TYR A OH   1 
ATOM   7048  N N    . ARG A 1 1089 ? 111.873 96.969  76.216  1.00 17.89 ?  1089 ARG A N    1 
ATOM   7049  C CA   . ARG A 1 1089 ? 112.507 96.921  77.531  1.00 18.49 ?  1089 ARG A CA   1 
ATOM   7050  C C    . ARG A 1 1089 ? 113.924 96.366  77.449  1.00 17.61 ?  1089 ARG A C    1 
ATOM   7051  O O    . ARG A 1 1089 ? 114.849 96.914  78.066  1.00 19.38 ?  1089 ARG A O    1 
ATOM   7052  C CB   . ARG A 1 1089 ? 111.663 96.081  78.488  1.00 20.23 ?  1089 ARG A CB   1 
ATOM   7053  C CG   . ARG A 1 1089 ? 110.462 96.804  79.068  1.00 19.03 ?  1089 ARG A CG   1 
ATOM   7054  C CD   . ARG A 1 1089 ? 109.539 95.828  79.777  1.00 20.44 ?  1089 ARG A CD   1 
ATOM   7055  N NE   . ARG A 1 1089 ? 108.802 95.000  78.830  1.00 24.59 ?  1089 ARG A NE   1 
ATOM   7056  C CZ   . ARG A 1 1089 ? 107.982 94.017  79.173  1.00 22.95 ?  1089 ARG A CZ   1 
ATOM   7057  N NH1  . ARG A 1 1089 ? 107.778 93.695  80.439  1.00 21.13 ?  1089 ARG A NH1  1 
ATOM   7058  N NH2  . ARG A 1 1089 ? 107.347 93.340  78.219  1.00 18.03 ?  1089 ARG A NH2  1 
ATOM   7059  N N    . LEU A 1 1090 ? 114.112 95.280  76.692  1.00 15.82 ?  1090 LEU A N    1 
ATOM   7060  C CA   . LEU A 1 1090 ? 115.444 94.704  76.533  1.00 20.27 ?  1090 LEU A CA   1 
ATOM   7061  C C    . LEU A 1 1090 ? 116.387 95.686  75.852  1.00 22.16 ?  1090 LEU A C    1 
ATOM   7062  O O    . LEU A 1 1090 ? 117.553 95.828  76.254  1.00 21.96 ?  1090 LEU A O    1 
ATOM   7063  C CB   . LEU A 1 1090 ? 115.358 93.404  75.733  1.00 18.29 ?  1090 LEU A CB   1 
ATOM   7064  C CG   . LEU A 1 1090 ? 115.336 92.081  76.501  1.00 20.93 ?  1090 LEU A CG   1 
ATOM   7065  C CD1  . LEU A 1 1090 ? 114.170 92.043  77.467  1.00 19.60 ?  1090 LEU A CD1  1 
ATOM   7066  C CD2  . LEU A 1 1090 ? 115.272 90.905  75.539  1.00 24.48 ?  1090 LEU A CD2  1 
ATOM   7067  N N    . TRP A 1 1091 ? 115.894 96.384  74.825  1.00 19.60 ?  1091 TRP A N    1 
ATOM   7068  C CA   . TRP A 1 1091 ? 116.722 97.354  74.123  1.00 19.83 ?  1091 TRP A CA   1 
ATOM   7069  C C    . TRP A 1 1091 ? 117.060 98.541  75.012  1.00 19.56 ?  1091 TRP A C    1 
ATOM   7070  O O    . TRP A 1 1091 ? 118.176 99.056  74.951  1.00 20.67 ?  1091 TRP A O    1 
ATOM   7071  C CB   . TRP A 1 1091 ? 116.027 97.807  72.842  1.00 19.03 ?  1091 TRP A CB   1 
ATOM   7072  C CG   . TRP A 1 1091 ? 116.440 97.003  71.651  1.00 19.10 ?  1091 TRP A CG   1 
ATOM   7073  C CD1  . TRP A 1 1091 ? 115.640 96.213  70.881  1.00 19.54 ?  1091 TRP A CD1  1 
ATOM   7074  C CD2  . TRP A 1 1091 ? 117.758 96.900  71.098  1.00 22.60 ?  1091 TRP A CD2  1 
ATOM   7075  N NE1  . TRP A 1 1091 ? 116.376 95.626  69.881  1.00 22.58 ?  1091 TRP A NE1  1 
ATOM   7076  C CE2  . TRP A 1 1091 ? 117.680 96.033  69.992  1.00 25.37 ?  1091 TRP A CE2  1 
ATOM   7077  C CE3  . TRP A 1 1091 ? 118.996 97.461  71.428  1.00 19.59 ?  1091 TRP A CE3  1 
ATOM   7078  C CZ2  . TRP A 1 1091 ? 118.790 95.712  69.216  1.00 24.51 ?  1091 TRP A CZ2  1 
ATOM   7079  C CZ3  . TRP A 1 1091 ? 120.096 97.140  70.659  1.00 18.52 ?  1091 TRP A CZ3  1 
ATOM   7080  C CH2  . TRP A 1 1091 ? 119.987 96.276  69.565  1.00 21.65 ?  1091 TRP A CH2  1 
ATOM   7081  N N    . ARG A 1 1092 ? 116.122 98.976  75.857  1.00 14.53 ?  1092 ARG A N    1 
ATOM   7082  C CA   . ARG A 1 1092 ? 116.416 100.056 76.795  1.00 13.32 ?  1092 ARG A CA   1 
ATOM   7083  C C    . ARG A 1 1092 ? 117.481 99.642  77.802  1.00 16.03 ?  1092 ARG A C    1 
ATOM   7084  O O    . ARG A 1 1092 ? 118.388 100.427 78.116  1.00 16.80 ?  1092 ARG A O    1 
ATOM   7085  C CB   . ARG A 1 1092 ? 115.140 100.488 77.518  1.00 14.12 ?  1092 ARG A CB   1 
ATOM   7086  C CG   . ARG A 1 1092 ? 115.368 101.544 78.586  1.00 11.95 ?  1092 ARG A CG   1 
ATOM   7087  C CD   . ARG A 1 1092 ? 114.148 102.424 78.783  1.00 14.27 ?  1092 ARG A CD   1 
ATOM   7088  N NE   . ARG A 1 1092 ? 114.465 103.618 79.556  1.00 14.93 ?  1092 ARG A NE   1 
ATOM   7089  C CZ   . ARG A 1 1092 ? 114.107 103.809 80.818  1.00 16.94 ?  1092 ARG A CZ   1 
ATOM   7090  N NH1  . ARG A 1 1092 ? 113.413 102.901 81.484  1.00 17.65 ?  1092 ARG A NH1  1 
ATOM   7091  N NH2  . ARG A 1 1092 ? 114.452 104.940 81.426  1.00 14.99 ?  1092 ARG A NH2  1 
ATOM   7092  N N    . VAL A 1 1093 ? 117.392 98.410  78.313  1.00 18.53 ?  1093 VAL A N    1 
ATOM   7093  C CA   . VAL A 1 1093 ? 118.370 97.936  79.293  1.00 15.22 ?  1093 VAL A CA   1 
ATOM   7094  C C    . VAL A 1 1093 ? 119.762 97.878  78.672  1.00 15.38 ?  1093 VAL A C    1 
ATOM   7095  O O    . VAL A 1 1093 ? 120.731 98.433  79.215  1.00 17.94 ?  1093 VAL A O    1 
ATOM   7096  C CB   . VAL A 1 1093 ? 117.944 96.567  79.854  1.00 12.38 ?  1093 VAL A CB   1 
ATOM   7097  C CG1  . VAL A 1 1093 ? 119.115 95.883  80.542  1.00 11.26 ?  1093 VAL A CG1  1 
ATOM   7098  C CG2  . VAL A 1 1093 ? 116.775 96.727  80.811  1.00 13.53 ?  1093 VAL A CG2  1 
ATOM   7099  N N    . VAL A 1 1094 ? 119.876 97.235  77.505  1.00 13.84 ?  1094 VAL A N    1 
ATOM   7100  C CA   . VAL A 1 1094 ? 121.190 97.127  76.876  1.00 14.24 ?  1094 VAL A CA   1 
ATOM   7101  C C    . VAL A 1 1094 ? 121.666 98.486  76.375  1.00 16.11 ?  1094 VAL A C    1 
ATOM   7102  O O    . VAL A 1 1094 ? 122.874 98.741  76.315  1.00 17.02 ?  1094 VAL A O    1 
ATOM   7103  C CB   . VAL A 1 1094 ? 121.178 96.070  75.754  1.00 15.51 ?  1094 VAL A CB   1 
ATOM   7104  C CG1  . VAL A 1 1094 ? 120.722 94.726  76.300  1.00 19.07 ?  1094 VAL A CG1  1 
ATOM   7105  C CG2  . VAL A 1 1094 ? 120.301 96.506  74.600  1.00 13.91 ?  1094 VAL A CG2  1 
ATOM   7106  N N    . ALA A 1 1095 ? 120.739 99.399  76.065  1.00 16.46 ?  1095 ALA A N    1 
ATOM   7107  C CA   . ALA A 1 1095 ? 121.114 100.729 75.607  1.00 18.09 ?  1095 ALA A CA   1 
ATOM   7108  C C    . ALA A 1 1095 ? 121.727 101.546 76.729  1.00 11.92 ?  1095 ALA A C    1 
ATOM   7109  O O    . ALA A 1 1095 ? 122.753 102.202 76.531  1.00 14.80 ?  1095 ALA A O    1 
ATOM   7110  C CB   . ALA A 1 1095 ? 119.894 101.445 75.033  1.00 17.95 ?  1095 ALA A CB   1 
ATOM   7111  N N    . ILE A 1 1096 ? 121.113 101.523 77.914  1.00 7.08  ?  1096 ILE A N    1 
ATOM   7112  C CA   . ILE A 1 1096 ? 121.699 102.218 79.057  1.00 6.70  ?  1096 ILE A CA   1 
ATOM   7113  C C    . ILE A 1 1096 ? 123.038 101.590 79.429  1.00 8.72  ?  1096 ILE A C    1 
ATOM   7114  O O    . ILE A 1 1096 ? 124.014 102.299 79.720  1.00 14.00 ?  1096 ILE A O    1 
ATOM   7115  C CB   . ILE A 1 1096 ? 120.717 102.227 80.242  1.00 7.01  ?  1096 ILE A CB   1 
ATOM   7116  C CG1  . ILE A 1 1096 ? 119.453 103.003 79.870  1.00 6.96  ?  1096 ILE A CG1  1 
ATOM   7117  C CG2  . ILE A 1 1096 ? 121.365 102.831 81.477  1.00 8.72  ?  1096 ILE A CG2  1 
ATOM   7118  C CD1  . ILE A 1 1096 ? 118.495 103.199 81.021  1.00 8.58  ?  1096 ILE A CD1  1 
ATOM   7119  N N    . ARG A 1 1097 ? 123.117 100.252 79.383  1.00 10.79 ?  1097 ARG A N    1 
ATOM   7120  C CA   . ARG A 1 1097 ? 124.365 99.571  79.722  1.00 13.40 ?  1097 ARG A CA   1 
ATOM   7121  C C    . ARG A 1 1097 ? 125.493 99.939  78.761  1.00 15.76 ?  1097 ARG A C    1 
ATOM   7122  O O    . ARG A 1 1097 ? 126.638 100.136 79.186  1.00 15.78 ?  1097 ARG A O    1 
ATOM   7123  C CB   . ARG A 1 1097 ? 124.146 98.057  79.741  1.00 13.00 ?  1097 ARG A CB   1 
ATOM   7124  C CG   . ARG A 1 1097 ? 125.412 97.245  79.972  1.00 11.97 ?  1097 ARG A CG   1 
ATOM   7125  C CD   . ARG A 1 1097 ? 125.104 95.765  80.133  1.00 15.13 ?  1097 ARG A CD   1 
ATOM   7126  N NE   . ARG A 1 1097 ? 124.012 95.537  81.071  1.00 14.51 ?  1097 ARG A NE   1 
ATOM   7127  C CZ   . ARG A 1 1097 ? 123.067 94.620  80.914  1.00 14.69 ?  1097 ARG A CZ   1 
ATOM   7128  N NH1  . ARG A 1 1097 ? 123.048 93.821  79.861  1.00 12.76 ?  1097 ARG A NH1  1 
ATOM   7129  N NH2  . ARG A 1 1097 ? 122.119 94.501  81.839  1.00 15.32 ?  1097 ARG A NH2  1 
ATOM   7130  N N    . ILE A 1 1098 ? 125.193 100.050 77.466  1.00 16.09 ?  1098 ILE A N    1 
ATOM   7131  C CA   . ILE A 1 1098 ? 126.226 100.381 76.489  1.00 14.33 ?  1098 ILE A CA   1 
ATOM   7132  C C    . ILE A 1 1098 ? 126.469 101.886 76.375  1.00 13.01 ?  1098 ILE A C    1 
ATOM   7133  O O    . ILE A 1 1098 ? 127.526 102.298 75.875  1.00 15.20 ?  1098 ILE A O    1 
ATOM   7134  C CB   . ILE A 1 1098 ? 125.864 99.781  75.116  1.00 16.22 ?  1098 ILE A CB   1 
ATOM   7135  C CG1  . ILE A 1 1098 ? 127.101 99.654  74.223  1.00 17.58 ?  1098 ILE A CG1  1 
ATOM   7136  C CG2  . ILE A 1 1098 ? 124.799 100.613 74.418  1.00 14.80 ?  1098 ILE A CG2  1 
ATOM   7137  C CD1  . ILE A 1 1098 ? 126.833 98.952  72.914  1.00 21.87 ?  1098 ILE A CD1  1 
ATOM   7138  N N    . ALA A 1 1099 ? 125.542 102.719 76.851  1.00 11.56 ?  1099 ALA A N    1 
ATOM   7139  C CA   . ALA A 1 1099 ? 125.677 104.163 76.729  1.00 12.33 ?  1099 ALA A CA   1 
ATOM   7140  C C    . ALA A 1 1099 ? 126.301 104.817 77.950  1.00 12.92 ?  1099 ALA A C    1 
ATOM   7141  O O    . ALA A 1 1099 ? 126.813 105.935 77.832  1.00 15.03 ?  1099 ALA A O    1 
ATOM   7142  C CB   . ALA A 1 1099 ? 124.310 104.801 76.466  1.00 12.80 ?  1099 ALA A CB   1 
ATOM   7143  N N    . THR A 1 1100 ? 126.251 104.169 79.115  1.00 15.10 ?  1100 THR A N    1 
ATOM   7144  C CA   . THR A 1 1100 ? 126.935 104.715 80.288  1.00 8.95  ?  1100 THR A CA   1 
ATOM   7145  C C    . THR A 1 1100 ? 128.441 104.903 80.084  1.00 9.26  ?  1100 THR A C    1 
ATOM   7146  O O    . THR A 1 1100 ? 128.946 105.991 80.420  1.00 16.02 ?  1100 THR A O    1 
ATOM   7147  C CB   . THR A 1 1100 ? 126.621 103.844 81.513  1.00 15.13 ?  1100 THR A CB   1 
ATOM   7148  O OG1  . THR A 1 1100 ? 125.291 104.119 81.969  1.00 15.75 ?  1100 THR A OG1  1 
ATOM   7149  C CG2  . THR A 1 1100 ? 127.603 104.109 82.641  1.00 16.10 ?  1100 THR A CG2  1 
ATOM   7150  N N    . PRO A 1 1101 ? 129.212 103.935 79.552  1.00 10.33 ?  1101 PRO A N    1 
ATOM   7151  C CA   . PRO A 1 1101 ? 130.650 104.200 79.359  1.00 12.72 ?  1101 PRO A CA   1 
ATOM   7152  C C    . PRO A 1 1101 ? 130.957 105.318 78.374  1.00 20.29 ?  1101 PRO A C    1 
ATOM   7153  O O    . PRO A 1 1101 ? 131.975 105.998 78.539  1.00 16.84 ?  1101 PRO A O    1 
ATOM   7154  C CB   . PRO A 1 1101 ? 131.194 102.852 78.862  1.00 12.58 ?  1101 PRO A CB   1 
ATOM   7155  C CG   . PRO A 1 1101 ? 130.213 101.854 79.322  1.00 15.95 ?  1101 PRO A CG   1 
ATOM   7156  C CD   . PRO A 1 1101 ? 128.899 102.539 79.188  1.00 12.79 ?  1101 PRO A CD   1 
ATOM   7157  N N    . LEU A 1 1102 ? 130.117 105.536 77.359  1.00 22.78 ?  1102 LEU A N    1 
ATOM   7158  C CA   . LEU A 1 1102 ? 130.395 106.591 76.386  1.00 14.44 ?  1102 LEU A CA   1 
ATOM   7159  C C    . LEU A 1 1102 ? 130.265 107.975 77.013  1.00 14.83 ?  1102 LEU A C    1 
ATOM   7160  O O    . LEU A 1 1102 ? 131.135 108.837 76.828  1.00 22.50 ?  1102 LEU A O    1 
ATOM   7161  C CB   . LEU A 1 1102 ? 129.466 106.450 75.180  1.00 15.48 ?  1102 LEU A CB   1 
ATOM   7162  C CG   . LEU A 1 1102 ? 129.620 105.161 74.370  1.00 17.27 ?  1102 LEU A CG   1 
ATOM   7163  C CD1  . LEU A 1 1102 ? 128.848 105.250 73.064  1.00 20.35 ?  1102 LEU A CD1  1 
ATOM   7164  C CD2  . LEU A 1 1102 ? 131.087 104.857 74.107  1.00 14.04 ?  1102 LEU A CD2  1 
ATOM   7165  N N    . ILE A 1 1103 ? 129.185 108.206 77.763  1.00 12.31 ?  1103 ILE A N    1 
ATOM   7166  C CA   . ILE A 1 1103 ? 129.032 109.470 78.477  1.00 12.87 ?  1103 ILE A CA   1 
ATOM   7167  C C    . ILE A 1 1103 ? 130.086 109.600 79.570  1.00 17.43 ?  1103 ILE A C    1 
ATOM   7168  O O    . ILE A 1 1103 ? 130.526 110.712 79.886  1.00 23.34 ?  1103 ILE A O    1 
ATOM   7169  C CB   . ILE A 1 1103 ? 127.606 109.603 79.043  1.00 10.86 ?  1103 ILE A CB   1 
ATOM   7170  C CG1  . ILE A 1 1103 ? 126.571 109.179 77.999  1.00 12.78 ?  1103 ILE A CG1  1 
ATOM   7171  C CG2  . ILE A 1 1103 ? 127.336 111.027 79.499  1.00 14.56 ?  1103 ILE A CG2  1 
ATOM   7172  C CD1  . ILE A 1 1103 ? 126.488 110.105 76.807  1.00 20.39 ?  1103 ILE A CD1  1 
ATOM   7173  N N    . MET A 1 1104 ? 130.500 108.480 80.171  1.00 18.41 ?  1104 MET A N    1 
ATOM   7174  C CA   . MET A 1 1104 ? 131.574 108.522 81.158  1.00 19.89 ?  1104 MET A CA   1 
ATOM   7175  C C    . MET A 1 1104 ? 132.887 108.973 80.524  1.00 22.81 ?  1104 MET A C    1 
ATOM   7176  O O    . MET A 1 1104 ? 133.630 109.770 81.109  1.00 21.39 ?  1104 MET A O    1 
ATOM   7177  C CB   . MET A 1 1104 ? 131.737 107.142 81.799  1.00 21.64 ?  1104 MET A CB   1 
ATOM   7178  C CG   . MET A 1 1104 ? 132.202 107.122 83.255  1.00 22.36 ?  1104 MET A CG   1 
ATOM   7179  S SD   . MET A 1 1104 ? 131.164 108.081 84.377  1.00 34.29 ?  1104 MET A SD   1 
ATOM   7180  C CE   . MET A 1 1104 ? 132.151 109.556 84.600  1.00 18.97 ?  1104 MET A CE   1 
ATOM   7181  N N    . GLU A 1 1105 ? 133.185 108.471 79.323  1.00 25.20 ?  1105 GLU A N    1 
ATOM   7182  C CA   . GLU A 1 1105 ? 134.437 108.779 78.642  1.00 23.26 ?  1105 GLU A CA   1 
ATOM   7183  C C    . GLU A 1 1105 ? 134.441 110.180 78.042  1.00 23.33 ?  1105 GLU A C    1 
ATOM   7184  O O    . GLU A 1 1105 ? 135.505 110.805 77.958  1.00 26.11 ?  1105 GLU A O    1 
ATOM   7185  C CB   . GLU A 1 1105 ? 134.703 107.730 77.554  1.00 20.31 ?  1105 GLU A CB   1 
ATOM   7186  C CG   . GLU A 1 1105 ? 135.959 107.953 76.716  1.00 20.26 ?  1105 GLU A CG   1 
ATOM   7187  C CD   . GLU A 1 1105 ? 137.238 107.748 77.505  1.00 29.24 ?  1105 GLU A CD   1 
ATOM   7188  O OE1  . GLU A 1 1105 ? 137.220 106.963 78.476  1.00 28.01 ?  1105 GLU A OE1  1 
ATOM   7189  O OE2  . GLU A 1 1105 ? 138.261 108.374 77.157  1.00 31.33 ?  1105 GLU A OE2  1 
ATOM   7190  N N    . GLN A 1 1106 ? 133.275 110.686 77.625  1.00 24.53 ?  1106 GLN A N    1 
ATOM   7191  C CA   . GLN A 1 1106 ? 133.211 112.002 76.990  1.00 23.87 ?  1106 GLN A CA   1 
ATOM   7192  C C    . GLN A 1 1106 ? 133.692 113.099 77.935  1.00 28.19 ?  1106 GLN A C    1 
ATOM   7193  O O    . GLN A 1 1106 ? 134.620 113.849 77.610  1.00 28.30 ?  1106 GLN A O    1 
ATOM   7194  C CB   . GLN A 1 1106 ? 131.784 112.283 76.516  1.00 22.28 ?  1106 GLN A CB   1 
ATOM   7195  C CG   . GLN A 1 1106 ? 131.492 113.748 76.230  1.00 24.21 ?  1106 GLN A CG   1 
ATOM   7196  C CD   . GLN A 1 1106 ? 130.006 114.054 76.204  1.00 27.95 ?  1106 GLN A CD   1 
ATOM   7197  O OE1  . GLN A 1 1106 ? 129.182 113.218 76.573  1.00 30.13 ?  1106 GLN A OE1  1 
ATOM   7198  N NE2  . GLN A 1 1106 ? 129.657 115.257 75.763  1.00 26.67 ?  1106 GLN A NE2  1 
ATOM   7199  N N    . MET A 1 1107 ? 133.086 113.181 79.124  1.00 28.07 ?  1107 MET A N    1 
ATOM   7200  C CA   . MET A 1 1107 ? 133.490 114.102 80.193  1.00 24.75 ?  1107 MET A CA   1 
ATOM   7201  C C    . MET A 1 1107 ? 133.568 115.552 79.706  1.00 30.02 ?  1107 MET A C    1 
ATOM   7202  O O    . MET A 1 1107 ? 134.589 116.230 79.849  1.00 31.22 ?  1107 MET A O    1 
ATOM   7203  C CB   . MET A 1 1107 ? 134.815 113.658 80.820  1.00 24.59 ?  1107 MET A CB   1 
ATOM   7204  C CG   . MET A 1 1107 ? 135.016 114.120 82.258  1.00 27.35 ?  1107 MET A CG   1 
ATOM   7205  S SD   . MET A 1 1107 ? 133.726 113.548 83.378  1.00 38.37 ?  1107 MET A SD   1 
ATOM   7206  C CE   . MET A 1 1107 ? 134.632 112.380 84.391  1.00 24.70 ?  1107 MET A CE   1 
ATOM   7207  N N    . ALA A 1 1108 ? 132.472 116.023 79.104  1.00 27.51 ?  1108 ALA A N    1 
ATOM   7208  C CA   . ALA A 1 1108 ? 132.406 117.420 78.684  1.00 30.58 ?  1108 ALA A CA   1 
ATOM   7209  C C    . ALA A 1 1108 ? 132.453 118.358 79.884  1.00 32.06 ?  1108 ALA A C    1 
ATOM   7210  O O    . ALA A 1 1108 ? 133.139 119.386 79.851  1.00 30.24 ?  1108 ALA A O    1 
ATOM   7211  C CB   . ALA A 1 1108 ? 131.145 117.666 77.857  1.00 29.54 ?  1108 ALA A CB   1 
ATOM   7212  N N    . PHE A 1 1109 ? 131.734 118.020 80.951  1.00 34.62 ?  1109 PHE A N    1 
ATOM   7213  C CA   . PHE A 1 1109 ? 131.766 118.764 82.201  1.00 30.32 ?  1109 PHE A CA   1 
ATOM   7214  C C    . PHE A 1 1109 ? 132.337 117.869 83.289  1.00 31.36 ?  1109 PHE A C    1 
ATOM   7215  O O    . PHE A 1 1109 ? 131.851 116.752 83.496  1.00 35.90 ?  1109 PHE A O    1 
ATOM   7216  C CB   . PHE A 1 1109 ? 130.369 119.253 82.593  1.00 29.51 ?  1109 PHE A CB   1 
ATOM   7217  C CG   . PHE A 1 1109 ? 129.645 119.971 81.490  1.00 33.90 ?  1109 PHE A CG   1 
ATOM   7218  C CD1  . PHE A 1 1109 ? 129.934 121.294 81.200  1.00 32.97 ?  1109 PHE A CD1  1 
ATOM   7219  C CD2  . PHE A 1 1109 ? 128.674 119.323 80.744  1.00 31.59 ?  1109 PHE A CD2  1 
ATOM   7220  C CE1  . PHE A 1 1109 ? 129.268 121.958 80.187  1.00 30.22 ?  1109 PHE A CE1  1 
ATOM   7221  C CE2  . PHE A 1 1109 ? 128.005 119.981 79.728  1.00 31.93 ?  1109 PHE A CE2  1 
ATOM   7222  C CZ   . PHE A 1 1109 ? 128.303 121.300 79.450  1.00 30.32 ?  1109 PHE A CZ   1 
ATOM   7223  N N    . GLN A 1 1110 ? 133.367 118.354 83.977  1.00 28.04 ?  1110 GLN A N    1 
ATOM   7224  C CA   . GLN A 1 1110 ? 133.973 117.581 85.048  1.00 27.54 ?  1110 GLN A CA   1 
ATOM   7225  C C    . GLN A 1 1110 ? 133.045 117.525 86.260  1.00 26.64 ?  1110 GLN A C    1 
ATOM   7226  O O    . GLN A 1 1110 ? 132.063 118.265 86.370  1.00 24.75 ?  1110 GLN A O    1 
ATOM   7227  C CB   . GLN A 1 1110 ? 135.331 118.164 85.436  1.00 25.34 ?  1110 GLN A CB   1 
ATOM   7228  C CG   . GLN A 1 1110 ? 136.404 117.986 84.376  1.00 27.27 ?  1110 GLN A CG   1 
ATOM   7229  C CD   . GLN A 1 1110 ? 136.952 116.570 84.330  1.00 28.15 ?  1110 GLN A CD   1 
ATOM   7230  O OE1  . GLN A 1 1110 ? 137.431 116.112 83.294  1.00 26.20 ?  1110 GLN A OE1  1 
ATOM   7231  N NE2  . GLN A 1 1110 ? 136.886 115.872 85.459  1.00 28.00 ?  1110 GLN A NE2  1 
ATOM   7232  N N    . GLY A 1 1111 ? 133.375 116.626 87.183  1.00 19.25 ?  1111 GLY A N    1 
ATOM   7233  C CA   . GLY A 1 1111 ? 132.493 116.329 88.289  1.00 20.44 ?  1111 GLY A CA   1 
ATOM   7234  C C    . GLY A 1 1111 ? 131.419 115.314 87.980  1.00 26.81 ?  1111 GLY A C    1 
ATOM   7235  O O    . GLY A 1 1111 ? 130.531 115.102 88.813  1.00 30.48 ?  1111 GLY A O    1 
ATOM   7236  N N    . TRP A 1 1112 ? 131.461 114.685 86.809  1.00 23.93 ?  1112 TRP A N    1 
ATOM   7237  C CA   . TRP A 1 1112 ? 130.440 113.713 86.437  1.00 21.50 ?  1112 TRP A CA   1 
ATOM   7238  C C    . TRP A 1 1112 ? 130.701 112.407 87.176  1.00 24.09 ?  1112 TRP A C    1 
ATOM   7239  O O    . TRP A 1 1112 ? 131.717 111.744 86.941  1.00 27.41 ?  1112 TRP A O    1 
ATOM   7240  C CB   . TRP A 1 1112 ? 130.441 113.488 84.928  1.00 21.65 ?  1112 TRP A CB   1 
ATOM   7241  C CG   . TRP A 1 1112 ? 129.390 114.260 84.184  1.00 24.80 ?  1112 TRP A CG   1 
ATOM   7242  C CD1  . TRP A 1 1112 ? 128.252 114.808 84.698  1.00 24.65 ?  1112 TRP A CD1  1 
ATOM   7243  C CD2  . TRP A 1 1112 ? 129.362 114.527 82.776  1.00 24.99 ?  1112 TRP A CD2  1 
ATOM   7244  N NE1  . TRP A 1 1112 ? 127.533 115.427 83.703  1.00 27.61 ?  1112 TRP A NE1  1 
ATOM   7245  C CE2  . TRP A 1 1112 ? 128.190 115.262 82.512  1.00 25.59 ?  1112 TRP A CE2  1 
ATOM   7246  C CE3  . TRP A 1 1112 ? 130.220 114.222 81.716  1.00 22.98 ?  1112 TRP A CE3  1 
ATOM   7247  C CZ2  . TRP A 1 1112 ? 127.855 115.698 81.229  1.00 25.40 ?  1112 TRP A CZ2  1 
ATOM   7248  C CZ3  . TRP A 1 1112 ? 129.886 114.653 80.446  1.00 24.81 ?  1112 TRP A CZ3  1 
ATOM   7249  C CH2  . TRP A 1 1112 ? 128.716 115.384 80.212  1.00 25.27 ?  1112 TRP A CH2  1 
ATOM   7250  N N    . THR A 1 1113 ? 129.804 112.039 88.084  1.00 24.06 ?  1113 THR A N    1 
ATOM   7251  C CA   . THR A 1 1113 ? 129.902 110.738 88.721  1.00 20.57 ?  1113 THR A CA   1 
ATOM   7252  C C    . THR A 1 1113 ? 129.179 109.690 87.882  1.00 17.50 ?  1113 THR A C    1 
ATOM   7253  O O    . THR A 1 1113 ? 128.372 110.008 87.006  1.00 17.46 ?  1113 THR A O    1 
ATOM   7254  C CB   . THR A 1 1113 ? 129.317 110.771 90.133  1.00 19.42 ?  1113 THR A CB   1 
ATOM   7255  O OG1  . THR A 1 1113 ? 127.893 110.627 90.068  1.00 21.82 ?  1113 THR A OG1  1 
ATOM   7256  C CG2  . THR A 1 1113 ? 129.655 112.078 90.819  1.00 18.10 ?  1113 THR A CG2  1 
ATOM   7257  N N    . GLN A 1 1114 ? 129.490 108.421 88.155  1.00 18.23 ?  1114 GLN A N    1 
ATOM   7258  C CA   . GLN A 1 1114 ? 128.806 107.331 87.467  1.00 18.27 ?  1114 GLN A CA   1 
ATOM   7259  C C    . GLN A 1 1114 ? 127.328 107.287 87.837  1.00 16.31 ?  1114 GLN A C    1 
ATOM   7260  O O    . GLN A 1 1114 ? 126.473 107.051 86.974  1.00 20.46 ?  1114 GLN A O    1 
ATOM   7261  C CB   . GLN A 1 1114 ? 129.481 106.000 87.792  1.00 21.03 ?  1114 GLN A CB   1 
ATOM   7262  C CG   . GLN A 1 1114 ? 128.771 104.792 87.210  1.00 17.92 ?  1114 GLN A CG   1 
ATOM   7263  C CD   . GLN A 1 1114 ? 129.313 104.396 85.855  1.00 20.25 ?  1114 GLN A CD   1 
ATOM   7264  O OE1  . GLN A 1 1114 ? 129.583 105.246 85.008  1.00 18.42 ?  1114 GLN A OE1  1 
ATOM   7265  N NE2  . GLN A 1 1114 ? 129.464 103.096 85.638  1.00 18.89 ?  1114 GLN A NE2  1 
ATOM   7266  N N    . GLU A 1 1115 ? 127.014 107.521 89.114  1.00 14.84 ?  1115 GLU A N    1 
ATOM   7267  C CA   . GLU A 1 1115 ? 125.624 107.521 89.560  1.00 11.68 ?  1115 GLU A CA   1 
ATOM   7268  C C    . GLU A 1 1115 ? 124.821 108.625 88.885  1.00 10.24 ?  1115 GLU A C    1 
ATOM   7269  O O    . GLU A 1 1115 ? 123.672 108.409 88.483  1.00 16.69 ?  1115 GLU A O    1 
ATOM   7270  C CB   . GLU A 1 1115 ? 125.566 107.674 91.079  1.00 16.59 ?  1115 GLU A CB   1 
ATOM   7271  C CG   . GLU A 1 1115 ? 124.159 107.689 91.654  1.00 20.16 ?  1115 GLU A CG   1 
ATOM   7272  C CD   . GLU A 1 1115 ? 124.092 107.104 93.051  1.00 22.00 ?  1115 GLU A CD   1 
ATOM   7273  O OE1  . GLU A 1 1115 ? 124.389 107.837 94.017  1.00 17.28 ?  1115 GLU A OE1  1 
ATOM   7274  O OE2  . GLU A 1 1115 ? 123.741 105.913 93.185  1.00 19.11 ?  1115 GLU A OE2  1 
ATOM   7275  N N    . LYS A 1 1116 ? 125.410 109.816 88.741  1.00 12.24 ?  1116 LYS A N    1 
ATOM   7276  C CA   . LYS A 1 1116 ? 124.669 110.920 88.140  1.00 15.54 ?  1116 LYS A CA   1 
ATOM   7277  C C    . LYS A 1 1116 ? 124.502 110.708 86.639  1.00 13.98 ?  1116 LYS A C    1 
ATOM   7278  O O    . LYS A 1 1116 ? 123.461 111.053 86.072  1.00 16.00 ?  1116 LYS A O    1 
ATOM   7279  C CB   . LYS A 1 1116 ? 125.362 112.251 88.438  1.00 15.96 ?  1116 LYS A CB   1 
ATOM   7280  C CG   . LYS A 1 1116 ? 124.725 113.449 87.746  1.00 18.51 ?  1116 LYS A CG   1 
ATOM   7281  C CD   . LYS A 1 1116 ? 125.736 114.410 87.161  1.00 19.09 ?  1116 LYS A CD   1 
ATOM   7282  C CE   . LYS A 1 1116 ? 125.035 115.455 86.306  1.00 19.57 ?  1116 LYS A CE   1 
ATOM   7283  N NZ   . LYS A 1 1116 ? 124.637 114.912 84.978  1.00 14.52 ?  1116 LYS A NZ   1 
ATOM   7284  N N    . VAL A 1 1117 ? 125.506 110.114 85.985  1.00 8.68  ?  1117 VAL A N    1 
ATOM   7285  C CA   . VAL A 1 1117 ? 125.373 109.744 84.576  1.00 1.86  ?  1117 VAL A CA   1 
ATOM   7286  C C    . VAL A 1 1117 ? 124.260 108.719 84.393  1.00 7.25  ?  1117 VAL A C    1 
ATOM   7287  O O    . VAL A 1 1117 ? 123.450 108.819 83.463  1.00 14.94 ?  1117 VAL A O    1 
ATOM   7288  C CB   . VAL A 1 1117 ? 126.718 109.226 84.031  1.00 8.71  ?  1117 VAL A CB   1 
ATOM   7289  C CG1  . VAL A 1 1117 ? 126.525 108.510 82.704  1.00 11.28 ?  1117 VAL A CG1  1 
ATOM   7290  C CG2  . VAL A 1 1117 ? 127.696 110.373 83.860  1.00 14.55 ?  1117 VAL A CG2  1 
ATOM   7291  N N    . LYS A 1 1118 ? 124.196 107.721 85.281  1.00 12.29 ?  1118 LYS A N    1 
ATOM   7292  C CA   . LYS A 1 1118 ? 123.145 106.710 85.186  1.00 4.51  ?  1118 LYS A CA   1 
ATOM   7293  C C    . LYS A 1 1118 ? 121.766 107.314 85.424  1.00 4.48  ?  1118 LYS A C    1 
ATOM   7294  O O    . LYS A 1 1118 ? 120.808 106.986 84.715  1.00 7.60  ?  1118 LYS A O    1 
ATOM   7295  C CB   . LYS A 1 1118 ? 123.413 105.578 86.176  1.00 8.19  ?  1118 LYS A CB   1 
ATOM   7296  C CG   . LYS A 1 1118 ? 124.449 104.572 85.698  1.00 11.09 ?  1118 LYS A CG   1 
ATOM   7297  C CD   . LYS A 1 1118 ? 124.440 103.305 86.541  1.00 9.24  ?  1118 LYS A CD   1 
ATOM   7298  C CE   . LYS A 1 1118 ? 124.466 103.618 88.029  1.00 13.07 ?  1118 LYS A CE   1 
ATOM   7299  N NZ   . LYS A 1 1118 ? 125.318 102.661 88.786  1.00 12.76 ?  1118 LYS A NZ   1 
ATOM   7300  N N    . LEU A 1 1119 ? 121.646 108.209 86.407  1.00 11.25 ?  1119 LEU A N    1 
ATOM   7301  C CA   . LEU A 1 1119 ? 120.351 108.827 86.677  1.00 10.14 ?  1119 LEU A CA   1 
ATOM   7302  C C    . LEU A 1 1119 ? 119.954 109.813 85.584  1.00 15.47 ?  1119 LEU A C    1 
ATOM   7303  O O    . LEU A 1 1119 ? 118.760 110.061 85.380  1.00 16.93 ?  1119 LEU A O    1 
ATOM   7304  C CB   . LEU A 1 1119 ? 120.372 109.518 88.038  1.00 8.45  ?  1119 LEU A CB   1 
ATOM   7305  C CG   . LEU A 1 1119 ? 119.845 108.677 89.201  1.00 11.41 ?  1119 LEU A CG   1 
ATOM   7306  C CD1  . LEU A 1 1119 ? 119.982 109.426 90.514  1.00 15.92 ?  1119 LEU A CD1  1 
ATOM   7307  C CD2  . LEU A 1 1119 ? 118.402 108.263 88.963  1.00 13.23 ?  1119 LEU A CD2  1 
ATOM   7308  N N    . HIS A 1 1120 ? 120.931 110.387 84.880  1.00 13.09 ?  1120 HIS A N    1 
ATOM   7309  C CA   . HIS A 1 1120 ? 120.624 111.248 83.744  1.00 9.35  ?  1120 HIS A CA   1 
ATOM   7310  C C    . HIS A 1 1120 ? 120.187 110.427 82.538  1.00 11.49 ?  1120 HIS A C    1 
ATOM   7311  O O    . HIS A 1 1120 ? 119.273 110.825 81.807  1.00 18.41 ?  1120 HIS A O    1 
ATOM   7312  C CB   . HIS A 1 1120 ? 121.841 112.112 83.412  1.00 12.43 ?  1120 HIS A CB   1 
ATOM   7313  C CG   . HIS A 1 1120 ? 121.924 112.528 81.976  1.00 14.84 ?  1120 HIS A CG   1 
ATOM   7314  N ND1  . HIS A 1 1120 ? 122.911 112.076 81.127  1.00 14.14 ?  1120 HIS A ND1  1 
ATOM   7315  C CD2  . HIS A 1 1120 ? 121.157 113.371 81.246  1.00 17.61 ?  1120 HIS A CD2  1 
ATOM   7316  C CE1  . HIS A 1 1120 ? 122.740 112.612 79.932  1.00 15.39 ?  1120 HIS A CE1  1 
ATOM   7317  N NE2  . HIS A 1 1120 ? 121.684 113.403 79.978  1.00 18.53 ?  1120 HIS A NE2  1 
ATOM   7318  N N    . LEU A 1 1121 ? 120.830 109.279 82.313  1.00 9.15  ?  1121 LEU A N    1 
ATOM   7319  C CA   . LEU A 1 1121 ? 120.436 108.393 81.224  1.00 6.38  ?  1121 LEU A CA   1 
ATOM   7320  C C    . LEU A 1 1121 ? 119.109 107.698 81.497  1.00 9.56  ?  1121 LEU A C    1 
ATOM   7321  O O    . LEU A 1 1121 ? 118.437 107.281 80.548  1.00 17.68 ?  1121 LEU A O    1 
ATOM   7322  C CB   . LEU A 1 1121 ? 121.522 107.347 80.978  1.00 6.78  ?  1121 LEU A CB   1 
ATOM   7323  C CG   . LEU A 1 1121 ? 122.657 107.707 80.018  1.00 9.91  ?  1121 LEU A CG   1 
ATOM   7324  C CD1  . LEU A 1 1121 ? 123.680 106.585 79.968  1.00 10.47 ?  1121 LEU A CD1  1 
ATOM   7325  C CD2  . LEU A 1 1121 ? 122.123 108.006 78.631  1.00 11.18 ?  1121 LEU A CD2  1 
ATOM   7326  N N    . GLU A 1 1122 ? 118.731 107.552 82.770  1.00 12.39 ?  1122 GLU A N    1 
ATOM   7327  C CA   . GLU A 1 1122 ? 117.462 106.915 83.108  1.00 11.90 ?  1122 GLU A CA   1 
ATOM   7328  C C    . GLU A 1 1122 ? 116.279 107.731 82.600  1.00 14.78 ?  1122 GLU A C    1 
ATOM   7329  O O    . GLU A 1 1122 ? 115.278 107.169 82.140  1.00 19.12 ?  1122 GLU A O    1 
ATOM   7330  C CB   . GLU A 1 1122 ? 117.372 106.715 84.623  1.00 10.68 ?  1122 GLU A CB   1 
ATOM   7331  C CG   . GLU A 1 1122 ? 116.019 106.242 85.125  1.00 12.11 ?  1122 GLU A CG   1 
ATOM   7332  C CD   . GLU A 1 1122 ? 115.876 104.733 85.083  1.00 21.10 ?  1122 GLU A CD   1 
ATOM   7333  O OE1  . GLU A 1 1122 ? 116.852 104.051 84.706  1.00 25.62 ?  1122 GLU A OE1  1 
ATOM   7334  O OE2  . GLU A 1 1122 ? 114.786 104.229 85.423  1.00 22.99 ?  1122 GLU A OE2  1 
ATOM   7335  N N    . ARG A 1 1123 ? 116.380 109.061 82.670  1.00 20.05 ?  1123 ARG A N    1 
ATOM   7336  C CA   . ARG A 1 1123 ? 115.303 109.931 82.213  1.00 24.59 ?  1123 ARG A CA   1 
ATOM   7337  C C    . ARG A 1 1123 ? 115.084 109.855 80.707  1.00 18.65 ?  1123 ARG A C    1 
ATOM   7338  O O    . ARG A 1 1123 ? 113.974 110.132 80.242  1.00 17.28 ?  1123 ARG A O    1 
ATOM   7339  C CB   . ARG A 1 1123 ? 115.594 111.378 82.611  1.00 21.56 ?  1123 ARG A CB   1 
ATOM   7340  C CG   . ARG A 1 1123 ? 114.926 111.832 83.897  1.00 21.11 ?  1123 ARG A CG   1 
ATOM   7341  C CD   . ARG A 1 1123 ? 114.940 113.351 84.014  1.00 22.92 ?  1123 ARG A CD   1 
ATOM   7342  N NE   . ARG A 1 1123 ? 116.285 113.876 84.228  1.00 22.40 ?  1123 ARG A NE   1 
ATOM   7343  C CZ   . ARG A 1 1123 ? 117.026 114.451 83.290  1.00 22.63 ?  1123 ARG A CZ   1 
ATOM   7344  N NH1  . ARG A 1 1123 ? 116.582 114.600 82.053  1.00 25.31 ?  1123 ARG A NH1  1 
ATOM   7345  N NH2  . ARG A 1 1123 ? 118.243 114.887 83.602  1.00 18.39 ?  1123 ARG A NH2  1 
ATOM   7346  N N    . GLY A 1 1124 ? 116.112 109.499 79.937  1.00 16.28 ?  1124 GLY A N    1 
ATOM   7347  C CA   . GLY A 1 1124 ? 115.965 109.424 78.502  1.00 17.79 ?  1124 GLY A CA   1 
ATOM   7348  C C    . GLY A 1 1124 ? 115.214 108.186 78.049  1.00 21.02 ?  1124 GLY A C    1 
ATOM   7349  O O    . GLY A 1 1124 ? 115.095 107.193 78.765  1.00 23.47 ?  1124 GLY A O    1 
ATOM   7350  N N    . TYR A 1 1125 ? 114.697 108.258 76.824  1.00 26.49 ?  1125 TYR A N    1 
ATOM   7351  C CA   . TYR A 1 1125 ? 113.984 107.150 76.207  1.00 25.12 ?  1125 TYR A CA   1 
ATOM   7352  C C    . TYR A 1 1125 ? 114.254 107.157 74.710  1.00 22.27 ?  1125 TYR A C    1 
ATOM   7353  O O    . TYR A 1 1125 ? 114.650 108.174 74.135  1.00 23.00 ?  1125 TYR A O    1 
ATOM   7354  C CB   . TYR A 1 1125 ? 112.471 107.221 76.462  1.00 20.42 ?  1125 TYR A CB   1 
ATOM   7355  C CG   . TYR A 1 1125 ? 112.069 107.125 77.917  1.00 21.97 ?  1125 TYR A CG   1 
ATOM   7356  C CD1  . TYR A 1 1125 ? 111.885 105.891 78.526  1.00 22.77 ?  1125 TYR A CD1  1 
ATOM   7357  C CD2  . TYR A 1 1125 ? 111.858 108.268 78.677  1.00 25.13 ?  1125 TYR A CD2  1 
ATOM   7358  C CE1  . TYR A 1 1125 ? 111.512 105.797 79.853  1.00 25.63 ?  1125 TYR A CE1  1 
ATOM   7359  C CE2  . TYR A 1 1125 ? 111.484 108.184 80.006  1.00 26.47 ?  1125 TYR A CE2  1 
ATOM   7360  C CZ   . TYR A 1 1125 ? 111.314 106.946 80.588  1.00 29.13 ?  1125 TYR A CZ   1 
ATOM   7361  O OH   . TYR A 1 1125 ? 110.942 106.855 81.910  1.00 29.53 ?  1125 TYR A OH   1 
ATOM   7362  N N    . LEU A 1 1126 ? 114.033 106.007 74.081  1.00 21.12 ?  1126 LEU A N    1 
ATOM   7363  C CA   . LEU A 1 1126 ? 114.193 105.858 72.643  1.00 24.64 ?  1126 LEU A CA   1 
ATOM   7364  C C    . LEU A 1 1126 ? 112.824 105.767 71.983  1.00 28.84 ?  1126 LEU A C    1 
ATOM   7365  O O    . LEU A 1 1126 ? 111.908 105.132 72.515  1.00 26.81 ?  1126 LEU A O    1 
ATOM   7366  C CB   . LEU A 1 1126 ? 115.033 104.622 72.300  1.00 25.84 ?  1126 LEU A CB   1 
ATOM   7367  C CG   . LEU A 1 1126 ? 114.651 103.259 72.883  1.00 25.53 ?  1126 LEU A CG   1 
ATOM   7368  C CD1  . LEU A 1 1126 ? 113.845 102.444 71.879  1.00 23.32 ?  1126 LEU A CD1  1 
ATOM   7369  C CD2  . LEU A 1 1126 ? 115.889 102.494 73.325  1.00 23.45 ?  1126 LEU A CD2  1 
ATOM   7370  N N    . VAL A 1 1127 ? 112.690 106.409 70.825  1.00 27.77 ?  1127 VAL A N    1 
ATOM   7371  C CA   . VAL A 1 1127 ? 111.443 106.443 70.070  1.00 26.78 ?  1127 VAL A CA   1 
ATOM   7372  C C    . VAL A 1 1127 ? 111.676 105.734 68.743  1.00 27.21 ?  1127 VAL A C    1 
ATOM   7373  O O    . VAL A 1 1127 ? 112.683 105.984 68.069  1.00 25.80 ?  1127 VAL A O    1 
ATOM   7374  C CB   . VAL A 1 1127 ? 110.955 107.886 69.852  1.00 24.17 ?  1127 VAL A CB   1 
ATOM   7375  C CG1  . VAL A 1 1127 ? 109.648 107.901 69.072  1.00 25.26 ?  1127 VAL A CG1  1 
ATOM   7376  C CG2  . VAL A 1 1127 ? 110.794 108.599 71.187  1.00 19.90 ?  1127 VAL A CG2  1 
ATOM   7377  N N    . ASP A 1 1128 ? 110.757 104.840 68.382  1.00 28.32 ?  1128 ASP A N    1 
ATOM   7378  C CA   . ASP A 1 1128 ? 110.889 104.074 67.151  1.00 29.79 ?  1128 ASP A CA   1 
ATOM   7379  C C    . ASP A 1 1128 ? 110.816 104.986 65.932  1.00 26.69 ?  1128 ASP A C    1 
ATOM   7380  O O    . ASP A 1 1128 ? 110.056 105.958 65.904  1.00 24.94 ?  1128 ASP A O    1 
ATOM   7381  C CB   . ASP A 1 1128 ? 109.796 103.008 67.070  1.00 29.57 ?  1128 ASP A CB   1 
ATOM   7382  C CG   . ASP A 1 1128 ? 108.406 103.585 67.248  1.00 29.92 ?  1128 ASP A CG   1 
ATOM   7383  O OD1  . ASP A 1 1128 ? 108.282 104.660 67.873  1.00 33.04 ?  1128 ASP A OD1  1 
ATOM   7384  O OD2  . ASP A 1 1128 ? 107.436 102.966 66.762  1.00 25.25 ?  1128 ASP A OD2  1 
ATOM   7385  N N    . LEU A 1 1129 ? 111.621 104.665 64.919  1.00 27.64 ?  1129 LEU A N    1 
ATOM   7386  C CA   . LEU A 1 1129 ? 111.655 105.447 63.691  1.00 27.71 ?  1129 LEU A CA   1 
ATOM   7387  C C    . LEU A 1 1129 ? 110.514 105.110 62.741  1.00 29.32 ?  1129 LEU A C    1 
ATOM   7388  O O    . LEU A 1 1129 ? 110.317 105.834 61.759  1.00 23.67 ?  1129 LEU A O    1 
ATOM   7389  C CB   . LEU A 1 1129 ? 112.994 105.243 62.978  1.00 24.81 ?  1129 LEU A CB   1 
ATOM   7390  C CG   . LEU A 1 1129 ? 114.249 105.655 63.749  1.00 23.93 ?  1129 LEU A CG   1 
ATOM   7391  C CD1  . LEU A 1 1129 ? 115.405 104.724 63.425  1.00 25.60 ?  1129 LEU A CD1  1 
ATOM   7392  C CD2  . LEU A 1 1129 ? 114.617 107.098 63.443  1.00 23.55 ?  1129 LEU A CD2  1 
ATOM   7393  N N    . ALA A 1 1130 ? 109.769 104.032 63.002  1.00 31.23 ?  1130 ALA A N    1 
ATOM   7394  C CA   . ALA A 1 1130 ? 108.643 103.676 62.144  1.00 30.18 ?  1130 ALA A CA   1 
ATOM   7395  C C    . ALA A 1 1130 ? 107.540 104.725 62.209  1.00 29.23 ?  1130 ALA A C    1 
ATOM   7396  O O    . ALA A 1 1130 ? 106.928 105.054 61.185  1.00 25.21 ?  1130 ALA A O    1 
ATOM   7397  C CB   . ALA A 1 1130 ? 108.102 102.301 62.534  1.00 25.12 ?  1130 ALA A CB   1 
ATOM   7398  N N    . GLU A 1 1131 ? 107.267 105.255 63.403  1.00 27.71 ?  1131 GLU A N    1 
ATOM   7399  C CA   . GLU A 1 1131 ? 106.248 106.290 63.541  1.00 26.62 ?  1131 GLU A CA   1 
ATOM   7400  C C    . GLU A 1 1131 ? 106.689 107.594 62.886  1.00 28.04 ?  1131 GLU A C    1 
ATOM   7401  O O    . GLU A 1 1131 ? 105.867 108.312 62.305  1.00 25.70 ?  1131 GLU A O    1 
ATOM   7402  C CB   . GLU A 1 1131 ? 105.925 106.515 65.017  1.00 23.08 ?  1131 GLU A CB   1 
ATOM   7403  C CG   . GLU A 1 1131 ? 104.612 107.239 65.262  1.00 23.24 ?  1131 GLU A CG   1 
ATOM   7404  C CD   . GLU A 1 1131 ? 103.429 106.293 65.328  1.00 25.02 ?  1131 GLU A CD   1 
ATOM   7405  O OE1  . GLU A 1 1131 ? 103.640 105.094 65.604  1.00 25.74 ?  1131 GLU A OE1  1 
ATOM   7406  O OE2  . GLU A 1 1131 ? 102.288 106.750 65.104  1.00 26.27 ?  1131 GLU A OE2  1 
ATOM   7407  N N    . SER A 1 1132 ? 107.980 107.915 62.967  1.00 26.25 ?  1132 SER A N    1 
ATOM   7408  C CA   . SER A 1 1132 ? 108.514 109.157 62.427  1.00 27.57 ?  1132 SER A CA   1 
ATOM   7409  C C    . SER A 1 1132 ? 109.038 109.008 61.003  1.00 26.29 ?  1132 SER A C    1 
ATOM   7410  O O    . SER A 1 1132 ? 109.838 109.842 60.565  1.00 24.45 ?  1132 SER A O    1 
ATOM   7411  C CB   . SER A 1 1132 ? 109.620 109.694 63.339  1.00 25.75 ?  1132 SER A CB   1 
ATOM   7412  O OG   . SER A 1 1132 ? 109.104 110.051 64.609  1.00 26.12 ?  1132 SER A OG   1 
ATOM   7413  N N    . HIS A 1 1133 ? 108.606 107.965 60.284  1.00 26.26 ?  1133 HIS A N    1 
ATOM   7414  C CA   . HIS A 1 1133 ? 108.958 107.739 58.876  1.00 29.84 ?  1133 HIS A CA   1 
ATOM   7415  C C    . HIS A 1 1133 ? 110.469 107.650 58.666  1.00 28.50 ?  1133 HIS A C    1 
ATOM   7416  O O    . HIS A 1 1133 ? 110.998 108.123 57.657  1.00 31.56 ?  1133 HIS A O    1 
ATOM   7417  C CB   . HIS A 1 1133 ? 108.348 108.814 57.972  1.00 31.15 ?  1133 HIS A CB   1 
ATOM   7418  C CG   . HIS A 1 1133 ? 106.876 109.005 58.168  1.00 34.24 ?  1133 HIS A CG   1 
ATOM   7419  N ND1  . HIS A 1 1133 ? 105.933 108.280 57.472  1.00 32.71 ?  1133 HIS A ND1  1 
ATOM   7420  C CD2  . HIS A 1 1133 ? 106.185 109.839 58.981  1.00 32.74 ?  1133 HIS A CD2  1 
ATOM   7421  C CE1  . HIS A 1 1133 ? 104.724 108.659 57.848  1.00 28.42 ?  1133 HIS A CE1  1 
ATOM   7422  N NE2  . HIS A 1 1133 ? 104.849 109.603 58.762  1.00 34.57 ?  1133 HIS A NE2  1 
ATOM   7423  N N    . PHE A 1 1134 ? 111.161 107.032 59.629  1.00 24.33 ?  1134 PHE A N    1 
ATOM   7424  C CA   . PHE A 1 1134 ? 112.605 106.778 59.563  1.00 26.94 ?  1134 PHE A CA   1 
ATOM   7425  C C    . PHE A 1 1134 ? 113.410 108.063 59.368  1.00 25.48 ?  1134 PHE A C    1 
ATOM   7426  O O    . PHE A 1 1134 ? 114.404 108.089 58.640  1.00 22.83 ?  1134 PHE A O    1 
ATOM   7427  C CB   . PHE A 1 1134 ? 112.941 105.758 58.470  1.00 27.83 ?  1134 PHE A CB   1 
ATOM   7428  C CG   . PHE A 1 1134 ? 112.173 104.471 58.582  1.00 29.60 ?  1134 PHE A CG   1 
ATOM   7429  C CD1  . PHE A 1 1134 ? 112.031 103.839 59.806  1.00 27.42 ?  1134 PHE A CD1  1 
ATOM   7430  C CD2  . PHE A 1 1134 ? 111.595 103.894 57.463  1.00 27.51 ?  1134 PHE A CD2  1 
ATOM   7431  C CE1  . PHE A 1 1134 ? 111.326 102.653 59.913  1.00 25.17 ?  1134 PHE A CE1  1 
ATOM   7432  C CE2  . PHE A 1 1134 ? 110.888 102.709 57.563  1.00 26.07 ?  1134 PHE A CE2  1 
ATOM   7433  C CZ   . PHE A 1 1134 ? 110.754 102.088 58.790  1.00 27.37 ?  1134 PHE A CZ   1 
ATOM   7434  N N    . GLN A 1 1135 ? 112.979 109.140 60.021  1.00 23.43 ?  1135 GLN A N    1 
ATOM   7435  C CA   . GLN A 1 1135 ? 113.743 110.379 60.025  1.00 24.14 ?  1135 GLN A CA   1 
ATOM   7436  C C    . GLN A 1 1135 ? 113.548 111.073 61.364  1.00 23.54 ?  1135 GLN A C    1 
ATOM   7437  O O    . GLN A 1 1135 ? 112.429 111.144 61.878  1.00 22.18 ?  1135 GLN A O    1 
ATOM   7438  C CB   . GLN A 1 1135 ? 113.338 111.310 58.874  1.00 20.70 ?  1135 GLN A CB   1 
ATOM   7439  C CG   . GLN A 1 1135 ? 111.856 111.322 58.552  1.00 21.94 ?  1135 GLN A CG   1 
ATOM   7440  C CD   . GLN A 1 1135 ? 111.108 112.412 59.295  1.00 26.88 ?  1135 GLN A CD   1 
ATOM   7441  O OE1  . GLN A 1 1135 ? 111.633 113.504 59.512  1.00 28.27 ?  1135 GLN A OE1  1 
ATOM   7442  N NE2  . GLN A 1 1135 ? 109.874 112.120 59.688  1.00 27.96 ?  1135 GLN A NE2  1 
ATOM   7443  N N    . PHE A 1 1136 ? 114.645 111.579 61.922  1.00 24.32 ?  1136 PHE A N    1 
ATOM   7444  C CA   . PHE A 1 1136 ? 114.643 112.225 63.225  1.00 25.30 ?  1136 PHE A CA   1 
ATOM   7445  C C    . PHE A 1 1136 ? 115.101 113.669 63.087  1.00 27.35 ?  1136 PHE A C    1 
ATOM   7446  O O    . PHE A 1 1136 ? 116.103 113.953 62.421  1.00 27.01 ?  1136 PHE A O    1 
ATOM   7447  C CB   . PHE A 1 1136 ? 115.548 111.477 64.212  1.00 22.14 ?  1136 PHE A CB   1 
ATOM   7448  C CG   . PHE A 1 1136 ? 115.626 112.115 65.571  1.00 23.23 ?  1136 PHE A CG   1 
ATOM   7449  C CD1  . PHE A 1 1136 ? 114.509 112.176 66.388  1.00 26.83 ?  1136 PHE A CD1  1 
ATOM   7450  C CD2  . PHE A 1 1136 ? 116.818 112.650 66.032  1.00 23.01 ?  1136 PHE A CD2  1 
ATOM   7451  C CE1  . PHE A 1 1136 ? 114.577 112.762 67.638  1.00 24.48 ?  1136 PHE A CE1  1 
ATOM   7452  C CE2  . PHE A 1 1136 ? 116.894 113.238 67.281  1.00 26.40 ?  1136 PHE A CE2  1 
ATOM   7453  C CZ   . PHE A 1 1136 ? 115.772 113.293 68.086  1.00 23.61 ?  1136 PHE A CZ   1 
ATOM   7454  N N    . ASN A 1 1137 ? 114.365 114.577 63.720  1.00 27.23 ?  1137 ASN A N    1 
ATOM   7455  C CA   . ASN A 1 1137 ? 114.690 115.997 63.720  1.00 27.83 ?  1137 ASN A CA   1 
ATOM   7456  C C    . ASN A 1 1137 ? 115.337 116.348 65.053  1.00 24.84 ?  1137 ASN A C    1 
ATOM   7457  O O    . ASN A 1 1137 ? 114.748 116.114 66.114  1.00 24.47 ?  1137 ASN A O    1 
ATOM   7458  C CB   . ASN A 1 1137 ? 113.438 116.843 63.486  1.00 27.51 ?  1137 ASN A CB   1 
ATOM   7459  C CG   . ASN A 1 1137 ? 112.235 116.328 64.255  1.00 28.50 ?  1137 ASN A CG   1 
ATOM   7460  O OD1  . ASN A 1 1137 ? 112.167 115.151 64.607  1.00 27.88 ?  1137 ASN A OD1  1 
ATOM   7461  N ND2  . ASN A 1 1137 ? 111.278 117.211 64.516  1.00 25.60 ?  1137 ASN A ND2  1 
ATOM   7462  N N    . ILE A 1 1138 ? 116.543 116.903 65.000  1.00 27.80 ?  1138 ILE A N    1 
ATOM   7463  C CA   . ILE A 1 1138 ? 117.297 117.220 66.206  1.00 28.38 ?  1138 ILE A CA   1 
ATOM   7464  C C    . ILE A 1 1138 ? 116.907 118.610 66.689  1.00 30.54 ?  1138 ILE A C    1 
ATOM   7465  O O    . ILE A 1 1138 ? 116.970 119.590 65.936  1.00 31.53 ?  1138 ILE A O    1 
ATOM   7466  C CB   . ILE A 1 1138 ? 118.814 117.118 65.956  1.00 27.78 ?  1138 ILE A CB   1 
ATOM   7467  C CG1  . ILE A 1 1138 ? 119.602 117.749 67.103  1.00 23.95 ?  1138 ILE A CG1  1 
ATOM   7468  C CG2  . ILE A 1 1138 ? 119.199 117.789 64.663  1.00 28.93 ?  1138 ILE A CG2  1 
ATOM   7469  C CD1  . ILE A 1 1138 ? 121.059 117.338 67.142  1.00 26.89 ?  1138 ILE A CD1  1 
ATOM   7470  N N    . ASP A 1 1139 ? 116.465 118.688 67.937  1.00 27.43 ?  1139 ASP A N    1 
ATOM   7471  C CA   . ASP A 1 1139 ? 116.321 119.950 68.637  1.00 25.33 ?  1139 ASP A CA   1 
ATOM   7472  C C    . ASP A 1 1139 ? 117.537 120.136 69.539  1.00 26.24 ?  1139 ASP A C    1 
ATOM   7473  O O    . ASP A 1 1139 ? 118.397 119.263 69.649  1.00 30.48 ?  1139 ASP A O    1 
ATOM   7474  C CB   . ASP A 1 1139 ? 115.018 119.978 69.440  1.00 24.87 ?  1139 ASP A CB   1 
ATOM   7475  C CG   . ASP A 1 1139 ? 113.811 119.576 68.613  1.00 29.18 ?  1139 ASP A CG   1 
ATOM   7476  O OD1  . ASP A 1 1139 ? 113.969 119.329 67.399  1.00 30.82 ?  1139 ASP A OD1  1 
ATOM   7477  O OD2  . ASP A 1 1139 ? 112.701 119.503 69.180  1.00 29.80 ?  1139 ASP A OD2  1 
ATOM   7478  N N    . ALA A 1 1140 ? 117.622 121.289 70.186  1.00 22.48 ?  1140 ALA A N    1 
ATOM   7479  C CA   . ALA A 1 1140 ? 118.633 121.474 71.214  1.00 22.34 ?  1140 ALA A CA   1 
ATOM   7480  C C    . ALA A 1 1140 ? 118.102 121.155 72.603  1.00 24.95 ?  1140 ALA A C    1 
ATOM   7481  O O    . ALA A 1 1140 ? 118.812 121.369 73.591  1.00 25.38 ?  1140 ALA A O    1 
ATOM   7482  C CB   . ALA A 1 1140 ? 119.189 122.897 71.170  1.00 18.09 ?  1140 ALA A CB   1 
ATOM   7483  N N    . THR A 1 1141 ? 116.868 120.651 72.695  1.00 26.16 ?  1141 THR A N    1 
ATOM   7484  C CA   . THR A 1 1141 ? 116.336 120.169 73.963  1.00 27.53 ?  1141 THR A CA   1 
ATOM   7485  C C    . THR A 1 1141 ? 117.030 118.898 74.432  1.00 23.41 ?  1141 THR A C    1 
ATOM   7486  O O    . THR A 1 1141 ? 116.894 118.526 75.602  1.00 21.22 ?  1141 THR A O    1 
ATOM   7487  C CB   . THR A 1 1141 ? 114.830 119.922 73.847  1.00 26.27 ?  1141 THR A CB   1 
ATOM   7488  O OG1  . THR A 1 1141 ? 114.585 118.894 72.879  1.00 24.46 ?  1141 THR A OG1  1 
ATOM   7489  C CG2  . THR A 1 1141 ? 114.112 121.195 73.424  1.00 22.73 ?  1141 THR A CG2  1 
ATOM   7490  N N    . LEU A 1 1142 ? 117.757 118.220 73.549  1.00 20.30 ?  1142 LEU A N    1 
ATOM   7491  C CA   . LEU A 1 1142 ? 118.532 117.055 73.942  1.00 24.49 ?  1142 LEU A CA   1 
ATOM   7492  C C    . LEU A 1 1142 ? 119.855 117.468 74.573  1.00 25.33 ?  1142 LEU A C    1 
ATOM   7493  O O    . LEU A 1 1142 ? 120.496 118.433 74.147  1.00 20.95 ?  1142 LEU A O    1 
ATOM   7494  C CB   . LEU A 1 1142 ? 118.778 116.145 72.737  1.00 23.42 ?  1142 LEU A CB   1 
ATOM   7495  C CG   . LEU A 1 1142 ? 119.313 116.774 71.450  1.00 17.32 ?  1142 LEU A CG   1 
ATOM   7496  C CD1  . LEU A 1 1142 ? 120.833 116.730 71.347  1.00 17.93 ?  1142 LEU A CD1  1 
ATOM   7497  C CD2  . LEU A 1 1142 ? 118.670 116.083 70.255  1.00 19.53 ?  1142 LEU A CD2  1 
ATOM   7498  N N    . GLU A 1 1143 ? 120.250 116.731 75.607  1.00 28.04 ?  1143 GLU A N    1 
ATOM   7499  C CA   . GLU A 1 1143 ? 121.545 116.914 76.245  1.00 23.28 ?  1143 GLU A CA   1 
ATOM   7500  C C    . GLU A 1 1143 ? 122.617 116.015 75.648  1.00 25.41 ?  1143 GLU A C    1 
ATOM   7501  O O    . GLU A 1 1143 ? 123.789 116.405 75.604  1.00 28.92 ?  1143 GLU A O    1 
ATOM   7502  C CB   . GLU A 1 1143 ? 121.431 116.648 77.749  1.00 23.06 ?  1143 GLU A CB   1 
ATOM   7503  C CG   . GLU A 1 1143 ? 122.393 117.454 78.604  1.00 25.08 ?  1143 GLU A CG   1 
ATOM   7504  C CD   . GLU A 1 1143 ? 121.779 117.873 79.927  1.00 30.56 ?  1143 GLU A CD   1 
ATOM   7505  O OE1  . GLU A 1 1143 ? 120.563 117.658 80.113  1.00 29.47 ?  1143 GLU A OE1  1 
ATOM   7506  O OE2  . GLU A 1 1143 ? 122.510 118.418 80.780  1.00 29.96 ?  1143 GLU A OE2  1 
ATOM   7507  N N    . ASP A 1 1144 ? 122.239 114.825 75.182  1.00 21.40 ?  1144 ASP A N    1 
ATOM   7508  C CA   . ASP A 1 1144 ? 123.177 113.885 74.588  1.00 20.41 ?  1144 ASP A CA   1 
ATOM   7509  C C    . ASP A 1 1144 ? 122.424 112.946 73.659  1.00 20.63 ?  1144 ASP A C    1 
ATOM   7510  O O    . ASP A 1 1144 ? 121.286 112.556 73.936  1.00 23.49 ?  1144 ASP A O    1 
ATOM   7511  C CB   . ASP A 1 1144 ? 123.922 113.077 75.659  1.00 22.30 ?  1144 ASP A CB   1 
ATOM   7512  C CG   . ASP A 1 1144 ? 125.240 113.710 76.057  1.00 21.17 ?  1144 ASP A CG   1 
ATOM   7513  O OD1  . ASP A 1 1144 ? 126.180 113.697 75.235  1.00 20.06 ?  1144 ASP A OD1  1 
ATOM   7514  O OD2  . ASP A 1 1144 ? 125.335 114.224 77.191  1.00 17.73 ?  1144 ASP A OD2  1 
ATOM   7515  N N    . VAL A 1 1145 ? 123.070 112.589 72.550  1.00 18.00 ?  1145 VAL A N    1 
ATOM   7516  C CA   . VAL A 1 1145 ? 122.549 111.610 71.602  1.00 21.36 ?  1145 VAL A CA   1 
ATOM   7517  C C    . VAL A 1 1145 ? 123.611 110.542 71.366  1.00 19.89 ?  1145 VAL A C    1 
ATOM   7518  O O    . VAL A 1 1145 ? 124.778 110.858 71.109  1.00 22.60 ?  1145 VAL A O    1 
ATOM   7519  C CB   . VAL A 1 1145 ? 122.090 112.264 70.281  1.00 24.60 ?  1145 VAL A CB   1 
ATOM   7520  C CG1  . VAL A 1 1145 ? 120.926 113.185 70.540  1.00 23.27 ?  1145 VAL A CG1  1 
ATOM   7521  C CG2  . VAL A 1 1145 ? 123.201 113.096 69.659  1.00 22.66 ?  1145 VAL A CG2  1 
ATOM   7522  N N    . ILE A 1 1146 ? 123.237 109.257 71.445  1.00 19.40 ?  1146 ILE A N    1 
ATOM   7523  C CA   . ILE A 1 1146 ? 124.202 108.148 71.315  1.00 21.97 ?  1146 ILE A CA   1 
ATOM   7524  C C    . ILE A 1 1146 ? 123.730 107.145 70.305  1.00 19.84 ?  1146 ILE A C    1 
ATOM   7525  O O    . ILE A 1 1146 ? 122.547 106.827 70.251  1.00 15.26 ?  1146 ILE A O    1 
ATOM   7526  C CB   . ILE A 1 1146 ? 124.422 107.402 72.655  1.00 22.28 ?  1146 ILE A CB   1 
ATOM   7527  C CG1  . ILE A 1 1146 ? 124.605 108.373 73.822  1.00 19.64 ?  1146 ILE A CG1  1 
ATOM   7528  C CG2  . ILE A 1 1146 ? 125.623 106.481 72.562  1.00 15.46 ?  1146 ILE A CG2  1 
ATOM   7529  C CD1  . ILE A 1 1146 ? 123.329 108.705 74.561  1.00 19.09 ?  1146 ILE A CD1  1 
ATOM   7530  N N    . LEU A 1 1147 ? 124.649 106.635 69.512  1.00 20.14 ?  1147 LEU A N    1 
ATOM   7531  C CA   . LEU A 1 1147 ? 124.288 105.648 68.515  1.00 22.67 ?  1147 LEU A CA   1 
ATOM   7532  C C    . LEU A 1 1147 ? 124.507 104.206 68.996  1.00 25.26 ?  1147 LEU A C    1 
ATOM   7533  O O    . LEU A 1 1147 ? 125.610 103.688 68.887  1.00 27.28 ?  1147 LEU A O    1 
ATOM   7534  C CB   . LEU A 1 1147 ? 125.088 105.920 67.256  1.00 18.59 ?  1147 LEU A CB   1 
ATOM   7535  C CG   . LEU A 1 1147 ? 124.973 104.921 66.106  1.00 21.80 ?  1147 LEU A CG   1 
ATOM   7536  C CD1  . LEU A 1 1147 ? 123.622 105.019 65.425  1.00 23.18 ?  1147 LEU A CD1  1 
ATOM   7537  C CD2  . LEU A 1 1147 ? 126.089 105.130 65.097  1.00 21.58 ?  1147 LEU A CD2  1 
ATOM   7538  N N    . ILE A 1 1148 ? 123.467 103.527 69.475  1.00 19.06 ?  1148 ILE A N    1 
ATOM   7539  C CA   . ILE A 1 1148 ? 123.633 102.196 70.071  1.00 16.99 ?  1148 ILE A CA   1 
ATOM   7540  C C    . ILE A 1 1148 ? 123.534 101.034 69.115  1.00 20.80 ?  1148 ILE A C    1 
ATOM   7541  O O    . ILE A 1 1148 ? 123.931 99.932  69.450  1.00 25.27 ?  1148 ILE A O    1 
ATOM   7542  C CB   . ILE A 1 1148 ? 122.600 101.957 71.191  1.00 20.11 ?  1148 ILE A CB   1 
ATOM   7543  C CG1  . ILE A 1 1148 ? 121.193 101.831 70.617  1.00 22.94 ?  1148 ILE A CG1  1 
ATOM   7544  C CG2  . ILE A 1 1148 ? 122.650 103.073 72.221  1.00 18.50 ?  1148 ILE A CG2  1 
ATOM   7545  C CD1  . ILE A 1 1148 ? 120.116 101.842 71.677  1.00 20.19 ?  1148 ILE A CD1  1 
ATOM   7546  N N    . ASN A 1 1149 ? 123.022 101.268 67.918  1.00 22.14 ?  1149 ASN A N    1 
ATOM   7547  C CA   . ASN A 1 1149 ? 122.934 100.205 66.917  1.00 20.12 ?  1149 ASN A CA   1 
ATOM   7548  C C    . ASN A 1 1149 ? 122.942 100.721 65.483  1.00 22.23 ?  1149 ASN A C    1 
ATOM   7549  O O    . ASN A 1 1149 ? 122.580 101.865 65.241  1.00 20.16 ?  1149 ASN A O    1 
ATOM   7550  C CB   . ASN A 1 1149 ? 121.667 99.394  67.152  1.00 21.76 ?  1149 ASN A CB   1 
ATOM   7551  C CG   . ASN A 1 1149 ? 121.724 98.029  66.498  1.00 22.55 ?  1149 ASN A CG   1 
ATOM   7552  O OD1  . ASN A 1 1149 ? 122.742 97.646  65.921  1.00 18.37 ?  1149 ASN A OD1  1 
ATOM   7553  N ND2  . ASN A 1 1149 ? 120.630 97.282  66.591  1.00 20.21 ?  1149 ASN A ND2  1 
ATOM   7554  N N    . GLY A 1 1150 ? 123.368 99.899  64.530  1.00 27.99 ?  1150 GLY A N    1 
ATOM   7555  C CA   . GLY A 1 1150 ? 123.339 100.279 63.118  1.00 26.26 ?  1150 GLY A CA   1 
ATOM   7556  C C    . GLY A 1 1150 ? 124.329 101.285 62.563  1.00 24.42 ?  1150 GLY A C    1 
ATOM   7557  O O    . GLY A 1 1150 ? 125.317 101.610 63.219  1.00 21.72 ?  1150 GLY A O    1 
ATOM   7558  N N    . THR A 1 1151 ? 124.087 101.766 61.344  1.00 27.05 ?  1151 THR A N    1 
ATOM   7559  C CA   . THR A 1 1151 ? 124.938 102.798 60.741  1.00 27.97 ?  1151 THR A CA   1 
ATOM   7560  C C    . THR A 1 1151 ? 124.141 104.081 60.510  1.00 29.93 ?  1151 THR A C    1 
ATOM   7561  O O    . THR A 1 1151 ? 123.105 104.052 59.848  1.00 31.83 ?  1151 THR A O    1 
ATOM   7562  C CB   . THR A 1 1151 ? 125.510 102.341 59.399  1.00 29.06 ?  1151 THR A CB   1 
ATOM   7563  O OG1  . THR A 1 1151 ? 126.333 101.187 59.599  1.00 31.74 ?  1151 THR A OG1  1 
ATOM   7564  C CG2  . THR A 1 1151 ? 126.342 103.452 58.774  1.00 23.86 ?  1151 THR A CG2  1 
ATOM   7565  N N    . ALA A 1 1152 ? 124.606 105.206 61.039  1.00 21.19 ?  1152 ALA A N    1 
ATOM   7566  C CA   . ALA A 1 1152 ? 123.870 106.457 60.926  1.00 18.35 ?  1152 ALA A CA   1 
ATOM   7567  C C    . ALA A 1 1152 ? 124.013 107.049 59.528  1.00 24.40 ?  1152 ALA A C    1 
ATOM   7568  O O    . ALA A 1 1152 ? 125.014 106.834 58.837  1.00 23.29 ?  1152 ALA A O    1 
ATOM   7569  C CB   . ALA A 1 1152 ? 124.353 107.462 61.972  1.00 20.92 ?  1152 ALA A CB   1 
ATOM   7570  N N    . TYR A 1 1153 ? 122.991 107.800 59.111  1.00 27.54 ?  1153 TYR A N    1 
ATOM   7571  C CA   . TYR A 1 1153 ? 123.005 108.457 57.803  1.00 25.25 ?  1153 TYR A CA   1 
ATOM   7572  C C    . TYR A 1 1153 ? 122.274 109.791 57.933  1.00 22.83 ?  1153 TYR A C    1 
ATOM   7573  O O    . TYR A 1 1153 ? 121.041 109.833 57.904  1.00 19.10 ?  1153 TYR A O    1 
ATOM   7574  C CB   . TYR A 1 1153 ? 122.382 107.572 56.733  1.00 24.39 ?  1153 TYR A CB   1 
ATOM   7575  C CG   . TYR A 1 1153 ? 123.385 106.672 56.046  1.00 21.45 ?  1153 TYR A CG   1 
ATOM   7576  C CD1  . TYR A 1 1153 ? 124.587 107.181 55.571  1.00 20.63 ?  1153 TYR A CD1  1 
ATOM   7577  C CD2  . TYR A 1 1153 ? 123.134 105.317 55.878  1.00 22.44 ?  1153 TYR A CD2  1 
ATOM   7578  C CE1  . TYR A 1 1153 ? 125.511 106.366 54.944  1.00 25.26 ?  1153 TYR A CE1  1 
ATOM   7579  C CE2  . TYR A 1 1153 ? 124.052 104.493 55.251  1.00 25.16 ?  1153 TYR A CE2  1 
ATOM   7580  C CZ   . TYR A 1 1153 ? 125.239 105.023 54.787  1.00 26.21 ?  1153 TYR A CZ   1 
ATOM   7581  O OH   . TYR A 1 1153 ? 126.156 104.210 54.163  1.00 18.43 ?  1153 TYR A OH   1 
ATOM   7582  N N    . ASN A 1 1154 ? 123.035 110.858 58.162  1.00 24.74 ?  1154 ASN A N    1 
ATOM   7583  C CA   . ASN A 1 1154 ? 122.442 112.179 58.357  1.00 25.62 ?  1154 ASN A CA   1 
ATOM   7584  C C    . ASN A 1 1154 ? 121.889 112.712 57.044  1.00 26.96 ?  1154 ASN A C    1 
ATOM   7585  O O    . ASN A 1 1154 ? 122.083 112.107 55.993  1.00 31.29 ?  1154 ASN A O    1 
ATOM   7586  C CB   . ASN A 1 1154 ? 123.488 113.139 58.932  1.00 22.87 ?  1154 ASN A CB   1 
ATOM   7587  C CG   . ASN A 1 1154 ? 122.901 114.470 59.346  1.00 24.95 ?  1154 ASN A CG   1 
ATOM   7588  O OD1  . ASN A 1 1154 ? 121.806 114.529 59.887  1.00 25.62 ?  1154 ASN A OD1  1 
ATOM   7589  N ND2  . ASN A 1 1154 ? 123.640 115.546 59.110  1.00 25.63 ?  1154 ASN A ND2  1 
ATOM   7590  N N    . ALA A 1 1155 ? 121.196 113.842 57.099  1.00 25.43 ?  1155 ALA A N    1 
ATOM   7591  C CA   . ALA A 1 1155 ? 120.620 114.421 55.884  1.00 26.59 ?  1155 ALA A CA   1 
ATOM   7592  C C    . ALA A 1 1155 ? 121.598 115.358 55.168  1.00 27.36 ?  1155 ALA A C    1 
ATOM   7593  O O    . ALA A 1 1155 ? 121.265 115.925 54.131  1.00 27.12 ?  1155 ALA A O    1 
ATOM   7594  C CB   . ALA A 1 1155 ? 119.300 115.121 56.196  1.00 24.99 ?  1155 ALA A CB   1 
ATOM   7595  N N    . HIS A 1 1156 ? 122.794 115.531 55.719  1.00 27.23 ?  1156 HIS A N    1 
ATOM   7596  C CA   . HIS A 1 1156 ? 123.806 116.339 55.059  1.00 24.89 ?  1156 HIS A CA   1 
ATOM   7597  C C    . HIS A 1 1156 ? 124.902 115.394 54.663  1.00 27.85 ?  1156 HIS A C    1 
ATOM   7598  O O    . HIS A 1 1156 ? 125.529 114.782 55.524  1.00 26.61 ?  1156 HIS A O    1 
ATOM   7599  C CB   . HIS A 1 1156 ? 124.384 117.401 55.984  1.00 22.41 ?  1156 HIS A CB   1 
ATOM   7600  C CG   . HIS A 1 1156 ? 123.405 118.454 56.397  1.00 26.33 ?  1156 HIS A CG   1 
ATOM   7601  N ND1  . HIS A 1 1156 ? 122.193 118.159 56.983  1.00 29.88 ?  1156 HIS A ND1  1 
ATOM   7602  C CD2  . HIS A 1 1156 ? 123.472 119.805 56.333  1.00 29.62 ?  1156 HIS A CD2  1 
ATOM   7603  C CE1  . HIS A 1 1156 ? 121.549 119.281 57.247  1.00 29.92 ?  1156 HIS A CE1  1 
ATOM   7604  N NE2  . HIS A 1 1156 ? 122.304 120.295 56.865  1.00 32.66 ?  1156 HIS A NE2  1 
ATOM   7605  N N    . THR A 1 1157 ? 125.124 115.240 53.364  1.00 25.83 ?  1157 THR A N    1 
ATOM   7606  C CA   . THR A 1 1157 ? 126.197 114.384 52.888  1.00 24.02 ?  1157 THR A CA   1 
ATOM   7607  C C    . THR A 1 1157 ? 126.005 112.968 53.395  1.00 25.44 ?  1157 THR A C    1 
ATOM   7608  O O    . THR A 1 1157 ? 126.925 112.154 53.323  1.00 24.22 ?  1157 THR A O    1 
ATOM   7609  C CB   . THR A 1 1157 ? 127.592 114.891 53.325  1.00 25.53 ?  1157 THR A CB   1 
ATOM   7610  O OG1  . THR A 1 1157 ? 127.815 114.584 54.707  1.00 23.50 ?  1157 THR A OG1  1 
ATOM   7611  C CG2  . THR A 1 1157 ? 127.710 116.393 53.112  1.00 24.56 ?  1157 THR A CG2  1 
ATOM   7612  N N    . ARG A 1 1158 ? 124.799 112.676 53.869  1.00 26.54 ?  1158 ARG A N    1 
ATOM   7613  C CA   . ARG A 1 1158 ? 124.502 111.338 54.348  1.00 27.23 ?  1158 ARG A CA   1 
ATOM   7614  C C    . ARG A 1 1158 ? 125.498 110.911 55.401  1.00 27.30 ?  1158 ARG A C    1 
ATOM   7615  O O    . ARG A 1 1158 ? 126.053 109.816 55.328  1.00 27.12 ?  1158 ARG A O    1 
ATOM   7616  C CB   . ARG A 1 1158 ? 124.521 110.355 53.183  1.00 24.11 ?  1158 ARG A CB   1 
ATOM   7617  C CG   . ARG A 1 1158 ? 123.381 110.534 52.197  1.00 25.28 ?  1158 ARG A CG   1 
ATOM   7618  C CD   . ARG A 1 1158 ? 122.046 110.215 52.846  1.00 26.92 ?  1158 ARG A CD   1 
ATOM   7619  N NE   . ARG A 1 1158 ? 120.994 110.016 51.855  1.00 27.57 ?  1158 ARG A NE   1 
ATOM   7620  C CZ   . ARG A 1 1158 ? 119.747 109.666 52.153  1.00 26.07 ?  1158 ARG A CZ   1 
ATOM   7621  N NH1  . ARG A 1 1158 ? 119.394 109.478 53.417  1.00 27.35 ?  1158 ARG A NH1  1 
ATOM   7622  N NH2  . ARG A 1 1158 ? 118.853 109.505 51.186  1.00 26.77 ?  1158 ARG A NH2  1 
ATOM   7623  N N    . GLU A 1 1159 ? 125.716 111.758 56.398  1.00 27.12 ?  1159 GLU A N    1 
ATOM   7624  C CA   . GLU A 1 1159 ? 126.728 111.454 57.398  1.00 28.75 ?  1159 GLU A CA   1 
ATOM   7625  C C    . GLU A 1 1159 ? 126.648 110.004 57.839  1.00 28.75 ?  1159 GLU A C    1 
ATOM   7626  O O    . GLU A 1 1159 ? 125.601 109.543 58.271  1.00 25.95 ?  1159 GLU A O    1 
ATOM   7627  C CB   . GLU A 1 1159 ? 126.586 112.390 58.591  1.00 24.90 ?  1159 GLU A CB   1 
ATOM   7628  C CG   . GLU A 1 1159 ? 127.730 112.297 59.579  1.00 25.16 ?  1159 GLU A CG   1 
ATOM   7629  C CD   . GLU A 1 1159 ? 129.070 112.593 58.940  1.00 28.83 ?  1159 GLU A CD   1 
ATOM   7630  O OE1  . GLU A 1 1159 ? 129.686 111.660 58.387  1.00 30.59 ?  1159 GLU A OE1  1 
ATOM   7631  O OE2  . GLU A 1 1159 ? 129.507 113.761 58.994  1.00 28.30 ?  1159 GLU A OE2  1 
ATOM   7632  N N    . GLU A 1 1160 ? 127.758 109.286 57.726  1.00 26.16 ?  1160 GLU A N    1 
ATOM   7633  C CA   . GLU A 1 1160 ? 127.795 107.885 58.126  1.00 26.10 ?  1160 GLU A CA   1 
ATOM   7634  C C    . GLU A 1 1160 ? 128.668 107.666 59.350  1.00 26.91 ?  1160 GLU A C    1 
ATOM   7635  O O    . GLU A 1 1160 ? 129.844 108.028 59.348  1.00 26.98 ?  1160 GLU A O    1 
ATOM   7636  C CB   . GLU A 1 1160 ? 128.325 107.030 56.984  1.00 24.62 ?  1160 GLU A CB   1 
ATOM   7637  C CG   . GLU A 1 1160 ? 128.508 105.570 57.345  1.00 24.91 ?  1160 GLU A CG   1 
ATOM   7638  C CD   . GLU A 1 1160 ? 128.908 104.727 56.154  1.00 25.85 ?  1160 GLU A CD   1 
ATOM   7639  O OE1  . GLU A 1 1160 ? 129.167 105.305 55.078  1.00 26.36 ?  1160 GLU A OE1  1 
ATOM   7640  O OE2  . GLU A 1 1160 ? 128.962 103.488 56.292  1.00 25.09 ?  1160 GLU A OE2  1 
ATOM   7641  N N    . ILE A 1 1161 ? 128.099 107.078 60.398  1.00 26.29 ?  1161 ILE A N    1 
ATOM   7642  C CA   . ILE A 1 1161 ? 128.862 106.791 61.608  1.00 25.38 ?  1161 ILE A CA   1 
ATOM   7643  C C    . ILE A 1 1161 ? 128.548 105.360 62.032  1.00 24.75 ?  1161 ILE A C    1 
ATOM   7644  O O    . ILE A 1 1161 ? 127.477 104.846 61.716  1.00 23.62 ?  1161 ILE A O    1 
ATOM   7645  C CB   . ILE A 1 1161 ? 128.541 107.784 62.741  1.00 25.99 ?  1161 ILE A CB   1 
ATOM   7646  C CG1  . ILE A 1 1161 ? 128.410 109.207 62.195  1.00 23.68 ?  1161 ILE A CG1  1 
ATOM   7647  C CG2  . ILE A 1 1161 ? 129.603 107.721 63.827  1.00 25.44 ?  1161 ILE A CG2  1 
ATOM   7648  C CD1  . ILE A 1 1161 ? 127.024 109.548 61.692  1.00 21.63 ?  1161 ILE A CD1  1 
ATOM   7649  N N    . ARG A 1 1162 ? 129.457 104.722 62.759  1.00 23.95 ?  1162 ARG A N    1 
ATOM   7650  C CA   . ARG A 1 1162 ? 129.241 103.334 63.154  1.00 24.33 ?  1162 ARG A CA   1 
ATOM   7651  C C    . ARG A 1 1162 ? 128.951 103.192 64.642  1.00 24.80 ?  1162 ARG A C    1 
ATOM   7652  O O    . ARG A 1 1162 ? 129.489 103.938 65.459  1.00 26.35 ?  1162 ARG A O    1 
ATOM   7653  C CB   . ARG A 1 1162 ? 130.446 102.474 62.767  1.00 23.76 ?  1162 ARG A CB   1 
ATOM   7654  C CG   . ARG A 1 1162 ? 130.140 100.988 62.720  1.00 26.37 ?  1162 ARG A CG   1 
ATOM   7655  C CD   . ARG A 1 1162 ? 128.867 100.727 61.929  1.00 26.63 ?  1162 ARG A CD   1 
ATOM   7656  N NE   . ARG A 1 1162 ? 128.855 101.446 60.658  1.00 28.29 ?  1162 ARG A NE   1 
ATOM   7657  C CZ   . ARG A 1 1162 ? 129.340 100.963 59.520  1.00 28.61 ?  1162 ARG A CZ   1 
ATOM   7658  N NH1  . ARG A 1 1162 ? 129.879 99.752  59.486  1.00 27.01 ?  1162 ARG A NH1  1 
ATOM   7659  N NH2  . ARG A 1 1162 ? 129.285 101.691 58.413  1.00 24.22 ?  1162 ARG A NH2  1 
ATOM   7660  N N    . SER A 1 1163 ? 128.101 102.233 64.996  1.00 22.82 ?  1163 SER A N    1 
ATOM   7661  C CA   . SER A 1 1163 ? 127.758 102.014 66.398  1.00 22.73 ?  1163 SER A CA   1 
ATOM   7662  C C    . SER A 1 1163 ? 128.846 101.232 67.123  1.00 25.31 ?  1163 SER A C    1 
ATOM   7663  O O    . SER A 1 1163 ? 129.769 100.715 66.495  1.00 21.57 ?  1163 SER A O    1 
ATOM   7664  C CB   . SER A 1 1163 ? 126.425 101.276 66.507  1.00 19.63 ?  1163 SER A CB   1 
ATOM   7665  O OG   . SER A 1 1163 ? 125.406 101.980 65.828  1.00 18.97 ?  1163 SER A OG   1 
ATOM   7666  N N    . PRO A 1 1164 ? 128.737 101.146 68.457  1.00 25.92 ?  1164 PRO A N    1 
ATOM   7667  C CA   . PRO A 1 1164 ? 128.202 102.240 69.272  1.00 22.00 ?  1164 PRO A CA   1 
ATOM   7668  C C    . PRO A 1 1164 ? 129.127 103.445 69.251  1.00 21.70 ?  1164 PRO A C    1 
ATOM   7669  O O    . PRO A 1 1164 ? 130.345 103.279 69.302  1.00 21.47 ?  1164 PRO A O    1 
ATOM   7670  C CB   . PRO A 1 1164 ? 128.150 101.636 70.678  1.00 22.52 ?  1164 PRO A CB   1 
ATOM   7671  C CG   . PRO A 1 1164 ? 129.178 100.558 70.665  1.00 22.02 ?  1164 PRO A CG   1 
ATOM   7672  C CD   . PRO A 1 1164 ? 129.147 99.993  69.275  1.00 24.50 ?  1164 PRO A CD   1 
ATOM   7673  N N    . CYS A 1 1165 ? 128.558 104.642 69.173  1.00 24.91 ?  1165 CYS A N    1 
ATOM   7674  C CA   . CYS A 1 1165 ? 129.372 105.850 69.117  1.00 26.76 ?  1165 CYS A CA   1 
ATOM   7675  C C    . CYS A 1 1165 ? 128.604 107.076 69.573  1.00 25.08 ?  1165 CYS A C    1 
ATOM   7676  O O    . CYS A 1 1165 ? 127.406 107.198 69.313  1.00 24.32 ?  1165 CYS A O    1 
ATOM   7677  C CB   . CYS A 1 1165 ? 129.894 106.073 67.697  1.00 24.69 ?  1165 CYS A CB   1 
ATOM   7678  S SG   . CYS A 1 1165 ? 130.834 107.602 67.485  1.00 29.39 ?  1165 CYS A SG   1 
ATOM   7679  N N    . LEU A 1 1166 ? 129.288 107.989 70.252  1.00 19.77 ?  1166 LEU A N    1 
ATOM   7680  C CA   . LEU A 1 1166 ? 128.643 109.224 70.677  1.00 18.29 ?  1166 LEU A CA   1 
ATOM   7681  C C    . LEU A 1 1166 ? 128.642 110.190 69.509  1.00 24.90 ?  1166 LEU A C    1 
ATOM   7682  O O    . LEU A 1 1166 ? 129.701 110.528 68.982  1.00 25.62 ?  1166 LEU A O    1 
ATOM   7683  C CB   . LEU A 1 1166 ? 129.363 109.829 71.879  1.00 19.58 ?  1166 LEU A CB   1 
ATOM   7684  C CG   . LEU A 1 1166 ? 128.662 111.013 72.547  1.00 25.54 ?  1166 LEU A CG   1 
ATOM   7685  C CD1  . LEU A 1 1166 ? 127.264 110.616 72.996  1.00 20.44 ?  1166 LEU A CD1  1 
ATOM   7686  C CD2  . LEU A 1 1166 ? 129.479 111.519 73.725  1.00 23.30 ?  1166 LEU A CD2  1 
ATOM   7687  N N    . ILE A 1 1167 ? 127.464 110.637 69.095  1.00 23.14 ?  1167 ILE A N    1 
ATOM   7688  C CA   . ILE A 1 1167 ? 127.367 111.508 67.927  1.00 20.65 ?  1167 ILE A CA   1 
ATOM   7689  C C    . ILE A 1 1167 ? 128.117 112.809 68.182  1.00 20.57 ?  1167 ILE A C    1 
ATOM   7690  O O    . ILE A 1 1167 ? 128.070 113.371 69.286  1.00 15.28 ?  1167 ILE A O    1 
ATOM   7691  C CB   . ILE A 1 1167 ? 125.892 111.770 67.573  1.00 20.46 ?  1167 ILE A CB   1 
ATOM   7692  C CG1  . ILE A 1 1167 ? 125.127 110.446 67.511  1.00 20.29 ?  1167 ILE A CG1  1 
ATOM   7693  C CG2  . ILE A 1 1167 ? 125.776 112.502 66.241  1.00 20.43 ?  1167 ILE A CG2  1 
ATOM   7694  C CD1  . ILE A 1 1167 ? 123.712 110.562 66.984  1.00 16.26 ?  1167 ILE A CD1  1 
ATOM   7695  N N    . SER A 1 1168 ? 128.842 113.275 67.164  1.00 25.24 ?  1168 SER A N    1 
ATOM   7696  C CA   . SER A 1 1168 ? 129.605 114.509 67.281  1.00 28.53 ?  1168 SER A CA   1 
ATOM   7697  C C    . SER A 1 1168 ? 128.676 115.684 67.552  1.00 29.50 ?  1168 SER A C    1 
ATOM   7698  O O    . SER A 1 1168 ? 127.525 115.714 67.107  1.00 28.65 ?  1168 SER A O    1 
ATOM   7699  C CB   . SER A 1 1168 ? 130.419 114.761 66.011  1.00 20.48 ?  1168 SER A CB   1 
ATOM   7700  O OG   . SER A 1 1168 ? 131.337 113.709 65.771  1.00 19.54 ?  1168 SER A OG   1 
ATOM   7701  N N    . ARG A 1 1169 ? 129.112 116.618 68.389  1.00 24.14 ?  1169 ARG A N    1 
ATOM   7702  C CA   . ARG A 1 1169 ? 128.219 117.706 68.775  1.00 23.20 ?  1169 ARG A CA   1 
ATOM   7703  C C    . ARG A 1 1169 ? 127.698 118.511 67.583  1.00 26.74 ?  1169 ARG A C    1 
ATOM   7704  O O    . ARG A 1 1169 ? 126.580 119.026 67.635  1.00 25.18 ?  1169 ARG A O    1 
ATOM   7705  C CB   . ARG A 1 1169 ? 128.919 118.622 69.777  1.00 22.68 ?  1169 ARG A CB   1 
ATOM   7706  C CG   . ARG A 1 1169 ? 127.975 119.459 70.614  1.00 24.52 ?  1169 ARG A CG   1 
ATOM   7707  C CD   . ARG A 1 1169 ? 127.519 118.687 71.838  1.00 24.89 ?  1169 ARG A CD   1 
ATOM   7708  N NE   . ARG A 1 1169 ? 126.439 119.368 72.542  1.00 28.39 ?  1169 ARG A NE   1 
ATOM   7709  C CZ   . ARG A 1 1169 ? 126.016 119.038 73.756  1.00 27.20 ?  1169 ARG A CZ   1 
ATOM   7710  N NH1  . ARG A 1 1169 ? 126.595 118.041 74.409  1.00 25.50 ?  1169 ARG A NH1  1 
ATOM   7711  N NH2  . ARG A 1 1169 ? 125.025 119.712 74.321  1.00 25.96 ?  1169 ARG A NH2  1 
ATOM   7712  N N    . THR A 1 1170 ? 128.469 118.608 66.506  1.00 24.31 ?  1170 THR A N    1 
ATOM   7713  C CA   . THR A 1 1170 ? 128.077 119.424 65.357  1.00 25.36 ?  1170 THR A CA   1 
ATOM   7714  C C    . THR A 1 1170 ? 127.459 118.507 64.302  1.00 25.91 ?  1170 THR A C    1 
ATOM   7715  O O    . THR A 1 1170 ? 128.160 117.994 63.425  1.00 24.78 ?  1170 THR A O    1 
ATOM   7716  C CB   . THR A 1 1170 ? 129.280 120.187 64.792  1.00 26.36 ?  1170 THR A CB   1 
ATOM   7717  O OG1  . THR A 1 1170 ? 130.031 120.767 65.866  1.00 25.49 ?  1170 THR A OG1  1 
ATOM   7718  C CG2  . THR A 1 1170 ? 128.821 121.287 63.845  1.00 24.59 ?  1170 THR A CG2  1 
ATOM   7719  N N    . VAL A 1 1171 ? 126.144 118.305 64.385  1.00 29.51 ?  1171 VAL A N    1 
ATOM   7720  C CA   . VAL A 1 1171 ? 125.394 117.487 63.440  1.00 28.48 ?  1171 VAL A CA   1 
ATOM   7721  C C    . VAL A 1 1171 ? 124.059 118.170 63.160  1.00 28.31 ?  1171 VAL A C    1 
ATOM   7722  O O    . VAL A 1 1171 ? 123.744 119.221 63.723  1.00 32.93 ?  1171 VAL A O    1 
ATOM   7723  C CB   . VAL A 1 1171 ? 125.167 116.050 63.953  1.00 25.91 ?  1171 VAL A CB   1 
ATOM   7724  C CG1  . VAL A 1 1171 ? 126.421 115.206 63.762  1.00 25.76 ?  1171 VAL A CG1  1 
ATOM   7725  C CG2  . VAL A 1 1171 ? 124.734 116.069 65.410  1.00 24.50 ?  1171 VAL A CG2  1 
ATOM   7726  N N    . HIS A 1 1172 ? 123.269 117.559 62.280  1.00 24.36 ?  1172 HIS A N    1 
ATOM   7727  C CA   . HIS A 1 1172 ? 121.958 118.081 61.907  1.00 25.68 ?  1172 HIS A CA   1 
ATOM   7728  C C    . HIS A 1 1172 ? 120.963 116.924 61.905  1.00 26.16 ?  1172 HIS A C    1 
ATOM   7729  O O    . HIS A 1 1172 ? 121.251 115.832 62.406  1.00 27.75 ?  1172 HIS A O    1 
ATOM   7730  C CB   . HIS A 1 1172 ? 122.025 118.809 60.558  1.00 27.72 ?  1172 HIS A CB   1 
ATOM   7731  C CG   . HIS A 1 1172 ? 123.114 119.833 60.479  1.00 30.53 ?  1172 HIS A CG   1 
ATOM   7732  N ND1  . HIS A 1 1172 ? 123.177 120.918 61.326  1.00 29.97 ?  1172 HIS A ND1  1 
ATOM   7733  C CD2  . HIS A 1 1172 ? 124.184 119.938 59.655  1.00 28.95 ?  1172 HIS A CD2  1 
ATOM   7734  C CE1  . HIS A 1 1172 ? 124.237 121.647 61.028  1.00 26.94 ?  1172 HIS A CE1  1 
ATOM   7735  N NE2  . HIS A 1 1172 ? 124.865 121.075 60.017  1.00 29.22 ?  1172 HIS A NE2  1 
ATOM   7736  N N    . LYS A 1 1173 ? 119.770 117.177 61.368  1.00 27.76 ?  1173 LYS A N    1 
ATOM   7737  C CA   . LYS A 1 1173 ? 118.702 116.185 61.402  1.00 28.08 ?  1173 LYS A CA   1 
ATOM   7738  C C    . LYS A 1 1173 ? 119.025 115.006 60.494  1.00 27.60 ?  1173 LYS A C    1 
ATOM   7739  O O    . LYS A 1 1173 ? 119.429 115.179 59.341  1.00 26.82 ?  1173 LYS A O    1 
ATOM   7740  C CB   . LYS A 1 1173 ? 117.372 116.819 60.994  1.00 26.14 ?  1173 LYS A CB   1 
ATOM   7741  C CG   . LYS A 1 1173 ? 117.092 118.157 61.662  1.00 23.96 ?  1173 LYS A CG   1 
ATOM   7742  C CD   . LYS A 1 1173 ? 115.747 118.725 61.238  1.00 28.38 ?  1173 LYS A CD   1 
ATOM   7743  C CE   . LYS A 1 1173 ? 115.465 120.050 61.930  1.00 28.32 ?  1173 LYS A CE   1 
ATOM   7744  N NZ   . LYS A 1 1173 ? 114.211 120.685 61.438  1.00 29.96 ?  1173 LYS A NZ   1 
ATOM   7745  N N    . LEU A 1 1174 ? 118.833 113.799 61.020  1.00 25.02 ?  1174 LEU A N    1 
ATOM   7746  C CA   . LEU A 1 1174 ? 119.238 112.574 60.349  1.00 26.26 ?  1174 LEU A CA   1 
ATOM   7747  C C    . LEU A 1 1174 ? 118.028 111.697 60.055  1.00 25.78 ?  1174 LEU A C    1 
ATOM   7748  O O    . LEU A 1 1174 ? 117.041 111.693 60.798  1.00 23.01 ?  1174 LEU A O    1 
ATOM   7749  C CB   . LEU A 1 1174 ? 120.267 111.794 61.190  1.00 24.33 ?  1174 LEU A CB   1 
ATOM   7750  C CG   . LEU A 1 1174 ? 119.807 110.833 62.292  1.00 26.19 ?  1174 LEU A CG   1 
ATOM   7751  C CD1  . LEU A 1 1174 ? 120.971 109.968 62.751  1.00 25.54 ?  1174 LEU A CD1  1 
ATOM   7752  C CD2  . LEU A 1 1174 ? 119.211 111.584 63.473  1.00 23.24 ?  1174 LEU A CD2  1 
ATOM   7753  N N    . THR A 1 1175 ? 118.113 110.965 58.950  1.00 25.21 ?  1175 THR A N    1 
ATOM   7754  C CA   . THR A 1 1175 ? 117.099 110.012 58.525  1.00 24.85 ?  1175 THR A CA   1 
ATOM   7755  C C    . THR A 1 1175 ? 117.698 108.608 58.528  1.00 25.12 ?  1175 THR A C    1 
ATOM   7756  O O    . THR A 1 1175 ? 118.850 108.403 58.915  1.00 28.25 ?  1175 THR A O    1 
ATOM   7757  C CB   . THR A 1 1175 ? 116.550 110.374 57.141  1.00 25.53 ?  1175 THR A CB   1 
ATOM   7758  O OG1  . THR A 1 1175 ? 115.531 109.437 56.768  1.00 24.23 ?  1175 THR A OG1  1 
ATOM   7759  C CG2  . THR A 1 1175 ? 117.661 110.353 56.102  1.00 20.96 ?  1175 THR A CG2  1 
ATOM   7760  N N    . PHE A 1 1176 ? 116.903 107.632 58.094  1.00 25.53 ?  1176 PHE A N    1 
ATOM   7761  C CA   . PHE A 1 1176 ? 117.360 106.250 58.081  1.00 23.89 ?  1176 PHE A CA   1 
ATOM   7762  C C    . PHE A 1 1176 ? 116.679 105.491 56.953  1.00 24.91 ?  1176 PHE A C    1 
ATOM   7763  O O    . PHE A 1 1176 ? 115.618 105.882 56.461  1.00 26.00 ?  1176 PHE A O    1 
ATOM   7764  C CB   . PHE A 1 1176 ? 117.101 105.561 59.426  1.00 24.27 ?  1176 PHE A CB   1 
ATOM   7765  C CG   . PHE A 1 1176 ? 118.130 105.876 60.468  1.00 25.20 ?  1176 PHE A CG   1 
ATOM   7766  C CD1  . PHE A 1 1176 ? 119.413 105.366 60.363  1.00 26.06 ?  1176 PHE A CD1  1 
ATOM   7767  C CD2  . PHE A 1 1176 ? 117.824 106.699 61.539  1.00 21.89 ?  1176 PHE A CD2  1 
ATOM   7768  C CE1  . PHE A 1 1176 ? 120.368 105.658 61.313  1.00 25.10 ?  1176 PHE A CE1  1 
ATOM   7769  C CE2  . PHE A 1 1176 ? 118.777 106.995 62.493  1.00 22.60 ?  1176 PHE A CE2  1 
ATOM   7770  C CZ   . PHE A 1 1176 ? 120.051 106.474 62.376  1.00 26.38 ?  1176 PHE A CZ   1 
ATOM   7771  N N    . GLN A 1 1177 ? 117.313 104.393 56.552  1.00 24.71 ?  1177 GLN A N    1 
ATOM   7772  C CA   . GLN A 1 1177 ? 116.808 103.512 55.511  1.00 26.83 ?  1177 GLN A CA   1 
ATOM   7773  C C    . GLN A 1 1177 ? 116.479 102.152 56.109  1.00 29.81 ?  1177 GLN A C    1 
ATOM   7774  O O    . GLN A 1 1177 ? 117.243 101.619 56.920  1.00 27.98 ?  1177 GLN A O    1 
ATOM   7775  C CB   . GLN A 1 1177 ? 117.829 103.356 54.380  1.00 25.41 ?  1177 GLN A CB   1 
ATOM   7776  C CG   . GLN A 1 1177 ? 117.290 102.656 53.142  1.00 26.13 ?  1177 GLN A CG   1 
ATOM   7777  C CD   . GLN A 1 1177 ? 116.118 103.390 52.520  1.00 27.74 ?  1177 GLN A CD   1 
ATOM   7778  O OE1  . GLN A 1 1177 ? 114.960 103.047 52.757  1.00 28.48 ?  1177 GLN A OE1  1 
ATOM   7779  N NE2  . GLN A 1 1177 ? 116.415 104.405 51.717  1.00 27.85 ?  1177 GLN A NE2  1 
ATOM   7780  N N    . TYR A 1 1178 ? 115.339 101.597 55.707  1.00 31.64 ?  1178 TYR A N    1 
ATOM   7781  C CA   . TYR A 1 1178 ? 114.877 100.310 56.223  1.00 31.55 ?  1178 TYR A CA   1 
ATOM   7782  C C    . TYR A 1 1178 ? 115.758 99.201  55.664  1.00 30.93 ?  1178 TYR A C    1 
ATOM   7783  O O    . TYR A 1 1178 ? 115.636 98.818  54.498  1.00 29.37 ?  1178 TYR A O    1 
ATOM   7784  C CB   . TYR A 1 1178 ? 113.413 100.089 55.859  1.00 31.00 ?  1178 TYR A CB   1 
ATOM   7785  C CG   . TYR A 1 1178 ? 112.868 98.743  56.284  1.00 34.28 ?  1178 TYR A CG   1 
ATOM   7786  C CD1  . TYR A 1 1178 ? 112.531 98.496  57.608  1.00 32.66 ?  1178 TYR A CD1  1 
ATOM   7787  C CD2  . TYR A 1 1178 ? 112.685 97.722  55.359  1.00 30.97 ?  1178 TYR A CD2  1 
ATOM   7788  C CE1  . TYR A 1 1178 ? 112.031 97.267  58.001  1.00 30.66 ?  1178 TYR A CE1  1 
ATOM   7789  C CE2  . TYR A 1 1178 ? 112.186 96.491  55.742  1.00 31.60 ?  1178 TYR A CE2  1 
ATOM   7790  C CZ   . TYR A 1 1178 ? 111.861 96.269  57.064  1.00 31.77 ?  1178 TYR A CZ   1 
ATOM   7791  O OH   . TYR A 1 1178 ? 111.363 95.046  57.450  1.00 33.71 ?  1178 TYR A OH   1 
ATOM   7792  N N    . THR A 1 1179 ? 116.654 98.681  56.498  1.00 29.57 ?  1179 THR A N    1 
ATOM   7793  C CA   . THR A 1 1179 ? 117.513 97.559  56.144  1.00 34.93 ?  1179 THR A CA   1 
ATOM   7794  C C    . THR A 1 1179 ? 117.079 96.348  56.958  1.00 31.91 ?  1179 THR A C    1 
ATOM   7795  O O    . THR A 1 1179 ? 117.036 96.408  58.191  1.00 31.11 ?  1179 THR A O    1 
ATOM   7796  C CB   . THR A 1 1179 ? 118.985 97.883  56.400  1.00 33.59 ?  1179 THR A CB   1 
ATOM   7797  O OG1  . THR A 1 1179 ? 119.224 97.956  57.811  1.00 32.62 ?  1179 THR A OG1  1 
ATOM   7798  C CG2  . THR A 1 1179 ? 119.359 99.210  55.756  1.00 29.77 ?  1179 THR A CG2  1 
ATOM   7799  N N    . ALA A 1 1180 ? 116.762 95.252  56.266  1.00 27.07 ?  1180 ALA A N    1 
ATOM   7800  C CA   . ALA A 1 1180 ? 116.226 94.079  56.948  1.00 26.59 ?  1180 ALA A CA   1 
ATOM   7801  C C    . ALA A 1 1180 ? 117.299 93.325  57.723  1.00 25.36 ?  1180 ALA A C    1 
ATOM   7802  O O    . ALA A 1 1180 ? 116.982 92.629  58.693  1.00 24.79 ?  1180 ALA A O    1 
ATOM   7803  C CB   . ALA A 1 1180 ? 115.550 93.150  55.941  1.00 23.54 ?  1180 ALA A CB   1 
ATOM   7804  N N    . THR A 1 1181 ? 118.565 93.441  57.318  1.00 29.11 ?  1181 THR A N    1 
ATOM   7805  C CA   . THR A 1 1181 ? 119.622 92.674  57.966  1.00 29.78 ?  1181 THR A CA   1 
ATOM   7806  C C    . THR A 1 1181 ? 119.999 93.219  59.340  1.00 28.71 ?  1181 THR A C    1 
ATOM   7807  O O    . THR A 1 1181 ? 120.321 92.428  60.236  1.00 28.36 ?  1181 THR A O    1 
ATOM   7808  C CB   . THR A 1 1181 ? 120.857 92.605  57.055  1.00 30.04 ?  1181 THR A CB   1 
ATOM   7809  O OG1  . THR A 1 1181 ? 121.896 91.853  57.696  1.00 30.95 ?  1181 THR A OG1  1 
ATOM   7810  C CG2  . THR A 1 1181 ? 121.366 93.997  56.674  1.00 29.14 ?  1181 THR A CG2  1 
ATOM   7811  N N    . GLU A 1 1182 ? 119.976 94.539  59.503  1.00 27.94 ?  1182 GLU A N    1 
ATOM   7812  C CA   . GLU A 1 1182 ? 120.322 95.156  60.781  1.00 31.20 ?  1182 GLU A CA   1 
ATOM   7813  C C    . GLU A 1 1182 ? 119.544 96.447  60.971  1.00 28.54 ?  1182 GLU A C    1 
ATOM   7814  O O    . GLU A 1 1182 ? 119.539 97.305  60.094  1.00 29.78 ?  1182 GLU A O    1 
ATOM   7815  C CB   . GLU A 1 1182 ? 121.820 95.450  60.858  1.00 29.42 ?  1182 GLU A CB   1 
ATOM   7816  C CG   . GLU A 1 1182 ? 122.714 94.222  60.811  1.00 28.32 ?  1182 GLU A CG   1 
ATOM   7817  C CD   . GLU A 1 1182 ? 124.185 94.570  60.931  1.00 31.23 ?  1182 GLU A CD   1 
ATOM   7818  O OE1  . GLU A 1 1182 ? 124.503 95.769  61.078  1.00 30.72 ?  1182 GLU A OE1  1 
ATOM   7819  O OE2  . GLU A 1 1182 ? 125.022 93.645  60.879  1.00 33.30 ?  1182 GLU A OE2  1 
ATOM   7820  N N    . GLU A 1 1183 ? 118.892 96.595  62.118  1.00 26.00 ?  1183 GLU A N    1 
ATOM   7821  C CA   . GLU A 1 1183 ? 118.092 97.789  62.365  1.00 29.36 ?  1183 GLU A CA   1 
ATOM   7822  C C    . GLU A 1 1183 ? 118.770 98.736  63.347  1.00 29.54 ?  1183 GLU A C    1 
ATOM   7823  O O    . GLU A 1 1183 ? 118.874 98.434  64.535  1.00 26.82 ?  1183 GLU A O    1 
ATOM   7824  C CB   . GLU A 1 1183 ? 116.705 97.400  62.878  1.00 27.08 ?  1183 GLU A CB   1 
ATOM   7825  C CG   . GLU A 1 1183 ? 115.917 96.538  61.906  1.00 24.19 ?  1183 GLU A CG   1 
ATOM   7826  C CD   . GLU A 1 1183 ? 114.550 96.158  62.438  1.00 29.36 ?  1183 GLU A CD   1 
ATOM   7827  O OE1  . GLU A 1 1183 ? 114.219 96.561  63.573  1.00 27.21 ?  1183 GLU A OE1  1 
ATOM   7828  O OE2  . GLU A 1 1183 ? 113.807 95.456  61.721  1.00 29.95 ?  1183 GLU A OE2  1 
ATOM   7829  N N    . PRO A 1 1184 ? 119.234 99.891  62.851  1.00 29.74 ?  1184 PRO A N    1 
ATOM   7830  C CA   . PRO A 1 1184 ? 119.866 100.881 63.729  1.00 24.83 ?  1184 PRO A CA   1 
ATOM   7831  C C    . PRO A 1 1184 ? 118.857 101.489 64.689  1.00 25.12 ?  1184 PRO A C    1 
ATOM   7832  O O    . PRO A 1 1184 ? 117.737 101.791 64.279  1.00 24.90 ?  1184 PRO A O    1 
ATOM   7833  C CB   . PRO A 1 1184 ? 120.366 101.953 62.752  1.00 25.40 ?  1184 PRO A CB   1 
ATOM   7834  C CG   . PRO A 1 1184 ? 120.382 101.297 61.411  1.00 25.44 ?  1184 PRO A CG   1 
ATOM   7835  C CD   . PRO A 1 1184 ? 119.261 100.304 61.439  1.00 28.47 ?  1184 PRO A CD   1 
ATOM   7836  N N    . ARG A 1 1185 ? 119.243 101.667 65.947  1.00 28.27 ?  1185 ARG A N    1 
ATOM   7837  C CA   . ARG A 1 1185 ? 118.351 102.260 66.923  1.00 27.50 ?  1185 ARG A CA   1 
ATOM   7838  C C    . ARG A 1 1185 ? 119.186 103.243 67.707  1.00 29.86 ?  1185 ARG A C    1 
ATOM   7839  O O    . ARG A 1 1185 ? 120.392 103.065 67.801  1.00 30.78 ?  1185 ARG A O    1 
ATOM   7840  C CB   . ARG A 1 1185 ? 117.748 101.186 67.810  1.00 24.06 ?  1185 ARG A CB   1 
ATOM   7841  C CG   . ARG A 1 1185 ? 116.466 101.587 68.513  1.00 24.04 ?  1185 ARG A CG   1 
ATOM   7842  C CD   . ARG A 1 1185 ? 116.021 100.466 69.433  1.00 24.93 ?  1185 ARG A CD   1 
ATOM   7843  N NE   . ARG A 1 1185 ? 115.890 99.204  68.713  1.00 26.96 ?  1185 ARG A NE   1 
ATOM   7844  C CZ   . ARG A 1 1185 ? 114.731 98.675  68.338  1.00 24.58 ?  1185 ARG A CZ   1 
ATOM   7845  N NH1  . ARG A 1 1185 ? 113.594 99.289  68.627  1.00 24.09 ?  1185 ARG A NH1  1 
ATOM   7846  N NH2  . ARG A 1 1185 ? 114.710 97.523  67.684  1.00 22.11 ?  1185 ARG A NH2  1 
ATOM   7847  N N    . LEU A 1 1186 ? 118.582 104.293 68.250  1.00 23.75 ?  1186 LEU A N    1 
ATOM   7848  C CA   . LEU A 1 1186 ? 119.379 105.315 68.920  1.00 21.50 ?  1186 LEU A CA   1 
ATOM   7849  C C    . LEU A 1 1186 ? 118.759 105.797 70.188  1.00 24.73 ?  1186 LEU A C    1 
ATOM   7850  O O    . LEU A 1 1186 ? 117.547 105.711 70.365  1.00 24.55 ?  1186 LEU A O    1 
ATOM   7851  C CB   . LEU A 1 1186 ? 119.660 106.504 68.010  1.00 17.95 ?  1186 LEU A CB   1 
ATOM   7852  C CG   . LEU A 1 1186 ? 120.775 106.401 66.970  1.00 18.24 ?  1186 LEU A CG   1 
ATOM   7853  C CD1  . LEU A 1 1186 ? 120.381 105.488 65.821  1.00 19.42 ?  1186 LEU A CD1  1 
ATOM   7854  C CD2  . LEU A 1 1186 ? 121.090 107.789 66.442  1.00 22.90 ?  1186 LEU A CD2  1 
ATOM   7855  N N    . PHE A 1 1187 ? 119.576 106.333 71.058  1.00 22.90 ?  1187 PHE A N    1 
ATOM   7856  C CA   . PHE A 1 1187 ? 119.166 106.744 72.393  1.00 19.53 ?  1187 PHE A CA   1 
ATOM   7857  C C    . PHE A 1 1187 ? 119.313 108.256 72.496  1.00 17.64 ?  1187 PHE A C    1 
ATOM   7858  O O    . PHE A 1 1187 ? 120.400 108.794 72.260  1.00 17.84 ?  1187 PHE A O    1 
ATOM   7859  C CB   . PHE A 1 1187 ? 119.994 106.041 73.470  1.00 22.31 ?  1187 PHE A CB   1 
ATOM   7860  C CG   . PHE A 1 1187 ? 119.298 105.936 74.796  1.00 19.97 ?  1187 PHE A CG   1 
ATOM   7861  C CD1  . PHE A 1 1187 ? 118.044 105.358 74.891  1.00 20.24 ?  1187 PHE A CD1  1 
ATOM   7862  C CD2  . PHE A 1 1187 ? 119.897 106.418 75.947  1.00 17.52 ?  1187 PHE A CD2  1 
ATOM   7863  C CE1  . PHE A 1 1187 ? 117.398 105.264 76.110  1.00 16.63 ?  1187 PHE A CE1  1 
ATOM   7864  C CE2  . PHE A 1 1187 ? 119.257 106.325 77.168  1.00 16.97 ?  1187 PHE A CE2  1 
ATOM   7865  C CZ   . PHE A 1 1187 ? 118.007 105.748 77.248  1.00 13.04 ?  1187 PHE A CZ   1 
ATOM   7866  N N    . VAL A 1 1188 ? 118.223 108.933 72.847  1.00 22.45 ?  1188 VAL A N    1 
ATOM   7867  C CA   . VAL A 1 1188 ? 118.179 110.387 72.932  1.00 20.91 ?  1188 VAL A CA   1 
ATOM   7868  C C    . VAL A 1 1188 ? 117.710 110.770 74.329  1.00 17.02 ?  1188 VAL A C    1 
ATOM   7869  O O    . VAL A 1 1188 ? 116.748 110.192 74.848  1.00 19.39 ?  1188 VAL A O    1 
ATOM   7870  C CB   . VAL A 1 1188 ? 117.263 110.992 71.851  1.00 24.31 ?  1188 VAL A CB   1 
ATOM   7871  C CG1  . VAL A 1 1188 ? 117.968 110.997 70.507  1.00 17.96 ?  1188 VAL A CG1  1 
ATOM   7872  C CG2  . VAL A 1 1188 ? 115.957 110.214 71.750  1.00 22.95 ?  1188 VAL A CG2  1 
ATOM   7873  N N    . VAL A 1 1189 ? 118.400 111.728 74.942  1.00 12.25 ?  1189 VAL A N    1 
ATOM   7874  C CA   . VAL A 1 1189 ? 118.084 112.195 76.287  1.00 17.91 ?  1189 VAL A CA   1 
ATOM   7875  C C    . VAL A 1 1189 ? 117.721 113.670 76.213  1.00 21.58 ?  1189 VAL A C    1 
ATOM   7876  O O    . VAL A 1 1189 ? 118.479 114.471 75.655  1.00 18.68 ?  1189 VAL A O    1 
ATOM   7877  C CB   . VAL A 1 1189 ? 119.259 111.979 77.259  1.00 18.20 ?  1189 VAL A CB   1 
ATOM   7878  C CG1  . VAL A 1 1189 ? 118.809 112.227 78.689  1.00 14.11 ?  1189 VAL A CG1  1 
ATOM   7879  C CG2  . VAL A 1 1189 ? 119.834 110.581 77.107  1.00 21.80 ?  1189 VAL A CG2  1 
ATOM   7880  N N    . ARG A 1 1190 ? 116.570 114.025 76.777  1.00 25.34 ?  1190 ARG A N    1 
ATOM   7881  C CA   . ARG A 1 1190 ? 116.152 115.415 76.853  1.00 23.83 ?  1190 ARG A CA   1 
ATOM   7882  C C    . ARG A 1 1190 ? 116.826 116.106 78.038  1.00 21.23 ?  1190 ARG A C    1 
ATOM   7883  O O    . ARG A 1 1190 ? 117.418 115.465 78.911  1.00 26.44 ?  1190 ARG A O    1 
ATOM   7884  C CB   . ARG A 1 1190 ? 114.631 115.509 76.980  1.00 21.81 ?  1190 ARG A CB   1 
ATOM   7885  C CG   . ARG A 1 1190 ? 113.848 115.243 75.696  1.00 22.09 ?  1190 ARG A CG   1 
ATOM   7886  C CD   . ARG A 1 1190 ? 114.615 115.639 74.441  1.00 19.96 ?  1190 ARG A CD   1 
ATOM   7887  N NE   . ARG A 1 1190 ? 113.838 115.384 73.234  1.00 23.71 ?  1190 ARG A NE   1 
ATOM   7888  C CZ   . ARG A 1 1190 ? 114.322 115.452 72.002  1.00 25.41 ?  1190 ARG A CZ   1 
ATOM   7889  N NH1  . ARG A 1 1190 ? 115.583 115.775 71.771  1.00 21.54 ?  1190 ARG A NH1  1 
ATOM   7890  N NH2  . ARG A 1 1190 ? 113.519 115.190 70.974  1.00 24.99 ?  1190 ARG A NH2  1 
ATOM   7891  N N    . ASN A 1 1191 ? 116.732 117.434 78.068  1.00 18.07 ?  1191 ASN A N    1 
ATOM   7892  C CA   . ASN A 1 1191 ? 117.223 118.173 79.221  1.00 19.29 ?  1191 ASN A CA   1 
ATOM   7893  C C    . ASN A 1 1191 ? 116.194 118.120 80.349  1.00 21.71 ?  1191 ASN A C    1 
ATOM   7894  O O    . ASN A 1 1191 ? 115.092 117.586 80.200  1.00 20.39 ?  1191 ASN A O    1 
ATOM   7895  C CB   . ASN A 1 1191 ? 117.566 119.615 78.844  1.00 22.69 ?  1191 ASN A CB   1 
ATOM   7896  C CG   . ASN A 1 1191 ? 116.467 120.304 78.051  1.00 26.07 ?  1191 ASN A CG   1 
ATOM   7897  O OD1  . ASN A 1 1191 ? 115.277 120.113 78.301  1.00 23.84 ?  1191 ASN A OD1  1 
ATOM   7898  N ND2  . ASN A 1 1191 ? 116.870 121.137 77.099  1.00 20.63 ?  1191 ASN A ND2  1 
ATOM   7899  N N    . ALA A 1 1192 ? 116.558 118.690 81.497  1.00 22.24 ?  1192 ALA A N    1 
ATOM   7900  C CA   . ALA A 1 1192 ? 115.678 118.672 82.657  1.00 22.96 ?  1192 ALA A CA   1 
ATOM   7901  C C    . ALA A 1 1192 ? 114.508 119.626 82.458  1.00 26.14 ?  1192 ALA A C    1 
ATOM   7902  O O    . ALA A 1 1192 ? 114.621 120.819 82.758  1.00 28.32 ?  1192 ALA A O    1 
ATOM   7903  C CB   . ALA A 1 1192 ? 116.454 119.033 83.925  1.00 22.60 ?  1192 ALA A CB   1 
ATOM   7904  N N    . GLU A 1 1193 ? 113.391 119.088 81.959  1.00 26.23 ?  1193 GLU A N    1 
ATOM   7905  C CA   . GLU A 1 1193 ? 112.141 119.801 81.649  1.00 26.22 ?  1193 GLU A CA   1 
ATOM   7906  C C    . GLU A 1 1193 ? 112.341 121.174 81.004  1.00 27.22 ?  1193 GLU A C    1 
ATOM   7907  O O    . GLU A 1 1193 ? 112.309 121.306 79.781  1.00 28.13 ?  1193 GLU A O    1 
ATOM   7908  C CB   . GLU A 1 1193 ? 111.274 119.941 82.912  1.00 22.21 ?  1193 GLU A CB   1 
ATOM   7909  C CG   . GLU A 1 1193 ? 111.676 121.045 83.881  1.00 26.61 ?  1193 GLU A CG   1 
ATOM   7910  C CD   . GLU A 1 1193 ? 110.829 122.294 83.728  1.00 27.33 ?  1193 GLU A CD   1 
ATOM   7911  O OE1  . GLU A 1 1193 ? 109.770 122.219 83.070  1.00 28.51 ?  1193 GLU A OE1  1 
ATOM   7912  O OE2  . GLU A 1 1193 ? 111.223 123.350 84.266  1.00 29.72 ?  1193 GLU A OE2  1 
ATOM   7913  N N    . ALA B 1 74   ? 118.425 112.441 157.250 1.00 19.66 ?  74   ALA B N    1 
ATOM   7914  C CA   . ALA B 1 74   ? 118.820 112.821 155.899 1.00 18.48 ?  74   ALA B CA   1 
ATOM   7915  C C    . ALA B 1 74   ? 117.675 112.599 154.918 1.00 14.97 ?  74   ALA B C    1 
ATOM   7916  O O    . ALA B 1 74   ? 117.164 111.485 154.804 1.00 19.80 ?  74   ALA B O    1 
ATOM   7917  C CB   . ALA B 1 74   ? 120.048 112.041 155.466 1.00 19.84 ?  74   ALA B CB   1 
ATOM   7918  N N    . PRO B 1 75   ? 117.268 113.663 154.223 1.00 14.45 ?  75   PRO B N    1 
ATOM   7919  C CA   . PRO B 1 75   ? 116.167 113.540 153.260 1.00 14.01 ?  75   PRO B CA   1 
ATOM   7920  C C    . PRO B 1 75   ? 116.527 112.628 152.096 1.00 14.71 ?  75   PRO B C    1 
ATOM   7921  O O    . PRO B 1 75   ? 117.683 112.537 151.679 1.00 13.53 ?  75   PRO B O    1 
ATOM   7922  C CB   . PRO B 1 75   ? 115.946 114.982 152.789 1.00 11.24 ?  75   PRO B CB   1 
ATOM   7923  C CG   . PRO B 1 75   ? 116.520 115.829 153.878 1.00 13.02 ?  75   PRO B CG   1 
ATOM   7924  C CD   . PRO B 1 75   ? 117.693 115.061 154.400 1.00 14.32 ?  75   PRO B CD   1 
ATOM   7925  N N    . LYS B 1 76   ? 115.509 111.949 151.571 1.00 8.89  ?  76   LYS B N    1 
ATOM   7926  C CA   . LYS B 1 76   ? 115.658 111.014 150.460 1.00 9.21  ?  76   LYS B CA   1 
ATOM   7927  C C    . LYS B 1 76   ? 114.904 111.581 149.264 1.00 9.61  ?  76   LYS B C    1 
ATOM   7928  O O    . LYS B 1 76   ? 113.671 111.662 149.283 1.00 17.80 ?  76   LYS B O    1 
ATOM   7929  C CB   . LYS B 1 76   ? 115.130 109.634 150.842 1.00 13.08 ?  76   LYS B CB   1 
ATOM   7930  C CG   . LYS B 1 76   ? 115.406 109.247 152.286 1.00 14.41 ?  76   LYS B CG   1 
ATOM   7931  C CD   . LYS B 1 76   ? 114.943 107.833 152.583 1.00 13.81 ?  76   LYS B CD   1 
ATOM   7932  C CE   . LYS B 1 76   ? 115.766 107.208 153.697 1.00 9.60  ?  76   LYS B CE   1 
ATOM   7933  N NZ   . LYS B 1 76   ? 117.157 106.901 153.268 1.00 14.95 ?  76   LYS B NZ   1 
ATOM   7934  N N    . VAL B 1 77   ? 115.641 111.975 148.227 1.00 6.32  ?  77   VAL B N    1 
ATOM   7935  C CA   . VAL B 1 77   ? 115.052 112.628 147.062 1.00 0.46  ?  77   VAL B CA   1 
ATOM   7936  C C    . VAL B 1 77   ? 115.393 111.941 145.749 1.00 5.41  ?  77   VAL B C    1 
ATOM   7937  O O    . VAL B 1 77   ? 114.724 112.216 144.743 1.00 15.81 ?  77   VAL B O    1 
ATOM   7938  C CB   . VAL B 1 77   ? 115.451 114.119 146.984 1.00 3.19  ?  77   VAL B CB   1 
ATOM   7939  C CG1  . VAL B 1 77   ? 115.126 114.846 148.282 1.00 10.05 ?  77   VAL B CG1  1 
ATOM   7940  C CG2  . VAL B 1 77   ? 116.924 114.259 146.642 1.00 6.09  ?  77   VAL B CG2  1 
ATOM   7941  N N    . ILE B 1 78   ? 116.398 111.061 145.714 1.00 3.03  ?  78   ILE B N    1 
ATOM   7942  C CA   . ILE B 1 78   ? 116.878 110.508 144.447 1.00 0.32  ?  78   ILE B CA   1 
ATOM   7943  C C    . ILE B 1 78   ? 115.798 109.673 143.769 1.00 0.00  ?  78   ILE B C    1 
ATOM   7944  O O    . ILE B 1 78   ? 115.566 109.797 142.558 1.00 0.00  ?  78   ILE B O    1 
ATOM   7945  C CB   . ILE B 1 78   ? 118.164 109.693 144.683 1.00 0.78  ?  78   ILE B CB   1 
ATOM   7946  C CG1  . ILE B 1 78   ? 119.363 110.624 144.851 1.00 3.69  ?  78   ILE B CG1  1 
ATOM   7947  C CG2  . ILE B 1 78   ? 118.413 108.708 143.551 1.00 0.99  ?  78   ILE B CG2  1 
ATOM   7948  C CD1  . ILE B 1 78   ? 120.518 109.991 145.578 1.00 2.59  ?  78   ILE B CD1  1 
ATOM   7949  N N    . VAL B 1 79   ? 115.108 108.830 144.541 1.00 2.78  ?  79   VAL B N    1 
ATOM   7950  C CA   . VAL B 1 79   ? 114.121 107.920 143.968 1.00 1.16  ?  79   VAL B CA   1 
ATOM   7951  C C    . VAL B 1 79   ? 112.945 108.692 143.385 1.00 0.00  ?  79   VAL B C    1 
ATOM   7952  O O    . VAL B 1 79   ? 112.468 108.375 142.291 1.00 3.70  ?  79   VAL B O    1 
ATOM   7953  C CB   . VAL B 1 79   ? 113.668 106.895 145.025 1.00 3.19  ?  79   VAL B CB   1 
ATOM   7954  C CG1  . VAL B 1 79   ? 112.515 106.053 144.502 1.00 4.61  ?  79   VAL B CG1  1 
ATOM   7955  C CG2  . VAL B 1 79   ? 114.834 106.008 145.428 1.00 0.00  ?  79   VAL B CG2  1 
ATOM   7956  N N    . PHE B 1 80   ? 112.475 109.729 144.085 1.00 1.11  ?  80   PHE B N    1 
ATOM   7957  C CA   . PHE B 1 80   ? 111.325 110.491 143.604 1.00 0.00  ?  80   PHE B CA   1 
ATOM   7958  C C    . PHE B 1 80   ? 111.640 111.223 142.303 1.00 0.00  ?  80   PHE B C    1 
ATOM   7959  O O    . PHE B 1 80   ? 110.860 111.161 141.348 1.00 4.29  ?  80   PHE B O    1 
ATOM   7960  C CB   . PHE B 1 80   ? 110.853 111.472 144.678 1.00 0.06  ?  80   PHE B CB   1 
ATOM   7961  C CG   . PHE B 1 80   ? 109.488 112.051 144.416 1.00 3.27  ?  80   PHE B CG   1 
ATOM   7962  C CD1  . PHE B 1 80   ? 108.352 111.429 144.903 1.00 1.59  ?  80   PHE B CD1  1 
ATOM   7963  C CD2  . PHE B 1 80   ? 109.342 113.228 143.697 1.00 11.13 ?  80   PHE B CD2  1 
ATOM   7964  C CE1  . PHE B 1 80   ? 107.098 111.962 144.665 1.00 3.07  ?  80   PHE B CE1  1 
ATOM   7965  C CE2  . PHE B 1 80   ? 108.090 113.764 143.458 1.00 0.81  ?  80   PHE B CE2  1 
ATOM   7966  C CZ   . PHE B 1 80   ? 106.969 113.130 143.944 1.00 0.89  ?  80   PHE B CZ   1 
ATOM   7967  N N    . ILE B 1 81   ? 112.784 111.911 142.240 1.00 0.00  ?  81   ILE B N    1 
ATOM   7968  C CA   . ILE B 1 81   ? 113.149 112.640 141.026 1.00 0.00  ?  81   ILE B CA   1 
ATOM   7969  C C    . ILE B 1 81   ? 113.397 111.680 139.867 1.00 6.34  ?  81   ILE B C    1 
ATOM   7970  O O    . ILE B 1 81   ? 112.947 111.922 138.737 1.00 11.76 ?  81   ILE B O    1 
ATOM   7971  C CB   . ILE B 1 81   ? 114.373 113.540 141.283 1.00 0.00  ?  81   ILE B CB   1 
ATOM   7972  C CG1  . ILE B 1 81   ? 114.168 114.402 142.531 1.00 0.00  ?  81   ILE B CG1  1 
ATOM   7973  C CG2  . ILE B 1 81   ? 114.663 114.408 140.068 1.00 2.63  ?  81   ILE B CG2  1 
ATOM   7974  C CD1  . ILE B 1 81   ? 113.235 115.566 142.337 1.00 0.00  ?  81   ILE B CD1  1 
ATOM   7975  N N    . SER B 1 82   ? 114.117 110.580 140.120 1.00 4.36  ?  82   SER B N    1 
ATOM   7976  C CA   . SER B 1 82   ? 114.408 109.621 139.057 1.00 0.00  ?  82   SER B CA   1 
ATOM   7977  C C    . SER B 1 82   ? 113.139 108.954 138.541 1.00 1.59  ?  82   SER B C    1 
ATOM   7978  O O    . SER B 1 82   ? 112.964 108.794 137.326 1.00 7.39  ?  82   SER B O    1 
ATOM   7979  C CB   . SER B 1 82   ? 115.397 108.572 139.559 1.00 5.35  ?  82   SER B CB   1 
ATOM   7980  O OG   . SER B 1 82   ? 116.388 109.159 140.383 1.00 11.91 ?  82   SER B OG   1 
ATOM   7981  N N    . GLY B 1 83   ? 112.240 108.561 139.447 1.00 2.88  ?  83   GLY B N    1 
ATOM   7982  C CA   . GLY B 1 83   ? 110.972 107.996 139.032 1.00 6.15  ?  83   GLY B CA   1 
ATOM   7983  C C    . GLY B 1 83   ? 110.088 108.988 138.310 1.00 9.93  ?  83   GLY B C    1 
ATOM   7984  O O    . GLY B 1 83   ? 109.366 108.611 137.388 1.00 14.39 ?  83   GLY B O    1 
ATOM   7985  N N    . SER B 1 84   ? 110.130 110.262 138.711 1.00 8.84  ?  84   SER B N    1 
ATOM   7986  C CA   . SER B 1 84   ? 109.384 111.286 137.990 1.00 8.41  ?  84   SER B CA   1 
ATOM   7987  C C    . SER B 1 84   ? 109.902 111.443 136.569 1.00 9.49  ?  84   SER B C    1 
ATOM   7988  O O    . SER B 1 84   ? 109.113 111.556 135.626 1.00 16.15 ?  84   SER B O    1 
ATOM   7989  C CB   . SER B 1 84   ? 109.458 112.617 138.739 1.00 8.89  ?  84   SER B CB   1 
ATOM   7990  O OG   . SER B 1 84   ? 108.372 112.758 139.637 1.00 9.27  ?  84   SER B OG   1 
ATOM   7991  N N    . CYS B 1 85   ? 111.227 111.430 136.394 1.00 4.65  ?  85   CYS B N    1 
ATOM   7992  C CA   . CYS B 1 85   ? 111.802 111.510 135.052 1.00 2.45  ?  85   CYS B CA   1 
ATOM   7993  C C    . CYS B 1 85   ? 111.408 110.301 134.209 1.00 4.74  ?  85   CYS B C    1 
ATOM   7994  O O    . CYS B 1 85   ? 110.998 110.441 133.047 1.00 10.46 ?  85   CYS B O    1 
ATOM   7995  C CB   . CYS B 1 85   ? 113.324 111.623 135.145 1.00 7.55  ?  85   CYS B CB   1 
ATOM   7996  S SG   . CYS B 1 85   ? 113.956 113.305 135.314 1.00 11.49 ?  85   CYS B SG   1 
ATOM   7997  N N    . LEU B 1 86   ? 111.509 109.101 134.791 1.00 7.76  ?  86   LEU B N    1 
ATOM   7998  C CA   . LEU B 1 86   ? 111.178 107.878 134.062 1.00 7.19  ?  86   LEU B CA   1 
ATOM   7999  C C    . LEU B 1 86   ? 109.699 107.827 133.692 1.00 7.78  ?  86   LEU B C    1 
ATOM   8000  O O    . LEU B 1 86   ? 109.349 107.472 132.560 1.00 13.04 ?  86   LEU B O    1 
ATOM   8001  C CB   . LEU B 1 86   ? 111.569 106.659 134.898 1.00 11.19 ?  86   LEU B CB   1 
ATOM   8002  C CG   . LEU B 1 86   ? 110.946 105.306 134.556 1.00 13.18 ?  86   LEU B CG   1 
ATOM   8003  C CD1  . LEU B 1 86   ? 111.760 104.597 133.486 1.00 9.34  ?  86   LEU B CD1  1 
ATOM   8004  C CD2  . LEU B 1 86   ? 110.829 104.445 135.803 1.00 10.83 ?  86   LEU B CD2  1 
ATOM   8005  N N    . PHE B 1 87   ? 108.817 108.190 134.627 1.00 6.45  ?  87   PHE B N    1 
ATOM   8006  C CA   . PHE B 1 87   ? 107.386 108.177 134.356 1.00 2.13  ?  87   PHE B CA   1 
ATOM   8007  C C    . PHE B 1 87   ? 106.989 109.265 133.372 1.00 0.00  ?  87   PHE B C    1 
ATOM   8008  O O    . PHE B 1 87   ? 106.074 109.060 132.569 1.00 10.32 ?  87   PHE B O    1 
ATOM   8009  C CB   . PHE B 1 87   ? 106.602 108.332 135.657 1.00 10.23 ?  87   PHE B CB   1 
ATOM   8010  C CG   . PHE B 1 87   ? 106.647 107.119 136.541 1.00 16.29 ?  87   PHE B CG   1 
ATOM   8011  C CD1  . PHE B 1 87   ? 106.761 105.851 135.998 1.00 14.19 ?  87   PHE B CD1  1 
ATOM   8012  C CD2  . PHE B 1 87   ? 106.567 107.249 137.917 1.00 9.74  ?  87   PHE B CD2  1 
ATOM   8013  C CE1  . PHE B 1 87   ? 106.802 104.736 136.813 1.00 11.25 ?  87   PHE B CE1  1 
ATOM   8014  C CE2  . PHE B 1 87   ? 106.607 106.139 138.736 1.00 9.36  ?  87   PHE B CE2  1 
ATOM   8015  C CZ   . PHE B 1 87   ? 106.724 104.881 138.183 1.00 12.16 ?  87   PHE B CZ   1 
ATOM   8016  N N    . GLY B 1 88   ? 107.650 110.425 133.419 1.00 1.18  ?  88   GLY B N    1 
ATOM   8017  C CA   . GLY B 1 88   ? 107.407 111.441 132.413 1.00 0.46  ?  88   GLY B CA   1 
ATOM   8018  C C    . GLY B 1 88   ? 107.794 110.975 131.026 1.00 0.08  ?  88   GLY B C    1 
ATOM   8019  O O    . GLY B 1 88   ? 107.059 111.197 130.063 1.00 5.50  ?  88   GLY B O    1 
ATOM   8020  N N    . ALA B 1 89   ? 108.938 110.293 130.912 1.00 3.70  ?  89   ALA B N    1 
ATOM   8021  C CA   . ALA B 1 89   ? 109.334 109.717 129.629 1.00 2.80  ?  89   ALA B CA   1 
ATOM   8022  C C    . ALA B 1 89   ? 108.333 108.670 129.153 1.00 0.20  ?  89   ALA B C    1 
ATOM   8023  O O    . ALA B 1 89   ? 107.966 108.643 127.971 1.00 3.94  ?  89   ALA B O    1 
ATOM   8024  C CB   . ALA B 1 89   ? 110.729 109.106 129.740 1.00 6.55  ?  89   ALA B CB   1 
ATOM   8025  N N    . ILE B 1 90   ? 107.870 107.810 130.065 1.00 3.39  ?  90   ILE B N    1 
ATOM   8026  C CA   . ILE B 1 90   ? 106.941 106.742 129.696 1.00 2.04  ?  90   ILE B CA   1 
ATOM   8027  C C    . ILE B 1 90   ? 105.612 107.325 129.225 1.00 3.94  ?  90   ILE B C    1 
ATOM   8028  O O    . ILE B 1 90   ? 105.088 106.946 128.171 1.00 11.49 ?  90   ILE B O    1 
ATOM   8029  C CB   . ILE B 1 90   ? 106.746 105.774 130.877 1.00 4.41  ?  90   ILE B CB   1 
ATOM   8030  C CG1  . ILE B 1 90   ? 107.950 104.841 131.008 1.00 9.56  ?  90   ILE B CG1  1 
ATOM   8031  C CG2  . ILE B 1 90   ? 105.468 104.965 130.715 1.00 6.35  ?  90   ILE B CG2  1 
ATOM   8032  C CD1  . ILE B 1 90   ? 107.994 104.093 132.318 1.00 7.57  ?  90   ILE B CD1  1 
ATOM   8033  N N    . SER B 1 91   ? 105.055 108.265 129.994 1.00 3.81  ?  91   SER B N    1 
ATOM   8034  C CA   . SER B 1 91   ? 103.784 108.879 129.625 1.00 0.00  ?  91   SER B CA   1 
ATOM   8035  C C    . SER B 1 91   ? 103.910 109.729 128.368 1.00 0.00  ?  91   SER B C    1 
ATOM   8036  O O    . SER B 1 91   ? 102.956 109.822 127.589 1.00 2.20  ?  91   SER B O    1 
ATOM   8037  C CB   . SER B 1 91   ? 103.254 109.723 130.782 1.00 3.59  ?  91   SER B CB   1 
ATOM   8038  O OG   . SER B 1 91   ? 103.359 109.028 132.012 1.00 13.07 ?  91   SER B OG   1 
ATOM   8039  N N    . ARG B 1 92   ? 105.067 110.359 128.158 1.00 4.93  ?  92   ARG B N    1 
ATOM   8040  C CA   . ARG B 1 92   ? 105.270 111.178 126.971 1.00 1.62  ?  92   ARG B CA   1 
ATOM   8041  C C    . ARG B 1 92   ? 105.353 110.316 125.718 1.00 7.57  ?  92   ARG B C    1 
ATOM   8042  O O    . ARG B 1 92   ? 104.771 110.653 124.681 1.00 8.25  ?  92   ARG B O    1 
ATOM   8043  C CB   . ARG B 1 92   ? 106.540 112.011 127.144 1.00 0.00  ?  92   ARG B CB   1 
ATOM   8044  C CG   . ARG B 1 92   ? 106.536 113.357 126.452 1.00 1.57  ?  92   ARG B CG   1 
ATOM   8045  C CD   . ARG B 1 92   ? 107.711 114.190 126.934 1.00 0.00  ?  92   ARG B CD   1 
ATOM   8046  N NE   . ARG B 1 92   ? 108.164 115.155 125.941 1.00 0.00  ?  92   ARG B NE   1 
ATOM   8047  C CZ   . ARG B 1 92   ? 107.660 116.373 125.798 1.00 5.66  ?  92   ARG B CZ   1 
ATOM   8048  N NH1  . ARG B 1 92   ? 106.686 116.814 126.576 1.00 6.23  ?  92   ARG B NH1  1 
ATOM   8049  N NH2  . ARG B 1 92   ? 108.150 117.171 124.853 1.00 10.21 ?  92   ARG B NH2  1 
ATOM   8050  N N    . SER B 1 93   ? 106.071 109.192 125.797 1.00 13.42 ?  93   SER B N    1 
ATOM   8051  C CA   . SER B 1 93   ? 106.235 108.341 124.622 1.00 10.07 ?  93   SER B CA   1 
ATOM   8052  C C    . SER B 1 93   ? 104.979 107.526 124.338 1.00 6.32  ?  93   SER B C    1 
ATOM   8053  O O    . SER B 1 93   ? 104.627 107.307 123.173 1.00 6.41  ?  93   SER B O    1 
ATOM   8054  C CB   . SER B 1 93   ? 107.438 107.418 124.807 1.00 9.43  ?  93   SER B CB   1 
ATOM   8055  O OG   . SER B 1 93   ? 108.617 108.161 125.065 1.00 8.62  ?  93   SER B OG   1 
ATOM   8056  N N    . LEU B 1 94   ? 104.289 107.069 125.381 1.00 8.32  ?  94   LEU B N    1 
ATOM   8057  C CA   . LEU B 1 94   ? 103.168 106.155 125.214 1.00 6.01  ?  94   LEU B CA   1 
ATOM   8058  C C    . LEU B 1 94   ? 101.853 106.869 124.913 1.00 8.97  ?  94   LEU B C    1 
ATOM   8059  O O    . LEU B 1 94   ? 100.892 106.214 124.497 1.00 9.36  ?  94   LEU B O    1 
ATOM   8060  C CB   . LEU B 1 94   ? 103.031 105.285 126.473 1.00 6.81  ?  94   LEU B CB   1 
ATOM   8061  C CG   . LEU B 1 94   ? 102.123 104.052 126.498 1.00 8.89  ?  94   LEU B CG   1 
ATOM   8062  C CD1  . LEU B 1 94   ? 102.861 102.886 127.135 1.00 9.82  ?  94   LEU B CD1  1 
ATOM   8063  C CD2  . LEU B 1 94   ? 100.831 104.326 127.240 1.00 7.71  ?  94   LEU B CD2  1 
ATOM   8064  N N    . PHE B 1 95   ? 101.789 108.190 125.085 1.00 13.37 ?  95   PHE B N    1 
ATOM   8065  C CA   . PHE B 1 95   ? 100.578 108.957 124.812 1.00 6.61  ?  95   PHE B CA   1 
ATOM   8066  C C    . PHE B 1 95   ? 100.783 109.956 123.677 1.00 12.74 ?  95   PHE B C    1 
ATOM   8067  O O    . PHE B 1 95   ? 100.125 110.998 123.635 1.00 13.07 ?  95   PHE B O    1 
ATOM   8068  C CB   . PHE B 1 95   ? 100.094 109.683 126.067 1.00 5.65  ?  95   PHE B CB   1 
ATOM   8069  C CG   . PHE B 1 95   ? 99.170  108.868 126.922 1.00 9.02  ?  95   PHE B CG   1 
ATOM   8070  C CD1  . PHE B 1 95   ? 99.628  107.742 127.583 1.00 11.88 ?  95   PHE B CD1  1 
ATOM   8071  C CD2  . PHE B 1 95   ? 97.841  109.222 127.058 1.00 12.44 ?  95   PHE B CD2  1 
ATOM   8072  C CE1  . PHE B 1 95   ? 98.778  106.991 128.371 1.00 15.57 ?  95   PHE B CE1  1 
ATOM   8073  C CE2  . PHE B 1 95   ? 96.985  108.473 127.842 1.00 10.47 ?  95   PHE B CE2  1 
ATOM   8074  C CZ   . PHE B 1 95   ? 97.454  107.355 128.497 1.00 15.71 ?  95   PHE B CZ   1 
ATOM   8075  N N    . LYS B 1 96   ? 101.705 109.658 122.758 1.00 12.73 ?  96   LYS B N    1 
ATOM   8076  C CA   . LYS B 1 96   ? 101.931 110.541 121.617 1.00 12.24 ?  96   LYS B CA   1 
ATOM   8077  C C    . LYS B 1 96   ? 100.733 110.544 120.675 1.00 17.62 ?  96   LYS B C    1 
ATOM   8078  O O    . LYS B 1 96   ? 100.271 111.606 120.242 1.00 19.09 ?  96   LYS B O    1 
ATOM   8079  C CB   . LYS B 1 96   ? 103.192 110.114 120.864 1.00 15.97 ?  96   LYS B CB   1 
ATOM   8080  C CG   . LYS B 1 96   ? 104.470 110.783 121.331 1.00 20.71 ?  96   LYS B CG   1 
ATOM   8081  C CD   . LYS B 1 96   ? 105.589 110.590 120.316 1.00 21.09 ?  96   LYS B CD   1 
ATOM   8082  C CE   . LYS B 1 96   ? 106.561 109.508 120.760 1.00 17.43 ?  96   LYS B CE   1 
ATOM   8083  N NZ   . LYS B 1 96   ? 107.955 109.786 120.314 1.00 15.41 ?  96   LYS B NZ   1 
ATOM   8084  N N    . LYS B 1 97   ? 100.222 109.358 120.340 1.00 15.20 ?  97   LYS B N    1 
ATOM   8085  C CA   . LYS B 1 97   ? 99.143  109.250 119.366 1.00 13.51 ?  97   LYS B CA   1 
ATOM   8086  C C    . LYS B 1 97   ? 97.788  109.620 119.955 1.00 16.95 ?  97   LYS B C    1 
ATOM   8087  O O    . LYS B 1 97   ? 96.921  110.120 119.230 1.00 19.64 ?  97   LYS B O    1 
ATOM   8088  C CB   . LYS B 1 97   ? 99.094  107.831 118.797 1.00 16.47 ?  97   LYS B CB   1 
ATOM   8089  C CG   . LYS B 1 97   ? 100.353 107.408 118.049 1.00 17.43 ?  97   LYS B CG   1 
ATOM   8090  C CD   . LYS B 1 97   ? 100.881 108.514 117.148 1.00 14.95 ?  97   LYS B CD   1 
ATOM   8091  C CE   . LYS B 1 97   ? 102.383 108.388 116.950 1.00 16.32 ?  97   LYS B CE   1 
ATOM   8092  N NZ   . LYS B 1 97   ? 102.949 109.563 116.234 1.00 15.63 ?  97   LYS B NZ   1 
ATOM   8093  N N    . LEU B 1 98   ? 97.585  109.372 121.246 1.00 18.75 ?  98   LEU B N    1 
ATOM   8094  C CA   . LEU B 1 98   ? 96.289  109.612 121.863 1.00 16.93 ?  98   LEU B CA   1 
ATOM   8095  C C    . LEU B 1 98   ? 95.982  111.108 121.902 1.00 17.29 ?  98   LEU B C    1 
ATOM   8096  O O    . LEU B 1 98   ? 96.893  111.926 122.065 1.00 17.40 ?  98   LEU B O    1 
ATOM   8097  C CB   . LEU B 1 98   ? 96.256  109.035 123.279 1.00 13.72 ?  98   LEU B CB   1 
ATOM   8098  C CG   . LEU B 1 98   ? 95.863  107.563 123.417 1.00 16.12 ?  98   LEU B CG   1 
ATOM   8099  C CD1  . LEU B 1 98   ? 97.063  106.654 123.199 1.00 17.99 ?  98   LEU B CD1  1 
ATOM   8100  C CD2  . LEU B 1 98   ? 95.229  107.306 124.775 1.00 17.59 ?  98   LEU B CD2  1 
ATOM   8101  N N    . PRO B 1 99   ? 94.712  111.499 121.752 1.00 17.21 ?  99   PRO B N    1 
ATOM   8102  C CA   . PRO B 1 99   ? 94.380  112.931 121.786 1.00 19.64 ?  99   PRO B CA   1 
ATOM   8103  C C    . PRO B 1 99   ? 94.493  113.554 123.166 1.00 17.74 ?  99   PRO B C    1 
ATOM   8104  O O    . PRO B 1 99   ? 94.657  114.777 123.260 1.00 16.51 ?  99   PRO B O    1 
ATOM   8105  C CB   . PRO B 1 99   ? 92.933  112.964 121.280 1.00 18.84 ?  99   PRO B CB   1 
ATOM   8106  C CG   . PRO B 1 99   ? 92.378  111.643 121.693 1.00 18.51 ?  99   PRO B CG   1 
ATOM   8107  C CD   . PRO B 1 99   ? 93.514  110.659 121.572 1.00 16.66 ?  99   PRO B CD   1 
ATOM   8108  N N    . ILE B 1 100  ? 94.410  112.763 124.231 1.00 16.00 ?  100  ILE B N    1 
ATOM   8109  C CA   . ILE B 1 100  ? 94.440  113.285 125.595 1.00 19.26 ?  100  ILE B CA   1 
ATOM   8110  C C    . ILE B 1 100  ? 95.866  113.738 125.902 1.00 19.28 ?  100  ILE B C    1 
ATOM   8111  O O    . ILE B 1 100  ? 96.826  113.177 125.349 1.00 17.78 ?  100  ILE B O    1 
ATOM   8112  C CB   . ILE B 1 100  ? 93.916  112.235 126.596 1.00 15.80 ?  100  ILE B CB   1 
ATOM   8113  C CG1  . ILE B 1 100  ? 93.067  112.890 127.687 1.00 17.30 ?  100  ILE B CG1  1 
ATOM   8114  C CG2  . ILE B 1 100  ? 95.042  111.438 127.234 1.00 15.84 ?  100  ILE B CG2  1 
ATOM   8115  C CD1  . ILE B 1 100  ? 92.215  111.910 128.456 1.00 20.34 ?  100  ILE B CD1  1 
ATOM   8116  N N    . PRO B 1 101  ? 96.056  114.782 126.707 1.00 14.27 ?  101  PRO B N    1 
ATOM   8117  C CA   . PRO B 1 101  ? 97.414  115.161 127.108 1.00 11.19 ?  101  PRO B CA   1 
ATOM   8118  C C    . PRO B 1 101  ? 98.027  114.139 128.051 1.00 8.60  ?  101  PRO B C    1 
ATOM   8119  O O    . PRO B 1 101  ? 97.329  113.431 128.779 1.00 10.14 ?  101  PRO B O    1 
ATOM   8120  C CB   . PRO B 1 101  ? 97.217  116.513 127.804 1.00 10.40 ?  101  PRO B CB   1 
ATOM   8121  C CG   . PRO B 1 101  ? 95.779  116.537 128.192 1.00 13.65 ?  101  PRO B CG   1 
ATOM   8122  C CD   . PRO B 1 101  ? 95.063  115.788 127.119 1.00 13.33 ?  101  PRO B CD   1 
ATOM   8123  N N    . TYR B 1 102  ? 99.358  114.070 128.028 1.00 4.16  ?  102  TYR B N    1 
ATOM   8124  C CA   . TYR B 1 102  ? 100.082 113.089 128.826 1.00 0.03  ?  102  TYR B CA   1 
ATOM   8125  C C    . TYR B 1 102  ? 100.203 113.482 130.291 1.00 7.06  ?  102  TYR B C    1 
ATOM   8126  O O    . TYR B 1 102  ? 100.598 112.643 131.107 1.00 10.47 ?  102  TYR B O    1 
ATOM   8127  C CB   . TYR B 1 102  ? 101.481 112.865 128.241 1.00 1.28  ?  102  TYR B CB   1 
ATOM   8128  C CG   . TYR B 1 102  ? 102.514 113.893 128.655 1.00 4.49  ?  102  TYR B CG   1 
ATOM   8129  C CD1  . TYR B 1 102  ? 102.603 115.118 128.009 1.00 3.40  ?  102  TYR B CD1  1 
ATOM   8130  C CD2  . TYR B 1 102  ? 103.426 113.620 129.668 1.00 3.85  ?  102  TYR B CD2  1 
ATOM   8131  C CE1  . TYR B 1 102  ? 103.550 116.053 128.380 1.00 0.00  ?  102  TYR B CE1  1 
ATOM   8132  C CE2  . TYR B 1 102  ? 104.374 114.547 130.044 1.00 5.44  ?  102  TYR B CE2  1 
ATOM   8133  C CZ   . TYR B 1 102  ? 104.433 115.761 129.397 1.00 4.04  ?  102  TYR B CZ   1 
ATOM   8134  O OH   . TYR B 1 102  ? 105.381 116.686 129.769 1.00 10.37 ?  102  TYR B OH   1 
ATOM   8135  N N    . THR B 1 103  ? 99.885  114.729 130.645 1.00 9.79  ?  103  THR B N    1 
ATOM   8136  C CA   . THR B 1 103  ? 100.073 115.188 132.016 1.00 1.26  ?  103  THR B CA   1 
ATOM   8137  C C    . THR B 1 103  ? 99.010  114.641 132.962 1.00 1.82  ?  103  THR B C    1 
ATOM   8138  O O    . THR B 1 103  ? 99.266  114.508 134.167 1.00 9.39  ?  103  THR B O    1 
ATOM   8139  C CB   . THR B 1 103  ? 100.088 116.716 132.055 1.00 0.21  ?  103  THR B CB   1 
ATOM   8140  O OG1  . THR B 1 103  ? 99.039  117.228 131.227 1.00 1.57  ?  103  THR B OG1  1 
ATOM   8141  C CG2  . THR B 1 103  ? 101.424 117.250 131.563 1.00 0.00  ?  103  THR B CG2  1 
ATOM   8142  N N    . VAL B 1 104  ? 97.823  114.311 132.447 1.00 0.13  ?  104  VAL B N    1 
ATOM   8143  C CA   . VAL B 1 104  ? 96.818  113.680 133.296 1.00 3.92  ?  104  VAL B CA   1 
ATOM   8144  C C    . VAL B 1 104  ? 97.278  112.288 133.717 1.00 8.68  ?  104  VAL B C    1 
ATOM   8145  O O    . VAL B 1 104  ? 96.936  111.816 134.808 1.00 16.25 ?  104  VAL B O    1 
ATOM   8146  C CB   . VAL B 1 104  ? 95.448  113.654 132.586 1.00 6.05  ?  104  VAL B CB   1 
ATOM   8147  C CG1  . VAL B 1 104  ? 95.449  112.699 131.403 1.00 6.97  ?  104  VAL B CG1  1 
ATOM   8148  C CG2  . VAL B 1 104  ? 94.343  113.296 133.568 1.00 6.09  ?  104  VAL B CG2  1 
ATOM   8149  N N    . VAL B 1 105  ? 98.087  111.627 132.885 1.00 5.17  ?  105  VAL B N    1 
ATOM   8150  C CA   . VAL B 1 105  ? 98.684  110.354 133.272 1.00 5.26  ?  105  VAL B CA   1 
ATOM   8151  C C    . VAL B 1 105  ? 99.641  110.558 134.436 1.00 8.20  ?  105  VAL B C    1 
ATOM   8152  O O    . VAL B 1 105  ? 99.700  109.741 135.363 1.00 11.17 ?  105  VAL B O    1 
ATOM   8153  C CB   . VAL B 1 105  ? 99.392  109.714 132.065 1.00 6.47  ?  105  VAL B CB   1 
ATOM   8154  C CG1  . VAL B 1 105  ? 99.699  108.252 132.340 1.00 11.72 ?  105  VAL B CG1  1 
ATOM   8155  C CG2  . VAL B 1 105  ? 98.552  109.883 130.813 1.00 7.11  ?  105  VAL B CG2  1 
ATOM   8156  N N    . LEU B 1 106  ? 100.401 111.657 134.403 1.00 7.35  ?  106  LEU B N    1 
ATOM   8157  C CA   . LEU B 1 106  ? 101.264 112.009 135.524 1.00 0.00  ?  106  LEU B CA   1 
ATOM   8158  C C    . LEU B 1 106  ? 100.441 112.227 136.784 1.00 0.00  ?  106  LEU B C    1 
ATOM   8159  O O    . LEU B 1 106  ? 100.840 111.811 137.879 1.00 7.59  ?  106  LEU B O    1 
ATOM   8160  C CB   . LEU B 1 106  ? 102.063 113.269 135.192 1.00 0.00  ?  106  LEU B CB   1 
ATOM   8161  C CG   . LEU B 1 106  ? 103.353 113.140 134.383 1.00 0.00  ?  106  LEU B CG   1 
ATOM   8162  C CD1  . LEU B 1 106  ? 103.721 114.476 133.754 1.00 0.84  ?  106  LEU B CD1  1 
ATOM   8163  C CD2  . LEU B 1 106  ? 104.485 112.628 135.238 1.00 2.31  ?  106  LEU B CD2  1 
ATOM   8164  N N    . LEU B 1 107  ? 99.275  112.864 136.640 1.00 0.00  ?  107  LEU B N    1 
ATOM   8165  C CA   . LEU B 1 107  ? 98.407  113.106 137.789 1.00 1.24  ?  107  LEU B CA   1 
ATOM   8166  C C    . LEU B 1 107  ? 97.881  111.807 138.396 1.00 8.61  ?  107  LEU B C    1 
ATOM   8167  O O    . LEU B 1 107  ? 97.901  111.638 139.621 1.00 11.52 ?  107  LEU B O    1 
ATOM   8168  C CB   . LEU B 1 107  ? 97.249  114.016 137.385 1.00 0.97  ?  107  LEU B CB   1 
ATOM   8169  C CG   . LEU B 1 107  ? 97.003  115.207 138.310 1.00 1.01  ?  107  LEU B CG   1 
ATOM   8170  C CD1  . LEU B 1 107  ? 98.281  115.977 138.513 1.00 4.90  ?  107  LEU B CD1  1 
ATOM   8171  C CD2  . LEU B 1 107  ? 95.939  116.113 137.741 1.00 3.26  ?  107  LEU B CD2  1 
ATOM   8172  N N    . ILE B 1 108  ? 97.409  110.874 137.561 1.00 11.44 ?  108  ILE B N    1 
ATOM   8173  C CA   . ILE B 1 108  ? 96.896  109.609 138.098 1.00 11.26 ?  108  ILE B CA   1 
ATOM   8174  C C    . ILE B 1 108  ? 98.022  108.769 138.694 1.00 9.42  ?  108  ILE B C    1 
ATOM   8175  O O    . ILE B 1 108  ? 97.827  108.085 139.708 1.00 12.29 ?  108  ILE B O    1 
ATOM   8176  C CB   . ILE B 1 108  ? 96.103  108.812 137.042 1.00 12.16 ?  108  ILE B CB   1 
ATOM   8177  C CG1  . ILE B 1 108  ? 95.173  109.707 136.223 1.00 10.72 ?  108  ILE B CG1  1 
ATOM   8178  C CG2  . ILE B 1 108  ? 95.302  107.698 137.702 1.00 13.12 ?  108  ILE B CG2  1 
ATOM   8179  C CD1  . ILE B 1 108  ? 94.191  110.518 137.052 1.00 6.44  ?  108  ILE B CD1  1 
ATOM   8180  N N    . LEU B 1 109  ? 99.209  108.790 138.078 1.00 6.14  ?  109  LEU B N    1 
ATOM   8181  C CA   . LEU B 1 109  ? 100.340 108.064 138.650 1.00 3.17  ?  109  LEU B CA   1 
ATOM   8182  C C    . LEU B 1 109  ? 100.722 108.628 140.014 1.00 5.96  ?  109  LEU B C    1 
ATOM   8183  O O    . LEU B 1 109  ? 100.982 107.870 140.959 1.00 12.28 ?  109  LEU B O    1 
ATOM   8184  C CB   . LEU B 1 109  ? 101.535 108.109 137.697 1.00 5.38  ?  109  LEU B CB   1 
ATOM   8185  C CG   . LEU B 1 109  ? 101.557 107.087 136.559 1.00 9.39  ?  109  LEU B CG   1 
ATOM   8186  C CD1  . LEU B 1 109  ? 102.465 107.558 135.432 1.00 7.49  ?  109  LEU B CD1  1 
ATOM   8187  C CD2  . LEU B 1 109  ? 101.992 105.722 137.068 1.00 9.73  ?  109  LEU B CD2  1 
ATOM   8188  N N    . GLY B 1 110  ? 100.742 109.959 140.140 1.00 6.12  ?  110  GLY B N    1 
ATOM   8189  C CA   . GLY B 1 110  ? 100.974 110.570 141.435 1.00 4.84  ?  110  GLY B CA   1 
ATOM   8190  C C    . GLY B 1 110  ? 99.892  110.250 142.446 1.00 8.30  ?  110  GLY B C    1 
ATOM   8191  O O    . GLY B 1 110  ? 100.178 110.098 143.632 1.00 14.39 ?  110  GLY B O    1 
ATOM   8192  N N    . ALA B 1 111  ? 98.641  110.137 141.994 1.00 7.97  ?  111  ALA B N    1 
ATOM   8193  C CA   . ALA B 1 111  ? 97.551  109.769 142.895 1.00 6.12  ?  111  ALA B CA   1 
ATOM   8194  C C    . ALA B 1 111  ? 97.719  108.350 143.431 1.00 13.16 ?  111  ALA B C    1 
ATOM   8195  O O    . ALA B 1 111  ? 97.517  108.100 144.630 1.00 11.79 ?  111  ALA B O    1 
ATOM   8196  C CB   . ALA B 1 111  ? 96.212  109.914 142.175 1.00 8.50  ?  111  ALA B CB   1 
ATOM   8197  N N    . ILE B 1 112  ? 98.075  107.409 142.552 1.00 20.50 ?  112  ILE B N    1 
ATOM   8198  C CA   . ILE B 1 112  ? 98.314  106.032 142.981 1.00 11.74 ?  112  ILE B CA   1 
ATOM   8199  C C    . ILE B 1 112  ? 99.490  105.972 143.949 1.00 9.35  ?  112  ILE B C    1 
ATOM   8200  O O    . ILE B 1 112  ? 99.426  105.295 144.986 1.00 15.36 ?  112  ILE B O    1 
ATOM   8201  C CB   . ILE B 1 112  ? 98.535  105.121 141.758 1.00 7.45  ?  112  ILE B CB   1 
ATOM   8202  C CG1  . ILE B 1 112  ? 97.293  105.107 140.863 1.00 8.91  ?  112  ILE B CG1  1 
ATOM   8203  C CG2  . ILE B 1 112  ? 98.885  103.710 142.195 1.00 11.60 ?  112  ILE B CG2  1 
ATOM   8204  C CD1  . ILE B 1 112  ? 96.014  104.747 141.589 1.00 13.21 ?  112  ILE B CD1  1 
ATOM   8205  N N    . LEU B 1 113  ? 100.572 106.694 143.637 1.00 6.40  ?  113  LEU B N    1 
ATOM   8206  C CA   . LEU B 1 113  ? 101.721 106.742 144.537 1.00 7.45  ?  113  LEU B CA   1 
ATOM   8207  C C    . LEU B 1 113  ? 101.347 107.362 145.879 1.00 8.02  ?  113  LEU B C    1 
ATOM   8208  O O    . LEU B 1 113  ? 101.843 106.936 146.928 1.00 14.00 ?  113  LEU B O    1 
ATOM   8209  C CB   . LEU B 1 113  ? 102.862 107.520 143.882 1.00 9.57  ?  113  LEU B CB   1 
ATOM   8210  C CG   . LEU B 1 113  ? 104.059 107.915 144.748 1.00 11.43 ?  113  LEU B CG   1 
ATOM   8211  C CD1  . LEU B 1 113  ? 105.050 106.768 144.844 1.00 12.41 ?  113  LEU B CD1  1 
ATOM   8212  C CD2  . LEU B 1 113  ? 104.728 109.162 144.195 1.00 10.84 ?  113  LEU B CD2  1 
ATOM   8213  N N    . GLY B 1 114  ? 100.462 108.359 145.865 1.00 7.76  ?  114  GLY B N    1 
ATOM   8214  C CA   . GLY B 1 114  ? 100.031 108.979 147.105 1.00 8.89  ?  114  GLY B CA   1 
ATOM   8215  C C    . GLY B 1 114  ? 99.224  108.048 147.985 1.00 13.69 ?  114  GLY B C    1 
ATOM   8216  O O    . GLY B 1 114  ? 99.428  108.003 149.200 1.00 16.79 ?  114  GLY B O    1 
ATOM   8217  N N    . VAL B 1 115  ? 98.300  107.290 147.390 1.00 17.97 ?  115  VAL B N    1 
ATOM   8218  C CA   . VAL B 1 115  ? 97.531  106.349 148.204 1.00 15.53 ?  115  VAL B CA   1 
ATOM   8219  C C    . VAL B 1 115  ? 98.425  105.208 148.700 1.00 15.76 ?  115  VAL B C    1 
ATOM   8220  O O    . VAL B 1 115  ? 98.252  104.721 149.828 1.00 15.24 ?  115  VAL B O    1 
ATOM   8221  C CB   . VAL B 1 115  ? 96.281  105.853 147.440 1.00 13.22 ?  115  VAL B CB   1 
ATOM   8222  C CG1  . VAL B 1 115  ? 96.575  104.660 146.539 1.00 12.50 ?  115  VAL B CG1  1 
ATOM   8223  C CG2  . VAL B 1 115  ? 95.165  105.523 148.419 1.00 12.55 ?  115  VAL B CG2  1 
ATOM   8224  N N    . VAL B 1 116  ? 99.421  104.801 147.903 1.00 11.35 ?  116  VAL B N    1 
ATOM   8225  C CA   . VAL B 1 116  ? 100.347 103.762 148.345 1.00 8.83  ?  116  VAL B CA   1 
ATOM   8226  C C    . VAL B 1 116  ? 101.192 104.258 149.515 1.00 13.43 ?  116  VAL B C    1 
ATOM   8227  O O    . VAL B 1 116  ? 101.378 103.545 150.509 1.00 20.39 ?  116  VAL B O    1 
ATOM   8228  C CB   . VAL B 1 116  ? 101.217 103.291 147.164 1.00 6.43  ?  116  VAL B CB   1 
ATOM   8229  C CG1  . VAL B 1 116  ? 102.443 102.540 147.656 1.00 10.33 ?  116  VAL B CG1  1 
ATOM   8230  C CG2  . VAL B 1 116  ? 100.400 102.417 146.227 1.00 6.17  ?  116  VAL B CG2  1 
ATOM   8231  N N    . ALA B 1 117  ? 101.702 105.490 149.424 1.00 11.29 ?  117  ALA B N    1 
ATOM   8232  C CA   . ALA B 1 117  ? 102.470 106.067 150.522 1.00 12.16 ?  117  ALA B CA   1 
ATOM   8233  C C    . ALA B 1 117  ? 101.608 106.288 151.757 1.00 14.34 ?  117  ALA B C    1 
ATOM   8234  O O    . ALA B 1 117  ? 102.099 106.161 152.884 1.00 14.30 ?  117  ALA B O    1 
ATOM   8235  C CB   . ALA B 1 117  ? 103.113 107.380 150.082 1.00 13.70 ?  117  ALA B CB   1 
ATOM   8236  N N    . SER B 1 118  ? 100.330 106.623 151.569 1.00 12.37 ?  118  SER B N    1 
ATOM   8237  C CA   . SER B 1 118  ? 99.418  106.708 152.702 1.00 15.30 ?  118  SER B CA   1 
ATOM   8238  C C    . SER B 1 118  ? 99.198  105.345 153.343 1.00 19.73 ?  118  SER B C    1 
ATOM   8239  O O    . SER B 1 118  ? 98.906  105.267 154.542 1.00 21.70 ?  118  SER B O    1 
ATOM   8240  C CB   . SER B 1 118  ? 98.085  107.311 152.261 1.00 17.55 ?  118  SER B CB   1 
ATOM   8241  O OG   . SER B 1 118  ? 97.245  107.557 153.374 1.00 18.14 ?  118  SER B OG   1 
ATOM   8242  N N    . ASN B 1 119  ? 99.333  104.266 152.571 1.00 21.11 ?  119  ASN B N    1 
ATOM   8243  C CA   . ASN B 1 119  ? 99.244  102.927 153.148 1.00 17.17 ?  119  ASN B CA   1 
ATOM   8244  C C    . ASN B 1 119  ? 100.609 102.407 153.605 1.00 16.71 ?  119  ASN B C    1 
ATOM   8245  O O    . ASN B 1 119  ? 100.794 102.092 154.784 1.00 14.91 ?  119  ASN B O    1 
ATOM   8246  C CB   . ASN B 1 119  ? 98.602  101.965 152.143 1.00 16.56 ?  119  ASN B CB   1 
ATOM   8247  C CG   . ASN B 1 119  ? 97.113  101.806 152.367 1.00 19.67 ?  119  ASN B CG   1 
ATOM   8248  O OD1  . ASN B 1 119  ? 96.533  102.455 153.237 1.00 18.13 ?  119  ASN B OD1  1 
ATOM   8249  N ND2  . ASN B 1 119  ? 96.484  100.940 151.581 1.00 24.42 ?  119  ASN B ND2  1 
ATOM   8250  N N    . VAL B 1 120  ? 101.568 102.317 152.688 1.00 18.01 ?  120  VAL B N    1 
ATOM   8251  C CA   . VAL B 1 120  ? 102.887 101.750 152.978 1.00 15.52 ?  120  VAL B CA   1 
ATOM   8252  C C    . VAL B 1 120  ? 103.796 102.811 153.593 1.00 18.13 ?  120  VAL B C    1 
ATOM   8253  O O    . VAL B 1 120  ? 103.925 103.911 153.036 1.00 19.06 ?  120  VAL B O    1 
ATOM   8254  C CB   . VAL B 1 120  ? 103.518 101.153 151.711 1.00 15.06 ?  120  VAL B CB   1 
ATOM   8255  C CG1  . VAL B 1 120  ? 104.728 100.305 152.065 1.00 16.27 ?  120  VAL B CG1  1 
ATOM   8256  C CG2  . VAL B 1 120  ? 102.491 100.331 150.952 1.00 14.28 ?  120  VAL B CG2  1 
ATOM   8257  N N    . PRO B 1 121  ? 104.449 102.531 154.731 1.00 19.61 ?  121  PRO B N    1 
ATOM   8258  C CA   . PRO B 1 121  ? 105.280 103.558 155.378 1.00 18.09 ?  121  PRO B CA   1 
ATOM   8259  C C    . PRO B 1 121  ? 106.622 103.802 154.701 1.00 19.81 ?  121  PRO B C    1 
ATOM   8260  O O    . PRO B 1 121  ? 107.163 104.907 154.794 1.00 19.49 ?  121  PRO B O    1 
ATOM   8261  C CB   . PRO B 1 121  ? 105.471 103.005 156.796 1.00 13.97 ?  121  PRO B CB   1 
ATOM   8262  C CG   . PRO B 1 121  ? 105.349 101.533 156.639 1.00 20.42 ?  121  PRO B CG   1 
ATOM   8263  C CD   . PRO B 1 121  ? 104.348 101.305 155.542 1.00 20.50 ?  121  PRO B CD   1 
ATOM   8264  N N    . LEU B 1 122  ? 107.181 102.786 154.037 1.00 20.17 ?  122  LEU B N    1 
ATOM   8265  C CA   . LEU B 1 122  ? 108.465 102.959 153.359 1.00 18.76 ?  122  LEU B CA   1 
ATOM   8266  C C    . LEU B 1 122  ? 108.344 103.923 152.183 1.00 16.88 ?  122  LEU B C    1 
ATOM   8267  O O    . LEU B 1 122  ? 109.192 104.810 152.000 1.00 20.34 ?  122  LEU B O    1 
ATOM   8268  C CB   . LEU B 1 122  ? 108.991 101.601 152.893 1.00 14.24 ?  122  LEU B CB   1 
ATOM   8269  C CG   . LEU B 1 122  ? 110.375 101.540 152.245 1.00 14.54 ?  122  LEU B CG   1 
ATOM   8270  C CD1  . LEU B 1 122  ? 111.449 101.302 153.296 1.00 15.93 ?  122  LEU B CD1  1 
ATOM   8271  C CD2  . LEU B 1 122  ? 110.417 100.458 151.177 1.00 14.98 ?  122  LEU B CD2  1 
ATOM   8272  N N    . VAL B 1 123  ? 107.286 103.770 151.384 1.00 13.99 ?  123  VAL B N    1 
ATOM   8273  C CA   . VAL B 1 123  ? 107.030 104.699 150.290 1.00 14.91 ?  123  VAL B CA   1 
ATOM   8274  C C    . VAL B 1 123  ? 106.733 106.088 150.834 1.00 13.78 ?  123  VAL B C    1 
ATOM   8275  O O    . VAL B 1 123  ? 107.107 107.095 150.222 1.00 14.52 ?  123  VAL B O    1 
ATOM   8276  C CB   . VAL B 1 123  ? 105.884 104.170 149.404 1.00 17.90 ?  123  VAL B CB   1 
ATOM   8277  C CG1  . VAL B 1 123  ? 105.747 105.008 148.142 1.00 15.24 ?  123  VAL B CG1  1 
ATOM   8278  C CG2  . VAL B 1 123  ? 106.116 102.708 149.060 1.00 15.79 ?  123  VAL B CG2  1 
ATOM   8279  N N    . GLU B 1 124  ? 106.071 106.170 151.991 1.00 15.59 ?  124  GLU B N    1 
ATOM   8280  C CA   . GLU B 1 124  ? 105.843 107.464 152.629 1.00 16.25 ?  124  GLU B CA   1 
ATOM   8281  C C    . GLU B 1 124  ? 107.159 108.127 153.018 1.00 14.17 ?  124  GLU B C    1 
ATOM   8282  O O    . GLU B 1 124  ? 107.335 109.336 152.825 1.00 17.44 ?  124  GLU B O    1 
ATOM   8283  C CB   . GLU B 1 124  ? 104.944 107.292 153.854 1.00 17.05 ?  124  GLU B CB   1 
ATOM   8284  C CG   . GLU B 1 124  ? 105.169 108.313 154.959 1.00 19.61 ?  124  GLU B CG   1 
ATOM   8285  C CD   . GLU B 1 124  ? 104.490 107.928 156.259 1.00 21.86 ?  124  GLU B CD   1 
ATOM   8286  O OE1  . GLU B 1 124  ? 103.430 107.270 156.208 1.00 19.38 ?  124  GLU B OE1  1 
ATOM   8287  O OE2  . GLU B 1 124  ? 105.018 108.285 157.333 1.00 22.40 ?  124  GLU B OE2  1 
ATOM   8288  N N    . GLU B 1 125  ? 108.098 107.347 153.560 1.00 14.96 ?  125  GLU B N    1 
ATOM   8289  C CA   . GLU B 1 125  ? 109.402 107.890 153.925 1.00 17.12 ?  125  GLU B CA   1 
ATOM   8290  C C    . GLU B 1 125  ? 110.159 108.374 152.694 1.00 16.11 ?  125  GLU B C    1 
ATOM   8291  O O    . GLU B 1 125  ? 110.817 109.421 152.730 1.00 16.70 ?  125  GLU B O    1 
ATOM   8292  C CB   . GLU B 1 125  ? 110.210 106.836 154.688 1.00 17.35 ?  125  GLU B CB   1 
ATOM   8293  C CG   . GLU B 1 125  ? 111.569 107.304 155.190 1.00 17.72 ?  125  GLU B CG   1 
ATOM   8294  C CD   . GLU B 1 125  ? 112.304 106.236 155.979 1.00 19.46 ?  125  GLU B CD   1 
ATOM   8295  O OE1  . GLU B 1 125  ? 111.773 105.113 156.106 1.00 18.90 ?  125  GLU B OE1  1 
ATOM   8296  O OE2  . GLU B 1 125  ? 113.416 106.521 156.471 1.00 20.26 ?  125  GLU B OE2  1 
ATOM   8297  N N    . HIS B 1 126  ? 110.060 107.638 151.588 1.00 11.38 ?  126  HIS B N    1 
ATOM   8298  C CA   . HIS B 1 126  ? 110.738 108.058 150.366 1.00 9.28  ?  126  HIS B CA   1 
ATOM   8299  C C    . HIS B 1 126  ? 110.003 109.157 149.601 1.00 15.53 ?  126  HIS B C    1 
ATOM   8300  O O    . HIS B 1 126  ? 110.594 109.748 148.691 1.00 14.76 ?  126  HIS B O    1 
ATOM   8301  C CB   . HIS B 1 126  ? 110.962 106.857 149.446 1.00 11.94 ?  126  HIS B CB   1 
ATOM   8302  C CG   . HIS B 1 126  ? 112.175 106.052 149.792 1.00 12.81 ?  126  HIS B CG   1 
ATOM   8303  N ND1  . HIS B 1 126  ? 113.391 106.240 149.173 1.00 12.75 ?  126  HIS B ND1  1 
ATOM   8304  C CD2  . HIS B 1 126  ? 112.361 105.062 150.696 1.00 14.06 ?  126  HIS B CD2  1 
ATOM   8305  C CE1  . HIS B 1 126  ? 114.275 105.398 149.679 1.00 15.58 ?  126  HIS B CE1  1 
ATOM   8306  N NE2  . HIS B 1 126  ? 113.675 104.672 150.605 1.00 14.41 ?  126  HIS B NE2  1 
ATOM   8307  N N    . THR B 1 127  ? 108.743 109.442 149.933 1.00 16.42 ?  127  THR B N    1 
ATOM   8308  C CA   . THR B 1 127  ? 107.961 110.442 149.212 1.00 6.63  ?  127  THR B CA   1 
ATOM   8309  C C    . THR B 1 127  ? 107.805 111.764 149.958 1.00 8.03  ?  127  THR B C    1 
ATOM   8310  O O    . THR B 1 127  ? 107.672 112.811 149.312 1.00 15.08 ?  127  THR B O    1 
ATOM   8311  C CB   . THR B 1 127  ? 106.566 109.884 148.897 1.00 4.24  ?  127  THR B CB   1 
ATOM   8312  O OG1  . THR B 1 127  ? 106.674 108.506 148.521 1.00 16.63 ?  127  THR B OG1  1 
ATOM   8313  C CG2  . THR B 1 127  ? 105.915 110.645 147.758 1.00 11.65 ?  127  THR B CG2  1 
ATOM   8314  N N    . ARG B 1 128  ? 107.846 111.745 151.294 1.00 8.99  ?  128  ARG B N    1 
ATOM   8315  C CA   . ARG B 1 128  ? 107.469 112.908 152.091 1.00 9.37  ?  128  ARG B CA   1 
ATOM   8316  C C    . ARG B 1 128  ? 108.437 114.079 151.963 1.00 13.74 ?  128  ARG B C    1 
ATOM   8317  O O    . ARG B 1 128  ? 108.057 115.210 152.279 1.00 13.90 ?  128  ARG B O    1 
ATOM   8318  C CB   . ARG B 1 128  ? 107.344 112.503 153.563 1.00 13.63 ?  128  ARG B CB   1 
ATOM   8319  C CG   . ARG B 1 128  ? 108.674 112.437 154.301 1.00 15.76 ?  128  ARG B CG   1 
ATOM   8320  C CD   . ARG B 1 128  ? 108.516 112.689 155.791 1.00 14.06 ?  128  ARG B CD   1 
ATOM   8321  N NE   . ARG B 1 128  ? 108.285 111.455 156.531 1.00 14.94 ?  128  ARG B NE   1 
ATOM   8322  C CZ   . ARG B 1 128  ? 109.243 110.620 156.913 1.00 18.15 ?  128  ARG B CZ   1 
ATOM   8323  N NH1  . ARG B 1 128  ? 110.516 110.862 156.649 1.00 17.61 ?  128  ARG B NH1  1 
ATOM   8324  N NH2  . ARG B 1 128  ? 108.915 109.516 157.578 1.00 21.18 ?  128  ARG B NH2  1 
ATOM   8325  N N    . ASP B 1 129  ? 109.670 113.847 151.513 1.00 14.55 ?  129  ASP B N    1 
ATOM   8326  C CA   . ASP B 1 129  ? 110.655 114.919 151.461 1.00 10.24 ?  129  ASP B CA   1 
ATOM   8327  C C    . ASP B 1 129  ? 110.593 115.731 150.176 1.00 9.27  ?  129  ASP B C    1 
ATOM   8328  O O    . ASP B 1 129  ? 111.164 116.825 150.125 1.00 12.25 ?  129  ASP B O    1 
ATOM   8329  C CB   . ASP B 1 129  ? 112.065 114.349 151.637 1.00 13.11 ?  129  ASP B CB   1 
ATOM   8330  C CG   . ASP B 1 129  ? 112.362 113.974 153.074 1.00 16.53 ?  129  ASP B CG   1 
ATOM   8331  O OD1  . ASP B 1 129  ? 112.225 114.848 153.956 1.00 22.15 ?  129  ASP B OD1  1 
ATOM   8332  O OD2  . ASP B 1 129  ? 112.729 112.807 153.324 1.00 14.46 ?  129  ASP B OD2  1 
ATOM   8333  N N    . VAL B 1 130  ? 109.918 115.227 149.144 1.00 11.49 ?  130  VAL B N    1 
ATOM   8334  C CA   . VAL B 1 130  ? 109.711 115.982 147.922 1.00 4.20  ?  130  VAL B CA   1 
ATOM   8335  C C    . VAL B 1 130  ? 108.241 116.323 147.700 1.00 2.51  ?  130  VAL B C    1 
ATOM   8336  O O    . VAL B 1 130  ? 107.944 117.343 147.067 1.00 2.83  ?  130  VAL B O    1 
ATOM   8337  C CB   . VAL B 1 130  ? 110.283 115.229 146.701 1.00 2.96  ?  130  VAL B CB   1 
ATOM   8338  C CG1  . VAL B 1 130  ? 110.496 116.179 145.531 1.00 2.85  ?  130  VAL B CG1  1 
ATOM   8339  C CG2  . VAL B 1 130  ? 111.581 114.528 147.059 1.00 6.43  ?  130  VAL B CG2  1 
ATOM   8340  N N    . ALA B 1 131  ? 107.312 115.508 148.208 1.00 6.43  ?  131  ALA B N    1 
ATOM   8341  C CA   . ALA B 1 131  ? 105.896 115.823 148.061 1.00 2.42  ?  131  ALA B CA   1 
ATOM   8342  C C    . ALA B 1 131  ? 105.518 117.064 148.858 1.00 3.93  ?  131  ALA B C    1 
ATOM   8343  O O    . ALA B 1 131  ? 104.739 117.899 148.385 1.00 9.64  ?  131  ALA B O    1 
ATOM   8344  C CB   . ALA B 1 131  ? 105.046 114.629 148.491 1.00 5.85  ?  131  ALA B CB   1 
ATOM   8345  N N    . HIS B 1 132  ? 106.059 117.205 150.063 1.00 3.45  ?  132  HIS B N    1 
ATOM   8346  C CA   . HIS B 1 132  ? 105.786 118.346 150.933 1.00 4.79  ?  132  HIS B CA   1 
ATOM   8347  C C    . HIS B 1 132  ? 107.082 119.137 151.084 1.00 7.24  ?  132  HIS B C    1 
ATOM   8348  O O    . HIS B 1 132  ? 107.850 118.930 152.025 1.00 12.87 ?  132  HIS B O    1 
ATOM   8349  C CB   . HIS B 1 132  ? 105.246 117.883 152.278 1.00 6.51  ?  132  HIS B CB   1 
ATOM   8350  C CG   . HIS B 1 132  ? 104.168 116.851 152.168 1.00 7.17  ?  132  HIS B CG   1 
ATOM   8351  N ND1  . HIS B 1 132  ? 104.416 115.500 152.278 1.00 13.82 ?  132  HIS B ND1  1 
ATOM   8352  C CD2  . HIS B 1 132  ? 102.839 116.973 151.946 1.00 6.99  ?  132  HIS B CD2  1 
ATOM   8353  C CE1  . HIS B 1 132  ? 103.284 114.834 152.135 1.00 11.03 ?  132  HIS B CE1  1 
ATOM   8354  N NE2  . HIS B 1 132  ? 102.312 115.705 151.933 1.00 5.41  ?  132  HIS B NE2  1 
ATOM   8355  N N    . MET B 1 133  ? 107.314 120.052 150.151 1.00 9.90  ?  133  MET B N    1 
ATOM   8356  C CA   . MET B 1 133  ? 108.514 120.868 150.122 1.00 9.40  ?  133  MET B CA   1 
ATOM   8357  C C    . MET B 1 133  ? 108.220 122.251 150.697 1.00 12.07 ?  133  MET B C    1 
ATOM   8358  O O    . MET B 1 133  ? 107.091 122.572 151.074 1.00 14.02 ?  133  MET B O    1 
ATOM   8359  C CB   . MET B 1 133  ? 109.045 120.969 148.692 1.00 5.12  ?  133  MET B CB   1 
ATOM   8360  C CG   . MET B 1 133  ? 110.008 119.865 148.306 1.00 9.04  ?  133  MET B CG   1 
ATOM   8361  S SD   . MET B 1 133  ? 110.921 120.266 146.807 1.00 5.79  ?  133  MET B SD   1 
ATOM   8362  C CE   . MET B 1 133  ? 109.615 120.968 145.804 1.00 6.22  ?  133  MET B CE   1 
ATOM   8363  N N    . ASP B 1 134  ? 109.256 123.079 150.764 1.00 6.92  ?  134  ASP B N    1 
ATOM   8364  C CA   . ASP B 1 134  ? 109.071 124.459 151.180 1.00 5.39  ?  134  ASP B CA   1 
ATOM   8365  C C    . ASP B 1 134  ? 108.388 125.247 150.064 1.00 9.97  ?  134  ASP B C    1 
ATOM   8366  O O    . ASP B 1 134  ? 108.677 125.025 148.883 1.00 9.89  ?  134  ASP B O    1 
ATOM   8367  C CB   . ASP B 1 134  ? 110.416 125.096 151.530 1.00 0.22  ?  134  ASP B CB   1 
ATOM   8368  C CG   . ASP B 1 134  ? 110.287 126.208 152.551 1.00 6.21  ?  134  ASP B CG   1 
ATOM   8369  O OD1  . ASP B 1 134  ? 109.661 125.978 153.606 1.00 5.85  ?  134  ASP B OD1  1 
ATOM   8370  O OD2  . ASP B 1 134  ? 110.819 127.310 152.303 1.00 12.11 ?  134  ASP B OD2  1 
ATOM   8371  N N    . PRO B 1 135  ? 107.468 126.156 150.399 1.00 2.74  ?  135  PRO B N    1 
ATOM   8372  C CA   . PRO B 1 135  ? 106.827 126.972 149.353 1.00 0.00  ?  135  PRO B CA   1 
ATOM   8373  C C    . PRO B 1 135  ? 107.793 127.871 148.603 1.00 2.18  ?  135  PRO B C    1 
ATOM   8374  O O    . PRO B 1 135  ? 107.499 128.264 147.467 1.00 6.06  ?  135  PRO B O    1 
ATOM   8375  C CB   . PRO B 1 135  ? 105.790 127.796 150.129 1.00 0.00  ?  135  PRO B CB   1 
ATOM   8376  C CG   . PRO B 1 135  ? 106.219 127.727 151.557 1.00 1.06  ?  135  PRO B CG   1 
ATOM   8377  C CD   . PRO B 1 135  ? 106.885 126.403 151.727 1.00 0.94  ?  135  PRO B CD   1 
ATOM   8378  N N    . HIS B 1 136  ? 108.940 128.207 149.197 1.00 0.00  ?  136  HIS B N    1 
ATOM   8379  C CA   . HIS B 1 136  ? 109.907 129.056 148.516 1.00 6.78  ?  136  HIS B CA   1 
ATOM   8380  C C    . HIS B 1 136  ? 110.672 128.312 147.433 1.00 5.11  ?  136  HIS B C    1 
ATOM   8381  O O    . HIS B 1 136  ? 111.253 128.956 146.557 1.00 7.51  ?  136  HIS B O    1 
ATOM   8382  C CB   . HIS B 1 136  ? 110.874 129.665 149.529 1.00 0.68  ?  136  HIS B CB   1 
ATOM   8383  C CG   . HIS B 1 136  ? 110.208 130.547 150.537 1.00 5.04  ?  136  HIS B CG   1 
ATOM   8384  N ND1  . HIS B 1 136  ? 109.748 131.809 150.230 1.00 8.91  ?  136  HIS B ND1  1 
ATOM   8385  C CD2  . HIS B 1 136  ? 109.913 130.347 151.843 1.00 5.53  ?  136  HIS B CD2  1 
ATOM   8386  C CE1  . HIS B 1 136  ? 109.204 132.351 151.304 1.00 4.45  ?  136  HIS B CE1  1 
ATOM   8387  N NE2  . HIS B 1 136  ? 109.291 131.485 152.297 1.00 8.15  ?  136  HIS B NE2  1 
ATOM   8388  N N    . VAL B 1 137  ? 110.679 126.979 147.464 1.00 1.51  ?  137  VAL B N    1 
ATOM   8389  C CA   . VAL B 1 137  ? 111.213 126.223 146.336 1.00 0.00  ?  137  VAL B CA   1 
ATOM   8390  C C    . VAL B 1 137  ? 110.340 126.430 145.107 1.00 7.67  ?  137  VAL B C    1 
ATOM   8391  O O    . VAL B 1 137  ? 110.841 126.604 143.990 1.00 8.19  ?  137  VAL B O    1 
ATOM   8392  C CB   . VAL B 1 137  ? 111.332 124.733 146.702 1.00 0.00  ?  137  VAL B CB   1 
ATOM   8393  C CG1  . VAL B 1 137  ? 111.836 123.931 145.518 1.00 0.00  ?  137  VAL B CG1  1 
ATOM   8394  C CG2  . VAL B 1 137  ? 112.242 124.553 147.900 1.00 6.12  ?  137  VAL B CG2  1 
ATOM   8395  N N    . LEU B 1 138  ? 109.021 126.427 145.296 1.00 0.60  ?  138  LEU B N    1 
ATOM   8396  C CA   . LEU B 1 138  ? 108.107 126.648 144.183 1.00 0.00  ?  138  LEU B CA   1 
ATOM   8397  C C    . LEU B 1 138  ? 108.089 128.113 143.763 1.00 1.10  ?  138  LEU B C    1 
ATOM   8398  O O    . LEU B 1 138  ? 108.018 128.421 142.568 1.00 2.68  ?  138  LEU B O    1 
ATOM   8399  C CB   . LEU B 1 138  ? 106.705 126.178 144.569 1.00 0.00  ?  138  LEU B CB   1 
ATOM   8400  C CG   . LEU B 1 138  ? 106.518 124.671 144.752 1.00 0.00  ?  138  LEU B CG   1 
ATOM   8401  C CD1  . LEU B 1 138  ? 105.661 124.378 145.972 1.00 0.00  ?  138  LEU B CD1  1 
ATOM   8402  C CD2  . LEU B 1 138  ? 105.896 124.063 143.513 1.00 0.25  ?  138  LEU B CD2  1 
ATOM   8403  N N    . LEU B 1 139  ? 108.154 129.032 144.728 1.00 0.00  ?  139  LEU B N    1 
ATOM   8404  C CA   . LEU B 1 139  ? 108.088 130.455 144.409 1.00 1.07  ?  139  LEU B CA   1 
ATOM   8405  C C    . LEU B 1 139  ? 109.390 130.995 143.827 1.00 4.24  ?  139  LEU B C    1 
ATOM   8406  O O    . LEU B 1 139  ? 109.359 131.954 143.050 1.00 6.33  ?  139  LEU B O    1 
ATOM   8407  C CB   . LEU B 1 139  ? 107.708 131.257 145.654 1.00 0.00  ?  139  LEU B CB   1 
ATOM   8408  C CG   . LEU B 1 139  ? 106.252 131.180 146.116 1.00 0.00  ?  139  LEU B CG   1 
ATOM   8409  C CD1  . LEU B 1 139  ? 106.100 131.761 147.511 1.00 0.00  ?  139  LEU B CD1  1 
ATOM   8410  C CD2  . LEU B 1 139  ? 105.342 131.897 145.135 1.00 0.00  ?  139  LEU B CD2  1 
ATOM   8411  N N    . GLN B 1 140  ? 110.535 130.405 144.179 1.00 4.06  ?  140  GLN B N    1 
ATOM   8412  C CA   . GLN B 1 140  ? 111.831 130.951 143.809 1.00 0.00  ?  140  GLN B CA   1 
ATOM   8413  C C    . GLN B 1 140  ? 112.529 130.202 142.683 1.00 0.00  ?  140  GLN B C    1 
ATOM   8414  O O    . GLN B 1 140  ? 113.430 130.770 142.060 1.00 0.43  ?  140  GLN B O    1 
ATOM   8415  C CB   . GLN B 1 140  ? 112.763 130.974 145.032 1.00 0.49  ?  140  GLN B CB   1 
ATOM   8416  C CG   . GLN B 1 140  ? 112.385 132.001 146.092 1.00 9.17  ?  140  GLN B CG   1 
ATOM   8417  C CD   . GLN B 1 140  ? 113.441 132.147 147.174 1.00 9.42  ?  140  GLN B CD   1 
ATOM   8418  O OE1  . GLN B 1 140  ? 114.617 131.862 146.954 1.00 2.80  ?  140  GLN B OE1  1 
ATOM   8419  N NE2  . GLN B 1 140  ? 113.021 132.590 148.353 1.00 7.87  ?  140  GLN B NE2  1 
ATOM   8420  N N    . ILE B 1 141  ? 112.150 128.954 142.407 1.00 0.00  ?  141  ILE B N    1 
ATOM   8421  C CA   . ILE B 1 141  ? 112.818 128.128 141.409 1.00 4.83  ?  141  ILE B CA   1 
ATOM   8422  C C    . ILE B 1 141  ? 111.870 127.720 140.288 1.00 4.81  ?  141  ILE B C    1 
ATOM   8423  O O    . ILE B 1 141  ? 112.197 127.851 139.105 1.00 1.15  ?  141  ILE B O    1 
ATOM   8424  C CB   . ILE B 1 141  ? 113.466 126.880 142.051 1.00 0.00  ?  141  ILE B CB   1 
ATOM   8425  C CG1  . ILE B 1 141  ? 114.360 127.277 143.224 1.00 0.00  ?  141  ILE B CG1  1 
ATOM   8426  C CG2  . ILE B 1 141  ? 114.257 126.094 141.020 1.00 0.00  ?  141  ILE B CG2  1 
ATOM   8427  C CD1  . ILE B 1 141  ? 114.927 126.101 143.972 1.00 0.00  ?  141  ILE B CD1  1 
ATOM   8428  N N    . PHE B 1 142  ? 110.683 127.223 140.640 1.00 0.00  ?  142  PHE B N    1 
ATOM   8429  C CA   . PHE B 1 142  ? 109.818 126.606 139.639 1.00 0.00  ?  142  PHE B CA   1 
ATOM   8430  C C    . PHE B 1 142  ? 109.107 127.649 138.785 1.00 0.58  ?  142  PHE B C    1 
ATOM   8431  O O    . PHE B 1 142  ? 109.159 127.591 137.550 1.00 1.19  ?  142  PHE B O    1 
ATOM   8432  C CB   . PHE B 1 142  ? 108.799 125.687 140.317 1.00 0.00  ?  142  PHE B CB   1 
ATOM   8433  C CG   . PHE B 1 142  ? 109.353 124.346 140.722 1.00 2.37  ?  142  PHE B CG   1 
ATOM   8434  C CD1  . PHE B 1 142  ? 110.707 124.075 140.636 1.00 0.00  ?  142  PHE B CD1  1 
ATOM   8435  C CD2  . PHE B 1 142  ? 108.512 123.355 141.192 1.00 0.00  ?  142  PHE B CD2  1 
ATOM   8436  C CE1  . PHE B 1 142  ? 111.207 122.846 141.012 1.00 0.00  ?  142  PHE B CE1  1 
ATOM   8437  C CE2  . PHE B 1 142  ? 109.009 122.123 141.567 1.00 3.12  ?  142  PHE B CE2  1 
ATOM   8438  C CZ   . PHE B 1 142  ? 110.356 121.870 141.476 1.00 0.00  ?  142  PHE B CZ   1 
ATOM   8439  N N    . LEU B 1 143  ? 108.422 128.595 139.426 1.00 0.00  ?  143  LEU B N    1 
ATOM   8440  C CA   . LEU B 1 143  ? 107.696 129.619 138.680 1.00 0.00  ?  143  LEU B CA   1 
ATOM   8441  C C    . LEU B 1 143  ? 108.593 130.528 137.838 1.00 0.00  ?  143  LEU B C    1 
ATOM   8442  O O    . LEU B 1 143  ? 108.210 130.811 136.688 1.00 7.23  ?  143  LEU B O    1 
ATOM   8443  C CB   . LEU B 1 143  ? 106.817 130.434 139.640 1.00 1.48  ?  143  LEU B CB   1 
ATOM   8444  C CG   . LEU B 1 143  ? 105.604 129.715 140.230 1.00 0.00  ?  143  LEU B CG   1 
ATOM   8445  C CD1  . LEU B 1 143  ? 104.909 130.599 141.247 1.00 0.00  ?  143  LEU B CD1  1 
ATOM   8446  C CD2  . LEU B 1 143  ? 104.646 129.298 139.133 1.00 5.17  ?  143  LEU B CD2  1 
ATOM   8447  N N    . PRO B 1 144  ? 109.744 131.038 138.321 1.00 3.13  ?  144  PRO B N    1 
ATOM   8448  C CA   . PRO B 1 144  ? 110.619 131.802 137.411 1.00 0.00  ?  144  PRO B CA   1 
ATOM   8449  C C    . PRO B 1 144  ? 111.052 131.028 136.178 1.00 2.62  ?  144  PRO B C    1 
ATOM   8450  O O    . PRO B 1 144  ? 111.076 131.597 135.081 1.00 8.17  ?  144  PRO B O    1 
ATOM   8451  C CB   . PRO B 1 144  ? 111.817 132.148 138.300 1.00 0.00  ?  144  PRO B CB   1 
ATOM   8452  C CG   . PRO B 1 144  ? 111.259 132.237 139.644 1.00 0.00  ?  144  PRO B CG   1 
ATOM   8453  C CD   . PRO B 1 144  ? 110.191 131.193 139.721 1.00 0.00  ?  144  PRO B CD   1 
ATOM   8454  N N    . VAL B 1 145  ? 111.365 129.739 136.321 1.00 9.18  ?  145  VAL B N    1 
ATOM   8455  C CA   . VAL B 1 145  ? 111.754 128.933 135.168 1.00 4.47  ?  145  VAL B CA   1 
ATOM   8456  C C    . VAL B 1 145  ? 110.580 128.756 134.213 1.00 5.52  ?  145  VAL B C    1 
ATOM   8457  O O    . VAL B 1 145  ? 110.723 128.917 132.993 1.00 9.66  ?  145  VAL B O    1 
ATOM   8458  C CB   . VAL B 1 145  ? 112.316 127.577 135.633 1.00 0.75  ?  145  VAL B CB   1 
ATOM   8459  C CG1  . VAL B 1 145  ? 112.358 126.591 134.482 1.00 5.88  ?  145  VAL B CG1  1 
ATOM   8460  C CG2  . VAL B 1 145  ? 113.704 127.755 136.217 1.00 0.00  ?  145  VAL B CG2  1 
ATOM   8461  N N    . LEU B 1 146  ? 109.398 128.443 134.753 1.00 2.25  ?  146  LEU B N    1 
ATOM   8462  C CA   . LEU B 1 146  ? 108.238 128.193 133.904 1.00 2.91  ?  146  LEU B CA   1 
ATOM   8463  C C    . LEU B 1 146  ? 107.779 129.447 133.172 1.00 0.00  ?  146  LEU B C    1 
ATOM   8464  O O    . LEU B 1 146  ? 107.208 129.346 132.081 1.00 0.00  ?  146  LEU B O    1 
ATOM   8465  C CB   . LEU B 1 146  ? 107.087 127.620 134.729 1.00 2.45  ?  146  LEU B CB   1 
ATOM   8466  C CG   . LEU B 1 146  ? 107.196 126.154 135.147 1.00 0.00  ?  146  LEU B CG   1 
ATOM   8467  C CD1  . LEU B 1 146  ? 105.994 125.754 135.978 1.00 0.00  ?  146  LEU B CD1  1 
ATOM   8468  C CD2  . LEU B 1 146  ? 107.328 125.263 133.926 1.00 0.00  ?  146  LEU B CD2  1 
ATOM   8469  N N    . ILE B 1 147  ? 108.006 130.629 133.744 1.00 7.52  ?  147  ILE B N    1 
ATOM   8470  C CA   . ILE B 1 147  ? 107.605 131.846 133.044 1.00 0.00  ?  147  ILE B CA   1 
ATOM   8471  C C    . ILE B 1 147  ? 108.697 132.309 132.080 1.00 0.00  ?  147  ILE B C    1 
ATOM   8472  O O    . ILE B 1 147  ? 108.402 132.776 130.970 1.00 5.45  ?  147  ILE B O    1 
ATOM   8473  C CB   . ILE B 1 147  ? 107.221 132.943 134.053 1.00 3.17  ?  147  ILE B CB   1 
ATOM   8474  C CG1  . ILE B 1 147  ? 106.125 132.440 134.991 1.00 0.32  ?  147  ILE B CG1  1 
ATOM   8475  C CG2  . ILE B 1 147  ? 106.700 134.162 133.335 1.00 0.00  ?  147  ILE B CG2  1 
ATOM   8476  C CD1  . ILE B 1 147  ? 104.808 132.154 134.308 1.00 6.36  ?  147  ILE B CD1  1 
ATOM   8477  N N    . PHE B 1 148  ? 109.970 132.184 132.475 1.00 5.35  ?  148  PHE B N    1 
ATOM   8478  C CA   . PHE B 1 148  ? 111.059 132.589 131.595 1.00 2.53  ?  148  PHE B CA   1 
ATOM   8479  C C    . PHE B 1 148  ? 111.143 131.717 130.353 1.00 0.00  ?  148  PHE B C    1 
ATOM   8480  O O    . PHE B 1 148  ? 111.501 132.218 129.286 1.00 8.81  ?  148  PHE B O    1 
ATOM   8481  C CB   . PHE B 1 148  ? 112.393 132.564 132.343 1.00 3.83  ?  148  PHE B CB   1 
ATOM   8482  C CG   . PHE B 1 148  ? 113.565 133.022 131.511 1.00 0.55  ?  148  PHE B CG   1 
ATOM   8483  C CD1  . PHE B 1 148  ? 113.852 134.368 131.380 1.00 0.00  ?  148  PHE B CD1  1 
ATOM   8484  C CD2  . PHE B 1 148  ? 114.386 132.107 130.871 1.00 0.00  ?  148  PHE B CD2  1 
ATOM   8485  C CE1  . PHE B 1 148  ? 114.926 134.793 130.622 1.00 0.00  ?  148  PHE B CE1  1 
ATOM   8486  C CE2  . PHE B 1 148  ? 115.458 132.529 130.110 1.00 0.00  ?  148  PHE B CE2  1 
ATOM   8487  C CZ   . PHE B 1 148  ? 115.728 133.872 129.987 1.00 0.00  ?  148  PHE B CZ   1 
ATOM   8488  N N    . GLU B 1 149  ? 110.842 130.419 130.463 1.00 3.41  ?  149  GLU B N    1 
ATOM   8489  C CA   . GLU B 1 149  ? 110.853 129.576 129.271 1.00 0.72  ?  149  GLU B CA   1 
ATOM   8490  C C    . GLU B 1 149  ? 109.779 130.009 128.281 1.00 7.26  ?  149  GLU B C    1 
ATOM   8491  O O    . GLU B 1 149  ? 110.019 130.039 127.067 1.00 10.93 ?  149  GLU B O    1 
ATOM   8492  C CB   . GLU B 1 149  ? 110.668 128.110 129.652 1.00 0.00  ?  149  GLU B CB   1 
ATOM   8493  C CG   . GLU B 1 149  ? 111.093 127.149 128.556 1.00 7.66  ?  149  GLU B CG   1 
ATOM   8494  C CD   . GLU B 1 149  ? 109.919 126.600 127.770 1.00 8.99  ?  149  GLU B CD   1 
ATOM   8495  O OE1  . GLU B 1 149  ? 108.867 126.327 128.384 1.00 11.08 ?  149  GLU B OE1  1 
ATOM   8496  O OE2  . GLU B 1 149  ? 110.049 126.441 126.538 1.00 4.85  ?  149  GLU B OE2  1 
ATOM   8497  N N    . SER B 1 150  ? 108.590 130.353 128.782 1.00 5.09  ?  150  SER B N    1 
ATOM   8498  C CA   . SER B 1 150  ? 107.526 130.840 127.909 1.00 0.45  ?  150  SER B CA   1 
ATOM   8499  C C    . SER B 1 150  ? 107.906 132.162 127.255 1.00 5.77  ?  150  SER B C    1 
ATOM   8500  O O    . SER B 1 150  ? 107.640 132.371 126.066 1.00 9.10  ?  150  SER B O    1 
ATOM   8501  C CB   . SER B 1 150  ? 106.227 130.989 128.700 1.00 1.90  ?  150  SER B CB   1 
ATOM   8502  O OG   . SER B 1 150  ? 105.977 129.839 129.488 1.00 7.34  ?  150  SER B OG   1 
ATOM   8503  N N    . ALA B 1 151  ? 108.519 133.070 128.019 1.00 9.00  ?  151  ALA B N    1 
ATOM   8504  C CA   . ALA B 1 151  ? 108.927 134.353 127.451 1.00 0.00  ?  151  ALA B CA   1 
ATOM   8505  C C    . ALA B 1 151  ? 110.044 134.186 126.424 1.00 0.00  ?  151  ALA B C    1 
ATOM   8506  O O    . ALA B 1 151  ? 110.043 134.852 125.383 1.00 5.83  ?  151  ALA B O    1 
ATOM   8507  C CB   . ALA B 1 151  ? 109.358 135.305 128.565 1.00 0.00  ?  151  ALA B CB   1 
ATOM   8508  N N    . PHE B 1 152  ? 111.004 133.304 126.701 1.00 0.61  ?  152  PHE B N    1 
ATOM   8509  C CA   . PHE B 1 152  ? 112.177 133.134 125.853 1.00 1.63  ?  152  PHE B CA   1 
ATOM   8510  C C    . PHE B 1 152  ? 111.881 132.323 124.597 1.00 3.21  ?  152  PHE B C    1 
ATOM   8511  O O    . PHE B 1 152  ? 112.544 132.518 123.572 1.00 7.26  ?  152  PHE B O    1 
ATOM   8512  C CB   . PHE B 1 152  ? 113.288 132.466 126.666 1.00 0.21  ?  152  PHE B CB   1 
ATOM   8513  C CG   . PHE B 1 152  ? 114.635 132.482 126.003 1.00 0.52  ?  152  PHE B CG   1 
ATOM   8514  C CD1  . PHE B 1 152  ? 115.236 133.677 125.648 1.00 2.46  ?  152  PHE B CD1  1 
ATOM   8515  C CD2  . PHE B 1 152  ? 115.312 131.299 125.759 1.00 5.98  ?  152  PHE B CD2  1 
ATOM   8516  C CE1  . PHE B 1 152  ? 116.482 133.689 125.048 1.00 9.65  ?  152  PHE B CE1  1 
ATOM   8517  C CE2  . PHE B 1 152  ? 116.555 131.306 125.159 1.00 5.97  ?  152  PHE B CE2  1 
ATOM   8518  C CZ   . PHE B 1 152  ? 117.141 132.501 124.804 1.00 6.98  ?  152  PHE B CZ   1 
ATOM   8519  N N    . ALA B 1 153  ? 110.907 131.411 124.654 1.00 5.65  ?  153  ALA B N    1 
ATOM   8520  C CA   . ALA B 1 153  ? 110.668 130.514 123.528 1.00 8.76  ?  153  ALA B CA   1 
ATOM   8521  C C    . ALA B 1 153  ? 109.977 131.224 122.369 1.00 17.08 ?  153  ALA B C    1 
ATOM   8522  O O    . ALA B 1 153  ? 110.318 130.992 121.203 1.00 19.87 ?  153  ALA B O    1 
ATOM   8523  C CB   . ALA B 1 153  ? 109.843 129.313 123.986 1.00 12.01 ?  153  ALA B CB   1 
ATOM   8524  N N    . MET B 1 154  ? 109.003 132.081 122.665 1.00 17.52 ?  154  MET B N    1 
ATOM   8525  C CA   . MET B 1 154  ? 108.173 132.677 121.627 1.00 15.76 ?  154  MET B CA   1 
ATOM   8526  C C    . MET B 1 154  ? 108.963 133.669 120.779 1.00 17.24 ?  154  MET B C    1 
ATOM   8527  O O    . MET B 1 154  ? 109.930 134.283 121.235 1.00 16.41 ?  154  MET B O    1 
ATOM   8528  C CB   . MET B 1 154  ? 106.968 133.384 122.249 1.00 13.50 ?  154  MET B CB   1 
ATOM   8529  C CG   . MET B 1 154  ? 107.323 134.616 123.068 1.00 14.13 ?  154  MET B CG   1 
ATOM   8530  S SD   . MET B 1 154  ? 105.892 135.458 123.767 1.00 29.93 ?  154  MET B SD   1 
ATOM   8531  C CE   . MET B 1 154  ? 104.991 134.079 124.465 1.00 13.47 ?  154  MET B CE   1 
ATOM   8532  N N    . ASP B 1 155  ? 108.544 133.812 119.524 1.00 19.19 ?  155  ASP B N    1 
ATOM   8533  C CA   . ASP B 1 155  ? 109.070 134.867 118.672 1.00 20.06 ?  155  ASP B CA   1 
ATOM   8534  C C    . ASP B 1 155  ? 108.365 136.182 118.984 1.00 22.60 ?  155  ASP B C    1 
ATOM   8535  O O    . ASP B 1 155  ? 107.176 136.212 119.316 1.00 23.89 ?  155  ASP B O    1 
ATOM   8536  C CB   . ASP B 1 155  ? 108.920 134.500 117.193 1.00 18.50 ?  155  ASP B CB   1 
ATOM   8537  C CG   . ASP B 1 155  ? 107.501 134.664 116.683 1.00 21.78 ?  155  ASP B CG   1 
ATOM   8538  O OD1  . ASP B 1 155  ? 106.563 134.212 117.373 1.00 21.38 ?  155  ASP B OD1  1 
ATOM   8539  O OD2  . ASP B 1 155  ? 107.323 135.242 115.590 1.00 27.96 ?  155  ASP B OD2  1 
ATOM   8540  N N    . VAL B 1 156  ? 109.116 137.276 118.896 1.00 20.94 ?  156  VAL B N    1 
ATOM   8541  C CA   . VAL B 1 156  ? 108.650 138.555 119.414 1.00 20.62 ?  156  VAL B CA   1 
ATOM   8542  C C    . VAL B 1 156  ? 108.486 139.623 118.343 1.00 22.89 ?  156  VAL B C    1 
ATOM   8543  O O    . VAL B 1 156  ? 107.809 140.631 118.605 1.00 22.22 ?  156  VAL B O    1 
ATOM   8544  C CB   . VAL B 1 156  ? 109.583 139.068 120.529 1.00 19.84 ?  156  VAL B CB   1 
ATOM   8545  C CG1  . VAL B 1 156  ? 109.408 138.238 121.786 1.00 20.25 ?  156  VAL B CG1  1 
ATOM   8546  C CG2  . VAL B 1 156  ? 111.027 139.043 120.061 1.00 17.41 ?  156  VAL B CG2  1 
ATOM   8547  N N    . HIS B 1 157  ? 109.062 139.457 117.150 1.00 24.61 ?  157  HIS B N    1 
ATOM   8548  C CA   . HIS B 1 157  ? 109.046 140.527 116.156 1.00 23.25 ?  157  HIS B CA   1 
ATOM   8549  C C    . HIS B 1 157  ? 107.647 140.832 115.635 1.00 20.39 ?  157  HIS B C    1 
ATOM   8550  O O    . HIS B 1 157  ? 107.420 141.930 115.117 1.00 21.00 ?  157  HIS B O    1 
ATOM   8551  C CB   . HIS B 1 157  ? 109.976 140.178 114.995 1.00 22.37 ?  157  HIS B CB   1 
ATOM   8552  C CG   . HIS B 1 157  ? 111.425 140.389 115.304 1.00 23.86 ?  157  HIS B CG   1 
ATOM   8553  N ND1  . HIS B 1 157  ? 111.921 141.593 115.754 1.00 28.00 ?  157  HIS B ND1  1 
ATOM   8554  C CD2  . HIS B 1 157  ? 112.484 139.549 115.233 1.00 22.43 ?  157  HIS B CD2  1 
ATOM   8555  C CE1  . HIS B 1 157  ? 113.224 141.487 115.944 1.00 26.06 ?  157  HIS B CE1  1 
ATOM   8556  N NE2  . HIS B 1 157  ? 113.591 140.256 115.635 1.00 26.74 ?  157  HIS B NE2  1 
ATOM   8557  N N    . THR B 1 158  ? 106.709 139.895 115.759 1.00 19.09 ?  158  THR B N    1 
ATOM   8558  C CA   . THR B 1 158  ? 105.312 140.181 115.463 1.00 22.07 ?  158  THR B CA   1 
ATOM   8559  C C    . THR B 1 158  ? 104.533 140.599 116.701 1.00 22.18 ?  158  THR B C    1 
ATOM   8560  O O    . THR B 1 158  ? 103.600 141.404 116.597 1.00 24.28 ?  158  THR B O    1 
ATOM   8561  C CB   . THR B 1 158  ? 104.641 138.960 114.828 1.00 21.66 ?  158  THR B CB   1 
ATOM   8562  O OG1  . THR B 1 158  ? 104.749 137.840 115.714 1.00 19.48 ?  158  THR B OG1  1 
ATOM   8563  C CG2  . THR B 1 158  ? 105.303 138.617 113.501 1.00 19.74 ?  158  THR B CG2  1 
ATOM   8564  N N    . PHE B 1 159  ? 104.899 140.068 117.870 1.00 18.91 ?  159  PHE B N    1 
ATOM   8565  C CA   . PHE B 1 159  ? 104.221 140.416 119.113 1.00 14.91 ?  159  PHE B CA   1 
ATOM   8566  C C    . PHE B 1 159  ? 104.631 141.794 119.621 1.00 19.40 ?  159  PHE B C    1 
ATOM   8567  O O    . PHE B 1 159  ? 103.803 142.506 120.201 1.00 22.99 ?  159  PHE B O    1 
ATOM   8568  C CB   . PHE B 1 159  ? 104.504 139.340 120.167 1.00 17.11 ?  159  PHE B CB   1 
ATOM   8569  C CG   . PHE B 1 159  ? 104.287 139.791 121.586 1.00 21.29 ?  159  PHE B CG   1 
ATOM   8570  C CD1  . PHE B 1 159  ? 103.015 140.093 122.050 1.00 21.22 ?  159  PHE B CD1  1 
ATOM   8571  C CD2  . PHE B 1 159  ? 105.355 139.898 122.461 1.00 18.65 ?  159  PHE B CD2  1 
ATOM   8572  C CE1  . PHE B 1 159  ? 102.819 140.503 123.355 1.00 19.01 ?  159  PHE B CE1  1 
ATOM   8573  C CE2  . PHE B 1 159  ? 105.164 140.306 123.767 1.00 14.55 ?  159  PHE B CE2  1 
ATOM   8574  C CZ   . PHE B 1 159  ? 103.894 140.609 124.214 1.00 14.93 ?  159  PHE B CZ   1 
ATOM   8575  N N    . MET B 1 160  ? 105.882 142.197 119.402 1.00 21.09 ?  160  MET B N    1 
ATOM   8576  C CA   . MET B 1 160  ? 106.362 143.485 119.888 1.00 20.62 ?  160  MET B CA   1 
ATOM   8577  C C    . MET B 1 160  ? 106.009 144.641 118.961 1.00 23.20 ?  160  MET B C    1 
ATOM   8578  O O    . MET B 1 160  ? 106.359 145.785 119.269 1.00 25.88 ?  160  MET B O    1 
ATOM   8579  C CB   . MET B 1 160  ? 107.879 143.440 120.099 1.00 24.69 ?  160  MET B CB   1 
ATOM   8580  C CG   . MET B 1 160  ? 108.302 142.812 121.421 1.00 28.40 ?  160  MET B CG   1 
ATOM   8581  S SD   . MET B 1 160  ? 110.089 142.803 121.664 1.00 34.57 ?  160  MET B SD   1 
ATOM   8582  C CE   . MET B 1 160  ? 110.209 143.482 123.317 1.00 25.52 ?  160  MET B CE   1 
ATOM   8583  N N    . ARG B 1 161  ? 105.343 144.376 117.834 1.00 21.75 ?  161  ARG B N    1 
ATOM   8584  C CA   . ARG B 1 161  ? 104.849 145.465 116.998 1.00 22.48 ?  161  ARG B CA   1 
ATOM   8585  C C    . ARG B 1 161  ? 103.709 146.208 117.684 1.00 20.35 ?  161  ARG B C    1 
ATOM   8586  O O    . ARG B 1 161  ? 103.649 147.443 117.641 1.00 20.20 ?  161  ARG B O    1 
ATOM   8587  C CB   . ARG B 1 161  ? 104.398 144.926 115.640 1.00 26.65 ?  161  ARG B CB   1 
ATOM   8588  C CG   . ARG B 1 161  ? 105.498 144.867 114.594 1.00 25.56 ?  161  ARG B CG   1 
ATOM   8589  C CD   . ARG B 1 161  ? 104.936 144.527 113.223 1.00 21.37 ?  161  ARG B CD   1 
ATOM   8590  N NE   . ARG B 1 161  ? 105.731 143.511 112.544 1.00 22.52 ?  161  ARG B NE   1 
ATOM   8591  C CZ   . ARG B 1 161  ? 105.260 142.340 112.138 1.00 23.50 ?  161  ARG B CZ   1 
ATOM   8592  N NH1  . ARG B 1 161  ? 103.993 142.005 112.318 1.00 22.58 ?  161  ARG B NH1  1 
ATOM   8593  N NH2  . ARG B 1 161  ? 106.081 141.483 111.536 1.00 22.44 ?  161  ARG B NH2  1 
ATOM   8594  N N    . SER B 1 162  ? 102.797 145.472 118.320 1.00 15.82 ?  162  SER B N    1 
ATOM   8595  C CA   . SER B 1 162  ? 101.689 146.046 119.073 1.00 22.62 ?  162  SER B CA   1 
ATOM   8596  C C    . SER B 1 162  ? 101.791 145.735 120.562 1.00 21.33 ?  162  SER B C    1 
ATOM   8597  O O    . SER B 1 162  ? 100.784 145.401 121.192 1.00 18.39 ?  162  SER B O    1 
ATOM   8598  C CB   . SER B 1 162  ? 100.356 145.546 118.515 1.00 24.07 ?  162  SER B CB   1 
ATOM   8599  O OG   . SER B 1 162  ? 100.296 144.130 118.529 1.00 23.20 ?  162  SER B OG   1 
ATOM   8600  N N    . PHE B 1 163  ? 102.995 145.847 121.130 1.00 20.97 ?  163  PHE B N    1 
ATOM   8601  C CA   . PHE B 1 163  ? 103.297 145.368 122.475 1.00 16.94 ?  163  PHE B CA   1 
ATOM   8602  C C    . PHE B 1 163  ? 102.445 146.023 123.562 1.00 19.89 ?  163  PHE B C    1 
ATOM   8603  O O    . PHE B 1 163  ? 101.892 145.339 124.433 1.00 21.44 ?  163  PHE B O    1 
ATOM   8604  C CB   . PHE B 1 163  ? 104.789 145.596 122.745 1.00 17.38 ?  163  PHE B CB   1 
ATOM   8605  C CG   . PHE B 1 163  ? 105.241 145.155 124.104 1.00 22.21 ?  163  PHE B CG   1 
ATOM   8606  C CD1  . PHE B 1 163  ? 105.393 143.810 124.397 1.00 25.37 ?  163  PHE B CD1  1 
ATOM   8607  C CD2  . PHE B 1 163  ? 105.533 146.087 125.086 1.00 19.67 ?  163  PHE B CD2  1 
ATOM   8608  C CE1  . PHE B 1 163  ? 105.817 143.403 125.647 1.00 19.94 ?  163  PHE B CE1  1 
ATOM   8609  C CE2  . PHE B 1 163  ? 105.957 145.687 126.337 1.00 20.94 ?  163  PHE B CE2  1 
ATOM   8610  C CZ   . PHE B 1 163  ? 106.100 144.342 126.618 1.00 18.71 ?  163  PHE B CZ   1 
ATOM   8611  N N    . SER B 1 164  ? 102.331 147.354 123.520 1.00 24.90 ?  164  SER B N    1 
ATOM   8612  C CA   . SER B 1 164  ? 101.641 148.089 124.579 1.00 22.84 ?  164  SER B CA   1 
ATOM   8613  C C    . SER B 1 164  ? 100.153 147.752 124.620 1.00 21.61 ?  164  SER B C    1 
ATOM   8614  O O    . SER B 1 164  ? 99.572  147.556 125.697 1.00 24.29 ?  164  SER B O    1 
ATOM   8615  C CB   . SER B 1 164  ? 101.846 149.591 124.379 1.00 18.19 ?  164  SER B CB   1 
ATOM   8616  O OG   . SER B 1 164  ? 103.224 149.906 124.268 1.00 19.90 ?  164  SER B OG   1 
ATOM   8617  N N    . GLN B 1 165  ? 99.522  147.679 123.446 1.00 18.08 ?  165  GLN B N    1 
ATOM   8618  C CA   . GLN B 1 165  ? 98.096  147.378 123.375 1.00 18.11 ?  165  GLN B CA   1 
ATOM   8619  C C    . GLN B 1 165  ? 97.804  145.965 123.871 1.00 21.61 ?  165  GLN B C    1 
ATOM   8620  O O    . GLN B 1 165  ? 96.824  145.736 124.592 1.00 25.27 ?  165  GLN B O    1 
ATOM   8621  C CB   . GLN B 1 165  ? 97.604  147.569 121.940 1.00 18.99 ?  165  GLN B CB   1 
ATOM   8622  C CG   . GLN B 1 165  ? 96.198  147.072 121.684 1.00 22.11 ?  165  GLN B CG   1 
ATOM   8623  C CD   . GLN B 1 165  ? 96.182  145.700 121.047 1.00 22.65 ?  165  GLN B CD   1 
ATOM   8624  O OE1  . GLN B 1 165  ? 96.998  145.400 120.176 1.00 24.59 ?  165  GLN B OE1  1 
ATOM   8625  N NE2  . GLN B 1 165  ? 95.258  144.854 121.487 1.00 21.70 ?  165  GLN B NE2  1 
ATOM   8626  N N    . VAL B 1 166  ? 98.649  145.002 123.492 1.00 21.49 ?  166  VAL B N    1 
ATOM   8627  C CA   . VAL B 1 166  ? 98.471  143.625 123.948 1.00 23.95 ?  166  VAL B CA   1 
ATOM   8628  C C    . VAL B 1 166  ? 98.672  143.532 125.457 1.00 17.41 ?  166  VAL B C    1 
ATOM   8629  O O    . VAL B 1 166  ? 97.960  142.790 126.149 1.00 17.52 ?  166  VAL B O    1 
ATOM   8630  C CB   . VAL B 1 166  ? 99.416  142.681 123.178 1.00 24.32 ?  166  VAL B CB   1 
ATOM   8631  C CG1  . VAL B 1 166  ? 99.298  141.257 123.693 1.00 19.48 ?  166  VAL B CG1  1 
ATOM   8632  C CG2  . VAL B 1 166  ? 99.094  142.716 121.692 1.00 19.50 ?  166  VAL B CG2  1 
ATOM   8633  N N    . CYS B 1 167  ? 99.634  144.294 125.992 1.00 16.44 ?  167  CYS B N    1 
ATOM   8634  C CA   . CYS B 1 167  ? 99.821  144.355 127.440 1.00 21.67 ?  167  CYS B CA   1 
ATOM   8635  C C    . CYS B 1 167  ? 98.565  144.863 128.138 1.00 25.59 ?  167  CYS B C    1 
ATOM   8636  O O    . CYS B 1 167  ? 98.105  144.275 129.127 1.00 25.29 ?  167  CYS B O    1 
ATOM   8637  C CB   . CYS B 1 167  ? 101.016 145.249 127.777 1.00 18.43 ?  167  CYS B CB   1 
ATOM   8638  S SG   . CYS B 1 167  ? 102.634 144.521 127.444 1.00 34.76 ?  167  CYS B SG   1 
ATOM   8639  N N    . ILE B 1 168  ? 97.992  145.954 127.619 1.00 20.35 ?  168  ILE B N    1 
ATOM   8640  C CA   . ILE B 1 168  ? 96.783  146.531 128.209 1.00 18.19 ?  168  ILE B CA   1 
ATOM   8641  C C    . ILE B 1 168  ? 95.637  145.524 128.169 1.00 19.10 ?  168  ILE B C    1 
ATOM   8642  O O    . ILE B 1 168  ? 94.917  145.332 129.160 1.00 25.67 ?  168  ILE B O    1 
ATOM   8643  C CB   . ILE B 1 168  ? 96.411  147.841 127.488 1.00 23.73 ?  168  ILE B CB   1 
ATOM   8644  C CG1  . ILE B 1 168  ? 97.428  148.941 127.807 1.00 19.95 ?  168  ILE B CG1  1 
ATOM   8645  C CG2  . ILE B 1 168  ? 95.004  148.288 127.857 1.00 23.28 ?  168  ILE B CG2  1 
ATOM   8646  C CD1  . ILE B 1 168  ? 97.371  149.439 129.237 1.00 18.97 ?  168  ILE B CD1  1 
ATOM   8647  N N    . LEU B 1 169  ? 95.470  144.852 127.025 1.00 13.82 ?  169  LEU B N    1 
ATOM   8648  C CA   . LEU B 1 169  ? 94.400  143.870 126.861 1.00 18.08 ?  169  LEU B CA   1 
ATOM   8649  C C    . LEU B 1 169  ? 94.535  142.721 127.855 1.00 18.16 ?  169  LEU B C    1 
ATOM   8650  O O    . LEU B 1 169  ? 93.560  142.336 128.517 1.00 19.16 ?  169  LEU B O    1 
ATOM   8651  C CB   . LEU B 1 169  ? 94.410  143.345 125.422 1.00 19.70 ?  169  LEU B CB   1 
ATOM   8652  C CG   . LEU B 1 169  ? 93.902  141.932 125.120 1.00 23.46 ?  169  LEU B CG   1 
ATOM   8653  C CD1  . LEU B 1 169  ? 92.383  141.846 125.208 1.00 26.22 ?  169  LEU B CD1  1 
ATOM   8654  C CD2  . LEU B 1 169  ? 94.396  141.468 123.756 1.00 19.93 ?  169  LEU B CD2  1 
ATOM   8655  N N    . ALA B 1 170  ? 95.748  142.171 127.980 1.00 19.76 ?  170  ALA B N    1 
ATOM   8656  C CA   . ALA B 1 170  ? 95.970  141.041 128.879 1.00 19.76 ?  170  ALA B CA   1 
ATOM   8657  C C    . ALA B 1 170  ? 95.723  141.430 130.331 1.00 19.86 ?  170  ALA B C    1 
ATOM   8658  O O    . ALA B 1 170  ? 95.060  140.694 131.079 1.00 15.80 ?  170  ALA B O    1 
ATOM   8659  C CB   . ALA B 1 170  ? 97.390  140.505 128.702 1.00 17.18 ?  170  ALA B CB   1 
ATOM   8660  N N    . LEU B 1 171  ? 96.245  142.591 130.746 1.00 19.57 ?  171  LEU B N    1 
ATOM   8661  C CA   . LEU B 1 171  ? 96.052  143.031 132.125 1.00 21.64 ?  171  LEU B CA   1 
ATOM   8662  C C    . LEU B 1 171  ? 94.574  143.241 132.432 1.00 17.00 ?  171  LEU B C    1 
ATOM   8663  O O    . LEU B 1 171  ? 94.070  142.766 133.458 1.00 16.89 ?  171  LEU B O    1 
ATOM   8664  C CB   . LEU B 1 171  ? 96.848  144.310 132.394 1.00 18.77 ?  171  LEU B CB   1 
ATOM   8665  C CG   . LEU B 1 171  ? 98.377  144.242 132.307 1.00 16.36 ?  171  LEU B CG   1 
ATOM   8666  C CD1  . LEU B 1 171  ? 99.005  145.472 132.945 1.00 19.96 ?  171  LEU B CD1  1 
ATOM   8667  C CD2  . LEU B 1 171  ? 98.923  142.971 132.937 1.00 15.92 ?  171  LEU B CD2  1 
ATOM   8668  N N    . PHE B 1 172  ? 93.852  143.918 131.531 1.00 13.62 ?  172  PHE B N    1 
ATOM   8669  C CA   . PHE B 1 172  ? 92.440  144.199 131.775 1.00 20.16 ?  172  PHE B CA   1 
ATOM   8670  C C    . PHE B 1 172  ? 91.621  142.915 131.846 1.00 22.81 ?  172  PHE B C    1 
ATOM   8671  O O    . PHE B 1 172  ? 90.766  142.761 132.734 1.00 21.98 ?  172  PHE B O    1 
ATOM   8672  C CB   . PHE B 1 172  ? 91.899  145.124 130.686 1.00 22.72 ?  172  PHE B CB   1 
ATOM   8673  C CG   . PHE B 1 172  ? 92.087  146.586 130.981 1.00 25.61 ?  172  PHE B CG   1 
ATOM   8674  C CD1  . PHE B 1 172  ? 93.323  147.074 131.378 1.00 22.38 ?  172  PHE B CD1  1 
ATOM   8675  C CD2  . PHE B 1 172  ? 91.032  147.473 130.855 1.00 23.73 ?  172  PHE B CD2  1 
ATOM   8676  C CE1  . PHE B 1 172  ? 93.502  148.417 131.647 1.00 20.36 ?  172  PHE B CE1  1 
ATOM   8677  C CE2  . PHE B 1 172  ? 91.204  148.819 131.122 1.00 21.81 ?  172  PHE B CE2  1 
ATOM   8678  C CZ   . PHE B 1 172  ? 92.441  149.291 131.519 1.00 22.38 ?  172  PHE B CZ   1 
ATOM   8679  N N    . GLY B 1 173  ? 91.878  141.977 130.930 1.00 18.11 ?  173  GLY B N    1 
ATOM   8680  C CA   . GLY B 1 173  ? 91.185  140.703 130.929 1.00 14.14 ?  173  GLY B CA   1 
ATOM   8681  C C    . GLY B 1 173  ? 91.407  139.894 132.189 1.00 15.94 ?  173  GLY B C    1 
ATOM   8682  O O    . GLY B 1 173  ? 90.450  139.360 132.770 1.00 18.01 ?  173  GLY B O    1 
ATOM   8683  N N    . LEU B 1 174  ? 92.665  139.807 132.636 1.00 15.77 ?  174  LEU B N    1 
ATOM   8684  C CA   . LEU B 1 174  ? 92.938  139.081 133.872 1.00 15.49 ?  174  LEU B CA   1 
ATOM   8685  C C    . LEU B 1 174  ? 92.250  139.735 135.061 1.00 16.57 ?  174  LEU B C    1 
ATOM   8686  O O    . LEU B 1 174  ? 91.671  139.042 135.908 1.00 19.37 ?  174  LEU B O    1 
ATOM   8687  C CB   . LEU B 1 174  ? 94.440  138.968 134.121 1.00 16.82 ?  174  LEU B CB   1 
ATOM   8688  C CG   . LEU B 1 174  ? 94.692  138.107 135.364 1.00 16.80 ?  174  LEU B CG   1 
ATOM   8689  C CD1  . LEU B 1 174  ? 95.628  136.983 135.073 1.00 15.14 ?  174  LEU B CD1  1 
ATOM   8690  C CD2  . LEU B 1 174  ? 95.234  138.940 136.513 1.00 11.39 ?  174  LEU B CD2  1 
ATOM   8691  N N    . VAL B 1 175  ? 92.296  141.070 135.142 1.00 18.91 ?  175  VAL B N    1 
ATOM   8692  C CA   . VAL B 1 175  ? 91.700  141.754 136.290 1.00 19.15 ?  175  VAL B CA   1 
ATOM   8693  C C    . VAL B 1 175  ? 90.199  141.495 136.350 1.00 13.05 ?  175  VAL B C    1 
ATOM   8694  O O    . VAL B 1 175  ? 89.660  141.122 137.404 1.00 10.72 ?  175  VAL B O    1 
ATOM   8695  C CB   . VAL B 1 175  ? 92.020  143.260 136.257 1.00 22.06 ?  175  VAL B CB   1 
ATOM   8696  C CG1  . VAL B 1 175  ? 91.268  143.976 137.360 1.00 17.87 ?  175  VAL B CG1  1 
ATOM   8697  C CG2  . VAL B 1 175  ? 93.507  143.487 136.455 1.00 19.38 ?  175  VAL B CG2  1 
ATOM   8698  N N    . VAL B 1 176  ? 89.505  141.639 135.214 1.00 10.80 ?  176  VAL B N    1 
ATOM   8699  C CA   . VAL B 1 176  ? 88.055  141.454 135.243 1.00 16.49 ?  176  VAL B CA   1 
ATOM   8700  C C    . VAL B 1 176  ? 87.695  140.000 135.557 1.00 18.00 ?  176  VAL B C    1 
ATOM   8701  O O    . VAL B 1 176  ? 86.808  139.741 136.384 1.00 18.13 ?  176  VAL B O    1 
ATOM   8702  C CB   . VAL B 1 176  ? 87.393  141.960 133.942 1.00 18.73 ?  176  VAL B CB   1 
ATOM   8703  C CG1  . VAL B 1 176  ? 87.586  143.463 133.805 1.00 18.98 ?  176  VAL B CG1  1 
ATOM   8704  C CG2  . VAL B 1 176  ? 87.908  141.248 132.703 1.00 20.31 ?  176  VAL B CG2  1 
ATOM   8705  N N    . ALA B 1 177  ? 88.401  139.033 134.951 1.00 16.72 ?  177  ALA B N    1 
ATOM   8706  C CA   . ALA B 1 177  ? 88.089  137.627 135.203 1.00 12.56 ?  177  ALA B CA   1 
ATOM   8707  C C    . ALA B 1 177  ? 88.319  137.267 136.666 1.00 13.28 ?  177  ALA B C    1 
ATOM   8708  O O    . ALA B 1 177  ? 87.531  136.525 137.271 1.00 13.57 ?  177  ALA B O    1 
ATOM   8709  C CB   . ALA B 1 177  ? 88.920  136.731 134.285 1.00 8.15  ?  177  ALA B CB   1 
ATOM   8710  N N    . SER B 1 178  ? 89.390  137.806 137.257 1.00 12.76 ?  178  SER B N    1 
ATOM   8711  C CA   . SER B 1 178  ? 89.662  137.568 138.669 1.00 6.03  ?  178  SER B CA   1 
ATOM   8712  C C    . SER B 1 178  ? 88.554  138.129 139.553 1.00 7.84  ?  178  SER B C    1 
ATOM   8713  O O    . SER B 1 178  ? 88.154  137.486 140.532 1.00 10.54 ?  178  SER B O    1 
ATOM   8714  C CB   . SER B 1 178  ? 91.011  138.175 139.049 1.00 7.24  ?  178  SER B CB   1 
ATOM   8715  O OG   . SER B 1 178  ? 91.955  137.996 138.008 1.00 8.88  ?  178  SER B OG   1 
ATOM   8716  N N    . VAL B 1 179  ? 88.043  139.324 139.229 1.00 11.12 ?  179  VAL B N    1 
ATOM   8717  C CA   . VAL B 1 179  ? 86.977  139.901 140.053 1.00 10.89 ?  179  VAL B CA   1 
ATOM   8718  C C    . VAL B 1 179  ? 85.696  139.073 139.963 1.00 16.22 ?  179  VAL B C    1 
ATOM   8719  O O    . VAL B 1 179  ? 85.035  138.827 140.983 1.00 19.20 ?  179  VAL B O    1 
ATOM   8720  C CB   . VAL B 1 179  ? 86.728  141.377 139.697 1.00 13.39 ?  179  VAL B CB   1 
ATOM   8721  C CG1  . VAL B 1 179  ? 85.744  141.979 140.678 1.00 16.30 ?  179  VAL B CG1  1 
ATOM   8722  C CG2  . VAL B 1 179  ? 88.011  142.157 139.817 1.00 12.81 ?  179  VAL B CG2  1 
ATOM   8723  N N    . LEU B 1 180  ? 85.312  138.633 138.754 1.00 11.13 ?  180  LEU B N    1 
ATOM   8724  C CA   . LEU B 1 180  ? 84.113  137.786 138.679 1.00 12.80 ?  180  LEU B CA   1 
ATOM   8725  C C    . LEU B 1 180  ? 84.298  136.463 139.421 1.00 10.44 ?  180  LEU B C    1 
ATOM   8726  O O    . LEU B 1 180  ? 83.369  135.994 140.096 1.00 11.40 ?  180  LEU B O    1 
ATOM   8727  C CB   . LEU B 1 180  ? 83.638  137.520 137.242 1.00 13.00 ?  180  LEU B CB   1 
ATOM   8728  C CG   . LEU B 1 180  ? 83.054  138.546 136.245 1.00 13.94 ?  180  LEU B CG   1 
ATOM   8729  C CD1  . LEU B 1 180  ? 82.060  139.476 136.952 1.00 10.75 ?  180  LEU B CD1  1 
ATOM   8730  C CD2  . LEU B 1 180  ? 83.993  139.317 135.342 1.00 15.60 ?  180  LEU B CD2  1 
ATOM   8731  N N    . THR B 1 181  ? 85.483  135.851 139.329 1.00 10.30 ?  181  THR B N    1 
ATOM   8732  C CA   . THR B 1 181  ? 85.697  134.599 140.052 1.00 12.48 ?  181  THR B CA   1 
ATOM   8733  C C    . THR B 1 181  ? 85.666  134.813 141.565 1.00 12.39 ?  181  THR B C    1 
ATOM   8734  O O    . THR B 1 181  ? 85.155  133.966 142.307 1.00 11.42 ?  181  THR B O    1 
ATOM   8735  C CB   . THR B 1 181  ? 87.012  133.950 139.620 1.00 15.16 ?  181  THR B CB   1 
ATOM   8736  O OG1  . THR B 1 181  ? 87.138  134.032 138.196 1.00 14.27 ?  181  THR B OG1  1 
ATOM   8737  C CG2  . THR B 1 181  ? 87.032  132.485 140.025 1.00 9.58  ?  181  THR B CG2  1 
ATOM   8738  N N    . ALA B 1 182  ? 86.196  135.944 142.043 1.00 11.80 ?  182  ALA B N    1 
ATOM   8739  C CA   . ALA B 1 182  ? 86.161  136.233 143.477 1.00 10.61 ?  182  ALA B CA   1 
ATOM   8740  C C    . ALA B 1 182  ? 84.735  136.477 143.971 1.00 19.29 ?  182  ALA B C    1 
ATOM   8741  O O    . ALA B 1 182  ? 84.363  136.038 145.071 1.00 19.53 ?  182  ALA B O    1 
ATOM   8742  C CB   . ALA B 1 182  ? 87.056  137.433 143.787 1.00 7.64  ?  182  ALA B CB   1 
ATOM   8743  N N    . VAL B 1 183  ? 83.924  137.181 143.176 1.00 19.94 ?  183  VAL B N    1 
ATOM   8744  C CA   . VAL B 1 183  ? 82.522  137.388 143.541 1.00 15.96 ?  183  VAL B CA   1 
ATOM   8745  C C    . VAL B 1 183  ? 81.780  136.055 143.599 1.00 16.19 ?  183  VAL B C    1 
ATOM   8746  O O    . VAL B 1 183  ? 80.989  135.801 144.524 1.00 17.60 ?  183  VAL B O    1 
ATOM   8747  C CB   . VAL B 1 183  ? 81.860  138.376 142.561 1.00 12.51 ?  183  VAL B CB   1 
ATOM   8748  C CG1  . VAL B 1 183  ? 80.363  138.450 142.792 1.00 14.77 ?  183  VAL B CG1  1 
ATOM   8749  C CG2  . VAL B 1 183  ? 82.473  139.756 142.719 1.00 15.17 ?  183  VAL B CG2  1 
ATOM   8750  N N    . LEU B 1 184  ? 82.035  135.177 142.620 1.00 17.00 ?  184  LEU B N    1 
ATOM   8751  C CA   . LEU B 1 184  ? 81.468  133.832 142.650 1.00 16.93 ?  184  LEU B CA   1 
ATOM   8752  C C    . LEU B 1 184  ? 81.916  133.045 143.874 1.00 18.24 ?  184  LEU B C    1 
ATOM   8753  O O    . LEU B 1 184  ? 81.102  132.331 144.470 1.00 16.69 ?  184  LEU B O    1 
ATOM   8754  C CB   . LEU B 1 184  ? 81.852  133.070 141.381 1.00 16.48 ?  184  LEU B CB   1 
ATOM   8755  C CG   . LEU B 1 184  ? 81.504  131.580 141.324 1.00 18.45 ?  184  LEU B CG   1 
ATOM   8756  C CD1  . LEU B 1 184  ? 80.053  131.374 140.915 1.00 16.89 ?  184  LEU B CD1  1 
ATOM   8757  C CD2  . LEU B 1 184  ? 82.447  130.840 140.389 1.00 17.32 ?  184  LEU B CD2  1 
ATOM   8758  N N    . ALA B 1 185  ? 83.182  133.171 144.269 1.00 17.35 ?  185  ALA B N    1 
ATOM   8759  C CA   . ALA B 1 185  ? 83.672  132.487 145.456 1.00 16.34 ?  185  ALA B CA   1 
ATOM   8760  C C    . ALA B 1 185  ? 83.024  132.995 146.735 1.00 16.95 ?  185  ALA B C    1 
ATOM   8761  O O    . ALA B 1 185  ? 82.878  132.217 147.684 1.00 12.77 ?  185  ALA B O    1 
ATOM   8762  C CB   . ALA B 1 185  ? 85.189  132.638 145.565 1.00 13.34 ?  185  ALA B CB   1 
ATOM   8763  N N    . MET B 1 186  ? 82.647  134.276 146.787 1.00 17.48 ?  186  MET B N    1 
ATOM   8764  C CA   . MET B 1 186  ? 81.920  134.788 147.950 1.00 16.45 ?  186  MET B CA   1 
ATOM   8765  C C    . MET B 1 186  ? 80.477  134.286 147.994 1.00 22.16 ?  186  MET B C    1 
ATOM   8766  O O    . MET B 1 186  ? 80.062  133.648 148.967 1.00 23.97 ?  186  MET B O    1 
ATOM   8767  C CB   . MET B 1 186  ? 81.892  136.325 147.982 1.00 17.36 ?  186  MET B CB   1 
ATOM   8768  C CG   . MET B 1 186  ? 83.156  137.100 148.361 1.00 20.27 ?  186  MET B CG   1 
ATOM   8769  S SD   . MET B 1 186  ? 82.663  138.844 148.348 1.00 34.04 ?  186  MET B SD   1 
ATOM   8770  C CE   . MET B 1 186  ? 84.230  139.694 148.445 1.00 20.38 ?  186  MET B CE   1 
ATOM   8771  N N    . ASN B 1 187  ? 79.693  134.587 146.956 1.00 23.73 ?  187  ASN B N    1 
ATOM   8772  C CA   . ASN B 1 187  ? 78.249  134.426 147.103 1.00 21.32 ?  187  ASN B CA   1 
ATOM   8773  C C    . ASN B 1 187  ? 77.823  132.963 147.023 1.00 21.96 ?  187  ASN B C    1 
ATOM   8774  O O    . ASN B 1 187  ? 76.958  132.525 147.791 1.00 21.41 ?  187  ASN B O    1 
ATOM   8775  C CB   . ASN B 1 187  ? 77.531  135.275 146.058 1.00 17.41 ?  187  ASN B CB   1 
ATOM   8776  C CG   . ASN B 1 187  ? 77.886  136.744 146.177 1.00 20.28 ?  187  ASN B CG   1 
ATOM   8777  O OD1  . ASN B 1 187  ? 77.221  137.506 146.878 1.00 26.14 ?  187  ASN B OD1  1 
ATOM   8778  N ND2  . ASN B 1 187  ? 78.947  137.147 145.493 1.00 19.49 ?  187  ASN B ND2  1 
ATOM   8779  N N    . LEU B 1 188  ? 78.443  132.181 146.141 1.00 17.91 ?  188  LEU B N    1 
ATOM   8780  C CA   . LEU B 1 188  ? 77.979  130.815 145.926 1.00 17.81 ?  188  LEU B CA   1 
ATOM   8781  C C    . LEU B 1 188  ? 78.527  129.857 146.981 1.00 16.30 ?  188  LEU B C    1 
ATOM   8782  O O    . LEU B 1 188  ? 77.770  129.081 147.575 1.00 19.43 ?  188  LEU B O    1 
ATOM   8783  C CB   . LEU B 1 188  ? 78.364  130.353 144.523 1.00 20.09 ?  188  LEU B CB   1 
ATOM   8784  C CG   . LEU B 1 188  ? 78.101  128.875 144.258 1.00 20.35 ?  188  LEU B CG   1 
ATOM   8785  C CD1  . LEU B 1 188  ? 76.685  128.698 143.734 1.00 17.40 ?  188  LEU B CD1  1 
ATOM   8786  C CD2  . LEU B 1 188  ? 79.118  128.318 143.288 1.00 20.85 ?  188  LEU B CD2  1 
ATOM   8787  N N    . PHE B 1 189  ? 79.835  129.897 147.230 1.00 16.50 ?  189  PHE B N    1 
ATOM   8788  C CA   . PHE B 1 189  ? 80.454  128.960 148.161 1.00 17.85 ?  189  PHE B CA   1 
ATOM   8789  C C    . PHE B 1 189  ? 80.008  129.242 149.592 1.00 18.15 ?  189  PHE B C    1 
ATOM   8790  O O    . PHE B 1 189  ? 79.785  130.393 149.975 1.00 21.39 ?  189  PHE B O    1 
ATOM   8791  C CB   . PHE B 1 189  ? 81.980  129.034 148.069 1.00 17.42 ?  189  PHE B CB   1 
ATOM   8792  C CG   . PHE B 1 189  ? 82.555  128.483 146.785 1.00 18.08 ?  189  PHE B CG   1 
ATOM   8793  C CD1  . PHE B 1 189  ? 81.754  127.852 145.847 1.00 17.99 ?  189  PHE B CD1  1 
ATOM   8794  C CD2  . PHE B 1 189  ? 83.911  128.600 146.522 1.00 18.46 ?  189  PHE B CD2  1 
ATOM   8795  C CE1  . PHE B 1 189  ? 82.293  127.354 144.674 1.00 16.87 ?  189  PHE B CE1  1 
ATOM   8796  C CE2  . PHE B 1 189  ? 84.454  128.102 145.351 1.00 16.11 ?  189  PHE B CE2  1 
ATOM   8797  C CZ   . PHE B 1 189  ? 83.643  127.479 144.428 1.00 15.59 ?  189  PHE B CZ   1 
ATOM   8798  N N    . ASN B 1 190  ? 79.880  128.179 150.387 1.00 14.20 ?  190  ASN B N    1 
ATOM   8799  C CA   . ASN B 1 190  ? 79.427  128.312 151.766 1.00 15.69 ?  190  ASN B CA   1 
ATOM   8800  C C    . ASN B 1 190  ? 80.556  128.600 152.746 1.00 19.23 ?  190  ASN B C    1 
ATOM   8801  O O    . ASN B 1 190  ? 80.277  128.872 153.919 1.00 20.59 ?  190  ASN B O    1 
ATOM   8802  C CB   . ASN B 1 190  ? 78.681  127.047 152.212 1.00 15.19 ?  190  ASN B CB   1 
ATOM   8803  C CG   . ASN B 1 190  ? 79.479  125.779 151.977 1.00 18.49 ?  190  ASN B CG   1 
ATOM   8804  O OD1  . ASN B 1 190  ? 80.578  125.813 151.424 1.00 21.00 ?  190  ASN B OD1  1 
ATOM   8805  N ND2  . ASN B 1 190  ? 78.928  124.648 152.404 1.00 19.99 ?  190  ASN B ND2  1 
ATOM   8806  N N    . TYR B 1 191  ? 81.811  128.543 152.307 1.00 17.68 ?  191  TYR B N    1 
ATOM   8807  C CA   . TYR B 1 191  ? 82.923  128.857 153.192 1.00 17.05 ?  191  TYR B CA   1 
ATOM   8808  C C    . TYR B 1 191  ? 82.952  130.348 153.503 1.00 19.64 ?  191  TYR B C    1 
ATOM   8809  O O    . TYR B 1 191  ? 82.715  131.187 152.630 1.00 21.36 ?  191  TYR B O    1 
ATOM   8810  C CB   . TYR B 1 191  ? 84.251  128.433 152.564 1.00 15.59 ?  191  TYR B CB   1 
ATOM   8811  C CG   . TYR B 1 191  ? 84.166  127.247 151.628 1.00 16.71 ?  191  TYR B CG   1 
ATOM   8812  C CD1  . TYR B 1 191  ? 83.964  125.963 152.116 1.00 16.17 ?  191  TYR B CD1  1 
ATOM   8813  C CD2  . TYR B 1 191  ? 84.309  127.411 150.257 1.00 15.01 ?  191  TYR B CD2  1 
ATOM   8814  C CE1  . TYR B 1 191  ? 83.895  124.878 151.262 1.00 15.87 ?  191  TYR B CE1  1 
ATOM   8815  C CE2  . TYR B 1 191  ? 84.241  126.333 149.396 1.00 12.77 ?  191  TYR B CE2  1 
ATOM   8816  C CZ   . TYR B 1 191  ? 84.034  125.069 149.903 1.00 15.07 ?  191  TYR B CZ   1 
ATOM   8817  O OH   . TYR B 1 191  ? 83.967  123.995 149.047 1.00 18.85 ?  191  TYR B OH   1 
ATOM   8818  N N    . ASN B 1 192  ? 83.245  130.678 154.759 1.00 19.13 ?  192  ASN B N    1 
ATOM   8819  C CA   . ASN B 1 192  ? 83.354  132.072 155.188 1.00 19.75 ?  192  ASN B CA   1 
ATOM   8820  C C    . ASN B 1 192  ? 84.685  132.618 154.684 1.00 21.83 ?  192  ASN B C    1 
ATOM   8821  O O    . ASN B 1 192  ? 85.699  132.593 155.382 1.00 26.31 ?  192  ASN B O    1 
ATOM   8822  C CB   . ASN B 1 192  ? 83.238  132.184 156.704 1.00 23.42 ?  192  ASN B CB   1 
ATOM   8823  C CG   . ASN B 1 192  ? 82.040  131.433 157.257 1.00 28.26 ?  192  ASN B CG   1 
ATOM   8824  O OD1  . ASN B 1 192  ? 81.202  130.935 156.505 1.00 24.58 ?  192  ASN B OD1  1 
ATOM   8825  N ND2  . ASN B 1 192  ? 81.957  131.344 158.580 1.00 27.85 ?  192  ASN B ND2  1 
ATOM   8826  N N    . TRP B 1 193  ? 84.679  133.118 153.451 1.00 14.45 ?  193  TRP B N    1 
ATOM   8827  C CA   . TRP B 1 193  ? 85.882  133.593 152.781 1.00 10.99 ?  193  TRP B CA   1 
ATOM   8828  C C    . TRP B 1 193  ? 85.843  135.111 152.656 1.00 16.09 ?  193  TRP B C    1 
ATOM   8829  O O    . TRP B 1 193  ? 84.815  135.682 152.277 1.00 19.70 ?  193  TRP B O    1 
ATOM   8830  C CB   . TRP B 1 193  ? 86.025  132.953 151.398 1.00 9.16  ?  193  TRP B CB   1 
ATOM   8831  C CG   . TRP B 1 193  ? 86.693  131.608 151.412 1.00 14.11 ?  193  TRP B CG   1 
ATOM   8832  C CD1  . TRP B 1 193  ? 87.081  130.895 152.508 1.00 14.57 ?  193  TRP B CD1  1 
ATOM   8833  C CD2  . TRP B 1 193  ? 87.059  130.820 150.273 1.00 12.42 ?  193  TRP B CD2  1 
ATOM   8834  N NE1  . TRP B 1 193  ? 87.661  129.710 152.123 1.00 12.70 ?  193  TRP B NE1  1 
ATOM   8835  C CE2  . TRP B 1 193  ? 87.660  129.641 150.755 1.00 12.86 ?  193  TRP B CE2  1 
ATOM   8836  C CE3  . TRP B 1 193  ? 86.935  130.997 148.893 1.00 11.83 ?  193  TRP B CE3  1 
ATOM   8837  C CZ2  . TRP B 1 193  ? 88.135  128.645 149.907 1.00 15.36 ?  193  TRP B CZ2  1 
ATOM   8838  C CZ3  . TRP B 1 193  ? 87.406  130.007 148.054 1.00 7.29  ?  193  TRP B CZ3  1 
ATOM   8839  C CH2  . TRP B 1 193  ? 87.999  128.847 148.563 1.00 11.54 ?  193  TRP B CH2  1 
ATOM   8840  N N    . ASN B 1 194  ? 86.965  135.756 152.973 1.00 16.70 ?  194  ASN B N    1 
ATOM   8841  C CA   . ASN B 1 194  ? 87.106  137.202 152.888 1.00 11.67 ?  194  ASN B CA   1 
ATOM   8842  C C    . ASN B 1 194  ? 87.341  137.616 151.434 1.00 16.31 ?  194  ASN B C    1 
ATOM   8843  O O    . ASN B 1 194  ? 87.406  136.785 150.526 1.00 20.54 ?  194  ASN B O    1 
ATOM   8844  C CB   . ASN B 1 194  ? 88.246  137.660 153.799 1.00 13.55 ?  194  ASN B CB   1 
ATOM   8845  C CG   . ASN B 1 194  ? 88.076  139.084 154.289 1.00 24.32 ?  194  ASN B CG   1 
ATOM   8846  O OD1  . ASN B 1 194  ? 86.963  139.608 154.340 1.00 27.50 ?  194  ASN B OD1  1 
ATOM   8847  N ND2  . ASN B 1 194  ? 89.183  139.712 154.670 1.00 20.86 ?  194  ASN B ND2  1 
ATOM   8848  N N    . PHE B 1 195  ? 87.465  138.925 151.198 1.00 20.17 ?  195  PHE B N    1 
ATOM   8849  C CA   . PHE B 1 195  ? 87.780  139.398 149.851 1.00 17.30 ?  195  PHE B CA   1 
ATOM   8850  C C    . PHE B 1 195  ? 89.205  139.052 149.440 1.00 15.23 ?  195  PHE B C    1 
ATOM   8851  O O    . PHE B 1 195  ? 89.456  138.793 148.259 1.00 16.46 ?  195  PHE B O    1 
ATOM   8852  C CB   . PHE B 1 195  ? 87.552  140.906 149.754 1.00 16.24 ?  195  PHE B CB   1 
ATOM   8853  C CG   . PHE B 1 195  ? 87.881  141.496 148.402 1.00 16.02 ?  195  PHE B CG   1 
ATOM   8854  C CD1  . PHE B 1 195  ? 87.165  141.147 147.266 1.00 9.48  ?  195  PHE B CD1  1 
ATOM   8855  C CD2  . PHE B 1 195  ? 88.916  142.413 148.275 1.00 18.86 ?  195  PHE B CD2  1 
ATOM   8856  C CE1  . PHE B 1 195  ? 87.475  141.700 146.036 1.00 12.98 ?  195  PHE B CE1  1 
ATOM   8857  C CE2  . PHE B 1 195  ? 89.235  142.970 147.048 1.00 17.73 ?  195  PHE B CE2  1 
ATOM   8858  C CZ   . PHE B 1 195  ? 88.513  142.615 145.927 1.00 16.28 ?  195  PHE B CZ   1 
ATOM   8859  N N    . SER B 1 196  ? 90.144  139.030 150.387 1.00 13.66 ?  196  SER B N    1 
ATOM   8860  C CA   . SER B 1 196  ? 91.526  138.722 150.037 1.00 10.18 ?  196  SER B CA   1 
ATOM   8861  C C    . SER B 1 196  ? 91.688  137.252 149.667 1.00 14.00 ?  196  SER B C    1 
ATOM   8862  O O    . SER B 1 196  ? 92.346  136.925 148.670 1.00 15.42 ?  196  SER B O    1 
ATOM   8863  C CB   . SER B 1 196  ? 92.452  139.092 151.193 1.00 11.55 ?  196  SER B CB   1 
ATOM   8864  O OG   . SER B 1 196  ? 91.878  138.740 152.440 1.00 13.52 ?  196  SER B OG   1 
ATOM   8865  N N    . GLU B 1 197  ? 91.085  136.356 150.451 1.00 15.28 ?  197  GLU B N    1 
ATOM   8866  C CA   . GLU B 1 197  ? 91.136  134.931 150.139 1.00 13.03 ?  197  GLU B CA   1 
ATOM   8867  C C    . GLU B 1 197  ? 90.417  134.627 148.830 1.00 12.81 ?  197  GLU B C    1 
ATOM   8868  O O    . GLU B 1 197  ? 90.909  133.844 148.009 1.00 15.68 ?  197  GLU B O    1 
ATOM   8869  C CB   . GLU B 1 197  ? 90.532  134.129 151.290 1.00 9.36  ?  197  GLU B CB   1 
ATOM   8870  C CG   . GLU B 1 197  ? 90.725  134.789 152.648 1.00 15.06 ?  197  GLU B CG   1 
ATOM   8871  C CD   . GLU B 1 197  ? 90.139  133.984 153.788 1.00 17.79 ?  197  GLU B CD   1 
ATOM   8872  O OE1  . GLU B 1 197  ? 90.678  132.901 154.094 1.00 14.64 ?  197  GLU B OE1  1 
ATOM   8873  O OE2  . GLU B 1 197  ? 89.142  134.439 154.387 1.00 19.26 ?  197  GLU B OE2  1 
ATOM   8874  N N    . ALA B 1 198  ? 89.260  135.258 148.608 1.00 7.79  ?  198  ALA B N    1 
ATOM   8875  C CA   . ALA B 1 198  ? 88.523  135.056 147.364 1.00 8.23  ?  198  ALA B CA   1 
ATOM   8876  C C    . ALA B 1 198  ? 89.282  135.611 146.165 1.00 12.42 ?  198  ALA B C    1 
ATOM   8877  O O    . ALA B 1 198  ? 89.229  135.035 145.074 1.00 20.28 ?  198  ALA B O    1 
ATOM   8878  C CB   . ALA B 1 198  ? 87.140  135.694 147.462 1.00 15.23 ?  198  ALA B CB   1 
ATOM   8879  N N    . MET B 1 199  ? 89.988  136.729 146.340 1.00 8.82  ?  199  MET B N    1 
ATOM   8880  C CA   . MET B 1 199  ? 90.741  137.303 145.230 1.00 4.80  ?  199  MET B CA   1 
ATOM   8881  C C    . MET B 1 199  ? 91.972  136.470 144.905 1.00 4.59  ?  199  MET B C    1 
ATOM   8882  O O    . MET B 1 199  ? 92.347  136.340 143.736 1.00 10.38 ?  199  MET B O    1 
ATOM   8883  C CB   . MET B 1 199  ? 91.137  138.743 145.547 1.00 9.85  ?  199  MET B CB   1 
ATOM   8884  C CG   . MET B 1 199  ? 90.311  139.781 144.814 1.00 11.82 ?  199  MET B CG   1 
ATOM   8885  S SD   . MET B 1 199  ? 90.184  139.461 143.045 1.00 21.89 ?  199  MET B SD   1 
ATOM   8886  C CE   . MET B 1 199  ? 91.886  139.683 142.539 1.00 9.19  ?  199  MET B CE   1 
ATOM   8887  N N    . MET B 1 200  ? 92.615  135.898 145.925 1.00 2.33  ?  200  MET B N    1 
ATOM   8888  C CA   . MET B 1 200  ? 93.707  134.961 145.675 1.00 2.62  ?  200  MET B CA   1 
ATOM   8889  C C    . MET B 1 200  ? 93.193  133.698 144.984 1.00 6.77  ?  200  MET B C    1 
ATOM   8890  O O    . MET B 1 200  ? 93.844  133.167 144.071 1.00 9.80  ?  200  MET B O    1 
ATOM   8891  C CB   . MET B 1 200  ? 94.418  134.657 146.997 1.00 4.26  ?  200  MET B CB   1 
ATOM   8892  C CG   . MET B 1 200  ? 95.251  133.396 147.048 1.00 7.60  ?  200  MET B CG   1 
ATOM   8893  S SD   . MET B 1 200  ? 95.973  133.153 148.689 1.00 8.65  ?  200  MET B SD   1 
ATOM   8894  C CE   . MET B 1 200  ? 94.549  132.643 149.645 1.00 8.10  ?  200  MET B CE   1 
ATOM   8895  N N    . PHE B 1 201  ? 92.005  133.234 145.384 1.00 4.66  ?  201  PHE B N    1 
ATOM   8896  C CA   . PHE B 1 201  ? 91.331  132.132 144.700 1.00 1.28  ?  201  PHE B CA   1 
ATOM   8897  C C    . PHE B 1 201  ? 91.088  132.455 143.229 1.00 1.87  ?  201  PHE B C    1 
ATOM   8898  O O    . PHE B 1 201  ? 91.375  131.639 142.346 1.00 6.70  ?  201  PHE B O    1 
ATOM   8899  C CB   . PHE B 1 201  ? 90.017  131.839 145.428 1.00 6.56  ?  201  PHE B CB   1 
ATOM   8900  C CG   . PHE B 1 201  ? 89.273  130.639 144.921 1.00 9.94  ?  201  PHE B CG   1 
ATOM   8901  C CD1  . PHE B 1 201  ? 89.518  129.383 145.448 1.00 7.23  ?  201  PHE B CD1  1 
ATOM   8902  C CD2  . PHE B 1 201  ? 88.276  130.777 143.970 1.00 7.51  ?  201  PHE B CD2  1 
ATOM   8903  C CE1  . PHE B 1 201  ? 88.815  128.282 145.005 1.00 2.16  ?  201  PHE B CE1  1 
ATOM   8904  C CE2  . PHE B 1 201  ? 87.571  129.679 143.522 1.00 6.71  ?  201  PHE B CE2  1 
ATOM   8905  C CZ   . PHE B 1 201  ? 87.841  128.431 144.040 1.00 8.16  ?  201  PHE B CZ   1 
ATOM   8906  N N    . GLY B 1 202  ? 90.560  133.647 142.950 1.00 0.00  ?  202  GLY B N    1 
ATOM   8907  C CA   . GLY B 1 202  ? 90.292  134.034 141.574 1.00 0.00  ?  202  GLY B CA   1 
ATOM   8908  C C    . GLY B 1 202  ? 91.553  134.242 140.758 1.00 0.00  ?  202  GLY B C    1 
ATOM   8909  O O    . GLY B 1 202  ? 91.564  134.006 139.547 1.00 9.55  ?  202  GLY B O    1 
ATOM   8910  N N    . ALA B 1 203  ? 92.626  134.705 141.401 1.00 0.57  ?  203  ALA B N    1 
ATOM   8911  C CA   . ALA B 1 203  ? 93.899  134.853 140.707 1.00 0.00  ?  203  ALA B CA   1 
ATOM   8912  C C    . ALA B 1 203  ? 94.515  133.504 140.376 1.00 0.00  ?  203  ALA B C    1 
ATOM   8913  O O    . ALA B 1 203  ? 95.252  133.388 139.391 1.00 0.67  ?  203  ALA B O    1 
ATOM   8914  C CB   . ALA B 1 203  ? 94.869  135.682 141.547 1.00 0.68  ?  203  ALA B CB   1 
ATOM   8915  N N    . ILE B 1 204  ? 94.244  132.482 141.191 1.00 5.62  ?  204  ILE B N    1 
ATOM   8916  C CA   . ILE B 1 204  ? 94.770  131.151 140.899 1.00 2.84  ?  204  ILE B CA   1 
ATOM   8917  C C    . ILE B 1 204  ? 94.112  130.576 139.647 1.00 3.78  ?  204  ILE B C    1 
ATOM   8918  O O    . ILE B 1 204  ? 94.789  130.059 138.751 1.00 4.68  ?  204  ILE B O    1 
ATOM   8919  C CB   . ILE B 1 204  ? 94.589  130.228 142.117 1.00 0.69  ?  204  ILE B CB   1 
ATOM   8920  C CG1  . ILE B 1 204  ? 95.715  130.464 143.122 1.00 1.64  ?  204  ILE B CG1  1 
ATOM   8921  C CG2  . ILE B 1 204  ? 94.582  128.768 141.696 1.00 0.74  ?  204  ILE B CG2  1 
ATOM   8922  C CD1  . ILE B 1 204  ? 95.673  129.540 144.311 1.00 2.40  ?  204  ILE B CD1  1 
ATOM   8923  N N    . MET B 1 205  ? 92.787  130.678 139.555 1.00 7.26  ?  205  MET B N    1 
ATOM   8924  C CA   . MET B 1 205  ? 92.027  130.066 138.471 1.00 4.22  ?  205  MET B CA   1 
ATOM   8925  C C    . MET B 1 205  ? 91.848  130.980 137.263 1.00 5.05  ?  205  MET B C    1 
ATOM   8926  O O    . MET B 1 205  ? 90.921  130.765 136.477 1.00 6.50  ?  205  MET B O    1 
ATOM   8927  C CB   . MET B 1 205  ? 90.655  129.612 138.977 1.00 0.00  ?  205  MET B CB   1 
ATOM   8928  C CG   . MET B 1 205  ? 90.613  128.174 139.470 1.00 3.67  ?  205  MET B CG   1 
ATOM   8929  S SD   . MET B 1 205  ? 89.649  127.999 140.981 1.00 21.21 ?  205  MET B SD   1 
ATOM   8930  C CE   . MET B 1 205  ? 90.942  128.097 142.214 1.00 10.58 ?  205  MET B CE   1 
ATOM   8931  N N    . SER B 1 206  ? 92.697  131.993 137.098 1.00 9.50  ?  206  SER B N    1 
ATOM   8932  C CA   . SER B 1 206  ? 92.643  132.871 135.936 1.00 8.87  ?  206  SER B CA   1 
ATOM   8933  C C    . SER B 1 206  ? 93.923  132.804 135.111 1.00 9.20  ?  206  SER B C    1 
ATOM   8934  O O    . SER B 1 206  ? 94.173  133.675 134.277 1.00 8.32  ?  206  SER B O    1 
ATOM   8935  C CB   . SER B 1 206  ? 92.358  134.312 136.357 1.00 5.87  ?  206  SER B CB   1 
ATOM   8936  O OG   . SER B 1 206  ? 90.965  134.568 136.370 1.00 6.57  ?  206  SER B OG   1 
ATOM   8937  N N    . ALA B 1 207  ? 94.734  131.771 135.326 1.00 9.33  ?  207  ALA B N    1 
ATOM   8938  C CA   . ALA B 1 207  ? 95.973  131.561 134.587 1.00 6.91  ?  207  ALA B CA   1 
ATOM   8939  C C    . ALA B 1 207  ? 95.776  130.379 133.650 1.00 12.70 ?  207  ALA B C    1 
ATOM   8940  O O    . ALA B 1 207  ? 95.539  129.255 134.106 1.00 17.81 ?  207  ALA B O    1 
ATOM   8941  C CB   . ALA B 1 207  ? 97.145  131.313 135.538 1.00 3.12  ?  207  ALA B CB   1 
ATOM   8942  N N    . THR B 1 208  ? 95.881  130.630 132.348 1.00 11.65 ?  208  THR B N    1 
ATOM   8943  C CA   . THR B 1 208  ? 95.535  129.663 131.316 1.00 9.30  ?  208  THR B CA   1 
ATOM   8944  C C    . THR B 1 208  ? 96.790  129.153 130.610 1.00 14.27 ?  208  THR B C    1 
ATOM   8945  O O    . THR B 1 208  ? 97.919  129.529 130.938 1.00 19.88 ?  208  THR B O    1 
ATOM   8946  C CB   . THR B 1 208  ? 94.567  130.283 130.305 1.00 13.00 ?  208  THR B CB   1 
ATOM   8947  O OG1  . THR B 1 208  ? 95.312  130.945 129.275 1.00 15.99 ?  208  THR B OG1  1 
ATOM   8948  C CG2  . THR B 1 208  ? 93.656  131.295 130.982 1.00 15.99 ?  208  THR B CG2  1 
ATOM   8949  N N    . ASP B 1 209  ? 96.572  128.329 129.582 1.00 12.79 ?  209  ASP B N    1 
ATOM   8950  C CA   . ASP B 1 209  ? 97.672  127.802 128.775 1.00 10.16 ?  209  ASP B CA   1 
ATOM   8951  C C    . ASP B 1 209  ? 97.153  127.640 127.350 1.00 15.90 ?  209  ASP B C    1 
ATOM   8952  O O    . ASP B 1 209  ? 96.196  126.899 127.128 1.00 17.64 ?  209  ASP B O    1 
ATOM   8953  C CB   . ASP B 1 209  ? 98.168  126.466 129.316 1.00 12.51 ?  209  ASP B CB   1 
ATOM   8954  C CG   . ASP B 1 209  ? 99.319  126.620 130.288 1.00 18.87 ?  209  ASP B CG   1 
ATOM   8955  O OD1  . ASP B 1 209  ? 99.857  127.740 130.407 1.00 20.80 ?  209  ASP B OD1  1 
ATOM   8956  O OD2  . ASP B 1 209  ? 99.694  125.615 130.926 1.00 18.81 ?  209  ASP B OD2  1 
ATOM   8957  N N    . PRO B 1 210  ? 97.767  128.327 126.373 1.00 18.49 ?  210  PRO B N    1 
ATOM   8958  C CA   . PRO B 1 210  ? 97.293  128.298 124.985 1.00 16.44 ?  210  PRO B CA   1 
ATOM   8959  C C    . PRO B 1 210  ? 97.933  127.207 124.142 1.00 15.54 ?  210  PRO B C    1 
ATOM   8960  O O    . PRO B 1 210  ? 97.839  127.262 122.912 1.00 18.16 ?  210  PRO B O    1 
ATOM   8961  C CB   . PRO B 1 210  ? 97.689  129.684 124.474 1.00 14.60 ?  210  PRO B CB   1 
ATOM   8962  C CG   . PRO B 1 210  ? 98.996  129.935 125.174 1.00 18.34 ?  210  PRO B CG   1 
ATOM   8963  C CD   . PRO B 1 210  ? 98.929  129.220 126.522 1.00 15.37 ?  210  PRO B CD   1 
ATOM   8964  N N    . VAL B 1 211  ? 98.596  126.237 124.782 1.00 18.62 ?  211  VAL B N    1 
ATOM   8965  C CA   . VAL B 1 211  ? 99.453  125.295 124.059 1.00 19.45 ?  211  VAL B CA   1 
ATOM   8966  C C    . VAL B 1 211  ? 98.655  124.486 123.040 1.00 21.50 ?  211  VAL B C    1 
ATOM   8967  O O    . VAL B 1 211  ? 99.080  124.325 121.887 1.00 20.83 ?  211  VAL B O    1 
ATOM   8968  C CB   . VAL B 1 211  ? 100.212 124.393 125.054 1.00 16.07 ?  211  VAL B CB   1 
ATOM   8969  C CG1  . VAL B 1 211  ? 101.312 125.185 125.738 1.00 13.13 ?  211  VAL B CG1  1 
ATOM   8970  C CG2  . VAL B 1 211  ? 99.270  123.832 126.110 1.00 15.53 ?  211  VAL B CG2  1 
ATOM   8971  N N    . ALA B 1 212  ? 97.478  123.991 123.431 1.00 20.65 ?  212  ALA B N    1 
ATOM   8972  C CA   . ALA B 1 212  ? 96.629  123.271 122.487 1.00 16.40 ?  212  ALA B CA   1 
ATOM   8973  C C    . ALA B 1 212  ? 96.133  124.189 121.376 1.00 16.94 ?  212  ALA B C    1 
ATOM   8974  O O    . ALA B 1 212  ? 96.113  123.796 120.204 1.00 19.98 ?  212  ALA B O    1 
ATOM   8975  C CB   . ALA B 1 212  ? 95.452  122.631 123.220 1.00 18.28 ?  212  ALA B CB   1 
ATOM   8976  N N    . VAL B 1 213  ? 95.741  125.417 121.725 1.00 16.44 ?  213  VAL B N    1 
ATOM   8977  C CA   . VAL B 1 213  ? 95.202  126.343 120.733 1.00 13.75 ?  213  VAL B CA   1 
ATOM   8978  C C    . VAL B 1 213  ? 96.271  126.727 119.716 1.00 16.49 ?  213  VAL B C    1 
ATOM   8979  O O    . VAL B 1 213  ? 96.027  126.708 118.505 1.00 19.96 ?  213  VAL B O    1 
ATOM   8980  C CB   . VAL B 1 213  ? 94.606  127.583 121.426 1.00 15.25 ?  213  VAL B CB   1 
ATOM   8981  C CG1  . VAL B 1 213  ? 94.481  128.743 120.448 1.00 17.72 ?  213  VAL B CG1  1 
ATOM   8982  C CG2  . VAL B 1 213  ? 93.255  127.248 122.023 1.00 17.80 ?  213  VAL B CG2  1 
ATOM   8983  N N    . VAL B 1 214  ? 97.474  127.066 120.187 1.00 18.17 ?  214  VAL B N    1 
ATOM   8984  C CA   . VAL B 1 214  ? 98.529  127.449 119.253 1.00 18.48 ?  214  VAL B CA   1 
ATOM   8985  C C    . VAL B 1 214  ? 98.991  126.245 118.433 1.00 16.09 ?  214  VAL B C    1 
ATOM   8986  O O    . VAL B 1 214  ? 99.288  126.381 117.237 1.00 17.80 ?  214  VAL B O    1 
ATOM   8987  C CB   . VAL B 1 214  ? 99.692  128.147 119.993 1.00 19.49 ?  214  VAL B CB   1 
ATOM   8988  C CG1  . VAL B 1 214  ? 100.425 127.202 120.941 1.00 18.50 ?  214  VAL B CG1  1 
ATOM   8989  C CG2  . VAL B 1 214  ? 100.660 128.776 119.000 1.00 18.42 ?  214  VAL B CG2  1 
ATOM   8990  N N    . ALA B 1 215  ? 99.019  125.048 119.034 1.00 19.01 ?  215  ALA B N    1 
ATOM   8991  C CA   . ALA B 1 215  ? 99.414  123.855 118.291 1.00 25.87 ?  215  ALA B CA   1 
ATOM   8992  C C    . ALA B 1 215  ? 98.412  123.523 117.191 1.00 22.42 ?  215  ALA B C    1 
ATOM   8993  O O    . ALA B 1 215  ? 98.805  123.153 116.078 1.00 18.70 ?  215  ALA B O    1 
ATOM   8994  C CB   . ALA B 1 215  ? 99.576  122.673 119.245 1.00 21.67 ?  215  ALA B CB   1 
ATOM   8995  N N    . LEU B 1 216  ? 97.115  123.652 117.477 1.00 21.62 ?  216  LEU B N    1 
ATOM   8996  C CA   . LEU B 1 216  ? 96.094  123.357 116.481 1.00 19.89 ?  216  LEU B CA   1 
ATOM   8997  C C    . LEU B 1 216  ? 95.830  124.520 115.534 1.00 19.63 ?  216  LEU B C    1 
ATOM   8998  O O    . LEU B 1 216  ? 95.136  124.331 114.529 1.00 22.33 ?  216  LEU B O    1 
ATOM   8999  C CB   . LEU B 1 216  ? 94.792  122.944 117.173 1.00 19.82 ?  216  LEU B CB   1 
ATOM   9000  C CG   . LEU B 1 216  ? 94.853  121.676 118.032 1.00 22.96 ?  216  LEU B CG   1 
ATOM   9001  C CD1  . LEU B 1 216  ? 93.456  121.187 118.376 1.00 21.59 ?  216  LEU B CD1  1 
ATOM   9002  C CD2  . LEU B 1 216  ? 95.648  120.578 117.338 1.00 21.45 ?  216  LEU B CD2  1 
ATOM   9003  N N    . LEU B 1 217  ? 96.353  125.710 115.826 1.00 16.32 ?  217  LEU B N    1 
ATOM   9004  C CA   . LEU B 1 217  ? 96.242  126.833 114.907 1.00 17.65 ?  217  LEU B CA   1 
ATOM   9005  C C    . LEU B 1 217  ? 97.455  126.983 114.002 1.00 19.74 ?  217  LEU B C    1 
ATOM   9006  O O    . LEU B 1 217  ? 97.351  127.634 112.956 1.00 20.95 ?  217  LEU B O    1 
ATOM   9007  C CB   . LEU B 1 217  ? 96.031  128.135 115.687 1.00 19.90 ?  217  LEU B CB   1 
ATOM   9008  C CG   . LEU B 1 217  ? 94.660  128.800 115.558 1.00 19.62 ?  217  LEU B CG   1 
ATOM   9009  C CD1  . LEU B 1 217  ? 93.577  127.898 116.121 1.00 17.53 ?  217  LEU B CD1  1 
ATOM   9010  C CD2  . LEU B 1 217  ? 94.650  130.152 116.254 1.00 18.90 ?  217  LEU B CD2  1 
ATOM   9011  N N    . LYS B 1 218  ? 98.601  126.411 114.382 1.00 18.50 ?  218  LYS B N    1 
ATOM   9012  C CA   . LYS B 1 218  ? 99.775  126.476 113.516 1.00 16.89 ?  218  LYS B CA   1 
ATOM   9013  C C    . LYS B 1 218  ? 99.583  125.640 112.254 1.00 21.33 ?  218  LYS B C    1 
ATOM   9014  O O    . LYS B 1 218  ? 99.826  126.117 111.139 1.00 18.15 ?  218  LYS B O    1 
ATOM   9015  C CB   . LYS B 1 218  ? 101.016 126.014 114.280 1.00 15.99 ?  218  LYS B CB   1 
ATOM   9016  C CG   . LYS B 1 218  ? 102.010 127.122 114.578 1.00 23.08 ?  218  LYS B CG   1 
ATOM   9017  C CD   . LYS B 1 218  ? 103.358 126.552 114.987 1.00 23.78 ?  218  LYS B CD   1 
ATOM   9018  C CE   . LYS B 1 218  ? 104.472 127.565 114.783 1.00 18.57 ?  218  LYS B CE   1 
ATOM   9019  N NZ   . LYS B 1 218  ? 105.808 126.912 114.712 1.00 14.86 ?  218  LYS B NZ   1 
ATOM   9020  N N    . ASP B 1 219  ? 99.145  124.388 112.409 1.00 26.01 ?  219  ASP B N    1 
ATOM   9021  C CA   . ASP B 1 219  ? 99.028  123.499 111.258 1.00 25.39 ?  219  ASP B CA   1 
ATOM   9022  C C    . ASP B 1 219  ? 97.792  123.795 110.416 1.00 24.63 ?  219  ASP B C    1 
ATOM   9023  O O    . ASP B 1 219  ? 97.821  123.600 109.196 1.00 26.06 ?  219  ASP B O    1 
ATOM   9024  C CB   . ASP B 1 219  ? 99.022  122.038 111.716 1.00 26.25 ?  219  ASP B CB   1 
ATOM   9025  C CG   . ASP B 1 219  ? 97.751  121.656 112.449 1.00 26.57 ?  219  ASP B CG   1 
ATOM   9026  O OD1  . ASP B 1 219  ? 97.187  122.515 113.159 1.00 26.35 ?  219  ASP B OD1  1 
ATOM   9027  O OD2  . ASP B 1 219  ? 97.315  120.494 112.313 1.00 27.27 ?  219  ASP B OD2  1 
ATOM   9028  N N    . LEU B 1 220  ? 96.706  124.262 111.036 1.00 18.64 ?  220  LEU B N    1 
ATOM   9029  C CA   . LEU B 1 220  ? 95.489  124.562 110.293 1.00 20.08 ?  220  LEU B CA   1 
ATOM   9030  C C    . LEU B 1 220  ? 95.618  125.818 109.442 1.00 20.29 ?  220  LEU B C    1 
ATOM   9031  O O    . LEU B 1 220  ? 94.794  126.025 108.544 1.00 17.51 ?  220  LEU B O    1 
ATOM   9032  C CB   . LEU B 1 220  ? 94.310  124.703 111.258 1.00 22.92 ?  220  LEU B CB   1 
ATOM   9033  C CG   . LEU B 1 220  ? 92.911  124.449 110.692 1.00 22.51 ?  220  LEU B CG   1 
ATOM   9034  C CD1  . LEU B 1 220  ? 92.593  122.962 110.689 1.00 18.30 ?  220  LEU B CD1  1 
ATOM   9035  C CD2  . LEU B 1 220  ? 91.867  125.222 111.478 1.00 23.79 ?  220  LEU B CD2  1 
ATOM   9036  N N    . GLY B 1 221  ? 96.628  126.644 109.691 1.00 18.80 ?  221  GLY B N    1 
ATOM   9037  C CA   . GLY B 1 221  ? 96.851  127.841 108.901 1.00 17.99 ?  221  GLY B CA   1 
ATOM   9038  C C    . GLY B 1 221  ? 95.788  128.907 109.049 1.00 19.41 ?  221  GLY B C    1 
ATOM   9039  O O    . GLY B 1 221  ? 95.433  129.561 108.059 1.00 17.67 ?  221  GLY B O    1 
ATOM   9040  N N    . ALA B 1 222  ? 95.260  129.094 110.261 1.00 21.97 ?  222  ALA B N    1 
ATOM   9041  C CA   . ALA B 1 222  ? 94.337  130.199 110.496 1.00 22.65 ?  222  ALA B CA   1 
ATOM   9042  C C    . ALA B 1 222  ? 95.050  131.537 110.355 1.00 25.24 ?  222  ALA B C    1 
ATOM   9043  O O    . ALA B 1 222  ? 94.605  132.412 109.603 1.00 25.24 ?  222  ALA B O    1 
ATOM   9044  C CB   . ALA B 1 222  ? 93.698  130.068 111.878 1.00 20.91 ?  222  ALA B CB   1 
ATOM   9045  N N    . SER B 1 223  ? 96.174  131.697 111.053 1.00 23.26 ?  223  SER B N    1 
ATOM   9046  C CA   . SER B 1 223  ? 97.048  132.857 110.948 1.00 20.53 ?  223  SER B CA   1 
ATOM   9047  C C    . SER B 1 223  ? 98.326  132.572 111.720 1.00 20.16 ?  223  SER B C    1 
ATOM   9048  O O    . SER B 1 223  ? 98.282  131.966 112.794 1.00 21.31 ?  223  SER B O    1 
ATOM   9049  C CB   . SER B 1 223  ? 96.385  134.128 111.501 1.00 20.54 ?  223  SER B CB   1 
ATOM   9050  O OG   . SER B 1 223  ? 97.160  135.276 111.203 1.00 26.18 ?  223  SER B OG   1 
ATOM   9051  N N    . LYS B 1 224  ? 99.456  133.008 111.170 1.00 21.25 ?  224  LYS B N    1 
ATOM   9052  C CA   . LYS B 1 224  ? 100.702 133.034 111.922 1.00 19.35 ?  224  LYS B CA   1 
ATOM   9053  C C    . LYS B 1 224  ? 100.854 134.307 112.740 1.00 19.91 ?  224  LYS B C    1 
ATOM   9054  O O    . LYS B 1 224  ? 101.778 134.398 113.555 1.00 26.03 ?  224  LYS B O    1 
ATOM   9055  C CB   . LYS B 1 224  ? 101.901 132.874 110.982 1.00 19.73 ?  224  LYS B CB   1 
ATOM   9056  C CG   . LYS B 1 224  ? 101.721 131.794 109.929 1.00 21.13 ?  224  LYS B CG   1 
ATOM   9057  C CD   . LYS B 1 224  ? 102.850 131.811 108.913 1.00 20.92 ?  224  LYS B CD   1 
ATOM   9058  C CE   . LYS B 1 224  ? 102.506 130.964 107.699 1.00 21.06 ?  224  LYS B CE   1 
ATOM   9059  N NZ   . LYS B 1 224  ? 101.287 131.461 107.002 1.00 21.89 ?  224  LYS B NZ   1 
ATOM   9060  N N    . GLN B 1 225  ? 99.972  135.283 112.539 1.00 20.67 ?  225  GLN B N    1 
ATOM   9061  C CA   . GLN B 1 225  ? 99.928  136.494 113.344 1.00 21.01 ?  225  GLN B CA   1 
ATOM   9062  C C    . GLN B 1 225  ? 98.882  136.429 114.448 1.00 23.94 ?  225  GLN B C    1 
ATOM   9063  O O    . GLN B 1 225  ? 98.679  137.425 115.148 1.00 27.82 ?  225  GLN B O    1 
ATOM   9064  C CB   . GLN B 1 225  ? 99.662  137.711 112.451 1.00 19.13 ?  225  GLN B CB   1 
ATOM   9065  C CG   . GLN B 1 225  ? 100.624 137.850 111.284 1.00 20.22 ?  225  GLN B CG   1 
ATOM   9066  C CD   . GLN B 1 225  ? 101.839 138.687 111.630 1.00 22.88 ?  225  GLN B CD   1 
ATOM   9067  O OE1  . GLN B 1 225  ? 101.944 139.221 112.734 1.00 24.76 ?  225  GLN B OE1  1 
ATOM   9068  N NE2  . GLN B 1 225  ? 102.766 138.805 110.686 1.00 21.20 ?  225  GLN B NE2  1 
ATOM   9069  N N    . LEU B 1 226  ? 98.209  135.291 114.615 1.00 14.86 ?  226  LEU B N    1 
ATOM   9070  C CA   . LEU B 1 226  ? 97.246  135.108 115.694 1.00 16.20 ?  226  LEU B CA   1 
ATOM   9071  C C    . LEU B 1 226  ? 97.739  134.189 116.800 1.00 18.61 ?  226  LEU B C    1 
ATOM   9072  O O    . LEU B 1 226  ? 97.374  134.394 117.959 1.00 20.08 ?  226  LEU B O    1 
ATOM   9073  C CB   . LEU B 1 226  ? 95.923  134.558 115.146 1.00 17.59 ?  226  LEU B CB   1 
ATOM   9074  C CG   . LEU B 1 226  ? 94.691  134.773 116.028 1.00 18.79 ?  226  LEU B CG   1 
ATOM   9075  C CD1  . LEU B 1 226  ? 94.195  136.207 115.926 1.00 16.41 ?  226  LEU B CD1  1 
ATOM   9076  C CD2  . LEU B 1 226  ? 93.586  133.792 115.665 1.00 18.18 ?  226  LEU B CD2  1 
ATOM   9077  N N    . GLY B 1 227  ? 98.549  133.180 116.472 1.00 18.14 ?  227  GLY B N    1 
ATOM   9078  C CA   . GLY B 1 227  ? 99.121  132.340 117.511 1.00 16.88 ?  227  GLY B CA   1 
ATOM   9079  C C    . GLY B 1 227  ? 100.107 133.089 118.386 1.00 17.10 ?  227  GLY B C    1 
ATOM   9080  O O    . GLY B 1 227  ? 100.165 132.873 119.600 1.00 17.48 ?  227  GLY B O    1 
ATOM   9081  N N    . THR B 1 228  ? 100.894 133.983 117.783 1.00 16.62 ?  228  THR B N    1 
ATOM   9082  C CA   . THR B 1 228  ? 101.836 134.784 118.557 1.00 18.61 ?  228  THR B CA   1 
ATOM   9083  C C    . THR B 1 228  ? 101.111 135.743 119.494 1.00 16.69 ?  228  THR B C    1 
ATOM   9084  O O    . THR B 1 228  ? 101.550 135.959 120.631 1.00 19.75 ?  228  THR B O    1 
ATOM   9085  C CB   . THR B 1 228  ? 102.762 135.556 117.619 1.00 17.92 ?  228  THR B CB   1 
ATOM   9086  O OG1  . THR B 1 228  ? 103.184 134.700 116.549 1.00 17.91 ?  228  THR B OG1  1 
ATOM   9087  C CG2  . THR B 1 228  ? 103.981 136.056 118.374 1.00 16.47 ?  228  THR B CG2  1 
ATOM   9088  N N    . ILE B 1 229  ? 99.998  136.318 119.035 1.00 14.95 ?  229  ILE B N    1 
ATOM   9089  C CA   . ILE B 1 229  ? 99.245  137.264 119.854 1.00 15.89 ?  229  ILE B CA   1 
ATOM   9090  C C    . ILE B 1 229  ? 98.675  136.571 121.086 1.00 17.08 ?  229  ILE B C    1 
ATOM   9091  O O    . ILE B 1 229  ? 98.818  137.062 122.213 1.00 25.26 ?  229  ILE B O    1 
ATOM   9092  C CB   . ILE B 1 229  ? 98.139  137.932 119.016 1.00 19.13 ?  229  ILE B CB   1 
ATOM   9093  C CG1  . ILE B 1 229  ? 98.744  138.929 118.025 1.00 19.40 ?  229  ILE B CG1  1 
ATOM   9094  C CG2  . ILE B 1 229  ? 97.121  138.620 119.913 1.00 17.76 ?  229  ILE B CG2  1 
ATOM   9095  C CD1  . ILE B 1 229  ? 99.661  139.950 118.660 1.00 21.78 ?  229  ILE B CD1  1 
ATOM   9096  N N    . ILE B 1 230  ? 98.043  135.410 120.897 1.00 12.54 ?  230  ILE B N    1 
ATOM   9097  C CA   . ILE B 1 230  ? 97.469  134.698 122.035 1.00 17.74 ?  230  ILE B CA   1 
ATOM   9098  C C    . ILE B 1 230  ? 98.569  134.138 122.935 1.00 17.18 ?  230  ILE B C    1 
ATOM   9099  O O    . ILE B 1 230  ? 98.406  134.088 124.161 1.00 18.82 ?  230  ILE B O    1 
ATOM   9100  C CB   . ILE B 1 230  ? 96.483  133.611 121.553 1.00 18.49 ?  230  ILE B CB   1 
ATOM   9101  C CG1  . ILE B 1 230  ? 95.734  132.993 122.736 1.00 16.59 ?  230  ILE B CG1  1 
ATOM   9102  C CG2  . ILE B 1 230  ? 97.176  132.539 120.727 1.00 18.49 ?  230  ILE B CG2  1 
ATOM   9103  C CD1  . ILE B 1 230  ? 94.740  131.930 122.335 1.00 19.62 ?  230  ILE B CD1  1 
ATOM   9104  N N    . GLU B 1 231  ? 99.715  133.754 122.359 1.00 12.36 ?  231  GLU B N    1 
ATOM   9105  C CA   . GLU B 1 231  ? 100.842 133.289 123.164 1.00 12.95 ?  231  GLU B CA   1 
ATOM   9106  C C    . GLU B 1 231  ? 101.354 134.392 124.088 1.00 19.44 ?  231  GLU B C    1 
ATOM   9107  O O    . GLU B 1 231  ? 101.521 134.182 125.298 1.00 26.22 ?  231  GLU B O    1 
ATOM   9108  C CB   . GLU B 1 231  ? 101.958 132.792 122.244 1.00 14.29 ?  231  GLU B CB   1 
ATOM   9109  C CG   . GLU B 1 231  ? 102.543 131.441 122.618 1.00 18.64 ?  231  GLU B CG   1 
ATOM   9110  C CD   . GLU B 1 231  ? 103.678 131.025 121.699 1.00 18.74 ?  231  GLU B CD   1 
ATOM   9111  O OE1  . GLU B 1 231  ? 104.064 131.831 120.826 1.00 15.56 ?  231  GLU B OE1  1 
ATOM   9112  O OE2  . GLU B 1 231  ? 104.184 129.893 121.848 1.00 17.37 ?  231  GLU B OE2  1 
ATOM   9113  N N    . GLY B 1 232  ? 101.594 135.583 123.533 1.00 15.10 ?  232  GLY B N    1 
ATOM   9114  C CA   . GLY B 1 232  ? 102.051 136.695 124.351 1.00 9.42  ?  232  GLY B CA   1 
ATOM   9115  C C    . GLY B 1 232  ? 101.016 137.148 125.364 1.00 9.52  ?  232  GLY B C    1 
ATOM   9116  O O    . GLY B 1 232  ? 101.360 137.518 126.494 1.00 15.51 ?  232  GLY B O    1 
ATOM   9117  N N    . GLU B 1 233  ? 99.736  137.123 124.977 1.00 6.25  ?  233  GLU B N    1 
ATOM   9118  C CA   . GLU B 1 233  ? 98.674  137.484 125.909 1.00 10.36 ?  233  GLU B CA   1 
ATOM   9119  C C    . GLU B 1 233  ? 98.628  136.521 127.087 1.00 16.74 ?  233  GLU B C    1 
ATOM   9120  O O    . GLU B 1 233  ? 98.480  136.947 128.237 1.00 27.09 ?  233  GLU B O    1 
ATOM   9121  C CB   . GLU B 1 233  ? 97.327  137.516 125.186 1.00 16.78 ?  233  GLU B CB   1 
ATOM   9122  C CG   . GLU B 1 233  ? 96.124  137.618 126.114 1.00 20.73 ?  233  GLU B CG   1 
ATOM   9123  C CD   . GLU B 1 233  ? 94.807  137.413 125.391 1.00 24.92 ?  233  GLU B CD   1 
ATOM   9124  O OE1  . GLU B 1 233  ? 94.830  137.176 124.166 1.00 25.17 ?  233  GLU B OE1  1 
ATOM   9125  O OE2  . GLU B 1 233  ? 93.749  137.491 126.050 1.00 24.98 ?  233  GLU B OE2  1 
ATOM   9126  N N    . SER B 1 234  ? 98.787  135.221 126.826 1.00 11.40 ?  234  SER B N    1 
ATOM   9127  C CA   . SER B 1 234  ? 98.793  134.246 127.912 1.00 10.25 ?  234  SER B CA   1 
ATOM   9128  C C    . SER B 1 234  ? 100.032 134.388 128.788 1.00 9.96  ?  234  SER B C    1 
ATOM   9129  O O    . SER B 1 234  ? 99.965  134.171 130.004 1.00 18.01 ?  234  SER B O    1 
ATOM   9130  C CB   . SER B 1 234  ? 98.703  132.833 127.346 1.00 14.04 ?  234  SER B CB   1 
ATOM   9131  O OG   . SER B 1 234  ? 99.988  132.242 127.288 1.00 14.90 ?  234  SER B OG   1 
ATOM   9132  N N    . LEU B 1 235  ? 101.174 134.742 128.191 1.00 7.20  ?  235  LEU B N    1 
ATOM   9133  C CA   . LEU B 1 235  ? 102.385 134.964 128.981 1.00 6.26  ?  235  LEU B CA   1 
ATOM   9134  C C    . LEU B 1 235  ? 102.208 136.135 129.947 1.00 6.17  ?  235  LEU B C    1 
ATOM   9135  O O    . LEU B 1 235  ? 102.514 136.028 131.146 1.00 14.28 ?  235  LEU B O    1 
ATOM   9136  C CB   . LEU B 1 235  ? 103.571 135.203 128.045 1.00 4.49  ?  235  LEU B CB   1 
ATOM   9137  C CG   . LEU B 1 235  ? 104.744 136.049 128.538 1.00 5.14  ?  235  LEU B CG   1 
ATOM   9138  C CD1  . LEU B 1 235  ? 105.602 135.267 129.520 1.00 6.43  ?  235  LEU B CD1  1 
ATOM   9139  C CD2  . LEU B 1 235  ? 105.573 136.545 127.364 1.00 5.17  ?  235  LEU B CD2  1 
ATOM   9140  N N    . LEU B 1 236  ? 101.692 137.259 129.440 1.00 1.54  ?  236  LEU B N    1 
ATOM   9141  C CA   . LEU B 1 236  ? 101.435 138.410 130.302 1.00 5.44  ?  236  LEU B CA   1 
ATOM   9142  C C    . LEU B 1 236  ? 100.360 138.100 131.335 1.00 5.33  ?  236  LEU B C    1 
ATOM   9143  O O    . LEU B 1 236  ? 100.430 138.583 132.475 1.00 13.74 ?  236  LEU B O    1 
ATOM   9144  C CB   . LEU B 1 236  ? 101.033 139.614 129.451 1.00 11.31 ?  236  LEU B CB   1 
ATOM   9145  C CG   . LEU B 1 236  ? 102.103 140.092 128.468 1.00 13.56 ?  236  LEU B CG   1 
ATOM   9146  C CD1  . LEU B 1 236  ? 101.515 141.061 127.462 1.00 12.92 ?  236  LEU B CD1  1 
ATOM   9147  C CD2  . LEU B 1 236  ? 103.267 140.728 129.209 1.00 9.47  ?  236  LEU B CD2  1 
ATOM   9148  N N    . ASN B 1 237  ? 99.372  137.288 130.952 1.00 3.08  ?  237  ASN B N    1 
ATOM   9149  C CA   . ASN B 1 237  ? 98.350  136.813 131.875 1.00 1.47  ?  237  ASN B CA   1 
ATOM   9150  C C    . ASN B 1 237  ? 98.961  136.050 133.044 1.00 6.49  ?  237  ASN B C    1 
ATOM   9151  O O    . ASN B 1 237  ? 98.626  136.304 134.207 1.00 12.11 ?  237  ASN B O    1 
ATOM   9152  C CB   . ASN B 1 237  ? 97.363  135.941 131.096 1.00 8.89  ?  237  ASN B CB   1 
ATOM   9153  C CG   . ASN B 1 237  ? 96.130  135.600 131.883 1.00 12.76 ?  237  ASN B CG   1 
ATOM   9154  O OD1  . ASN B 1 237  ? 96.196  134.834 132.838 1.00 18.98 ?  237  ASN B OD1  1 
ATOM   9155  N ND2  . ASN B 1 237  ? 94.995  136.168 131.495 1.00 12.08 ?  237  ASN B ND2  1 
ATOM   9156  N N    . ASP B 1 238  ? 99.872  135.119 132.753 1.00 9.77  ?  238  ASP B N    1 
ATOM   9157  C CA   . ASP B 1 238  ? 100.526 134.361 133.816 1.00 5.07  ?  238  ASP B CA   1 
ATOM   9158  C C    . ASP B 1 238  ? 101.340 135.273 134.726 1.00 9.92  ?  238  ASP B C    1 
ATOM   9159  O O    . ASP B 1 238  ? 101.299 135.133 135.959 1.00 16.13 ?  238  ASP B O    1 
ATOM   9160  C CB   . ASP B 1 238  ? 101.415 133.275 133.212 1.00 11.18 ?  238  ASP B CB   1 
ATOM   9161  C CG   . ASP B 1 238  ? 100.622 132.089 132.696 1.00 19.05 ?  238  ASP B CG   1 
ATOM   9162  O OD1  . ASP B 1 238  ? 99.483  131.881 133.166 1.00 22.61 ?  238  ASP B OD1  1 
ATOM   9163  O OD2  . ASP B 1 238  ? 101.136 131.365 131.818 1.00 11.75 ?  238  ASP B OD2  1 
ATOM   9164  N N    . GLY B 1 239  ? 102.072 136.224 134.137 1.00 10.67 ?  239  GLY B N    1 
ATOM   9165  C CA   . GLY B 1 239  ? 102.875 137.133 134.947 1.00 3.35  ?  239  GLY B CA   1 
ATOM   9166  C C    . GLY B 1 239  ? 102.045 137.975 135.903 1.00 2.35  ?  239  GLY B C    1 
ATOM   9167  O O    . GLY B 1 239  ? 102.343 138.062 137.102 1.00 12.80 ?  239  GLY B O    1 
ATOM   9168  N N    . CYS B 1 240  ? 100.972 138.589 135.393 1.00 1.38  ?  240  CYS B N    1 
ATOM   9169  C CA   . CYS B 1 240  ? 100.160 139.429 136.268 1.00 6.87  ?  240  CYS B CA   1 
ATOM   9170  C C    . CYS B 1 240  ? 99.364  138.597 137.267 1.00 6.84  ?  240  CYS B C    1 
ATOM   9171  O O    . CYS B 1 240  ? 99.087  139.070 138.379 1.00 14.73 ?  240  CYS B O    1 
ATOM   9172  C CB   . CYS B 1 240  ? 99.231  140.326 135.452 1.00 11.35 ?  240  CYS B CB   1 
ATOM   9173  S SG   . CYS B 1 240  ? 98.085  139.478 134.363 1.00 24.82 ?  240  CYS B SG   1 
ATOM   9174  N N    . ALA B 1 241  ? 99.012  137.356 136.909 1.00 5.06  ?  241  ALA B N    1 
ATOM   9175  C CA   . ALA B 1 241  ? 98.381  136.464 137.875 1.00 1.63  ?  241  ALA B CA   1 
ATOM   9176  C C    . ALA B 1 241  ? 99.311  136.182 139.046 1.00 1.90  ?  241  ALA B C    1 
ATOM   9177  O O    . ALA B 1 241  ? 98.884  136.213 140.206 1.00 4.98  ?  241  ALA B O    1 
ATOM   9178  C CB   . ALA B 1 241  ? 97.970  135.159 137.197 1.00 6.88  ?  241  ALA B CB   1 
ATOM   9179  N N    . ILE B 1 242  ? 100.592 135.933 138.758 1.00 4.46  ?  242  ILE B N    1 
ATOM   9180  C CA   . ILE B 1 242  ? 101.568 135.717 139.826 1.00 2.43  ?  242  ILE B CA   1 
ATOM   9181  C C    . ILE B 1 242  ? 101.703 136.965 140.694 1.00 3.20  ?  242  ILE B C    1 
ATOM   9182  O O    . ILE B 1 242  ? 101.764 136.877 141.931 1.00 4.98  ?  242  ILE B O    1 
ATOM   9183  C CB   . ILE B 1 242  ? 102.922 135.286 139.231 1.00 0.00  ?  242  ILE B CB   1 
ATOM   9184  C CG1  . ILE B 1 242  ? 102.806 133.901 138.594 1.00 1.06  ?  242  ILE B CG1  1 
ATOM   9185  C CG2  . ILE B 1 242  ? 104.014 135.295 140.287 1.00 3.33  ?  242  ILE B CG2  1 
ATOM   9186  C CD1  . ILE B 1 242  ? 104.035 133.482 137.833 1.00 3.56  ?  242  ILE B CD1  1 
ATOM   9187  N N    . VAL B 1 243  ? 101.736 138.144 140.063 1.00 5.76  ?  243  VAL B N    1 
ATOM   9188  C CA   . VAL B 1 243  ? 101.924 139.388 140.815 1.00 2.88  ?  243  VAL B CA   1 
ATOM   9189  C C    . VAL B 1 243  ? 100.765 139.621 141.786 1.00 5.08  ?  243  VAL B C    1 
ATOM   9190  O O    . VAL B 1 243  ? 100.972 139.872 142.984 1.00 10.29 ?  243  VAL B O    1 
ATOM   9191  C CB   . VAL B 1 243  ? 102.097 140.575 139.851 1.00 0.00  ?  243  VAL B CB   1 
ATOM   9192  C CG1  . VAL B 1 243  ? 101.959 141.890 140.597 1.00 3.36  ?  243  VAL B CG1  1 
ATOM   9193  C CG2  . VAL B 1 243  ? 103.440 140.495 139.149 1.00 3.54  ?  243  VAL B CG2  1 
ATOM   9194  N N    . ILE B 1 244  ? 99.526  139.530 141.290 1.00 5.76  ?  244  ILE B N    1 
ATOM   9195  C CA   . ILE B 1 244  ? 98.378  139.758 142.168 1.00 1.43  ?  244  ILE B CA   1 
ATOM   9196  C C    . ILE B 1 244  ? 98.228  138.644 143.202 1.00 2.72  ?  244  ILE B C    1 
ATOM   9197  O O    . ILE B 1 244  ? 97.782  138.899 144.333 1.00 4.67  ?  244  ILE B O    1 
ATOM   9198  C CB   . ILE B 1 244  ? 97.092  139.969 141.344 1.00 1.97  ?  244  ILE B CB   1 
ATOM   9199  C CG1  . ILE B 1 244  ? 97.341  140.980 140.226 1.00 5.81  ?  244  ILE B CG1  1 
ATOM   9200  C CG2  . ILE B 1 244  ? 95.946  140.434 142.218 1.00 6.14  ?  244  ILE B CG2  1 
ATOM   9201  C CD1  . ILE B 1 244  ? 96.199  141.108 139.255 1.00 6.81  ?  244  ILE B CD1  1 
ATOM   9202  N N    . PHE B 1 245  ? 98.610  137.407 142.859 1.00 7.05  ?  245  PHE B N    1 
ATOM   9203  C CA   . PHE B 1 245  ? 98.605  136.344 143.858 1.00 0.57  ?  245  PHE B CA   1 
ATOM   9204  C C    . PHE B 1 245  ? 99.545  136.666 145.008 1.00 3.01  ?  245  PHE B C    1 
ATOM   9205  O O    . PHE B 1 245  ? 99.201  136.445 146.171 1.00 5.37  ?  245  PHE B O    1 
ATOM   9206  C CB   . PHE B 1 245  ? 98.991  135.004 143.233 1.00 3.32  ?  245  PHE B CB   1 
ATOM   9207  C CG   . PHE B 1 245  ? 99.244  133.918 144.249 1.00 4.18  ?  245  PHE B CG   1 
ATOM   9208  C CD1  . PHE B 1 245  ? 98.190  133.225 144.812 1.00 3.76  ?  245  PHE B CD1  1 
ATOM   9209  C CD2  . PHE B 1 245  ? 100.536 133.596 144.643 1.00 0.44  ?  245  PHE B CD2  1 
ATOM   9210  C CE1  . PHE B 1 245  ? 98.415  132.238 145.745 1.00 0.63  ?  245  PHE B CE1  1 
ATOM   9211  C CE2  . PHE B 1 245  ? 100.765 132.607 145.578 1.00 0.00  ?  245  PHE B CE2  1 
ATOM   9212  C CZ   . PHE B 1 245  ? 99.703  131.927 146.128 1.00 0.00  ?  245  PHE B CZ   1 
ATOM   9213  N N    . ASN B 1 246  ? 100.743 137.171 144.703 1.00 6.51  ?  246  ASN B N    1 
ATOM   9214  C CA   . ASN B 1 246  ? 101.667 137.549 145.770 1.00 3.82  ?  246  ASN B CA   1 
ATOM   9215  C C    . ASN B 1 246  ? 101.109 138.692 146.607 1.00 7.31  ?  246  ASN B C    1 
ATOM   9216  O O    . ASN B 1 246  ? 101.194 138.666 147.846 1.00 9.60  ?  246  ASN B O    1 
ATOM   9217  C CB   . ASN B 1 246  ? 103.022 137.929 145.183 1.00 2.63  ?  246  ASN B CB   1 
ATOM   9218  C CG   . ASN B 1 246  ? 104.006 136.790 145.233 1.00 14.68 ?  246  ASN B CG   1 
ATOM   9219  O OD1  . ASN B 1 246  ? 104.856 136.728 146.121 1.00 19.56 ?  246  ASN B OD1  1 
ATOM   9220  N ND2  . ASN B 1 246  ? 103.887 135.865 144.288 1.00 10.92 ?  246  ASN B ND2  1 
ATOM   9221  N N    . VAL B 1 247  ? 100.517 139.691 145.943 1.00 10.72 ?  247  VAL B N    1 
ATOM   9222  C CA   . VAL B 1 247  ? 99.977  140.854 146.647 1.00 5.76  ?  247  VAL B CA   1 
ATOM   9223  C C    . VAL B 1 247  ? 98.901  140.433 147.641 1.00 4.41  ?  247  VAL B C    1 
ATOM   9224  O O    . VAL B 1 247  ? 98.872  140.906 148.784 1.00 2.36  ?  247  VAL B O    1 
ATOM   9225  C CB   . VAL B 1 247  ? 99.449  141.890 145.636 1.00 6.51  ?  247  VAL B CB   1 
ATOM   9226  C CG1  . VAL B 1 247  ? 98.482  142.862 146.299 1.00 3.71  ?  247  VAL B CG1  1 
ATOM   9227  C CG2  . VAL B 1 247  ? 100.606 142.643 145.003 1.00 9.10  ?  247  VAL B CG2  1 
ATOM   9228  N N    . PHE B 1 248  ? 98.017  139.518 147.238 1.00 9.23  ?  248  PHE B N    1 
ATOM   9229  C CA   . PHE B 1 248  ? 96.960  139.096 148.153 1.00 1.28  ?  248  PHE B CA   1 
ATOM   9230  C C    . PHE B 1 248  ? 97.417  138.021 149.138 1.00 7.25  ?  248  PHE B C    1 
ATOM   9231  O O    . PHE B 1 248  ? 96.847  137.911 150.230 1.00 13.85 ?  248  PHE B O    1 
ATOM   9232  C CB   . PHE B 1 248  ? 95.743  138.622 147.361 1.00 0.89  ?  248  PHE B CB   1 
ATOM   9233  C CG   . PHE B 1 248  ? 94.855  139.741 146.904 1.00 0.63  ?  248  PHE B CG   1 
ATOM   9234  C CD1  . PHE B 1 248  ? 93.881  140.253 147.742 1.00 5.98  ?  248  PHE B CD1  1 
ATOM   9235  C CD2  . PHE B 1 248  ? 95.008  140.297 145.648 1.00 2.31  ?  248  PHE B CD2  1 
ATOM   9236  C CE1  . PHE B 1 248  ? 93.064  141.289 147.330 1.00 9.91  ?  248  PHE B CE1  1 
ATOM   9237  C CE2  . PHE B 1 248  ? 94.194  141.334 145.231 1.00 7.51  ?  248  PHE B CE2  1 
ATOM   9238  C CZ   . PHE B 1 248  ? 93.222  141.829 146.073 1.00 9.95  ?  248  PHE B CZ   1 
ATOM   9239  N N    . MET B 1 249  ? 98.438  137.232 148.789 1.00 11.20 ?  249  MET B N    1 
ATOM   9240  C CA   . MET B 1 249  ? 98.959  136.233 149.717 1.00 6.69  ?  249  MET B CA   1 
ATOM   9241  C C    . MET B 1 249  ? 99.635  136.897 150.908 1.00 7.45  ?  249  MET B C    1 
ATOM   9242  O O    . MET B 1 249  ? 99.521  136.411 152.043 1.00 6.60  ?  249  MET B O    1 
ATOM   9243  C CB   . MET B 1 249  ? 99.926  135.299 148.986 1.00 5.85  ?  249  MET B CB   1 
ATOM   9244  C CG   . MET B 1 249  ? 100.950 134.601 149.871 1.00 11.03 ?  249  MET B CG   1 
ATOM   9245  S SD   . MET B 1 249  ? 102.257 133.793 148.927 1.00 11.95 ?  249  MET B SD   1 
ATOM   9246  C CE   . MET B 1 249  ? 103.624 134.913 149.205 1.00 4.52  ?  249  MET B CE   1 
ATOM   9247  N N    . LYS B 1 250  ? 100.332 138.015 150.670 1.00 12.06 ?  250  LYS B N    1 
ATOM   9248  C CA   . LYS B 1 250  ? 100.898 138.777 151.782 1.00 10.89 ?  250  LYS B CA   1 
ATOM   9249  C C    . LYS B 1 250  ? 99.813  139.247 152.745 1.00 10.82 ?  250  LYS B C    1 
ATOM   9250  O O    . LYS B 1 250  ? 100.003 139.217 153.966 1.00 15.51 ?  250  LYS B O    1 
ATOM   9251  C CB   . LYS B 1 250  ? 101.693 139.975 151.262 1.00 13.03 ?  250  LYS B CB   1 
ATOM   9252  C CG   . LYS B 1 250  ? 102.882 139.625 150.388 1.00 12.73 ?  250  LYS B CG   1 
ATOM   9253  C CD   . LYS B 1 250  ? 103.745 138.550 151.019 1.00 14.36 ?  250  LYS B CD   1 
ATOM   9254  C CE   . LYS B 1 250  ? 105.019 138.338 150.220 1.00 16.09 ?  250  LYS B CE   1 
ATOM   9255  N NZ   . LYS B 1 250  ? 105.534 139.615 149.652 1.00 15.99 ?  250  LYS B NZ   1 
ATOM   9256  N N    . MET B 1 251  ? 98.666  139.677 152.215 1.00 12.50 ?  251  MET B N    1 
ATOM   9257  C CA   . MET B 1 251  ? 97.587  140.152 153.075 1.00 9.00  ?  251  MET B CA   1 
ATOM   9258  C C    . MET B 1 251  ? 96.890  139.009 153.802 1.00 11.86 ?  251  MET B C    1 
ATOM   9259  O O    . MET B 1 251  ? 96.460  139.180 154.948 1.00 20.47 ?  251  MET B O    1 
ATOM   9260  C CB   . MET B 1 251  ? 96.575  140.947 152.254 1.00 8.50  ?  251  MET B CB   1 
ATOM   9261  C CG   . MET B 1 251  ? 97.186  142.094 151.468 1.00 13.60 ?  251  MET B CG   1 
ATOM   9262  S SD   . MET B 1 251  ? 96.068  142.824 150.254 1.00 25.50 ?  251  MET B SD   1 
ATOM   9263  C CE   . MET B 1 251  ? 94.469  142.433 150.960 1.00 14.19 ?  251  MET B CE   1 
ATOM   9264  N N    . VAL B 1 252  ? 96.762  137.846 153.161 1.00 10.29 ?  252  VAL B N    1 
ATOM   9265  C CA   . VAL B 1 252  ? 96.050  136.732 153.786 1.00 10.29 ?  252  VAL B CA   1 
ATOM   9266  C C    . VAL B 1 252  ? 96.905  136.085 154.869 1.00 12.72 ?  252  VAL B C    1 
ATOM   9267  O O    . VAL B 1 252  ? 96.489  135.971 156.027 1.00 12.32 ?  252  VAL B O    1 
ATOM   9268  C CB   . VAL B 1 252  ? 95.623  135.695 152.733 1.00 9.24  ?  252  VAL B CB   1 
ATOM   9269  C CG1  . VAL B 1 252  ? 95.116  134.435 153.415 1.00 12.40 ?  252  VAL B CG1  1 
ATOM   9270  C CG2  . VAL B 1 252  ? 94.553  136.259 151.836 1.00 8.50  ?  252  VAL B CG2  1 
ATOM   9271  N N    . PHE B 1 253  ? 98.112  135.650 154.508 1.00 14.43 ?  253  PHE B N    1 
ATOM   9272  C CA   . PHE B 1 253  ? 98.876  134.773 155.385 1.00 8.05  ?  253  PHE B CA   1 
ATOM   9273  C C    . PHE B 1 253  ? 99.858  135.506 156.286 1.00 9.31  ?  253  PHE B C    1 
ATOM   9274  O O    . PHE B 1 253  ? 100.293 134.935 157.292 1.00 11.67 ?  253  PHE B O    1 
ATOM   9275  C CB   . PHE B 1 253  ? 99.625  133.729 154.552 1.00 8.72  ?  253  PHE B CB   1 
ATOM   9276  C CG   . PHE B 1 253  ? 98.734  132.667 153.977 1.00 9.14  ?  253  PHE B CG   1 
ATOM   9277  C CD1  . PHE B 1 253  ? 97.917  131.911 154.801 1.00 5.86  ?  253  PHE B CD1  1 
ATOM   9278  C CD2  . PHE B 1 253  ? 98.704  132.432 152.614 1.00 10.38 ?  253  PHE B CD2  1 
ATOM   9279  C CE1  . PHE B 1 253  ? 97.093  130.936 154.277 1.00 4.67  ?  253  PHE B CE1  1 
ATOM   9280  C CE2  . PHE B 1 253  ? 97.881  131.458 152.084 1.00 11.85 ?  253  PHE B CE2  1 
ATOM   9281  C CZ   . PHE B 1 253  ? 97.075  130.709 152.918 1.00 7.71  ?  253  PHE B CZ   1 
ATOM   9282  N N    . PHE B 1 254  ? 100.210 136.749 155.968 1.00 9.69  ?  254  PHE B N    1 
ATOM   9283  C CA   . PHE B 1 254  ? 101.137 137.540 156.778 1.00 8.65  ?  254  PHE B CA   1 
ATOM   9284  C C    . PHE B 1 254  ? 100.496 138.884 157.099 1.00 12.59 ?  254  PHE B C    1 
ATOM   9285  O O    . PHE B 1 254  ? 100.907 139.926 156.575 1.00 17.17 ?  254  PHE B O    1 
ATOM   9286  C CB   . PHE B 1 254  ? 102.474 137.723 156.058 1.00 7.68  ?  254  PHE B CB   1 
ATOM   9287  C CG   . PHE B 1 254  ? 103.054 136.446 155.519 1.00 8.93  ?  254  PHE B CG   1 
ATOM   9288  C CD1  . PHE B 1 254  ? 103.524 135.465 156.376 1.00 10.07 ?  254  PHE B CD1  1 
ATOM   9289  C CD2  . PHE B 1 254  ? 103.130 136.227 154.154 1.00 10.22 ?  254  PHE B CD2  1 
ATOM   9290  C CE1  . PHE B 1 254  ? 104.059 134.289 155.880 1.00 9.73  ?  254  PHE B CE1  1 
ATOM   9291  C CE2  . PHE B 1 254  ? 103.664 135.055 153.653 1.00 9.31  ?  254  PHE B CE2  1 
ATOM   9292  C CZ   . PHE B 1 254  ? 104.128 134.085 154.517 1.00 8.81  ?  254  PHE B CZ   1 
ATOM   9293  N N    . PRO B 1 255  ? 99.495  138.900 157.981 1.00 16.23 ?  255  PRO B N    1 
ATOM   9294  C CA   . PRO B 1 255  ? 98.759  140.137 158.258 1.00 17.25 ?  255  PRO B CA   1 
ATOM   9295  C C    . PRO B 1 255  ? 99.443  141.079 159.236 1.00 19.15 ?  255  PRO B C    1 
ATOM   9296  O O    . PRO B 1 255  ? 98.825  142.065 159.647 1.00 19.37 ?  255  PRO B O    1 
ATOM   9297  C CB   . PRO B 1 255  ? 97.441  139.610 158.844 1.00 14.68 ?  255  PRO B CB   1 
ATOM   9298  C CG   . PRO B 1 255  ? 97.828  138.342 159.539 1.00 16.12 ?  255  PRO B CG   1 
ATOM   9299  C CD   . PRO B 1 255  ? 99.072  137.801 158.867 1.00 15.02 ?  255  PRO B CD   1 
ATOM   9300  N N    . GLN B 1 256  ? 100.692 140.806 159.621 1.00 24.22 ?  256  GLN B N    1 
ATOM   9301  C CA   . GLN B 1 256  ? 101.411 141.697 160.522 1.00 22.50 ?  256  GLN B CA   1 
ATOM   9302  C C    . GLN B 1 256  ? 101.844 142.987 159.838 1.00 22.22 ?  256  GLN B C    1 
ATOM   9303  O O    . GLN B 1 256  ? 102.123 143.974 160.525 1.00 23.60 ?  256  GLN B O    1 
ATOM   9304  C CB   . GLN B 1 256  ? 102.631 140.978 161.101 1.00 20.04 ?  256  GLN B CB   1 
ATOM   9305  C CG   . GLN B 1 256  ? 103.035 141.444 162.490 1.00 20.97 ?  256  GLN B CG   1 
ATOM   9306  C CD   . GLN B 1 256  ? 104.303 140.773 162.980 1.00 22.46 ?  256  GLN B CD   1 
ATOM   9307  O OE1  . GLN B 1 256  ? 105.003 140.108 162.216 1.00 23.66 ?  256  GLN B OE1  1 
ATOM   9308  N NE2  . GLN B 1 256  ? 104.606 140.942 164.262 1.00 22.60 ?  256  GLN B NE2  1 
ATOM   9309  N N    . LEU B 1 257  ? 101.905 143.000 158.509 1.00 21.50 ?  257  LEU B N    1 
ATOM   9310  C CA   . LEU B 1 257  ? 102.325 144.190 157.784 1.00 23.88 ?  257  LEU B CA   1 
ATOM   9311  C C    . LEU B 1 257  ? 101.230 145.252 157.808 1.00 23.78 ?  257  LEU B C    1 
ATOM   9312  O O    . LEU B 1 257  ? 100.034 144.948 157.773 1.00 24.42 ?  257  LEU B O    1 
ATOM   9313  C CB   . LEU B 1 257  ? 102.687 143.843 156.338 1.00 23.93 ?  257  LEU B CB   1 
ATOM   9314  C CG   . LEU B 1 257  ? 104.097 143.321 156.026 1.00 22.39 ?  257  LEU B CG   1 
ATOM   9315  C CD1  . LEU B 1 257  ? 105.150 144.351 156.419 1.00 23.30 ?  257  LEU B CD1  1 
ATOM   9316  C CD2  . LEU B 1 257  ? 104.392 141.965 156.665 1.00 17.19 ?  257  LEU B CD2  1 
ATOM   9317  N N    . THR B 1 258  ? 101.653 146.513 157.869 1.00 24.21 ?  258  THR B N    1 
ATOM   9318  C CA   . THR B 1 258  ? 100.756 147.659 157.991 1.00 25.83 ?  258  THR B CA   1 
ATOM   9319  C C    . THR B 1 258  ? 101.149 148.757 157.009 1.00 25.77 ?  258  THR B C    1 
ATOM   9320  O O    . THR B 1 258  ? 101.285 149.929 157.369 1.00 26.10 ?  258  THR B O    1 
ATOM   9321  C CB   . THR B 1 258  ? 100.746 148.199 159.419 1.00 25.93 ?  258  THR B CB   1 
ATOM   9322  O OG1  . THR B 1 258  ? 102.078 148.184 159.947 1.00 24.71 ?  258  THR B OG1  1 
ATOM   9323  C CG2  . THR B 1 258  ? 99.842  147.352 160.304 1.00 22.57 ?  258  THR B CG2  1 
ATOM   9324  N N    . SER B 1 259  ? 101.352 148.382 155.747 1.00 26.43 ?  259  SER B N    1 
ATOM   9325  C CA   . SER B 1 259  ? 101.684 149.357 154.717 1.00 30.67 ?  259  SER B CA   1 
ATOM   9326  C C    . SER B 1 259  ? 100.507 150.293 154.462 1.00 27.87 ?  259  SER B C    1 
ATOM   9327  O O    . SER B 1 259  ? 99.344  149.880 154.494 1.00 25.40 ?  259  SER B O    1 
ATOM   9328  C CB   . SER B 1 259  ? 102.082 148.649 153.423 1.00 28.27 ?  259  SER B CB   1 
ATOM   9329  O OG   . SER B 1 259  ? 103.250 147.868 153.606 1.00 29.28 ?  259  SER B OG   1 
ATOM   9330  N N    . THR B 1 260  ? 100.815 151.563 154.210 1.00 25.64 ?  260  THR B N    1 
ATOM   9331  C CA   . THR B 1 260  ? 99.798  152.588 154.038 1.00 25.92 ?  260  THR B CA   1 
ATOM   9332  C C    . THR B 1 260  ? 99.454  152.745 152.556 1.00 23.06 ?  260  THR B C    1 
ATOM   9333  O O    . THR B 1 260  ? 99.904  151.974 151.704 1.00 21.76 ?  260  THR B O    1 
ATOM   9334  C CB   . THR B 1 260  ? 100.267 153.908 154.649 1.00 27.33 ?  260  THR B CB   1 
ATOM   9335  O OG1  . THR B 1 260  ? 100.996 154.658 153.670 1.00 23.65 ?  260  THR B OG1  1 
ATOM   9336  C CG2  . THR B 1 260  ? 101.160 153.651 155.855 1.00 24.01 ?  260  THR B CG2  1 
ATOM   9337  N N    . VAL B 1 261  ? 98.636  153.752 152.239 1.00 21.94 ?  261  VAL B N    1 
ATOM   9338  C CA   . VAL B 1 261  ? 98.241  153.990 150.853 1.00 22.75 ?  261  VAL B CA   1 
ATOM   9339  C C    . VAL B 1 261  ? 99.421  154.501 150.037 1.00 24.16 ?  261  VAL B C    1 
ATOM   9340  O O    . VAL B 1 261  ? 99.637  154.072 148.896 1.00 23.99 ?  261  VAL B O    1 
ATOM   9341  C CB   . VAL B 1 261  ? 97.050  154.963 150.798 1.00 22.10 ?  261  VAL B CB   1 
ATOM   9342  C CG1  . VAL B 1 261  ? 96.479  155.026 149.390 1.00 22.06 ?  261  VAL B CG1  1 
ATOM   9343  C CG2  . VAL B 1 261  ? 95.980  154.547 151.796 1.00 21.85 ?  261  VAL B CG2  1 
ATOM   9344  N N    . GLY B 1 262  ? 100.197 155.430 150.600 1.00 21.93 ?  262  GLY B N    1 
ATOM   9345  C CA   . GLY B 1 262  ? 101.387 155.903 149.910 1.00 21.46 ?  262  GLY B CA   1 
ATOM   9346  C C    . GLY B 1 262  ? 102.430 154.815 149.744 1.00 24.00 ?  262  GLY B C    1 
ATOM   9347  O O    . GLY B 1 262  ? 103.088 154.724 148.703 1.00 23.75 ?  262  GLY B O    1 
ATOM   9348  N N    . GLN B 1 263  ? 102.588 153.968 150.765 1.00 24.59 ?  263  GLN B N    1 
ATOM   9349  C CA   . GLN B 1 263  ? 103.493 152.829 150.651 1.00 23.85 ?  263  GLN B CA   1 
ATOM   9350  C C    . GLN B 1 263  ? 103.008 151.845 149.595 1.00 24.91 ?  263  GLN B C    1 
ATOM   9351  O O    . GLN B 1 263  ? 103.816 151.265 148.863 1.00 22.51 ?  263  GLN B O    1 
ATOM   9352  C CB   . GLN B 1 263  ? 103.642 152.138 152.007 1.00 19.65 ?  263  GLN B CB   1 
ATOM   9353  C CG   . GLN B 1 263  ? 103.955 153.082 153.158 1.00 20.63 ?  263  GLN B CG   1 
ATOM   9354  C CD   . GLN B 1 263  ? 105.439 153.370 153.293 1.00 25.19 ?  263  GLN B CD   1 
ATOM   9355  O OE1  . GLN B 1 263  ? 106.128 152.761 154.111 1.00 25.23 ?  263  GLN B OE1  1 
ATOM   9356  N NE2  . GLN B 1 263  ? 105.937 154.306 152.493 1.00 26.35 ?  263  GLN B NE2  1 
ATOM   9357  N N    . ASN B 1 264  ? 101.690 151.648 149.495 1.00 22.27 ?  264  ASN B N    1 
ATOM   9358  C CA   . ASN B 1 264  ? 101.147 150.772 148.460 1.00 21.66 ?  264  ASN B CA   1 
ATOM   9359  C C    . ASN B 1 264  ? 101.378 151.346 147.066 1.00 23.53 ?  264  ASN B C    1 
ATOM   9360  O O    . ASN B 1 264  ? 101.691 150.603 146.128 1.00 30.33 ?  264  ASN B O    1 
ATOM   9361  C CB   . ASN B 1 264  ? 99.658  150.531 148.702 1.00 23.59 ?  264  ASN B CB   1 
ATOM   9362  C CG   . ASN B 1 264  ? 99.403  149.464 149.746 1.00 26.22 ?  264  ASN B CG   1 
ATOM   9363  O OD1  . ASN B 1 264  ? 100.338 148.888 150.302 1.00 25.72 ?  264  ASN B OD1  1 
ATOM   9364  N ND2  . ASN B 1 264  ? 98.132  149.193 150.017 1.00 26.74 ?  264  ASN B ND2  1 
ATOM   9365  N N    . VAL B 1 265  ? 101.229 152.664 146.912 1.00 16.54 ?  265  VAL B N    1 
ATOM   9366  C CA   . VAL B 1 265  ? 101.490 153.303 145.624 1.00 17.80 ?  265  VAL B CA   1 
ATOM   9367  C C    . VAL B 1 265  ? 102.966 153.181 145.255 1.00 20.37 ?  265  VAL B C    1 
ATOM   9368  O O    . VAL B 1 265  ? 103.313 152.887 144.102 1.00 23.72 ?  265  VAL B O    1 
ATOM   9369  C CB   . VAL B 1 265  ? 101.024 154.771 145.661 1.00 17.47 ?  265  VAL B CB   1 
ATOM   9370  C CG1  . VAL B 1 265  ? 101.616 155.565 144.505 1.00 15.71 ?  265  VAL B CG1  1 
ATOM   9371  C CG2  . VAL B 1 265  ? 99.505  154.843 145.637 1.00 16.45 ?  265  VAL B CG2  1 
ATOM   9372  N N    . LEU B 1 266  ? 103.855 153.391 146.229 1.00 15.99 ?  266  LEU B N    1 
ATOM   9373  C CA   . LEU B 1 266  ? 105.286 153.236 145.982 1.00 17.15 ?  266  LEU B CA   1 
ATOM   9374  C C    . LEU B 1 266  ? 105.634 151.794 145.628 1.00 16.71 ?  266  LEU B C    1 
ATOM   9375  O O    . LEU B 1 266  ? 106.486 151.549 144.768 1.00 18.55 ?  266  LEU B O    1 
ATOM   9376  C CB   . LEU B 1 266  ? 106.081 153.698 147.202 1.00 18.69 ?  266  LEU B CB   1 
ATOM   9377  C CG   . LEU B 1 266  ? 107.419 154.384 146.921 1.00 16.37 ?  266  LEU B CG   1 
ATOM   9378  C CD1  . LEU B 1 266  ? 107.239 155.536 145.944 1.00 12.25 ?  266  LEU B CD1  1 
ATOM   9379  C CD2  . LEU B 1 266  ? 108.059 154.866 148.213 1.00 15.89 ?  266  LEU B CD2  1 
ATOM   9380  N N    . TYR B 1 267  ? 104.987 150.827 146.282 1.00 14.62 ?  267  TYR B N    1 
ATOM   9381  C CA   . TYR B 1 267  ? 105.208 149.420 145.960 1.00 19.33 ?  267  TYR B CA   1 
ATOM   9382  C C    . TYR B 1 267  ? 104.726 149.089 144.552 1.00 16.05 ?  267  TYR B C    1 
ATOM   9383  O O    . TYR B 1 267  ? 105.376 148.321 143.832 1.00 21.27 ?  267  TYR B O    1 
ATOM   9384  C CB   . TYR B 1 267  ? 104.506 148.538 146.993 1.00 20.26 ?  267  TYR B CB   1 
ATOM   9385  C CG   . TYR B 1 267  ? 104.627 147.053 146.738 1.00 19.01 ?  267  TYR B CG   1 
ATOM   9386  C CD1  . TYR B 1 267  ? 105.795 146.368 147.048 1.00 18.93 ?  267  TYR B CD1  1 
ATOM   9387  C CD2  . TYR B 1 267  ? 103.569 146.334 146.199 1.00 19.17 ?  267  TYR B CD2  1 
ATOM   9388  C CE1  . TYR B 1 267  ? 105.908 145.009 146.821 1.00 20.67 ?  267  TYR B CE1  1 
ATOM   9389  C CE2  . TYR B 1 267  ? 103.672 144.976 145.968 1.00 18.59 ?  267  TYR B CE2  1 
ATOM   9390  C CZ   . TYR B 1 267  ? 104.843 144.319 146.281 1.00 20.59 ?  267  TYR B CZ   1 
ATOM   9391  O OH   . TYR B 1 267  ? 104.948 142.966 146.053 1.00 21.71 ?  267  TYR B OH   1 
ATOM   9392  N N    . PHE B 1 268  ? 103.585 149.652 144.147 1.00 10.76 ?  268  PHE B N    1 
ATOM   9393  C CA   . PHE B 1 268  ? 103.095 149.451 142.787 1.00 13.17 ?  268  PHE B CA   1 
ATOM   9394  C C    . PHE B 1 268  ? 104.057 150.043 141.764 1.00 13.31 ?  268  PHE B C    1 
ATOM   9395  O O    . PHE B 1 268  ? 104.305 149.441 140.713 1.00 21.04 ?  268  PHE B O    1 
ATOM   9396  C CB   . PHE B 1 268  ? 101.703 150.064 142.635 1.00 19.69 ?  268  PHE B CB   1 
ATOM   9397  C CG   . PHE B 1 268  ? 101.320 150.362 141.211 1.00 19.51 ?  268  PHE B CG   1 
ATOM   9398  C CD1  . PHE B 1 268  ? 101.041 149.334 140.324 1.00 18.72 ?  268  PHE B CD1  1 
ATOM   9399  C CD2  . PHE B 1 268  ? 101.233 151.670 140.761 1.00 17.54 ?  268  PHE B CD2  1 
ATOM   9400  C CE1  . PHE B 1 268  ? 100.687 149.604 139.015 1.00 19.95 ?  268  PHE B CE1  1 
ATOM   9401  C CE2  . PHE B 1 268  ? 100.880 151.947 139.453 1.00 19.77 ?  268  PHE B CE2  1 
ATOM   9402  C CZ   . PHE B 1 268  ? 100.606 150.912 138.580 1.00 21.80 ?  268  PHE B CZ   1 
ATOM   9403  N N    . LEU B 1 269  ? 104.603 151.227 142.055 1.00 9.96  ?  269  LEU B N    1 
ATOM   9404  C CA   . LEU B 1 269  ? 105.602 151.821 141.170 1.00 12.91 ?  269  LEU B CA   1 
ATOM   9405  C C    . LEU B 1 269  ? 106.867 150.973 141.114 1.00 14.79 ?  269  LEU B C    1 
ATOM   9406  O O    . LEU B 1 269  ? 107.484 150.833 140.053 1.00 19.84 ?  269  LEU B O    1 
ATOM   9407  C CB   . LEU B 1 269  ? 105.931 153.243 141.627 1.00 14.41 ?  269  LEU B CB   1 
ATOM   9408  C CG   . LEU B 1 269  ? 104.938 154.356 141.285 1.00 13.67 ?  269  LEU B CG   1 
ATOM   9409  C CD1  . LEU B 1 269  ? 105.597 155.717 141.435 1.00 13.97 ?  269  LEU B CD1  1 
ATOM   9410  C CD2  . LEU B 1 269  ? 104.388 154.183 139.878 1.00 15.15 ?  269  LEU B CD2  1 
ATOM   9411  N N    . GLN B 1 270  ? 107.271 150.408 142.254 1.00 13.47 ?  270  GLN B N    1 
ATOM   9412  C CA   . GLN B 1 270  ? 108.462 149.566 142.302 1.00 12.51 ?  270  GLN B CA   1 
ATOM   9413  C C    . GLN B 1 270  ? 108.274 148.288 141.493 1.00 11.20 ?  270  GLN B C    1 
ATOM   9414  O O    . GLN B 1 270  ? 109.198 147.839 140.806 1.00 12.89 ?  270  GLN B O    1 
ATOM   9415  C CB   . GLN B 1 270  ? 108.798 149.235 143.756 1.00 12.36 ?  270  GLN B CB   1 
ATOM   9416  C CG   . GLN B 1 270  ? 110.202 149.614 144.191 1.00 11.27 ?  270  GLN B CG   1 
ATOM   9417  C CD   . GLN B 1 270  ? 110.359 149.614 145.700 1.00 17.19 ?  270  GLN B CD   1 
ATOM   9418  O OE1  . GLN B 1 270  ? 109.375 149.576 146.438 1.00 17.61 ?  270  GLN B OE1  1 
ATOM   9419  N NE2  . GLN B 1 270  ? 111.601 149.664 146.167 1.00 19.54 ?  270  GLN B NE2  1 
ATOM   9420  N N    . VAL B 1 271  ? 107.084 147.692 141.560 1.00 11.04 ?  271  VAL B N    1 
ATOM   9421  C CA   . VAL B 1 271  ? 106.852 146.415 140.892 1.00 12.78 ?  271  VAL B CA   1 
ATOM   9422  C C    . VAL B 1 271  ? 106.610 146.613 139.401 1.00 11.99 ?  271  VAL B C    1 
ATOM   9423  O O    . VAL B 1 271  ? 107.263 145.982 138.563 1.00 19.82 ?  271  VAL B O    1 
ATOM   9424  C CB   . VAL B 1 271  ? 105.680 145.671 141.559 1.00 10.84 ?  271  VAL B CB   1 
ATOM   9425  C CG1  . VAL B 1 271  ? 105.225 144.509 140.692 1.00 7.89  ?  271  VAL B CG1  1 
ATOM   9426  C CG2  . VAL B 1 271  ? 106.081 145.183 142.940 1.00 12.00 ?  271  VAL B CG2  1 
ATOM   9427  N N    . ALA B 1 272  ? 105.675 147.494 139.043 1.00 9.83  ?  272  ALA B N    1 
ATOM   9428  C CA   . ALA B 1 272  ? 105.204 147.578 137.666 1.00 11.49 ?  272  ALA B CA   1 
ATOM   9429  C C    . ALA B 1 272  ? 106.094 148.417 136.759 1.00 13.63 ?  272  ALA B C    1 
ATOM   9430  O O    . ALA B 1 272  ? 105.887 148.399 135.541 1.00 13.47 ?  272  ALA B O    1 
ATOM   9431  C CB   . ALA B 1 272  ? 103.782 148.142 137.636 1.00 13.84 ?  272  ALA B CB   1 
ATOM   9432  N N    . VAL B 1 273  ? 107.070 149.148 137.300 1.00 14.67 ?  273  VAL B N    1 
ATOM   9433  C CA   . VAL B 1 273  ? 107.922 150.031 136.513 1.00 13.51 ?  273  VAL B CA   1 
ATOM   9434  C C    . VAL B 1 273  ? 109.398 149.693 136.689 1.00 9.47  ?  273  VAL B C    1 
ATOM   9435  O O    . VAL B 1 273  ? 110.112 149.454 135.711 1.00 9.17  ?  273  VAL B O    1 
ATOM   9436  C CB   . VAL B 1 273  ? 107.660 151.516 136.850 1.00 15.32 ?  273  VAL B CB   1 
ATOM   9437  C CG1  . VAL B 1 273  ? 108.664 152.406 136.134 1.00 15.39 ?  273  VAL B CG1  1 
ATOM   9438  C CG2  . VAL B 1 273  ? 106.240 151.907 136.477 1.00 15.53 ?  273  VAL B CG2  1 
ATOM   9439  N N    . ALA B 1 274  ? 109.874 149.668 137.937 1.00 7.67  ?  274  ALA B N    1 
ATOM   9440  C CA   . ALA B 1 274  ? 111.307 149.549 138.187 1.00 6.48  ?  274  ALA B CA   1 
ATOM   9441  C C    . ALA B 1 274  ? 111.846 148.170 137.824 1.00 11.72 ?  274  ALA B C    1 
ATOM   9442  O O    . ALA B 1 274  ? 112.989 148.057 137.366 1.00 12.90 ?  274  ALA B O    1 
ATOM   9443  C CB   . ALA B 1 274  ? 111.608 149.868 139.650 1.00 7.89  ?  274  ALA B CB   1 
ATOM   9444  N N    . GLY B 1 275  ? 111.051 147.121 138.019 1.00 9.06  ?  275  GLY B N    1 
ATOM   9445  C CA   . GLY B 1 275  ? 111.458 145.774 137.691 1.00 3.20  ?  275  GLY B CA   1 
ATOM   9446  C C    . GLY B 1 275  ? 111.726 145.555 136.213 1.00 8.56  ?  275  GLY B C    1 
ATOM   9447  O O    . GLY B 1 275  ? 112.814 145.115 135.819 1.00 11.33 ?  275  GLY B O    1 
ATOM   9448  N N    . PRO B 1 276  ? 110.725 145.828 135.368 1.00 7.16  ?  276  PRO B N    1 
ATOM   9449  C CA   . PRO B 1 276  ? 110.962 145.772 133.916 1.00 2.00  ?  276  PRO B CA   1 
ATOM   9450  C C    . PRO B 1 276  ? 112.092 146.671 133.447 1.00 4.26  ?  276  PRO B C    1 
ATOM   9451  O O    . PRO B 1 276  ? 112.808 146.300 132.511 1.00 9.46  ?  276  PRO B O    1 
ATOM   9452  C CB   . PRO B 1 276  ? 109.617 146.210 133.317 1.00 1.70  ?  276  PRO B CB   1 
ATOM   9453  C CG   . PRO B 1 276  ? 108.625 146.205 134.442 1.00 1.79  ?  276  PRO B CG   1 
ATOM   9454  C CD   . PRO B 1 276  ? 109.291 145.745 135.693 1.00 3.34  ?  276  PRO B CD   1 
ATOM   9455  N N    . LEU B 1 277  ? 112.284 147.836 134.073 1.00 5.52  ?  277  LEU B N    1 
ATOM   9456  C CA   . LEU B 1 277  ? 113.412 148.693 133.718 1.00 0.74  ?  277  LEU B CA   1 
ATOM   9457  C C    . LEU B 1 277  ? 114.745 148.034 134.054 1.00 1.12  ?  277  LEU B C    1 
ATOM   9458  O O    . LEU B 1 277  ? 115.697 148.115 133.267 1.00 8.72  ?  277  LEU B O    1 
ATOM   9459  C CB   . LEU B 1 277  ? 113.292 150.042 134.424 1.00 3.70  ?  277  LEU B CB   1 
ATOM   9460  C CG   . LEU B 1 277  ? 112.877 151.239 133.566 1.00 5.45  ?  277  LEU B CG   1 
ATOM   9461  C CD1  . LEU B 1 277  ? 111.392 151.202 133.244 1.00 8.60  ?  277  LEU B CD1  1 
ATOM   9462  C CD2  . LEU B 1 277  ? 113.248 152.535 134.267 1.00 9.10  ?  277  LEU B CD2  1 
ATOM   9463  N N    . TRP B 1 278  ? 114.834 147.385 135.220 1.00 0.08  ?  278  TRP B N    1 
ATOM   9464  C CA   . TRP B 1 278  ? 116.054 146.668 135.585 1.00 1.71  ?  278  TRP B CA   1 
ATOM   9465  C C    . TRP B 1 278  ? 116.336 145.533 134.610 1.00 1.83  ?  278  TRP B C    1 
ATOM   9466  O O    . TRP B 1 278  ? 117.480 145.345 134.172 1.00 4.93  ?  278  TRP B O    1 
ATOM   9467  C CB   . TRP B 1 278  ? 115.936 146.134 137.014 1.00 5.84  ?  278  TRP B CB   1 
ATOM   9468  C CG   . TRP B 1 278  ? 116.952 145.084 137.369 1.00 5.15  ?  278  TRP B CG   1 
ATOM   9469  C CD1  . TRP B 1 278  ? 116.725 143.748 137.533 1.00 3.34  ?  278  TRP B CD1  1 
ATOM   9470  C CD2  . TRP B 1 278  ? 118.349 145.285 137.619 1.00 3.79  ?  278  TRP B CD2  1 
ATOM   9471  N NE1  . TRP B 1 278  ? 117.893 143.105 137.860 1.00 3.25  ?  278  TRP B NE1  1 
ATOM   9472  C CE2  . TRP B 1 278  ? 118.905 144.026 137.920 1.00 0.00  ?  278  TRP B CE2  1 
ATOM   9473  C CE3  . TRP B 1 278  ? 119.183 146.407 137.613 1.00 0.95  ?  278  TRP B CE3  1 
ATOM   9474  C CZ2  . TRP B 1 278  ? 120.257 143.858 138.210 1.00 0.00  ?  278  TRP B CZ2  1 
ATOM   9475  C CZ3  . TRP B 1 278  ? 120.525 146.237 137.902 1.00 2.54  ?  278  TRP B CZ3  1 
ATOM   9476  C CH2  . TRP B 1 278  ? 121.048 144.973 138.197 1.00 4.12  ?  278  TRP B CH2  1 
ATOM   9477  N N    . GLY B 1 279  ? 115.296 144.779 134.247 1.00 0.00  ?  279  GLY B N    1 
ATOM   9478  C CA   . GLY B 1 279  ? 115.470 143.706 133.280 1.00 0.00  ?  279  GLY B CA   1 
ATOM   9479  C C    . GLY B 1 279  ? 115.906 144.213 131.920 1.00 0.03  ?  279  GLY B C    1 
ATOM   9480  O O    . GLY B 1 279  ? 116.787 143.630 131.282 1.00 7.33  ?  279  GLY B O    1 
ATOM   9481  N N    . TYR B 1 280  ? 115.314 145.325 131.472 1.00 2.79  ?  280  TYR B N    1 
ATOM   9482  C CA   . TYR B 1 280  ? 115.680 145.927 130.193 1.00 0.00  ?  280  TYR B CA   1 
ATOM   9483  C C    . TYR B 1 280  ? 117.126 146.411 130.193 1.00 2.32  ?  280  TYR B C    1 
ATOM   9484  O O    . TYR B 1 280  ? 117.852 146.213 129.212 1.00 12.82 ?  280  TYR B O    1 
ATOM   9485  C CB   . TYR B 1 280  ? 114.722 147.078 129.881 1.00 2.83  ?  280  TYR B CB   1 
ATOM   9486  C CG   . TYR B 1 280  ? 115.101 147.917 128.681 1.00 4.77  ?  280  TYR B CG   1 
ATOM   9487  C CD1  . TYR B 1 280  ? 114.833 147.480 127.391 1.00 8.01  ?  280  TYR B CD1  1 
ATOM   9488  C CD2  . TYR B 1 280  ? 115.709 149.156 128.840 1.00 2.85  ?  280  TYR B CD2  1 
ATOM   9489  C CE1  . TYR B 1 280  ? 115.173 148.246 126.293 1.00 7.62  ?  280  TYR B CE1  1 
ATOM   9490  C CE2  . TYR B 1 280  ? 116.053 149.928 127.748 1.00 6.85  ?  280  TYR B CE2  1 
ATOM   9491  C CZ   . TYR B 1 280  ? 115.782 149.468 126.478 1.00 11.07 ?  280  TYR B CZ   1 
ATOM   9492  O OH   . TYR B 1 280  ? 116.121 150.233 125.386 1.00 17.44 ?  280  TYR B OH   1 
ATOM   9493  N N    . ALA B 1 281  ? 117.561 147.051 131.283 1.00 0.00  ?  281  ALA B N    1 
ATOM   9494  C CA   . ALA B 1 281  ? 118.936 147.539 131.358 1.00 0.00  ?  281  ALA B CA   1 
ATOM   9495  C C    . ALA B 1 281  ? 119.941 146.393 131.360 1.00 0.00  ?  281  ALA B C    1 
ATOM   9496  O O    . ALA B 1 281  ? 120.959 146.450 130.653 1.00 6.63  ?  281  ALA B O    1 
ATOM   9497  C CB   . ALA B 1 281  ? 119.115 148.410 132.599 1.00 0.00  ?  281  ALA B CB   1 
ATOM   9498  N N    . VAL B 1 282  ? 119.672 145.342 132.144 1.00 2.55  ?  282  VAL B N    1 
ATOM   9499  C CA   . VAL B 1 282  ? 120.579 144.198 132.171 1.00 1.16  ?  282  VAL B CA   1 
ATOM   9500  C C    . VAL B 1 282  ? 120.620 143.519 130.807 1.00 0.11  ?  282  VAL B C    1 
ATOM   9501  O O    . VAL B 1 282  ? 121.688 143.105 130.335 1.00 0.61  ?  282  VAL B O    1 
ATOM   9502  C CB   . VAL B 1 282  ? 120.175 143.218 133.289 1.00 0.00  ?  282  VAL B CB   1 
ATOM   9503  C CG1  . VAL B 1 282  ? 121.020 141.963 133.227 1.00 0.03  ?  282  VAL B CG1  1 
ATOM   9504  C CG2  . VAL B 1 282  ? 120.331 143.876 134.641 1.00 0.57  ?  282  VAL B CG2  1 
ATOM   9505  N N    . ALA B 1 283  ? 119.467 143.424 130.137 1.00 1.31  ?  283  ALA B N    1 
ATOM   9506  C CA   . ALA B 1 283  ? 119.423 142.834 128.804 1.00 0.00  ?  283  ALA B CA   1 
ATOM   9507  C C    . ALA B 1 283  ? 120.229 143.651 127.800 1.00 1.98  ?  283  ALA B C    1 
ATOM   9508  O O    . ALA B 1 283  ? 120.962 143.086 126.982 1.00 3.80  ?  283  ALA B O    1 
ATOM   9509  C CB   . ALA B 1 283  ? 117.973 142.700 128.346 1.00 0.00  ?  283  ALA B CB   1 
ATOM   9510  N N    . LYS B 1 284  ? 120.106 144.981 127.847 1.00 7.41  ?  284  LYS B N    1 
ATOM   9511  C CA   . LYS B 1 284  ? 120.864 145.833 126.934 1.00 0.42  ?  284  LYS B CA   1 
ATOM   9512  C C    . LYS B 1 284  ? 122.365 145.690 127.151 1.00 2.15  ?  284  LYS B C    1 
ATOM   9513  O O    . LYS B 1 284  ? 123.133 145.597 126.184 1.00 6.52  ?  284  LYS B O    1 
ATOM   9514  C CB   . LYS B 1 284  ? 120.434 147.289 127.101 1.00 0.00  ?  284  LYS B CB   1 
ATOM   9515  C CG   . LYS B 1 284  ? 119.159 147.643 126.365 1.00 0.00  ?  284  LYS B CG   1 
ATOM   9516  C CD   . LYS B 1 284  ? 119.277 147.308 124.889 1.00 2.62  ?  284  LYS B CD   1 
ATOM   9517  C CE   . LYS B 1 284  ? 117.926 146.989 124.280 1.00 1.92  ?  284  LYS B CE   1 
ATOM   9518  N NZ   . LYS B 1 284  ? 118.065 146.179 123.042 1.00 5.95  ?  284  LYS B NZ   1 
ATOM   9519  N N    . VAL B 1 285  ? 122.800 145.652 128.415 1.00 1.00  ?  285  VAL B N    1 
ATOM   9520  C CA   . VAL B 1 285  ? 124.222 145.466 128.700 1.00 0.00  ?  285  VAL B CA   1 
ATOM   9521  C C    . VAL B 1 285  ? 124.693 144.100 128.206 1.00 4.15  ?  285  VAL B C    1 
ATOM   9522  O O    . VAL B 1 285  ? 125.800 143.963 127.660 1.00 8.31  ?  285  VAL B O    1 
ATOM   9523  C CB   . VAL B 1 285  ? 124.490 145.657 130.206 1.00 1.46  ?  285  VAL B CB   1 
ATOM   9524  C CG1  . VAL B 1 285  ? 125.921 145.283 130.557 1.00 9.54  ?  285  VAL B CG1  1 
ATOM   9525  C CG2  . VAL B 1 285  ? 124.200 147.090 130.617 1.00 1.79  ?  285  VAL B CG2  1 
ATOM   9526  N N    . THR B 1 286  ? 123.852 143.073 128.369 1.00 4.91  ?  286  THR B N    1 
ATOM   9527  C CA   . THR B 1 286  ? 124.221 141.726 127.944 1.00 1.84  ?  286  THR B CA   1 
ATOM   9528  C C    . THR B 1 286  ? 124.393 141.641 126.430 1.00 2.10  ?  286  THR B C    1 
ATOM   9529  O O    . THR B 1 286  ? 125.361 141.049 125.945 1.00 5.73  ?  286  THR B O    1 
ATOM   9530  C CB   . THR B 1 286  ? 123.176 140.721 128.427 1.00 9.59  ?  286  THR B CB   1 
ATOM   9531  O OG1  . THR B 1 286  ? 122.963 140.896 129.833 1.00 10.32 ?  286  THR B OG1  1 
ATOM   9532  C CG2  . THR B 1 286  ? 123.645 139.296 128.167 1.00 6.87  ?  286  THR B CG2  1 
ATOM   9533  N N    . VAL B 1 287  ? 123.466 142.229 125.664 1.00 5.19  ?  287  VAL B N    1 
ATOM   9534  C CA   . VAL B 1 287  ? 123.622 142.226 124.207 1.00 1.47  ?  287  VAL B CA   1 
ATOM   9535  C C    . VAL B 1 287  ? 124.818 143.067 123.777 1.00 1.82  ?  287  VAL B C    1 
ATOM   9536  O O    . VAL B 1 287  ? 125.518 142.716 122.817 1.00 2.86  ?  287  VAL B O    1 
ATOM   9537  C CB   . VAL B 1 287  ? 122.336 142.676 123.488 1.00 5.33  ?  287  VAL B CB   1 
ATOM   9538  C CG1  . VAL B 1 287  ? 122.360 142.194 122.064 1.00 14.43 ?  287  VAL B CG1  1 
ATOM   9539  C CG2  . VAL B 1 287  ? 121.134 142.047 124.120 1.00 7.63  ?  287  VAL B CG2  1 
ATOM   9540  N N    . PHE B 1 288  ? 125.075 144.185 124.467 1.00 2.56  ?  288  PHE B N    1 
ATOM   9541  C CA   . PHE B 1 288  ? 126.236 144.999 124.118 1.00 0.00  ?  288  PHE B CA   1 
ATOM   9542  C C    . PHE B 1 288  ? 127.531 144.220 124.293 1.00 3.24  ?  288  PHE B C    1 
ATOM   9543  O O    . PHE B 1 288  ? 128.421 144.283 123.438 1.00 7.59  ?  288  PHE B O    1 
ATOM   9544  C CB   . PHE B 1 288  ? 126.280 146.275 124.958 1.00 6.61  ?  288  PHE B CB   1 
ATOM   9545  C CG   . PHE B 1 288  ? 127.597 146.998 124.879 1.00 8.52  ?  288  PHE B CG   1 
ATOM   9546  C CD1  . PHE B 1 288  ? 127.987 147.624 123.706 1.00 9.51  ?  288  PHE B CD1  1 
ATOM   9547  C CD2  . PHE B 1 288  ? 128.449 147.040 125.969 1.00 8.70  ?  288  PHE B CD2  1 
ATOM   9548  C CE1  . PHE B 1 288  ? 129.200 148.282 123.624 1.00 8.11  ?  288  PHE B CE1  1 
ATOM   9549  C CE2  . PHE B 1 288  ? 129.665 147.698 125.892 1.00 8.82  ?  288  PHE B CE2  1 
ATOM   9550  C CZ   . PHE B 1 288  ? 130.039 148.319 124.718 1.00 8.53  ?  288  PHE B CZ   1 
ATOM   9551  N N    . PHE B 1 289  ? 127.654 143.472 125.389 1.00 7.12  ?  289  PHE B N    1 
ATOM   9552  C CA   . PHE B 1 289  ? 128.871 142.691 125.587 1.00 3.34  ?  289  PHE B CA   1 
ATOM   9553  C C    . PHE B 1 289  ? 128.901 141.427 124.732 1.00 0.00  ?  289  PHE B C    1 
ATOM   9554  O O    . PHE B 1 289  ? 129.987 140.934 124.411 1.00 0.00  ?  289  PHE B O    1 
ATOM   9555  C CB   . PHE B 1 289  ? 129.043 142.348 127.066 1.00 3.24  ?  289  PHE B CB   1 
ATOM   9556  C CG   . PHE B 1 289  ? 129.650 143.463 127.871 1.00 10.48 ?  289  PHE B CG   1 
ATOM   9557  C CD1  . PHE B 1 289  ? 130.915 143.940 127.569 1.00 9.64  ?  289  PHE B CD1  1 
ATOM   9558  C CD2  . PHE B 1 289  ? 128.955 144.040 128.920 1.00 9.50  ?  289  PHE B CD2  1 
ATOM   9559  C CE1  . PHE B 1 289  ? 131.478 144.968 128.301 1.00 9.43  ?  289  PHE B CE1  1 
ATOM   9560  C CE2  . PHE B 1 289  ? 129.513 145.070 129.657 1.00 6.69  ?  289  PHE B CE2  1 
ATOM   9561  C CZ   . PHE B 1 289  ? 130.776 145.533 129.346 1.00 8.40  ?  289  PHE B CZ   1 
ATOM   9562  N N    . LEU B 1 290  ? 127.740 140.892 124.350 1.00 5.80  ?  290  LEU B N    1 
ATOM   9563  C CA   . LEU B 1 290  ? 127.708 139.703 123.506 1.00 1.23  ?  290  LEU B CA   1 
ATOM   9564  C C    . LEU B 1 290  ? 128.039 140.013 122.053 1.00 4.65  ?  290  LEU B C    1 
ATOM   9565  O O    . LEU B 1 290  ? 128.564 139.146 121.347 1.00 7.39  ?  290  LEU B O    1 
ATOM   9566  C CB   . LEU B 1 290  ? 126.335 139.031 123.589 1.00 1.48  ?  290  LEU B CB   1 
ATOM   9567  C CG   . LEU B 1 290  ? 126.084 138.050 124.736 1.00 0.00  ?  290  LEU B CG   1 
ATOM   9568  C CD1  . LEU B 1 290  ? 124.894 137.159 124.424 1.00 0.35  ?  290  LEU B CD1  1 
ATOM   9569  C CD2  . LEU B 1 290  ? 127.319 137.211 125.013 1.00 4.41  ?  290  LEU B CD2  1 
ATOM   9570  N N    . SER B 1 291  ? 127.740 141.229 121.587 1.00 9.34  ?  291  SER B N    1 
ATOM   9571  C CA   . SER B 1 291  ? 128.000 141.580 120.195 1.00 1.97  ?  291  SER B CA   1 
ATOM   9572  C C    . SER B 1 291  ? 129.485 141.675 119.864 1.00 7.10  ?  291  SER B C    1 
ATOM   9573  O O    . SER B 1 291  ? 129.834 141.679 118.680 1.00 8.49  ?  291  SER B O    1 
ATOM   9574  C CB   . SER B 1 291  ? 127.318 142.904 119.852 1.00 3.76  ?  291  SER B CB   1 
ATOM   9575  O OG   . SER B 1 291  ? 128.088 144.005 120.303 1.00 3.75  ?  291  SER B OG   1 
ATOM   9576  N N    . HIS B 1 292  ? 130.361 141.746 120.865 1.00 14.30 ?  292  HIS B N    1 
ATOM   9577  C CA   . HIS B 1 292  ? 131.791 141.907 120.646 1.00 7.40  ?  292  HIS B CA   1 
ATOM   9578  C C    . HIS B 1 292  ? 132.564 140.601 120.775 1.00 10.16 ?  292  HIS B C    1 
ATOM   9579  O O    . HIS B 1 292  ? 133.797 140.627 120.816 1.00 15.96 ?  292  HIS B O    1 
ATOM   9580  C CB   . HIS B 1 292  ? 132.355 142.944 121.619 1.00 4.14  ?  292  HIS B CB   1 
ATOM   9581  C CG   . HIS B 1 292  ? 131.974 144.351 121.284 1.00 13.15 ?  292  HIS B CG   1 
ATOM   9582  N ND1  . HIS B 1 292  ? 132.171 144.897 120.034 1.00 15.87 ?  292  HIS B ND1  1 
ATOM   9583  C CD2  . HIS B 1 292  ? 131.401 145.323 122.032 1.00 15.12 ?  292  HIS B CD2  1 
ATOM   9584  C CE1  . HIS B 1 292  ? 131.740 146.145 120.027 1.00 14.40 ?  292  HIS B CE1  1 
ATOM   9585  N NE2  . HIS B 1 292  ? 131.268 146.428 121.228 1.00 12.84 ?  292  HIS B NE2  1 
ATOM   9586  N N    . ILE B 1 293  ? 131.874 139.466 120.840 1.00 6.20  ?  293  ILE B N    1 
ATOM   9587  C CA   . ILE B 1 293  ? 132.506 138.160 120.983 1.00 3.60  ?  293  ILE B CA   1 
ATOM   9588  C C    . ILE B 1 293  ? 132.313 137.396 119.682 1.00 3.53  ?  293  ILE B C    1 
ATOM   9589  O O    . ILE B 1 293  ? 131.176 137.158 119.256 1.00 7.92  ?  293  ILE B O    1 
ATOM   9590  C CB   . ILE B 1 293  ? 131.930 137.380 122.175 1.00 10.71 ?  293  ILE B CB   1 
ATOM   9591  C CG1  . ILE B 1 293  ? 132.308 138.059 123.491 1.00 6.03  ?  293  ILE B CG1  1 
ATOM   9592  C CG2  . ILE B 1 293  ? 132.412 135.941 122.160 1.00 6.57  ?  293  ILE B CG2  1 
ATOM   9593  C CD1  . ILE B 1 293  ? 131.289 137.865 124.584 1.00 5.12  ?  293  ILE B CD1  1 
ATOM   9594  N N    . PHE B 1 294  ? 133.421 137.009 119.055 1.00 6.20  ?  294  PHE B N    1 
ATOM   9595  C CA   . PHE B 1 294  ? 133.409 136.276 117.797 1.00 5.96  ?  294  PHE B CA   1 
ATOM   9596  C C    . PHE B 1 294  ? 134.053 134.913 118.002 1.00 8.81  ?  294  PHE B C    1 
ATOM   9597  O O    . PHE B 1 294  ? 135.136 134.820 118.591 1.00 12.64 ?  294  PHE B O    1 
ATOM   9598  C CB   . PHE B 1 294  ? 134.148 137.049 116.698 1.00 9.75  ?  294  PHE B CB   1 
ATOM   9599  C CG   . PHE B 1 294  ? 133.649 138.455 116.501 1.00 12.00 ?  294  PHE B CG   1 
ATOM   9600  C CD1  . PHE B 1 294  ? 132.486 138.699 115.793 1.00 5.19  ?  294  PHE B CD1  1 
ATOM   9601  C CD2  . PHE B 1 294  ? 134.349 139.532 117.017 1.00 12.48 ?  294  PHE B CD2  1 
ATOM   9602  C CE1  . PHE B 1 294  ? 132.027 139.988 115.611 1.00 7.18  ?  294  PHE B CE1  1 
ATOM   9603  C CE2  . PHE B 1 294  ? 133.893 140.825 116.836 1.00 8.60  ?  294  PHE B CE2  1 
ATOM   9604  C CZ   . PHE B 1 294  ? 132.731 141.051 116.133 1.00 6.87  ?  294  PHE B CZ   1 
ATOM   9605  N N    . ASN B 1 295  ? 133.375 133.864 117.525 1.00 11.17 ?  295  ASN B N    1 
ATOM   9606  C CA   . ASN B 1 295  ? 133.887 132.489 117.528 1.00 14.12 ?  295  ASN B CA   1 
ATOM   9607  C C    . ASN B 1 295  ? 134.185 131.995 118.945 1.00 16.13 ?  295  ASN B C    1 
ATOM   9608  O O    . ASN B 1 295  ? 135.279 131.510 119.244 1.00 12.43 ?  295  ASN B O    1 
ATOM   9609  C CB   . ASN B 1 295  ? 135.121 132.358 116.629 1.00 17.45 ?  295  ASN B CB   1 
ATOM   9610  C CG   . ASN B 1 295  ? 135.353 130.935 116.159 1.00 19.28 ?  295  ASN B CG   1 
ATOM   9611  O OD1  . ASN B 1 295  ? 134.428 130.124 116.113 1.00 20.33 ?  295  ASN B OD1  1 
ATOM   9612  N ND2  . ASN B 1 295  ? 136.597 130.623 115.814 1.00 14.46 ?  295  ASN B ND2  1 
ATOM   9613  N N    . ASP B 1 296  ? 133.191 132.120 119.826 1.00 13.01 ?  296  ASP B N    1 
ATOM   9614  C CA   . ASP B 1 296  ? 133.306 131.601 121.189 1.00 6.49  ?  296  ASP B CA   1 
ATOM   9615  C C    . ASP B 1 296  ? 131.898 131.276 121.679 1.00 4.05  ?  296  ASP B C    1 
ATOM   9616  O O    . ASP B 1 296  ? 131.177 132.171 122.126 1.00 11.18 ?  296  ASP B O    1 
ATOM   9617  C CB   . ASP B 1 296  ? 133.997 132.602 122.104 1.00 8.53  ?  296  ASP B CB   1 
ATOM   9618  C CG   . ASP B 1 296  ? 135.066 131.963 122.964 1.00 14.54 ?  296  ASP B CG   1 
ATOM   9619  O OD1  . ASP B 1 296  ? 134.865 130.814 123.410 1.00 14.84 ?  296  ASP B OD1  1 
ATOM   9620  O OD2  . ASP B 1 296  ? 136.108 132.611 123.195 1.00 14.06 ?  296  ASP B OD2  1 
ATOM   9621  N N    . ALA B 1 297  ? 131.520 130.000 121.599 1.00 3.82  ?  297  ALA B N    1 
ATOM   9622  C CA   . ALA B 1 297  ? 130.193 129.594 122.049 1.00 0.00  ?  297  ALA B CA   1 
ATOM   9623  C C    . ALA B 1 297  ? 130.111 129.509 123.568 1.00 0.12  ?  297  ALA B C    1 
ATOM   9624  O O    . ALA B 1 297  ? 129.085 129.867 124.158 1.00 5.24  ?  297  ALA B O    1 
ATOM   9625  C CB   . ALA B 1 297  ? 129.815 128.253 121.422 1.00 0.41  ?  297  ALA B CB   1 
ATOM   9626  N N    . LEU B 1 298  ? 131.183 129.039 124.212 1.00 0.00  ?  298  LEU B N    1 
ATOM   9627  C CA   . LEU B 1 298  ? 131.169 128.864 125.661 1.00 0.00  ?  298  LEU B CA   1 
ATOM   9628  C C    . LEU B 1 298  ? 131.056 130.199 126.384 1.00 0.00  ?  298  LEU B C    1 
ATOM   9629  O O    . LEU B 1 298  ? 130.307 130.318 127.361 1.00 0.00  ?  298  LEU B O    1 
ATOM   9630  C CB   . LEU B 1 298  ? 132.425 128.117 126.108 1.00 1.55  ?  298  LEU B CB   1 
ATOM   9631  C CG   . LEU B 1 298  ? 132.557 126.654 125.678 1.00 0.00  ?  298  LEU B CG   1 
ATOM   9632  C CD1  . LEU B 1 298  ? 133.659 125.971 126.464 1.00 0.83  ?  298  LEU B CD1  1 
ATOM   9633  C CD2  . LEU B 1 298  ? 131.241 125.917 125.853 1.00 2.71  ?  298  LEU B CD2  1 
ATOM   9634  N N    . VAL B 1 299  ? 131.786 131.214 125.913 1.00 0.47  ?  299  VAL B N    1 
ATOM   9635  C CA   . VAL B 1 299  ? 131.731 132.532 126.539 1.00 1.47  ?  299  VAL B CA   1 
ATOM   9636  C C    . VAL B 1 299  ? 130.331 133.118 126.429 1.00 3.16  ?  299  VAL B C    1 
ATOM   9637  O O    . VAL B 1 299  ? 129.780 133.629 127.409 1.00 10.55 ?  299  VAL B O    1 
ATOM   9638  C CB   . VAL B 1 299  ? 132.782 133.467 125.913 1.00 0.00  ?  299  VAL B CB   1 
ATOM   9639  C CG1  . VAL B 1 299  ? 132.585 134.887 126.403 1.00 0.00  ?  299  VAL B CG1  1 
ATOM   9640  C CG2  . VAL B 1 299  ? 134.178 132.989 126.243 1.00 1.10  ?  299  VAL B CG2  1 
ATOM   9641  N N    . GLU B 1 300  ? 129.726 133.026 125.242 1.00 0.00  ?  300  GLU B N    1 
ATOM   9642  C CA   . GLU B 1 300  ? 128.383 133.560 125.042 1.00 0.00  ?  300  GLU B CA   1 
ATOM   9643  C C    . GLU B 1 300  ? 127.360 132.829 125.904 1.00 3.02  ?  300  GLU B C    1 
ATOM   9644  O O    . GLU B 1 300  ? 126.502 133.464 126.532 1.00 10.98 ?  300  GLU B O    1 
ATOM   9645  C CB   . GLU B 1 300  ? 128.005 133.470 123.564 1.00 0.00  ?  300  GLU B CB   1 
ATOM   9646  C CG   . GLU B 1 300  ? 128.853 134.345 122.651 1.00 6.66  ?  300  GLU B CG   1 
ATOM   9647  C CD   . GLU B 1 300  ? 128.198 134.603 121.307 1.00 9.37  ?  300  GLU B CD   1 
ATOM   9648  O OE1  . GLU B 1 300  ? 127.043 135.078 121.285 1.00 8.89  ?  300  GLU B OE1  1 
ATOM   9649  O OE2  . GLU B 1 300  ? 128.840 134.332 120.270 1.00 9.27  ?  300  GLU B OE2  1 
ATOM   9650  N N    . ILE B 1 301  ? 127.454 131.497 125.969 1.00 3.93  ?  301  ILE B N    1 
ATOM   9651  C CA   . ILE B 1 301  ? 126.492 130.709 126.738 1.00 0.00  ?  301  ILE B CA   1 
ATOM   9652  C C    . ILE B 1 301  ? 126.603 131.029 128.225 1.00 0.00  ?  301  ILE B C    1 
ATOM   9653  O O    . ILE B 1 301  ? 125.595 131.270 128.905 1.00 0.00  ?  301  ILE B O    1 
ATOM   9654  C CB   . ILE B 1 301  ? 126.697 129.207 126.465 1.00 0.00  ?  301  ILE B CB   1 
ATOM   9655  C CG1  . ILE B 1 301  ? 126.074 128.818 125.124 1.00 0.00  ?  301  ILE B CG1  1 
ATOM   9656  C CG2  . ILE B 1 301  ? 126.108 128.362 127.582 1.00 0.00  ?  301  ILE B CG2  1 
ATOM   9657  C CD1  . ILE B 1 301  ? 126.682 127.582 124.512 1.00 0.00  ?  301  ILE B CD1  1 
ATOM   9658  N N    . THR B 1 302  ? 127.834 131.064 128.748 1.00 0.00  ?  302  THR B N    1 
ATOM   9659  C CA   . THR B 1 302  ? 128.017 131.322 130.172 1.00 3.70  ?  302  THR B CA   1 
ATOM   9660  C C    . THR B 1 302  ? 127.649 132.755 130.535 1.00 0.00  ?  302  THR B C    1 
ATOM   9661  O O    . THR B 1 302  ? 127.073 132.993 131.601 1.00 3.17  ?  302  THR B O    1 
ATOM   9662  C CB   . THR B 1 302  ? 129.454 131.015 130.592 1.00 0.00  ?  302  THR B CB   1 
ATOM   9663  O OG1  . THR B 1 302  ? 130.366 131.779 129.795 1.00 0.00  ?  302  THR B OG1  1 
ATOM   9664  C CG2  . THR B 1 302  ? 129.754 129.528 130.444 1.00 2.79  ?  302  THR B CG2  1 
ATOM   9665  N N    . ILE B 1 303  ? 127.952 133.719 129.660 1.00 2.70  ?  303  ILE B N    1 
ATOM   9666  C CA   . ILE B 1 303  ? 127.578 135.106 129.924 1.00 0.02  ?  303  ILE B CA   1 
ATOM   9667  C C    . ILE B 1 303  ? 126.063 135.261 129.938 1.00 5.41  ?  303  ILE B C    1 
ATOM   9668  O O    . ILE B 1 303  ? 125.506 135.922 130.823 1.00 1.69  ?  303  ILE B O    1 
ATOM   9669  C CB   . ILE B 1 303  ? 128.245 136.043 128.898 1.00 1.42  ?  303  ILE B CB   1 
ATOM   9670  C CG1  . ILE B 1 303  ? 129.723 136.256 129.238 1.00 5.21  ?  303  ILE B CG1  1 
ATOM   9671  C CG2  . ILE B 1 303  ? 127.522 137.383 128.821 1.00 5.66  ?  303  ILE B CG2  1 
ATOM   9672  C CD1  . ILE B 1 303  ? 129.984 136.592 130.691 1.00 7.69  ?  303  ILE B CD1  1 
ATOM   9673  N N    . THR B 1 304  ? 125.370 134.638 128.978 1.00 0.00  ?  304  THR B N    1 
ATOM   9674  C CA   . THR B 1 304  ? 123.912 134.718 128.947 1.00 0.00  ?  304  THR B CA   1 
ATOM   9675  C C    . THR B 1 304  ? 123.290 134.085 130.187 1.00 7.78  ?  304  THR B C    1 
ATOM   9676  O O    . THR B 1 304  ? 122.385 134.665 130.803 1.00 8.57  ?  304  THR B O    1 
ATOM   9677  C CB   . THR B 1 304  ? 123.379 134.043 127.684 1.00 0.00  ?  304  THR B CB   1 
ATOM   9678  O OG1  . THR B 1 304  ? 124.246 134.335 126.582 1.00 0.00  ?  304  THR B OG1  1 
ATOM   9679  C CG2  . THR B 1 304  ? 121.982 134.540 127.366 1.00 0.00  ?  304  THR B CG2  1 
ATOM   9680  N N    . LEU B 1 305  ? 123.776 132.905 130.582 1.00 0.00  ?  305  LEU B N    1 
ATOM   9681  C CA   . LEU B 1 305  ? 123.198 132.222 131.736 1.00 0.00  ?  305  LEU B CA   1 
ATOM   9682  C C    . LEU B 1 305  ? 123.487 132.969 133.035 1.00 0.00  ?  305  LEU B C    1 
ATOM   9683  O O    . LEU B 1 305  ? 122.616 133.065 133.911 1.00 1.21  ?  305  LEU B O    1 
ATOM   9684  C CB   . LEU B 1 305  ? 123.720 130.789 131.803 1.00 0.00  ?  305  LEU B CB   1 
ATOM   9685  C CG   . LEU B 1 305  ? 123.162 129.825 130.751 1.00 1.30  ?  305  LEU B CG   1 
ATOM   9686  C CD1  . LEU B 1 305  ? 123.685 128.415 130.969 1.00 0.00  ?  305  LEU B CD1  1 
ATOM   9687  C CD2  . LEU B 1 305  ? 121.643 129.845 130.750 1.00 0.00  ?  305  LEU B CD2  1 
ATOM   9688  N N    . ALA B 1 306  ? 124.697 133.518 133.174 1.00 3.31  ?  306  ALA B N    1 
ATOM   9689  C CA   . ALA B 1 306  ? 125.034 134.284 134.368 1.00 0.00  ?  306  ALA B CA   1 
ATOM   9690  C C    . ALA B 1 306  ? 124.244 135.584 134.435 1.00 5.51  ?  306  ALA B C    1 
ATOM   9691  O O    . ALA B 1 306  ? 123.844 136.013 135.523 1.00 5.58  ?  306  ALA B O    1 
ATOM   9692  C CB   . ALA B 1 306  ? 126.535 134.563 134.402 1.00 0.00  ?  306  ALA B CB   1 
ATOM   9693  N N    . ALA B 1 307  ? 124.009 136.224 133.285 1.00 1.61  ?  307  ALA B N    1 
ATOM   9694  C CA   . ALA B 1 307  ? 123.162 137.411 133.257 1.00 0.00  ?  307  ALA B CA   1 
ATOM   9695  C C    . ALA B 1 307  ? 121.738 137.079 133.675 1.00 0.00  ?  307  ALA B C    1 
ATOM   9696  O O    . ALA B 1 307  ? 121.108 137.841 134.419 1.00 10.30 ?  307  ALA B O    1 
ATOM   9697  C CB   . ALA B 1 307  ? 123.180 138.033 131.863 1.00 0.00  ?  307  ALA B CB   1 
ATOM   9698  N N    . THR B 1 308  ? 121.219 135.937 133.213 1.00 4.60  ?  308  THR B N    1 
ATOM   9699  C CA   . THR B 1 308  ? 119.888 135.496 133.624 1.00 0.00  ?  308  THR B CA   1 
ATOM   9700  C C    . THR B 1 308  ? 119.814 135.291 135.134 1.00 0.00  ?  308  THR B C    1 
ATOM   9701  O O    . THR B 1 308  ? 118.886 135.782 135.796 1.00 0.00  ?  308  THR B O    1 
ATOM   9702  C CB   . THR B 1 308  ? 119.518 134.203 132.897 1.00 0.00  ?  308  THR B CB   1 
ATOM   9703  O OG1  . THR B 1 308  ? 119.726 134.365 131.489 1.00 4.64  ?  308  THR B OG1  1 
ATOM   9704  C CG2  . THR B 1 308  ? 118.069 133.849 133.151 1.00 0.00  ?  308  THR B CG2  1 
ATOM   9705  N N    . TYR B 1 309  ? 120.800 134.585 135.700 1.00 6.50  ?  309  TYR B N    1 
ATOM   9706  C CA   . TYR B 1 309  ? 120.791 134.355 137.143 1.00 0.00  ?  309  TYR B CA   1 
ATOM   9707  C C    . TYR B 1 309  ? 120.922 135.652 137.928 1.00 0.00  ?  309  TYR B C    1 
ATOM   9708  O O    . TYR B 1 309  ? 120.261 135.820 138.956 1.00 11.31 ?  309  TYR B O    1 
ATOM   9709  C CB   . TYR B 1 309  ? 121.897 133.394 137.574 1.00 0.00  ?  309  TYR B CB   1 
ATOM   9710  C CG   . TYR B 1 309  ? 121.932 133.254 139.085 1.00 0.00  ?  309  TYR B CG   1 
ATOM   9711  C CD1  . TYR B 1 309  ? 120.940 132.556 139.760 1.00 0.00  ?  309  TYR B CD1  1 
ATOM   9712  C CD2  . TYR B 1 309  ? 122.934 133.857 139.839 1.00 0.00  ?  309  TYR B CD2  1 
ATOM   9713  C CE1  . TYR B 1 309  ? 120.954 132.445 141.137 1.00 0.00  ?  309  TYR B CE1  1 
ATOM   9714  C CE2  . TYR B 1 309  ? 122.954 133.752 141.217 1.00 0.00  ?  309  TYR B CE2  1 
ATOM   9715  C CZ   . TYR B 1 309  ? 121.962 133.044 141.860 1.00 0.00  ?  309  TYR B CZ   1 
ATOM   9716  O OH   . TYR B 1 309  ? 121.976 132.931 143.230 1.00 0.00  ?  309  TYR B OH   1 
ATOM   9717  N N    . LEU B 1 310  ? 121.785 136.567 137.490 1.00 0.00  ?  310  LEU B N    1 
ATOM   9718  C CA   . LEU B 1 310  ? 121.995 137.781 138.271 1.00 0.00  ?  310  LEU B CA   1 
ATOM   9719  C C    . LEU B 1 310  ? 120.785 138.702 138.196 1.00 0.00  ?  310  LEU B C    1 
ATOM   9720  O O    . LEU B 1 310  ? 120.423 139.340 139.194 1.00 5.09  ?  310  LEU B O    1 
ATOM   9721  C CB   . LEU B 1 310  ? 123.263 138.491 137.806 1.00 0.00  ?  310  LEU B CB   1 
ATOM   9722  C CG   . LEU B 1 310  ? 124.540 137.786 138.274 1.00 0.00  ?  310  LEU B CG   1 
ATOM   9723  C CD1  . LEU B 1 310  ? 125.761 138.279 137.513 1.00 0.12  ?  310  LEU B CD1  1 
ATOM   9724  C CD2  . LEU B 1 310  ? 124.726 137.952 139.774 1.00 0.00  ?  310  LEU B CD2  1 
ATOM   9725  N N    . THR B 1 311  ? 120.130 138.762 137.031 1.00 2.53  ?  311  THR B N    1 
ATOM   9726  C CA   . THR B 1 311  ? 118.863 139.477 136.927 1.00 0.00  ?  311  THR B CA   1 
ATOM   9727  C C    . THR B 1 311  ? 117.834 138.895 137.884 1.00 0.66  ?  311  THR B C    1 
ATOM   9728  O O    . THR B 1 311  ? 117.184 139.633 138.640 1.00 11.90 ?  311  THR B O    1 
ATOM   9729  C CB   . THR B 1 311  ? 118.346 139.411 135.492 1.00 0.00  ?  311  THR B CB   1 
ATOM   9730  O OG1  . THR B 1 311  ? 119.446 139.525 134.585 1.00 3.18  ?  311  THR B OG1  1 
ATOM   9731  C CG2  . THR B 1 311  ? 117.366 140.539 135.230 1.00 3.78  ?  311  THR B CG2  1 
ATOM   9732  N N    . TYR B 1 312  ? 117.699 137.563 137.889 1.00 7.87  ?  312  TYR B N    1 
ATOM   9733  C CA   . TYR B 1 312  ? 116.743 136.920 138.785 1.00 3.82  ?  312  TYR B CA   1 
ATOM   9734  C C    . TYR B 1 312  ? 117.075 137.193 140.246 1.00 0.00  ?  312  TYR B C    1 
ATOM   9735  O O    . TYR B 1 312  ? 116.178 137.455 141.047 1.00 0.63  ?  312  TYR B O    1 
ATOM   9736  C CB   . TYR B 1 312  ? 116.697 135.414 138.528 1.00 0.00  ?  312  TYR B CB   1 
ATOM   9737  C CG   . TYR B 1 312  ? 116.232 134.619 139.731 1.00 3.24  ?  312  TYR B CG   1 
ATOM   9738  C CD1  . TYR B 1 312  ? 114.891 134.601 140.098 1.00 4.53  ?  312  TYR B CD1  1 
ATOM   9739  C CD2  . TYR B 1 312  ? 117.133 133.890 140.500 1.00 2.75  ?  312  TYR B CD2  1 
ATOM   9740  C CE1  . TYR B 1 312  ? 114.463 133.884 141.198 1.00 3.62  ?  312  TYR B CE1  1 
ATOM   9741  C CE2  . TYR B 1 312  ? 116.713 133.172 141.601 1.00 0.00  ?  312  TYR B CE2  1 
ATOM   9742  C CZ   . TYR B 1 312  ? 115.379 133.172 141.944 1.00 0.00  ?  312  TYR B CZ   1 
ATOM   9743  O OH   . TYR B 1 312  ? 114.957 132.453 143.037 1.00 4.27  ?  312  TYR B OH   1 
ATOM   9744  N N    . TYR B 1 313  ? 118.357 137.142 140.608 1.00 1.61  ?  313  TYR B N    1 
ATOM   9745  C CA   . TYR B 1 313  ? 118.752 137.286 142.007 1.00 0.00  ?  313  TYR B CA   1 
ATOM   9746  C C    . TYR B 1 313  ? 118.509 138.702 142.512 1.00 0.00  ?  313  TYR B C    1 
ATOM   9747  O O    . TYR B 1 313  ? 117.965 138.898 143.609 1.00 5.81  ?  313  TYR B O    1 
ATOM   9748  C CB   . TYR B 1 313  ? 120.222 136.900 142.168 1.00 0.00  ?  313  TYR B CB   1 
ATOM   9749  C CG   . TYR B 1 313  ? 120.770 137.080 143.565 1.00 2.58  ?  313  TYR B CG   1 
ATOM   9750  C CD1  . TYR B 1 313  ? 120.410 136.215 144.588 1.00 0.00  ?  313  TYR B CD1  1 
ATOM   9751  C CD2  . TYR B 1 313  ? 121.656 138.107 143.859 1.00 2.44  ?  313  TYR B CD2  1 
ATOM   9752  C CE1  . TYR B 1 313  ? 120.912 136.370 145.865 1.00 0.00  ?  313  TYR B CE1  1 
ATOM   9753  C CE2  . TYR B 1 313  ? 122.161 138.272 145.134 1.00 0.00  ?  313  TYR B CE2  1 
ATOM   9754  C CZ   . TYR B 1 313  ? 121.786 137.401 146.132 1.00 0.00  ?  313  TYR B CZ   1 
ATOM   9755  O OH   . TYR B 1 313  ? 122.287 137.559 147.403 1.00 0.19  ?  313  TYR B OH   1 
ATOM   9756  N N    . ILE B 1 314  ? 118.908 139.707 141.726 1.00 6.71  ?  314  ILE B N    1 
ATOM   9757  C CA   . ILE B 1 314  ? 118.711 141.090 142.150 1.00 0.78  ?  314  ILE B CA   1 
ATOM   9758  C C    . ILE B 1 314  ? 117.227 141.436 142.180 1.00 0.00  ?  314  ILE B C    1 
ATOM   9759  O O    . ILE B 1 314  ? 116.767 142.166 143.066 1.00 0.00  ?  314  ILE B O    1 
ATOM   9760  C CB   . ILE B 1 314  ? 119.513 142.049 141.251 1.00 0.00  ?  314  ILE B CB   1 
ATOM   9761  C CG1  . ILE B 1 314  ? 121.000 141.696 141.297 1.00 0.06  ?  314  ILE B CG1  1 
ATOM   9762  C CG2  . ILE B 1 314  ? 119.315 143.493 141.685 1.00 3.39  ?  314  ILE B CG2  1 
ATOM   9763  C CD1  . ILE B 1 314  ? 121.652 141.963 142.634 1.00 0.37  ?  314  ILE B CD1  1 
ATOM   9764  N N    . GLY B 1 315  ? 116.446 140.910 141.232 1.00 8.16  ?  315  GLY B N    1 
ATOM   9765  C CA   . GLY B 1 315  ? 115.006 141.094 141.308 1.00 1.23  ?  315  GLY B CA   1 
ATOM   9766  C C    . GLY B 1 315  ? 114.377 140.371 142.486 1.00 1.93  ?  315  GLY B C    1 
ATOM   9767  O O    . GLY B 1 315  ? 113.412 140.855 143.078 1.00 4.56  ?  315  GLY B O    1 
ATOM   9768  N N    . ASP B 1 316  ? 114.915 139.203 142.840 1.00 4.66  ?  316  ASP B N    1 
ATOM   9769  C CA   . ASP B 1 316  ? 114.296 138.352 143.849 1.00 2.93  ?  316  ASP B CA   1 
ATOM   9770  C C    . ASP B 1 316  ? 114.526 138.891 145.253 1.00 6.14  ?  316  ASP B C    1 
ATOM   9771  O O    . ASP B 1 316  ? 113.619 138.876 146.092 1.00 11.36 ?  316  ASP B O    1 
ATOM   9772  C CB   . ASP B 1 316  ? 114.838 136.927 143.720 1.00 2.34  ?  316  ASP B CB   1 
ATOM   9773  C CG   . ASP B 1 316  ? 114.625 136.106 144.974 1.00 6.55  ?  316  ASP B CG   1 
ATOM   9774  O OD1  . ASP B 1 316  ? 113.483 135.657 145.202 1.00 10.04 ?  316  ASP B OD1  1 
ATOM   9775  O OD2  . ASP B 1 316  ? 115.597 135.911 145.733 1.00 7.05  ?  316  ASP B OD2  1 
ATOM   9776  N N    . ILE B 1 317  ? 115.741 139.365 145.539 1.00 7.37  ?  317  ILE B N    1 
ATOM   9777  C CA   . ILE B 1 317  ? 116.027 139.867 146.878 1.00 5.02  ?  317  ILE B CA   1 
ATOM   9778  C C    . ILE B 1 317  ? 115.351 141.201 147.163 1.00 8.16  ?  317  ILE B C    1 
ATOM   9779  O O    . ILE B 1 317  ? 115.386 141.672 148.303 1.00 12.07 ?  317  ILE B O    1 
ATOM   9780  C CB   . ILE B 1 317  ? 117.548 139.996 147.120 1.00 0.32  ?  317  ILE B CB   1 
ATOM   9781  C CG1  . ILE B 1 317  ? 118.129 141.150 146.303 1.00 0.00  ?  317  ILE B CG1  1 
ATOM   9782  C CG2  . ILE B 1 317  ? 118.252 138.679 146.830 1.00 6.55  ?  317  ILE B CG2  1 
ATOM   9783  C CD1  . ILE B 1 317  ? 119.456 141.647 146.821 1.00 0.00  ?  317  ILE B CD1  1 
ATOM   9784  N N    . TRP B 1 318  ? 114.730 141.814 146.160 1.00 7.46  ?  318  TRP B N    1 
ATOM   9785  C CA   . TRP B 1 318  ? 114.169 143.155 146.261 1.00 4.23  ?  318  TRP B CA   1 
ATOM   9786  C C    . TRP B 1 318  ? 112.659 143.191 146.073 1.00 7.72  ?  318  TRP B C    1 
ATOM   9787  O O    . TRP B 1 318  ? 111.970 143.882 146.826 1.00 11.54 ?  318  TRP B O    1 
ATOM   9788  C CB   . TRP B 1 318  ? 114.863 144.059 145.231 1.00 4.68  ?  318  TRP B CB   1 
ATOM   9789  C CG   . TRP B 1 318  ? 114.194 145.354 144.850 1.00 4.39  ?  318  TRP B CG   1 
ATOM   9790  C CD1  . TRP B 1 318  ? 113.526 146.222 145.667 1.00 6.56  ?  318  TRP B CD1  1 
ATOM   9791  C CD2  . TRP B 1 318  ? 114.172 145.939 143.544 1.00 6.36  ?  318  TRP B CD2  1 
ATOM   9792  N NE1  . TRP B 1 318  ? 113.074 147.298 144.945 1.00 6.20  ?  318  TRP B NE1  1 
ATOM   9793  C CE2  . TRP B 1 318  ? 113.459 147.149 143.639 1.00 3.07  ?  318  TRP B CE2  1 
ATOM   9794  C CE3  . TRP B 1 318  ? 114.679 145.552 142.300 1.00 10.74 ?  318  TRP B CE3  1 
ATOM   9795  C CZ2  . TRP B 1 318  ? 113.242 147.974 142.540 1.00 5.64  ?  318  TRP B CZ2  1 
ATOM   9796  C CZ3  . TRP B 1 318  ? 114.462 146.370 141.212 1.00 9.07  ?  318  TRP B CZ3  1 
ATOM   9797  C CH2  . TRP B 1 318  ? 113.751 147.568 141.338 1.00 7.58  ?  318  TRP B CH2  1 
ATOM   9798  N N    . LEU B 1 319  ? 112.115 142.453 145.105 1.00 8.47  ?  319  LEU B N    1 
ATOM   9799  C CA   . LEU B 1 319  ? 110.684 142.474 144.822 1.00 7.59  ?  319  LEU B CA   1 
ATOM   9800  C C    . LEU B 1 319  ? 110.017 141.139 145.141 1.00 9.82  ?  319  LEU B C    1 
ATOM   9801  O O    . LEU B 1 319  ? 108.829 140.958 144.866 1.00 11.43 ?  319  LEU B O    1 
ATOM   9802  C CB   . LEU B 1 319  ? 110.429 142.858 143.365 1.00 8.66  ?  319  LEU B CB   1 
ATOM   9803  C CG   . LEU B 1 319  ? 111.140 144.098 142.822 1.00 8.82  ?  319  LEU B CG   1 
ATOM   9804  C CD1  . LEU B 1 319  ? 111.500 143.909 141.358 1.00 6.33  ?  319  LEU B CD1  1 
ATOM   9805  C CD2  . LEU B 1 319  ? 110.278 145.334 143.010 1.00 13.81 ?  319  LEU B CD2  1 
ATOM   9806  N N    . GLU B 1 320  ? 110.766 140.212 145.746 1.00 10.55 ?  320  GLU B N    1 
ATOM   9807  C CA   . GLU B 1 320  ? 110.317 138.846 146.080 1.00 8.54  ?  320  GLU B CA   1 
ATOM   9808  C C    . GLU B 1 320  ? 109.818 138.167 144.803 1.00 7.87  ?  320  GLU B C    1 
ATOM   9809  O O    . GLU B 1 320  ? 110.520 138.205 143.783 1.00 9.09  ?  320  GLU B O    1 
ATOM   9810  C CB   . GLU B 1 320  ? 109.313 138.907 147.227 1.00 13.37 ?  320  GLU B CB   1 
ATOM   9811  C CG   . GLU B 1 320  ? 109.885 139.350 148.573 1.00 11.63 ?  320  GLU B CG   1 
ATOM   9812  C CD   . GLU B 1 320  ? 111.191 138.660 148.936 1.00 15.10 ?  320  GLU B CD   1 
ATOM   9813  O OE1  . GLU B 1 320  ? 111.299 137.428 148.745 1.00 12.06 ?  320  GLU B OE1  1 
ATOM   9814  O OE2  . GLU B 1 320  ? 112.112 139.350 149.421 1.00 15.18 ?  320  GLU B OE2  1 
ATOM   9815  N N    . VAL B 1 321  ? 108.640 137.543 144.808 1.00 7.50  ?  321  VAL B N    1 
ATOM   9816  C CA   . VAL B 1 321  ? 108.161 136.822 143.632 1.00 8.03  ?  321  VAL B CA   1 
ATOM   9817  C C    . VAL B 1 321  ? 107.520 137.759 142.611 1.00 9.95  ?  321  VAL B C    1 
ATOM   9818  O O    . VAL B 1 321  ? 107.428 137.405 141.426 1.00 10.74 ?  321  VAL B O    1 
ATOM   9819  C CB   . VAL B 1 321  ? 107.187 135.711 144.069 1.00 4.54  ?  321  VAL B CB   1 
ATOM   9820  C CG1  . VAL B 1 321  ? 106.877 134.742 142.927 1.00 10.28 ?  321  VAL B CG1  1 
ATOM   9821  C CG2  . VAL B 1 321  ? 107.743 134.966 145.268 1.00 7.47  ?  321  VAL B CG2  1 
ATOM   9822  N N    . SER B 1 322  ? 107.122 138.965 143.021 1.00 9.79  ?  322  SER B N    1 
ATOM   9823  C CA   . SER B 1 322  ? 106.620 139.950 142.070 1.00 4.53  ?  322  SER B CA   1 
ATOM   9824  C C    . SER B 1 322  ? 107.711 140.466 141.140 1.00 6.86  ?  322  SER B C    1 
ATOM   9825  O O    . SER B 1 322  ? 107.401 141.162 140.168 1.00 9.92  ?  322  SER B O    1 
ATOM   9826  C CB   . SER B 1 322  ? 105.975 141.122 142.810 1.00 9.03  ?  322  SER B CB   1 
ATOM   9827  O OG   . SER B 1 322  ? 105.046 140.669 143.778 1.00 7.69  ?  322  SER B OG   1 
ATOM   9828  N N    . GLY B 1 323  ? 108.975 140.154 141.419 1.00 6.42  ?  323  GLY B N    1 
ATOM   9829  C CA   . GLY B 1 323  ? 110.067 140.552 140.557 1.00 5.30  ?  323  GLY B CA   1 
ATOM   9830  C C    . GLY B 1 323  ? 110.391 139.537 139.481 1.00 6.66  ?  323  GLY B C    1 
ATOM   9831  O O    . GLY B 1 323  ? 111.553 139.386 139.093 1.00 8.97  ?  323  GLY B O    1 
ATOM   9832  N N    . VAL B 1 324  ? 109.372 138.819 138.999 1.00 8.72  ?  324  VAL B N    1 
ATOM   9833  C CA   . VAL B 1 324  ? 109.550 137.961 137.830 1.00 5.06  ?  324  VAL B CA   1 
ATOM   9834  C C    . VAL B 1 324  ? 109.479 138.743 136.532 1.00 7.24  ?  324  VAL B C    1 
ATOM   9835  O O    . VAL B 1 324  ? 110.144 138.361 135.559 1.00 12.08 ?  324  VAL B O    1 
ATOM   9836  C CB   . VAL B 1 324  ? 108.510 136.825 137.795 1.00 7.29  ?  324  VAL B CB   1 
ATOM   9837  C CG1  . VAL B 1 324  ? 108.830 135.781 138.850 1.00 8.52  ?  324  VAL B CG1  1 
ATOM   9838  C CG2  . VAL B 1 324  ? 107.103 137.373 138.000 1.00 4.80  ?  324  VAL B CG2  1 
ATOM   9839  N N    . LEU B 1 325  ? 108.725 139.852 136.513 1.00 6.61  ?  325  LEU B N    1 
ATOM   9840  C CA   . LEU B 1 325  ? 108.550 140.653 135.305 1.00 0.00  ?  325  LEU B CA   1 
ATOM   9841  C C    . LEU B 1 325  ? 109.886 141.055 134.703 1.00 0.00  ?  325  LEU B C    1 
ATOM   9842  O O    . LEU B 1 325  ? 110.060 140.981 133.479 1.00 3.16  ?  325  LEU B O    1 
ATOM   9843  C CB   . LEU B 1 325  ? 107.728 141.901 135.626 1.00 0.44  ?  325  LEU B CB   1 
ATOM   9844  C CG   . LEU B 1 325  ? 106.266 141.700 136.028 1.00 0.00  ?  325  LEU B CG   1 
ATOM   9845  C CD1  . LEU B 1 325  ? 105.528 143.030 136.051 1.00 0.91  ?  325  LEU B CD1  1 
ATOM   9846  C CD2  . LEU B 1 325  ? 105.579 140.717 135.098 1.00 4.21  ?  325  LEU B CD2  1 
ATOM   9847  N N    . ALA B 1 326  ? 110.849 141.412 135.559 1.00 0.00  ?  326  ALA B N    1 
ATOM   9848  C CA   . ALA B 1 326  ? 112.188 141.774 135.109 1.00 0.00  ?  326  ALA B CA   1 
ATOM   9849  C C    . ALA B 1 326  ? 112.783 140.690 134.226 1.00 2.35  ?  326  ALA B C    1 
ATOM   9850  O O    . ALA B 1 326  ? 113.147 140.951 133.070 1.00 3.34  ?  326  ALA B O    1 
ATOM   9851  C CB   . ALA B 1 326  ? 113.089 142.020 136.317 1.00 2.45  ?  326  ALA B CB   1 
ATOM   9852  N N    . VAL B 1 327  ? 112.806 139.447 134.718 1.00 1.96  ?  327  VAL B N    1 
ATOM   9853  C CA   . VAL B 1 327  ? 113.443 138.401 133.930 1.00 2.91  ?  327  VAL B CA   1 
ATOM   9854  C C    . VAL B 1 327  ? 112.625 138.147 132.672 1.00 3.40  ?  327  VAL B C    1 
ATOM   9855  O O    . VAL B 1 327  ? 113.198 137.890 131.603 1.00 5.98  ?  327  VAL B O    1 
ATOM   9856  C CB   . VAL B 1 327  ? 113.677 137.122 134.766 1.00 0.00  ?  327  VAL B CB   1 
ATOM   9857  C CG1  . VAL B 1 327  ? 112.421 136.270 134.915 1.00 1.42  ?  327  VAL B CG1  1 
ATOM   9858  C CG2  . VAL B 1 327  ? 114.819 136.307 134.184 1.00 0.00  ?  327  VAL B CG2  1 
ATOM   9859  N N    . VAL B 1 328  ? 111.301 138.342 132.754 1.00 0.00  ?  328  VAL B N    1 
ATOM   9860  C CA   . VAL B 1 328  ? 110.443 138.208 131.582 1.00 0.00  ?  328  VAL B CA   1 
ATOM   9861  C C    . VAL B 1 328  ? 110.891 139.180 130.507 1.00 0.74  ?  328  VAL B C    1 
ATOM   9862  O O    . VAL B 1 328  ? 111.111 138.797 129.349 1.00 3.86  ?  328  VAL B O    1 
ATOM   9863  C CB   . VAL B 1 328  ? 108.972 138.443 131.968 1.00 0.00  ?  328  VAL B CB   1 
ATOM   9864  C CG1  . VAL B 1 328  ? 108.136 138.770 130.739 1.00 0.00  ?  328  VAL B CG1  1 
ATOM   9865  C CG2  . VAL B 1 328  ? 108.424 137.249 132.701 1.00 1.76  ?  328  VAL B CG2  1 
ATOM   9866  N N    . VAL B 1 329  ? 111.119 140.437 130.906 1.00 3.55  ?  329  VAL B N    1 
ATOM   9867  C CA   . VAL B 1 329  ? 111.572 141.452 129.965 1.00 0.76  ?  329  VAL B CA   1 
ATOM   9868  C C    . VAL B 1 329  ? 112.891 141.028 129.347 1.00 0.00  ?  329  VAL B C    1 
ATOM   9869  O O    . VAL B 1 329  ? 113.067 141.092 128.122 1.00 0.27  ?  329  VAL B O    1 
ATOM   9870  C CB   . VAL B 1 329  ? 111.682 142.817 130.668 1.00 0.00  ?  329  VAL B CB   1 
ATOM   9871  C CG1  . VAL B 1 329  ? 112.435 143.804 129.801 1.00 2.64  ?  329  VAL B CG1  1 
ATOM   9872  C CG2  . VAL B 1 329  ? 110.302 143.344 131.013 1.00 0.00  ?  329  VAL B CG2  1 
ATOM   9873  N N    . LEU B 1 330  ? 113.800 140.498 130.176 1.00 0.86  ?  330  LEU B N    1 
ATOM   9874  C CA   . LEU B 1 330  ? 115.080 140.029 129.662 1.00 2.96  ?  330  LEU B CA   1 
ATOM   9875  C C    . LEU B 1 330  ? 114.865 138.945 128.622 1.00 0.00  ?  330  LEU B C    1 
ATOM   9876  O O    . LEU B 1 330  ? 115.406 139.026 127.510 1.00 2.58  ?  330  LEU B O    1 
ATOM   9877  C CB   . LEU B 1 330  ? 115.947 139.520 130.814 1.00 0.00  ?  330  LEU B CB   1 
ATOM   9878  C CG   . LEU B 1 330  ? 117.366 139.045 130.496 1.00 0.00  ?  330  LEU B CG   1 
ATOM   9879  C CD1  . LEU B 1 330  ? 118.352 139.661 131.466 1.00 0.00  ?  330  LEU B CD1  1 
ATOM   9880  C CD2  . LEU B 1 330  ? 117.460 137.528 130.543 1.00 2.87  ?  330  LEU B CD2  1 
ATOM   9881  N N    . GLY B 1 331  ? 113.977 137.992 128.927 1.00 0.00  ?  331  GLY B N    1 
ATOM   9882  C CA   . GLY B 1 331  ? 113.711 136.909 127.999 1.00 2.88  ?  331  GLY B CA   1 
ATOM   9883  C C    . GLY B 1 331  ? 113.156 137.406 126.683 1.00 0.00  ?  331  GLY B C    1 
ATOM   9884  O O    . GLY B 1 331  ? 113.394 136.807 125.633 1.00 3.00  ?  331  GLY B O    1 
ATOM   9885  N N    . LEU B 1 332  ? 112.412 138.514 126.718 1.00 2.69  ?  332  LEU B N    1 
ATOM   9886  C CA   . LEU B 1 332  ? 111.952 139.094 125.466 1.00 0.00  ?  332  LEU B CA   1 
ATOM   9887  C C    . LEU B 1 332  ? 113.091 139.799 124.743 1.00 0.00  ?  332  LEU B C    1 
ATOM   9888  O O    . LEU B 1 332  ? 113.323 139.552 123.552 1.00 6.25  ?  332  LEU B O    1 
ATOM   9889  C CB   . LEU B 1 332  ? 110.789 140.051 125.722 1.00 0.00  ?  332  LEU B CB   1 
ATOM   9890  C CG   . LEU B 1 332  ? 109.562 139.426 126.391 1.00 0.00  ?  332  LEU B CG   1 
ATOM   9891  C CD1  . LEU B 1 332  ? 108.575 140.497 126.828 1.00 0.20  ?  332  LEU B CD1  1 
ATOM   9892  C CD2  . LEU B 1 332  ? 108.895 138.417 125.475 1.00 0.30  ?  332  LEU B CD2  1 
ATOM   9893  N N    . ILE B 1 333  ? 113.855 140.629 125.461 1.00 2.22  ?  333  ILE B N    1 
ATOM   9894  C CA   . ILE B 1 333  ? 114.770 141.546 124.786 1.00 0.00  ?  333  ILE B CA   1 
ATOM   9895  C C    . ILE B 1 333  ? 115.920 140.779 124.154 1.00 0.00  ?  333  ILE B C    1 
ATOM   9896  O O    . ILE B 1 333  ? 116.264 140.999 122.985 1.00 10.73 ?  333  ILE B O    1 
ATOM   9897  C CB   . ILE B 1 333  ? 115.271 142.627 125.761 1.00 0.00  ?  333  ILE B CB   1 
ATOM   9898  C CG1  . ILE B 1 333  ? 114.110 143.509 126.225 1.00 0.00  ?  333  ILE B CG1  1 
ATOM   9899  C CG2  . ILE B 1 333  ? 116.337 143.484 125.101 1.00 0.73  ?  333  ILE B CG2  1 
ATOM   9900  C CD1  . ILE B 1 333  ? 113.492 144.346 125.129 1.00 1.20  ?  333  ILE B CD1  1 
ATOM   9901  N N    . VAL B 1 334  ? 116.494 139.832 124.898 1.00 0.31  ?  334  VAL B N    1 
ATOM   9902  C CA   . VAL B 1 334  ? 117.530 138.960 124.360 1.00 0.37  ?  334  VAL B CA   1 
ATOM   9903  C C    . VAL B 1 334  ? 116.994 138.168 123.172 1.00 5.33  ?  334  VAL B C    1 
ATOM   9904  O O    . VAL B 1 334  ? 117.717 137.911 122.201 1.00 10.48 ?  334  VAL B O    1 
ATOM   9905  C CB   . VAL B 1 334  ? 118.067 138.050 125.482 1.00 1.82  ?  334  VAL B CB   1 
ATOM   9906  C CG1  . VAL B 1 334  ? 118.817 136.843 124.930 1.00 1.69  ?  334  VAL B CG1  1 
ATOM   9907  C CG2  . VAL B 1 334  ? 118.957 138.849 126.421 1.00 2.00  ?  334  VAL B CG2  1 
ATOM   9908  N N    . ASN B 1 335  ? 115.705 137.814 123.202 1.00 8.57  ?  335  ASN B N    1 
ATOM   9909  C CA   . ASN B 1 335  ? 115.126 137.108 122.065 1.00 9.71  ?  335  ASN B CA   1 
ATOM   9910  C C    . ASN B 1 335  ? 114.988 138.026 120.858 1.00 11.85 ?  335  ASN B C    1 
ATOM   9911  O O    . ASN B 1 335  ? 115.102 137.575 119.713 1.00 13.36 ?  335  ASN B O    1 
ATOM   9912  C CB   . ASN B 1 335  ? 113.771 136.515 122.440 1.00 8.56  ?  335  ASN B CB   1 
ATOM   9913  C CG   . ASN B 1 335  ? 113.437 135.282 121.632 1.00 8.57  ?  335  ASN B CG   1 
ATOM   9914  O OD1  . ASN B 1 335  ? 112.524 135.295 120.810 1.00 15.06 ?  335  ASN B OD1  1 
ATOM   9915  N ND2  . ASN B 1 335  ? 114.175 134.204 121.865 1.00 5.95  ?  335  ASN B ND2  1 
ATOM   9916  N N    . ALA B 1 336  ? 114.734 139.317 121.091 1.00 12.04 ?  336  ALA B N    1 
ATOM   9917  C CA   . ALA B 1 336  ? 114.591 140.244 119.974 1.00 10.26 ?  336  ALA B CA   1 
ATOM   9918  C C    . ALA B 1 336  ? 115.931 140.496 119.296 1.00 15.78 ?  336  ALA B C    1 
ATOM   9919  O O    . ALA B 1 336  ? 116.007 140.584 118.065 1.00 15.03 ?  336  ALA B O    1 
ATOM   9920  C CB   . ALA B 1 336  ? 113.970 141.555 120.453 1.00 9.25  ?  336  ALA B CB   1 
ATOM   9921  N N    . GLU B 1 337  ? 116.999 140.608 120.083 1.00 19.86 ?  337  GLU B N    1 
ATOM   9922  C CA   . GLU B 1 337  ? 118.338 140.852 119.548 1.00 15.08 ?  337  GLU B CA   1 
ATOM   9923  C C    . GLU B 1 337  ? 119.082 139.523 119.408 1.00 12.21 ?  337  GLU B C    1 
ATOM   9924  O O    . GLU B 1 337  ? 120.046 139.223 120.113 1.00 13.23 ?  337  GLU B O    1 
ATOM   9925  C CB   . GLU B 1 337  ? 119.089 141.833 120.438 1.00 13.19 ?  337  GLU B CB   1 
ATOM   9926  C CG   . GLU B 1 337  ? 118.880 143.294 120.065 1.00 16.98 ?  337  GLU B CG   1 
ATOM   9927  C CD   . GLU B 1 337  ? 117.693 143.926 120.773 1.00 19.09 ?  337  GLU B CD   1 
ATOM   9928  O OE1  . GLU B 1 337  ? 116.759 143.194 121.158 1.00 18.76 ?  337  GLU B OE1  1 
ATOM   9929  O OE2  . GLU B 1 337  ? 117.692 145.163 120.939 1.00 19.44 ?  337  GLU B OE2  1 
ATOM   9930  N N    . LYS B 1 338  ? 118.602 138.717 118.463 1.00 12.00 ?  338  LYS B N    1 
ATOM   9931  C CA   . LYS B 1 338  ? 119.185 137.411 118.191 1.00 12.41 ?  338  LYS B CA   1 
ATOM   9932  C C    . LYS B 1 338  ? 120.351 137.468 117.212 1.00 13.30 ?  338  LYS B C    1 
ATOM   9933  O O    . LYS B 1 338  ? 121.042 136.458 117.040 1.00 9.65  ?  338  LYS B O    1 
ATOM   9934  C CB   . LYS B 1 338  ? 118.115 136.459 117.645 1.00 12.74 ?  338  LYS B CB   1 
ATOM   9935  C CG   . LYS B 1 338  ? 117.641 135.407 118.635 1.00 12.81 ?  338  LYS B CG   1 
ATOM   9936  C CD   . LYS B 1 338  ? 116.820 134.333 117.937 1.00 12.93 ?  338  LYS B CD   1 
ATOM   9937  C CE   . LYS B 1 338  ? 116.319 133.290 118.922 1.00 14.84 ?  338  LYS B CE   1 
ATOM   9938  N NZ   . LYS B 1 338  ? 116.008 131.997 118.252 1.00 14.64 ?  338  LYS B NZ   1 
ATOM   9939  N N    . THR B 1 339  ? 120.587 138.613 116.569 1.00 16.62 ?  339  THR B N    1 
ATOM   9940  C CA   . THR B 1 339  ? 121.677 138.720 115.607 1.00 12.38 ?  339  THR B CA   1 
ATOM   9941  C C    . THR B 1 339  ? 123.041 138.857 116.271 1.00 13.05 ?  339  THR B C    1 
ATOM   9942  O O    . THR B 1 339  ? 124.060 138.624 115.612 1.00 13.59 ?  339  THR B O    1 
ATOM   9943  C CB   . THR B 1 339  ? 121.440 139.900 114.660 1.00 11.18 ?  339  THR B CB   1 
ATOM   9944  O OG1  . THR B 1 339  ? 122.418 139.878 113.612 1.00 14.08 ?  339  THR B OG1  1 
ATOM   9945  C CG2  . THR B 1 339  ? 121.525 141.225 115.406 1.00 14.03 ?  339  THR B CG2  1 
ATOM   9946  N N    . SER B 1 340  ? 123.087 139.221 117.549 1.00 14.17 ?  340  SER B N    1 
ATOM   9947  C CA   . SER B 1 340  ? 124.333 139.243 118.302 1.00 13.09 ?  340  SER B CA   1 
ATOM   9948  C C    . SER B 1 340  ? 124.657 137.892 118.919 1.00 10.16 ?  340  SER B C    1 
ATOM   9949  O O    . SER B 1 340  ? 125.677 137.764 119.602 1.00 13.26 ?  340  SER B O    1 
ATOM   9950  C CB   . SER B 1 340  ? 124.269 140.298 119.407 1.00 11.90 ?  340  SER B CB   1 
ATOM   9951  O OG   . SER B 1 340  ? 123.785 139.720 120.605 1.00 8.41  ?  340  SER B OG   1 
ATOM   9952  N N    . ILE B 1 341  ? 123.809 136.893 118.699 1.00 10.52 ?  341  ILE B N    1 
ATOM   9953  C CA   . ILE B 1 341  ? 123.960 135.566 119.278 1.00 11.69 ?  341  ILE B CA   1 
ATOM   9954  C C    . ILE B 1 341  ? 124.085 134.570 118.135 1.00 15.84 ?  341  ILE B C    1 
ATOM   9955  O O    . ILE B 1 341  ? 123.264 134.576 117.210 1.00 21.30 ?  341  ILE B O    1 
ATOM   9956  C CB   . ILE B 1 341  ? 122.770 135.221 120.194 1.00 12.78 ?  341  ILE B CB   1 
ATOM   9957  C CG1  . ILE B 1 341  ? 122.804 136.078 121.460 1.00 16.08 ?  341  ILE B CG1  1 
ATOM   9958  C CG2  . ILE B 1 341  ? 122.775 133.761 120.563 1.00 7.92  ?  341  ILE B CG2  1 
ATOM   9959  C CD1  . ILE B 1 341  ? 121.518 136.040 122.257 1.00 10.73 ?  341  ILE B CD1  1 
ATOM   9960  N N    . SER B 1 342  ? 125.122 133.736 118.187 1.00 11.29 ?  342  SER B N    1 
ATOM   9961  C CA   . SER B 1 342  ? 125.337 132.740 117.149 1.00 9.79  ?  342  SER B CA   1 
ATOM   9962  C C    . SER B 1 342  ? 124.197 131.721 117.153 1.00 15.95 ?  342  SER B C    1 
ATOM   9963  O O    . SER B 1 342  ? 123.642 131.412 118.210 1.00 20.76 ?  342  SER B O    1 
ATOM   9964  C CB   . SER B 1 342  ? 126.676 132.038 117.363 1.00 11.93 ?  342  SER B CB   1 
ATOM   9965  O OG   . SER B 1 342  ? 127.670 132.957 117.782 1.00 10.12 ?  342  SER B OG   1 
ATOM   9966  N N    . PRO B 1 343  ? 123.823 131.191 115.980 1.00 14.67 ?  343  PRO B N    1 
ATOM   9967  C CA   . PRO B 1 343  ? 122.673 130.266 115.918 1.00 10.89 ?  343  PRO B CA   1 
ATOM   9968  C C    . PRO B 1 343  ? 122.843 129.009 116.757 1.00 14.25 ?  343  PRO B C    1 
ATOM   9969  O O    . PRO B 1 343  ? 121.853 128.495 117.303 1.00 18.56 ?  343  PRO B O    1 
ATOM   9970  C CB   . PRO B 1 343  ? 122.575 129.936 114.422 1.00 15.87 ?  343  PRO B CB   1 
ATOM   9971  C CG   . PRO B 1 343  ? 123.258 131.074 113.733 1.00 16.42 ?  343  PRO B CG   1 
ATOM   9972  C CD   . PRO B 1 343  ? 124.370 131.483 114.644 1.00 15.24 ?  343  PRO B CD   1 
ATOM   9973  N N    . GLU B 1 344  ? 124.075 128.507 116.881 1.00 15.90 ?  344  GLU B N    1 
ATOM   9974  C CA   . GLU B 1 344  ? 124.337 127.383 117.774 1.00 12.04 ?  344  GLU B CA   1 
ATOM   9975  C C    . GLU B 1 344  ? 124.030 127.752 119.220 1.00 11.44 ?  344  GLU B C    1 
ATOM   9976  O O    . GLU B 1 344  ? 123.480 126.940 119.977 1.00 12.66 ?  344  GLU B O    1 
ATOM   9977  C CB   . GLU B 1 344  ? 125.790 126.929 117.620 1.00 14.98 ?  344  GLU B CB   1 
ATOM   9978  C CG   . GLU B 1 344  ? 126.791 128.073 117.491 1.00 12.62 ?  344  GLU B CG   1 
ATOM   9979  C CD   . GLU B 1 344  ? 128.196 127.596 117.166 1.00 15.19 ?  344  GLU B CD   1 
ATOM   9980  O OE1  . GLU B 1 344  ? 128.462 126.384 117.305 1.00 12.09 ?  344  GLU B OE1  1 
ATOM   9981  O OE2  . GLU B 1 344  ? 129.033 128.433 116.768 1.00 17.99 ?  344  GLU B OE2  1 
ATOM   9982  N N    . VAL B 1 345  ? 124.354 128.984 119.614 1.00 9.02  ?  345  VAL B N    1 
ATOM   9983  C CA   . VAL B 1 345  ? 124.033 129.442 120.960 1.00 4.02  ?  345  VAL B CA   1 
ATOM   9984  C C    . VAL B 1 345  ? 122.523 129.533 121.148 1.00 2.33  ?  345  VAL B C    1 
ATOM   9985  O O    . VAL B 1 345  ? 121.999 129.183 122.213 1.00 12.05 ?  345  VAL B O    1 
ATOM   9986  C CB   . VAL B 1 345  ? 124.733 130.783 121.242 1.00 3.87  ?  345  VAL B CB   1 
ATOM   9987  C CG1  . VAL B 1 345  ? 124.533 131.201 122.687 1.00 4.42  ?  345  VAL B CG1  1 
ATOM   9988  C CG2  . VAL B 1 345  ? 126.209 130.690 120.904 1.00 6.15  ?  345  VAL B CG2  1 
ATOM   9989  N N    . GLU B 1 346  ? 121.797 129.984 120.117 1.00 1.08  ?  346  GLU B N    1 
ATOM   9990  C CA   . GLU B 1 346  ? 120.340 130.058 120.210 1.00 4.45  ?  346  GLU B CA   1 
ATOM   9991  C C    . GLU B 1 346  ? 119.722 128.679 120.404 1.00 2.94  ?  346  GLU B C    1 
ATOM   9992  O O    . GLU B 1 346  ? 118.859 128.493 121.273 1.00 8.51  ?  346  GLU B O    1 
ATOM   9993  C CB   . GLU B 1 346  ? 119.744 130.727 118.967 1.00 9.68  ?  346  GLU B CB   1 
ATOM   9994  C CG   . GLU B 1 346  ? 120.509 131.915 118.418 1.00 15.68 ?  346  GLU B CG   1 
ATOM   9995  C CD   . GLU B 1 346  ? 120.001 132.359 117.056 1.00 22.93 ?  346  GLU B CD   1 
ATOM   9996  O OE1  . GLU B 1 346  ? 119.119 131.675 116.496 1.00 21.26 ?  346  GLU B OE1  1 
ATOM   9997  O OE2  . GLU B 1 346  ? 120.479 133.396 116.548 1.00 19.01 ?  346  GLU B OE2  1 
ATOM   9998  N N    . VAL B 1 347  ? 120.152 127.694 119.608 1.00 4.00  ?  347  VAL B N    1 
ATOM   9999  C CA   . VAL B 1 347  ? 119.535 126.374 119.718 1.00 2.09  ?  347  VAL B CA   1 
ATOM   10000 C C    . VAL B 1 347  ? 119.906 125.715 121.045 1.00 4.02  ?  347  VAL B C    1 
ATOM   10001 O O    . VAL B 1 347  ? 119.065 125.057 121.677 1.00 9.42  ?  347  VAL B O    1 
ATOM   10002 C CB   . VAL B 1 347  ? 119.877 125.484 118.504 1.00 0.00  ?  347  VAL B CB   1 
ATOM   10003 C CG1  . VAL B 1 347  ? 119.249 126.049 117.236 1.00 10.38 ?  347  VAL B CG1  1 
ATOM   10004 C CG2  . VAL B 1 347  ? 121.365 125.295 118.325 1.00 0.01  ?  347  VAL B CG2  1 
ATOM   10005 N N    . PHE B 1 348  ? 121.147 125.915 121.515 1.00 0.00  ?  348  PHE B N    1 
ATOM   10006 C CA   . PHE B 1 348  ? 121.527 125.376 122.818 1.00 1.77  ?  348  PHE B CA   1 
ATOM   10007 C C    . PHE B 1 348  ? 120.705 125.988 123.943 1.00 2.91  ?  348  PHE B C    1 
ATOM   10008 O O    . PHE B 1 348  ? 120.222 125.271 124.824 1.00 4.35  ?  348  PHE B O    1 
ATOM   10009 C CB   . PHE B 1 348  ? 123.015 125.587 123.090 1.00 0.00  ?  348  PHE B CB   1 
ATOM   10010 C CG   . PHE B 1 348  ? 123.458 125.042 124.424 1.00 0.00  ?  348  PHE B CG   1 
ATOM   10011 C CD1  . PHE B 1 348  ? 123.653 123.684 124.608 1.00 2.22  ?  348  PHE B CD1  1 
ATOM   10012 C CD2  . PHE B 1 348  ? 123.656 125.890 125.502 1.00 0.00  ?  348  PHE B CD2  1 
ATOM   10013 C CE1  . PHE B 1 348  ? 124.044 123.190 125.837 1.00 0.00  ?  348  PHE B CE1  1 
ATOM   10014 C CE2  . PHE B 1 348  ? 124.047 125.398 126.729 1.00 0.00  ?  348  PHE B CE2  1 
ATOM   10015 C CZ   . PHE B 1 348  ? 124.242 124.048 126.896 1.00 0.00  ?  348  PHE B CZ   1 
ATOM   10016 N N    . LEU B 1 349  ? 120.541 127.315 123.939 1.00 5.92  ?  349  LEU B N    1 
ATOM   10017 C CA   . LEU B 1 349  ? 119.810 127.954 125.030 1.00 0.00  ?  349  LEU B CA   1 
ATOM   10018 C C    . LEU B 1 349  ? 118.337 127.571 125.010 1.00 0.00  ?  349  LEU B C    1 
ATOM   10019 O O    . LEU B 1 349  ? 117.732 127.352 126.070 1.00 13.42 ?  349  LEU B O    1 
ATOM   10020 C CB   . LEU B 1 349  ? 119.979 129.470 124.962 1.00 0.00  ?  349  LEU B CB   1 
ATOM   10021 C CG   . LEU B 1 349  ? 121.374 129.987 125.317 1.00 1.49  ?  349  LEU B CG   1 
ATOM   10022 C CD1  . LEU B 1 349  ? 121.524 131.443 124.912 1.00 2.04  ?  349  LEU B CD1  1 
ATOM   10023 C CD2  . LEU B 1 349  ? 121.660 129.800 126.797 1.00 0.00  ?  349  LEU B CD2  1 
ATOM   10024 N N    . HIS B 1 350  ? 117.750 127.456 123.814 1.00 2.40  ?  350  HIS B N    1 
ATOM   10025 C CA   . HIS B 1 350  ? 116.351 127.052 123.725 1.00 4.92  ?  350  HIS B CA   1 
ATOM   10026 C C    . HIS B 1 350  ? 116.146 125.628 124.231 1.00 6.74  ?  350  HIS B C    1 
ATOM   10027 O O    . HIS B 1 350  ? 115.214 125.370 125.003 1.00 4.28  ?  350  HIS B O    1 
ATOM   10028 C CB   . HIS B 1 350  ? 115.855 127.202 122.288 1.00 0.71  ?  350  HIS B CB   1 
ATOM   10029 C CG   . HIS B 1 350  ? 115.403 128.590 121.952 1.00 7.20  ?  350  HIS B CG   1 
ATOM   10030 N ND1  . HIS B 1 350  ? 116.222 129.513 121.340 1.00 14.97 ?  350  HIS B ND1  1 
ATOM   10031 C CD2  . HIS B 1 350  ? 114.218 129.213 122.152 1.00 6.38  ?  350  HIS B CD2  1 
ATOM   10032 C CE1  . HIS B 1 350  ? 115.560 130.644 121.174 1.00 8.93  ?  350  HIS B CE1  1 
ATOM   10033 N NE2  . HIS B 1 350  ? 114.341 130.488 121.658 1.00 7.46  ?  350  HIS B NE2  1 
ATOM   10034 N N    . ARG B 1 351  ? 117.023 124.695 123.838 1.00 3.72  ?  351  ARG B N    1 
ATOM   10035 C CA   . ARG B 1 351  ? 116.898 123.324 124.330 1.00 0.00  ?  351  ARG B CA   1 
ATOM   10036 C C    . ARG B 1 351  ? 117.151 123.238 125.834 1.00 0.00  ?  351  ARG B C    1 
ATOM   10037 O O    . ARG B 1 351  ? 116.479 122.473 126.539 1.00 7.82  ?  351  ARG B O    1 
ATOM   10038 C CB   . ARG B 1 351  ? 117.850 122.409 123.564 1.00 0.00  ?  351  ARG B CB   1 
ATOM   10039 C CG   . ARG B 1 351  ? 117.652 120.931 123.850 1.00 4.58  ?  351  ARG B CG   1 
ATOM   10040 C CD   . ARG B 1 351  ? 116.254 120.472 123.498 1.00 2.34  ?  351  ARG B CD   1 
ATOM   10041 N NE   . ARG B 1 351  ? 116.087 120.285 122.063 1.00 2.84  ?  351  ARG B NE   1 
ATOM   10042 C CZ   . ARG B 1 351  ? 114.914 120.239 121.448 1.00 4.55  ?  351  ARG B CZ   1 
ATOM   10043 N NH1  . ARG B 1 351  ? 113.779 120.373 122.115 1.00 2.87  ?  351  ARG B NH1  1 
ATOM   10044 N NH2  . ARG B 1 351  ? 114.879 120.053 120.132 1.00 7.69  ?  351  ARG B NH2  1 
ATOM   10045 N N    . PHE B 1 352  ? 118.102 124.030 126.339 1.00 1.60  ?  352  PHE B N    1 
ATOM   10046 C CA   . PHE B 1 352  ? 118.405 124.065 127.768 1.00 0.00  ?  352  PHE B CA   1 
ATOM   10047 C C    . PHE B 1 352  ? 117.190 124.489 128.585 1.00 0.00  ?  352  PHE B C    1 
ATOM   10048 O O    . PHE B 1 352  ? 116.787 123.803 129.539 1.00 7.25  ?  352  PHE B O    1 
ATOM   10049 C CB   . PHE B 1 352  ? 119.578 125.024 127.992 1.00 0.00  ?  352  PHE B CB   1 
ATOM   10050 C CG   . PHE B 1 352  ? 120.074 125.087 129.408 1.00 0.00  ?  352  PHE B CG   1 
ATOM   10051 C CD1  . PHE B 1 352  ? 120.992 124.165 129.876 1.00 2.99  ?  352  PHE B CD1  1 
ATOM   10052 C CD2  . PHE B 1 352  ? 119.654 126.096 130.258 1.00 0.56  ?  352  PHE B CD2  1 
ATOM   10053 C CE1  . PHE B 1 352  ? 121.458 124.231 131.172 1.00 3.00  ?  352  PHE B CE1  1 
ATOM   10054 C CE2  . PHE B 1 352  ? 120.116 126.166 131.555 1.00 0.00  ?  352  PHE B CE2  1 
ATOM   10055 C CZ   . PHE B 1 352  ? 121.020 125.233 132.012 1.00 0.00  ?  352  PHE B CZ   1 
ATOM   10056 N N    . TRP B 1 353  ? 116.575 125.614 128.209 1.00 0.00  ?  353  TRP B N    1 
ATOM   10057 C CA   . TRP B 1 353  ? 115.439 126.099 128.982 1.00 0.00  ?  353  TRP B CA   1 
ATOM   10058 C C    . TRP B 1 353  ? 114.207 125.225 128.780 1.00 1.75  ?  353  TRP B C    1 
ATOM   10059 O O    . TRP B 1 353  ? 113.399 125.079 129.708 1.00 17.39 ?  353  TRP B O    1 
ATOM   10060 C CB   . TRP B 1 353  ? 115.153 127.558 128.636 1.00 6.10  ?  353  TRP B CB   1 
ATOM   10061 C CG   . TRP B 1 353  ? 116.187 128.481 129.205 1.00 4.44  ?  353  TRP B CG   1 
ATOM   10062 C CD1  . TRP B 1 353  ? 117.160 129.146 128.522 1.00 0.97  ?  353  TRP B CD1  1 
ATOM   10063 C CD2  . TRP B 1 353  ? 116.381 128.796 130.588 1.00 9.91  ?  353  TRP B CD2  1 
ATOM   10064 N NE1  . TRP B 1 353  ? 117.932 129.877 129.390 1.00 4.88  ?  353  TRP B NE1  1 
ATOM   10065 C CE2  . TRP B 1 353  ? 117.475 129.677 130.666 1.00 10.76 ?  353  TRP B CE2  1 
ATOM   10066 C CE3  . TRP B 1 353  ? 115.727 128.428 131.767 1.00 11.67 ?  353  TRP B CE3  1 
ATOM   10067 C CZ2  . TRP B 1 353  ? 117.930 130.195 131.875 1.00 12.52 ?  353  TRP B CZ2  1 
ATOM   10068 C CZ3  . TRP B 1 353  ? 116.179 128.942 132.964 1.00 6.99  ?  353  TRP B CZ3  1 
ATOM   10069 C CH2  . TRP B 1 353  ? 117.270 129.816 133.011 1.00 7.71  ?  353  TRP B CH2  1 
ATOM   10070 N N    . GLU B 1 354  ? 114.068 124.604 127.602 1.00 5.49  ?  354  GLU B N    1 
ATOM   10071 C CA   . GLU B 1 354  ? 112.989 123.644 127.392 1.00 0.00  ?  354  GLU B CA   1 
ATOM   10072 C C    . GLU B 1 354  ? 113.118 122.450 128.329 1.00 4.67  ?  354  GLU B C    1 
ATOM   10073 O O    . GLU B 1 354  ? 112.126 122.010 128.924 1.00 14.88 ?  354  GLU B O    1 
ATOM   10074 C CB   . GLU B 1 354  ? 112.985 123.183 125.935 1.00 0.82  ?  354  GLU B CB   1 
ATOM   10075 C CG   . GLU B 1 354  ? 111.698 122.511 125.491 1.00 8.19  ?  354  GLU B CG   1 
ATOM   10076 C CD   . GLU B 1 354  ? 111.655 122.259 123.995 1.00 6.82  ?  354  GLU B CD   1 
ATOM   10077 O OE1  . GLU B 1 354  ? 112.655 122.562 123.310 1.00 1.48  ?  354  GLU B OE1  1 
ATOM   10078 O OE2  . GLU B 1 354  ? 110.623 121.756 123.505 1.00 7.84  ?  354  GLU B OE2  1 
ATOM   10079 N N    . MET B 1 355  ? 114.336 121.923 128.489 1.00 0.00  ?  355  MET B N    1 
ATOM   10080 C CA   . MET B 1 355  ? 114.540 120.783 129.380 1.00 0.00  ?  355  MET B CA   1 
ATOM   10081 C C    . MET B 1 355  ? 114.293 121.158 130.838 1.00 0.00  ?  355  MET B C    1 
ATOM   10082 O O    . MET B 1 355  ? 113.671 120.387 131.586 1.00 11.05 ?  355  MET B O    1 
ATOM   10083 C CB   . MET B 1 355  ? 115.946 120.212 129.172 1.00 9.39  ?  355  MET B CB   1 
ATOM   10084 C CG   . MET B 1 355  ? 116.634 119.662 130.414 1.00 16.78 ?  355  MET B CG   1 
ATOM   10085 S SD   . MET B 1 355  ? 118.434 119.794 130.314 1.00 6.55  ?  355  MET B SD   1 
ATOM   10086 C CE   . MET B 1 355  ? 118.739 121.330 131.175 1.00 8.92  ?  355  MET B CE   1 
ATOM   10087 N N    . LEU B 1 356  ? 114.745 122.348 131.254 1.00 2.80  ?  356  LEU B N    1 
ATOM   10088 C CA   . LEU B 1 356  ? 114.490 122.794 132.626 1.00 1.94  ?  356  LEU B CA   1 
ATOM   10089 C C    . LEU B 1 356  ? 112.993 122.925 132.906 1.00 0.00  ?  356  LEU B C    1 
ATOM   10090 O O    . LEU B 1 356  ? 112.492 122.448 133.939 1.00 5.32  ?  356  LEU B O    1 
ATOM   10091 C CB   . LEU B 1 356  ? 115.202 124.123 132.886 1.00 9.53  ?  356  LEU B CB   1 
ATOM   10092 C CG   . LEU B 1 356  ? 116.710 124.108 133.136 1.00 3.69  ?  356  LEU B CG   1 
ATOM   10093 C CD1  . LEU B 1 356  ? 117.149 125.423 133.751 1.00 7.11  ?  356  LEU B CD1  1 
ATOM   10094 C CD2  . LEU B 1 356  ? 117.083 122.956 134.049 1.00 8.67  ?  356  LEU B CD2  1 
ATOM   10095 N N    . ALA B 1 357  ? 112.256 123.550 131.980 1.00 1.62  ?  357  ALA B N    1 
ATOM   10096 C CA   . ALA B 1 357  ? 110.818 123.719 132.169 1.00 0.00  ?  357  ALA B CA   1 
ATOM   10097 C C    . ALA B 1 357  ? 110.086 122.383 132.142 1.00 1.07  ?  357  ALA B C    1 
ATOM   10098 O O    . ALA B 1 357  ? 109.100 122.198 132.865 1.00 3.29  ?  357  ALA B O    1 
ATOM   10099 C CB   . ALA B 1 357  ? 110.260 124.657 131.104 1.00 3.50  ?  357  ALA B CB   1 
ATOM   10100 N N    . TYR B 1 358  ? 110.553 121.441 131.317 1.00 10.84 ?  358  TYR B N    1 
ATOM   10101 C CA   . TYR B 1 358  ? 109.958 120.107 131.274 1.00 0.00  ?  358  TYR B CA   1 
ATOM   10102 C C    . TYR B 1 358  ? 110.102 119.388 132.610 1.00 0.00  ?  358  TYR B C    1 
ATOM   10103 O O    . TYR B 1 358  ? 109.137 118.790 133.116 1.00 8.01  ?  358  TYR B O    1 
ATOM   10104 C CB   . TYR B 1 358  ? 110.618 119.311 130.147 1.00 0.50  ?  358  TYR B CB   1 
ATOM   10105 C CG   . TYR B 1 358  ? 110.455 117.810 130.210 1.00 2.28  ?  358  TYR B CG   1 
ATOM   10106 C CD1  . TYR B 1 358  ? 109.243 117.206 129.908 1.00 1.70  ?  358  TYR B CD1  1 
ATOM   10107 C CD2  . TYR B 1 358  ? 111.526 116.994 130.546 1.00 0.44  ?  358  TYR B CD2  1 
ATOM   10108 C CE1  . TYR B 1 358  ? 109.099 115.832 129.955 1.00 0.00  ?  358  TYR B CE1  1 
ATOM   10109 C CE2  . TYR B 1 358  ? 111.392 115.623 130.597 1.00 1.43  ?  358  TYR B CE2  1 
ATOM   10110 C CZ   . TYR B 1 358  ? 110.178 115.047 130.300 1.00 2.64  ?  358  TYR B CZ   1 
ATOM   10111 O OH   . TYR B 1 358  ? 110.044 113.680 130.348 1.00 10.76 ?  358  TYR B OH   1 
ATOM   10112 N N    . LEU B 1 359  ? 111.298 119.452 133.205 1.00 0.00  ?  359  LEU B N    1 
ATOM   10113 C CA   . LEU B 1 359  ? 111.506 118.839 134.515 1.00 0.00  ?  359  LEU B CA   1 
ATOM   10114 C C    . LEU B 1 359  ? 110.614 119.474 135.574 1.00 0.00  ?  359  LEU B C    1 
ATOM   10115 O O    . LEU B 1 359  ? 109.995 118.765 136.384 1.00 4.09  ?  359  LEU B O    1 
ATOM   10116 C CB   . LEU B 1 359  ? 112.973 118.954 134.919 1.00 1.61  ?  359  LEU B CB   1 
ATOM   10117 C CG   . LEU B 1 359  ? 113.988 118.287 133.997 1.00 0.00  ?  359  LEU B CG   1 
ATOM   10118 C CD1  . LEU B 1 359  ? 115.385 118.750 134.348 1.00 0.00  ?  359  LEU B CD1  1 
ATOM   10119 C CD2  . LEU B 1 359  ? 113.878 116.779 134.103 1.00 0.20  ?  359  LEU B CD2  1 
ATOM   10120 N N    . ALA B 1 360  ? 110.522 120.810 135.570 1.00 1.97  ?  360  ALA B N    1 
ATOM   10121 C CA   . ALA B 1 360  ? 109.678 121.494 136.549 1.00 0.00  ?  360  ALA B CA   1 
ATOM   10122 C C    . ALA B 1 360  ? 108.210 121.112 136.389 1.00 0.00  ?  360  ALA B C    1 
ATOM   10123 O O    . ALA B 1 360  ? 107.507 120.889 137.384 1.00 3.16  ?  360  ALA B O    1 
ATOM   10124 C CB   . ALA B 1 360  ? 109.855 123.006 136.425 1.00 2.78  ?  360  ALA B CB   1 
ATOM   10125 N N    . ASN B 1 361  ? 107.739 121.017 135.141 1.00 10.14 ?  361  ASN B N    1 
ATOM   10126 C CA   . ASN B 1 361  ? 106.350 120.661 134.865 1.00 1.24  ?  361  ASN B CA   1 
ATOM   10127 C C    . ASN B 1 361  ? 106.014 119.273 135.400 1.00 5.84  ?  361  ASN B C    1 
ATOM   10128 O O    . ASN B 1 361  ? 105.007 119.086 136.103 1.00 12.18 ?  361  ASN B O    1 
ATOM   10129 C CB   . ASN B 1 361  ? 106.108 120.715 133.356 1.00 4.38  ?  361  ASN B CB   1 
ATOM   10130 C CG   . ASN B 1 361  ? 105.205 121.853 132.944 1.00 12.58 ?  361  ASN B CG   1 
ATOM   10131 O OD1  . ASN B 1 361  ? 104.493 122.424 133.763 1.00 11.74 ?  361  ASN B OD1  1 
ATOM   10132 N ND2  . ASN B 1 361  ? 105.231 122.190 131.660 1.00 17.76 ?  361  ASN B ND2  1 
ATOM   10133 N N    . THR B 1 362  ? 106.850 118.281 135.068 1.00 12.54 ?  362  THR B N    1 
ATOM   10134 C CA   . THR B 1 362  ? 106.577 116.915 135.511 1.00 2.49  ?  362  THR B CA   1 
ATOM   10135 C C    . THR B 1 362  ? 106.631 116.798 137.030 1.00 0.00  ?  362  THR B C    1 
ATOM   10136 O O    . THR B 1 362  ? 105.799 116.105 137.637 1.00 8.64  ?  362  THR B O    1 
ATOM   10137 C CB   . THR B 1 362  ? 107.555 115.935 134.863 1.00 8.71  ?  362  THR B CB   1 
ATOM   10138 O OG1  . THR B 1 362  ? 108.887 116.220 135.303 1.00 15.86 ?  362  THR B OG1  1 
ATOM   10139 C CG2  . THR B 1 362  ? 107.485 116.023 133.347 1.00 11.53 ?  362  THR B CG2  1 
ATOM   10140 N N    . LEU B 1 363  ? 107.596 117.476 137.666 1.00 0.00  ?  363  LEU B N    1 
ATOM   10141 C CA   . LEU B 1 363  ? 107.679 117.430 139.123 1.00 0.00  ?  363  LEU B CA   1 
ATOM   10142 C C    . LEU B 1 363  ? 106.446 118.045 139.774 1.00 0.00  ?  363  LEU B C    1 
ATOM   10143 O O    . LEU B 1 363  ? 105.916 117.499 140.752 1.00 8.62  ?  363  LEU B O    1 
ATOM   10144 C CB   . LEU B 1 363  ? 108.942 118.139 139.605 1.00 2.80  ?  363  LEU B CB   1 
ATOM   10145 C CG   . LEU B 1 363  ? 110.157 117.241 139.825 1.00 1.97  ?  363  LEU B CG   1 
ATOM   10146 C CD1  . LEU B 1 363  ? 111.409 118.076 140.016 1.00 0.00  ?  363  LEU B CD1  1 
ATOM   10147 C CD2  . LEU B 1 363  ? 109.915 116.336 141.017 1.00 4.53  ?  363  LEU B CD2  1 
ATOM   10148 N N    . ILE B 1 364  ? 105.971 119.175 139.239 1.00 6.25  ?  364  ILE B N    1 
ATOM   10149 C CA   . ILE B 1 364  ? 104.790 119.829 139.797 1.00 0.42  ?  364  ILE B CA   1 
ATOM   10150 C C    . ILE B 1 364  ? 103.572 118.921 139.696 1.00 4.77  ?  364  ILE B C    1 
ATOM   10151 O O    . ILE B 1 364  ? 102.810 118.778 140.661 1.00 7.57  ?  364  ILE B O    1 
ATOM   10152 C CB   . ILE B 1 364  ? 104.551 121.184 139.103 1.00 0.00  ?  364  ILE B CB   1 
ATOM   10153 C CG1  . ILE B 1 364  ? 105.513 122.236 139.651 1.00 0.00  ?  364  ILE B CG1  1 
ATOM   10154 C CG2  . ILE B 1 364  ? 103.110 121.641 139.265 1.00 1.87  ?  364  ILE B CG2  1 
ATOM   10155 C CD1  . ILE B 1 364  ? 105.520 123.518 138.865 1.00 0.00  ?  364  ILE B CD1  1 
ATOM   10156 N N    . PHE B 1 365  ? 103.378 118.280 138.538 1.00 7.74  ?  365  PHE B N    1 
ATOM   10157 C CA   . PHE B 1 365  ? 102.205 117.418 138.377 1.00 0.00  ?  365  PHE B CA   1 
ATOM   10158 C C    . PHE B 1 365  ? 102.259 116.201 139.302 1.00 0.00  ?  365  PHE B C    1 
ATOM   10159 O O    . PHE B 1 365  ? 101.254 115.858 139.944 1.00 3.70  ?  365  PHE B O    1 
ATOM   10160 C CB   . PHE B 1 365  ? 102.052 116.999 136.915 1.00 0.00  ?  365  PHE B CB   1 
ATOM   10161 C CG   . PHE B 1 365  ? 101.299 118.000 136.074 1.00 0.63  ?  365  PHE B CG   1 
ATOM   10162 C CD1  . PHE B 1 365  ? 99.917  118.065 136.124 1.00 0.00  ?  365  PHE B CD1  1 
ATOM   10163 C CD2  . PHE B 1 365  ? 101.971 118.880 135.244 1.00 0.00  ?  365  PHE B CD2  1 
ATOM   10164 C CE1  . PHE B 1 365  ? 99.221  118.981 135.357 1.00 0.00  ?  365  PHE B CE1  1 
ATOM   10165 C CE2  . PHE B 1 365  ? 101.278 119.800 134.477 1.00 0.00  ?  365  PHE B CE2  1 
ATOM   10166 C CZ   . PHE B 1 365  ? 99.903  119.848 134.535 1.00 0.00  ?  365  PHE B CZ   1 
ATOM   10167 N N    . MET B 1 366  ? 103.429 115.558 139.422 1.00 0.00  ?  366  MET B N    1 
ATOM   10168 C CA   . MET B 1 366  ? 103.552 114.431 140.351 1.00 0.00  ?  366  MET B CA   1 
ATOM   10169 C C    . MET B 1 366  ? 103.273 114.840 141.793 1.00 0.00  ?  366  MET B C    1 
ATOM   10170 O O    . MET B 1 366  ? 102.526 114.156 142.513 1.00 11.61 ?  366  MET B O    1 
ATOM   10171 C CB   . MET B 1 366  ? 104.936 113.794 140.250 1.00 0.00  ?  366  MET B CB   1 
ATOM   10172 C CG   . MET B 1 366  ? 105.113 112.864 139.083 1.00 2.85  ?  366  MET B CG   1 
ATOM   10173 S SD   . MET B 1 366  ? 104.775 111.197 139.685 1.00 15.36 ?  366  MET B SD   1 
ATOM   10174 C CE   . MET B 1 366  ? 104.656 110.287 138.154 1.00 7.65  ?  366  MET B CE   1 
ATOM   10175 N N    . MET B 1 367  ? 103.866 115.951 142.241 1.00 1.40  ?  367  MET B N    1 
ATOM   10176 C CA   . MET B 1 367  ? 103.701 116.295 143.647 1.00 0.41  ?  367  MET B CA   1 
ATOM   10177 C C    . MET B 1 367  ? 102.299 116.805 143.957 1.00 0.41  ?  367  MET B C    1 
ATOM   10178 O O    . MET B 1 367  ? 101.785 116.536 145.052 1.00 0.00  ?  367  MET B O    1 
ATOM   10179 C CB   . MET B 1 367  ? 104.776 117.286 144.102 1.00 1.86  ?  367  MET B CB   1 
ATOM   10180 C CG   . MET B 1 367  ? 104.550 118.731 143.747 1.00 4.21  ?  367  MET B CG   1 
ATOM   10181 S SD   . MET B 1 367  ? 106.005 119.743 144.078 1.00 0.14  ?  367  MET B SD   1 
ATOM   10182 C CE   . MET B 1 367  ? 107.305 118.732 143.383 1.00 2.70  ?  367  MET B CE   1 
ATOM   10183 N N    . VAL B 1 368  ? 101.635 117.480 143.012 1.00 1.56  ?  368  VAL B N    1 
ATOM   10184 C CA   . VAL B 1 368  ? 100.255 117.870 143.281 1.00 0.00  ?  368  VAL B CA   1 
ATOM   10185 C C    . VAL B 1 368  ? 99.356  116.641 143.308 1.00 0.00  ?  368  VAL B C    1 
ATOM   10186 O O    . VAL B 1 368  ? 98.420  116.579 144.113 1.00 5.26  ?  368  VAL B O    1 
ATOM   10187 C CB   . VAL B 1 368  ? 99.755  118.944 142.289 1.00 7.06  ?  368  VAL B CB   1 
ATOM   10188 C CG1  . VAL B 1 368  ? 99.618  118.412 140.888 1.00 0.00  ?  368  VAL B CG1  1 
ATOM   10189 C CG2  . VAL B 1 368  ? 98.433  119.513 142.752 1.00 0.16  ?  368  VAL B CG2  1 
ATOM   10190 N N    . GLY B 1 369  ? 99.650  115.622 142.489 1.00 8.38  ?  369  GLY B N    1 
ATOM   10191 C CA   . GLY B 1 369  ? 98.876  114.390 142.565 1.00 0.00  ?  369  GLY B CA   1 
ATOM   10192 C C    . GLY B 1 369  ? 98.986  113.699 143.913 1.00 0.00  ?  369  GLY B C    1 
ATOM   10193 O O    . GLY B 1 369  ? 97.971  113.351 144.533 1.00 0.44  ?  369  GLY B O    1 
ATOM   10194 N N    . VAL B 1 370  ? 100.219 113.516 144.403 1.00 1.49  ?  370  VAL B N    1 
ATOM   10195 C CA   . VAL B 1 370  ? 100.379 112.799 145.671 1.00 0.00  ?  370  VAL B CA   1 
ATOM   10196 C C    . VAL B 1 370  ? 99.799  113.609 146.829 1.00 2.15  ?  370  VAL B C    1 
ATOM   10197 O O    . VAL B 1 370  ? 99.101  113.063 147.695 1.00 5.33  ?  370  VAL B O    1 
ATOM   10198 C CB   . VAL B 1 370  ? 101.849 112.401 145.925 1.00 0.00  ?  370  VAL B CB   1 
ATOM   10199 C CG1  . VAL B 1 370  ? 102.779 113.534 145.674 1.00 0.00  ?  370  VAL B CG1  1 
ATOM   10200 C CG2  . VAL B 1 370  ? 102.041 111.922 147.355 1.00 2.44  ?  370  VAL B CG2  1 
ATOM   10201 N N    . VAL B 1 371  ? 100.029 114.925 146.845 1.00 7.09  ?  371  VAL B N    1 
ATOM   10202 C CA   . VAL B 1 371  ? 99.545  115.719 147.968 1.00 2.99  ?  371  VAL B CA   1 
ATOM   10203 C C    . VAL B 1 371  ? 98.048  116.006 147.889 1.00 1.64  ?  371  VAL B C    1 
ATOM   10204 O O    . VAL B 1 371  ? 97.450  116.390 148.902 1.00 3.69  ?  371  VAL B O    1 
ATOM   10205 C CB   . VAL B 1 371  ? 100.356 117.021 148.074 1.00 0.00  ?  371  VAL B CB   1 
ATOM   10206 C CG1  . VAL B 1 371  ? 99.773  118.073 147.178 1.00 3.73  ?  371  VAL B CG1  1 
ATOM   10207 C CG2  . VAL B 1 371  ? 100.402 117.506 149.511 1.00 8.00  ?  371  VAL B CG2  1 
ATOM   10208 N N    . VAL B 1 372  ? 97.411  115.820 146.733 1.00 5.97  ?  372  VAL B N    1 
ATOM   10209 C CA   . VAL B 1 372  ? 95.961  115.952 146.688 1.00 3.42  ?  372  VAL B CA   1 
ATOM   10210 C C    . VAL B 1 372  ? 95.278  114.626 147.011 1.00 5.12  ?  372  VAL B C    1 
ATOM   10211 O O    . VAL B 1 372  ? 94.139  114.622 147.490 1.00 7.44  ?  372  VAL B O    1 
ATOM   10212 C CB   . VAL B 1 372  ? 95.497  116.514 145.328 1.00 2.19  ?  372  VAL B CB   1 
ATOM   10213 C CG1  . VAL B 1 372  ? 95.374  115.421 144.272 1.00 3.31  ?  372  VAL B CG1  1 
ATOM   10214 C CG2  . VAL B 1 372  ? 94.183  117.259 145.484 1.00 3.70  ?  372  VAL B CG2  1 
ATOM   10215 N N    . THR B 1 373  ? 95.948  113.495 146.774 1.00 10.02 ?  373  THR B N    1 
ATOM   10216 C CA   . THR B 1 373  ? 95.382  112.231 147.233 1.00 7.83  ?  373  THR B CA   1 
ATOM   10217 C C    . THR B 1 373  ? 95.544  112.062 148.741 1.00 10.18 ?  373  THR B C    1 
ATOM   10218 O O    . THR B 1 373  ? 94.615  111.607 149.419 1.00 11.59 ?  373  THR B O    1 
ATOM   10219 C CB   . THR B 1 373  ? 96.021  111.066 146.479 1.00 11.06 ?  373  THR B CB   1 
ATOM   10220 O OG1  . THR B 1 373  ? 95.649  111.149 145.102 1.00 8.70  ?  373  THR B OG1  1 
ATOM   10221 C CG2  . THR B 1 373  ? 95.550  109.731 147.033 1.00 14.84 ?  373  THR B CG2  1 
ATOM   10222 N N    . GLN B 1 374  ? 96.701  112.448 149.285 1.00 12.63 ?  374  GLN B N    1 
ATOM   10223 C CA   . GLN B 1 374  ? 96.968  112.218 150.703 1.00 11.04 ?  374  GLN B CA   1 
ATOM   10224 C C    . GLN B 1 374  ? 96.106  113.107 151.596 1.00 14.03 ?  374  GLN B C    1 
ATOM   10225 O O    . GLN B 1 374  ? 95.517  112.632 152.574 1.00 14.35 ?  374  GLN B O    1 
ATOM   10226 C CB   . GLN B 1 374  ? 98.451  112.443 150.999 1.00 11.70 ?  374  GLN B CB   1 
ATOM   10227 C CG   . GLN B 1 374  ? 99.293  111.181 150.962 1.00 12.09 ?  374  GLN B CG   1 
ATOM   10228 C CD   . GLN B 1 374  ? 100.586 111.322 151.739 1.00 16.08 ?  374  GLN B CD   1 
ATOM   10229 O OE1  . GLN B 1 374  ? 100.614 111.910 152.820 1.00 20.37 ?  374  GLN B OE1  1 
ATOM   10230 N NE2  . GLN B 1 374  ? 101.668 110.779 151.193 1.00 18.02 ?  374  GLN B NE2  1 
ATOM   10231 N N    . LYS B 1 375  ? 96.018  114.398 151.280 1.00 16.41 ?  375  LYS B N    1 
ATOM   10232 C CA   . LYS B 1 375  ? 95.439  115.384 152.186 1.00 13.95 ?  375  LYS B CA   1 
ATOM   10233 C C    . LYS B 1 375  ? 94.055  115.864 151.777 1.00 14.88 ?  375  LYS B C    1 
ATOM   10234 O O    . LYS B 1 375  ? 93.118  115.797 152.578 1.00 14.29 ?  375  LYS B O    1 
ATOM   10235 C CB   . LYS B 1 375  ? 96.376  116.595 152.306 1.00 14.06 ?  375  LYS B CB   1 
ATOM   10236 C CG   . LYS B 1 375  ? 97.711  116.296 152.960 1.00 14.30 ?  375  LYS B CG   1 
ATOM   10237 C CD   . LYS B 1 375  ? 98.286  117.546 153.600 1.00 16.20 ?  375  LYS B CD   1 
ATOM   10238 C CE   . LYS B 1 375  ? 99.777  117.657 153.360 1.00 12.24 ?  375  LYS B CE   1 
ATOM   10239 N NZ   . LYS B 1 375  ? 100.206 119.070 153.163 1.00 9.58  ?  375  LYS B NZ   1 
ATOM   10240 N N    . ALA B 1 376  ? 93.898  116.356 150.549 1.00 15.40 ?  376  ALA B N    1 
ATOM   10241 C CA   . ALA B 1 376  ? 92.690  117.076 150.164 1.00 14.70 ?  376  ALA B CA   1 
ATOM   10242 C C    . ALA B 1 376  ? 91.496  116.172 149.889 1.00 17.29 ?  376  ALA B C    1 
ATOM   10243 O O    . ALA B 1 376  ? 90.394  116.687 149.676 1.00 22.38 ?  376  ALA B O    1 
ATOM   10244 C CB   . ALA B 1 376  ? 92.965  117.938 148.931 1.00 7.47  ?  376  ALA B CB   1 
ATOM   10245 N N    . LEU B 1 377  ? 91.674  114.853 149.881 1.00 15.82 ?  377  LEU B N    1 
ATOM   10246 C CA   . LEU B 1 377  ? 90.586  113.931 149.589 1.00 15.49 ?  377  LEU B CA   1 
ATOM   10247 C C    . LEU B 1 377  ? 89.983  113.311 150.843 1.00 19.17 ?  377  LEU B C    1 
ATOM   10248 O O    . LEU B 1 377  ? 89.227  112.340 150.740 1.00 19.02 ?  377  LEU B O    1 
ATOM   10249 C CB   . LEU B 1 377  ? 91.062  112.833 148.635 1.00 20.11 ?  377  LEU B CB   1 
ATOM   10250 C CG   . LEU B 1 377  ? 90.939  113.139 147.138 1.00 19.24 ?  377  LEU B CG   1 
ATOM   10251 C CD1  . LEU B 1 377  ? 90.981  111.859 146.320 1.00 17.71 ?  377  LEU B CD1  1 
ATOM   10252 C CD2  . LEU B 1 377  ? 89.668  113.921 146.838 1.00 14.40 ?  377  LEU B CD2  1 
ATOM   10253 N N    . VAL B 1 378  ? 90.298  113.845 152.022 1.00 24.07 ?  378  VAL B N    1 
ATOM   10254 C CA   . VAL B 1 378  ? 89.702  113.391 153.273 1.00 25.22 ?  378  VAL B CA   1 
ATOM   10255 C C    . VAL B 1 378  ? 88.745  114.412 153.862 1.00 24.56 ?  378  VAL B C    1 
ATOM   10256 O O    . VAL B 1 378  ? 88.136  114.143 154.908 1.00 25.32 ?  378  VAL B O    1 
ATOM   10257 C CB   . VAL B 1 378  ? 90.783  113.012 154.304 1.00 22.78 ?  378  VAL B CB   1 
ATOM   10258 C CG1  . VAL B 1 378  ? 91.857  112.154 153.654 1.00 21.81 ?  378  VAL B CG1  1 
ATOM   10259 C CG2  . VAL B 1 378  ? 91.394  114.259 154.926 1.00 21.95 ?  378  VAL B CG2  1 
ATOM   10260 N N    . ALA B 1 379  ? 88.582  115.568 153.224 1.00 20.17 ?  379  ALA B N    1 
ATOM   10261 C CA   . ALA B 1 379  ? 87.734  116.645 153.725 1.00 20.73 ?  379  ALA B CA   1 
ATOM   10262 C C    . ALA B 1 379  ? 86.856  117.198 152.610 1.00 18.81 ?  379  ALA B C    1 
ATOM   10263 O O    . ALA B 1 379  ? 86.764  118.409 152.398 1.00 17.90 ?  379  ALA B O    1 
ATOM   10264 C CB   . ALA B 1 379  ? 88.577  117.752 154.350 1.00 21.97 ?  379  ALA B CB   1 
ATOM   10265 N N    . VAL B 1 380  ? 86.195  116.308 151.874 1.00 19.84 ?  380  VAL B N    1 
ATOM   10266 C CA   . VAL B 1 380  ? 85.332  116.690 150.763 1.00 20.70 ?  380  VAL B CA   1 
ATOM   10267 C C    . VAL B 1 380  ? 83.950  116.084 150.971 1.00 21.73 ?  380  VAL B C    1 
ATOM   10268 O O    . VAL B 1 380  ? 83.818  114.972 151.494 1.00 22.46 ?  380  VAL B O    1 
ATOM   10269 C CB   . VAL B 1 380  ? 85.920  116.255 149.404 1.00 21.88 ?  380  VAL B CB   1 
ATOM   10270 C CG1  . VAL B 1 380  ? 87.093  117.143 149.030 1.00 19.97 ?  380  VAL B CG1  1 
ATOM   10271 C CG2  . VAL B 1 380  ? 86.345  114.796 149.448 1.00 19.81 ?  380  VAL B CG2  1 
ATOM   10272 N N    . ASP B 1 381  ? 82.926  116.827 150.569 1.00 22.39 ?  381  ASP B N    1 
ATOM   10273 C CA   . ASP B 1 381  ? 81.536  116.393 150.600 1.00 23.92 ?  381  ASP B CA   1 
ATOM   10274 C C    . ASP B 1 381  ? 80.976  116.424 149.180 1.00 23.20 ?  381  ASP B C    1 
ATOM   10275 O O    . ASP B 1 381  ? 81.665  116.792 148.227 1.00 24.47 ?  381  ASP B O    1 
ATOM   10276 C CB   . ASP B 1 381  ? 80.714  117.279 151.543 1.00 22.85 ?  381  ASP B CB   1 
ATOM   10277 C CG   . ASP B 1 381  ? 79.536  116.547 152.160 1.00 24.65 ?  381  ASP B CG   1 
ATOM   10278 O OD1  . ASP B 1 381  ? 78.904  115.729 151.459 1.00 26.02 ?  381  ASP B OD1  1 
ATOM   10279 O OD2  . ASP B 1 381  ? 79.238  116.795 153.348 1.00 26.47 ?  381  ASP B OD2  1 
ATOM   10280 N N    . LYS B 1 382  ? 79.708  116.024 149.044 1.00 21.34 ?  382  LYS B N    1 
ATOM   10281 C CA   . LYS B 1 382  ? 79.038  116.090 147.747 1.00 22.15 ?  382  LYS B CA   1 
ATOM   10282 C C    . LYS B 1 382  ? 78.880  117.536 147.286 1.00 24.21 ?  382  LYS B C    1 
ATOM   10283 O O    . LYS B 1 382  ? 78.980  117.832 146.084 1.00 25.49 ?  382  LYS B O    1 
ATOM   10284 C CB   . LYS B 1 382  ? 77.683  115.383 147.835 1.00 20.98 ?  382  LYS B CB   1 
ATOM   10285 C CG   . LYS B 1 382  ? 76.700  115.712 146.721 1.00 21.98 ?  382  LYS B CG   1 
ATOM   10286 C CD   . LYS B 1 382  ? 77.144  115.128 145.391 1.00 20.86 ?  382  LYS B CD   1 
ATOM   10287 C CE   . LYS B 1 382  ? 76.273  115.638 144.256 1.00 19.28 ?  382  LYS B CE   1 
ATOM   10288 N NZ   . LYS B 1 382  ? 76.905  115.409 142.929 1.00 19.08 ?  382  LYS B NZ   1 
ATOM   10289 N N    . MET B 1 383  ? 78.651  118.449 148.234 1.00 18.77 ?  383  MET B N    1 
ATOM   10290 C CA   . MET B 1 383  ? 78.544  119.866 147.907 1.00 18.88 ?  383  MET B CA   1 
ATOM   10291 C C    . MET B 1 383  ? 79.828  120.400 147.290 1.00 21.85 ?  383  MET B C    1 
ATOM   10292 O O    . MET B 1 383  ? 79.779  121.307 146.455 1.00 24.60 ?  383  MET B O    1 
ATOM   10293 C CB   . MET B 1 383  ? 78.185  120.665 149.160 1.00 19.47 ?  383  MET B CB   1 
ATOM   10294 C CG   . MET B 1 383  ? 76.801  120.364 149.712 1.00 21.98 ?  383  MET B CG   1 
ATOM   10295 S SD   . MET B 1 383  ? 75.492  120.601 148.496 1.00 35.95 ?  383  MET B SD   1 
ATOM   10296 C CE   . MET B 1 383  ? 75.714  122.332 148.095 1.00 19.90 ?  383  MET B CE   1 
ATOM   10297 N N    . ASP B 1 384  ? 80.982  119.846 147.674 1.00 21.02 ?  384  ASP B N    1 
ATOM   10298 C CA   . ASP B 1 384  ? 82.239  120.255 147.057 1.00 16.65 ?  384  ASP B CA   1 
ATOM   10299 C C    . ASP B 1 384  ? 82.279  119.888 145.577 1.00 17.87 ?  384  ASP B C    1 
ATOM   10300 O O    . ASP B 1 384  ? 82.726  120.688 144.748 1.00 23.98 ?  384  ASP B O    1 
ATOM   10301 C CB   . ASP B 1 384  ? 83.416  119.627 147.801 1.00 16.02 ?  384  ASP B CB   1 
ATOM   10302 C CG   . ASP B 1 384  ? 83.683  120.296 149.134 1.00 22.05 ?  384  ASP B CG   1 
ATOM   10303 O OD1  . ASP B 1 384  ? 82.985  121.279 149.458 1.00 27.10 ?  384  ASP B OD1  1 
ATOM   10304 O OD2  . ASP B 1 384  ? 84.593  119.840 149.857 1.00 20.47 ?  384  ASP B OD2  1 
ATOM   10305 N N    . TRP B 1 385  ? 81.805  118.690 145.224 1.00 10.09 ?  385  TRP B N    1 
ATOM   10306 C CA   . TRP B 1 385  ? 81.760  118.297 143.818 1.00 10.44 ?  385  TRP B CA   1 
ATOM   10307 C C    . TRP B 1 385  ? 80.753  119.137 143.040 1.00 16.43 ?  385  TRP B C    1 
ATOM   10308 O O    . TRP B 1 385  ? 81.007  119.520 141.887 1.00 19.23 ?  385  TRP B O    1 
ATOM   10309 C CB   . TRP B 1 385  ? 81.427  116.810 143.702 1.00 11.99 ?  385  TRP B CB   1 
ATOM   10310 C CG   . TRP B 1 385  ? 82.465  115.915 144.306 1.00 12.09 ?  385  TRP B CG   1 
ATOM   10311 C CD1  . TRP B 1 385  ? 82.503  115.455 145.588 1.00 10.81 ?  385  TRP B CD1  1 
ATOM   10312 C CD2  . TRP B 1 385  ? 83.619  115.375 143.652 1.00 14.02 ?  385  TRP B CD2  1 
ATOM   10313 N NE1  . TRP B 1 385  ? 83.606  114.660 145.775 1.00 9.42  ?  385  TRP B NE1  1 
ATOM   10314 C CE2  . TRP B 1 385  ? 84.309  114.595 144.601 1.00 12.32 ?  385  TRP B CE2  1 
ATOM   10315 C CE3  . TRP B 1 385  ? 84.136  115.474 142.357 1.00 15.60 ?  385  TRP B CE3  1 
ATOM   10316 C CZ2  . TRP B 1 385  ? 85.486  113.919 144.296 1.00 14.21 ?  385  TRP B CZ2  1 
ATOM   10317 C CZ3  . TRP B 1 385  ? 85.305  114.802 142.057 1.00 11.15 ?  385  TRP B CZ3  1 
ATOM   10318 C CH2  . TRP B 1 385  ? 85.967  114.034 143.022 1.00 12.26 ?  385  TRP B CH2  1 
ATOM   10319 N N    . PHE B 1 386  ? 79.605  119.435 143.658 1.00 14.30 ?  386  PHE B N    1 
ATOM   10320 C CA   . PHE B 1 386  ? 78.621  120.308 143.021 1.00 14.44 ?  386  PHE B CA   1 
ATOM   10321 C C    . PHE B 1 386  ? 79.203  121.696 142.767 1.00 18.99 ?  386  PHE B C    1 
ATOM   10322 O O    . PHE B 1 386  ? 79.018  122.272 141.685 1.00 15.78 ?  386  PHE B O    1 
ATOM   10323 C CB   . PHE B 1 386  ? 77.366  120.387 143.894 1.00 13.37 ?  386  PHE B CB   1 
ATOM   10324 C CG   . PHE B 1 386  ? 76.341  121.379 143.415 1.00 15.58 ?  386  PHE B CG   1 
ATOM   10325 C CD1  . PHE B 1 386  ? 75.475  121.056 142.384 1.00 17.54 ?  386  PHE B CD1  1 
ATOM   10326 C CD2  . PHE B 1 386  ? 76.222  122.621 144.019 1.00 14.83 ?  386  PHE B CD2  1 
ATOM   10327 C CE1  . PHE B 1 386  ? 74.525  121.962 141.948 1.00 17.80 ?  386  PHE B CE1  1 
ATOM   10328 C CE2  . PHE B 1 386  ? 75.275  123.532 143.587 1.00 16.14 ?  386  PHE B CE2  1 
ATOM   10329 C CZ   . PHE B 1 386  ? 74.425  123.201 142.551 1.00 16.37 ?  386  PHE B CZ   1 
ATOM   10330 N N    . TYR B 1 387  ? 79.932  122.234 143.747 1.00 15.87 ?  387  TYR B N    1 
ATOM   10331 C CA   . TYR B 1 387  ? 80.561  123.540 143.591 1.00 13.05 ?  387  TYR B CA   1 
ATOM   10332 C C    . TYR B 1 387  ? 81.653  123.503 142.532 1.00 8.81  ?  387  TYR B C    1 
ATOM   10333 O O    . TYR B 1 387  ? 81.849  124.482 141.807 1.00 15.99 ?  387  TYR B O    1 
ATOM   10334 C CB   . TYR B 1 387  ? 81.126  124.007 144.931 1.00 14.81 ?  387  TYR B CB   1 
ATOM   10335 C CG   . TYR B 1 387  ? 80.068  124.397 145.937 1.00 17.47 ?  387  TYR B CG   1 
ATOM   10336 C CD1  . TYR B 1 387  ? 78.804  124.798 145.526 1.00 17.60 ?  387  TYR B CD1  1 
ATOM   10337 C CD2  . TYR B 1 387  ? 80.331  124.359 147.300 1.00 18.29 ?  387  TYR B CD2  1 
ATOM   10338 C CE1  . TYR B 1 387  ? 77.833  125.153 146.442 1.00 20.43 ?  387  TYR B CE1  1 
ATOM   10339 C CE2  . TYR B 1 387  ? 79.367  124.711 148.224 1.00 17.02 ?  387  TYR B CE2  1 
ATOM   10340 C CZ   . TYR B 1 387  ? 78.120  125.107 147.789 1.00 20.00 ?  387  TYR B CZ   1 
ATOM   10341 O OH   . TYR B 1 387  ? 77.156  125.460 148.705 1.00 20.25 ?  387  TYR B OH   1 
ATOM   10342 N N    . LEU B 1 388  ? 82.374  122.383 142.428 1.00 2.40  ?  388  LEU B N    1 
ATOM   10343 C CA   . LEU B 1 388  ? 83.380  122.239 141.379 1.00 8.77  ?  388  LEU B CA   1 
ATOM   10344 C C    . LEU B 1 388  ? 82.741  122.276 139.996 1.00 12.92 ?  388  LEU B C    1 
ATOM   10345 O O    . LEU B 1 388  ? 83.262  122.925 139.080 1.00 13.59 ?  388  LEU B O    1 
ATOM   10346 C CB   . LEU B 1 388  ? 84.160  120.939 141.580 1.00 6.75  ?  388  LEU B CB   1 
ATOM   10347 C CG   . LEU B 1 388  ? 85.068  120.443 140.450 1.00 4.91  ?  388  LEU B CG   1 
ATOM   10348 C CD1  . LEU B 1 388  ? 86.142  121.468 140.117 1.00 4.58  ?  388  LEU B CD1  1 
ATOM   10349 C CD2  . LEU B 1 388  ? 85.693  119.103 140.807 1.00 8.59  ?  388  LEU B CD2  1 
ATOM   10350 N N    . ILE B 1 389  ? 81.602  121.597 139.830 1.00 15.06 ?  389  ILE B N    1 
ATOM   10351 C CA   . ILE B 1 389  ? 80.903  121.613 138.543 1.00 12.45 ?  389  ILE B CA   1 
ATOM   10352 C C    . ILE B 1 389  ? 80.402  123.020 138.215 1.00 13.15 ?  389  ILE B C    1 
ATOM   10353 O O    . ILE B 1 389  ? 80.552  123.506 137.081 1.00 12.76 ?  389  ILE B O    1 
ATOM   10354 C CB   . ILE B 1 389  ? 79.759  120.580 138.550 1.00 12.77 ?  389  ILE B CB   1 
ATOM   10355 C CG1  . ILE B 1 389  ? 80.308  119.178 138.282 1.00 13.98 ?  389  ILE B CG1  1 
ATOM   10356 C CG2  . ILE B 1 389  ? 78.688  120.932 137.526 1.00 13.41 ?  389  ILE B CG2  1 
ATOM   10357 C CD1  . ILE B 1 389  ? 79.563  118.081 139.008 1.00 13.55 ?  389  ILE B CD1  1 
ATOM   10358 N N    . ILE B 1 390  ? 79.816  123.701 139.207 1.00 14.41 ?  390  ILE B N    1 
ATOM   10359 C CA   . ILE B 1 390  ? 79.310  125.056 138.984 1.00 13.48 ?  390  ILE B CA   1 
ATOM   10360 C C    . ILE B 1 390  ? 80.452  126.007 138.634 1.00 13.29 ?  390  ILE B C    1 
ATOM   10361 O O    . ILE B 1 390  ? 80.324  126.854 137.741 1.00 10.32 ?  390  ILE B O    1 
ATOM   10362 C CB   . ILE B 1 390  ? 78.518  125.544 140.212 1.00 10.20 ?  390  ILE B CB   1 
ATOM   10363 C CG1  . ILE B 1 390  ? 77.289  124.664 140.444 1.00 10.99 ?  390  ILE B CG1  1 
ATOM   10364 C CG2  . ILE B 1 390  ? 78.082  126.987 140.030 1.00 7.73  ?  390  ILE B CG2  1 
ATOM   10365 C CD1  . ILE B 1 390  ? 76.255  124.747 139.344 1.00 14.96 ?  390  ILE B CD1  1 
ATOM   10366 N N    . LEU B 1 391  ? 81.589  125.873 139.321 1.00 9.99  ?  391  LEU B N    1 
ATOM   10367 C CA   . LEU B 1 391  ? 82.750  126.709 139.034 1.00 9.75  ?  391  LEU B CA   1 
ATOM   10368 C C    . LEU B 1 391  ? 83.309  126.427 137.644 1.00 10.25 ?  391  LEU B C    1 
ATOM   10369 O O    . LEU B 1 391  ? 83.770  127.347 136.958 1.00 13.19 ?  391  LEU B O    1 
ATOM   10370 C CB   . LEU B 1 391  ? 83.817  126.492 140.109 1.00 11.05 ?  391  LEU B CB   1 
ATOM   10371 C CG   . LEU B 1 391  ? 85.251  126.956 139.853 1.00 10.67 ?  391  LEU B CG   1 
ATOM   10372 C CD1  . LEU B 1 391  ? 85.339  128.472 139.880 1.00 9.90  ?  391  LEU B CD1  1 
ATOM   10373 C CD2  . LEU B 1 391  ? 86.198  126.344 140.872 1.00 7.08  ?  391  LEU B CD2  1 
ATOM   10374 N N    . TYR B 1 392  ? 83.281  125.161 137.213 1.00 7.92  ?  392  TYR B N    1 
ATOM   10375 C CA   . TYR B 1 392  ? 83.737  124.832 135.865 1.00 9.69  ?  392  TYR B CA   1 
ATOM   10376 C C    . TYR B 1 392  ? 82.850  125.475 134.808 1.00 14.31 ?  392  TYR B C    1 
ATOM   10377 O O    . TYR B 1 392  ? 83.341  125.927 133.767 1.00 16.38 ?  392  TYR B O    1 
ATOM   10378 C CB   . TYR B 1 392  ? 83.778  123.319 135.664 1.00 7.76  ?  392  TYR B CB   1 
ATOM   10379 C CG   . TYR B 1 392  ? 84.129  122.930 134.246 1.00 10.52 ?  392  TYR B CG   1 
ATOM   10380 C CD1  . TYR B 1 392  ? 85.363  123.262 133.703 1.00 10.41 ?  392  TYR B CD1  1 
ATOM   10381 C CD2  . TYR B 1 392  ? 83.222  122.253 133.443 1.00 11.64 ?  392  TYR B CD2  1 
ATOM   10382 C CE1  . TYR B 1 392  ? 85.689  122.918 132.407 1.00 10.73 ?  392  TYR B CE1  1 
ATOM   10383 C CE2  . TYR B 1 392  ? 83.539  121.905 132.143 1.00 7.29  ?  392  TYR B CE2  1 
ATOM   10384 C CZ   . TYR B 1 392  ? 84.774  122.241 131.631 1.00 5.82  ?  392  TYR B CZ   1 
ATOM   10385 O OH   . TYR B 1 392  ? 85.096  121.898 130.339 1.00 6.35  ?  392  TYR B OH   1 
ATOM   10386 N N    . LEU B 1 393  ? 81.536  125.497 135.040 1.00 15.55 ?  393  LEU B N    1 
ATOM   10387 C CA   . LEU B 1 393  ? 80.658  126.231 134.126 1.00 14.43 ?  393  LEU B CA   1 
ATOM   10388 C C    . LEU B 1 393  ? 80.948  127.731 134.158 1.00 13.39 ?  393  LEU B C    1 
ATOM   10389 O O    . LEU B 1 393  ? 80.998  128.389 133.106 1.00 15.71 ?  393  LEU B O    1 
ATOM   10390 C CB   . LEU B 1 393  ? 79.192  125.960 134.465 1.00 13.44 ?  393  LEU B CB   1 
ATOM   10391 C CG   . LEU B 1 393  ? 78.491  124.813 133.729 1.00 9.31  ?  393  LEU B CG   1 
ATOM   10392 C CD1  . LEU B 1 393  ? 78.685  124.948 132.227 1.00 15.17 ?  393  LEU B CD1  1 
ATOM   10393 C CD2  . LEU B 1 393  ? 78.968  123.453 134.212 1.00 8.62  ?  393  LEU B CD2  1 
ATOM   10394 N N    . ALA B 1 394  ? 81.161  128.281 135.356 1.00 13.61 ?  394  ALA B N    1 
ATOM   10395 C CA   . ALA B 1 394  ? 81.288  129.727 135.510 1.00 13.91 ?  394  ALA B CA   1 
ATOM   10396 C C    . ALA B 1 394  ? 82.574  130.256 134.887 1.00 12.28 ?  394  ALA B C    1 
ATOM   10397 O O    . ALA B 1 394  ? 82.581  131.355 134.318 1.00 17.40 ?  394  ALA B O    1 
ATOM   10398 C CB   . ALA B 1 394  ? 81.217  130.103 136.988 1.00 11.85 ?  394  ALA B CB   1 
ATOM   10399 N N    . ILE B 1 395  ? 83.675  129.507 134.995 1.00 8.59  ?  395  ILE B N    1 
ATOM   10400 C CA   . ILE B 1 395  ? 84.933  129.986 134.425 1.00 10.64 ?  395  ILE B CA   1 
ATOM   10401 C C    . ILE B 1 395  ? 84.843  130.048 132.903 1.00 12.91 ?  395  ILE B C    1 
ATOM   10402 O O    . ILE B 1 395  ? 85.331  130.999 132.284 1.00 15.98 ?  395  ILE B O    1 
ATOM   10403 C CB   . ILE B 1 395  ? 86.126  129.133 134.905 1.00 12.59 ?  395  ILE B CB   1 
ATOM   10404 C CG1  . ILE B 1 395  ? 85.954  127.655 134.546 1.00 15.09 ?  395  ILE B CG1  1 
ATOM   10405 C CG2  . ILE B 1 395  ? 86.348  129.315 136.398 1.00 10.56 ?  395  ILE B CG2  1 
ATOM   10406 C CD1  . ILE B 1 395  ? 87.251  126.952 134.223 1.00 9.96  ?  395  ILE B CD1  1 
ATOM   10407 N N    . THR B 1 396  ? 84.179  129.068 132.281 1.00 15.86 ?  396  THR B N    1 
ATOM   10408 C CA   . THR B 1 396  ? 83.965  129.116 130.838 1.00 18.05 ?  396  THR B CA   1 
ATOM   10409 C C    . THR B 1 396  ? 83.053  130.274 130.450 1.00 19.33 ?  396  THR B C    1 
ATOM   10410 O O    . THR B 1 396  ? 83.298  130.957 129.445 1.00 17.19 ?  396  THR B O    1 
ATOM   10411 C CB   . THR B 1 396  ? 83.382  127.791 130.347 1.00 13.63 ?  396  THR B CB   1 
ATOM   10412 O OG1  . THR B 1 396  ? 83.954  126.709 131.093 1.00 14.65 ?  396  THR B OG1  1 
ATOM   10413 C CG2  . THR B 1 396  ? 83.673  127.593 128.868 1.00 12.82 ?  396  THR B CG2  1 
ATOM   10414 N N    . ILE B 1 397  ? 82.003  130.516 131.243 1.00 16.73 ?  397  ILE B N    1 
ATOM   10415 C CA   . ILE B 1 397  ? 81.076  131.605 130.937 1.00 8.52  ?  397  ILE B CA   1 
ATOM   10416 C C    . ILE B 1 397  ? 81.791  132.953 130.988 1.00 10.28 ?  397  ILE B C    1 
ATOM   10417 O O    . ILE B 1 397  ? 81.664  133.779 130.076 1.00 13.09 ?  397  ILE B O    1 
ATOM   10418 C CB   . ILE B 1 397  ? 79.866  131.564 131.888 1.00 9.79  ?  397  ILE B CB   1 
ATOM   10419 C CG1  . ILE B 1 397  ? 78.877  130.490 131.434 1.00 15.62 ?  397  ILE B CG1  1 
ATOM   10420 C CG2  . ILE B 1 397  ? 79.178  132.919 131.957 1.00 13.78 ?  397  ILE B CG2  1 
ATOM   10421 C CD1  . ILE B 1 397  ? 77.677  130.343 132.341 1.00 14.95 ?  397  ILE B CD1  1 
ATOM   10422 N N    . ILE B 1 398  ? 82.585  133.186 132.037 1.00 13.21 ?  398  ILE B N    1 
ATOM   10423 C CA   . ILE B 1 398  ? 83.266  134.476 132.142 1.00 13.99 ?  398  ILE B CA   1 
ATOM   10424 C C    . ILE B 1 398  ? 84.433  134.574 131.161 1.00 13.37 ?  398  ILE B C    1 
ATOM   10425 O O    . ILE B 1 398  ? 84.791  135.679 130.730 1.00 16.74 ?  398  ILE B O    1 
ATOM   10426 C CB   . ILE B 1 398  ? 83.703  134.755 133.594 1.00 9.67  ?  398  ILE B CB   1 
ATOM   10427 C CG1  . ILE B 1 398  ? 84.934  133.928 133.977 1.00 9.37  ?  398  ILE B CG1  1 
ATOM   10428 C CG2  . ILE B 1 398  ? 82.536  134.561 134.557 1.00 11.53 ?  398  ILE B CG2  1 
ATOM   10429 C CD1  . ILE B 1 398  ? 85.239  133.937 135.456 1.00 11.63 ?  398  ILE B CD1  1 
ATOM   10430 N N    . ALA B 1 399  ? 85.027  133.441 130.766 1.00 11.36 ?  399  ALA B N    1 
ATOM   10431 C CA   . ALA B 1 399  ? 86.055  133.474 129.732 1.00 12.91 ?  399  ALA B CA   1 
ATOM   10432 C C    . ALA B 1 399  ? 85.463  133.867 128.387 1.00 17.55 ?  399  ALA B C    1 
ATOM   10433 O O    . ALA B 1 399  ? 86.116  134.548 127.589 1.00 22.42 ?  399  ALA B O    1 
ATOM   10434 C CB   . ALA B 1 399  ? 86.754  132.126 129.634 1.00 30.00 ?  399  ALA B CB   1 
ATOM   10435 N N    . GLY B 1 400  ? 84.234  133.429 128.110 1.00 17.17 ?  400  GLY B N    1 
ATOM   10436 C CA   . GLY B 1 400  ? 83.530  133.942 126.946 1.00 16.81 ?  400  GLY B CA   1 
ATOM   10437 C C    . GLY B 1 400  ? 83.156  135.406 127.093 1.00 14.03 ?  400  GLY B C    1 
ATOM   10438 O O    . GLY B 1 400  ? 83.225  136.175 126.129 1.00 11.96 ?  400  GLY B O    1 
ATOM   10439 N N    . MET B 1 401  ? 82.755  135.808 128.302 1.00 17.55 ?  401  MET B N    1 
ATOM   10440 C CA   . MET B 1 401  ? 82.286  137.173 128.528 1.00 20.79 ?  401  MET B CA   1 
ATOM   10441 C C    . MET B 1 401  ? 83.398  138.199 128.323 1.00 22.07 ?  401  MET B C    1 
ATOM   10442 O O    . MET B 1 401  ? 83.168  139.252 127.713 1.00 23.77 ?  401  MET B O    1 
ATOM   10443 C CB   . MET B 1 401  ? 81.693  137.287 129.933 1.00 16.14 ?  401  MET B CB   1 
ATOM   10444 C CG   . MET B 1 401  ? 81.631  138.701 130.487 1.00 17.04 ?  401  MET B CG   1 
ATOM   10445 S SD   . MET B 1 401  ? 80.934  138.796 132.149 1.00 37.63 ?  401  MET B SD   1 
ATOM   10446 C CE   . MET B 1 401  ? 79.843  137.374 132.161 1.00 17.91 ?  401  MET B CE   1 
ATOM   10447 N N    . VAL B 1 402  ? 84.606  137.914 128.821 1.00 19.57 ?  402  VAL B N    1 
ATOM   10448 C CA   . VAL B 1 402  ? 85.691  138.891 128.721 1.00 21.16 ?  402  VAL B CA   1 
ATOM   10449 C C    . VAL B 1 402  ? 86.089  139.116 127.263 1.00 22.00 ?  402  VAL B C    1 
ATOM   10450 O O    . VAL B 1 402  ? 86.272  140.260 126.827 1.00 22.39 ?  402  VAL B O    1 
ATOM   10451 C CB   . VAL B 1 402  ? 86.893  138.475 129.596 1.00 21.02 ?  402  VAL B CB   1 
ATOM   10452 C CG1  . VAL B 1 402  ? 87.334  137.044 129.318 1.00 18.62 ?  402  VAL B CG1  1 
ATOM   10453 C CG2  . VAL B 1 402  ? 88.055  139.440 129.404 1.00 21.28 ?  402  VAL B CG2  1 
ATOM   10454 N N    . ILE B 1 403  ? 86.206  138.039 126.479 1.00 21.09 ?  403  ILE B N    1 
ATOM   10455 C CA   . ILE B 1 403  ? 86.571  138.197 125.075 1.00 22.72 ?  403  ILE B CA   1 
ATOM   10456 C C    . ILE B 1 403  ? 85.419  138.812 124.285 1.00 22.67 ?  403  ILE B C    1 
ATOM   10457 O O    . ILE B 1 403  ? 85.649  139.552 123.321 1.00 21.92 ?  403  ILE B O    1 
ATOM   10458 C CB   . ILE B 1 403  ? 87.040  136.853 124.476 1.00 22.26 ?  403  ILE B CB   1 
ATOM   10459 C CG1  . ILE B 1 403  ? 87.487  137.032 123.022 1.00 20.58 ?  403  ILE B CG1  1 
ATOM   10460 C CG2  . ILE B 1 403  ? 85.961  135.791 124.576 1.00 20.16 ?  403  ILE B CG2  1 
ATOM   10461 C CD1  . ILE B 1 403  ? 87.717  135.744 122.284 1.00 20.77 ?  403  ILE B CD1  1 
ATOM   10462 N N    . SER B 1 404  ? 84.169  138.546 124.681 1.00 20.33 ?  404  SER B N    1 
ATOM   10463 C CA   . SER B 1 404  ? 83.041  139.175 124.003 1.00 24.27 ?  404  SER B CA   1 
ATOM   10464 C C    . SER B 1 404  ? 83.012  140.679 124.247 1.00 24.97 ?  404  SER B C    1 
ATOM   10465 O O    . SER B 1 404  ? 82.689  141.454 123.339 1.00 24.16 ?  404  SER B O    1 
ATOM   10466 C CB   . SER B 1 404  ? 81.731  138.533 124.458 1.00 22.29 ?  404  SER B CB   1 
ATOM   10467 O OG   . SER B 1 404  ? 81.338  139.025 125.727 1.00 22.43 ?  404  SER B OG   1 
ATOM   10468 N N    . LEU B 1 405  ? 83.341  141.111 125.463 1.00 23.36 ?  405  LEU B N    1 
ATOM   10469 C CA   . LEU B 1 405  ? 83.267  142.524 125.807 1.00 24.75 ?  405  LEU B CA   1 
ATOM   10470 C C    . LEU B 1 405  ? 84.555  143.294 125.539 1.00 23.53 ?  405  LEU B C    1 
ATOM   10471 O O    . LEU B 1 405  ? 84.544  144.527 125.629 1.00 22.87 ?  405  LEU B O    1 
ATOM   10472 C CB   . LEU B 1 405  ? 82.885  142.690 127.282 1.00 20.72 ?  405  LEU B CB   1 
ATOM   10473 C CG   . LEU B 1 405  ? 81.421  142.428 127.637 1.00 22.26 ?  405  LEU B CG   1 
ATOM   10474 C CD1  . LEU B 1 405  ? 81.188  142.631 129.125 1.00 24.46 ?  405  LEU B CD1  1 
ATOM   10475 C CD2  . LEU B 1 405  ? 80.504  143.325 126.821 1.00 23.29 ?  405  LEU B CD2  1 
ATOM   10476 N N    . PHE B 1 406  ? 85.658  142.621 125.212 1.00 24.57 ?  406  PHE B N    1 
ATOM   10477 C CA   . PHE B 1 406  ? 86.930  143.317 125.053 1.00 25.76 ?  406  PHE B CA   1 
ATOM   10478 C C    . PHE B 1 406  ? 87.513  143.196 123.654 1.00 25.10 ?  406  PHE B C    1 
ATOM   10479 O O    . PHE B 1 406  ? 87.960  144.202 123.088 1.00 25.07 ?  406  PHE B O    1 
ATOM   10480 C CB   . PHE B 1 406  ? 87.940  142.799 126.090 1.00 27.93 ?  406  PHE B CB   1 
ATOM   10481 C CG   . PHE B 1 406  ? 87.818  143.461 127.434 1.00 29.36 ?  406  PHE B CG   1 
ATOM   10482 C CD1  . PHE B 1 406  ? 86.715  143.226 128.239 1.00 25.14 ?  406  PHE B CD1  1 
ATOM   10483 C CD2  . PHE B 1 406  ? 88.801  144.323 127.890 1.00 28.24 ?  406  PHE B CD2  1 
ATOM   10484 C CE1  . PHE B 1 406  ? 86.598  143.834 129.475 1.00 23.46 ?  406  PHE B CE1  1 
ATOM   10485 C CE2  . PHE B 1 406  ? 88.689  144.935 129.125 1.00 26.40 ?  406  PHE B CE2  1 
ATOM   10486 C CZ   . PHE B 1 406  ? 87.586  144.689 129.918 1.00 24.47 ?  406  PHE B CZ   1 
ATOM   10487 N N    . SER B 1 407  ? 87.539  141.991 123.084 1.00 23.08 ?  407  SER B N    1 
ATOM   10488 C CA   . SER B 1 407  ? 88.176  141.794 121.783 1.00 27.62 ?  407  SER B CA   1 
ATOM   10489 C C    . SER B 1 407  ? 87.521  142.542 120.618 1.00 26.02 ?  407  SER B C    1 
ATOM   10490 O O    . SER B 1 407  ? 88.272  143.090 119.792 1.00 22.91 ?  407  SER B O    1 
ATOM   10491 C CB   . SER B 1 407  ? 88.275  140.293 121.481 1.00 28.59 ?  407  SER B CB   1 
ATOM   10492 O OG   . SER B 1 407  ? 89.285  139.684 122.266 1.00 32.13 ?  407  SER B OG   1 
ATOM   10493 N N    . PRO B 1 408  ? 86.186  142.582 120.452 1.00 28.59 ?  408  PRO B N    1 
ATOM   10494 C CA   . PRO B 1 408  ? 85.631  143.372 119.335 1.00 29.00 ?  408  PRO B CA   1 
ATOM   10495 C C    . PRO B 1 408  ? 85.953  144.855 119.406 1.00 24.62 ?  408  PRO B C    1 
ATOM   10496 O O    . PRO B 1 408  ? 86.015  145.513 118.360 1.00 28.28 ?  408  PRO B O    1 
ATOM   10497 C CB   . PRO B 1 408  ? 84.120  143.121 119.443 1.00 28.60 ?  408  PRO B CB   1 
ATOM   10498 C CG   . PRO B 1 408  ? 84.008  141.823 120.124 1.00 28.62 ?  408  PRO B CG   1 
ATOM   10499 C CD   . PRO B 1 408  ? 85.115  141.821 121.127 1.00 26.21 ?  408  PRO B CD   1 
ATOM   10500 N N    . ILE B 1 409  ? 86.145  145.404 120.607 1.00 19.46 ?  409  ILE B N    1 
ATOM   10501 C CA   . ILE B 1 409  ? 86.591  146.788 120.726 1.00 22.97 ?  409  ILE B CA   1 
ATOM   10502 C C    . ILE B 1 409  ? 87.998  146.940 120.161 1.00 23.33 ?  409  ILE B C    1 
ATOM   10503 O O    . ILE B 1 409  ? 88.311  147.931 119.490 1.00 22.27 ?  409  ILE B O    1 
ATOM   10504 C CB   . ILE B 1 409  ? 86.512  147.249 122.193 1.00 23.82 ?  409  ILE B CB   1 
ATOM   10505 C CG1  . ILE B 1 409  ? 85.093  147.064 122.732 1.00 24.91 ?  409  ILE B CG1  1 
ATOM   10506 C CG2  . ILE B 1 409  ? 86.947  148.703 122.327 1.00 20.08 ?  409  ILE B CG2  1 
ATOM   10507 C CD1  . ILE B 1 409  ? 84.902  147.576 124.144 1.00 23.68 ?  409  ILE B CD1  1 
ATOM   10508 N N    . LEU B 1 410  ? 88.862  145.957 120.408 1.00 24.43 ?  410  LEU B N    1 
ATOM   10509 C CA   . LEU B 1 410  ? 90.244  145.996 119.928 1.00 25.80 ?  410  LEU B CA   1 
ATOM   10510 C C    . LEU B 1 410  ? 90.344  145.422 118.513 1.00 23.65 ?  410  LEU B C    1 
ATOM   10511 O O    . LEU B 1 410  ? 90.994  144.409 118.258 1.00 21.43 ?  410  LEU B O    1 
ATOM   10512 C CB   . LEU B 1 410  ? 91.160  145.253 120.895 1.00 20.93 ?  410  LEU B CB   1 
ATOM   10513 C CG   . LEU B 1 410  ? 91.817  146.084 122.001 1.00 24.61 ?  410  LEU B CG   1 
ATOM   10514 C CD1  . LEU B 1 410  ? 92.506  147.306 121.412 1.00 23.52 ?  410  LEU B CD1  1 
ATOM   10515 C CD2  . LEU B 1 410  ? 90.812  146.491 123.071 1.00 20.87 ?  410  LEU B CD2  1 
ATOM   10516 N N    . SER B 1 411  ? 89.674  146.100 117.583 1.00 23.69 ?  411  SER B N    1 
ATOM   10517 C CA   . SER B 1 411  ? 89.800  145.787 116.166 1.00 23.00 ?  411  SER B CA   1 
ATOM   10518 C C    . SER B 1 411  ? 90.984  146.491 115.519 1.00 23.47 ?  411  SER B C    1 
ATOM   10519 O O    . SER B 1 411  ? 91.244  146.270 114.331 1.00 22.24 ?  411  SER B O    1 
ATOM   10520 C CB   . SER B 1 411  ? 88.512  146.155 115.426 1.00 22.60 ?  411  SER B CB   1 
ATOM   10521 O OG   . SER B 1 411  ? 88.634  145.902 114.037 1.00 26.57 ?  411  SER B OG   1 
ATOM   10522 N N    . ARG B 1 412  ? 91.701  147.327 116.270 1.00 26.39 ?  412  ARG B N    1 
ATOM   10523 C CA   . ARG B 1 412  ? 92.884  148.017 115.771 1.00 26.39 ?  412  ARG B CA   1 
ATOM   10524 C C    . ARG B 1 412  ? 94.083  147.092 115.617 1.00 25.87 ?  412  ARG B C    1 
ATOM   10525 O O    . ARG B 1 412  ? 95.102  147.515 115.060 1.00 25.37 ?  412  ARG B O    1 
ATOM   10526 C CB   . ARG B 1 412  ? 93.251  149.179 116.701 1.00 25.86 ?  412  ARG B CB   1 
ATOM   10527 C CG   . ARG B 1 412  ? 92.352  150.409 116.578 1.00 29.26 ?  412  ARG B CG   1 
ATOM   10528 C CD   . ARG B 1 412  ? 91.106  150.300 117.448 1.00 27.17 ?  412  ARG B CD   1 
ATOM   10529 N NE   . ARG B 1 412  ? 90.134  151.346 117.153 1.00 28.20 ?  412  ARG B NE   1 
ATOM   10530 C CZ   . ARG B 1 412  ? 88.905  151.388 117.650 1.00 26.52 ?  412  ARG B CZ   1 
ATOM   10531 N NH1  . ARG B 1 412  ? 88.459  150.451 118.471 1.00 24.94 ?  412  ARG B NH1  1 
ATOM   10532 N NH2  . ARG B 1 412  ? 88.103  152.394 117.314 1.00 27.38 ?  412  ARG B NH2  1 
ATOM   10533 N N    . ILE B 1 413  ? 93.989  145.852 116.106 1.00 26.22 ?  413  ILE B N    1 
ATOM   10534 C CA   . ILE B 1 413  ? 95.083  144.897 115.985 1.00 29.33 ?  413  ILE B CA   1 
ATOM   10535 C C    . ILE B 1 413  ? 95.349  144.506 114.537 1.00 32.45 ?  413  ILE B C    1 
ATOM   10536 O O    . ILE B 1 413  ? 96.477  144.129 114.200 1.00 30.20 ?  413  ILE B O    1 
ATOM   10537 C CB   . ILE B 1 413  ? 94.793  143.645 116.836 1.00 27.42 ?  413  ILE B CB   1 
ATOM   10538 C CG1  . ILE B 1 413  ? 93.473  142.995 116.417 1.00 25.05 ?  413  ILE B CG1  1 
ATOM   10539 C CG2  . ILE B 1 413  ? 94.734  144.006 118.302 1.00 28.04 ?  413  ILE B CG2  1 
ATOM   10540 C CD1  . ILE B 1 413  ? 93.099  141.776 117.239 1.00 23.16 ?  413  ILE B CD1  1 
ATOM   10541 N N    . GLY B 1 414  ? 94.345  144.590 113.667 1.00 27.51 ?  414  GLY B N    1 
ATOM   10542 C CA   . GLY B 1 414  ? 94.463  144.088 112.316 1.00 25.98 ?  414  GLY B CA   1 
ATOM   10543 C C    . GLY B 1 414  ? 94.211  142.604 112.174 1.00 25.28 ?  414  GLY B C    1 
ATOM   10544 O O    . GLY B 1 414  ? 94.401  142.060 111.079 1.00 22.43 ?  414  GLY B O    1 
ATOM   10545 N N    . TYR B 1 415  ? 93.793  141.934 113.244 1.00 25.29 ?  415  TYR B N    1 
ATOM   10546 C CA   . TYR B 1 415  ? 93.503  140.505 113.262 1.00 27.89 ?  415  TYR B CA   1 
ATOM   10547 C C    . TYR B 1 415  ? 92.099  140.269 113.797 1.00 28.73 ?  415  TYR B C    1 
ATOM   10548 O O    . TYR B 1 415  ? 91.883  139.483 114.722 1.00 26.50 ?  415  TYR B O    1 
ATOM   10549 C CB   . TYR B 1 415  ? 94.528  139.738 114.094 1.00 26.49 ?  415  TYR B CB   1 
ATOM   10550 C CG   . TYR B 1 415  ? 95.922  140.318 114.047 1.00 27.14 ?  415  TYR B CG   1 
ATOM   10551 C CD1  . TYR B 1 415  ? 96.663  140.303 112.873 1.00 28.31 ?  415  TYR B CD1  1 
ATOM   10552 C CD2  . TYR B 1 415  ? 96.503  140.870 115.182 1.00 24.37 ?  415  TYR B CD2  1 
ATOM   10553 C CE1  . TYR B 1 415  ? 97.939  140.831 112.826 1.00 30.22 ?  415  TYR B CE1  1 
ATOM   10554 C CE2  . TYR B 1 415  ? 97.780  141.397 115.146 1.00 26.19 ?  415  TYR B CE2  1 
ATOM   10555 C CZ   . TYR B 1 415  ? 98.492  141.376 113.966 1.00 28.87 ?  415  TYR B CZ   1 
ATOM   10556 O OH   . TYR B 1 415  ? 99.763  141.900 113.924 1.00 27.84 ?  415  TYR B OH   1 
ATOM   10557 N N    . GLY B 1 416  ? 91.131  140.993 113.229 1.00 26.31 ?  416  GLY B N    1 
ATOM   10558 C CA   . GLY B 1 416  ? 89.744  140.957 113.658 1.00 22.26 ?  416  GLY B CA   1 
ATOM   10559 C C    . GLY B 1 416  ? 89.145  139.569 113.744 1.00 22.68 ?  416  GLY B C    1 
ATOM   10560 O O    . GLY B 1 416  ? 89.316  138.748 112.838 1.00 23.66 ?  416  GLY B O    1 
ATOM   10561 N N    . LEU B 1 417  ? 88.452  139.301 114.848 1.00 18.77 ?  417  LEU B N    1 
ATOM   10562 C CA   . LEU B 1 417  ? 87.996  137.953 115.149 1.00 17.89 ?  417  LEU B CA   1 
ATOM   10563 C C    . LEU B 1 417  ? 86.913  137.502 114.177 1.00 19.28 ?  417  LEU B C    1 
ATOM   10564 O O    . LEU B 1 417  ? 86.017  138.268 113.813 1.00 19.77 ?  417  LEU B O    1 
ATOM   10565 C CB   . LEU B 1 417  ? 87.479  137.881 116.587 1.00 17.85 ?  417  LEU B CB   1 
ATOM   10566 C CG   . LEU B 1 417  ? 86.333  138.819 116.983 1.00 22.44 ?  417  LEU B CG   1 
ATOM   10567 C CD1  . LEU B 1 417  ? 85.008  138.069 117.062 1.00 19.07 ?  417  LEU B CD1  1 
ATOM   10568 C CD2  . LEU B 1 417  ? 86.634  139.523 118.293 1.00 21.08 ?  417  LEU B CD2  1 
ATOM   10569 N N    . THR B 1 418  ? 87.017  136.251 113.742 1.00 17.87 ?  418  THR B N    1 
ATOM   10570 C CA   . THR B 1 418  ? 85.949  135.609 113.000 1.00 19.77 ?  418  THR B CA   1 
ATOM   10571 C C    . THR B 1 418  ? 85.026  134.896 113.982 1.00 21.28 ?  418  THR B C    1 
ATOM   10572 O O    . THR B 1 418  ? 85.180  134.993 115.202 1.00 22.59 ?  418  THR B O    1 
ATOM   10573 C CB   . THR B 1 418  ? 86.519  134.638 111.967 1.00 20.87 ?  418  THR B CB   1 
ATOM   10574 O OG1  . THR B 1 418  ? 86.848  133.398 112.606 1.00 21.34 ?  418  THR B OG1  1 
ATOM   10575 C CG2  . THR B 1 418  ? 87.770  135.219 111.326 1.00 19.95 ?  418  THR B CG2  1 
ATOM   10576 N N    . TRP B 1 419  ? 84.044  134.169 113.450 1.00 25.12 ?  419  TRP B N    1 
ATOM   10577 C CA   . TRP B 1 419  ? 83.197  133.369 114.325 1.00 26.99 ?  419  TRP B CA   1 
ATOM   10578 C C    . TRP B 1 419  ? 83.930  132.135 114.831 1.00 25.84 ?  419  TRP B C    1 
ATOM   10579 O O    . TRP B 1 419  ? 83.691  131.694 115.960 1.00 26.93 ?  419  TRP B O    1 
ATOM   10580 C CB   . TRP B 1 419  ? 81.914  132.968 113.599 1.00 26.46 ?  419  TRP B CB   1 
ATOM   10581 C CG   . TRP B 1 419  ? 80.748  132.827 114.518 1.00 27.40 ?  419  TRP B CG   1 
ATOM   10582 C CD1  . TRP B 1 419  ? 80.393  131.720 115.232 1.00 25.39 ?  419  TRP B CD1  1 
ATOM   10583 C CD2  . TRP B 1 419  ? 79.792  133.840 114.846 1.00 29.15 ?  419  TRP B CD2  1 
ATOM   10584 N NE1  . TRP B 1 419  ? 79.267  131.977 115.974 1.00 27.20 ?  419  TRP B NE1  1 
ATOM   10585 C CE2  . TRP B 1 419  ? 78.879  133.273 115.756 1.00 28.31 ?  419  TRP B CE2  1 
ATOM   10586 C CE3  . TRP B 1 419  ? 79.617  135.170 114.454 1.00 25.23 ?  419  TRP B CE3  1 
ATOM   10587 C CZ2  . TRP B 1 419  ? 77.806  133.990 116.280 1.00 26.20 ?  419  TRP B CZ2  1 
ATOM   10588 C CZ3  . TRP B 1 419  ? 78.552  135.880 114.974 1.00 26.47 ?  419  TRP B CZ3  1 
ATOM   10589 C CH2  . TRP B 1 419  ? 77.660  135.289 115.877 1.00 28.13 ?  419  TRP B CH2  1 
ATOM   10590 N N    . ARG B 1 420  ? 84.819  131.566 114.015 1.00 20.35 ?  420  ARG B N    1 
ATOM   10591 C CA   . ARG B 1 420  ? 85.536  130.360 114.416 1.00 25.09 ?  420  ARG B CA   1 
ATOM   10592 C C    . ARG B 1 420  ? 86.626  130.666 115.439 1.00 26.73 ?  420  ARG B C    1 
ATOM   10593 O O    . ARG B 1 420  ? 86.775  129.942 116.435 1.00 24.90 ?  420  ARG B O    1 
ATOM   10594 C CB   . ARG B 1 420  ? 86.131  129.683 113.179 1.00 25.45 ?  420  ARG B CB   1 
ATOM   10595 C CG   . ARG B 1 420  ? 87.012  128.483 113.482 1.00 25.02 ?  420  ARG B CG   1 
ATOM   10596 C CD   . ARG B 1 420  ? 88.262  128.459 112.608 1.00 22.82 ?  420  ARG B CD   1 
ATOM   10597 N NE   . ARG B 1 420  ? 88.033  127.879 111.290 1.00 22.39 ?  420  ARG B NE   1 
ATOM   10598 C CZ   . ARG B 1 420  ? 88.976  127.721 110.370 1.00 24.91 ?  420  ARG B CZ   1 
ATOM   10599 N NH1  . ARG B 1 420  ? 90.225  128.100 110.588 1.00 22.19 ?  420  ARG B NH1  1 
ATOM   10600 N NH2  . ARG B 1 420  ? 88.660  127.164 109.204 1.00 26.71 ?  420  ARG B NH2  1 
ATOM   10601 N N    . ASN B 1 421  ? 87.394  131.737 115.209 1.00 23.03 ?  421  ASN B N    1 
ATOM   10602 C CA   . ASN B 1 421  ? 88.583  132.005 116.015 1.00 20.95 ?  421  ASN B CA   1 
ATOM   10603 C C    . ASN B 1 421  ? 88.227  132.383 117.447 1.00 20.76 ?  421  ASN B C    1 
ATOM   10604 O O    . ASN B 1 421  ? 88.913  131.968 118.389 1.00 24.64 ?  421  ASN B O    1 
ATOM   10605 C CB   . ASN B 1 421  ? 89.415  133.110 115.368 1.00 21.41 ?  421  ASN B CB   1 
ATOM   10606 C CG   . ASN B 1 421  ? 90.096  132.654 114.096 1.00 22.98 ?  421  ASN B CG   1 
ATOM   10607 O OD1  . ASN B 1 421  ? 90.086  131.469 113.764 1.00 21.36 ?  421  ASN B OD1  1 
ATOM   10608 N ND2  . ASN B 1 421  ? 90.699  133.594 113.378 1.00 19.57 ?  421  ASN B ND2  1 
ATOM   10609 N N    . ALA B 1 422  ? 87.173  133.183 117.629 1.00 17.36 ?  422  ALA B N    1 
ATOM   10610 C CA   . ALA B 1 422  ? 86.783  133.596 118.973 1.00 19.58 ?  422  ALA B CA   1 
ATOM   10611 C C    . ALA B 1 422  ? 86.368  132.399 119.818 1.00 23.48 ?  422  ALA B C    1 
ATOM   10612 O O    . ALA B 1 422  ? 86.770  132.279 120.981 1.00 21.73 ?  422  ALA B O    1 
ATOM   10613 C CB   . ALA B 1 422  ? 85.652  134.621 118.901 1.00 19.41 ?  422  ALA B CB   1 
ATOM   10614 N N    . VAL B 1 423  ? 85.588  131.486 119.237 1.00 24.02 ?  423  VAL B N    1 
ATOM   10615 C CA   . VAL B 1 423  ? 85.155  130.306 119.977 1.00 21.36 ?  423  VAL B CA   1 
ATOM   10616 C C    . VAL B 1 423  ? 86.328  129.364 120.229 1.00 21.18 ?  423  VAL B C    1 
ATOM   10617 O O    . VAL B 1 423  ? 86.412  128.739 121.294 1.00 25.12 ?  423  VAL B O    1 
ATOM   10618 C CB   . VAL B 1 423  ? 83.997  129.609 119.242 1.00 22.28 ?  423  VAL B CB   1 
ATOM   10619 C CG1  . VAL B 1 423  ? 83.432  128.480 120.085 1.00 20.39 ?  423  VAL B CG1  1 
ATOM   10620 C CG2  . VAL B 1 423  ? 82.906  130.612 118.925 1.00 21.54 ?  423  VAL B CG2  1 
ATOM   10621 N N    . ILE B 1 424  ? 87.254  129.250 119.269 1.00 18.85 ?  424  ILE B N    1 
ATOM   10622 C CA   . ILE B 1 424  ? 88.433  128.409 119.483 1.00 21.35 ?  424  ILE B CA   1 
ATOM   10623 C C    . ILE B 1 424  ? 89.270  128.937 120.643 1.00 18.78 ?  424  ILE B C    1 
ATOM   10624 O O    . ILE B 1 424  ? 89.667  128.182 121.539 1.00 20.51 ?  424  ILE B O    1 
ATOM   10625 C CB   . ILE B 1 424  ? 89.268  128.298 118.193 1.00 22.33 ?  424  ILE B CB   1 
ATOM   10626 C CG1  . ILE B 1 424  ? 88.689  127.230 117.269 1.00 23.13 ?  424  ILE B CG1  1 
ATOM   10627 C CG2  . ILE B 1 424  ? 90.725  127.983 118.504 1.00 17.14 ?  424  ILE B CG2  1 
ATOM   10628 C CD1  . ILE B 1 424  ? 89.381  127.163 115.933 1.00 20.99 ?  424  ILE B CD1  1 
ATOM   10629 N N    . MET B 1 425  ? 89.524  130.245 120.667 1.00 15.51 ?  425  MET B N    1 
ATOM   10630 C CA   . MET B 1 425  ? 90.387  130.783 121.709 1.00 15.36 ?  425  MET B CA   1 
ATOM   10631 C C    . MET B 1 425  ? 89.656  131.019 123.025 1.00 17.88 ?  425  MET B C    1 
ATOM   10632 O O    . MET B 1 425  ? 90.314  131.281 124.037 1.00 24.92 ?  425  MET B O    1 
ATOM   10633 C CB   . MET B 1 425  ? 91.058  132.075 121.232 1.00 19.43 ?  425  MET B CB   1 
ATOM   10634 C CG   . MET B 1 425  ? 90.270  133.339 121.491 1.00 21.16 ?  425  MET B CG   1 
ATOM   10635 S SD   . MET B 1 425  ? 90.931  134.773 120.616 1.00 25.73 ?  425  MET B SD   1 
ATOM   10636 C CE   . MET B 1 425  ? 91.486  134.027 119.085 1.00 20.01 ?  425  MET B CE   1 
ATOM   10637 N N    . THR B 1 426  ? 88.325  130.923 123.048 1.00 11.49 ?  426  THR B N    1 
ATOM   10638 C CA   . THR B 1 426  ? 87.596  130.935 124.309 1.00 18.63 ?  426  THR B CA   1 
ATOM   10639 C C    . THR B 1 426  ? 87.283  129.539 124.837 1.00 16.46 ?  426  THR B C    1 
ATOM   10640 O O    . THR B 1 426  ? 86.919  129.408 126.010 1.00 12.07 ?  426  THR B O    1 
ATOM   10641 C CB   . THR B 1 426  ? 86.292  131.737 124.174 1.00 19.41 ?  426  THR B CB   1 
ATOM   10642 O OG1  . THR B 1 426  ? 85.890  132.213 125.464 1.00 14.46 ?  426  THR B OG1  1 
ATOM   10643 C CG2  . THR B 1 426  ? 85.177  130.881 123.597 1.00 15.26 ?  426  THR B CG2  1 
ATOM   10644 N N    . TRP B 1 427  ? 87.419  128.499 124.012 1.00 21.51 ?  427  TRP B N    1 
ATOM   10645 C CA   . TRP B 1 427  ? 87.171  127.127 124.441 1.00 12.92 ?  427  TRP B CA   1 
ATOM   10646 C C    . TRP B 1 427  ? 88.443  126.383 124.814 1.00 14.77 ?  427  TRP B C    1 
ATOM   10647 O O    . TRP B 1 427  ? 88.432  125.581 125.752 1.00 18.13 ?  427  TRP B O    1 
ATOM   10648 C CB   . TRP B 1 427  ? 86.436  126.350 123.344 1.00 6.79  ?  427  TRP B CB   1 
ATOM   10649 C CG   . TRP B 1 427  ? 86.175  124.911 123.690 1.00 8.69  ?  427  TRP B CG   1 
ATOM   10650 C CD1  . TRP B 1 427  ? 86.739  123.814 123.107 1.00 12.70 ?  427  TRP B CD1  1 
ATOM   10651 C CD2  . TRP B 1 427  ? 85.278  124.415 124.692 1.00 11.04 ?  427  TRP B CD2  1 
ATOM   10652 N NE1  . TRP B 1 427  ? 86.253  122.667 123.686 1.00 11.40 ?  427  TRP B NE1  1 
ATOM   10653 C CE2  . TRP B 1 427  ? 85.354  123.008 124.661 1.00 10.10 ?  427  TRP B CE2  1 
ATOM   10654 C CE3  . TRP B 1 427  ? 84.419  125.023 125.612 1.00 13.22 ?  427  TRP B CE3  1 
ATOM   10655 C CZ2  . TRP B 1 427  ? 84.605  122.202 125.514 1.00 9.84  ?  427  TRP B CZ2  1 
ATOM   10656 C CZ3  . TRP B 1 427  ? 83.677  124.219 126.458 1.00 9.95  ?  427  TRP B CZ3  1 
ATOM   10657 C CH2  . TRP B 1 427  ? 83.775  122.825 126.403 1.00 9.42  ?  427  TRP B CH2  1 
ATOM   10658 N N    . GLY B 1 428  ? 89.542  126.630 124.108 1.00 11.89 ?  428  GLY B N    1 
ATOM   10659 C CA   . GLY B 1 428  ? 90.793  125.964 124.411 1.00 7.84  ?  428  GLY B CA   1 
ATOM   10660 C C    . GLY B 1 428  ? 91.599  126.662 125.486 1.00 12.66 ?  428  GLY B C    1 
ATOM   10661 O O    . GLY B 1 428  ? 92.812  126.840 125.346 1.00 17.55 ?  428  GLY B O    1 
ATOM   10662 N N    . GLY B 1 429  ? 90.932  127.071 126.562 1.00 14.68 ?  429  GLY B N    1 
ATOM   10663 C CA   . GLY B 1 429  ? 91.605  127.679 127.691 1.00 11.26 ?  429  GLY B CA   1 
ATOM   10664 C C    . GLY B 1 429  ? 92.066  126.656 128.706 1.00 11.73 ?  429  GLY B C    1 
ATOM   10665 O O    . GLY B 1 429  ? 91.493  126.551 129.794 1.00 11.49 ?  429  GLY B O    1 
ATOM   10666 N N    . LEU B 1 430  ? 93.092  125.887 128.356 1.00 12.84 ?  430  LEU B N    1 
ATOM   10667 C CA   . LEU B 1 430  ? 93.605  124.868 129.258 1.00 8.91  ?  430  LEU B CA   1 
ATOM   10668 C C    . LEU B 1 430  ? 94.324  125.505 130.441 1.00 10.13 ?  430  LEU B C    1 
ATOM   10669 O O    . LEU B 1 430  ? 94.971  126.547 130.317 1.00 20.33 ?  430  LEU B O    1 
ATOM   10670 C CB   . LEU B 1 430  ? 94.561  123.930 128.521 1.00 9.02  ?  430  LEU B CB   1 
ATOM   10671 C CG   . LEU B 1 430  ? 93.950  122.901 127.572 1.00 9.94  ?  430  LEU B CG   1 
ATOM   10672 C CD1  . LEU B 1 430  ? 95.038  122.038 126.954 1.00 11.15 ?  430  LEU B CD1  1 
ATOM   10673 C CD2  . LEU B 1 430  ? 92.933  122.043 128.302 1.00 14.11 ?  430  LEU B CD2  1 
ATOM   10674 N N    . ARG B 1 431  ? 94.194  124.871 131.599 1.00 2.15  ?  431  ARG B N    1 
ATOM   10675 C CA   . ARG B 1 431  ? 94.950  125.266 132.774 1.00 2.86  ?  431  ARG B CA   1 
ATOM   10676 C C    . ARG B 1 431  ? 96.230  124.442 132.860 1.00 7.72  ?  431  ARG B C    1 
ATOM   10677 O O    . ARG B 1 431  ? 96.318  123.331 132.331 1.00 11.88 ?  431  ARG B O    1 
ATOM   10678 C CB   . ARG B 1 431  ? 94.110  125.092 134.039 1.00 6.30  ?  431  ARG B CB   1 
ATOM   10679 C CG   . ARG B 1 431  ? 92.749  125.766 133.971 1.00 1.60  ?  431  ARG B CG   1 
ATOM   10680 C CD   . ARG B 1 431  ? 92.802  127.183 134.506 1.00 0.00  ?  431  ARG B CD   1 
ATOM   10681 N NE   . ARG B 1 431  ? 91.491  127.822 134.495 1.00 9.38  ?  431  ARG B NE   1 
ATOM   10682 C CZ   . ARG B 1 431  ? 91.068  128.646 133.547 1.00 9.08  ?  431  ARG B CZ   1 
ATOM   10683 N NH1  . ARG B 1 431  ? 91.821  128.939 132.500 1.00 8.67  ?  431  ARG B NH1  1 
ATOM   10684 N NH2  . ARG B 1 431  ? 89.858  129.187 133.649 1.00 5.15  ?  431  ARG B NH2  1 
ATOM   10685 N N    . GLY B 1 432  ? 97.231  125.000 133.536 1.00 7.93  ?  432  GLY B N    1 
ATOM   10686 C CA   . GLY B 1 432  ? 98.556  124.423 133.550 1.00 12.07 ?  432  GLY B CA   1 
ATOM   10687 C C    . GLY B 1 432  ? 99.101  124.272 134.957 1.00 4.69  ?  432  GLY B C    1 
ATOM   10688 O O    . GLY B 1 432  ? 98.364  124.050 135.918 1.00 1.71  ?  432  GLY B O    1 
ATOM   10689 N N    . ALA B 1 433  ? 100.425 124.389 135.059 1.00 2.80  ?  433  ALA B N    1 
ATOM   10690 C CA   . ALA B 1 433  ? 101.133 124.152 136.308 1.00 0.00  ?  433  ALA B CA   1 
ATOM   10691 C C    . ALA B 1 433  ? 101.379 125.414 137.120 1.00 2.92  ?  433  ALA B C    1 
ATOM   10692 O O    . ALA B 1 433  ? 101.806 125.307 138.273 1.00 10.54 ?  433  ALA B O    1 
ATOM   10693 C CB   . ALA B 1 433  ? 102.472 123.465 136.035 1.00 0.00  ?  433  ALA B CB   1 
ATOM   10694 N N    . VAL B 1 434  ? 101.131 126.598 136.559 1.00 3.00  ?  434  VAL B N    1 
ATOM   10695 C CA   . VAL B 1 434  ? 101.277 127.825 137.336 1.00 0.00  ?  434  VAL B CA   1 
ATOM   10696 C C    . VAL B 1 434  ? 100.228 127.877 138.441 1.00 7.94  ?  434  VAL B C    1 
ATOM   10697 O O    . VAL B 1 434  ? 100.546 128.115 139.614 1.00 14.08 ?  434  VAL B O    1 
ATOM   10698 C CB   . VAL B 1 434  ? 101.191 129.055 136.415 1.00 0.00  ?  434  VAL B CB   1 
ATOM   10699 C CG1  . VAL B 1 434  ? 100.961 130.317 137.228 1.00 1.97  ?  434  VAL B CG1  1 
ATOM   10700 C CG2  . VAL B 1 434  ? 102.452 129.178 135.576 1.00 0.00  ?  434  VAL B CG2  1 
ATOM   10701 N N    . GLY B 1 435  ? 98.967  127.626 138.086 1.00 0.00  ?  435  GLY B N    1 
ATOM   10702 C CA   . GLY B 1 435  ? 97.914  127.602 139.087 1.00 0.00  ?  435  GLY B CA   1 
ATOM   10703 C C    . GLY B 1 435  ? 98.066  126.457 140.068 1.00 2.66  ?  435  GLY B C    1 
ATOM   10704 O O    . GLY B 1 435  ? 97.762  126.602 141.255 1.00 1.88  ?  435  GLY B O    1 
ATOM   10705 N N    . LEU B 1 436  ? 98.545  125.305 139.590 1.00 1.42  ?  436  LEU B N    1 
ATOM   10706 C CA   . LEU B 1 436  ? 98.809  124.182 140.484 1.00 0.03  ?  436  LEU B CA   1 
ATOM   10707 C C    . LEU B 1 436  ? 99.908  124.520 141.482 1.00 3.94  ?  436  LEU B C    1 
ATOM   10708 O O    . LEU B 1 436  ? 99.804  124.183 142.666 1.00 9.53  ?  436  LEU B O    1 
ATOM   10709 C CB   . LEU B 1 436  ? 99.186  122.941 139.675 1.00 0.00  ?  436  LEU B CB   1 
ATOM   10710 C CG   . LEU B 1 436  ? 98.052  122.189 138.977 1.00 0.00  ?  436  LEU B CG   1 
ATOM   10711 C CD1  . LEU B 1 436  ? 98.586  120.936 138.311 1.00 0.00  ?  436  LEU B CD1  1 
ATOM   10712 C CD2  . LEU B 1 436  ? 96.949  121.847 139.962 1.00 0.00  ?  436  LEU B CD2  1 
ATOM   10713 N N    . ALA B 1 437  ? 100.963 125.200 141.024 1.00 0.00  ?  437  ALA B N    1 
ATOM   10714 C CA   . ALA B 1 437  ? 102.036 125.619 141.919 1.00 0.00  ?  437  ALA B CA   1 
ATOM   10715 C C    . ALA B 1 437  ? 101.546 126.634 142.945 1.00 0.00  ?  437  ALA B C    1 
ATOM   10716 O O    . ALA B 1 437  ? 101.929 126.568 144.119 1.00 13.88 ?  437  ALA B O    1 
ATOM   10717 C CB   . ALA B 1 437  ? 103.197 126.192 141.109 1.00 0.00  ?  437  ALA B CB   1 
ATOM   10718 N N    . LEU B 1 438  ? 100.706 127.583 142.522 1.00 3.08  ?  438  LEU B N    1 
ATOM   10719 C CA   . LEU B 1 438  ? 100.158 128.548 143.474 1.00 0.00  ?  438  LEU B CA   1 
ATOM   10720 C C    . LEU B 1 438  ? 99.259  127.870 144.502 1.00 2.09  ?  438  LEU B C    1 
ATOM   10721 O O    . LEU B 1 438  ? 99.285  128.223 145.689 1.00 2.07  ?  438  LEU B O    1 
ATOM   10722 C CB   . LEU B 1 438  ? 99.395  129.647 142.738 1.00 0.00  ?  438  LEU B CB   1 
ATOM   10723 C CG   . LEU B 1 438  ? 100.201 130.479 141.741 1.00 0.00  ?  438  LEU B CG   1 
ATOM   10724 C CD1  . LEU B 1 438  ? 99.341  131.571 141.124 1.00 0.64  ?  438  LEU B CD1  1 
ATOM   10725 C CD2  . LEU B 1 438  ? 101.444 131.051 142.385 1.00 0.00  ?  438  LEU B CD2  1 
ATOM   10726 N N    . ALA B 1 439  ? 98.459  126.892 144.068 1.00 0.00  ?  439  ALA B N    1 
ATOM   10727 C CA   . ALA B 1 439  ? 97.628  126.140 145.003 1.00 0.00  ?  439  ALA B CA   1 
ATOM   10728 C C    . ALA B 1 439  ? 98.480  125.334 145.975 1.00 0.00  ?  439  ALA B C    1 
ATOM   10729 O O    . ALA B 1 439  ? 98.133  125.204 147.154 1.00 3.87  ?  439  ALA B O    1 
ATOM   10730 C CB   . ALA B 1 439  ? 96.678  125.224 144.235 1.00 0.00  ?  439  ALA B CB   1 
ATOM   10731 N N    . LEU B 1 440  ? 99.601  124.790 145.494 1.00 0.44  ?  440  LEU B N    1 
ATOM   10732 C CA   . LEU B 1 440  ? 100.541 124.091 146.366 1.00 0.00  ?  440  LEU B CA   1 
ATOM   10733 C C    . LEU B 1 440  ? 101.130 125.031 147.408 1.00 0.00  ?  440  LEU B C    1 
ATOM   10734 O O    . LEU B 1 440  ? 101.280 124.661 148.579 1.00 6.33  ?  440  LEU B O    1 
ATOM   10735 C CB   . LEU B 1 440  ? 101.657 123.478 145.525 1.00 2.42  ?  440  LEU B CB   1 
ATOM   10736 C CG   . LEU B 1 440  ? 101.314 122.222 144.730 1.00 0.00  ?  440  LEU B CG   1 
ATOM   10737 C CD1  . LEU B 1 440  ? 102.545 121.699 144.030 1.00 0.00  ?  440  LEU B CD1  1 
ATOM   10738 C CD2  . LEU B 1 440  ? 100.732 121.179 145.642 1.00 0.00  ?  440  LEU B CD2  1 
ATOM   10739 N N    . VAL B 1 441  ? 101.479 126.249 146.990 1.00 6.33  ?  441  VAL B N    1 
ATOM   10740 C CA   . VAL B 1 441  ? 102.022 127.243 147.913 1.00 0.00  ?  441  VAL B CA   1 
ATOM   10741 C C    . VAL B 1 441  ? 100.993 127.601 148.979 1.00 0.00  ?  441  VAL B C    1 
ATOM   10742 O O    . VAL B 1 441  ? 101.317 127.696 150.171 1.00 10.50 ?  441  VAL B O    1 
ATOM   10743 C CB   . VAL B 1 441  ? 102.493 128.484 147.130 1.00 0.00  ?  441  VAL B CB   1 
ATOM   10744 C CG1  . VAL B 1 441  ? 102.714 129.663 148.058 1.00 0.00  ?  441  VAL B CG1  1 
ATOM   10745 C CG2  . VAL B 1 441  ? 103.756 128.168 146.349 1.00 1.47  ?  441  VAL B CG2  1 
ATOM   10746 N N    . VAL B 1 442  ? 99.736  127.792 148.569 1.00 9.50  ?  442  VAL B N    1 
ATOM   10747 C CA   . VAL B 1 442  ? 98.670  128.101 149.522 1.00 4.07  ?  442  VAL B CA   1 
ATOM   10748 C C    . VAL B 1 442  ? 98.466  126.948 150.498 1.00 0.00  ?  442  VAL B C    1 
ATOM   10749 O O    . VAL B 1 442  ? 98.306  127.160 151.707 1.00 4.59  ?  442  VAL B O    1 
ATOM   10750 C CB   . VAL B 1 442  ? 97.367  128.442 148.775 1.00 0.16  ?  442  VAL B CB   1 
ATOM   10751 C CG1  . VAL B 1 442  ? 96.196  128.513 149.738 1.00 4.54  ?  442  VAL B CG1  1 
ATOM   10752 C CG2  . VAL B 1 442  ? 97.515  129.750 148.045 1.00 0.85  ?  442  VAL B CG2  1 
ATOM   10753 N N    . GLU B 1 443  ? 98.472  125.711 149.992 1.00 7.22  ?  443  GLU B N    1 
ATOM   10754 C CA   . GLU B 1 443  ? 98.279  124.549 150.854 1.00 2.88  ?  443  GLU B CA   1 
ATOM   10755 C C    . GLU B 1 443  ? 99.419  124.400 151.853 1.00 5.10  ?  443  GLU B C    1 
ATOM   10756 O O    . GLU B 1 443  ? 99.194  124.011 153.005 1.00 9.79  ?  443  GLU B O    1 
ATOM   10757 C CB   . GLU B 1 443  ? 98.143  123.287 150.005 1.00 1.80  ?  443  GLU B CB   1 
ATOM   10758 C CG   . GLU B 1 443  ? 97.271  122.214 150.628 1.00 8.56  ?  443  GLU B CG   1 
ATOM   10759 C CD   . GLU B 1 443  ? 98.055  120.988 151.045 1.00 15.70 ?  443  GLU B CD   1 
ATOM   10760 O OE1  . GLU B 1 443  ? 99.193  120.811 150.560 1.00 13.31 ?  443  GLU B OE1  1 
ATOM   10761 O OE2  . GLU B 1 443  ? 97.532  120.200 151.860 1.00 16.86 ?  443  GLU B OE2  1 
ATOM   10762 N N    . ASN B 1 444  ? 100.651 124.689 151.429 1.00 5.92  ?  444  ASN B N    1 
ATOM   10763 C CA   . ASN B 1 444  ? 101.777 124.651 152.357 1.00 1.19  ?  444  ASN B CA   1 
ATOM   10764 C C    . ASN B 1 444  ? 101.674 125.749 153.409 1.00 1.99  ?  444  ASN B C    1 
ATOM   10765 O O    . ASN B 1 444  ? 101.949 125.510 154.590 1.00 3.45  ?  444  ASN B O    1 
ATOM   10766 C CB   . ASN B 1 444  ? 103.095 124.763 151.593 1.00 4.33  ?  444  ASN B CB   1 
ATOM   10767 C CG   . ASN B 1 444  ? 103.702 123.410 151.279 1.00 10.36 ?  444  ASN B CG   1 
ATOM   10768 O OD1  . ASN B 1 444  ? 103.655 122.944 150.141 1.00 6.98  ?  444  ASN B OD1  1 
ATOM   10769 N ND2  . ASN B 1 444  ? 104.279 122.772 152.291 1.00 9.32  ?  444  ASN B ND2  1 
ATOM   10770 N N    . LEU B 1 445  ? 101.278 126.960 153.004 1.00 2.19  ?  445  LEU B N    1 
ATOM   10771 C CA   . LEU B 1 445  ? 101.237 128.071 153.952 1.00 0.00  ?  445  LEU B CA   1 
ATOM   10772 C C    . LEU B 1 445  ? 100.069 127.960 154.926 1.00 4.70  ?  445  LEU B C    1 
ATOM   10773 O O    . LEU B 1 445  ? 100.150 128.487 156.041 1.00 14.05 ?  445  LEU B O    1 
ATOM   10774 C CB   . LEU B 1 445  ? 101.167 129.404 153.206 1.00 0.00  ?  445  LEU B CB   1 
ATOM   10775 C CG   . LEU B 1 445  ? 102.411 129.850 152.439 1.00 0.01  ?  445  LEU B CG   1 
ATOM   10776 C CD1  . LEU B 1 445  ? 102.189 131.216 151.812 1.00 3.40  ?  445  LEU B CD1  1 
ATOM   10777 C CD2  . LEU B 1 445  ? 103.622 129.871 153.352 1.00 0.00  ?  445  LEU B CD2  1 
ATOM   10778 N N    . ALA B 1 446  ? 98.982  127.293 154.528 1.00 7.11  ?  446  ALA B N    1 
ATOM   10779 C CA   . ALA B 1 446  ? 97.780  127.264 155.358 1.00 4.20  ?  446  ALA B CA   1 
ATOM   10780 C C    . ALA B 1 446  ? 98.000  126.490 156.653 1.00 7.67  ?  446  ALA B C    1 
ATOM   10781 O O    . ALA B 1 446  ? 97.589  126.941 157.728 1.00 9.06  ?  446  ALA B O    1 
ATOM   10782 C CB   . ALA B 1 446  ? 96.615  126.666 154.571 1.00 9.57  ?  446  ALA B CB   1 
ATOM   10783 N N    . GLY B 1 447  ? 98.635  125.337 156.575 1.00 19.55 ?  447  GLY B N    1 
ATOM   10784 C CA   . GLY B 1 447  ? 98.861  124.510 157.758 1.00 20.84 ?  447  GLY B CA   1 
ATOM   10785 C C    . GLY B 1 447  ? 97.767  123.461 157.916 1.00 23.93 ?  447  GLY B C    1 
ATOM   10786 O O    . GLY B 1 447  ? 97.542  122.662 157.011 1.00 21.55 ?  447  GLY B O    1 
ATOM   10787 N N    . ASN B 1 448  ? 97.097  123.472 159.066 1.00 26.97 ?  448  ASN B N    1 
ATOM   10788 C CA   . ASN B 1 448  ? 96.014  122.539 159.345 1.00 25.07 ?  448  ASN B CA   1 
ATOM   10789 C C    . ASN B 1 448  ? 94.642  123.091 158.982 1.00 27.70 ?  448  ASN B C    1 
ATOM   10790 O O    . ASN B 1 448  ? 93.641  122.393 159.174 1.00 29.09 ?  448  ASN B O    1 
ATOM   10791 C CB   . ASN B 1 448  ? 96.030  122.138 160.824 1.00 23.77 ?  448  ASN B CB   1 
ATOM   10792 C CG   . ASN B 1 448  ? 96.871  120.905 161.084 1.00 26.53 ?  448  ASN B CG   1 
ATOM   10793 O OD1  . ASN B 1 448  ? 96.520  119.801 160.667 1.00 29.63 ?  448  ASN B OD1  1 
ATOM   10794 N ND2  . ASN B 1 448  ? 97.989  121.087 161.777 1.00 27.05 ?  448  ASN B ND2  1 
ATOM   10795 N N    . ASP B 1 449  ? 94.568  124.317 158.472 1.00 22.28 ?  449  ASP B N    1 
ATOM   10796 C CA   . ASP B 1 449  ? 93.287  124.899 158.100 1.00 16.40 ?  449  ASP B CA   1 
ATOM   10797 C C    . ASP B 1 449  ? 92.758  124.268 156.817 1.00 18.33 ?  449  ASP B C    1 
ATOM   10798 O O    . ASP B 1 449  ? 93.517  123.779 155.977 1.00 18.47 ?  449  ASP B O    1 
ATOM   10799 C CB   . ASP B 1 449  ? 93.419  126.411 157.927 1.00 18.00 ?  449  ASP B CB   1 
ATOM   10800 C CG   . ASP B 1 449  ? 94.255  127.051 159.016 1.00 22.65 ?  449  ASP B CG   1 
ATOM   10801 O OD1  . ASP B 1 449  ? 94.263  126.520 160.146 1.00 23.14 ?  449  ASP B OD1  1 
ATOM   10802 O OD2  . ASP B 1 449  ? 94.903  128.083 158.743 1.00 21.45 ?  449  ASP B OD2  1 
ATOM   10803 N N    . VAL B 1 450  ? 91.429  124.288 156.670 1.00 22.11 ?  450  VAL B N    1 
ATOM   10804 C CA   . VAL B 1 450  ? 90.786  123.664 155.515 1.00 20.94 ?  450  VAL B CA   1 
ATOM   10805 C C    . VAL B 1 450  ? 90.864  124.509 154.254 1.00 17.88 ?  450  VAL B C    1 
ATOM   10806 O O    . VAL B 1 450  ? 90.477  124.030 153.179 1.00 19.18 ?  450  VAL B O    1 
ATOM   10807 C CB   . VAL B 1 450  ? 89.308  123.351 155.814 1.00 19.34 ?  450  VAL B CB   1 
ATOM   10808 C CG1  . VAL B 1 450  ? 89.190  122.499 157.068 1.00 21.94 ?  450  VAL B CG1  1 
ATOM   10809 C CG2  . VAL B 1 450  ? 88.512  124.637 155.966 1.00 16.12 ?  450  VAL B CG2  1 
ATOM   10810 N N    . ILE B 1 451  ? 91.354  125.749 154.354 1.00 12.76 ?  451  ILE B N    1 
ATOM   10811 C CA   . ILE B 1 451  ? 91.437  126.624 153.185 1.00 10.49 ?  451  ILE B CA   1 
ATOM   10812 C C    . ILE B 1 451  ? 92.386  126.051 152.137 1.00 10.46 ?  451  ILE B C    1 
ATOM   10813 O O    . ILE B 1 451  ? 92.079  126.058 150.938 1.00 17.40 ?  451  ILE B O    1 
ATOM   10814 C CB   . ILE B 1 451  ? 91.835  128.054 153.606 1.00 9.52  ?  451  ILE B CB   1 
ATOM   10815 C CG1  . ILE B 1 451  ? 91.987  128.952 152.370 1.00 10.81 ?  451  ILE B CG1  1 
ATOM   10816 C CG2  . ILE B 1 451  ? 93.053  128.056 154.536 1.00 13.61 ?  451  ILE B CG2  1 
ATOM   10817 C CD1  . ILE B 1 451  ? 92.247  130.409 152.674 1.00 14.75 ?  451  ILE B CD1  1 
ATOM   10818 N N    . GLY B 1 452  ? 93.543  125.542 152.566 1.00 9.26  ?  452  GLY B N    1 
ATOM   10819 C CA   . GLY B 1 452  ? 94.475  124.956 151.617 1.00 7.81  ?  452  GLY B CA   1 
ATOM   10820 C C    . GLY B 1 452  ? 93.914  123.720 150.944 1.00 8.56  ?  452  GLY B C    1 
ATOM   10821 O O    . GLY B 1 452  ? 94.118  123.505 149.746 1.00 15.60 ?  452  GLY B O    1 
ATOM   10822 N N    . SER B 1 453  ? 93.185  122.899 151.705 1.00 7.34  ?  453  SER B N    1 
ATOM   10823 C CA   . SER B 1 453  ? 92.558  121.711 151.135 1.00 4.97  ?  453  SER B CA   1 
ATOM   10824 C C    . SER B 1 453  ? 91.507  122.082 150.097 1.00 9.48  ?  453  SER B C    1 
ATOM   10825 O O    . SER B 1 453  ? 91.454  121.478 149.019 1.00 10.31 ?  453  SER B O    1 
ATOM   10826 C CB   . SER B 1 453  ? 91.937  120.865 152.245 1.00 4.87  ?  453  SER B CB   1 
ATOM   10827 O OG   . SER B 1 453  ? 90.598  121.256 152.486 1.00 8.00  ?  453  SER B OG   1 
ATOM   10828 N N    . LYS B 1 454  ? 90.669  123.082 150.396 1.00 12.02 ?  454  LYS B N    1 
ATOM   10829 C CA   . LYS B 1 454  ? 89.664  123.516 149.427 1.00 4.95  ?  454  LYS B CA   1 
ATOM   10830 C C    . LYS B 1 454  ? 90.310  124.107 148.179 1.00 3.89  ?  454  LYS B C    1 
ATOM   10831 O O    . LYS B 1 454  ? 89.879  123.817 147.053 1.00 12.36 ?  454  LYS B O    1 
ATOM   10832 C CB   . LYS B 1 454  ? 88.715  124.529 150.067 1.00 7.46  ?  454  LYS B CB   1 
ATOM   10833 C CG   . LYS B 1 454  ? 87.908  123.978 151.227 1.00 11.15 ?  454  LYS B CG   1 
ATOM   10834 C CD   . LYS B 1 454  ? 86.974  122.872 150.772 1.00 13.64 ?  454  LYS B CD   1 
ATOM   10835 C CE   . LYS B 1 454  ? 86.882  121.774 151.817 1.00 12.52 ?  454  LYS B CE   1 
ATOM   10836 N NZ   . LYS B 1 454  ? 85.805  122.034 152.810 1.00 15.27 ?  454  LYS B NZ   1 
ATOM   10837 N N    . PHE B 1 455  ? 91.350  124.928 148.361 1.00 1.48  ?  455  PHE B N    1 
ATOM   10838 C CA   . PHE B 1 455  ? 92.064  125.512 147.229 1.00 0.00  ?  455  PHE B CA   1 
ATOM   10839 C C    . PHE B 1 455  ? 92.646  124.434 146.328 1.00 1.54  ?  455  PHE B C    1 
ATOM   10840 O O    . PHE B 1 455  ? 92.464  124.465 145.104 1.00 11.87 ?  455  PHE B O    1 
ATOM   10841 C CB   . PHE B 1 455  ? 93.180  126.428 147.733 1.00 2.15  ?  455  PHE B CB   1 
ATOM   10842 C CG   . PHE B 1 455  ? 92.793  127.872 147.833 1.00 4.99  ?  455  PHE B CG   1 
ATOM   10843 C CD1  . PHE B 1 455  ? 91.796  128.283 148.699 1.00 5.99  ?  455  PHE B CD1  1 
ATOM   10844 C CD2  . PHE B 1 455  ? 93.446  128.824 147.071 1.00 0.91  ?  455  PHE B CD2  1 
ATOM   10845 C CE1  . PHE B 1 455  ? 91.450  129.614 148.793 1.00 2.69  ?  455  PHE B CE1  1 
ATOM   10846 C CE2  . PHE B 1 455  ? 93.106  130.153 147.161 1.00 3.65  ?  455  PHE B CE2  1 
ATOM   10847 C CZ   . PHE B 1 455  ? 92.106  130.550 148.022 1.00 5.46  ?  455  PHE B CZ   1 
ATOM   10848 N N    . LEU B 1 456  ? 93.341  123.462 146.923 1.00 1.55  ?  456  LEU B N    1 
ATOM   10849 C CA   . LEU B 1 456  ? 93.981  122.421 146.130 1.00 1.26  ?  456  LEU B CA   1 
ATOM   10850 C C    . LEU B 1 456  ? 92.953  121.531 145.447 1.00 4.95  ?  456  LEU B C    1 
ATOM   10851 O O    . LEU B 1 456  ? 93.124  121.172 144.277 1.00 11.86 ?  456  LEU B O    1 
ATOM   10852 C CB   . LEU B 1 456  ? 94.913  121.590 147.008 1.00 3.27  ?  456  LEU B CB   1 
ATOM   10853 C CG   . LEU B 1 456  ? 96.008  120.808 146.285 1.00 0.06  ?  456  LEU B CG   1 
ATOM   10854 C CD1  . LEU B 1 456  ? 96.477  121.541 145.039 1.00 0.00  ?  456  LEU B CD1  1 
ATOM   10855 C CD2  . LEU B 1 456  ? 97.163  120.580 147.227 1.00 4.79  ?  456  LEU B CD2  1 
ATOM   10856 N N    . PHE B 1 457  ? 91.872  121.182 146.153 1.00 0.00  ?  457  PHE B N    1 
ATOM   10857 C CA   . PHE B 1 457  ? 90.842  120.332 145.567 1.00 0.00  ?  457  PHE B CA   1 
ATOM   10858 C C    . PHE B 1 457  ? 90.194  121.002 144.364 1.00 0.00  ?  457  PHE B C    1 
ATOM   10859 O O    . PHE B 1 457  ? 90.078  120.395 143.292 1.00 5.28  ?  457  PHE B O    1 
ATOM   10860 C CB   . PHE B 1 457  ? 89.789  119.989 146.621 1.00 7.05  ?  457  PHE B CB   1 
ATOM   10861 C CG   . PHE B 1 457  ? 88.530  119.401 146.052 1.00 7.15  ?  457  PHE B CG   1 
ATOM   10862 C CD1  . PHE B 1 457  ? 88.533  118.139 145.482 1.00 10.23 ?  457  PHE B CD1  1 
ATOM   10863 C CD2  . PHE B 1 457  ? 87.344  120.115 146.079 1.00 8.99  ?  457  PHE B CD2  1 
ATOM   10864 C CE1  . PHE B 1 457  ? 87.375  117.598 144.956 1.00 8.45  ?  457  PHE B CE1  1 
ATOM   10865 C CE2  . PHE B 1 457  ? 86.185  119.579 145.552 1.00 11.46 ?  457  PHE B CE2  1 
ATOM   10866 C CZ   . PHE B 1 457  ? 86.201  118.320 144.991 1.00 10.48 ?  457  PHE B CZ   1 
ATOM   10867 N N    . HIS B 1 458  ? 89.798  122.270 144.509 1.00 2.00  ?  458  HIS B N    1 
ATOM   10868 C CA   . HIS B 1 458  ? 89.125  122.947 143.405 1.00 0.00  ?  458  HIS B CA   1 
ATOM   10869 C C    . HIS B 1 458  ? 90.076  123.215 142.244 1.00 0.00  ?  458  HIS B C    1 
ATOM   10870 O O    . HIS B 1 458  ? 89.689  123.056 141.079 1.00 9.93  ?  458  HIS B O    1 
ATOM   10871 C CB   . HIS B 1 458  ? 88.479  124.239 143.897 1.00 1.66  ?  458  HIS B CB   1 
ATOM   10872 C CG   . HIS B 1 458  ? 87.216  124.018 144.668 1.00 6.03  ?  458  HIS B CG   1 
ATOM   10873 N ND1  . HIS B 1 458  ? 87.178  123.994 146.045 1.00 10.76 ?  458  HIS B ND1  1 
ATOM   10874 C CD2  . HIS B 1 458  ? 85.946  123.801 144.253 1.00 9.23  ?  458  HIS B CD2  1 
ATOM   10875 C CE1  . HIS B 1 458  ? 85.938  123.776 146.446 1.00 9.32  ?  458  HIS B CE1  1 
ATOM   10876 N NE2  . HIS B 1 458  ? 85.171  123.655 145.378 1.00 14.91 ?  458  HIS B NE2  1 
ATOM   10877 N N    . THR B 1 459  ? 91.326  123.597 142.531 1.00 0.08  ?  459  THR B N    1 
ATOM   10878 C CA   . THR B 1 459  ? 92.282  123.836 141.454 1.00 0.00  ?  459  THR B CA   1 
ATOM   10879 C C    . THR B 1 459  ? 92.592  122.556 140.685 1.00 7.91  ?  459  THR B C    1 
ATOM   10880 O O    . THR B 1 459  ? 92.604  122.560 139.447 1.00 18.29 ?  459  THR B O    1 
ATOM   10881 C CB   . THR B 1 459  ? 93.567  124.444 142.015 1.00 0.95  ?  459  THR B CB   1 
ATOM   10882 O OG1  . THR B 1 459  ? 93.241  125.541 142.876 1.00 5.26  ?  459  THR B OG1  1 
ATOM   10883 C CG2  . THR B 1 459  ? 94.454  124.941 140.887 1.00 0.00  ?  459  THR B CG2  1 
ATOM   10884 N N    . ALA B 1 460  ? 92.826  121.449 141.398 1.00 7.17  ?  460  ALA B N    1 
ATOM   10885 C CA   . ALA B 1 460  ? 93.109  120.183 140.732 1.00 0.23  ?  460  ALA B CA   1 
ATOM   10886 C C    . ALA B 1 460  ? 91.906  119.692 139.939 1.00 1.56  ?  460  ALA B C    1 
ATOM   10887 O O    . ALA B 1 460  ? 92.063  119.176 138.826 1.00 6.05  ?  460  ALA B O    1 
ATOM   10888 C CB   . ALA B 1 460  ? 93.543  119.137 141.757 1.00 0.00  ?  460  ALA B CB   1 
ATOM   10889 N N    . GLY B 1 461  ? 90.697  119.849 140.488 1.00 0.00  ?  461  GLY B N    1 
ATOM   10890 C CA   . GLY B 1 461  ? 89.507  119.452 139.755 1.00 0.00  ?  461  GLY B CA   1 
ATOM   10891 C C    . GLY B 1 461  ? 89.304  120.255 138.484 1.00 0.00  ?  461  GLY B C    1 
ATOM   10892 O O    . GLY B 1 461  ? 88.951  119.700 137.441 1.00 9.65  ?  461  GLY B O    1 
ATOM   10893 N N    . ILE B 1 462  ? 89.537  121.569 138.551 1.00 0.00  ?  462  ILE B N    1 
ATOM   10894 C CA   . ILE B 1 462  ? 89.387  122.413 137.368 1.00 0.00  ?  462  ILE B CA   1 
ATOM   10895 C C    . ILE B 1 462  ? 90.431  122.051 136.319 1.00 0.00  ?  462  ILE B C    1 
ATOM   10896 O O    . ILE B 1 462  ? 90.129  121.985 135.119 1.00 8.29  ?  462  ILE B O    1 
ATOM   10897 C CB   . ILE B 1 462  ? 89.463  123.898 137.767 1.00 0.39  ?  462  ILE B CB   1 
ATOM   10898 C CG1  . ILE B 1 462  ? 88.170  124.319 138.462 1.00 1.98  ?  462  ILE B CG1  1 
ATOM   10899 C CG2  . ILE B 1 462  ? 89.714  124.783 136.557 1.00 3.12  ?  462  ILE B CG2  1 
ATOM   10900 C CD1  . ILE B 1 462  ? 86.949  124.200 137.594 1.00 5.65  ?  462  ILE B CD1  1 
ATOM   10901 N N    . VAL B 1 463  ? 91.668  121.789 136.754 1.00 0.96  ?  463  VAL B N    1 
ATOM   10902 C CA   . VAL B 1 463  ? 92.722  121.401 135.817 1.00 0.00  ?  463  VAL B CA   1 
ATOM   10903 C C    . VAL B 1 463  ? 92.381  120.077 135.142 1.00 1.58  ?  463  VAL B C    1 
ATOM   10904 O O    . VAL B 1 463  ? 92.540  119.928 133.924 1.00 5.45  ?  463  VAL B O    1 
ATOM   10905 C CB   . VAL B 1 463  ? 94.082  121.344 136.538 1.00 2.83  ?  463  VAL B CB   1 
ATOM   10906 C CG1  . VAL B 1 463  ? 95.116  120.628 135.688 1.00 5.38  ?  463  VAL B CG1  1 
ATOM   10907 C CG2  . VAL B 1 463  ? 94.561  122.745 136.866 1.00 5.19  ?  463  VAL B CG2  1 
ATOM   10908 N N    . VAL B 1 464  ? 91.886  119.107 135.918 1.00 1.79  ?  464  VAL B N    1 
ATOM   10909 C CA   . VAL B 1 464  ? 91.511  117.805 135.364 1.00 1.05  ?  464  VAL B CA   1 
ATOM   10910 C C    . VAL B 1 464  ? 90.379  117.957 134.354 1.00 2.56  ?  464  VAL B C    1 
ATOM   10911 O O    . VAL B 1 464  ? 90.428  117.401 133.247 1.00 7.67  ?  464  VAL B O    1 
ATOM   10912 C CB   . VAL B 1 464  ? 91.124  116.840 136.500 1.00 3.05  ?  464  VAL B CB   1 
ATOM   10913 C CG1  . VAL B 1 464  ? 90.248  115.709 135.985 1.00 5.75  ?  464  VAL B CG1  1 
ATOM   10914 C CG2  . VAL B 1 464  ? 92.358  116.289 137.176 1.00 1.70  ?  464  VAL B CG2  1 
ATOM   10915 N N    . LEU B 1 465  ? 89.345  118.723 134.721 1.00 4.07  ?  465  LEU B N    1 
ATOM   10916 C CA   . LEU B 1 465  ? 88.190  118.892 133.846 1.00 0.00  ?  465  LEU B CA   1 
ATOM   10917 C C    . LEU B 1 465  ? 88.576  119.582 132.545 1.00 0.23  ?  465  LEU B C    1 
ATOM   10918 O O    . LEU B 1 465  ? 88.135  119.170 131.466 1.00 10.73 ?  465  LEU B O    1 
ATOM   10919 C CB   . LEU B 1 465  ? 87.097  119.679 134.566 1.00 0.00  ?  465  LEU B CB   1 
ATOM   10920 C CG   . LEU B 1 465  ? 86.285  118.916 135.613 1.00 0.00  ?  465  LEU B CG   1 
ATOM   10921 C CD1  . LEU B 1 465  ? 85.167  119.787 136.160 1.00 3.73  ?  465  LEU B CD1  1 
ATOM   10922 C CD2  . LEU B 1 465  ? 85.732  117.624 135.039 1.00 5.76  ?  465  LEU B CD2  1 
ATOM   10923 N N    . THR B 1 466  ? 89.406  120.626 132.622 1.00 0.00  ?  466  THR B N    1 
ATOM   10924 C CA   . THR B 1 466  ? 89.868  121.285 131.405 1.00 0.94  ?  466  THR B CA   1 
ATOM   10925 C C    . THR B 1 466  ? 90.685  120.330 130.546 1.00 2.70  ?  466  THR B C    1 
ATOM   10926 O O    . THR B 1 466  ? 90.362  120.113 129.372 1.00 7.75  ?  466  THR B O    1 
ATOM   10927 C CB   . THR B 1 466  ? 90.686  122.528 131.751 1.00 1.53  ?  466  THR B CB   1 
ATOM   10928 O OG1  . THR B 1 466  ? 91.661  122.201 132.748 1.00 1.95  ?  466  THR B OG1  1 
ATOM   10929 C CG2  . THR B 1 466  ? 89.783  123.632 132.272 1.00 4.95  ?  466  THR B CG2  1 
ATOM   10930 N N    . LEU B 1 467  ? 91.699  119.691 131.145 1.00 8.93  ?  467  LEU B N    1 
ATOM   10931 C CA   . LEU B 1 467  ? 92.616  118.825 130.413 1.00 8.31  ?  467  LEU B CA   1 
ATOM   10932 C C    . LEU B 1 467  ? 91.923  117.627 129.786 1.00 6.49  ?  467  LEU B C    1 
ATOM   10933 O O    . LEU B 1 467  ? 92.443  117.065 128.817 1.00 7.90  ?  467  LEU B O    1 
ATOM   10934 C CB   . LEU B 1 467  ? 93.726  118.336 131.345 1.00 4.49  ?  467  LEU B CB   1 
ATOM   10935 C CG   . LEU B 1 467  ? 94.998  119.176 131.458 1.00 4.60  ?  467  LEU B CG   1 
ATOM   10936 C CD1  . LEU B 1 467  ? 96.097  118.357 132.106 1.00 5.36  ?  467  LEU B CD1  1 
ATOM   10937 C CD2  . LEU B 1 467  ? 95.442  119.688 130.100 1.00 3.77  ?  467  LEU B CD2  1 
ATOM   10938 N N    . VAL B 1 468  ? 90.776  117.209 130.313 1.00 9.25  ?  468  VAL B N    1 
ATOM   10939 C CA   . VAL B 1 468  ? 90.033  116.148 129.645 1.00 10.12 ?  468  VAL B CA   1 
ATOM   10940 C C    . VAL B 1 468  ? 89.127  116.764 128.585 1.00 12.45 ?  468  VAL B C    1 
ATOM   10941 O O    . VAL B 1 468  ? 89.352  116.579 127.381 1.00 17.52 ?  468  VAL B O    1 
ATOM   10942 C CB   . VAL B 1 468  ? 89.220  115.310 130.649 1.00 4.50  ?  468  VAL B CB   1 
ATOM   10943 C CG1  . VAL B 1 468  ? 88.299  114.353 129.913 1.00 10.96 ?  468  VAL B CG1  1 
ATOM   10944 C CG2  . VAL B 1 468  ? 90.149  114.550 131.575 1.00 3.19  ?  468  VAL B CG2  1 
ATOM   10945 N N    . ILE B 1 469  ? 88.144  117.558 129.027 1.00 7.15  ?  469  ILE B N    1 
ATOM   10946 C CA   . ILE B 1 469  ? 87.045  117.955 128.152 1.00 5.54  ?  469  ILE B CA   1 
ATOM   10947 C C    . ILE B 1 469  ? 87.534  118.872 127.039 1.00 5.48  ?  469  ILE B C    1 
ATOM   10948 O O    . ILE B 1 469  ? 87.326  118.588 125.853 1.00 12.84 ?  469  ILE B O    1 
ATOM   10949 C CB   . ILE B 1 469  ? 85.920  118.617 128.969 1.00 5.84  ?  469  ILE B CB   1 
ATOM   10950 C CG1  . ILE B 1 469  ? 85.527  117.739 130.159 1.00 6.71  ?  469  ILE B CG1  1 
ATOM   10951 C CG2  . ILE B 1 469  ? 84.720  118.904 128.083 1.00 6.65  ?  469  ILE B CG2  1 
ATOM   10952 C CD1  . ILE B 1 469  ? 85.040  116.366 129.769 1.00 9.81  ?  469  ILE B CD1  1 
ATOM   10953 N N    . ASN B 1 470  ? 88.177  119.989 127.397 1.00 0.44  ?  470  ASN B N    1 
ATOM   10954 C CA   . ASN B 1 470  ? 88.547  120.964 126.379 1.00 2.11  ?  470  ASN B CA   1 
ATOM   10955 C C    . ASN B 1 470  ? 89.619  120.410 125.452 1.00 10.39 ?  470  ASN B C    1 
ATOM   10956 O O    . ASN B 1 470  ? 89.522  120.553 124.227 1.00 18.61 ?  470  ASN B O    1 
ATOM   10957 C CB   . ASN B 1 470  ? 89.022  122.256 127.041 1.00 4.59  ?  470  ASN B CB   1 
ATOM   10958 C CG   . ASN B 1 470  ? 87.996  122.833 127.991 1.00 6.36  ?  470  ASN B CG   1 
ATOM   10959 O OD1  . ASN B 1 470  ? 87.155  122.113 128.526 1.00 10.15 ?  470  ASN B OD1  1 
ATOM   10960 N ND2  . ASN B 1 470  ? 88.065  124.138 128.212 1.00 1.66  ?  470  ASN B ND2  1 
ATOM   10961 N N    . ALA B 1 471  ? 90.623  119.738 126.016 1.00 10.70 ?  471  ALA B N    1 
ATOM   10962 C CA   . ALA B 1 471  ? 91.726  119.226 125.216 1.00 13.15 ?  471  ALA B CA   1 
ATOM   10963 C C    . ALA B 1 471  ? 91.315  118.066 124.321 1.00 14.92 ?  471  ALA B C    1 
ATOM   10964 O O    . ALA B 1 471  ? 91.998  117.805 123.324 1.00 17.24 ?  471  ALA B O    1 
ATOM   10965 C CB   . ALA B 1 471  ? 92.882  118.802 126.119 1.00 12.96 ?  471  ALA B CB   1 
ATOM   10966 N N    . THR B 1 472  ? 90.224  117.361 124.637 1.00 14.06 ?  472  THR B N    1 
ATOM   10967 C CA   . THR B 1 472  ? 89.743  116.331 123.728 1.00 13.87 ?  472  THR B CA   1 
ATOM   10968 C C    . THR B 1 472  ? 88.665  116.816 122.765 1.00 12.55 ?  472  THR B C    1 
ATOM   10969 O O    . THR B 1 472  ? 88.493  116.207 121.704 1.00 15.82 ?  472  THR B O    1 
ATOM   10970 C CB   . THR B 1 472  ? 89.203  115.131 124.516 1.00 10.12 ?  472  THR B CB   1 
ATOM   10971 O OG1  . THR B 1 472  ? 88.346  115.592 125.567 1.00 12.23 ?  472  THR B OG1  1 
ATOM   10972 C CG2  . THR B 1 472  ? 90.348  114.326 125.112 1.00 9.18  ?  472  THR B CG2  1 
ATOM   10973 N N    . THR B 1 473  ? 87.947  117.891 123.091 1.00 10.44 ?  473  THR B N    1 
ATOM   10974 C CA   . THR B 1 473  ? 86.790  118.307 122.311 1.00 11.21 ?  473  THR B CA   1 
ATOM   10975 C C    . THR B 1 473  ? 87.063  119.575 121.496 1.00 14.16 ?  473  THR B C    1 
ATOM   10976 O O    . THR B 1 473  ? 86.194  120.013 120.731 1.00 16.70 ?  473  THR B O    1 
ATOM   10977 C CB   . THR B 1 473  ? 85.597  118.482 123.273 1.00 10.99 ?  473  THR B CB   1 
ATOM   10978 O OG1  . THR B 1 473  ? 85.475  117.296 124.066 1.00 10.32 ?  473  THR B OG1  1 
ATOM   10979 C CG2  . THR B 1 473  ? 84.260  118.619 122.544 1.00 11.79 ?  473  THR B CG2  1 
ATOM   10980 N N    . ILE B 1 474  ? 88.263  120.156 121.605 1.00 14.68 ?  474  ILE B N    1 
ATOM   10981 C CA   . ILE B 1 474  ? 88.583  121.352 120.823 1.00 16.19 ?  474  ILE B CA   1 
ATOM   10982 C C    . ILE B 1 474  ? 88.535  121.059 119.324 1.00 19.29 ?  474  ILE B C    1 
ATOM   10983 O O    . ILE B 1 474  ? 88.023  121.866 118.536 1.00 17.42 ?  474  ILE B O    1 
ATOM   10984 C CB   . ILE B 1 474  ? 89.949  121.921 121.261 1.00 13.19 ?  474  ILE B CB   1 
ATOM   10985 C CG1  . ILE B 1 474  ? 90.360  123.102 120.376 1.00 12.49 ?  474  ILE B CG1  1 
ATOM   10986 C CG2  . ILE B 1 474  ? 91.026  120.831 121.308 1.00 15.93 ?  474  ILE B CG2  1 
ATOM   10987 C CD1  . ILE B 1 474  ? 91.131  124.173 121.109 1.00 14.29 ?  474  ILE B CD1  1 
ATOM   10988 N N    . GLN B 1 475  ? 89.041  119.894 118.909 1.00 21.79 ?  475  GLN B N    1 
ATOM   10989 C CA   . GLN B 1 475  ? 89.067  119.541 117.492 1.00 22.67 ?  475  GLN B CA   1 
ATOM   10990 C C    . GLN B 1 475  ? 87.651  119.297 116.971 1.00 18.67 ?  475  GLN B C    1 
ATOM   10991 O O    . GLN B 1 475  ? 87.306  119.711 115.860 1.00 13.34 ?  475  GLN B O    1 
ATOM   10992 C CB   . GLN B 1 475  ? 89.954  118.305 117.311 1.00 21.01 ?  475  GLN B CB   1 
ATOM   10993 C CG   . GLN B 1 475  ? 90.225  117.775 115.895 1.00 21.32 ?  475  GLN B CG   1 
ATOM   10994 C CD   . GLN B 1 475  ? 90.323  118.847 114.822 1.00 22.56 ?  475  GLN B CD   1 
ATOM   10995 O OE1  . GLN B 1 475  ? 89.336  119.216 114.197 1.00 19.39 ?  475  GLN B OE1  1 
ATOM   10996 N NE2  . GLN B 1 475  ? 91.539  119.330 114.585 1.00 24.88 ?  475  GLN B NE2  1 
ATOM   10997 N N    . THR B 1 476  ? 86.809  118.647 117.779 1.00 19.71 ?  476  THR B N    1 
ATOM   10998 C CA   . THR B 1 476  ? 85.416  118.424 117.396 1.00 17.25 ?  476  THR B CA   1 
ATOM   10999 C C    . THR B 1 476  ? 84.656  119.741 117.283 1.00 18.96 ?  476  THR B C    1 
ATOM   11000 O O    . THR B 1 476  ? 83.836  119.923 116.373 1.00 16.69 ?  476  THR B O    1 
ATOM   11001 C CB   . THR B 1 476  ? 84.747  117.498 118.411 1.00 14.70 ?  476  THR B CB   1 
ATOM   11002 O OG1  . THR B 1 476  ? 85.401  116.224 118.392 1.00 14.60 ?  476  THR B OG1  1 
ATOM   11003 C CG2  . THR B 1 476  ? 83.273  117.305 118.090 1.00 15.27 ?  476  THR B CG2  1 
ATOM   11004 N N    . LEU B 1 477  ? 84.921  120.676 118.197 1.00 21.07 ?  477  LEU B N    1 
ATOM   11005 C CA   . LEU B 1 477  ? 84.303  121.995 118.113 1.00 21.56 ?  477  LEU B CA   1 
ATOM   11006 C C    . LEU B 1 477  ? 84.765  122.748 116.871 1.00 24.85 ?  477  LEU B C    1 
ATOM   11007 O O    . LEU B 1 477  ? 83.964  123.430 116.219 1.00 23.26 ?  477  LEU B O    1 
ATOM   11008 C CB   . LEU B 1 477  ? 84.613  122.796 119.375 1.00 17.74 ?  477  LEU B CB   1 
ATOM   11009 C CG   . LEU B 1 477  ? 83.580  123.855 119.760 1.00 20.97 ?  477  LEU B CG   1 
ATOM   11010 C CD1  . LEU B 1 477  ? 82.351  123.216 120.382 1.00 18.81 ?  477  LEU B CD1  1 
ATOM   11011 C CD2  . LEU B 1 477  ? 84.191  124.872 120.708 1.00 21.42 ?  477  LEU B CD2  1 
ATOM   11012 N N    . LEU B 1 478  ? 86.053  122.643 116.532 1.00 24.30 ?  478  LEU B N    1 
ATOM   11013 C CA   . LEU B 1 478  ? 86.554  123.285 115.320 1.00 23.22 ?  478  LEU B CA   1 
ATOM   11014 C C    . LEU B 1 478  ? 85.924  122.673 114.073 1.00 25.93 ?  478  LEU B C    1 
ATOM   11015 O O    . LEU B 1 478  ? 85.616  123.384 113.111 1.00 25.03 ?  478  LEU B O    1 
ATOM   11016 C CB   . LEU B 1 478  ? 88.081  123.190 115.270 1.00 20.06 ?  478  LEU B CB   1 
ATOM   11017 C CG   . LEU B 1 478  ? 88.787  123.306 113.915 1.00 24.74 ?  478  LEU B CG   1 
ATOM   11018 C CD1  . LEU B 1 478  ? 88.643  124.700 113.313 1.00 20.91 ?  478  LEU B CD1  1 
ATOM   11019 C CD2  . LEU B 1 478  ? 90.256  122.927 114.038 1.00 26.38 ?  478  LEU B CD2  1 
ATOM   11020 N N    . ARG B 1 479  ? 85.724  121.352 114.074 1.00 25.75 ?  479  ARG B N    1 
ATOM   11021 C CA   . ARG B 1 479  ? 85.060  120.696 112.951 1.00 25.20 ?  479  ARG B CA   1 
ATOM   11022 C C    . ARG B 1 479  ? 83.593  121.101 112.852 1.00 26.40 ?  479  ARG B C    1 
ATOM   11023 O O    . ARG B 1 479  ? 83.044  121.183 111.747 1.00 27.03 ?  479  ARG B O    1 
ATOM   11024 C CB   . ARG B 1 479  ? 85.193  119.177 113.085 1.00 24.05 ?  479  ARG B CB   1 
ATOM   11025 C CG   . ARG B 1 479  ? 84.527  118.376 111.977 1.00 21.81 ?  479  ARG B CG   1 
ATOM   11026 C CD   . ARG B 1 479  ? 84.373  116.915 112.364 1.00 23.75 ?  479  ARG B CD   1 
ATOM   11027 N NE   . ARG B 1 479  ? 85.571  116.381 113.002 1.00 23.88 ?  479  ARG B NE   1 
ATOM   11028 C CZ   . ARG B 1 479  ? 85.585  115.320 113.797 1.00 24.90 ?  479  ARG B CZ   1 
ATOM   11029 N NH1  . ARG B 1 479  ? 84.477  114.651 114.075 1.00 22.39 ?  479  ARG B NH1  1 
ATOM   11030 N NH2  . ARG B 1 479  ? 86.738  114.918 114.324 1.00 27.59 ?  479  ARG B NH2  1 
ATOM   11031 N N    . ILE B 1 480  ? 82.993  121.345 113.988 1.00 24.69 ?  480  ILE B N    1 
ATOM   11032 C CA   . ILE B 1 480  ? 81.620  121.836 113.947 1.00 23.45 ?  480  ILE B CA   1 
ATOM   11033 C C    . ILE B 1 480  ? 81.577  123.243 113.360 1.00 21.76 ?  480  ILE B C    1 
ATOM   11034 O O    . ILE B 1 480  ? 80.714  123.561 112.531 1.00 24.72 ?  480  ILE B O    1 
ATOM   11035 C CB   . ILE B 1 480  ? 80.992  121.777 115.353 1.00 25.17 ?  480  ILE B CB   1 
ATOM   11036 C CG1  . ILE B 1 480  ? 80.606  120.336 115.699 1.00 24.65 ?  480  ILE B CG1  1 
ATOM   11037 C CG2  . ILE B 1 480  ? 79.786  122.703 115.462 1.00 23.83 ?  480  ILE B CG2  1 
ATOM   11038 C CD1  . ILE B 1 480  ? 79.376  119.836 114.970 1.00 22.83 ?  480  ILE B CD1  1 
ATOM   11039 N N    . LEU B 1 481  ? 82.524  124.096 113.757 1.00 19.39 ?  481  LEU B N    1 
ATOM   11040 C CA   . LEU B 1 481  ? 82.496  125.495 113.336 1.00 24.87 ?  481  LEU B CA   1 
ATOM   11041 C C    . LEU B 1 481  ? 82.875  125.646 111.866 1.00 26.06 ?  481  LEU B C    1 
ATOM   11042 O O    . LEU B 1 481  ? 82.067  126.094 111.045 1.00 25.45 ?  481  LEU B O    1 
ATOM   11043 C CB   . LEU B 1 481  ? 83.432  126.320 114.219 1.00 23.73 ?  481  LEU B CB   1 
ATOM   11044 C CG   . LEU B 1 481  ? 82.989  126.552 115.662 1.00 27.04 ?  481  LEU B CG   1 
ATOM   11045 C CD1  . LEU B 1 481  ? 84.136  127.136 116.463 1.00 25.92 ?  481  LEU B CD1  1 
ATOM   11046 C CD2  . LEU B 1 481  ? 81.777  127.468 115.712 1.00 26.04 ?  481  LEU B CD2  1 
ATOM   11047 N N    . GLY B 1 482  ? 84.104  125.275 111.514 1.00 27.88 ?  482  GLY B N    1 
ATOM   11048 C CA   . GLY B 1 482  ? 84.589  125.479 110.162 1.00 25.06 ?  482  GLY B CA   1 
ATOM   11049 C C    . GLY B 1 482  ? 85.114  124.224 109.497 1.00 26.47 ?  482  GLY B C    1 
ATOM   11050 O O    . GLY B 1 482  ? 86.029  124.292 108.670 1.00 25.92 ?  482  GLY B O    1 
ATOM   11051 N N    . MET B 1 483  ? 84.564  123.070 109.891 1.00 26.43 ?  483  MET B N    1 
ATOM   11052 C CA   . MET B 1 483  ? 84.837  121.756 109.307 1.00 28.83 ?  483  MET B CA   1 
ATOM   11053 C C    . MET B 1 483  ? 86.278  121.287 109.493 1.00 30.01 ?  483  MET B C    1 
ATOM   11054 O O    . MET B 1 483  ? 86.642  120.216 108.995 1.00 34.55 ?  483  MET B O    1 
ATOM   11055 C CB   . MET B 1 483  ? 84.472  121.738 107.818 1.00 27.69 ?  483  MET B CB   1 
ATOM   11056 C CG   . MET B 1 483  ? 83.112  121.129 107.523 1.00 30.39 ?  483  MET B CG   1 
ATOM   11057 S SD   . MET B 1 483  ? 82.993  120.471 105.849 1.00 43.58 ?  483  MET B SD   1 
ATOM   11058 C CE   . MET B 1 483  ? 84.460  119.445 105.786 1.00 31.01 ?  483  MET B CE   1 
ATOM   11059 N N    . SER B 1 484  ? 87.084  122.077 110.195 1.00 23.64 ?  484  SER B N    1 
ATOM   11060 C CA   . SER B 1 484  ? 88.484  121.724 110.408 1.00 26.27 ?  484  SER B CA   1 
ATOM   11061 C C    . SER B 1 484  ? 89.127  121.276 109.105 1.00 26.24 ?  484  SER B C    1 
ATOM   11062 O O    . SER B 1 484  ? 90.118  120.547 109.114 1.00 26.66 ?  484  SER B O    1 
ATOM   11063 C CB   . SER B 1 484  ? 88.606  120.628 111.468 1.00 26.28 ?  484  SER B CB   1 
ATOM   11064 O OG   . SER B 1 484  ? 89.964  120.355 111.764 1.00 25.26 ?  484  SER B OG   1 
ATOM   11065 N N    . ASP B 1 485  ? 88.566  121.710 107.982 1.00 25.95 ?  485  ASP B N    1 
ATOM   11066 C CA   . ASP B 1 485  ? 89.094  121.311 106.680 1.00 27.79 ?  485  ASP B CA   1 
ATOM   11067 C C    . ASP B 1 485  ? 90.465  121.914 106.400 1.00 30.13 ?  485  ASP B C    1 
ATOM   11068 O O    . ASP B 1 485  ? 90.703  123.087 106.687 1.00 28.11 ?  485  ASP B O    1 
ATOM   11069 C CB   . ASP B 1 485  ? 88.112  121.688 105.565 1.00 27.64 ?  485  ASP B CB   1 
ATOM   11070 C CG   . ASP B 1 485  ? 87.669  123.138 105.637 1.00 31.38 ?  485  ASP B CG   1 
ATOM   11071 O OD1  . ASP B 1 485  ? 88.017  123.830 106.617 1.00 30.52 -1 485  ASP B OD1  1 
ATOM   11072 O OD2  . ASP B 1 485  ? 86.966  123.588 104.710 1.00 28.86 -1 485  ASP B OD2  1 
ATOM   11073 N N    . ILE B 1 486  ? 91.348  121.180 105.764 1.00 27.20 ?  486  ILE B N    1 
ATOM   11074 C CA   . ILE B 1 486  ? 92.699  121.681 105.545 1.00 25.32 ?  486  ILE B CA   1 
ATOM   11075 C C    . ILE B 1 486  ? 92.791  122.752 104.463 1.00 26.90 ?  486  ILE B C    1 
ATOM   11076 O O    . ILE B 1 486  ? 93.845  123.359 104.306 1.00 23.37 ?  486  ILE B O    1 
ATOM   11077 C CB   . ILE B 1 486  ? 93.600  120.495 105.187 1.00 22.67 ?  486  ILE B CB   1 
ATOM   11078 C CG1  . ILE B 1 486  ? 93.093  119.834 103.899 1.00 23.96 ?  486  ILE B CG1  1 
ATOM   11079 C CG2  . ILE B 1 486  ? 93.718  119.547 106.378 1.00 23.04 ?  486  ILE B CG2  1 
ATOM   11080 C CD1  . ILE B 1 486  ? 94.030  118.789 103.338 1.00 23.91 ?  486  ILE B CD1  1 
ATOM   11081 N N    . SER B 1 487  ? 91.705  122.976 103.721 1.00 25.65 ?  487  SER B N    1 
ATOM   11082 C CA   . SER B 1 487  ? 91.666  123.981 102.648 1.00 24.73 ?  487  SER B CA   1 
ATOM   11083 C C    . SER B 1 487  ? 92.543  123.627 101.474 1.00 22.61 ?  487  SER B C    1 
ATOM   11084 O O    . SER B 1 487  ? 92.891  122.471 101.292 1.00 20.36 ?  487  SER B O    1 
ATOM   11085 C CB   . SER B 1 487  ? 92.039  125.368 103.167 1.00 22.84 ?  487  SER B CB   1 
ATOM   11086 O OG   . SER B 1 487  ? 93.408  125.466 103.512 1.00 25.56 ?  487  SER B OG   1 
ATOM   11087 N N    . ILE B 1 488  ? 92.874  124.607 100.641 1.00 22.10 ?  488  ILE B N    1 
ATOM   11088 C CA   . ILE B 1 488  ? 93.644  124.325 99.423  1.00 27.49 ?  488  ILE B CA   1 
ATOM   11089 C C    . ILE B 1 488  ? 95.142  124.088 99.640  1.00 27.21 ?  488  ILE B C    1 
ATOM   11090 O O    . ILE B 1 488  ? 95.714  123.176 99.040  1.00 25.60 ?  488  ILE B O    1 
ATOM   11091 C CB   . ILE B 1 488  ? 93.470  125.453 98.387  1.00 26.80 ?  488  ILE B CB   1 
ATOM   11092 C CG1  . ILE B 1 488  ? 91.999  125.589 98.002  1.00 25.06 ?  488  ILE B CG1  1 
ATOM   11093 C CG2  . ILE B 1 488  ? 94.321  125.185 97.156  1.00 25.70 ?  488  ILE B CG2  1 
ATOM   11094 C CD1  . ILE B 1 488  ? 91.396  124.311 97.462  1.00 22.23 ?  488  ILE B CD1  1 
ATOM   11095 N N    . PRO B 1 489  ? 95.784  124.900 100.496 1.00 26.09 ?  489  PRO B N    1 
ATOM   11096 C CA   . PRO B 1 489  ? 97.231  124.748 100.663 1.00 27.13 ?  489  PRO B CA   1 
ATOM   11097 C C    . PRO B 1 489  ? 97.636  123.290 100.810 1.00 25.20 ?  489  PRO B C    1 
ATOM   11098 O O    . PRO B 1 489  ? 98.722  122.913 100.380 1.00 28.48 ?  489  PRO B O    1 
ATOM   11099 C CB   . PRO B 1 489  ? 97.499  125.489 101.969 1.00 26.01 ?  489  PRO B CB   1 
ATOM   11100 C CG   . PRO B 1 489  ? 96.458  126.556 102.011 1.00 28.01 ?  489  PRO B CG   1 
ATOM   11101 C CD   . PRO B 1 489  ? 95.275  126.086 101.207 1.00 24.24 ?  489  PRO B CD   1 
ATOM   11102 N N    . LYS B 1 490  ? 96.777  122.480 101.414 1.00 20.14 ?  490  LYS B N    1 
ATOM   11103 C CA   . LYS B 1 490  ? 97.086  121.072 101.597 1.00 24.01 ?  490  LYS B CA   1 
ATOM   11104 C C    . LYS B 1 490  ? 96.428  120.222 100.517 1.00 27.43 ?  490  LYS B C    1 
ATOM   11105 O O    . LYS B 1 490  ? 96.984  119.207 100.098 1.00 27.20 ?  490  LYS B O    1 
ATOM   11106 C CB   . LYS B 1 490  ? 96.637  120.615 102.982 1.00 25.17 ?  490  LYS B CB   1 
ATOM   11107 C CG   . LYS B 1 490  ? 96.916  121.621 104.086 1.00 26.42 ?  490  LYS B CG   1 
ATOM   11108 C CD   . LYS B 1 490  ? 98.381  122.026 104.115 1.00 24.74 ?  490  LYS B CD   1 
ATOM   11109 C CE   . LYS B 1 490  ? 98.656  122.996 105.251 1.00 29.45 ?  490  LYS B CE   1 
ATOM   11110 N NZ   . LYS B 1 490  ? 98.290  122.413 106.571 1.00 29.83 1  490  LYS B NZ   1 
ATOM   11111 N N    . ARG B 1 491  ? 95.249  120.633 100.059 1.00 27.20 ?  491  ARG B N    1 
ATOM   11112 C CA   . ARG B 1 491  ? 94.538  119.882 99.033  1.00 26.06 ?  491  ARG B CA   1 
ATOM   11113 C C    . ARG B 1 491  ? 95.377  119.667 97.783  1.00 22.46 ?  491  ARG B C    1 
ATOM   11114 O O    . ARG B 1 491  ? 95.377  118.575 97.217  1.00 24.30 ?  491  ARG B O    1 
ATOM   11115 C CB   . ARG B 1 491  ? 93.246  120.607 98.658  1.00 27.09 ?  491  ARG B CB   1 
ATOM   11116 C CG   . ARG B 1 491  ? 92.102  119.678 98.299  1.00 25.90 ?  491  ARG B CG   1 
ATOM   11117 C CD   . ARG B 1 491  ? 91.723  118.817 99.492  1.00 26.57 ?  491  ARG B CD   1 
ATOM   11118 N NE   . ARG B 1 491  ? 90.623  117.908 99.186  1.00 28.36 ?  491  ARG B NE   1 
ATOM   11119 C CZ   . ARG B 1 491  ? 90.097  117.055 100.057 1.00 28.81 ?  491  ARG B CZ   1 
ATOM   11120 N NH1  . ARG B 1 491  ? 90.570  116.991 101.295 1.00 23.88 1  491  ARG B NH1  1 
ATOM   11121 N NH2  . ARG B 1 491  ? 89.098  116.263 99.692  1.00 28.66 ?  491  ARG B NH2  1 
ATOM   11122 N N    . LEU B 1 492  ? 96.094  120.697 97.347  1.00 21.71 ?  492  LEU B N    1 
ATOM   11123 C CA   . LEU B 1 492  ? 96.860  120.586 96.107  1.00 24.99 ?  492  LEU B CA   1 
ATOM   11124 C C    . LEU B 1 492  ? 98.361  120.498 96.339  1.00 26.30 ?  492  LEU B C    1 
ATOM   11125 O O    . LEU B 1 492  ? 99.004  119.550 95.891  1.00 27.95 ?  492  LEU B O    1 
ATOM   11126 C CB   . LEU B 1 492  ? 96.543  121.776 95.193  1.00 25.37 ?  492  LEU B CB   1 
ATOM   11127 C CG   . LEU B 1 492  ? 95.122  121.920 94.639  1.00 25.78 ?  492  LEU B CG   1 
ATOM   11128 C CD1  . LEU B 1 492  ? 94.977  123.233 93.884  1.00 23.90 ?  492  LEU B CD1  1 
ATOM   11129 C CD2  . LEU B 1 492  ? 94.720  120.745 93.760  1.00 24.32 ?  492  LEU B CD2  1 
ATOM   11130 N N    . ALA B 1 493  ? 98.926  121.483 97.027  1.00 19.07 ?  493  ALA B N    1 
ATOM   11131 C CA   . ALA B 1 493  ? 100.371 121.505 97.240  1.00 17.81 ?  493  ALA B CA   1 
ATOM   11132 C C    . ALA B 1 493  ? 100.886 120.165 97.733  1.00 20.67 ?  493  ALA B C    1 
ATOM   11133 O O    . ALA B 1 493  ? 101.691 119.520 97.061  1.00 21.16 ?  493  ALA B O    1 
ATOM   11134 C CB   . ALA B 1 493  ? 100.743 122.608 98.220  1.00 18.94 ?  493  ALA B CB   1 
ATOM   11135 N N    . MET B 1 494  ? 100.427 119.740 98.903  1.00 20.89 ?  494  MET B N    1 
ATOM   11136 C CA   . MET B 1 494  ? 100.894 118.502 99.462  1.00 19.20 ?  494  MET B CA   1 
ATOM   11137 C C    . MET B 1 494  ? 100.603 117.349 98.529  1.00 20.18 ?  494  MET B C    1 
ATOM   11138 O O    . MET B 1 494  ? 101.142 116.278 98.719  1.00 21.87 ?  494  MET B O    1 
ATOM   11139 C CB   . MET B 1 494  ? 100.244 118.247 100.795 1.00 19.04 ?  494  MET B CB   1 
ATOM   11140 C CG   . MET B 1 494  ? 101.103 117.453 101.758 1.00 20.98 ?  494  MET B CG   1 
ATOM   11141 S SD   . MET B 1 494  ? 102.641 118.309 102.131 1.00 29.48 ?  494  MET B SD   1 
ATOM   11142 C CE   . MET B 1 494  ? 103.055 117.577 103.709 1.00 23.73 ?  494  MET B CE   1 
ATOM   11143 N N    . ALA B 1 495  ? 99.740  117.519 97.537  1.00 17.49 ?  495  ALA B N    1 
ATOM   11144 C CA   . ALA B 1 495  ? 99.588  116.408 96.599  1.00 16.06 ?  495  ALA B CA   1 
ATOM   11145 C C    . ALA B 1 495  ? 100.668 116.372 95.552  1.00 20.40 ?  495  ALA B C    1 
ATOM   11146 O O    . ALA B 1 495  ? 101.094 115.300 95.149  1.00 23.93 ?  495  ALA B O    1 
ATOM   11147 C CB   . ALA B 1 495  ? 98.264  116.493 95.907  1.00 17.97 ?  495  ALA B CB   1 
ATOM   11148 N N    . GLY B 1 496  ? 101.087 117.521 95.058  1.00 21.99 ?  496  GLY B N    1 
ATOM   11149 C CA   . GLY B 1 496  ? 102.165 117.613 94.087  1.00 19.45 ?  496  GLY B CA   1 
ATOM   11150 C C    . GLY B 1 496  ? 103.429 117.030 94.635  1.00 18.50 ?  496  GLY B C    1 
ATOM   11151 O O    . GLY B 1 496  ? 104.019 116.175 94.014  1.00 22.30 ?  496  GLY B O    1 
ATOM   11152 N N    . ALA B 1 497  ? 103.817 117.439 95.822  1.00 15.57 ?  497  ALA B N    1 
ATOM   11153 C CA   . ALA B 1 497  ? 105.031 116.974 96.426  1.00 15.99 ?  497  ALA B CA   1 
ATOM   11154 C C    . ALA B 1 497  ? 105.039 115.513 96.625  1.00 11.99 ?  497  ALA B C    1 
ATOM   11155 O O    . ALA B 1 497  ? 106.078 114.911 96.516  1.00 13.20 ?  497  ALA B O    1 
ATOM   11156 C CB   . ALA B 1 497  ? 105.204 117.626 97.761  1.00 19.74 ?  497  ALA B CB   1 
ATOM   11157 N N    . VAL B 1 498  ? 103.926 114.910 96.963  1.00 11.64 ?  498  VAL B N    1 
ATOM   11158 C CA   . VAL B 1 498  ? 103.975 113.505 97.250  1.00 12.25 ?  498  VAL B CA   1 
ATOM   11159 C C    . VAL B 1 498  ? 103.942 112.744 95.968  1.00 15.54 ?  498  VAL B C    1 
ATOM   11160 O O    . VAL B 1 498  ? 104.558 111.718 95.859  1.00 20.50 ?  498  VAL B O    1 
ATOM   11161 C CB   . VAL B 1 498  ? 102.826 113.082 98.131  1.00 13.61 ?  498  VAL B CB   1 
ATOM   11162 C CG1  . VAL B 1 498  ? 102.614 111.583 98.055  1.00 17.21 ?  498  VAL B CG1  1 
ATOM   11163 C CG2  . VAL B 1 498  ? 103.089 113.524 99.558  1.00 17.41 ?  498  VAL B CG2  1 
ATOM   11164 N N    . ARG B 1 499  ? 103.238 113.226 94.974  1.00 17.55 ?  499  ARG B N    1 
ATOM   11165 C CA   . ARG B 1 499  ? 103.295 112.549 93.679  1.00 17.03 ?  499  ARG B CA   1 
ATOM   11166 C C    . ARG B 1 499  ? 104.689 112.626 93.066  1.00 15.98 ?  499  ARG B C    1 
ATOM   11167 O O    . ARG B 1 499  ? 105.217 111.618 92.573  1.00 21.47 ?  499  ARG B O    1 
ATOM   11168 C CB   . ARG B 1 499  ? 102.264 113.153 92.726  1.00 20.47 ?  499  ARG B CB   1 
ATOM   11169 C CG   . ARG B 1 499  ? 101.819 112.215 91.615  1.00 22.99 ?  499  ARG B CG   1 
ATOM   11170 C CD   . ARG B 1 499  ? 100.543 112.701 90.941  1.00 25.58 ?  499  ARG B CD   1 
ATOM   11171 N NE   . ARG B 1 499  ? 100.762 113.911 90.157  1.00 21.77 ?  499  ARG B NE   1 
ATOM   11172 C CZ   . ARG B 1 499  ? 101.198 113.924 88.905  1.00 22.68 ?  499  ARG B CZ   1 
ATOM   11173 N NH1  . ARG B 1 499  ? 101.477 112.804 88.259  1.00 23.06 1  499  ARG B NH1  1 
ATOM   11174 N NH2  . ARG B 1 499  ? 101.360 115.090 88.285  1.00 20.71 ?  499  ARG B NH2  1 
ATOM   11175 N N    . ARG B 1 500  ? 105.390 113.794 93.085  1.00 10.26 ?  500  ARG B N    1 
ATOM   11176 C CA   . ARG B 1 500  ? 106.706 113.873 92.460  1.00 14.02 ?  500  ARG B CA   1 
ATOM   11177 C C    . ARG B 1 500  ? 107.785 113.223 93.322  1.00 19.49 ?  500  ARG B C    1 
ATOM   11178 O O    . ARG B 1 500  ? 108.769 112.706 92.780  1.00 23.47 ?  500  ARG B O    1 
ATOM   11179 C CB   . ARG B 1 500  ? 107.058 115.323 92.119  1.00 8.62  ?  500  ARG B CB   1 
ATOM   11180 C CG   . ARG B 1 500  ? 107.609 116.164 93.244  1.00 11.77 ?  500  ARG B CG   1 
ATOM   11181 C CD   . ARG B 1 500  ? 108.499 117.264 92.678  1.00 14.06 ?  500  ARG B CD   1 
ATOM   11182 N NE   . ARG B 1 500  ? 108.030 117.762 91.389  1.00 17.53 ?  500  ARG B NE   1 
ATOM   11183 C CZ   . ARG B 1 500  ? 107.075 118.669 91.232  1.00 18.47 ?  500  ARG B CZ   1 
ATOM   11184 N NH1  . ARG B 1 500  ? 106.466 119.220 92.270  1.00 20.32 ?  500  ARG B NH1  1 
ATOM   11185 N NH2  . ARG B 1 500  ? 106.724 119.036 90.003  1.00 13.97 ?  500  ARG B NH2  1 
ATOM   11186 N N    . ILE B 1 501  ? 107.600 113.190 94.647  1.00 13.95 ?  501  ILE B N    1 
ATOM   11187 C CA   . ILE B 1 501  ? 108.490 112.405 95.501  1.00 6.09  ?  501  ILE B CA   1 
ATOM   11188 C C    . ILE B 1 501  ? 108.381 110.925 95.160  1.00 7.06  ?  501  ILE B C    1 
ATOM   11189 O O    . ILE B 1 501  ? 109.392 110.217 95.067  1.00 16.55 ?  501  ILE B O    1 
ATOM   11190 C CB   . ILE B 1 501  ? 108.175 112.675 96.985  1.00 9.11  ?  501  ILE B CB   1 
ATOM   11191 C CG1  . ILE B 1 501  ? 108.756 114.019 97.418  1.00 11.78 ?  501  ILE B CG1  1 
ATOM   11192 C CG2  . ILE B 1 501  ? 108.712 111.564 97.875  1.00 6.62  ?  501  ILE B CG2  1 
ATOM   11193 C CD1  . ILE B 1 501  ? 108.316 114.442 98.793  1.00 8.38  ?  501  ILE B CD1  1 
ATOM   11194 N N    . HIS B 1 502  ? 107.152 110.439 94.953  1.00 6.61  ?  502  HIS B N    1 
ATOM   11195 C CA   . HIS B 1 502  ? 106.948 109.045 94.569  1.00 4.33  ?  502  HIS B CA   1 
ATOM   11196 C C    . HIS B 1 502  ? 107.595 108.739 93.226  1.00 12.50 ?  502  HIS B C    1 
ATOM   11197 O O    . HIS B 1 502  ? 108.203 107.677 93.049  1.00 20.86 ?  502  HIS B O    1 
ATOM   11198 C CB   . HIS B 1 502  ? 105.455 108.731 94.510  1.00 7.52  ?  502  HIS B CB   1 
ATOM   11199 C CG   . HIS B 1 502  ? 104.887 108.240 95.802  1.00 13.71 ?  502  HIS B CG   1 
ATOM   11200 N ND1  . HIS B 1 502  ? 104.824 109.026 96.932  1.00 17.54 ?  502  HIS B ND1  1 
ATOM   11201 C CD2  . HIS B 1 502  ? 104.343 107.048 96.142  1.00 18.05 ?  502  HIS B CD2  1 
ATOM   11202 C CE1  . HIS B 1 502  ? 104.270 108.338 97.914  1.00 15.63 ?  502  HIS B CE1  1 
ATOM   11203 N NE2  . HIS B 1 502  ? 103.969 107.134 97.461  1.00 19.53 ?  502  HIS B NE2  1 
ATOM   11204 N N    . GLU B 1 503  ? 107.464 109.654 92.262  1.00 11.20 ?  503  GLU B N    1 
ATOM   11205 C CA   . GLU B 1 503  ? 108.065 109.430 90.949  1.00 13.23 ?  503  GLU B CA   1 
ATOM   11206 C C    . GLU B 1 503  ? 109.590 109.412 91.031  1.00 12.94 ?  503  GLU B C    1 
ATOM   11207 O O    . GLU B 1 503  ? 110.242 108.579 90.387  1.00 15.72 ?  503  GLU B O    1 
ATOM   11208 C CB   . GLU B 1 503  ? 107.590 110.496 89.960  1.00 11.81 ?  503  GLU B CB   1 
ATOM   11209 C CG   . GLU B 1 503  ? 106.098 110.463 89.534  1.00 18.20 ?  503  GLU B CG   1 
ATOM   11210 C CD   . GLU B 1 503  ? 105.504 109.091 89.175  1.00 19.63 ?  503  GLU B CD   1 
ATOM   11211 O OE1  . GLU B 1 503  ? 106.236 108.128 88.854  1.00 18.46 ?  503  GLU B OE1  1 
ATOM   11212 O OE2  . GLU B 1 503  ? 104.259 108.986 89.204  1.00 15.55 ?  503  GLU B OE2  1 
ATOM   11213 N N    . GLY B 1 504  ? 110.177 110.321 91.816  1.00 13.22 ?  504  GLY B N    1 
ATOM   11214 C CA   . GLY B 1 504  ? 111.620 110.302 92.002  1.00 11.26 ?  504  GLY B CA   1 
ATOM   11215 C C    . GLY B 1 504  ? 112.108 109.044 92.696  1.00 11.87 ?  504  GLY B C    1 
ATOM   11216 O O    . GLY B 1 504  ? 113.159 108.497 92.348  1.00 16.88 ?  504  GLY B O    1 
ATOM   11217 N N    . GLN B 1 505  ? 111.348 108.564 93.685  1.00 10.38 ?  505  GLN B N    1 
ATOM   11218 C CA   . GLN B 1 505  ? 111.700 107.318 94.359  1.00 8.83  ?  505  GLN B CA   1 
ATOM   11219 C C    . GLN B 1 505  ? 111.614 106.128 93.411  1.00 10.24 ?  505  GLN B C    1 
ATOM   11220 O O    . GLN B 1 505  ? 112.466 105.233 93.454  1.00 16.44 ?  505  GLN B O    1 
ATOM   11221 C CB   . GLN B 1 505  ? 110.795 107.106 95.571  1.00 4.44  ?  505  GLN B CB   1 
ATOM   11222 C CG   . GLN B 1 505  ? 111.311 107.744 96.848  1.00 8.02  ?  505  GLN B CG   1 
ATOM   11223 C CD   . GLN B 1 505  ? 110.421 107.463 98.040  1.00 11.91 ?  505  GLN B CD   1 
ATOM   11224 O OE1  . GLN B 1 505  ? 109.322 106.929 97.896  1.00 8.09  ?  505  GLN B OE1  1 
ATOM   11225 N NE2  . GLN B 1 505  ? 110.892 107.823 99.228  1.00 12.33 ?  505  GLN B NE2  1 
ATOM   11226 N N    . ASN B 1 506  ? 110.592 106.099 92.550  1.00 9.22  ?  506  ASN B N    1 
ATOM   11227 C CA   . ASN B 1 506  ? 110.480 105.029 91.562  1.00 7.07  ?  506  ASN B CA   1 
ATOM   11228 C C    . ASN B 1 506  ? 111.637 105.067 90.572  1.00 7.65  ?  506  ASN B C    1 
ATOM   11229 O O    . ASN B 1 506  ? 112.162 104.019 90.177  1.00 11.36 ?  506  ASN B O    1 
ATOM   11230 C CB   . ASN B 1 506  ? 109.146 105.130 90.824  1.00 10.37 ?  506  ASN B CB   1 
ATOM   11231 C CG   . ASN B 1 506  ? 108.520 103.775 90.560  1.00 10.03 ?  506  ASN B CG   1 
ATOM   11232 O OD1  . ASN B 1 506  ? 109.145 102.895 89.969  1.00 7.77  ?  506  ASN B OD1  1 
ATOM   11233 N ND2  . ASN B 1 506  ? 107.274 103.605 90.987  1.00 10.66 ?  506  ASN B ND2  1 
ATOM   11234 N N    . ARG B 1 507  ? 112.046 106.271 90.161  1.00 11.16 ?  507  ARG B N    1 
ATOM   11235 C CA   . ARG B 1 507  ? 113.195 106.407 89.268  1.00 10.85 ?  507  ARG B CA   1 
ATOM   11236 C C    . ARG B 1 507  ? 114.477 105.909 89.929  1.00 13.31 ?  507  ARG B C    1 
ATOM   11237 O O    . ARG B 1 507  ? 115.275 105.200 89.301  1.00 19.34 ?  507  ARG B O    1 
ATOM   11238 C CB   . ARG B 1 507  ? 113.341 107.865 88.839  1.00 11.93 ?  507  ARG B CB   1 
ATOM   11239 C CG   . ARG B 1 507  ? 114.544 108.154 87.960  1.00 14.64 ?  507  ARG B CG   1 
ATOM   11240 C CD   . ARG B 1 507  ? 114.211 109.153 86.859  1.00 19.72 ?  507  ARG B CD   1 
ATOM   11241 N NE   . ARG B 1 507  ? 113.128 110.060 87.225  1.00 14.42 ?  507  ARG B NE   1 
ATOM   11242 C CZ   . ARG B 1 507  ? 113.285 111.177 87.923  1.00 15.56 ?  507  ARG B CZ   1 
ATOM   11243 N NH1  . ARG B 1 507  ? 114.476 111.569 88.343  1.00 20.82 ?  507  ARG B NH1  1 
ATOM   11244 N NH2  . ARG B 1 507  ? 112.219 111.921 88.204  1.00 16.27 ?  507  ARG B NH2  1 
ATOM   11245 N N    . THR B 1 508  ? 114.687 106.264 91.200  1.00 12.19 ?  508  THR B N    1 
ATOM   11246 C CA   . THR B 1 508  ? 115.871 105.792 91.915  1.00 6.17  ?  508  THR B CA   1 
ATOM   11247 C C    . THR B 1 508  ? 115.852 104.276 92.088  1.00 0.08  ?  508  THR B C    1 
ATOM   11248 O O    . THR B 1 508  ? 116.890 103.616 91.956  1.00 2.80  ?  508  THR B O    1 
ATOM   11249 C CB   . THR B 1 508  ? 115.978 106.486 93.273  1.00 3.02  ?  508  THR B CB   1 
ATOM   11250 O OG1  . THR B 1 508  ? 115.849 107.902 93.096  1.00 11.69 ?  508  THR B OG1  1 
ATOM   11251 C CG2  . THR B 1 508  ? 117.321 106.190 93.915  1.00 3.19  ?  508  THR B CG2  1 
ATOM   11252 N N    . LEU B 1 509  ? 114.681 103.704 92.381  1.00 3.13  ?  509  LEU B N    1 
ATOM   11253 C CA   . LEU B 1 509  ? 114.576 102.256 92.530  1.00 2.92  ?  509  LEU B CA   1 
ATOM   11254 C C    . LEU B 1 509  ? 114.838 101.541 91.209  1.00 4.31  ?  509  LEU B C    1 
ATOM   11255 O O    . LEU B 1 509  ? 115.474 100.479 91.188  1.00 10.99 ?  509  LEU B O    1 
ATOM   11256 C CB   . LEU B 1 509  ? 113.199 101.889 93.085  1.00 3.27  ?  509  LEU B CB   1 
ATOM   11257 C CG   . LEU B 1 509  ? 113.042 100.613 93.918  1.00 0.20  ?  509  LEU B CG   1 
ATOM   11258 C CD1  . LEU B 1 509  ? 111.851 100.750 94.851  1.00 8.94  ?  509  LEU B CD1  1 
ATOM   11259 C CD2  . LEU B 1 509  ? 112.883 99.383  93.042  1.00 0.92  ?  509  LEU B CD2  1 
ATOM   11260 N N    . ASN B 1 510  ? 114.354 102.102 90.096  1.00 7.44  ?  510  ASN B N    1 
ATOM   11261 C CA   . ASN B 1 510  ? 114.630 101.511 88.790  1.00 9.09  ?  510  ASN B CA   1 
ATOM   11262 C C    . ASN B 1 510  ? 116.102 101.629 88.417  1.00 8.86  ?  510  ASN B C    1 
ATOM   11263 O O    . ASN B 1 510  ? 116.635 100.752 87.728  1.00 13.14 ?  510  ASN B O    1 
ATOM   11264 C CB   . ASN B 1 510  ? 113.758 102.164 87.720  1.00 10.73 ?  510  ASN B CB   1 
ATOM   11265 C CG   . ASN B 1 510  ? 113.147 101.153 86.770  1.00 13.24 ?  510  ASN B CG   1 
ATOM   11266 O OD1  . ASN B 1 510  ? 113.543 99.988  86.748  1.00 9.91  ?  510  ASN B OD1  1 
ATOM   11267 N ND2  . ASN B 1 510  ? 112.177 101.596 85.979  1.00 14.32 ?  510  ASN B ND2  1 
ATOM   11268 N N    . MET B 1 511  ? 116.766 102.708 88.839  1.00 8.55  ?  511  MET B N    1 
ATOM   11269 C CA   . MET B 1 511  ? 118.214 102.790 88.669  1.00 5.10  ?  511  MET B CA   1 
ATOM   11270 C C    . MET B 1 511  ? 118.923 101.721 89.491  1.00 4.31  ?  511  MET B C    1 
ATOM   11271 O O    . MET B 1 511  ? 119.883 101.099 89.021  1.00 6.30  ?  511  MET B O    1 
ATOM   11272 C CB   . MET B 1 511  ? 118.718 104.177 89.065  1.00 10.50 ?  511  MET B CB   1 
ATOM   11273 C CG   . MET B 1 511  ? 120.216 104.371 88.872  1.00 10.12 ?  511  MET B CG   1 
ATOM   11274 S SD   . MET B 1 511  ? 121.181 104.166 90.384  1.00 11.70 ?  511  MET B SD   1 
ATOM   11275 C CE   . MET B 1 511  ? 120.927 105.745 91.182  1.00 6.08  ?  511  MET B CE   1 
ATOM   11276 N N    . LEU B 1 512  ? 118.465 101.499 90.727  1.00 8.55  ?  512  LEU B N    1 
ATOM   11277 C CA   . LEU B 1 512  ? 119.129 100.547 91.613  1.00 4.80  ?  512  LEU B CA   1 
ATOM   11278 C C    . LEU B 1 512  ? 118.926 99.105  91.165  1.00 5.81  ?  512  LEU B C    1 
ATOM   11279 O O    . LEU B 1 512  ? 119.815 98.271  91.365  1.00 5.18  ?  512  LEU B O    1 
ATOM   11280 C CB   . LEU B 1 512  ? 118.628 100.717 93.046  1.00 1.07  ?  512  LEU B CB   1 
ATOM   11281 C CG   . LEU B 1 512  ? 119.136 101.922 93.834  1.00 2.10  ?  512  LEU B CG   1 
ATOM   11282 C CD1  . LEU B 1 512  ? 118.440 101.990 95.176  1.00 2.38  ?  512  LEU B CD1  1 
ATOM   11283 C CD2  . LEU B 1 512  ? 120.641 101.857 94.014  1.00 1.65  ?  512  LEU B CD2  1 
ATOM   11284 N N    . LYS B 1 513  ? 117.769 98.786  90.582  1.00 6.48  ?  513  LYS B N    1 
ATOM   11285 C CA   . LYS B 1 513  ? 117.510 97.411  90.164  1.00 3.91  ?  513  LYS B CA   1 
ATOM   11286 C C    . LYS B 1 513  ? 118.410 96.968  89.018  1.00 11.99 ?  513  LYS B C    1 
ATOM   11287 O O    . LYS B 1 513  ? 118.679 95.769  88.889  1.00 17.65 ?  513  LYS B O    1 
ATOM   11288 C CB   . LYS B 1 513  ? 116.042 97.242  89.769  1.00 3.56  ?  513  LYS B CB   1 
ATOM   11289 C CG   . LYS B 1 513  ? 115.097 97.137  90.954  1.00 5.99  ?  513  LYS B CG   1 
ATOM   11290 C CD   . LYS B 1 513  ? 113.680 96.808  90.517  1.00 7.31  ?  513  LYS B CD   1 
ATOM   11291 C CE   . LYS B 1 513  ? 113.271 95.420  90.976  1.00 9.31  ?  513  LYS B CE   1 
ATOM   11292 N NZ   . LYS B 1 513  ? 111.884 95.402  91.517  1.00 13.52 ?  513  LYS B NZ   1 
ATOM   11293 N N    . SER B 1 514  ? 118.885 97.899  88.191  1.00 17.18 ?  514  SER B N    1 
ATOM   11294 C CA   . SER B 1 514  ? 119.797 97.589  87.100  1.00 11.14 ?  514  SER B CA   1 
ATOM   11295 C C    . SER B 1 514  ? 121.262 97.736  87.498  1.00 9.41  ?  514  SER B C    1 
ATOM   11296 O O    . SER B 1 514  ? 122.115 97.942  86.628  1.00 13.35 ?  514  SER B O    1 
ATOM   11297 C CB   . SER B 1 514  ? 119.494 98.473  85.888  1.00 11.42 ?  514  SER B CB   1 
ATOM   11298 O OG   . SER B 1 514  ? 118.171 98.268  85.423  1.00 10.76 ?  514  SER B OG   1 
ATOM   11299 N N    . ASP B 1 515  ? 121.572 97.633  88.788  1.00 11.36 ?  515  ASP B N    1 
ATOM   11300 C CA   . ASP B 1 515  ? 122.942 97.732  89.264  1.00 12.23 ?  515  ASP B CA   1 
ATOM   11301 C C    . ASP B 1 515  ? 123.678 96.413  89.031  1.00 17.77 ?  515  ASP B C    1 
ATOM   11302 O O    . ASP B 1 515  ? 123.162 95.477  88.415  1.00 24.62 ?  515  ASP B O    1 
ATOM   11303 C CB   . ASP B 1 515  ? 122.963 98.111  90.744  1.00 11.44 ?  515  ASP B CB   1 
ATOM   11304 C CG   . ASP B 1 515  ? 124.108 99.036  91.094  1.00 14.06 ?  515  ASP B CG   1 
ATOM   11305 O OD1  . ASP B 1 515  ? 125.254 98.735  90.702  1.00 15.78 ?  515  ASP B OD1  1 
ATOM   11306 O OD2  . ASP B 1 515  ? 123.865 100.056 91.773  1.00 15.52 ?  515  ASP B OD2  1 
ATOM   11307 N N    . ARG B 1 516  ? 124.912 96.341  89.532  1.00 10.79 ?  516  ARG B N    1 
ATOM   11308 C CA   . ARG B 1 516  ? 125.710 95.127  89.463  1.00 14.65 ?  516  ARG B CA   1 
ATOM   11309 C C    . ARG B 1 516  ? 126.064 94.554  90.825  1.00 15.94 ?  516  ARG B C    1 
ATOM   11310 O O    . ARG B 1 516  ? 126.472 93.390  90.896  1.00 17.03 ?  516  ARG B O    1 
ATOM   11311 C CB   . ARG B 1 516  ? 127.008 95.384  88.678  1.00 18.19 ?  516  ARG B CB   1 
ATOM   11312 C CG   . ARG B 1 516  ? 127.464 94.217  87.814  1.00 18.41 ?  516  ARG B CG   1 
ATOM   11313 C CD   . ARG B 1 516  ? 128.769 94.526  87.085  1.00 19.63 ?  516  ARG B CD   1 
ATOM   11314 N NE   . ARG B 1 516  ? 129.952 94.420  87.933  1.00 19.07 ?  516  ARG B NE   1 
ATOM   11315 C CZ   . ARG B 1 516  ? 130.569 95.451  88.494  1.00 16.09 ?  516  ARG B CZ   1 
ATOM   11316 N NH1  . ARG B 1 516  ? 130.114 96.686  88.361  1.00 14.04 ?  516  ARG B NH1  1 
ATOM   11317 N NH2  . ARG B 1 516  ? 131.673 95.238  89.205  1.00 15.56 ?  516  ARG B NH2  1 
ATOM   11318 N N    . PHE B 1 517  ? 125.916 95.326  91.898  1.00 16.35 ?  517  PHE B N    1 
ATOM   11319 C CA   . PHE B 1 517  ? 126.230 94.878  93.248  1.00 10.81 ?  517  PHE B CA   1 
ATOM   11320 C C    . PHE B 1 517  ? 125.009 94.716  94.138  1.00 8.89  ?  517  PHE B C    1 
ATOM   11321 O O    . PHE B 1 517  ? 124.989 93.807  94.968  1.00 12.46 ?  517  PHE B O    1 
ATOM   11322 C CB   . PHE B 1 517  ? 127.214 95.852  93.911  1.00 10.26 ?  517  PHE B CB   1 
ATOM   11323 C CG   . PHE B 1 517  ? 128.639 95.703  93.437  1.00 13.95 ?  517  PHE B CG   1 
ATOM   11324 C CD1  . PHE B 1 517  ? 128.994 94.716  92.529  1.00 12.92 ?  517  PHE B CD1  1 
ATOM   11325 C CD2  . PHE B 1 517  ? 129.634 96.517  93.949  1.00 13.51 ?  517  PHE B CD2  1 
ATOM   11326 C CE1  . PHE B 1 517  ? 130.306 94.574  92.115  1.00 12.80 ?  517  PHE B CE1  1 
ATOM   11327 C CE2  . PHE B 1 517  ? 130.945 96.385  93.535  1.00 12.50 ?  517  PHE B CE2  1 
ATOM   11328 C CZ   . PHE B 1 517  ? 131.282 95.410  92.620  1.00 12.26 ?  517  PHE B CZ   1 
ATOM   11329 N N    . LEU B 1 518  ? 123.986 95.558  93.981  1.00 5.66  ?  518  LEU B N    1 
ATOM   11330 C CA   . LEU B 1 518  ? 122.750 95.432  94.745  1.00 0.00  ?  518  LEU B CA   1 
ATOM   11331 C C    . LEU B 1 518  ? 121.697 94.602  94.020  1.00 4.89  ?  518  LEU B C    1 
ATOM   11332 O O    . LEU B 1 518  ? 120.497 94.805  94.238  1.00 12.86 ?  518  LEU B O    1 
ATOM   11333 C CB   . LEU B 1 518  ? 122.194 96.816  95.085  1.00 0.00  ?  518  LEU B CB   1 
ATOM   11334 C CG   . LEU B 1 518  ? 123.164 97.863  95.633  1.00 0.00  ?  518  LEU B CG   1 
ATOM   11335 C CD1  . LEU B 1 518  ? 122.425 99.146  95.970  1.00 6.93  ?  518  LEU B CD1  1 
ATOM   11336 C CD2  . LEU B 1 518  ? 123.887 97.334  96.860  1.00 0.00  ?  518  LEU B CD2  1 
ATOM   11337 N N    . ALA B 1 519  ? 122.115 93.665  93.169  1.00 4.22  ?  519  ALA B N    1 
ATOM   11338 C CA   . ALA B 1 519  ? 121.181 92.873  92.380  1.00 7.64  ?  519  ALA B CA   1 
ATOM   11339 C C    . ALA B 1 519  ? 120.561 91.723  93.160  1.00 9.81  ?  519  ALA B C    1 
ATOM   11340 O O    . ALA B 1 519  ? 119.659 91.060  92.638  1.00 7.31  ?  519  ALA B O    1 
ATOM   11341 C CB   . ALA B 1 519  ? 121.880 92.323  91.135  1.00 10.71 ?  519  ALA B CB   1 
ATOM   11342 N N    . ASP B 1 520  ? 121.015 91.469  94.386  1.00 7.77  ?  520  ASP B N    1 
ATOM   11343 C CA   . ASP B 1 520  ? 120.457 90.406  95.210  1.00 6.34  ?  520  ASP B CA   1 
ATOM   11344 C C    . ASP B 1 520  ? 119.706 90.927  96.430  1.00 5.88  ?  520  ASP B C    1 
ATOM   11345 O O    . ASP B 1 520  ? 119.312 90.130  97.286  1.00 11.80 ?  520  ASP B O    1 
ATOM   11346 C CB   . ASP B 1 520  ? 121.564 89.406  95.590  1.00 8.60  ?  520  ASP B CB   1 
ATOM   11347 C CG   . ASP B 1 520  ? 122.573 89.933  96.628  1.00 15.60 ?  520  ASP B CG   1 
ATOM   11348 O OD1  . ASP B 1 520  ? 122.221 90.589  97.629  1.00 19.44 ?  520  ASP B OD1  1 
ATOM   11349 O OD2  . ASP B 1 520  ? 123.776 89.665  96.424  1.00 12.39 ?  520  ASP B OD2  1 
ATOM   11350 N N    . ALA B 1 521  ? 119.496 92.237  96.526  1.00 2.83  ?  521  ALA B N    1 
ATOM   11351 C CA   . ALA B 1 521  ? 118.816 92.813  97.676  1.00 2.99  ?  521  ALA B CA   1 
ATOM   11352 C C    . ALA B 1 521  ? 117.348 92.404  97.705  1.00 8.33  ?  521  ALA B C    1 
ATOM   11353 O O    . ALA B 1 521  ? 116.746 92.091  96.675  1.00 13.49 ?  521  ALA B O    1 
ATOM   11354 C CB   . ALA B 1 521  ? 118.928 94.336  97.656  1.00 1.09  ?  521  ALA B CB   1 
ATOM   11355 N N    . ASP B 1 522  ? 116.772 92.411  98.904  1.00 6.61  ?  522  ASP B N    1 
ATOM   11356 C CA   . ASP B 1 522  ? 115.361 92.077  99.079  1.00 10.03 ?  522  ASP B CA   1 
ATOM   11357 C C    . ASP B 1 522  ? 114.543 93.294  98.675  1.00 12.62 ?  522  ASP B C    1 
ATOM   11358 O O    . ASP B 1 522  ? 114.381 94.239  99.450  1.00 16.63 ?  522  ASP B O    1 
ATOM   11359 C CB   . ASP B 1 522  ? 115.079 91.659  100.517 1.00 12.43 ?  522  ASP B CB   1 
ATOM   11360 C CG   . ASP B 1 522  ? 114.847 90.168  100.651 1.00 16.13 ?  522  ASP B CG   1 
ATOM   11361 O OD1  . ASP B 1 522  ? 115.339 89.413  99.788  1.00 15.42 ?  522  ASP B OD1  1 
ATOM   11362 O OD2  . ASP B 1 522  ? 114.177 89.749  101.618 1.00 17.75 ?  522  ASP B OD2  1 
ATOM   11363 N N    . TRP B 1 523  ? 114.027 93.274  97.447  1.00 9.73  ?  523  TRP B N    1 
ATOM   11364 C CA   . TRP B 1 523  ? 113.367 94.447  96.894  1.00 9.49  ?  523  TRP B CA   1 
ATOM   11365 C C    . TRP B 1 523  ? 111.973 94.666  97.458  1.00 14.90 ?  523  TRP B C    1 
ATOM   11366 O O    . TRP B 1 523  ? 111.474 95.796  97.409  1.00 18.33 ?  523  TRP B O    1 
ATOM   11367 C CB   . TRP B 1 523  ? 113.311 94.338  95.371  1.00 10.12 ?  523  TRP B CB   1 
ATOM   11368 C CG   . TRP B 1 523  ? 114.660 94.476  94.744  1.00 9.80  ?  523  TRP B CG   1 
ATOM   11369 C CD1  . TRP B 1 523  ? 115.343 93.522  94.049  1.00 9.54  ?  523  TRP B CD1  1 
ATOM   11370 C CD2  . TRP B 1 523  ? 115.504 95.632  94.774  1.00 8.79  ?  523  TRP B CD2  1 
ATOM   11371 N NE1  . TRP B 1 523  ? 116.555 94.017  93.634  1.00 7.47  ?  523  TRP B NE1  1 
ATOM   11372 C CE2  . TRP B 1 523  ? 116.677 95.311  94.068  1.00 8.17  ?  523  TRP B CE2  1 
ATOM   11373 C CE3  . TRP B 1 523  ? 115.378 96.912  95.324  1.00 6.10  ?  523  TRP B CE3  1 
ATOM   11374 C CZ2  . TRP B 1 523  ? 117.715 96.219  93.898  1.00 8.18  ?  523  TRP B CZ2  1 
ATOM   11375 C CZ3  . TRP B 1 523  ? 116.409 97.810  95.156  1.00 3.80  ?  523  TRP B CZ3  1 
ATOM   11376 C CH2  . TRP B 1 523  ? 117.563 97.461  94.449  1.00 7.81  ?  523  TRP B CH2  1 
ATOM   11377 N N    . ASP B 1 524  ? 111.339 93.622  97.997  1.00 15.48 ?  524  ASP B N    1 
ATOM   11378 C CA   . ASP B 1 524  ? 110.067 93.806  98.686  1.00 13.01 ?  524  ASP B CA   1 
ATOM   11379 C C    . ASP B 1 524  ? 110.242 94.691  99.913  1.00 13.95 ?  524  ASP B C    1 
ATOM   11380 O O    . ASP B 1 524  ? 109.449 95.611  100.149 1.00 13.75 ?  524  ASP B O    1 
ATOM   11381 C CB   . ASP B 1 524  ? 109.481 92.450  99.079  1.00 15.73 ?  524  ASP B CB   1 
ATOM   11382 C CG   . ASP B 1 524  ? 109.541 91.440  97.951  1.00 20.82 ?  524  ASP B CG   1 
ATOM   11383 O OD1  . ASP B 1 524  ? 108.647 91.467  97.080  1.00 21.65 ?  524  ASP B OD1  1 
ATOM   11384 O OD2  . ASP B 1 524  ? 110.481 90.617  97.936  1.00 20.65 ?  524  ASP B OD2  1 
ATOM   11385 N N    . ILE B 1 525  ? 111.297 94.439  100.693 1.00 14.19 ?  525  ILE B N    1 
ATOM   11386 C CA   . ILE B 1 525  ? 111.551 95.219  101.903 1.00 11.92 ?  525  ILE B CA   1 
ATOM   11387 C C    . ILE B 1 525  ? 111.838 96.673  101.549 1.00 10.19 ?  525  ILE B C    1 
ATOM   11388 O O    . ILE B 1 525  ? 111.287 97.596  102.159 1.00 11.55 ?  525  ILE B O    1 
ATOM   11389 C CB   . ILE B 1 525  ? 112.699 94.593  102.721 1.00 12.92 ?  525  ILE B CB   1 
ATOM   11390 C CG1  . ILE B 1 525  ? 112.209 93.391  103.536 1.00 15.27 ?  525  ILE B CG1  1 
ATOM   11391 C CG2  . ILE B 1 525  ? 113.325 95.616  103.658 1.00 10.55 ?  525  ILE B CG2  1 
ATOM   11392 C CD1  . ILE B 1 525  ? 112.138 92.085  102.774 1.00 13.83 ?  525  ILE B CD1  1 
ATOM   11393 N N    . ALA B 1 526  ? 112.691 96.897  100.545 1.00 11.19 ?  526  ALA B N    1 
ATOM   11394 C CA   . ALA B 1 526  ? 113.035 98.262  100.155 1.00 10.44 ?  526  ALA B CA   1 
ATOM   11395 C C    . ALA B 1 526  ? 111.827 99.006  99.597  1.00 13.16 ?  526  ALA B C    1 
ATOM   11396 O O    . ALA B 1 526  ? 111.585 100.167 99.952  1.00 14.43 ?  526  ALA B O    1 
ATOM   11397 C CB   . ALA B 1 526  ? 114.173 98.245  99.135  1.00 8.96  ?  526  ALA B CB   1 
ATOM   11398 N N    . THR B 1 527  ? 111.047 98.346  98.737  1.00 14.96 ?  527  THR B N    1 
ATOM   11399 C CA   . THR B 1 527  ? 109.877 98.989  98.147  1.00 14.78 ?  527  THR B CA   1 
ATOM   11400 C C    . THR B 1 527  ? 108.821 99.306  99.200  1.00 16.03 ?  527  THR B C    1 
ATOM   11401 O O    . THR B 1 527  ? 108.187 100.367 99.149  1.00 15.41 ?  527  THR B O    1 
ATOM   11402 C CB   . THR B 1 527  ? 109.290 98.104  97.049  1.00 11.83 ?  527  THR B CB   1 
ATOM   11403 O OG1  . THR B 1 527  ? 110.354 97.513  96.292  1.00 10.08 ?  527  THR B OG1  1 
ATOM   11404 C CG2  . THR B 1 527  ? 108.414 98.925  96.119  1.00 15.41 ?  527  THR B CG2  1 
ATOM   11405 N N    . ALA B 1 528  ? 108.614 98.405  100.164 1.00 17.56 ?  528  ALA B N    1 
ATOM   11406 C CA   . ALA B 1 528  ? 107.609 98.644  101.192 1.00 14.88 ?  528  ALA B CA   1 
ATOM   11407 C C    . ALA B 1 528  ? 108.074 99.643  102.244 1.00 13.75 ?  528  ALA B C    1 
ATOM   11408 O O    . ALA B 1 528  ? 107.244 100.353 102.820 1.00 19.01 ?  528  ALA B O    1 
ATOM   11409 C CB   . ALA B 1 528  ? 107.218 97.326  101.860 1.00 13.09 ?  528  ALA B CB   1 
ATOM   11410 N N    . ALA B 1 529  ? 109.377 99.717  102.514 1.00 12.08 ?  529  ALA B N    1 
ATOM   11411 C CA   . ALA B 1 529  ? 109.904 100.575 103.563 1.00 10.61 ?  529  ALA B CA   1 
ATOM   11412 C C    . ALA B 1 529  ? 110.470 101.887 103.042 1.00 14.19 ?  529  ALA B C    1 
ATOM   11413 O O    . ALA B 1 529  ? 111.018 102.661 103.831 1.00 14.34 ?  529  ALA B O    1 
ATOM   11414 C CB   . ALA B 1 529  ? 110.982 99.832  104.357 1.00 11.97 ?  529  ALA B CB   1 
ATOM   11415 N N    . CYS B 1 530  ? 110.369 102.153 101.738 1.00 20.68 ?  530  CYS B N    1 
ATOM   11416 C CA   . CYS B 1 530  ? 110.836 103.419 101.195 1.00 17.72 ?  530  CYS B CA   1 
ATOM   11417 C C    . CYS B 1 530  ? 109.719 104.353 100.749 1.00 20.31 ?  530  CYS B C    1 
ATOM   11418 O O    . CYS B 1 530  ? 109.971 105.551 100.594 1.00 20.21 ?  530  CYS B O    1 
ATOM   11419 C CB   . CYS B 1 530  ? 111.785 103.172 100.015 1.00 15.32 ?  530  CYS B CB   1 
ATOM   11420 S SG   . CYS B 1 530  ? 113.451 102.693 100.525 1.00 29.99 ?  530  CYS B SG   1 
ATOM   11421 N N    . GLU B 1 531  ? 108.507 103.847 100.543 1.00 21.17 ?  531  GLU B N    1 
ATOM   11422 C CA   . GLU B 1 531  ? 107.395 104.698 100.147 1.00 22.81 ?  531  GLU B CA   1 
ATOM   11423 C C    . GLU B 1 531  ? 106.894 105.517 101.332 1.00 22.26 ?  531  GLU B C    1 
ATOM   11424 O O    . GLU B 1 531  ? 106.996 105.105 102.491 1.00 20.49 ?  531  GLU B O    1 
ATOM   11425 C CB   . GLU B 1 531  ? 106.254 103.863 99.561  1.00 22.19 ?  531  GLU B CB   1 
ATOM   11426 C CG   . GLU B 1 531  ? 105.470 103.047 100.580 1.00 21.90 ?  531  GLU B CG   1 
ATOM   11427 C CD   . GLU B 1 531  ? 104.198 102.457 100.002 1.00 25.59 ?  531  GLU B CD   1 
ATOM   11428 O OE1  . GLU B 1 531  ? 103.313 103.237 99.592  1.00 28.59 ?  531  GLU B OE1  1 
ATOM   11429 O OE2  . GLU B 1 531  ? 104.082 101.214 99.958  1.00 21.71 ?  531  GLU B OE2  1 
ATOM   11430 N N    . ILE B 1 532  ? 106.355 106.696 101.028 1.00 24.39 ?  532  ILE B N    1 
ATOM   11431 C CA   . ILE B 1 532  ? 105.842 107.615 102.034 1.00 25.35 ?  532  ILE B CA   1 
ATOM   11432 C C    . ILE B 1 532  ? 104.339 107.784 101.824 1.00 27.44 ?  532  ILE B C    1 
ATOM   11433 O O    . ILE B 1 532  ? 103.783 107.392 100.798 1.00 26.74 ?  532  ILE B O    1 
ATOM   11434 C CB   . ILE B 1 532  ? 106.569 108.977 102.010 1.00 25.64 ?  532  ILE B CB   1 
ATOM   11435 C CG1  . ILE B 1 532  ? 105.909 109.942 101.022 1.00 22.15 ?  532  ILE B CG1  1 
ATOM   11436 C CG2  . ILE B 1 532  ? 108.045 108.799 101.680 1.00 24.83 ?  532  ILE B CG2  1 
ATOM   11437 C CD1  . ILE B 1 532  ? 106.303 111.385 101.233 1.00 23.17 ?  532  ILE B CD1  1 
ATOM   11438 N N    . SER B 1 533  ? 103.681 108.364 102.826 1.00 23.07 ?  533  SER B N    1 
ATOM   11439 C CA   . SER B 1 533  ? 102.244 108.587 102.794 1.00 23.14 ?  533  SER B CA   1 
ATOM   11440 C C    . SER B 1 533  ? 101.939 110.074 102.918 1.00 21.51 ?  533  SER B C    1 
ATOM   11441 O O    . SER B 1 533  ? 102.702 110.835 103.521 1.00 19.68 ?  533  SER B O    1 
ATOM   11442 C CB   . SER B 1 533  ? 101.534 107.818 103.916 1.00 22.21 ?  533  SER B CB   1 
ATOM   11443 O OG   . SER B 1 533  ? 101.183 106.511 103.497 1.00 24.50 ?  533  SER B OG   1 
ATOM   11444 N N    . ASP B 1 534  ? 100.819 110.477 102.331 1.00 21.45 ?  534  ASP B N    1 
ATOM   11445 C CA   . ASP B 1 534  ? 100.372 111.861 102.433 1.00 22.44 ?  534  ASP B CA   1 
ATOM   11446 C C    . ASP B 1 534  ? 99.951  112.158 103.868 1.00 23.28 ?  534  ASP B C    1 
ATOM   11447 O O    . ASP B 1 534  ? 99.138  111.417 104.434 1.00 19.62 ?  534  ASP B O    1 
ATOM   11448 C CB   . ASP B 1 534  ? 99.205  112.108 101.476 1.00 21.42 ?  534  ASP B CB   1 
ATOM   11449 C CG   . ASP B 1 534  ? 99.179  113.524 100.930 1.00 21.81 ?  534  ASP B CG   1 
ATOM   11450 O OD1  . ASP B 1 534  ? 99.770  114.424 101.559 1.00 18.96 ?  534  ASP B OD1  1 
ATOM   11451 O OD2  . ASP B 1 534  ? 98.559  113.737 99.867  1.00 20.94 ?  534  ASP B OD2  1 
ATOM   11452 N N    . PRO B 1 535  ? 100.497 113.203 104.500 1.00 26.06 ?  535  PRO B N    1 
ATOM   11453 C CA   . PRO B 1 535  ? 100.025 113.571 105.846 1.00 28.03 ?  535  PRO B CA   1 
ATOM   11454 C C    . PRO B 1 535  ? 98.552  113.941 105.896 1.00 29.83 ?  535  PRO B C    1 
ATOM   11455 O O    . PRO B 1 535  ? 97.901  113.713 106.923 1.00 28.46 ?  535  PRO B O    1 
ATOM   11456 C CB   . PRO B 1 535  ? 100.921 114.761 106.216 1.00 23.86 ?  535  PRO B CB   1 
ATOM   11457 C CG   . PRO B 1 535  ? 102.147 114.579 105.390 1.00 22.71 ?  535  PRO B CG   1 
ATOM   11458 C CD   . PRO B 1 535  ? 101.682 113.979 104.098 1.00 24.68 ?  535  PRO B CD   1 
ATOM   11459 N N    . TYR B 1 536  ? 98.007  114.503 104.822 1.00 27.94 ?  536  TYR B N    1 
ATOM   11460 C CA   . TYR B 1 536  ? 96.591  114.845 104.774 1.00 27.33 ?  536  TYR B CA   1 
ATOM   11461 C C    . TYR B 1 536  ? 95.821  113.866 103.893 1.00 23.47 ?  536  TYR B C    1 
ATOM   11462 O O    . TYR B 1 536  ? 96.362  112.849 103.459 1.00 22.37 ?  536  TYR B O    1 
ATOM   11463 C CB   . TYR B 1 536  ? 96.400  116.273 104.264 1.00 25.08 ?  536  TYR B CB   1 
ATOM   11464 C CG   . TYR B 1 536  ? 97.306  117.285 104.926 1.00 26.68 ?  536  TYR B CG   1 
ATOM   11465 C CD1  . TYR B 1 536  ? 97.199  117.558 106.284 1.00 24.54 ?  536  TYR B CD1  1 
ATOM   11466 C CD2  . TYR B 1 536  ? 98.269  117.967 104.194 1.00 24.46 ?  536  TYR B CD2  1 
ATOM   11467 C CE1  . TYR B 1 536  ? 98.026  118.482 106.894 1.00 26.64 ?  536  TYR B CE1  1 
ATOM   11468 C CE2  . TYR B 1 536  ? 99.100  118.894 104.795 1.00 22.71 ?  536  TYR B CE2  1 
ATOM   11469 C CZ   . TYR B 1 536  ? 98.974  119.147 106.145 1.00 25.62 ?  536  TYR B CZ   1 
ATOM   11470 O OH   . TYR B 1 536  ? 99.799  120.068 106.748 1.00 22.60 ?  536  TYR B OH   1 
ATOM   11471 N N    . PRO B 1 570  ? 83.016  134.178 76.290  1.00 26.21 ?  570  PRO B N    1 
ATOM   11472 C CA   . PRO B 1 570  ? 81.922  135.029 75.813  1.00 26.75 ?  570  PRO B CA   1 
ATOM   11473 C C    . PRO B 1 570  ? 80.911  135.358 76.909  1.00 28.66 ?  570  PRO B C    1 
ATOM   11474 O O    . PRO B 1 570  ? 80.508  136.513 77.046  1.00 30.95 ?  570  PRO B O    1 
ATOM   11475 C CB   . PRO B 1 570  ? 81.278  134.182 74.714  1.00 26.43 ?  570  PRO B CB   1 
ATOM   11476 C CG   . PRO B 1 570  ? 82.395  133.348 74.194  1.00 28.17 ?  570  PRO B CG   1 
ATOM   11477 C CD   . PRO B 1 570  ? 83.287  133.057 75.372  1.00 27.12 ?  570  PRO B CD   1 
ATOM   11478 N N    . SER B 1 571  ? 80.507  134.345 77.670  1.00 24.06 ?  571  SER B N    1 
ATOM   11479 C CA   . SER B 1 571  ? 79.552  134.559 78.747  1.00 26.51 ?  571  SER B CA   1 
ATOM   11480 C C    . SER B 1 571  ? 80.202  135.352 79.880  1.00 27.80 ?  571  SER B C    1 
ATOM   11481 O O    . SER B 1 571  ? 81.391  135.170 80.162  1.00 24.35 ?  571  SER B O    1 
ATOM   11482 C CB   . SER B 1 571  ? 79.033  133.223 79.275  1.00 22.70 ?  571  SER B CB   1 
ATOM   11483 O OG   . SER B 1 571  ? 78.312  133.397 80.482  1.00 21.83 ?  571  SER B OG   1 
ATOM   11484 N N    . PRO B 1 572  ? 79.458  136.255 80.527  1.00 24.78 ?  572  PRO B N    1 
ATOM   11485 C CA   . PRO B 1 572  ? 80.020  136.977 81.681  1.00 25.15 ?  572  PRO B CA   1 
ATOM   11486 C C    . PRO B 1 572  ? 80.415  136.071 82.836  1.00 23.62 ?  572  PRO B C    1 
ATOM   11487 O O    . PRO B 1 572  ? 81.409  136.354 83.519  1.00 22.38 ?  572  PRO B O    1 
ATOM   11488 C CB   . PRO B 1 572  ? 78.888  137.936 82.079  1.00 24.35 ?  572  PRO B CB   1 
ATOM   11489 C CG   . PRO B 1 572  ? 78.044  138.067 80.849  1.00 24.51 ?  572  PRO B CG   1 
ATOM   11490 C CD   . PRO B 1 572  ? 78.111  136.733 80.175  1.00 20.85 ?  572  PRO B CD   1 
ATOM   11491 N N    . ARG B 1 573  ? 79.667  134.991 83.076  1.00 23.20 ?  573  ARG B N    1 
ATOM   11492 C CA   . ARG B 1 573  ? 80.026  134.061 84.143  1.00 25.45 ?  573  ARG B CA   1 
ATOM   11493 C C    . ARG B 1 573  ? 81.325  133.331 83.825  1.00 25.30 ?  573  ARG B C    1 
ATOM   11494 O O    . ARG B 1 573  ? 82.174  133.148 84.707  1.00 20.52 ?  573  ARG B O    1 
ATOM   11495 C CB   . ARG B 1 573  ? 78.888  133.069 84.379  1.00 25.52 ?  573  ARG B CB   1 
ATOM   11496 C CG   . ARG B 1 573  ? 77.504  133.640 84.107  1.00 23.62 ?  573  ARG B CG   1 
ATOM   11497 C CD   . ARG B 1 573  ? 76.909  134.277 85.356  1.00 21.73 ?  573  ARG B CD   1 
ATOM   11498 N NE   . ARG B 1 573  ? 77.418  135.625 85.580  1.00 23.57 ?  573  ARG B NE   1 
ATOM   11499 C CZ   . ARG B 1 573  ? 76.957  136.713 84.978  1.00 27.07 ?  573  ARG B CZ   1 
ATOM   11500 N NH1  . ARG B 1 573  ? 75.964  136.651 84.105  1.00 27.66 ?  573  ARG B NH1  1 
ATOM   11501 N NH2  . ARG B 1 573  ? 77.504  137.892 85.258  1.00 23.22 ?  573  ARG B NH2  1 
ATOM   11502 N N    . GLU B 1 574  ? 81.502  132.917 82.567  1.00 32.13 ?  574  GLU B N    1 
ATOM   11503 C CA   . GLU B 1 574  ? 82.765  132.312 82.155  1.00 31.26 ?  574  GLU B CA   1 
ATOM   11504 C C    . GLU B 1 574  ? 83.916  133.301 82.282  1.00 32.18 ?  574  GLU B C    1 
ATOM   11505 O O    . GLU B 1 574  ? 85.014  132.934 82.717  1.00 25.87 ?  574  GLU B O    1 
ATOM   11506 C CB   . GLU B 1 574  ? 82.658  131.795 80.721  1.00 28.46 ?  574  GLU B CB   1 
ATOM   11507 C CG   . GLU B 1 574  ? 81.577  130.749 80.514  1.00 28.77 ?  574  GLU B CG   1 
ATOM   11508 C CD   . GLU B 1 574  ? 82.091  129.338 80.718  1.00 33.88 ?  574  GLU B CD   1 
ATOM   11509 O OE1  . GLU B 1 574  ? 83.293  129.101 80.471  1.00 34.22 ?  574  GLU B OE1  1 
ATOM   11510 O OE2  . GLU B 1 574  ? 81.295  128.466 81.123  1.00 34.83 ?  574  GLU B OE2  1 
ATOM   11511 N N    . PHE B 1 575  ? 83.680  134.562 81.904  1.00 30.80 ?  575  PHE B N    1 
ATOM   11512 C CA   . PHE B 1 575  ? 84.708  135.590 82.036  1.00 28.56 ?  575  PHE B CA   1 
ATOM   11513 C C    . PHE B 1 575  ? 85.104  135.787 83.493  1.00 28.30 ?  575  PHE B C    1 
ATOM   11514 O O    . PHE B 1 575  ? 86.292  135.914 83.808  1.00 26.53 ?  575  PHE B O    1 
ATOM   11515 C CB   . PHE B 1 575  ? 84.212  136.904 81.431  1.00 28.18 ?  575  PHE B CB   1 
ATOM   11516 C CG   . PHE B 1 575  ? 85.300  137.912 81.191  1.00 31.65 ?  575  PHE B CG   1 
ATOM   11517 C CD1  . PHE B 1 575  ? 86.080  137.853 80.048  1.00 31.07 ?  575  PHE B CD1  1 
ATOM   11518 C CD2  . PHE B 1 575  ? 85.537  138.924 82.107  1.00 30.15 ?  575  PHE B CD2  1 
ATOM   11519 C CE1  . PHE B 1 575  ? 87.079  138.783 79.825  1.00 28.46 ?  575  PHE B CE1  1 
ATOM   11520 C CE2  . PHE B 1 575  ? 86.535  139.857 81.891  1.00 29.70 ?  575  PHE B CE2  1 
ATOM   11521 C CZ   . PHE B 1 575  ? 87.306  139.786 80.748  1.00 27.28 ?  575  PHE B CZ   1 
ATOM   11522 N N    . ALA B 1 576  ? 84.121  135.794 84.398  1.00 26.54 ?  576  ALA B N    1 
ATOM   11523 C CA   . ALA B 1 576  ? 84.422  135.896 85.822  1.00 28.59 ?  576  ALA B CA   1 
ATOM   11524 C C    . ALA B 1 576  ? 85.186  134.673 86.316  1.00 27.17 ?  576  ALA B C    1 
ATOM   11525 O O    . ALA B 1 576  ? 86.065  134.788 87.179  1.00 23.51 ?  576  ALA B O    1 
ATOM   11526 C CB   . ALA B 1 576  ? 83.132  136.082 86.621  1.00 25.95 ?  576  ALA B CB   1 
ATOM   11527 N N    . ASP B 1 577  ? 84.868  133.493 85.775  1.00 24.06 ?  577  ASP B N    1 
ATOM   11528 C CA   . ASP B 1 577  ? 85.568  132.276 86.179  1.00 25.70 ?  577  ASP B CA   1 
ATOM   11529 C C    . ASP B 1 577  ? 87.044  132.331 85.795  1.00 25.93 ?  577  ASP B C    1 
ATOM   11530 O O    . ASP B 1 577  ? 87.924  132.060 86.626  1.00 25.51 ?  577  ASP B O    1 
ATOM   11531 C CB   . ASP B 1 577  ? 84.891  131.054 85.557  1.00 23.83 ?  577  ASP B CB   1 
ATOM   11532 C CG   . ASP B 1 577  ? 83.601  130.681 86.262  1.00 25.02 ?  577  ASP B CG   1 
ATOM   11533 O OD1  . ASP B 1 577  ? 83.380  131.164 87.393  1.00 22.69 ?  577  ASP B OD1  1 
ATOM   11534 O OD2  . ASP B 1 577  ? 82.809  129.906 85.687  1.00 29.52 ?  577  ASP B OD2  1 
ATOM   11535 N N    . MET B 1 578  ? 87.340  132.691 84.540  1.00 26.74 ?  578  MET B N    1 
ATOM   11536 C CA   . MET B 1 578  ? 88.748  132.812 84.155  1.00 26.33 ?  578  MET B CA   1 
ATOM   11537 C C    . MET B 1 578  ? 89.431  133.986 84.848  1.00 28.49 ?  578  MET B C    1 
ATOM   11538 O O    . MET B 1 578  ? 90.637  133.920 85.108  1.00 26.75 ?  578  MET B O    1 
ATOM   11539 C CB   . MET B 1 578  ? 88.928  132.923 82.636  1.00 22.70 ?  578  MET B CB   1 
ATOM   11540 C CG   . MET B 1 578  ? 87.845  132.299 81.789  1.00 26.80 ?  578  MET B CG   1 
ATOM   11541 S SD   . MET B 1 578  ? 88.346  131.972 80.088  1.00 36.64 ?  578  MET B SD   1 
ATOM   11542 C CE   . MET B 1 578  ? 89.241  133.471 79.701  1.00 27.31 ?  578  MET B CE   1 
ATOM   11543 N N    . MET B 1 579  ? 88.691  135.051 85.173  1.00 30.99 ?  579  MET B N    1 
ATOM   11544 C CA   . MET B 1 579  ? 89.273  136.154 85.932  1.00 28.72 ?  579  MET B CA   1 
ATOM   11545 C C    . MET B 1 579  ? 89.705  135.697 87.322  1.00 29.16 ?  579  MET B C    1 
ATOM   11546 O O    . MET B 1 579  ? 90.808  136.020 87.781  1.00 33.34 ?  579  MET B O    1 
ATOM   11547 C CB   . MET B 1 579  ? 88.270  137.304 86.028  1.00 27.62 ?  579  MET B CB   1 
ATOM   11548 C CG   . MET B 1 579  ? 88.685  138.420 86.971  1.00 30.71 ?  579  MET B CG   1 
ATOM   11549 S SD   . MET B 1 579  ? 90.159  139.293 86.413  1.00 40.31 ?  579  MET B SD   1 
ATOM   11550 C CE   . MET B 1 579  ? 90.661  140.106 87.927  1.00 29.93 ?  579  MET B CE   1 
ATOM   11551 N N    . GLU B 1 580  ? 88.849  134.927 87.999  1.00 23.13 ?  580  GLU B N    1 
ATOM   11552 C CA   . GLU B 1 580  ? 89.195  134.410 89.320  1.00 26.35 ?  580  GLU B CA   1 
ATOM   11553 C C    . GLU B 1 580  ? 90.357  133.428 89.242  1.00 24.07 ?  580  GLU B C    1 
ATOM   11554 O O    . GLU B 1 580  ? 91.248  133.438 90.104  1.00 23.05 ?  580  GLU B O    1 
ATOM   11555 C CB   . GLU B 1 580  ? 87.974  133.749 89.958  1.00 23.47 ?  580  GLU B CB   1 
ATOM   11556 C CG   . GLU B 1 580  ? 86.966  134.733 90.525  1.00 24.58 ?  580  GLU B CG   1 
ATOM   11557 C CD   . GLU B 1 580  ? 87.548  135.589 91.631  1.00 27.66 ?  580  GLU B CD   1 
ATOM   11558 O OE1  . GLU B 1 580  ? 88.256  135.039 92.500  1.00 21.31 ?  580  GLU B OE1  1 
ATOM   11559 O OE2  . GLU B 1 580  ? 87.300  136.813 91.628  1.00 32.57 ?  580  GLU B OE2  1 
ATOM   11560 N N    . GLU B 1 581  ? 90.365  132.572 88.215  1.00 21.67 ?  581  GLU B N    1 
ATOM   11561 C CA   . GLU B 1 581  ? 91.469  131.631 88.044  1.00 25.64 ?  581  GLU B CA   1 
ATOM   11562 C C    . GLU B 1 581  ? 92.788  132.360 87.810  1.00 27.91 ?  581  GLU B C    1 
ATOM   11563 O O    . GLU B 1 581  ? 93.816  132.001 88.396  1.00 27.90 ?  581  GLU B O    1 
ATOM   11564 C CB   . GLU B 1 581  ? 91.167  130.674 86.891  1.00 24.75 ?  581  GLU B CB   1 
ATOM   11565 C CG   . GLU B 1 581  ? 91.744  129.277 87.067  1.00 25.16 ?  581  GLU B CG   1 
ATOM   11566 C CD   . GLU B 1 581  ? 93.227  129.212 86.761  1.00 27.09 ?  581  GLU B CD   1 
ATOM   11567 O OE1  . GLU B 1 581  ? 93.696  130.005 85.917  1.00 24.54 ?  581  GLU B OE1  1 
ATOM   11568 O OE2  . GLU B 1 581  ? 93.925  128.369 87.363  1.00 26.55 ?  581  GLU B OE2  1 
ATOM   11569 N N    . ALA B 1 582  ? 92.773  133.400 86.970  1.00 25.24 ?  582  ALA B N    1 
ATOM   11570 C CA   . ALA B 1 582  ? 93.985  134.171 86.709  1.00 25.42 ?  582  ALA B CA   1 
ATOM   11571 C C    . ALA B 1 582  ? 94.451  134.917 87.953  1.00 22.52 ?  582  ALA B C    1 
ATOM   11572 O O    . ALA B 1 582  ? 95.657  135.016 88.205  1.00 24.65 ?  582  ALA B O    1 
ATOM   11573 C CB   . ALA B 1 582  ? 93.749  135.143 85.554  1.00 19.79 ?  582  ALA B CB   1 
ATOM   11574 N N    . ARG B 1 583  ? 93.512  135.456 88.738  1.00 16.07 ?  583  ARG B N    1 
ATOM   11575 C CA   . ARG B 1 583  ? 93.883  136.152 89.967  1.00 21.77 ?  583  ARG B CA   1 
ATOM   11576 C C    . ARG B 1 583  ? 94.533  135.204 90.971  1.00 23.37 ?  583  ARG B C    1 
ATOM   11577 O O    . ARG B 1 583  ? 95.563  135.535 91.577  1.00 28.19 ?  583  ARG B O    1 
ATOM   11578 C CB   . ARG B 1 583  ? 92.650  136.819 90.575  1.00 22.01 ?  583  ARG B CB   1 
ATOM   11579 C CG   . ARG B 1 583  ? 92.878  137.424 91.945  1.00 22.18 ?  583  ARG B CG   1 
ATOM   11580 C CD   . ARG B 1 583  ? 91.594  137.434 92.753  1.00 21.07 ?  583  ARG B CD   1 
ATOM   11581 N NE   . ARG B 1 583  ? 91.850  137.554 94.182  1.00 25.14 ?  583  ARG B NE   1 
ATOM   11582 C CZ   . ARG B 1 583  ? 91.022  137.132 95.127  1.00 24.76 ?  583  ARG B CZ   1 
ATOM   11583 N NH1  . ARG B 1 583  ? 89.874  136.546 94.829  1.00 23.52 ?  583  ARG B NH1  1 
ATOM   11584 N NH2  . ARG B 1 583  ? 91.354  137.301 96.403  1.00 24.63 ?  583  ARG B NH2  1 
ATOM   11585 N N    . LEU B 1 584  ? 93.952  134.013 91.149  1.00 19.10 ?  584  LEU B N    1 
ATOM   11586 C CA   . LEU B 1 584  ? 94.545  133.036 92.058  1.00 18.24 ?  584  LEU B CA   1 
ATOM   11587 C C    . LEU B 1 584  ? 95.903  132.562 91.552  1.00 18.82 ?  584  LEU B C    1 
ATOM   11588 O O    . LEU B 1 584  ? 96.830  132.355 92.347  1.00 22.44 ?  584  LEU B O    1 
ATOM   11589 C CB   . LEU B 1 584  ? 93.595  131.854 92.252  1.00 22.33 ?  584  LEU B CB   1 
ATOM   11590 C CG   . LEU B 1 584  ? 92.287  132.141 92.995  1.00 22.29 ?  584  LEU B CG   1 
ATOM   11591 C CD1  . LEU B 1 584  ? 91.590  130.845 93.380  1.00 18.73 ?  584  LEU B CD1  1 
ATOM   11592 C CD2  . LEU B 1 584  ? 92.535  133.005 94.224  1.00 20.52 ?  584  LEU B CD2  1 
ATOM   11593 N N    . ARG B 1 585  ? 96.043  132.400 90.232  1.00 18.04 ?  585  ARG B N    1 
ATOM   11594 C CA   . ARG B 1 585  ? 97.327  132.008 89.660  1.00 21.73 ?  585  ARG B CA   1 
ATOM   11595 C C    . ARG B 1 585  ? 98.390  133.076 89.893  1.00 20.97 ?  585  ARG B C    1 
ATOM   11596 O O    . ARG B 1 585  ? 99.539  132.755 90.223  1.00 21.43 ?  585  ARG B O    1 
ATOM   11597 C CB   . ARG B 1 585  ? 97.164  131.726 88.167  1.00 20.14 ?  585  ARG B CB   1 
ATOM   11598 C CG   . ARG B 1 585  ? 98.269  130.875 87.565  1.00 20.05 ?  585  ARG B CG   1 
ATOM   11599 C CD   . ARG B 1 585  ? 97.850  130.295 86.223  1.00 22.04 ?  585  ARG B CD   1 
ATOM   11600 N NE   . ARG B 1 585  ? 96.761  129.335 86.358  1.00 23.77 ?  585  ARG B NE   1 
ATOM   11601 C CZ   . ARG B 1 585  ? 96.841  128.059 86.005  1.00 24.25 ?  585  ARG B CZ   1 
ATOM   11602 N NH1  . ARG B 1 585  ? 97.947  127.553 85.486  1.00 21.01 ?  585  ARG B NH1  1 
ATOM   11603 N NH2  . ARG B 1 585  ? 95.784  127.271 86.179  1.00 20.64 ?  585  ARG B NH2  1 
ATOM   11604 N N    . MET B 1 586  ? 98.025  134.353 89.731  1.00 16.33 ?  586  MET B N    1 
ATOM   11605 C CA   . MET B 1 586  ? 98.975  135.432 89.990  1.00 16.57 ?  586  MET B CA   1 
ATOM   11606 C C    . MET B 1 586  ? 99.383  135.478 91.455  1.00 17.55 ?  586  MET B C    1 
ATOM   11607 O O    . MET B 1 586  ? 100.561 135.687 91.767  1.00 24.15 ?  586  MET B O    1 
ATOM   11608 C CB   . MET B 1 586  ? 98.396  136.782 89.574  1.00 15.31 ?  586  MET B CB   1 
ATOM   11609 C CG   . MET B 1 586  ? 98.661  137.168 88.133  1.00 17.50 ?  586  MET B CG   1 
ATOM   11610 S SD   . MET B 1 586  ? 98.084  138.839 87.781  1.00 17.23 ?  586  MET B SD   1 
ATOM   11611 C CE   . MET B 1 586  ? 98.501  139.675 89.312  1.00 19.05 ?  586  MET B CE   1 
ATOM   11612 N N    . LEU B 1 587  ? 98.424  135.306 92.370  1.00 13.56 ?  587  LEU B N    1 
ATOM   11613 C CA   . LEU B 1 587  ? 98.767  135.317 93.791  1.00 12.24 ?  587  LEU B CA   1 
ATOM   11614 C C    . LEU B 1 587  ? 99.689  134.155 94.147  1.00 10.83 ?  587  LEU B C    1 
ATOM   11615 O O    . LEU B 1 587  ? 100.658 134.326 94.903  1.00 21.31 ?  587  LEU B O    1 
ATOM   11616 C CB   . LEU B 1 587  ? 97.498  135.284 94.642  1.00 12.33 ?  587  LEU B CB   1 
ATOM   11617 C CG   . LEU B 1 587  ? 96.846  136.648 94.879  1.00 14.51 ?  587  LEU B CG   1 
ATOM   11618 C CD1  . LEU B 1 587  ? 95.330  136.530 94.909  1.00 15.75 ?  587  LEU B CD1  1 
ATOM   11619 C CD2  . LEU B 1 587  ? 97.368  137.289 96.156  1.00 16.00 ?  587  LEU B CD2  1 
ATOM   11620 N N    . LYS B 1 588  ? 99.418  132.970 93.591  1.00 3.43  ?  588  LYS B N    1 
ATOM   11621 C CA   . LYS B 1 588  ? 100.282 131.818 93.833  1.00 8.27  ?  588  LYS B CA   1 
ATOM   11622 C C    . LYS B 1 588  ? 101.685 132.051 93.285  1.00 11.69 ?  588  LYS B C    1 
ATOM   11623 O O    . LYS B 1 588  ? 102.679 131.747 93.957  1.00 12.48 ?  588  LYS B O    1 
ATOM   11624 C CB   . LYS B 1 588  ? 99.664  130.567 93.209  1.00 12.86 ?  588  LYS B CB   1 
ATOM   11625 C CG   . LYS B 1 588  ? 100.462 129.295 93.435  1.00 13.89 ?  588  LYS B CG   1 
ATOM   11626 C CD   . LYS B 1 588  ? 100.534 128.945 94.910  1.00 17.10 ?  588  LYS B CD   1 
ATOM   11627 C CE   . LYS B 1 588  ? 99.274  128.227 95.363  1.00 18.01 ?  588  LYS B CE   1 
ATOM   11628 N NZ   . LYS B 1 588  ? 99.218  126.829 94.852  1.00 20.49 ?  588  LYS B NZ   1 
ATOM   11629 N N    . ALA B 1 589  ? 101.786 132.605 92.073  1.00 12.65 ?  589  ALA B N    1 
ATOM   11630 C CA   . ALA B 1 589  ? 103.094 132.867 91.478  1.00 9.80  ?  589  ALA B CA   1 
ATOM   11631 C C    . ALA B 1 589  ? 103.867 133.916 92.270  1.00 14.61 ?  589  ALA B C    1 
ATOM   11632 O O    . ALA B 1 589  ? 105.089 133.807 92.426  1.00 18.98 ?  589  ALA B O    1 
ATOM   11633 C CB   . ALA B 1 589  ? 102.929 133.300 90.023  1.00 8.48  ?  589  ALA B CB   1 
ATOM   11634 N N    . GLU B 1 590  ? 103.172 134.940 92.775  1.00 11.80 ?  590  GLU B N    1 
ATOM   11635 C CA   . GLU B 1 590  ? 103.821 135.941 93.616  1.00 1.74  ?  590  GLU B CA   1 
ATOM   11636 C C    . GLU B 1 590  ? 104.354 135.325 94.903  1.00 0.18  ?  590  GLU B C    1 
ATOM   11637 O O    . GLU B 1 590  ? 105.464 135.653 95.343  1.00 6.85  ?  590  GLU B O    1 
ATOM   11638 C CB   . GLU B 1 590  ? 102.844 137.074 93.927  1.00 3.83  ?  590  GLU B CB   1 
ATOM   11639 C CG   . GLU B 1 590  ? 102.708 138.098 92.815  1.00 9.29  ?  590  GLU B CG   1 
ATOM   11640 C CD   . GLU B 1 590  ? 101.518 139.010 93.005  1.00 11.05 ?  590  GLU B CD   1 
ATOM   11641 O OE1  . GLU B 1 590  ? 100.931 138.989 94.103  1.00 14.30 ?  590  GLU B OE1  1 
ATOM   11642 O OE2  . GLU B 1 590  ? 101.173 139.749 92.059  1.00 10.99 ?  590  GLU B OE2  1 
ATOM   11643 N N    . LYS B 1 591  ? 103.576 134.432 95.524  1.00 3.42  ?  591  LYS B N    1 
ATOM   11644 C CA   . LYS B 1 591  ? 104.049 133.759 96.732  1.00 1.49  ?  591  LYS B CA   1 
ATOM   11645 C C    . LYS B 1 591  ? 105.270 132.889 96.443  1.00 4.81  ?  591  LYS B C    1 
ATOM   11646 O O    . LYS B 1 591  ? 106.222 132.851 97.238  1.00 11.12 ?  591  LYS B O    1 
ATOM   11647 C CB   . LYS B 1 591  ? 102.922 132.927 97.340  1.00 6.65  ?  591  LYS B CB   1 
ATOM   11648 C CG   . LYS B 1 591  ? 103.139 132.548 98.795  1.00 12.76 ?  591  LYS B CG   1 
ATOM   11649 C CD   . LYS B 1 591  ? 102.401 131.267 99.147  1.00 12.61 ?  591  LYS B CD   1 
ATOM   11650 C CE   . LYS B 1 591  ? 101.667 131.404 100.470 1.00 11.71 ?  591  LYS B CE   1 
ATOM   11651 N NZ   . LYS B 1 591  ? 100.489 132.307 100.348 1.00 9.93  ?  591  LYS B NZ   1 
ATOM   11652 N N    . ILE B 1 592  ? 105.262 132.191 95.301  1.00 3.48  ?  592  ILE B N    1 
ATOM   11653 C CA   . ILE B 1 592  ? 106.416 131.385 94.901  1.00 4.91  ?  592  ILE B CA   1 
ATOM   11654 C C    . ILE B 1 592  ? 107.640 132.271 94.701  1.00 7.77  ?  592  ILE B C    1 
ATOM   11655 O O    . ILE B 1 592  ? 108.755 131.919 95.107  1.00 9.31  ?  592  ILE B O    1 
ATOM   11656 C CB   . ILE B 1 592  ? 106.099 130.573 93.628  1.00 6.87  ?  592  ILE B CB   1 
ATOM   11657 C CG1  . ILE B 1 592  ? 104.944 129.588 93.848  1.00 13.54 ?  592  ILE B CG1  1 
ATOM   11658 C CG2  . ILE B 1 592  ? 107.331 129.824 93.138  1.00 6.26  ?  592  ILE B CG2  1 
ATOM   11659 C CD1  . ILE B 1 592  ? 104.933 128.898 95.190  1.00 12.26 ?  592  ILE B CD1  1 
ATOM   11660 N N    . SER B 1 593  ? 107.448 133.436 94.075  1.00 7.42  ?  593  SER B N    1 
ATOM   11661 C CA   . SER B 1 593  ? 108.555 134.360 93.849  1.00 3.20  ?  593  SER B CA   1 
ATOM   11662 C C    . SER B 1 593  ? 109.129 134.881 95.161  1.00 2.61  ?  593  SER B C    1 
ATOM   11663 O O    . SER B 1 593  ? 110.352 134.978 95.313  1.00 6.69  ?  593  SER B O    1 
ATOM   11664 C CB   . SER B 1 593  ? 108.095 135.522 92.971  1.00 3.49  ?  593  SER B CB   1 
ATOM   11665 O OG   . SER B 1 593  ? 109.147 136.447 92.767  1.00 6.55  ?  593  SER B OG   1 
ATOM   11666 N N    . TYR B 1 594  ? 108.263 135.225 96.119  1.00 5.99  ?  594  TYR B N    1 
ATOM   11667 C CA   . TYR B 1 594  ? 108.749 135.703 97.413  1.00 1.97  ?  594  TYR B CA   1 
ATOM   11668 C C    . TYR B 1 594  ? 109.527 134.619 98.150  1.00 3.81  ?  594  TYR B C    1 
ATOM   11669 O O    . TYR B 1 594  ? 110.588 134.890 98.732  1.00 2.55  ?  594  TYR B O    1 
ATOM   11670 C CB   . TYR B 1 594  ? 107.587 136.205 98.274  1.00 0.00  ?  594  TYR B CB   1 
ATOM   11671 C CG   . TYR B 1 594  ? 106.752 137.296 97.641  1.00 0.00  ?  594  TYR B CG   1 
ATOM   11672 C CD1  . TYR B 1 594  ? 107.307 138.190 96.737  1.00 1.87  ?  594  TYR B CD1  1 
ATOM   11673 C CD2  . TYR B 1 594  ? 105.407 137.433 97.954  1.00 3.74  ?  594  TYR B CD2  1 
ATOM   11674 C CE1  . TYR B 1 594  ? 106.546 139.185 96.158  1.00 1.60  ?  594  TYR B CE1  1 
ATOM   11675 C CE2  . TYR B 1 594  ? 104.639 138.426 97.380  1.00 3.23  ?  594  TYR B CE2  1 
ATOM   11676 C CZ   . TYR B 1 594  ? 105.214 139.299 96.484  1.00 0.00  ?  594  TYR B CZ   1 
ATOM   11677 O OH   . TYR B 1 594  ? 104.454 140.290 95.909  1.00 0.00  ?  594  TYR B OH   1 
ATOM   11678 N N    . TRP B 1 595  ? 109.028 133.379 98.125  1.00 10.03 ?  595  TRP B N    1 
ATOM   11679 C CA   . TRP B 1 595  ? 109.756 132.295 98.780  1.00 7.73  ?  595  TRP B CA   1 
ATOM   11680 C C    . TRP B 1 595  ? 111.100 132.037 98.107  1.00 4.10  ?  595  TRP B C    1 
ATOM   11681 O O    . TRP B 1 595  ? 112.116 131.855 98.790  1.00 9.76  ?  595  TRP B O    1 
ATOM   11682 C CB   . TRP B 1 595  ? 108.907 131.026 98.808  1.00 8.70  ?  595  TRP B CB   1 
ATOM   11683 C CG   . TRP B 1 595  ? 108.020 130.958 100.008 1.00 11.41 ?  595  TRP B CG   1 
ATOM   11684 C CD1  . TRP B 1 595  ? 106.664 131.093 100.036 1.00 7.31  ?  595  TRP B CD1  1 
ATOM   11685 C CD2  . TRP B 1 595  ? 108.431 130.758 101.365 1.00 11.78 ?  595  TRP B CD2  1 
ATOM   11686 N NE1  . TRP B 1 595  ? 106.204 130.981 101.325 1.00 7.70  ?  595  TRP B NE1  1 
ATOM   11687 C CE2  . TRP B 1 595  ? 107.270 130.776 102.161 1.00 9.67  ?  595  TRP B CE2  1 
ATOM   11688 C CE3  . TRP B 1 595  ? 109.670 130.562 101.985 1.00 10.78 ?  595  TRP B CE3  1 
ATOM   11689 C CZ2  . TRP B 1 595  ? 107.309 130.605 103.543 1.00 8.70  ?  595  TRP B CZ2  1 
ATOM   11690 C CZ3  . TRP B 1 595  ? 109.707 130.392 103.356 1.00 8.96  ?  595  TRP B CZ3  1 
ATOM   11691 C CH2  . TRP B 1 595  ? 108.534 130.414 104.120 1.00 9.70  ?  595  TRP B CH2  1 
ATOM   11692 N N    . LYS B 1 596  ? 111.131 132.051 96.771  1.00 0.82  ?  596  LYS B N    1 
ATOM   11693 C CA   . LYS B 1 596  ? 112.385 131.852 96.050  1.00 3.17  ?  596  LYS B CA   1 
ATOM   11694 C C    . LYS B 1 596  ? 113.377 132.974 96.323  1.00 5.25  ?  596  LYS B C    1 
ATOM   11695 O O    . LYS B 1 596  ? 114.588 132.732 96.357  1.00 7.70  ?  596  LYS B O    1 
ATOM   11696 C CB   . LYS B 1 596  ? 112.116 131.744 94.551  1.00 6.77  ?  596  LYS B CB   1 
ATOM   11697 C CG   . LYS B 1 596  ? 112.852 130.608 93.865  1.00 7.89  ?  596  LYS B CG   1 
ATOM   11698 C CD   . LYS B 1 596  ? 112.513 130.546 92.385  1.00 6.66  ?  596  LYS B CD   1 
ATOM   11699 C CE   . LYS B 1 596  ? 111.012 130.539 92.151  1.00 6.22  ?  596  LYS B CE   1 
ATOM   11700 N NZ   . LYS B 1 596  ? 110.672 130.992 90.774  1.00 12.78 ?  596  LYS B NZ   1 
ATOM   11701 N N    . GLN B 1 597  ? 112.887 134.203 96.508  1.00 11.77 ?  597  GLN B N    1 
ATOM   11702 C CA   . GLN B 1 597  ? 113.767 135.291 96.922  1.00 3.09  ?  597  GLN B CA   1 
ATOM   11703 C C    . GLN B 1 597  ? 114.312 135.054 98.324  1.00 3.54  ?  597  GLN B C    1 
ATOM   11704 O O    . GLN B 1 597  ? 115.459 135.409 98.615  1.00 5.71  ?  597  GLN B O    1 
ATOM   11705 C CB   . GLN B 1 597  ? 113.032 136.629 96.854  1.00 2.83  ?  597  GLN B CB   1 
ATOM   11706 C CG   . GLN B 1 597  ? 112.839 137.171 95.449  1.00 5.39  ?  597  GLN B CG   1 
ATOM   11707 C CD   . GLN B 1 597  ? 112.274 138.576 95.441  1.00 0.00  ?  597  GLN B CD   1 
ATOM   11708 O OE1  . GLN B 1 597  ? 112.924 139.520 95.887  1.00 3.09  ?  597  GLN B OE1  1 
ATOM   11709 N NE2  . GLN B 1 597  ? 111.058 138.723 94.930  1.00 2.03  ?  597  GLN B NE2  1 
ATOM   11710 N N    . PHE B 1 598  ? 113.498 134.472 99.213  1.00 6.30  ?  598  PHE B N    1 
ATOM   11711 C CA   . PHE B 1 598  ? 113.984 134.177 100.561 1.00 2.95  ?  598  PHE B CA   1 
ATOM   11712 C C    . PHE B 1 598  ? 115.096 133.133 100.538 1.00 8.97  ?  598  PHE B C    1 
ATOM   11713 O O    . PHE B 1 598  ? 116.123 133.299 101.206 1.00 12.87 ?  598  PHE B O    1 
ATOM   11714 C CB   . PHE B 1 598  ? 112.849 133.693 101.461 1.00 5.14  ?  598  PHE B CB   1 
ATOM   11715 C CG   . PHE B 1 598  ? 113.305 133.301 102.847 1.00 10.13 ?  598  PHE B CG   1 
ATOM   11716 C CD1  . PHE B 1 598  ? 114.174 134.114 103.562 1.00 14.61 ?  598  PHE B CD1  1 
ATOM   11717 C CD2  . PHE B 1 598  ? 112.907 132.100 103.414 1.00 15.68 ?  598  PHE B CD2  1 
ATOM   11718 C CE1  . PHE B 1 598  ? 114.605 133.756 104.826 1.00 12.99 ?  598  PHE B CE1  1 
ATOM   11719 C CE2  . PHE B 1 598  ? 113.337 131.737 104.680 1.00 15.55 ?  598  PHE B CE2  1 
ATOM   11720 C CZ   . PHE B 1 598  ? 114.188 132.566 105.384 1.00 12.78 ?  598  PHE B CZ   1 
ATOM   11721 N N    . GLU B 1 599  ? 114.903 132.038 99.790  1.00 15.95 ?  599  GLU B N    1 
ATOM   11722 C CA   . GLU B 1 599  ? 115.890 130.956 99.805  1.00 10.09 ?  599  GLU B CA   1 
ATOM   11723 C C    . GLU B 1 599  ? 117.244 131.374 99.242  1.00 10.90 ?  599  GLU B C    1 
ATOM   11724 O O    . GLU B 1 599  ? 118.259 130.766 99.597  1.00 19.01 ?  599  GLU B O    1 
ATOM   11725 C CB   . GLU B 1 599  ? 115.388 129.729 99.037  1.00 9.80  ?  599  GLU B CB   1 
ATOM   11726 C CG   . GLU B 1 599  ? 113.931 129.378 99.246  1.00 15.27 ?  599  GLU B CG   1 
ATOM   11727 C CD   . GLU B 1 599  ? 113.664 128.736 100.593 1.00 18.30 ?  599  GLU B CD   1 
ATOM   11728 O OE1  . GLU B 1 599  ? 112.496 128.744 101.035 1.00 11.42 ?  599  GLU B OE1  1 
ATOM   11729 O OE2  . GLU B 1 599  ? 114.619 128.214 101.204 1.00 22.85 ?  599  GLU B OE2  1 
ATOM   11730 N N    . HIS B 1 600  ? 117.287 132.387 98.383  1.00 8.71  ?  600  HIS B N    1 
ATOM   11731 C CA   . HIS B 1 600  ? 118.543 132.883 97.840  1.00 10.35 ?  600  HIS B CA   1 
ATOM   11732 C C    . HIS B 1 600  ? 119.214 133.913 98.739  1.00 15.67 ?  600  HIS B C    1 
ATOM   11733 O O    . HIS B 1 600  ? 120.300 134.394 98.401  1.00 18.27 ?  600  HIS B O    1 
ATOM   11734 C CB   . HIS B 1 600  ? 118.317 133.488 96.452  1.00 14.57 ?  600  HIS B CB   1 
ATOM   11735 C CG   . HIS B 1 600  ? 119.368 133.116 95.454  1.00 19.25 ?  600  HIS B CG   1 
ATOM   11736 N ND1  . HIS B 1 600  ? 119.562 131.822 95.022  1.00 19.77 ?  600  HIS B ND1  1 
ATOM   11737 C CD2  . HIS B 1 600  ? 120.284 133.871 94.802  1.00 17.95 ?  600  HIS B CD2  1 
ATOM   11738 C CE1  . HIS B 1 600  ? 120.552 131.795 94.148  1.00 18.81 ?  600  HIS B CE1  1 
ATOM   11739 N NE2  . HIS B 1 600  ? 121.007 133.026 93.996  1.00 18.47 ?  600  HIS B NE2  1 
ATOM   11740 N N    . GLY B 1 601  ? 118.601 134.262 99.868  1.00 17.05 ?  601  GLY B N    1 
ATOM   11741 C CA   . GLY B 1 601  ? 119.160 135.258 100.757 1.00 12.35 ?  601  GLY B CA   1 
ATOM   11742 C C    . GLY B 1 601  ? 118.962 136.692 100.325 1.00 13.25 ?  601  GLY B C    1 
ATOM   11743 O O    . GLY B 1 601  ? 119.632 137.580 100.862 1.00 21.09 ?  601  GLY B O    1 
ATOM   11744 N N    . MET B 1 602  ? 118.067 136.949 99.374  1.00 10.71 ?  602  MET B N    1 
ATOM   11745 C CA   . MET B 1 602  ? 117.775 138.304 98.929  1.00 10.92 ?  602  MET B CA   1 
ATOM   11746 C C    . MET B 1 602  ? 116.680 138.974 99.747  1.00 12.49 ?  602  MET B C    1 
ATOM   11747 O O    . MET B 1 602  ? 116.413 140.163 99.543  1.00 13.45 ?  602  MET B O    1 
ATOM   11748 C CB   . MET B 1 602  ? 117.375 138.295 97.450  1.00 12.82 ?  602  MET B CB   1 
ATOM   11749 C CG   . MET B 1 602  ? 118.479 138.737 96.504  1.00 15.26 ?  602  MET B CG   1 
ATOM   11750 S SD   . MET B 1 602  ? 117.853 139.220 94.884  1.00 24.59 ?  602  MET B SD   1 
ATOM   11751 C CE   . MET B 1 602  ? 116.804 137.820 94.498  1.00 16.93 ?  602  MET B CE   1 
ATOM   11752 N N    . LEU B 1 603  ? 116.047 138.246 100.664 1.00 11.96 ?  603  LEU B N    1 
ATOM   11753 C CA   . LEU B 1 603  ? 114.994 138.782 101.510 1.00 10.21 ?  603  LEU B CA   1 
ATOM   11754 C C    . LEU B 1 603  ? 115.237 138.360 102.950 1.00 15.06 ?  603  LEU B C    1 
ATOM   11755 O O    . LEU B 1 603  ? 115.725 137.259 103.218 1.00 14.31 ?  603  LEU B O    1 
ATOM   11756 C CB   . LEU B 1 603  ? 113.605 138.300 101.066 1.00 3.36  ?  603  LEU B CB   1 
ATOM   11757 C CG   . LEU B 1 603  ? 112.748 139.237 100.215 1.00 0.00  ?  603  LEU B CG   1 
ATOM   11758 C CD1  . LEU B 1 603  ? 111.361 138.648 100.008 1.00 0.56  ?  603  LEU B CD1  1 
ATOM   11759 C CD2  . LEU B 1 603  ? 112.659 140.607 100.855 1.00 6.82  ?  603  LEU B CD2  1 
ATOM   11760 N N    . ALA B 1 604  ? 114.893 139.249 103.876 1.00 14.22 ?  604  ALA B N    1 
ATOM   11761 C CA   . ALA B 1 604  ? 114.917 138.904 105.285 1.00 9.08  ?  604  ALA B CA   1 
ATOM   11762 C C    . ALA B 1 604  ? 113.618 138.203 105.672 1.00 13.65 ?  604  ALA B C    1 
ATOM   11763 O O    . ALA B 1 604  ? 112.628 138.226 104.936 1.00 14.36 ?  604  ALA B O    1 
ATOM   11764 C CB   . ALA B 1 604  ? 115.132 140.150 106.141 1.00 12.83 ?  604  ALA B CB   1 
ATOM   11765 N N    . ARG B 1 605  ? 113.636 137.560 106.842 1.00 16.85 ?  605  ARG B N    1 
ATOM   11766 C CA   . ARG B 1 605  ? 112.487 136.764 107.266 1.00 15.94 ?  605  ARG B CA   1 
ATOM   11767 C C    . ARG B 1 605  ? 111.264 137.633 107.537 1.00 18.57 ?  605  ARG B C    1 
ATOM   11768 O O    . ARG B 1 605  ? 110.142 137.257 107.179 1.00 22.86 ?  605  ARG B O    1 
ATOM   11769 C CB   . ARG B 1 605  ? 112.846 135.936 108.499 1.00 20.06 ?  605  ARG B CB   1 
ATOM   11770 C CG   . ARG B 1 605  ? 111.772 134.936 108.899 1.00 18.84 ?  605  ARG B CG   1 
ATOM   11771 C CD   . ARG B 1 605  ? 112.257 134.005 109.996 1.00 21.79 ?  605  ARG B CD   1 
ATOM   11772 N NE   . ARG B 1 605  ? 113.508 133.350 109.636 1.00 22.02 ?  605  ARG B NE   1 
ATOM   11773 C CZ   . ARG B 1 605  ? 113.591 132.146 109.086 1.00 22.61 ?  605  ARG B CZ   1 
ATOM   11774 N NH1  . ARG B 1 605  ? 112.509 131.432 108.820 1.00 19.93 ?  605  ARG B NH1  1 
ATOM   11775 N NH2  . ARG B 1 605  ? 114.788 131.645 108.797 1.00 21.88 ?  605  ARG B NH2  1 
ATOM   11776 N N    . GLU B 1 606  ? 111.455 138.796 108.167 1.00 15.08 ?  606  GLU B N    1 
ATOM   11777 C CA   . GLU B 1 606  ? 110.321 139.660 108.487 1.00 15.11 ?  606  GLU B CA   1 
ATOM   11778 C C    . GLU B 1 606  ? 109.668 140.223 107.228 1.00 15.90 ?  606  GLU B C    1 
ATOM   11779 O O    . GLU B 1 606  ? 108.436 140.287 107.140 1.00 16.17 ?  606  GLU B O    1 
ATOM   11780 C CB   . GLU B 1 606  ? 110.759 140.792 109.419 1.00 16.01 ?  606  GLU B CB   1 
ATOM   11781 C CG   . GLU B 1 606  ? 111.773 140.392 110.486 1.00 23.24 ?  606  GLU B CG   1 
ATOM   11782 C CD   . GLU B 1 606  ? 113.213 140.555 110.037 1.00 22.18 ?  606  GLU B CD   1 
ATOM   11783 O OE1  . GLU B 1 606  ? 113.438 140.815 108.838 1.00 16.95 ?  606  GLU B OE1  1 
ATOM   11784 O OE2  . GLU B 1 606  ? 114.120 140.422 110.885 1.00 21.52 ?  606  GLU B OE2  1 
ATOM   11785 N N    . ALA B 1 607  ? 110.475 140.632 106.245 1.00 13.48 ?  607  ALA B N    1 
ATOM   11786 C CA   . ALA B 1 607  ? 109.922 141.150 104.996 1.00 9.75  ?  607  ALA B CA   1 
ATOM   11787 C C    . ALA B 1 607  ? 109.165 140.072 104.231 1.00 14.57 ?  607  ALA B C    1 
ATOM   11788 O O    . ALA B 1 607  ? 108.085 140.333 103.685 1.00 15.45 ?  607  ALA B O    1 
ATOM   11789 C CB   . ALA B 1 607  ? 111.037 141.732 104.131 1.00 7.37  ?  607  ALA B CB   1 
ATOM   11790 N N    . LEU B 1 608  ? 109.719 138.857 104.179 1.00 16.49 ?  608  LEU B N    1 
ATOM   11791 C CA   . LEU B 1 608  ? 109.030 137.749 103.525 1.00 13.65 ?  608  LEU B CA   1 
ATOM   11792 C C    . LEU B 1 608  ? 107.722 137.429 104.231 1.00 11.43 ?  608  LEU B C    1 
ATOM   11793 O O    . LEU B 1 608  ? 106.703 137.173 103.579 1.00 10.45 ?  608  LEU B O    1 
ATOM   11794 C CB   . LEU B 1 608  ? 109.931 136.514 103.495 1.00 9.84  ?  608  LEU B CB   1 
ATOM   11795 C CG   . LEU B 1 608  ? 109.213 135.168 103.353 1.00 10.61 ?  608  LEU B CG   1 
ATOM   11796 C CD1  . LEU B 1 608  ? 108.857 134.894 101.898 1.00 12.48 ?  608  LEU B CD1  1 
ATOM   11797 C CD2  . LEU B 1 608  ? 110.018 134.031 103.949 1.00 9.39  ?  608  LEU B CD2  1 
ATOM   11798 N N    . ARG B 1 609  ? 107.734 137.441 105.568 1.00 14.25 ?  609  ARG B N    1 
ATOM   11799 C CA   . ARG B 1 609  ? 106.519 137.186 106.334 1.00 14.88 ?  609  ARG B CA   1 
ATOM   11800 C C    . ARG B 1 609  ? 105.463 138.248 106.063 1.00 13.84 ?  609  ARG B C    1 
ATOM   11801 O O    . ARG B 1 609  ? 104.282 137.925 105.900 1.00 16.69 ?  609  ARG B O    1 
ATOM   11802 C CB   . ARG B 1 609  ? 106.845 137.123 107.826 1.00 16.06 ?  609  ARG B CB   1 
ATOM   11803 C CG   . ARG B 1 609  ? 107.403 135.787 108.287 1.00 15.93 ?  609  ARG B CG   1 
ATOM   11804 C CD   . ARG B 1 609  ? 107.317 135.642 109.798 1.00 15.96 ?  609  ARG B CD   1 
ATOM   11805 N NE   . ARG B 1 609  ? 107.715 136.863 110.489 1.00 22.33 ?  609  ARG B NE   1 
ATOM   11806 C CZ   . ARG B 1 609  ? 108.540 136.903 111.527 1.00 26.23 ?  609  ARG B CZ   1 
ATOM   11807 N NH1  . ARG B 1 609  ? 109.075 135.802 112.028 1.00 23.03 ?  609  ARG B NH1  1 
ATOM   11808 N NH2  . ARG B 1 609  ? 108.836 138.078 112.076 1.00 24.48 ?  609  ARG B NH2  1 
ATOM   11809 N N    . LEU B 1 610  ? 105.872 139.518 105.992 1.00 11.21 ?  610  LEU B N    1 
ATOM   11810 C CA   . LEU B 1 610  ? 104.933 140.589 105.666 1.00 12.92 ?  610  LEU B CA   1 
ATOM   11811 C C    . LEU B 1 610  ? 104.346 140.407 104.271 1.00 15.29 ?  610  LEU B C    1 
ATOM   11812 O O    . LEU B 1 610  ? 103.134 140.568 104.070 1.00 15.20 ?  610  LEU B O    1 
ATOM   11813 C CB   . LEU B 1 610  ? 105.630 141.946 105.772 1.00 12.04 ?  610  LEU B CB   1 
ATOM   11814 C CG   . LEU B 1 610  ? 105.354 142.825 106.993 1.00 14.57 ?  610  LEU B CG   1 
ATOM   11815 C CD1  . LEU B 1 610  ? 106.048 142.274 108.224 1.00 16.10 ?  610  LEU B CD1  1 
ATOM   11816 C CD2  . LEU B 1 610  ? 105.795 144.254 106.722 1.00 14.07 ?  610  LEU B CD2  1 
ATOM   11817 N N    . LEU B 1 611  ? 105.191 140.056 103.298 1.00 13.51 ?  611  LEU B N    1 
ATOM   11818 C CA   . LEU B 1 611  ? 104.717 139.909 101.925 1.00 10.16 ?  611  LEU B CA   1 
ATOM   11819 C C    . LEU B 1 611  ? 103.758 138.731 101.787 1.00 12.85 ?  611  LEU B C    1 
ATOM   11820 O O    . LEU B 1 611  ? 102.712 138.851 101.138 1.00 17.09 ?  611  LEU B O    1 
ATOM   11821 C CB   . LEU B 1 611  ? 105.905 139.756 100.976 1.00 8.57  ?  611  LEU B CB   1 
ATOM   11822 C CG   . LEU B 1 611  ? 106.717 141.026 100.711 1.00 1.06  ?  611  LEU B CG   1 
ATOM   11823 C CD1  . LEU B 1 611  ? 108.150 140.682 100.349 1.00 1.60  ?  611  LEU B CD1  1 
ATOM   11824 C CD2  . LEU B 1 611  ? 106.070 141.863 99.621  1.00 2.27  ?  611  LEU B CD2  1 
ATOM   11825 N N    . VAL B 1 612  ? 104.078 137.592 102.409 1.00 13.66 ?  612  VAL B N    1 
ATOM   11826 C CA   . VAL B 1 612  ? 103.190 136.439 102.294 1.00 13.01 ?  612  VAL B CA   1 
ATOM   11827 C C    . VAL B 1 612  ? 101.931 136.636 103.131 1.00 14.49 ?  612  VAL B C    1 
ATOM   11828 O O    . VAL B 1 612  ? 100.872 136.097 102.794 1.00 17.43 ?  612  VAL B O    1 
ATOM   11829 C CB   . VAL B 1 612  ? 103.921 135.130 102.657 1.00 10.34 ?  612  VAL B CB   1 
ATOM   11830 C CG1  . VAL B 1 612  ? 105.142 134.943 101.771 1.00 13.06 ?  612  VAL B CG1  1 
ATOM   11831 C CG2  . VAL B 1 612  ? 104.299 135.092 104.130 1.00 15.52 ?  612  VAL B CG2  1 
ATOM   11832 N N    . GLN B 1 613  ? 102.007 137.418 104.213 1.00 13.66 ?  613  GLN B N    1 
ATOM   11833 C CA   . GLN B 1 613  ? 100.804 137.761 104.961 1.00 11.17 ?  613  GLN B CA   1 
ATOM   11834 C C    . GLN B 1 613  ? 99.867  138.619 104.122 1.00 14.73 ?  613  GLN B C    1 
ATOM   11835 O O    . GLN B 1 613  ? 98.653  138.387 104.107 1.00 16.90 ?  613  GLN B O    1 
ATOM   11836 C CB   . GLN B 1 613  ? 101.188 138.472 106.260 1.00 12.62 ?  613  GLN B CB   1 
ATOM   11837 C CG   . GLN B 1 613  ? 100.136 139.423 106.807 1.00 15.47 ?  613  GLN B CG   1 
ATOM   11838 C CD   . GLN B 1 613  ? 100.718 140.442 107.770 1.00 18.66 ?  613  GLN B CD   1 
ATOM   11839 O OE1  . GLN B 1 613  ? 101.779 140.225 108.356 1.00 16.83 ?  613  GLN B OE1  1 
ATOM   11840 N NE2  . GLN B 1 613  ? 100.022 141.560 107.940 1.00 17.95 ?  613  GLN B NE2  1 
ATOM   11841 N N    . HIS B 1 614  ? 100.417 139.599 103.399 1.00 16.79 ?  614  HIS B N    1 
ATOM   11842 C CA   . HIS B 1 614  ? 99.593  140.394 102.491 1.00 20.17 ?  614  HIS B CA   1 
ATOM   11843 C C    . HIS B 1 614  ? 99.017  139.535 101.371 1.00 15.88 ?  614  HIS B C    1 
ATOM   11844 O O    . HIS B 1 614  ? 97.859  139.716 100.973 1.00 17.98 ?  614  HIS B O    1 
ATOM   11845 C CB   . HIS B 1 614  ? 100.407 141.551 101.915 1.00 18.85 ?  614  HIS B CB   1 
ATOM   11846 C CG   . HIS B 1 614  ? 100.816 142.566 102.934 1.00 18.88 ?  614  HIS B CG   1 
ATOM   11847 N ND1  . HIS B 1 614  ? 102.105 142.662 103.413 1.00 17.77 ?  614  HIS B ND1  1 
ATOM   11848 C CD2  . HIS B 1 614  ? 100.107 143.531 103.565 1.00 17.68 ?  614  HIS B CD2  1 
ATOM   11849 C CE1  . HIS B 1 614  ? 102.171 143.642 104.297 1.00 19.13 ?  614  HIS B CE1  1 
ATOM   11850 N NE2  . HIS B 1 614  ? 100.973 144.186 104.407 1.00 19.12 ?  614  HIS B NE2  1 
ATOM   11851 N N    . ALA B 1 615  ? 99.811  138.591 100.854 1.00 9.83  ?  615  ALA B N    1 
ATOM   11852 C CA   . ALA B 1 615  ? 99.321  137.707 99.798  1.00 17.19 ?  615  ALA B CA   1 
ATOM   11853 C C    . ALA B 1 615  ? 98.176  136.828 100.289 1.00 24.77 ?  615  ALA B C    1 
ATOM   11854 O O    . ALA B 1 615  ? 97.161  136.677 99.599  1.00 21.42 ?  615  ALA B O    1 
ATOM   11855 C CB   . ALA B 1 615  ? 100.466 136.848 99.262  1.00 14.23 ?  615  ALA B CB   1 
ATOM   11856 N N    . GLU B 1 616  ? 98.312  136.254 101.488 1.00 21.22 ?  616  GLU B N    1 
ATOM   11857 C CA   . GLU B 1 616  ? 97.245  135.429 102.046 1.00 14.20 ?  616  GLU B CA   1 
ATOM   11858 C C    . GLU B 1 616  ? 96.009  136.254 102.382 1.00 12.50 ?  616  GLU B C    1 
ATOM   11859 O O    . GLU B 1 616  ? 94.883  135.764 102.234 1.00 15.17 ?  616  GLU B O    1 
ATOM   11860 C CB   . GLU B 1 616  ? 97.746  134.691 103.287 1.00 14.09 ?  616  GLU B CB   1 
ATOM   11861 C CG   . GLU B 1 616  ? 98.681  133.533 102.982 1.00 14.09 ?  616  GLU B CG   1 
ATOM   11862 C CD   . GLU B 1 616  ? 99.569  133.176 104.157 1.00 15.88 ?  616  GLU B CD   1 
ATOM   11863 O OE1  . GLU B 1 616  ? 99.458  133.836 105.211 1.00 15.97 ?  616  GLU B OE1  1 
ATOM   11864 O OE2  . GLU B 1 616  ? 100.379 132.234 104.028 1.00 17.37 ?  616  GLU B OE2  1 
ATOM   11865 N N    . VAL B 1 617  ? 96.196  137.493 102.844 1.00 13.16 ?  617  VAL B N    1 
ATOM   11866 C CA   . VAL B 1 617  ? 95.063  138.373 103.115 1.00 19.16 ?  617  VAL B CA   1 
ATOM   11867 C C    . VAL B 1 617  ? 94.314  138.693 101.826 1.00 20.82 ?  617  VAL B C    1 
ATOM   11868 O O    . VAL B 1 617  ? 93.078  138.693 101.793 1.00 23.05 ?  617  VAL B O    1 
ATOM   11869 C CB   . VAL B 1 617  ? 95.549  139.646 103.837 1.00 21.70 ?  617  VAL B CB   1 
ATOM   11870 C CG1  . VAL B 1 617  ? 94.588  140.809 103.625 1.00 17.80 ?  617  VAL B CG1  1 
ATOM   11871 C CG2  . VAL B 1 617  ? 95.738  139.370 105.321 1.00 19.97 ?  617  VAL B CG2  1 
ATOM   11872 N N    . ALA B 1 618  ? 95.044  138.959 100.742 1.00 24.34 ?  618  ALA B N    1 
ATOM   11873 C CA   . ALA B 1 618  ? 94.399  139.251 99.469  1.00 23.90 ?  618  ALA B CA   1 
ATOM   11874 C C    . ALA B 1 618  ? 93.818  138.013 98.796  1.00 18.78 ?  618  ALA B C    1 
ATOM   11875 O O    . ALA B 1 618  ? 92.935  138.151 97.942  1.00 21.11 ?  618  ALA B O    1 
ATOM   11876 C CB   . ALA B 1 618  ? 95.389  139.931 98.522  1.00 20.93 ?  618  ALA B CB   1 
ATOM   11877 N N    . ALA B 1 619  ? 94.296  136.816 99.149  1.00 13.80 ?  619  ALA B N    1 
ATOM   11878 C CA   . ALA B 1 619  ? 93.865  135.608 98.450  1.00 22.36 ?  619  ALA B CA   1 
ATOM   11879 C C    . ALA B 1 619  ? 92.414  135.252 98.761  1.00 22.52 ?  619  ALA B C    1 
ATOM   11880 O O    . ALA B 1 619  ? 91.623  134.990 97.847  1.00 17.88 ?  619  ALA B O    1 
ATOM   11881 C CB   . ALA B 1 619  ? 94.789  134.443 98.806  1.00 21.25 ?  619  ALA B CB   1 
ATOM   11882 N N    . ASP B 1 620  ? 92.040  135.235 100.042 1.00 23.15 ?  620  ASP B N    1 
ATOM   11883 C CA   . ASP B 1 620  ? 90.714  134.754 100.415 1.00 23.59 ?  620  ASP B CA   1 
ATOM   11884 C C    . ASP B 1 620  ? 89.605  135.762 100.133 1.00 22.80 ?  620  ASP B C    1 
ATOM   11885 O O    . ASP B 1 620  ? 88.427  135.397 100.216 1.00 24.29 ?  620  ASP B O    1 
ATOM   11886 C CB   . ASP B 1 620  ? 90.688  134.343 101.895 1.00 21.73 ?  620  ASP B CB   1 
ATOM   11887 C CG   . ASP B 1 620  ? 90.935  135.505 102.845 1.00 22.79 ?  620  ASP B CG   1 
ATOM   11888 O OD1  . ASP B 1 620  ? 91.329  136.598 102.393 1.00 23.68 ?  620  ASP B OD1  1 
ATOM   11889 O OD2  . ASP B 1 620  ? 90.728  135.320 104.063 1.00 22.03 ?  620  ASP B OD2  1 
ATOM   11890 N N    . GLU B 1 621  ? 89.948  137.005 99.808  1.00 24.65 ?  621  GLU B N    1 
ATOM   11891 C CA   . GLU B 1 621  ? 88.949  137.997 99.445  1.00 27.15 ?  621  GLU B CA   1 
ATOM   11892 C C    . GLU B 1 621  ? 88.342  137.643 98.088  1.00 26.73 ?  621  GLU B C    1 
ATOM   11893 O O    . GLU B 1 621  ? 88.897  136.852 97.320  1.00 26.38 ?  621  GLU B O    1 
ATOM   11894 C CB   . GLU B 1 621  ? 89.584  139.392 99.422  1.00 26.27 ?  621  GLU B CB   1 
ATOM   11895 C CG   . GLU B 1 621  ? 88.699  140.537 99.919  1.00 25.68 ?  621  GLU B CG   1 
ATOM   11896 C CD   . GLU B 1 621  ? 87.696  141.020 98.892  1.00 29.06 ?  621  GLU B CD   1 
ATOM   11897 O OE1  . GLU B 1 621  ? 88.059  141.104 97.700  1.00 26.81 ?  621  GLU B OE1  1 
ATOM   11898 O OE2  . GLU B 1 621  ? 86.547  141.320 99.276  1.00 28.77 ?  621  GLU B OE2  1 
ATOM   11899 N N    . LYS B 1 622  ? 87.167  138.214 97.812  1.00 26.60 ?  622  LYS B N    1 
ATOM   11900 C CA   . LYS B 1 622  ? 86.480  137.937 96.552  1.00 30.00 ?  622  LYS B CA   1 
ATOM   11901 C C    . LYS B 1 622  ? 87.295  138.420 95.357  1.00 29.95 ?  622  LYS B C    1 
ATOM   11902 O O    . LYS B 1 622  ? 87.543  137.659 94.414  1.00 26.24 ?  622  LYS B O    1 
ATOM   11903 C CB   . LYS B 1 622  ? 85.094  138.584 96.558  1.00 27.15 ?  622  LYS B CB   1 
ATOM   11904 C CG   . LYS B 1 622  ? 84.365  138.514 95.222  1.00 25.74 ?  622  LYS B CG   1 
ATOM   11905 C CD   . LYS B 1 622  ? 84.124  137.077 94.782  1.00 27.22 ?  622  LYS B CD   1 
ATOM   11906 C CE   . LYS B 1 622  ? 83.187  136.349 95.731  1.00 30.33 ?  622  LYS B CE   1 
ATOM   11907 N NZ   . LYS B 1 622  ? 83.027  134.918 95.352  1.00 29.58 ?  622  LYS B NZ   1 
ATOM   11908 N N    . ASP B 1 623  ? 87.722  139.682 95.377  1.00 25.99 ?  623  ASP B N    1 
ATOM   11909 C CA   . ASP B 1 623  ? 88.541  140.225 94.294  1.00 26.37 ?  623  ASP B CA   1 
ATOM   11910 C C    . ASP B 1 623  ? 89.397  141.345 94.878  1.00 27.09 ?  623  ASP B C    1 
ATOM   11911 O O    . ASP B 1 623  ? 88.922  142.474 95.035  1.00 26.48 ?  623  ASP B O    1 
ATOM   11912 C CB   . ASP B 1 623  ? 87.675  140.722 93.144  1.00 25.76 ?  623  ASP B CB   1 
ATOM   11913 C CG   . ASP B 1 623  ? 88.452  140.869 91.850  1.00 27.11 ?  623  ASP B CG   1 
ATOM   11914 O OD1  . ASP B 1 623  ? 89.624  140.441 91.807  1.00 28.10 ?  623  ASP B OD1  1 
ATOM   11915 O OD2  . ASP B 1 623  ? 87.888  141.410 90.876  1.00 25.48 ?  623  ASP B OD2  1 
ATOM   11916 N N    . GLN B 1 624  ? 90.651  141.027 95.192  1.00 27.98 ?  624  GLN B N    1 
ATOM   11917 C CA   . GLN B 1 624  ? 91.580  142.016 95.733  1.00 27.36 ?  624  GLN B CA   1 
ATOM   11918 C C    . GLN B 1 624  ? 92.997  141.532 95.482  1.00 27.80 ?  624  GLN B C    1 
ATOM   11919 O O    . GLN B 1 624  ? 93.359  140.433 95.913  1.00 27.94 ?  624  GLN B O    1 
ATOM   11920 C CB   . GLN B 1 624  ? 91.341  142.237 97.228  1.00 24.36 ?  624  GLN B CB   1 
ATOM   11921 C CG   . GLN B 1 624  ? 92.438  143.033 97.918  1.00 23.39 ?  624  GLN B CG   1 
ATOM   11922 C CD   . GLN B 1 624  ? 92.459  142.824 99.420  1.00 27.13 ?  624  GLN B CD   1 
ATOM   11923 O OE1  . GLN B 1 624  ? 91.646  142.079 99.966  1.00 26.15 ?  624  GLN B OE1  1 
ATOM   11924 N NE2  . GLN B 1 624  ? 93.393  143.483 100.096 1.00 27.64 ?  624  GLN B NE2  1 
ATOM   11925 N N    . PHE B 1 625  ? 93.791  142.341 94.789  1.00 26.94 ?  625  PHE B N    1 
ATOM   11926 C CA   . PHE B 1 625  ? 95.189  142.031 94.540  1.00 26.18 ?  625  PHE B CA   1 
ATOM   11927 C C    . PHE B 1 625  ? 96.041  142.590 95.678  1.00 28.47 ?  625  PHE B C    1 
ATOM   11928 O O    . PHE B 1 625  ? 95.529  143.007 96.721  1.00 28.86 ?  625  PHE B O    1 
ATOM   11929 C CB   . PHE B 1 625  ? 95.623  142.582 93.184  1.00 23.08 ?  625  PHE B CB   1 
ATOM   11930 C CG   . PHE B 1 625  ? 94.927  141.944 92.019  1.00 23.69 ?  625  PHE B CG   1 
ATOM   11931 C CD1  . PHE B 1 625  ? 95.431  140.790 91.443  1.00 23.47 ?  625  PHE B CD1  1 
ATOM   11932 C CD2  . PHE B 1 625  ? 93.771  142.500 91.495  1.00 26.53 ?  625  PHE B CD2  1 
ATOM   11933 C CE1  . PHE B 1 625  ? 94.794  140.200 90.369  1.00 25.37 ?  625  PHE B CE1  1 
ATOM   11934 C CE2  . PHE B 1 625  ? 93.129  141.915 90.421  1.00 28.52 ?  625  PHE B CE2  1 
ATOM   11935 C CZ   . PHE B 1 625  ? 93.641  140.764 89.859  1.00 26.84 ?  625  PHE B CZ   1 
ATOM   11936 N N    . ILE B 1 626  ? 97.359  142.599 95.491  1.00 22.97 ?  626  ILE B N    1 
ATOM   11937 C CA   . ILE B 1 626  ? 98.276  143.190 96.462  1.00 19.22 ?  626  ILE B CA   1 
ATOM   11938 C C    . ILE B 1 626  ? 98.152  144.705 96.332  1.00 20.57 ?  626  ILE B C    1 
ATOM   11939 O O    . ILE B 1 626  ? 98.642  145.299 95.371  1.00 22.06 ?  626  ILE B O    1 
ATOM   11940 C CB   . ILE B 1 626  ? 99.717  142.723 96.248  1.00 16.34 ?  626  ILE B CB   1 
ATOM   11941 C CG1  . ILE B 1 626  ? 99.763  141.205 96.090  1.00 15.39 ?  626  ILE B CG1  1 
ATOM   11942 C CG2  . ILE B 1 626  ? 100.601 143.184 97.397  1.00 18.52 ?  626  ILE B CG2  1 
ATOM   11943 C CD1  . ILE B 1 626  ? 99.697  140.450 97.392  1.00 17.15 ?  626  ILE B CD1  1 
ATOM   11944 N N    . LEU B 1 627  ? 97.492  145.335 97.298  1.00 24.18 ?  627  LEU B N    1 
ATOM   11945 C CA   . LEU B 1 627  ? 97.324  146.779 97.276  1.00 25.58 ?  627  LEU B CA   1 
ATOM   11946 C C    . LEU B 1 627  ? 98.545  147.461 97.878  1.00 20.90 ?  627  LEU B C    1 
ATOM   11947 O O    . LEU B 1 627  ? 99.114  146.991 98.868  1.00 20.33 ?  627  LEU B O    1 
ATOM   11948 C CB   . LEU B 1 627  ? 96.061  147.184 98.035  1.00 26.69 ?  627  LEU B CB   1 
ATOM   11949 C CG   . LEU B 1 627  ? 95.591  148.631 97.875  1.00 26.00 ?  627  LEU B CG   1 
ATOM   11950 C CD1  . LEU B 1 627  ? 95.028  148.864 96.482  1.00 23.89 ?  627  LEU B CD1  1 
ATOM   11951 C CD2  . LEU B 1 627  ? 94.561  148.980 98.938  1.00 23.01 ?  627  LEU B CD2  1 
ATOM   11952 N N    . VAL B 1 628  ? 98.949  148.575 97.262  1.00 15.82 ?  628  VAL B N    1 
ATOM   11953 C CA   . VAL B 1 628  ? 100.116 149.318 97.719  1.00 16.52 ?  628  VAL B CA   1 
ATOM   11954 C C    . VAL B 1 628  ? 99.883  149.940 99.091  1.00 17.63 ?  628  VAL B C    1 
ATOM   11955 O O    . VAL B 1 628  ? 100.841 150.155 99.842  1.00 16.46 ?  628  VAL B O    1 
ATOM   11956 C CB   . VAL B 1 628  ? 100.484 150.383 96.666  1.00 20.98 ?  628  VAL B CB   1 
ATOM   11957 C CG1  . VAL B 1 628  ? 101.809 151.062 96.995  1.00 21.45 ?  628  VAL B CG1  1 
ATOM   11958 C CG2  . VAL B 1 628  ? 100.529 149.761 95.281  1.00 19.78 ?  628  VAL B CG2  1 
ATOM   11959 N N    . ASP B 1 629  ? 98.625  150.218 99.447  1.00 19.09 ?  629  ASP B N    1 
ATOM   11960 C CA   . ASP B 1 629  ? 98.333  150.874 100.717 1.00 20.72 ?  629  ASP B CA   1 
ATOM   11961 C C    . ASP B 1 629  ? 98.663  149.989 101.913 1.00 22.54 ?  629  ASP B C    1 
ATOM   11962 O O    . ASP B 1 629  ? 99.077  150.500 102.960 1.00 24.11 ?  629  ASP B O    1 
ATOM   11963 C CB   . ASP B 1 629  ? 96.866  151.300 100.760 1.00 22.85 ?  629  ASP B CB   1 
ATOM   11964 C CG   . ASP B 1 629  ? 96.569  152.456 99.825  1.00 24.68 ?  629  ASP B CG   1 
ATOM   11965 O OD1  . ASP B 1 629  ? 96.646  152.263 98.593  1.00 24.56 ?  629  ASP B OD1  1 
ATOM   11966 O OD2  . ASP B 1 629  ? 96.259  153.559 100.323 1.00 24.99 ?  629  ASP B OD2  1 
ATOM   11967 N N    . ASP B 1 630  ? 98.479  148.671 101.791 1.00 20.60 ?  630  ASP B N    1 
ATOM   11968 C CA   . ASP B 1 630  ? 98.875  147.780 102.877 1.00 19.85 ?  630  ASP B CA   1 
ATOM   11969 C C    . ASP B 1 630  ? 100.391 147.718 103.014 1.00 17.37 ?  630  ASP B C    1 
ATOM   11970 O O    . ASP B 1 630  ? 100.919 147.686 104.131 1.00 20.68 ?  630  ASP B O    1 
ATOM   11971 C CB   . ASP B 1 630  ? 98.305  146.378 102.658 1.00 22.45 ?  630  ASP B CB   1 
ATOM   11972 C CG   . ASP B 1 630  ? 96.908  146.396 102.074 1.00 25.04 ?  630  ASP B CG   1 
ATOM   11973 O OD1  . ASP B 1 630  ? 95.970  146.829 102.775 1.00 27.58 ?  630  ASP B OD1  1 
ATOM   11974 O OD2  . ASP B 1 630  ? 96.746  145.952 100.920 1.00 19.02 ?  630  ASP B OD2  1 
ATOM   11975 N N    . LEU B 1 631  ? 101.107 147.701 101.887 1.00 19.02 ?  631  LEU B N    1 
ATOM   11976 C CA   . LEU B 1 631  ? 102.564 147.637 101.920 1.00 18.22 ?  631  LEU B CA   1 
ATOM   11977 C C    . LEU B 1 631  ? 103.191 148.949 102.367 1.00 16.52 ?  631  LEU B C    1 
ATOM   11978 O O    . LEU B 1 631  ? 104.329 148.945 102.848 1.00 18.26 ?  631  LEU B O    1 
ATOM   11979 C CB   . LEU B 1 631  ? 103.106 147.261 100.541 1.00 16.00 ?  631  LEU B CB   1 
ATOM   11980 C CG   . LEU B 1 631  ? 102.729 145.896 99.969  1.00 9.39  ?  631  LEU B CG   1 
ATOM   11981 C CD1  . LEU B 1 631  ? 102.834 145.933 98.457  1.00 12.18 ?  631  LEU B CD1  1 
ATOM   11982 C CD2  . LEU B 1 631  ? 103.608 144.800 100.543 1.00 9.02  ?  631  LEU B CD2  1 
ATOM   11983 N N    . LYS B 1 632  ? 102.472 150.066 102.219 1.00 14.72 ?  632  LYS B N    1 
ATOM   11984 C CA   . LYS B 1 632  ? 103.023 151.382 102.522 1.00 13.06 ?  632  LYS B CA   1 
ATOM   11985 C C    . LYS B 1 632  ? 103.337 151.559 104.001 1.00 12.08 ?  632  LYS B C    1 
ATOM   11986 O O    . LYS B 1 632  ? 104.097 152.465 104.356 1.00 11.79 ?  632  LYS B O    1 
ATOM   11987 C CB   . LYS B 1 632  ? 102.047 152.463 102.054 1.00 15.24 ?  632  LYS B CB   1 
ATOM   11988 C CG   . LYS B 1 632  ? 102.697 153.783 101.686 1.00 13.23 ?  632  LYS B CG   1 
ATOM   11989 C CD   . LYS B 1 632  ? 101.675 154.909 101.659 1.00 15.21 ?  632  LYS B CD   1 
ATOM   11990 C CE   . LYS B 1 632  ? 100.529 154.598 100.706 1.00 18.69 ?  632  LYS B CE   1 
ATOM   11991 N NZ   . LYS B 1 632  ? 101.012 154.265 99.337  1.00 17.68 ?  632  LYS B NZ   1 
ATOM   11992 N N    . LYS B 1 633  ? 102.789 150.708 104.866 1.00 21.46 ?  633  LYS B N    1 
ATOM   11993 C CA   . LYS B 1 633  ? 103.045 150.755 106.299 1.00 22.45 ?  633  LYS B CA   1 
ATOM   11994 C C    . LYS B 1 633  ? 104.340 150.047 106.691 1.00 19.87 ?  633  LYS B C    1 
ATOM   11995 O O    . LYS B 1 633  ? 104.487 149.642 107.850 1.00 20.06 ?  633  LYS B O    1 
ATOM   11996 C CB   . LYS B 1 633  ? 101.862 150.156 107.062 1.00 15.10 ?  633  LYS B CB   1 
ATOM   11997 C CG   . LYS B 1 633  ? 100.500 150.584 106.531 1.00 17.31 ?  633  LYS B CG   1 
ATOM   11998 C CD   . LYS B 1 633  ? 100.297 152.088 106.645 1.00 18.68 ?  633  LYS B CD   1 
ATOM   11999 C CE   . LYS B 1 633  ? 99.398  152.612 105.534 1.00 17.74 ?  633  LYS B CE   1 
ATOM   12000 N NZ   . LYS B 1 633  ? 98.135  151.832 105.415 1.00 19.59 ?  633  LYS B NZ   1 
ATOM   12001 N N    . SER B 1 634  ? 105.262 149.860 105.748 1.00 16.55 ?  634  SER B N    1 
ATOM   12002 C CA   . SER B 1 634  ? 106.572 149.293 106.031 1.00 13.45 ?  634  SER B CA   1 
ATOM   12003 C C    . SER B 1 634  ? 107.698 150.312 105.973 1.00 15.96 ?  634  SER B C    1 
ATOM   12004 O O    . SER B 1 634  ? 108.668 150.180 106.720 1.00 24.67 ?  634  SER B O    1 
ATOM   12005 C CB   . SER B 1 634  ? 106.884 148.155 105.052 1.00 17.76 ?  634  SER B CB   1 
ATOM   12006 O OG   . SER B 1 634  ? 105.712 147.429 104.727 1.00 18.26 ?  634  SER B OG   1 
ATOM   12007 N N    . TRP B 1 635  ? 107.597 151.321 105.108 1.00 14.44 ?  635  TRP B N    1 
ATOM   12008 C CA   . TRP B 1 635  ? 108.609 152.363 105.019 1.00 11.69 ?  635  TRP B CA   1 
ATOM   12009 C C    . TRP B 1 635  ? 108.096 153.737 105.427 1.00 16.16 ?  635  TRP B C    1 
ATOM   12010 O O    . TRP B 1 635  ? 108.884 154.690 105.452 1.00 23.93 ?  635  TRP B O    1 
ATOM   12011 C CB   . TRP B 1 635  ? 109.190 152.429 103.599 1.00 10.93 ?  635  TRP B CB   1 
ATOM   12012 C CG   . TRP B 1 635  ? 108.182 152.676 102.519 1.00 13.55 ?  635  TRP B CG   1 
ATOM   12013 C CD1  . TRP B 1 635  ? 107.631 153.873 102.166 1.00 11.16 ?  635  TRP B CD1  1 
ATOM   12014 C CD2  . TRP B 1 635  ? 107.620 151.701 101.634 1.00 13.60 ?  635  TRP B CD2  1 
ATOM   12015 N NE1  . TRP B 1 635  ? 106.754 153.702 101.123 1.00 8.41  ?  635  TRP B NE1  1 
ATOM   12016 C CE2  . TRP B 1 635  ? 106.730 152.377 100.777 1.00 10.40 ?  635  TRP B CE2  1 
ATOM   12017 C CE3  . TRP B 1 635  ? 107.781 150.320 101.486 1.00 8.42  ?  635  TRP B CE3  1 
ATOM   12018 C CZ2  . TRP B 1 635  ? 106.003 151.719 99.788  1.00 11.23 ?  635  TRP B CZ2  1 
ATOM   12019 C CZ3  . TRP B 1 635  ? 107.058 149.670 100.505 1.00 6.15  ?  635  TRP B CZ3  1 
ATOM   12020 C CH2  . TRP B 1 635  ? 106.181 150.369 99.668  1.00 7.56  ?  635  TRP B CH2  1 
ATOM   12021 N N    . GLN B 1 636  ? 106.809 153.871 105.743 1.00 16.23 ?  636  GLN B N    1 
ATOM   12022 C CA   . GLN B 1 636  ? 106.255 155.129 106.227 1.00 19.22 ?  636  GLN B CA   1 
ATOM   12023 C C    . GLN B 1 636  ? 106.415 155.306 107.729 1.00 22.20 ?  636  GLN B C    1 
ATOM   12024 O O    . GLN B 1 636  ? 106.100 156.382 108.248 1.00 20.91 ?  636  GLN B O    1 
ATOM   12025 C CB   . GLN B 1 636  ? 104.769 155.229 105.867 1.00 16.89 ?  636  GLN B CB   1 
ATOM   12026 C CG   . GLN B 1 636  ? 104.317 156.616 105.445 1.00 15.78 ?  636  GLN B CG   1 
ATOM   12027 C CD   . GLN B 1 636  ? 104.766 156.974 104.044 1.00 19.60 ?  636  GLN B CD   1 
ATOM   12028 O OE1  . GLN B 1 636  ? 104.179 156.527 103.059 1.00 20.42 ?  636  GLN B OE1  1 
ATOM   12029 N NE2  . GLN B 1 636  ? 105.813 157.785 103.947 1.00 17.85 ?  636  GLN B NE2  1 
ATOM   12030 N N    . ILE B 1 637  ? 106.901 154.280 108.436 1.00 21.01 ?  637  ILE B N    1 
ATOM   12031 C CA   . ILE B 1 637  ? 107.020 154.328 109.893 1.00 23.63 ?  637  ILE B CA   1 
ATOM   12032 C C    . ILE B 1 637  ? 108.211 155.155 110.354 1.00 22.19 ?  637  ILE B C    1 
ATOM   12033 O O    . ILE B 1 637  ? 108.435 155.287 111.564 1.00 22.01 ?  637  ILE B O    1 
ATOM   12034 C CB   . ILE B 1 637  ? 107.061 152.878 110.423 1.00 22.43 ?  637  ILE B CB   1 
ATOM   12035 C CG1  . ILE B 1 637  ? 106.171 151.982 109.560 1.00 17.84 ?  637  ILE B CG1  1 
ATOM   12036 C CG2  . ILE B 1 637  ? 106.583 152.785 111.866 1.00 17.65 ?  637  ILE B CG2  1 
ATOM   12037 C CD1  . ILE B 1 637  ? 104.679 152.208 109.783 1.00 20.19 ?  637  ILE B CD1  1 
ATOM   12038 N N    . LYS B 1 638  ? 108.987 155.723 109.430 1.00 17.42 ?  638  LYS B N    1 
ATOM   12039 C CA   . LYS B 1 638  ? 110.002 156.691 109.831 1.00 20.72 ?  638  LYS B CA   1 
ATOM   12040 C C    . LYS B 1 638  ? 109.361 157.965 110.373 1.00 24.55 ?  638  LYS B C    1 
ATOM   12041 O O    . LYS B 1 638  ? 109.837 158.534 111.363 1.00 29.39 ?  638  LYS B O    1 
ATOM   12042 C CB   . LYS B 1 638  ? 110.928 157.008 108.655 1.00 20.58 ?  638  LYS B CB   1 
ATOM   12043 C CG   . LYS B 1 638  ? 112.061 157.958 109.011 1.00 24.03 ?  638  LYS B CG   1 
ATOM   12044 C CD   . LYS B 1 638  ? 112.953 158.245 107.823 1.00 23.81 ?  638  LYS B CD   1 
ATOM   12045 C CE   . LYS B 1 638  ? 112.211 159.058 106.773 1.00 23.41 ?  638  LYS B CE   1 
ATOM   12046 N NZ   . LYS B 1 638  ? 111.852 160.412 107.276 1.00 19.17 ?  638  LYS B NZ   1 
ATOM   12047 N N    . GLY B 1 639  ? 108.261 158.404 109.765 1.00 18.22 ?  639  GLY B N    1 
ATOM   12048 C CA   . GLY B 1 639  ? 107.644 159.670 110.116 1.00 18.48 ?  639  GLY B CA   1 
ATOM   12049 C C    . GLY B 1 639  ? 106.935 159.690 111.456 1.00 20.91 ?  639  GLY B C    1 
ATOM   12050 O O    . GLY B 1 639  ? 105.738 159.986 111.532 1.00 22.50 ?  639  GLY B O    1 
ATOM   12051 N N    . ILE B 1 640  ? 107.668 159.367 112.522 1.00 23.55 ?  640  ILE B N    1 
ATOM   12052 C CA   . ILE B 1 640  ? 107.181 159.462 113.894 1.00 19.98 ?  640  ILE B CA   1 
ATOM   12053 C C    . ILE B 1 640  ? 108.240 160.256 114.653 1.00 21.15 ?  640  ILE B C    1 
ATOM   12054 O O    . ILE B 1 640  ? 109.148 160.831 114.042 1.00 24.80 ?  640  ILE B O    1 
ATOM   12055 C CB   . ILE B 1 640  ? 106.922 158.083 114.538 1.00 20.87 ?  640  ILE B CB   1 
ATOM   12056 C CG1  . ILE B 1 640  ? 106.374 157.082 113.530 1.00 21.16 ?  640  ILE B CG1  1 
ATOM   12057 C CG2  . ILE B 1 640  ? 105.821 158.170 115.590 1.00 18.84 ?  640  ILE B CG2  1 
ATOM   12058 C CD1  . ILE B 1 640  ? 106.401 155.667 114.051 1.00 20.47 ?  640  ILE B CD1  1 
ATOM   12059 N N    . TYR B 1 641  ? 108.117 160.311 115.979 1.00 19.97 ?  641  TYR B N    1 
ATOM   12060 C CA   . TYR B 1 641  ? 109.037 161.074 116.824 1.00 23.18 ?  641  TYR B CA   1 
ATOM   12061 C C    . TYR B 1 641  ? 110.541 160.814 116.657 1.00 25.47 ?  641  TYR B C    1 
ATOM   12062 O O    . TYR B 1 641  ? 111.314 161.704 117.048 1.00 20.39 ?  641  TYR B O    1 
ATOM   12063 C CB   . TYR B 1 641  ? 108.670 160.896 118.311 1.00 21.59 ?  641  TYR B CB   1 
ATOM   12064 C CG   . TYR B 1 641  ? 108.756 159.490 118.889 1.00 21.90 ?  641  TYR B CG   1 
ATOM   12065 C CD1  . TYR B 1 641  ? 107.934 158.462 118.438 1.00 21.90 ?  641  TYR B CD1  1 
ATOM   12066 C CD2  . TYR B 1 641  ? 109.687 159.190 119.876 1.00 20.83 ?  641  TYR B CD2  1 
ATOM   12067 C CE1  . TYR B 1 641  ? 108.025 157.187 118.963 1.00 21.47 ?  641  TYR B CE1  1 
ATOM   12068 C CE2  . TYR B 1 641  ? 109.787 157.917 120.406 1.00 22.35 ?  641  TYR B CE2  1 
ATOM   12069 C CZ   . TYR B 1 641  ? 108.953 156.919 119.947 1.00 24.13 ?  641  TYR B CZ   1 
ATOM   12070 O OH   . TYR B 1 641  ? 109.050 155.652 120.473 1.00 27.59 ?  641  TYR B OH   1 
ATOM   12071 N N    . PRO B 1 642  ? 111.053 159.632 116.163 1.00 25.56 ?  642  PRO B N    1 
ATOM   12072 C CA   . PRO B 1 642  ? 112.511 159.535 115.954 1.00 21.09 ?  642  PRO B CA   1 
ATOM   12073 C C    . PRO B 1 642  ? 113.108 160.585 115.026 1.00 23.42 ?  642  PRO B C    1 
ATOM   12074 O O    . PRO B 1 642  ? 114.196 161.102 115.305 1.00 25.52 ?  642  PRO B O    1 
ATOM   12075 C CB   . PRO B 1 642  ? 112.695 158.125 115.367 1.00 19.07 ?  642  PRO B CB   1 
ATOM   12076 C CG   . PRO B 1 642  ? 111.327 157.598 115.115 1.00 19.42 ?  642  PRO B CG   1 
ATOM   12077 C CD   . PRO B 1 642  ? 110.465 158.282 116.105 1.00 21.83 ?  642  PRO B CD   1 
ATOM   12078 N N    . TRP B 1 643  ? 112.412 160.921 113.936 1.00 18.88 ?  643  TRP B N    1 
ATOM   12079 C CA   . TRP B 1 643  ? 112.926 161.933 113.016 1.00 18.60 ?  643  TRP B CA   1 
ATOM   12080 C C    . TRP B 1 643  ? 112.996 163.302 113.681 1.00 20.17 ?  643  TRP B C    1 
ATOM   12081 O O    . TRP B 1 643  ? 113.998 164.017 113.549 1.00 17.95 ?  643  TRP B O    1 
ATOM   12082 C CB   . TRP B 1 643  ? 112.055 161.996 111.763 1.00 21.85 ?  643  TRP B CB   1 
ATOM   12083 C CG   . TRP B 1 643  ? 112.185 163.289 111.014 1.00 26.19 ?  643  TRP B CG   1 
ATOM   12084 C CD1  . TRP B 1 643  ? 113.294 163.756 110.371 1.00 23.07 ?  643  TRP B CD1  1 
ATOM   12085 C CD2  . TRP B 1 643  ? 111.170 164.286 110.841 1.00 27.60 ?  643  TRP B CD2  1 
ATOM   12086 N NE1  . TRP B 1 643  ? 113.031 164.980 109.803 1.00 22.73 ?  643  TRP B NE1  1 
ATOM   12087 C CE2  . TRP B 1 643  ? 111.734 165.327 110.077 1.00 24.31 ?  643  TRP B CE2  1 
ATOM   12088 C CE3  . TRP B 1 643  ? 109.839 164.397 111.255 1.00 24.82 ?  643  TRP B CE3  1 
ATOM   12089 C CZ2  . TRP B 1 643  ? 111.014 166.465 109.719 1.00 21.60 ?  643  TRP B CZ2  1 
ATOM   12090 C CZ3  . TRP B 1 643  ? 109.126 165.528 110.898 1.00 24.08 ?  643  TRP B CZ3  1 
ATOM   12091 C CH2  . TRP B 1 643  ? 109.714 166.546 110.138 1.00 21.33 ?  643  TRP B CH2  1 
ATOM   12092 N N    . LEU B 1 644  ? 111.940 163.678 114.407 1.00 22.88 ?  644  LEU B N    1 
ATOM   12093 C CA   . LEU B 1 644  ? 111.930 164.956 115.111 1.00 23.80 ?  644  LEU B CA   1 
ATOM   12094 C C    . LEU B 1 644  ? 112.997 164.995 116.198 1.00 21.86 ?  644  LEU B C    1 
ATOM   12095 O O    . LEU B 1 644  ? 113.651 166.024 116.394 1.00 19.31 ?  644  LEU B O    1 
ATOM   12096 C CB   . LEU B 1 644  ? 110.546 165.211 115.707 1.00 22.95 ?  644  LEU B CB   1 
ATOM   12097 C CG   . LEU B 1 644  ? 110.403 166.417 116.636 1.00 20.31 ?  644  LEU B CG   1 
ATOM   12098 C CD1  . LEU B 1 644  ? 109.883 167.624 115.872 1.00 20.41 ?  644  LEU B CD1  1 
ATOM   12099 C CD2  . LEU B 1 644  ? 109.500 166.088 117.813 1.00 19.36 ?  644  LEU B CD2  1 
ATOM   12100 N N    . LYS B 1 645  ? 113.183 163.883 116.911 1.00 20.14 ?  645  LYS B N    1 
ATOM   12101 C CA   . LYS B 1 645  ? 114.192 163.823 117.963 1.00 17.50 ?  645  LYS B CA   1 
ATOM   12102 C C    . LYS B 1 645  ? 115.599 163.960 117.389 1.00 20.86 ?  645  LYS B C    1 
ATOM   12103 O O    . LYS B 1 645  ? 116.442 164.675 117.950 1.00 22.84 ?  645  LYS B O    1 
ATOM   12104 C CB   . LYS B 1 645  ? 114.035 162.515 118.741 1.00 18.54 ?  645  LYS B CB   1 
ATOM   12105 C CG   . LYS B 1 645  ? 115.173 162.183 119.681 1.00 19.83 ?  645  LYS B CG   1 
ATOM   12106 C CD   . LYS B 1 645  ? 114.952 160.840 120.365 1.00 21.91 ?  645  LYS B CD   1 
ATOM   12107 C CE   . LYS B 1 645  ? 116.179 160.414 121.159 1.00 20.98 ?  645  LYS B CE   1 
ATOM   12108 N NZ   . LYS B 1 645  ? 116.046 159.042 121.724 1.00 23.00 ?  645  LYS B NZ   1 
ATOM   12109 N N    . ARG B 1 646  ? 115.863 163.299 116.257 1.00 20.94 ?  646  ARG B N    1 
ATOM   12110 C CA   . ARG B 1 646  ? 117.154 163.442 115.590 1.00 20.93 ?  646  ARG B CA   1 
ATOM   12111 C C    . ARG B 1 646  ? 117.368 164.869 115.101 1.00 21.22 ?  646  ARG B C    1 
ATOM   12112 O O    . ARG B 1 646  ? 118.471 165.416 115.224 1.00 18.86 ?  646  ARG B O    1 
ATOM   12113 C CB   . ARG B 1 646  ? 117.251 162.456 114.426 1.00 19.55 ?  646  ARG B CB   1 
ATOM   12114 C CG   . ARG B 1 646  ? 118.552 162.535 113.650 1.00 19.18 ?  646  ARG B CG   1 
ATOM   12115 C CD   . ARG B 1 646  ? 118.697 161.356 112.706 1.00 18.20 ?  646  ARG B CD   1 
ATOM   12116 N NE   . ARG B 1 646  ? 117.729 161.395 111.617 1.00 23.11 ?  646  ARG B NE   1 
ATOM   12117 C CZ   . ARG B 1 646  ? 117.964 161.926 110.425 1.00 21.16 ?  646  ARG B CZ   1 
ATOM   12118 N NH1  . ARG B 1 646  ? 119.135 162.463 110.126 1.00 20.14 ?  646  ARG B NH1  1 
ATOM   12119 N NH2  . ARG B 1 646  ? 117.001 161.914 109.508 1.00 19.01 ?  646  ARG B NH2  1 
ATOM   12120 N N    . LYS B 1 647  ? 116.320 165.489 114.551 1.00 19.09 ?  647  LYS B N    1 
ATOM   12121 C CA   . LYS B 1 647  ? 116.422 166.876 114.105 1.00 20.39 ?  647  LYS B CA   1 
ATOM   12122 C C    . LYS B 1 647  ? 116.719 167.814 115.270 1.00 23.95 ?  647  LYS B C    1 
ATOM   12123 O O    . LYS B 1 647  ? 117.541 168.730 115.145 1.00 23.86 ?  647  LYS B O    1 
ATOM   12124 C CB   . LYS B 1 647  ? 115.131 167.288 113.395 1.00 22.97 ?  647  LYS B CB   1 
ATOM   12125 C CG   . LYS B 1 647  ? 115.025 168.774 113.080 1.00 21.26 ?  647  LYS B CG   1 
ATOM   12126 C CD   . LYS B 1 647  ? 116.130 169.232 112.141 1.00 21.43 ?  647  LYS B CD   1 
ATOM   12127 C CE   . LYS B 1 647  ? 116.444 170.706 112.348 1.00 22.22 ?  647  LYS B CE   1 
ATOM   12128 N NZ   . LYS B 1 647  ? 117.756 171.086 111.756 1.00 27.08 ?  647  LYS B NZ   1 
ATOM   12129 N N    . LEU B 1 648  ? 116.062 167.598 116.412 1.00 21.99 ?  648  LEU B N    1 
ATOM   12130 C CA   . LEU B 1 648  ? 116.290 168.450 117.575 1.00 21.23 ?  648  LEU B CA   1 
ATOM   12131 C C    . LEU B 1 648  ? 117.698 168.271 118.133 1.00 21.28 ?  648  LEU B C    1 
ATOM   12132 O O    . LEU B 1 648  ? 118.338 169.250 118.533 1.00 20.23 ?  648  LEU B O    1 
ATOM   12133 C CB   . LEU B 1 648  ? 115.240 168.167 118.650 1.00 20.64 ?  648  LEU B CB   1 
ATOM   12134 C CG   . LEU B 1 648  ? 113.810 168.628 118.347 1.00 23.25 ?  648  LEU B CG   1 
ATOM   12135 C CD1  . LEU B 1 648  ? 112.946 168.570 119.598 1.00 21.00 ?  648  LEU B CD1  1 
ATOM   12136 C CD2  . LEU B 1 648  ? 113.795 170.028 117.748 1.00 22.21 ?  648  LEU B CD2  1 
ATOM   12137 N N    . GLU B 1 649  ? 118.202 167.035 118.169 1.00 22.57 ?  649  GLU B N    1 
ATOM   12138 C CA   . GLU B 1 649  ? 119.566 166.828 118.644 1.00 22.37 ?  649  GLU B CA   1 
ATOM   12139 C C    . GLU B 1 649  ? 120.629 167.255 117.640 1.00 24.96 ?  649  GLU B C    1 
ATOM   12140 O O    . GLU B 1 649  ? 121.788 167.430 118.032 1.00 22.25 ?  649  GLU B O    1 
ATOM   12141 C CB   . GLU B 1 649  ? 119.796 165.365 119.026 1.00 16.37 ?  649  GLU B CB   1 
ATOM   12142 C CG   . GLU B 1 649  ? 119.335 165.009 120.426 1.00 20.55 ?  649  GLU B CG   1 
ATOM   12143 C CD   . GLU B 1 649  ? 119.061 163.531 120.592 1.00 22.24 ?  649  GLU B CD   1 
ATOM   12144 O OE1  . GLU B 1 649  ? 117.928 163.175 120.969 1.00 20.97 ?  649  GLU B OE1  1 
ATOM   12145 O OE2  . GLU B 1 649  ? 119.974 162.724 120.325 1.00 21.53 ?  649  GLU B OE2  1 
ATOM   12146 N N    . ASP B 1 650  ? 120.279 167.402 116.360 1.00 22.89 ?  650  ASP B N    1 
ATOM   12147 C CA   . ASP B 1 650  ? 121.267 167.848 115.383 1.00 22.47 ?  650  ASP B CA   1 
ATOM   12148 C C    . ASP B 1 650  ? 121.715 169.278 115.661 1.00 25.88 ?  650  ASP B C    1 
ATOM   12149 O O    . ASP B 1 650  ? 122.906 169.594 115.558 1.00 23.54 ?  650  ASP B O    1 
ATOM   12150 C CB   . ASP B 1 650  ? 120.694 167.730 113.971 1.00 23.51 ?  650  ASP B CB   1 
ATOM   12151 C CG   . ASP B 1 650  ? 121.545 168.436 112.931 1.00 26.84 ?  650  ASP B CG   1 
ATOM   12152 O OD1  . ASP B 1 650  ? 122.770 168.188 112.894 1.00 26.04 ?  650  ASP B OD1  1 
ATOM   12153 O OD2  . ASP B 1 650  ? 120.988 169.231 112.146 1.00 20.98 ?  650  ASP B OD2  1 
ATOM   12154 N N    . LEU B 1 651  ? 120.776 170.153 116.022 1.00 24.92 ?  651  LEU B N    1 
ATOM   12155 C CA   . LEU B 1 651  ? 121.101 171.552 116.261 1.00 23.43 ?  651  LEU B CA   1 
ATOM   12156 C C    . LEU B 1 651  ? 121.883 171.759 117.553 1.00 22.91 ?  651  LEU B C    1 
ATOM   12157 O O    . LEU B 1 651  ? 122.706 172.679 117.619 1.00 26.60 ?  651  LEU B O    1 
ATOM   12158 C CB   . LEU B 1 651  ? 119.802 172.384 116.212 1.00 22.23 ?  651  LEU B CB   1 
ATOM   12159 C CG   . LEU B 1 651  ? 118.677 172.472 117.264 1.00 25.10 ?  651  LEU B CG   1 
ATOM   12160 C CD1  . LEU B 1 651  ? 119.039 173.265 118.507 1.00 24.48 ?  651  LEU B CD1  1 
ATOM   12161 C CD2  . LEU B 1 651  ? 117.430 173.075 116.628 1.00 25.93 ?  651  LEU B CD2  1 
ATOM   12162 N N    . ILE B 1 652  ? 121.695 170.886 118.544 1.00 19.89 ?  652  ILE B N    1 
ATOM   12163 C CA   . ILE B 1 652  ? 122.358 171.043 119.836 1.00 20.15 ?  652  ILE B CA   1 
ATOM   12164 C C    . ILE B 1 652  ? 123.864 170.837 119.694 1.00 23.08 ?  652  ILE B C    1 
ATOM   12165 O O    . ILE B 1 652  ? 124.669 171.612 120.224 1.00 20.76 ?  652  ILE B O    1 
ATOM   12166 C CB   . ILE B 1 652  ? 121.735 170.072 120.856 1.00 22.89 ?  652  ILE B CB   1 
ATOM   12167 C CG1  . ILE B 1 652  ? 120.414 170.639 121.379 1.00 21.88 ?  652  ILE B CG1  1 
ATOM   12168 C CG2  . ILE B 1 652  ? 122.684 169.799 122.019 1.00 21.98 ?  652  ILE B CG2  1 
ATOM   12169 C CD1  . ILE B 1 652  ? 119.747 169.773 122.424 1.00 19.75 ?  652  ILE B CD1  1 
ATOM   12170 N N    . SER B 1 653  ? 124.264 169.803 118.961 1.00 25.84 ?  653  SER B N    1 
ATOM   12171 C CA   . SER B 1 653  ? 125.675 169.529 118.714 1.00 26.25 ?  653  SER B CA   1 
ATOM   12172 C C    . SER B 1 653  ? 126.226 170.421 117.607 1.00 24.67 ?  653  SER B C    1 
ATOM   12173 O O    . SER B 1 653  ? 126.184 171.647 117.705 1.00 22.74 ?  653  SER B O    1 
ATOM   12174 C CB   . SER B 1 653  ? 125.878 168.059 118.350 1.00 25.85 ?  653  SER B CB   1 
ATOM   12175 O OG   . SER B 1 653  ? 127.131 167.863 117.720 1.00 28.29 ?  653  SER B OG   1 
ATOM   12176 N N    . LEU B 1 670  ? 145.701 174.157 119.907 1.00 24.11 ?  670  LEU B N    1 
ATOM   12177 C CA   . LEU B 1 670  ? 146.843 173.531 120.562 1.00 23.42 ?  670  LEU B CA   1 
ATOM   12178 C C    . LEU B 1 670  ? 146.399 172.339 121.405 1.00 25.94 ?  670  LEU B C    1 
ATOM   12179 O O    . LEU B 1 670  ? 147.215 171.512 121.808 1.00 24.43 ?  670  LEU B O    1 
ATOM   12180 C CB   . LEU B 1 670  ? 147.590 174.552 121.426 1.00 22.75 ?  670  LEU B CB   1 
ATOM   12181 C CG   . LEU B 1 670  ? 146.829 175.192 122.590 1.00 23.76 ?  670  LEU B CG   1 
ATOM   12182 C CD1  . LEU B 1 670  ? 147.220 174.559 123.920 1.00 23.06 ?  670  LEU B CD1  1 
ATOM   12183 C CD2  . LEU B 1 670  ? 147.055 176.696 122.621 1.00 22.02 ?  670  LEU B CD2  1 
ATOM   12184 N N    . MET B 1 671  ? 145.099 172.265 121.673 1.00 27.47 ?  671  MET B N    1 
ATOM   12185 C CA   . MET B 1 671  ? 144.518 171.168 122.435 1.00 25.68 ?  671  MET B CA   1 
ATOM   12186 C C    . MET B 1 671  ? 143.411 170.433 121.696 1.00 29.39 ?  671  MET B C    1 
ATOM   12187 O O    . MET B 1 671  ? 143.203 169.245 121.953 1.00 29.59 ?  671  MET B O    1 
ATOM   12188 C CB   . MET B 1 671  ? 143.966 171.681 123.775 1.00 26.30 ?  671  MET B CB   1 
ATOM   12189 C CG   . MET B 1 671  ? 142.861 172.712 123.629 1.00 27.56 ?  671  MET B CG   1 
ATOM   12190 S SD   . MET B 1 671  ? 142.121 173.214 125.190 1.00 40.85 ?  671  MET B SD   1 
ATOM   12191 C CE   . MET B 1 671  ? 141.443 174.800 124.713 1.00 26.58 ?  671  MET B CE   1 
ATOM   12192 N N    . TYR B 1 672  ? 142.696 171.102 120.789 1.00 32.74 ?  672  TYR B N    1 
ATOM   12193 C CA   . TYR B 1 672  ? 141.631 170.448 120.041 1.00 34.64 ?  672  TYR B CA   1 
ATOM   12194 C C    . TYR B 1 672  ? 142.167 169.536 118.947 1.00 34.53 ?  672  TYR B C    1 
ATOM   12195 O O    . TYR B 1 672  ? 141.439 168.651 118.486 1.00 32.39 ?  672  TYR B O    1 
ATOM   12196 C CB   . TYR B 1 672  ? 140.691 171.494 119.436 1.00 33.55 ?  672  TYR B CB   1 
ATOM   12197 C CG   . TYR B 1 672  ? 141.281 172.265 118.274 1.00 32.30 ?  672  TYR B CG   1 
ATOM   12198 C CD1  . TYR B 1 672  ? 142.215 173.273 118.484 1.00 32.48 ?  672  TYR B CD1  1 
ATOM   12199 C CD2  . TYR B 1 672  ? 140.898 171.991 116.966 1.00 30.65 ?  672  TYR B CD2  1 
ATOM   12200 C CE1  . TYR B 1 672  ? 142.755 173.980 117.427 1.00 33.22 ?  672  TYR B CE1  1 
ATOM   12201 C CE2  . TYR B 1 672  ? 141.433 172.693 115.902 1.00 33.57 ?  672  TYR B CE2  1 
ATOM   12202 C CZ   . TYR B 1 672  ? 142.360 173.686 116.139 1.00 36.18 ?  672  TYR B CZ   1 
ATOM   12203 O OH   . TYR B 1 672  ? 142.895 174.389 115.084 1.00 33.41 ?  672  TYR B OH   1 
ATOM   12204 N N    . LYS B 1 673  ? 143.406 169.741 118.510 1.00 28.10 ?  673  LYS B N    1 
ATOM   12205 C CA   . LYS B 1 673  ? 144.027 168.899 117.495 1.00 29.03 ?  673  LYS B CA   1 
ATOM   12206 C C    . LYS B 1 673  ? 145.324 168.254 117.954 1.00 28.59 ?  673  LYS B C    1 
ATOM   12207 O O    . LYS B 1 673  ? 145.532 167.063 117.708 1.00 30.66 ?  673  LYS B O    1 
ATOM   12208 C CB   . LYS B 1 673  ? 144.289 169.719 116.223 1.00 27.22 ?  673  LYS B CB   1 
ATOM   12209 C CG   . LYS B 1 673  ? 144.778 168.899 115.042 1.00 27.88 ?  673  LYS B CG   1 
ATOM   12210 C CD   . LYS B 1 673  ? 145.071 169.786 113.844 1.00 26.78 ?  673  LYS B CD   1 
ATOM   12211 C CE   . LYS B 1 673  ? 145.534 168.970 112.650 1.00 26.82 ?  673  LYS B CE   1 
ATOM   12212 N NZ   . LYS B 1 673  ? 145.796 169.829 111.463 1.00 25.48 ?  673  LYS B NZ   1 
ATOM   12213 N N    . ILE B 1 674  ? 146.207 169.010 118.612 1.00 22.16 ?  674  ILE B N    1 
ATOM   12214 C CA   . ILE B 1 674  ? 147.481 168.450 119.056 1.00 22.69 ?  674  ILE B CA   1 
ATOM   12215 C C    . ILE B 1 674  ? 147.269 167.477 120.208 1.00 25.07 ?  674  ILE B C    1 
ATOM   12216 O O    . ILE B 1 674  ? 147.841 166.380 120.227 1.00 25.59 ?  674  ILE B O    1 
ATOM   12217 C CB   . ILE B 1 674  ? 148.457 169.578 119.435 1.00 25.28 ?  674  ILE B CB   1 
ATOM   12218 C CG1  . ILE B 1 674  ? 148.577 170.587 118.291 1.00 23.79 ?  674  ILE B CG1  1 
ATOM   12219 C CG2  . ILE B 1 674  ? 149.822 169.007 119.791 1.00 24.70 ?  674  ILE B CG2  1 
ATOM   12220 C CD1  . ILE B 1 674  ? 149.052 169.981 116.987 1.00 22.45 ?  674  ILE B CD1  1 
ATOM   12221 N N    . CYS B 1 675  ? 146.444 167.854 121.182 1.00 27.65 ?  675  CYS B N    1 
ATOM   12222 C CA   . CYS B 1 675  ? 146.104 166.964 122.284 1.00 28.15 ?  675  CYS B CA   1 
ATOM   12223 C C    . CYS B 1 675  ? 144.977 166.004 121.933 1.00 28.27 ?  675  CYS B C    1 
ATOM   12224 O O    . CYS B 1 675  ? 144.620 165.162 122.764 1.00 29.70 ?  675  CYS B O    1 
ATOM   12225 C CB   . CYS B 1 675  ? 145.723 167.777 123.524 1.00 27.53 ?  675  CYS B CB   1 
ATOM   12226 S SG   . CYS B 1 675  ? 147.017 168.891 124.118 1.00 40.77 ?  675  CYS B SG   1 
ATOM   12227 N N    . HIS B 1 676  ? 144.411 166.115 120.733 1.00 27.00 ?  676  HIS B N    1 
ATOM   12228 C CA   . HIS B 1 676  ? 143.333 165.229 120.318 1.00 25.55 ?  676  HIS B CA   1 
ATOM   12229 C C    . HIS B 1 676  ? 143.841 163.806 120.133 1.00 27.36 ?  676  HIS B C    1 
ATOM   12230 O O    . HIS B 1 676  ? 144.923 163.579 119.585 1.00 26.31 ?  676  HIS B O    1 
ATOM   12231 C CB   . HIS B 1 676  ? 142.706 165.729 119.018 1.00 26.31 ?  676  HIS B CB   1 
ATOM   12232 C CG   . HIS B 1 676  ? 141.475 164.980 118.614 1.00 29.67 ?  676  HIS B CG   1 
ATOM   12233 N ND1  . HIS B 1 676  ? 140.210 165.357 119.012 1.00 30.56 ?  676  HIS B ND1  1 
ATOM   12234 C CD2  . HIS B 1 676  ? 141.315 163.876 117.847 1.00 26.97 ?  676  HIS B CD2  1 
ATOM   12235 C CE1  . HIS B 1 676  ? 139.324 164.517 118.507 1.00 28.28 ?  676  HIS B CE1  1 
ATOM   12236 N NE2  . HIS B 1 676  ? 139.968 163.609 117.796 1.00 27.65 ?  676  HIS B NE2  1 
ATOM   12237 N N    . HIS B 1 677  ? 143.042 162.848 120.590 1.00 28.15 ?  677  HIS B N    1 
ATOM   12238 C CA   . HIS B 1 677  ? 143.363 161.431 120.489 1.00 28.85 ?  677  HIS B CA   1 
ATOM   12239 C C    . HIS B 1 677  ? 142.074 160.650 120.701 1.00 28.02 ?  677  HIS B C    1 
ATOM   12240 O O    . HIS B 1 677  ? 140.988 161.226 120.816 1.00 28.19 ?  677  HIS B O    1 
ATOM   12241 C CB   . HIS B 1 677  ? 144.440 161.033 121.505 1.00 25.17 ?  677  HIS B CB   1 
ATOM   12242 C CG   . HIS B 1 677  ? 145.284 159.874 121.073 1.00 29.06 ?  677  HIS B CG   1 
ATOM   12243 N ND1  . HIS B 1 677  ? 145.047 158.583 121.494 1.00 28.51 ?  677  HIS B ND1  1 
ATOM   12244 C CD2  . HIS B 1 677  ? 146.362 159.811 120.256 1.00 31.18 ?  677  HIS B CD2  1 
ATOM   12245 C CE1  . HIS B 1 677  ? 145.942 157.775 120.956 1.00 27.34 ?  677  HIS B CE1  1 
ATOM   12246 N NE2  . HIS B 1 677  ? 146.752 158.495 120.200 1.00 31.06 ?  677  HIS B NE2  1 
ATOM   12247 N N    . MET B 1 678  ? 142.200 159.324 120.751 1.00 24.99 ?  678  MET B N    1 
ATOM   12248 C CA   . MET B 1 678  ? 141.070 158.485 121.127 1.00 26.80 ?  678  MET B CA   1 
ATOM   12249 C C    . MET B 1 678  ? 140.754 158.569 122.613 1.00 29.92 ?  678  MET B C    1 
ATOM   12250 O O    . MET B 1 678  ? 139.712 158.058 123.037 1.00 30.99 ?  678  MET B O    1 
ATOM   12251 C CB   . MET B 1 678  ? 141.339 157.030 120.736 1.00 28.27 ?  678  MET B CB   1 
ATOM   12252 C CG   . MET B 1 678  ? 141.033 156.713 119.282 1.00 28.22 ?  678  MET B CG   1 
ATOM   12253 S SD   . MET B 1 678  ? 140.319 155.071 119.068 1.00 34.07 ?  678  MET B SD   1 
ATOM   12254 C CE   . MET B 1 678  ? 140.071 155.037 117.295 1.00 28.95 ?  678  MET B CE   1 
ATOM   12255 N N    . ALA B 1 679  ? 141.624 159.195 123.410 1.00 29.64 ?  679  ALA B N    1 
ATOM   12256 C CA   . ALA B 1 679  ? 141.421 159.345 124.845 1.00 26.68 ?  679  ALA B CA   1 
ATOM   12257 C C    . ALA B 1 679  ? 141.660 160.782 125.295 1.00 26.34 ?  679  ALA B C    1 
ATOM   12258 O O    . ALA B 1 679  ? 142.189 161.015 126.385 1.00 27.10 ?  679  ALA B O    1 
ATOM   12259 C CB   . ALA B 1 679  ? 142.318 158.385 125.626 1.00 26.75 ?  679  ALA B CB   1 
ATOM   12260 N N    . PHE B 1 680  ? 141.284 161.760 124.469 1.00 26.76 ?  680  PHE B N    1 
ATOM   12261 C CA   . PHE B 1 680  ? 141.455 163.159 124.854 1.00 29.57 ?  680  PHE B CA   1 
ATOM   12262 C C    . PHE B 1 680  ? 140.397 163.579 125.867 1.00 30.05 ?  680  PHE B C    1 
ATOM   12263 O O    . PHE B 1 680  ? 140.717 163.941 127.006 1.00 29.03 ?  680  PHE B O    1 
ATOM   12264 C CB   . PHE B 1 680  ? 141.405 164.055 123.614 1.00 28.72 ?  680  PHE B CB   1 
ATOM   12265 C CG   . PHE B 1 680  ? 141.283 165.520 123.929 1.00 28.76 ?  680  PHE B CG   1 
ATOM   12266 C CD1  . PHE B 1 680  ? 142.256 166.168 124.675 1.00 27.40 ?  680  PHE B CD1  1 
ATOM   12267 C CD2  . PHE B 1 680  ? 140.194 166.250 123.481 1.00 27.46 ?  680  PHE B CD2  1 
ATOM   12268 C CE1  . PHE B 1 680  ? 142.145 167.515 124.967 1.00 27.31 ?  680  PHE B CE1  1 
ATOM   12269 C CE2  . PHE B 1 680  ? 140.077 167.598 123.769 1.00 28.88 ?  680  PHE B CE2  1 
ATOM   12270 C CZ   . PHE B 1 680  ? 141.055 168.231 124.513 1.00 29.48 ?  680  PHE B CZ   1 
ATOM   12271 N N    . GLU B 1 681  ? 139.124 163.540 125.468 1.00 28.71 ?  681  GLU B N    1 
ATOM   12272 C CA   . GLU B 1 681  ? 138.034 163.805 126.398 1.00 29.69 ?  681  GLU B CA   1 
ATOM   12273 C C    . GLU B 1 681  ? 137.721 162.598 127.271 1.00 27.09 ?  681  GLU B C    1 
ATOM   12274 O O    . GLU B 1 681  ? 137.058 162.743 128.306 1.00 25.32 ?  681  GLU B O    1 
ATOM   12275 C CB   . GLU B 1 681  ? 136.783 164.235 125.627 1.00 29.66 ?  681  GLU B CB   1 
ATOM   12276 C CG   . GLU B 1 681  ? 135.797 165.059 126.437 1.00 28.93 ?  681  GLU B CG   1 
ATOM   12277 C CD   . GLU B 1 681  ? 134.414 165.077 125.821 1.00 32.57 ?  681  GLU B CD   1 
ATOM   12278 O OE1  . GLU B 1 681  ? 134.279 164.672 124.647 1.00 31.87 ?  681  GLU B OE1  1 
ATOM   12279 O OE2  . GLU B 1 681  ? 133.460 165.491 126.512 1.00 33.78 ?  681  GLU B OE2  1 
ATOM   12280 N N    . VAL B 1 682  ? 138.192 161.412 126.877 1.00 26.81 ?  682  VAL B N    1 
ATOM   12281 C CA   . VAL B 1 682  ? 137.997 160.223 127.696 1.00 29.35 ?  682  VAL B CA   1 
ATOM   12282 C C    . VAL B 1 682  ? 138.781 160.335 128.998 1.00 29.03 ?  682  VAL B C    1 
ATOM   12283 O O    . VAL B 1 682  ? 138.388 159.752 130.012 1.00 26.54 ?  682  VAL B O    1 
ATOM   12284 C CB   . VAL B 1 682  ? 138.374 158.961 126.897 1.00 30.40 ?  682  VAL B CB   1 
ATOM   12285 C CG1  . VAL B 1 682  ? 137.909 157.701 127.614 1.00 28.58 ?  682  VAL B CG1  1 
ATOM   12286 C CG2  . VAL B 1 682  ? 137.767 159.028 125.505 1.00 26.43 ?  682  VAL B CG2  1 
ATOM   12287 N N    . THR B 1 683  ? 139.881 161.094 129.009 1.00 26.08 ?  683  THR B N    1 
ATOM   12288 C CA   . THR B 1 683  ? 140.580 161.357 130.265 1.00 27.78 ?  683  THR B CA   1 
ATOM   12289 C C    . THR B 1 683  ? 139.705 162.146 131.234 1.00 28.65 ?  683  THR B C    1 
ATOM   12290 O O    . THR B 1 683  ? 139.648 161.830 132.429 1.00 25.38 ?  683  THR B O    1 
ATOM   12291 C CB   . THR B 1 683  ? 141.890 162.102 130.000 1.00 26.15 ?  683  THR B CB   1 
ATOM   12292 O OG1  . THR B 1 683  ? 141.684 163.100 128.992 1.00 25.50 ?  683  THR B OG1  1 
ATOM   12293 C CG2  . THR B 1 683  ? 142.977 161.135 129.551 1.00 25.69 ?  683  THR B CG2  1 
ATOM   12294 N N    . ILE B 1 684  ? 139.000 163.164 130.736 1.00 27.34 ?  684  ILE B N    1 
ATOM   12295 C CA   . ILE B 1 684  ? 138.107 163.938 131.595 1.00 27.00 ?  684  ILE B CA   1 
ATOM   12296 C C    . ILE B 1 684  ? 136.915 163.091 132.028 1.00 26.82 ?  684  ILE B C    1 
ATOM   12297 O O    . ILE B 1 684  ? 136.435 163.202 133.164 1.00 24.60 ?  684  ILE B O    1 
ATOM   12298 C CB   . ILE B 1 684  ? 137.659 165.226 130.881 1.00 27.86 ?  684  ILE B CB   1 
ATOM   12299 C CG1  . ILE B 1 684  ? 138.808 165.813 130.057 1.00 26.12 ?  684  ILE B CG1  1 
ATOM   12300 C CG2  . ILE B 1 684  ? 137.157 166.243 131.894 1.00 27.18 ?  684  ILE B CG2  1 
ATOM   12301 C CD1  . ILE B 1 684  ? 139.932 166.400 130.889 1.00 25.24 ?  684  ILE B CD1  1 
ATOM   12302 N N    . ASN B 1 685  ? 136.416 162.236 131.130 1.00 26.92 ?  685  ASN B N    1 
ATOM   12303 C CA   . ASN B 1 685  ? 135.334 161.324 131.496 1.00 26.34 ?  685  ASN B CA   1 
ATOM   12304 C C    . ASN B 1 685  ? 135.775 160.345 132.581 1.00 26.94 ?  685  ASN B C    1 
ATOM   12305 O O    . ASN B 1 685  ? 135.014 160.051 133.511 1.00 27.86 ?  685  ASN B O    1 
ATOM   12306 C CB   . ASN B 1 685  ? 134.838 160.572 130.260 1.00 27.22 ?  685  ASN B CB   1 
ATOM   12307 C CG   . ASN B 1 685  ? 134.351 161.504 129.165 1.00 31.32 ?  685  ASN B CG   1 
ATOM   12308 O OD1  . ASN B 1 685  ? 133.973 162.646 129.427 1.00 30.38 ?  685  ASN B OD1  1 
ATOM   12309 N ND2  . ASN B 1 685  ? 134.358 161.019 127.928 1.00 28.99 ?  685  ASN B ND2  1 
ATOM   12310 N N    . ILE B 1 686  ? 137.004 159.835 132.480 1.00 23.51 ?  686  ILE B N    1 
ATOM   12311 C CA   . ILE B 1 686  ? 137.556 158.951 133.502 1.00 27.72 ?  686  ILE B CA   1 
ATOM   12312 C C    . ILE B 1 686  ? 137.728 159.700 134.817 1.00 24.42 ?  686  ILE B C    1 
ATOM   12313 O O    . ILE B 1 686  ? 137.496 159.145 135.897 1.00 19.51 ?  686  ILE B O    1 
ATOM   12314 C CB   . ILE B 1 686  ? 138.881 158.339 133.002 1.00 27.85 ?  686  ILE B CB   1 
ATOM   12315 C CG1  . ILE B 1 686  ? 138.608 157.198 132.021 1.00 24.39 ?  686  ILE B CG1  1 
ATOM   12316 C CG2  . ILE B 1 686  ? 139.755 157.846 134.153 1.00 23.49 ?  686  ILE B CG2  1 
ATOM   12317 C CD1  . ILE B 1 686  ? 139.779 156.885 131.116 1.00 21.24 ?  686  ILE B CD1  1 
ATOM   12318 N N    . ALA B 1 687  ? 138.122 160.975 134.749 1.00 22.83 ?  687  ALA B N    1 
ATOM   12319 C CA   . ALA B 1 687  ? 138.210 161.790 135.957 1.00 26.23 ?  687  ALA B CA   1 
ATOM   12320 C C    . ALA B 1 687  ? 136.845 161.952 136.616 1.00 28.48 ?  687  ALA B C    1 
ATOM   12321 O O    . ALA B 1 687  ? 136.730 161.893 137.845 1.00 29.21 ?  687  ALA B O    1 
ATOM   12322 C CB   . ALA B 1 687  ? 138.814 163.155 135.628 1.00 25.97 ?  687  ALA B CB   1 
ATOM   12323 N N    . ILE B 1 688  ? 135.798 162.147 135.811 1.00 24.22 ?  688  ILE B N    1 
ATOM   12324 C CA   . ILE B 1 688  ? 134.441 162.252 136.348 1.00 24.57 ?  688  ILE B CA   1 
ATOM   12325 C C    . ILE B 1 688  ? 134.008 160.933 136.987 1.00 24.98 ?  688  ILE B C    1 
ATOM   12326 O O    . ILE B 1 688  ? 133.399 160.914 138.067 1.00 24.92 ?  688  ILE B O    1 
ATOM   12327 C CB   . ILE B 1 688  ? 133.471 162.701 135.238 1.00 21.92 ?  688  ILE B CB   1 
ATOM   12328 C CG1  . ILE B 1 688  ? 133.751 164.153 134.840 1.00 22.73 ?  688  ILE B CG1  1 
ATOM   12329 C CG2  . ILE B 1 688  ? 132.022 162.541 135.673 1.00 22.22 ?  688  ILE B CG2  1 
ATOM   12330 C CD1  . ILE B 1 688  ? 133.394 165.166 135.908 1.00 24.51 ?  688  ILE B CD1  1 
ATOM   12331 N N    . VAL B 1 689  ? 134.314 159.811 136.329 1.00 20.47 ?  689  VAL B N    1 
ATOM   12332 C CA   . VAL B 1 689  ? 133.949 158.498 136.859 1.00 26.96 ?  689  VAL B CA   1 
ATOM   12333 C C    . VAL B 1 689  ? 134.704 158.208 138.156 1.00 29.69 ?  689  VAL B C    1 
ATOM   12334 O O    . VAL B 1 689  ? 134.160 157.605 139.089 1.00 28.32 ?  689  VAL B O    1 
ATOM   12335 C CB   . VAL B 1 689  ? 134.191 157.413 135.790 1.00 26.81 ?  689  VAL B CB   1 
ATOM   12336 C CG1  . VAL B 1 689  ? 134.052 156.014 136.373 1.00 21.05 ?  689  VAL B CG1  1 
ATOM   12337 C CG2  . VAL B 1 689  ? 133.221 157.590 134.631 1.00 24.78 ?  689  VAL B CG2  1 
ATOM   12338 N N    . LEU B 1 690  ? 135.961 158.645 138.247 1.00 26.41 ?  690  LEU B N    1 
ATOM   12339 C CA   . LEU B 1 690  ? 136.715 158.481 139.487 1.00 26.30 ?  690  LEU B CA   1 
ATOM   12340 C C    . LEU B 1 690  ? 136.230 159.424 140.582 1.00 25.55 ?  690  LEU B C    1 
ATOM   12341 O O    . LEU B 1 690  ? 136.318 159.084 141.767 1.00 29.37 ?  690  LEU B O    1 
ATOM   12342 C CB   . LEU B 1 690  ? 138.212 158.691 139.240 1.00 25.61 ?  690  LEU B CB   1 
ATOM   12343 C CG   . LEU B 1 690  ? 139.122 157.520 138.838 1.00 26.59 ?  690  LEU B CG   1 
ATOM   12344 C CD1  . LEU B 1 690  ? 139.438 156.662 140.054 1.00 26.19 ?  690  LEU B CD1  1 
ATOM   12345 C CD2  . LEU B 1 690  ? 138.545 156.658 137.726 1.00 25.23 ?  690  LEU B CD2  1 
ATOM   12346 N N    . ASN B 1 691  ? 135.735 160.608 140.219 1.00 22.93 ?  691  ASN B N    1 
ATOM   12347 C CA   . ASN B 1 691  ? 135.298 161.587 141.205 1.00 26.81 ?  691  ASN B CA   1 
ATOM   12348 C C    . ASN B 1 691  ? 133.855 161.405 141.661 1.00 27.09 ?  691  ASN B C    1 
ATOM   12349 O O    . ASN B 1 691  ? 133.462 162.029 142.651 1.00 22.43 ?  691  ASN B O    1 
ATOM   12350 C CB   . ASN B 1 691  ? 135.469 163.010 140.658 1.00 25.96 ?  691  ASN B CB   1 
ATOM   12351 C CG   . ASN B 1 691  ? 136.064 163.962 141.681 1.00 25.47 ?  691  ASN B CG   1 
ATOM   12352 O OD1  . ASN B 1 691  ? 136.682 163.536 142.657 1.00 27.15 ?  691  ASN B OD1  1 
ATOM   12353 N ND2  . ASN B 1 691  ? 135.871 165.259 141.467 1.00 22.41 ?  691  ASN B ND2  1 
ATOM   12354 N N    . ILE B 1 692  ? 133.052 160.593 140.965 1.00 26.67 ?  692  ILE B N    1 
ATOM   12355 C CA   . ILE B 1 692  ? 131.680 160.391 141.431 1.00 28.25 ?  692  ILE B CA   1 
ATOM   12356 C C    . ILE B 1 692  ? 131.654 159.625 142.755 1.00 28.79 ?  692  ILE B C    1 
ATOM   12357 O O    . ILE B 1 692  ? 130.780 159.865 143.596 1.00 24.61 ?  692  ILE B O    1 
ATOM   12358 C CB   . ILE B 1 692  ? 130.813 159.702 140.352 1.00 27.61 ?  692  ILE B CB   1 
ATOM   12359 C CG1  . ILE B 1 692  ? 129.334 159.719 140.758 1.00 29.13 ?  692  ILE B CG1  1 
ATOM   12360 C CG2  . ILE B 1 692  ? 131.252 158.274 140.093 1.00 21.77 ?  692  ILE B CG2  1 
ATOM   12361 C CD1  . ILE B 1 692  ? 128.430 158.908 139.845 1.00 25.86 ?  692  ILE B CD1  1 
ATOM   12362 N N    . VAL B 1 693  ? 132.600 158.713 142.971 1.00 28.36 ?  693  VAL B N    1 
ATOM   12363 C CA   . VAL B 1 693  ? 132.633 157.890 144.181 1.00 29.21 ?  693  VAL B CA   1 
ATOM   12364 C C    . VAL B 1 693  ? 132.865 158.744 145.430 1.00 25.24 ?  693  VAL B C    1 
ATOM   12365 O O    . VAL B 1 693  ? 132.144 158.549 146.420 1.00 24.21 ?  693  VAL B O    1 
ATOM   12366 C CB   . VAL B 1 693  ? 133.666 156.753 144.056 1.00 28.46 ?  693  VAL B CB   1 
ATOM   12367 C CG1  . VAL B 1 693  ? 133.587 155.825 145.258 1.00 27.97 ?  693  VAL B CG1  1 
ATOM   12368 C CG2  . VAL B 1 693  ? 133.450 155.981 142.764 1.00 27.28 ?  693  VAL B CG2  1 
ATOM   12369 N N    . PRO B 1 694  ? 133.823 159.688 145.471 1.00 24.88 ?  694  PRO B N    1 
ATOM   12370 C CA   . PRO B 1 694  ? 133.844 160.617 146.615 1.00 26.71 ?  694  PRO B CA   1 
ATOM   12371 C C    . PRO B 1 694  ? 132.691 161.606 146.613 1.00 27.51 ?  694  PRO B C    1 
ATOM   12372 O O    . PRO B 1 694  ? 132.364 162.149 147.675 1.00 26.55 ?  694  PRO B O    1 
ATOM   12373 C CB   . PRO B 1 694  ? 135.193 161.335 146.471 1.00 24.35 ?  694  PRO B CB   1 
ATOM   12374 C CG   . PRO B 1 694  ? 135.537 161.209 145.051 1.00 22.68 ?  694  PRO B CG   1 
ATOM   12375 C CD   . PRO B 1 694  ? 135.030 159.871 144.638 1.00 22.70 ?  694  PRO B CD   1 
ATOM   12376 N N    . ILE B 1 695  ? 132.082 161.878 145.458 1.00 26.07 ?  695  ILE B N    1 
ATOM   12377 C CA   . ILE B 1 695  ? 130.913 162.751 145.423 1.00 27.01 ?  695  ILE B CA   1 
ATOM   12378 C C    . ILE B 1 695  ? 129.699 162.047 146.021 1.00 28.87 ?  695  ILE B C    1 
ATOM   12379 O O    . ILE B 1 695  ? 128.944 162.636 146.805 1.00 26.63 ?  695  ILE B O    1 
ATOM   12380 C CB   . ILE B 1 695  ? 130.655 163.231 143.981 1.00 26.72 ?  695  ILE B CB   1 
ATOM   12381 C CG1  . ILE B 1 695  ? 131.500 164.470 143.676 1.00 25.73 ?  695  ILE B CG1  1 
ATOM   12382 C CG2  . ILE B 1 695  ? 129.180 163.536 143.746 1.00 26.62 ?  695  ILE B CG2  1 
ATOM   12383 C CD1  . ILE B 1 695  ? 131.514 164.859 142.213 1.00 27.29 ?  695  ILE B CD1  1 
ATOM   12384 N N    . ILE B 1 696  ? 129.507 160.769 145.687 1.00 25.16 ?  696  ILE B N    1 
ATOM   12385 C CA   . ILE B 1 696  ? 128.269 160.083 146.046 1.00 27.23 ?  696  ILE B CA   1 
ATOM   12386 C C    . ILE B 1 696  ? 128.252 159.606 147.496 1.00 23.88 ?  696  ILE B C    1 
ATOM   12387 O O    . ILE B 1 696  ? 127.176 159.282 148.015 1.00 17.13 ?  696  ILE B O    1 
ATOM   12388 C CB   . ILE B 1 696  ? 128.018 158.906 145.085 1.00 24.92 ?  696  ILE B CB   1 
ATOM   12389 C CG1  . ILE B 1 696  ? 126.518 158.639 144.924 1.00 24.49 ?  696  ILE B CG1  1 
ATOM   12390 C CG2  . ILE B 1 696  ? 128.747 157.649 145.550 1.00 22.00 ?  696  ILE B CG2  1 
ATOM   12391 C CD1  . ILE B 1 696  ? 125.710 159.867 144.562 1.00 20.83 ?  696  ILE B CD1  1 
ATOM   12392 N N    . MET B 1 697  ? 129.400 159.561 148.177 1.00 25.61 ?  697  MET B N    1 
ATOM   12393 C CA   . MET B 1 697  ? 129.408 159.069 149.550 1.00 24.08 ?  697  MET B CA   1 
ATOM   12394 C C    . MET B 1 697  ? 128.900 160.097 150.553 1.00 26.43 ?  697  MET B C    1 
ATOM   12395 O O    . MET B 1 697  ? 128.593 159.725 151.691 1.00 27.89 ?  697  MET B O    1 
ATOM   12396 C CB   . MET B 1 697  ? 130.815 158.588 149.944 1.00 24.07 ?  697  MET B CB   1 
ATOM   12397 C CG   . MET B 1 697  ? 131.991 159.549 149.701 1.00 25.91 ?  697  MET B CG   1 
ATOM   12398 S SD   . MET B 1 697  ? 132.041 161.086 150.654 1.00 39.09 ?  697  MET B SD   1 
ATOM   12399 C CE   . MET B 1 697  ? 132.633 160.492 152.238 1.00 27.74 ?  697  MET B CE   1 
ATOM   12400 N N    . GLU B 1 698  ? 128.813 161.372 150.162 1.00 24.16 ?  698  GLU B N    1 
ATOM   12401 C CA   . GLU B 1 698  ? 128.334 162.404 151.075 1.00 26.00 ?  698  GLU B CA   1 
ATOM   12402 C C    . GLU B 1 698  ? 126.871 162.188 151.442 1.00 27.28 ?  698  GLU B C    1 
ATOM   12403 O O    . GLU B 1 698  ? 126.488 162.339 152.608 1.00 26.61 ?  698  GLU B O    1 
ATOM   12404 C CB   . GLU B 1 698  ? 128.532 163.785 150.450 1.00 29.29 ?  698  GLU B CB   1 
ATOM   12405 C CG   . GLU B 1 698  ? 129.860 163.959 149.729 1.00 29.72 ?  698  GLU B CG   1 
ATOM   12406 C CD   . GLU B 1 698  ? 130.929 164.570 150.611 1.00 30.51 ?  698  GLU B CD   1 
ATOM   12407 O OE1  . GLU B 1 698  ? 130.574 165.206 151.625 1.00 29.66 ?  698  GLU B OE1  1 
ATOM   12408 O OE2  . GLU B 1 698  ? 132.126 164.418 150.288 1.00 26.39 ?  698  GLU B OE2  1 
ATOM   12409 N N    . PHE B 1 699  ? 126.039 161.836 150.462 1.00 25.82 ?  699  PHE B N    1 
ATOM   12410 C CA   . PHE B 1 699  ? 124.625 161.593 150.715 1.00 22.83 ?  699  PHE B CA   1 
ATOM   12411 C C    . PHE B 1 699  ? 124.349 160.190 151.238 1.00 21.44 ?  699  PHE B C    1 
ATOM   12412 O O    . PHE B 1 699  ? 123.238 159.933 151.716 1.00 24.65 ?  699  PHE B O    1 
ATOM   12413 C CB   . PHE B 1 699  ? 123.815 161.835 149.438 1.00 23.90 ?  699  PHE B CB   1 
ATOM   12414 C CG   . PHE B 1 699  ? 122.375 162.179 149.690 1.00 26.54 ?  699  PHE B CG   1 
ATOM   12415 C CD1  . PHE B 1 699  ? 122.031 163.376 150.297 1.00 25.95 ?  699  PHE B CD1  1 
ATOM   12416 C CD2  . PHE B 1 699  ? 121.365 161.307 149.319 1.00 23.44 ?  699  PHE B CD2  1 
ATOM   12417 C CE1  . PHE B 1 699  ? 120.707 163.697 150.531 1.00 26.36 ?  699  PHE B CE1  1 
ATOM   12418 C CE2  . PHE B 1 699  ? 120.038 161.621 149.550 1.00 25.14 ?  699  PHE B CE2  1 
ATOM   12419 C CZ   . PHE B 1 699  ? 119.709 162.818 150.156 1.00 27.11 ?  699  PHE B CZ   1 
ATOM   12420 N N    . VAL B 1 700  ? 125.320 159.284 151.163 1.00 20.81 ?  700  VAL B N    1 
ATOM   12421 C CA   . VAL B 1 700  ? 125.143 157.927 151.663 1.00 23.90 ?  700  VAL B CA   1 
ATOM   12422 C C    . VAL B 1 700  ? 126.017 157.702 152.891 1.00 21.63 ?  700  VAL B C    1 
ATOM   12423 O O    . VAL B 1 700  ? 127.196 157.367 152.774 1.00 15.15 ?  700  VAL B O    1 
ATOM   12424 C CB   . VAL B 1 700  ? 125.458 156.884 150.575 1.00 24.49 ?  700  VAL B CB   1 
ATOM   12425 C CG1  . VAL B 1 700  ? 125.008 155.501 151.021 1.00 20.92 ?  700  VAL B CG1  1 
ATOM   12426 C CG2  . VAL B 1 700  ? 124.793 157.268 149.262 1.00 22.90 ?  700  VAL B CG2  1 
ATOM   12427 N N    . ASP B 1 730  ? 137.412 160.857 159.753 1.00 30.79 ?  730  ASP B N    1 
ATOM   12428 C CA   . ASP B 1 730  ? 137.896 159.537 159.366 1.00 32.21 ?  730  ASP B CA   1 
ATOM   12429 C C    . ASP B 1 730  ? 138.501 159.562 157.966 1.00 35.20 ?  730  ASP B C    1 
ATOM   12430 O O    . ASP B 1 730  ? 139.699 159.794 157.801 1.00 35.59 ?  730  ASP B O    1 
ATOM   12431 C CB   . ASP B 1 730  ? 136.763 158.511 159.432 1.00 27.27 ?  730  ASP B CB   1 
ATOM   12432 C CG   . ASP B 1 730  ? 136.498 158.025 160.844 1.00 32.10 ?  730  ASP B CG   1 
ATOM   12433 O OD1  . ASP B 1 730  ? 137.287 158.366 161.750 1.00 33.16 ?  730  ASP B OD1  1 
ATOM   12434 O OD2  . ASP B 1 730  ? 135.500 157.302 161.048 1.00 34.13 ?  730  ASP B OD2  1 
ATOM   12435 N N    . ALA B 1 731  ? 137.662 159.323 156.960 1.00 30.75 ?  731  ALA B N    1 
ATOM   12436 C CA   . ALA B 1 731  ? 138.087 159.301 155.568 1.00 30.14 ?  731  ALA B CA   1 
ATOM   12437 C C    . ALA B 1 731  ? 137.755 160.592 154.832 1.00 26.78 ?  731  ALA B C    1 
ATOM   12438 O O    . ALA B 1 731  ? 137.848 160.634 153.601 1.00 27.72 ?  731  ALA B O    1 
ATOM   12439 C CB   . ALA B 1 731  ? 137.456 158.110 154.843 1.00 26.01 ?  731  ALA B CB   1 
ATOM   12440 N N    . LEU B 1 732  ? 137.363 161.643 155.555 1.00 23.64 ?  732  LEU B N    1 
ATOM   12441 C CA   . LEU B 1 732  ? 137.014 162.901 154.904 1.00 28.36 ?  732  LEU B CA   1 
ATOM   12442 C C    . LEU B 1 732  ? 138.250 163.651 154.420 1.00 29.71 ?  732  LEU B C    1 
ATOM   12443 O O    . LEU B 1 732  ? 138.174 164.391 153.433 1.00 28.65 ?  732  LEU B O    1 
ATOM   12444 C CB   . LEU B 1 732  ? 136.200 163.775 155.860 1.00 26.43 ?  732  LEU B CB   1 
ATOM   12445 C CG   . LEU B 1 732  ? 135.565 165.049 155.298 1.00 27.19 ?  732  LEU B CG   1 
ATOM   12446 C CD1  . LEU B 1 732  ? 134.833 164.761 153.995 1.00 26.79 ?  732  LEU B CD1  1 
ATOM   12447 C CD2  . LEU B 1 732  ? 134.628 165.680 156.316 1.00 25.31 ?  732  LEU B CD2  1 
ATOM   12448 N N    . ARG B 1 733  ? 139.391 163.469 155.091 1.00 29.84 ?  733  ARG B N    1 
ATOM   12449 C CA   . ARG B 1 733  ? 140.585 164.239 154.752 1.00 30.33 ?  733  ARG B CA   1 
ATOM   12450 C C    . ARG B 1 733  ? 141.154 163.834 153.396 1.00 27.43 ?  733  ARG B C    1 
ATOM   12451 O O    . ARG B 1 733  ? 141.516 164.699 152.590 1.00 24.01 ?  733  ARG B O    1 
ATOM   12452 C CB   . ARG B 1 733  ? 141.638 164.078 155.848 1.00 31.38 ?  733  ARG B CB   1 
ATOM   12453 C CG   . ARG B 1 733  ? 141.269 164.748 157.164 1.00 29.53 ?  733  ARG B CG   1 
ATOM   12454 C CD   . ARG B 1 733  ? 141.500 166.252 157.111 1.00 28.26 ?  733  ARG B CD   1 
ATOM   12455 N NE   . ARG B 1 733  ? 140.309 166.979 156.689 1.00 33.47 ?  733  ARG B NE   1 
ATOM   12456 C CZ   . ARG B 1 733  ? 139.328 167.349 157.500 1.00 32.50 ?  733  ARG B CZ   1 
ATOM   12457 N NH1  . ARG B 1 733  ? 139.362 167.078 158.795 1.00 29.35 ?  733  ARG B NH1  1 
ATOM   12458 N NH2  . ARG B 1 733  ? 138.285 168.006 157.000 1.00 29.24 ?  733  ARG B NH2  1 
ATOM   12459 N N    . ILE B 1 734  ? 141.242 162.529 153.126 1.00 25.47 ?  734  ILE B N    1 
ATOM   12460 C CA   . ILE B 1 734  ? 141.771 162.069 151.844 1.00 28.07 ?  734  ILE B CA   1 
ATOM   12461 C C    . ILE B 1 734  ? 140.827 162.451 150.707 1.00 26.59 ?  734  ILE B C    1 
ATOM   12462 O O    . ILE B 1 734  ? 141.268 162.843 149.617 1.00 21.97 ?  734  ILE B O    1 
ATOM   12463 C CB   . ILE B 1 734  ? 142.039 160.551 151.897 1.00 27.57 ?  734  ILE B CB   1 
ATOM   12464 C CG1  . ILE B 1 734  ? 142.297 159.982 150.499 1.00 23.38 ?  734  ILE B CG1  1 
ATOM   12465 C CG2  . ILE B 1 734  ? 140.895 159.818 152.588 1.00 26.59 ?  734  ILE B CG2  1 
ATOM   12466 C CD1  . ILE B 1 734  ? 142.652 158.511 150.493 1.00 25.00 ?  734  ILE B CD1  1 
ATOM   12467 N N    . SER B 1 735  ? 139.515 162.362 150.949 1.00 25.98 ?  735  SER B N    1 
ATOM   12468 C CA   . SER B 1 735  ? 138.540 162.783 149.949 1.00 26.55 ?  735  SER B CA   1 
ATOM   12469 C C    . SER B 1 735  ? 138.651 164.276 149.664 1.00 29.12 ?  735  SER B C    1 
ATOM   12470 O O    . SER B 1 735  ? 138.581 164.700 148.506 1.00 26.10 ?  735  SER B O    1 
ATOM   12471 C CB   . SER B 1 735  ? 137.126 162.428 150.410 1.00 26.17 ?  735  SER B CB   1 
ATOM   12472 O OG   . SER B 1 735  ? 136.746 163.203 151.533 1.00 23.74 ?  735  SER B OG   1 
ATOM   12473 N N    . ASN B 1 736  ? 138.841 165.088 150.707 1.00 27.11 ?  736  ASN B N    1 
ATOM   12474 C CA   . ASN B 1 736  ? 139.020 166.523 150.508 1.00 26.25 ?  736  ASN B CA   1 
ATOM   12475 C C    . ASN B 1 736  ? 140.310 166.824 149.753 1.00 28.67 ?  736  ASN B C    1 
ATOM   12476 O O    . ASN B 1 736  ? 140.341 167.719 148.900 1.00 26.65 ?  736  ASN B O    1 
ATOM   12477 C CB   . ASN B 1 736  ? 139.005 167.244 151.856 1.00 26.32 ?  736  ASN B CB   1 
ATOM   12478 C CG   . ASN B 1 736  ? 137.992 168.371 151.903 1.00 30.65 ?  736  ASN B CG   1 
ATOM   12479 O OD1  . ASN B 1 736  ? 137.111 168.465 151.048 1.00 32.73 ?  736  ASN B OD1  1 
ATOM   12480 N ND2  . ASN B 1 736  ? 138.111 169.233 152.906 1.00 27.68 ?  736  ASN B ND2  1 
ATOM   12481 N N    . TYR B 1 737  ? 141.383 166.085 150.051 1.00 27.87 ?  737  TYR B N    1 
ATOM   12482 C CA   . TYR B 1 737  ? 142.652 166.304 149.363 1.00 29.38 ?  737  TYR B CA   1 
ATOM   12483 C C    . TYR B 1 737  ? 142.555 165.957 147.881 1.00 28.28 ?  737  TYR B C    1 
ATOM   12484 O O    . TYR B 1 737  ? 143.030 166.718 147.028 1.00 26.43 ?  737  TYR B O    1 
ATOM   12485 C CB   . TYR B 1 737  ? 143.760 165.491 150.033 1.00 29.91 ?  737  TYR B CB   1 
ATOM   12486 C CG   . TYR B 1 737  ? 144.123 165.972 151.421 1.00 29.93 ?  737  TYR B CG   1 
ATOM   12487 C CD1  . TYR B 1 737  ? 143.895 167.288 151.804 1.00 29.16 ?  737  TYR B CD1  1 
ATOM   12488 C CD2  . TYR B 1 737  ? 144.693 165.109 152.349 1.00 27.82 ?  737  TYR B CD2  1 
ATOM   12489 C CE1  . TYR B 1 737  ? 144.224 167.732 153.072 1.00 29.06 ?  737  TYR B CE1  1 
ATOM   12490 C CE2  . TYR B 1 737  ? 145.025 165.543 153.620 1.00 26.33 ?  737  TYR B CE2  1 
ATOM   12491 C CZ   . TYR B 1 737  ? 144.789 166.855 153.975 1.00 29.78 ?  737  TYR B CZ   1 
ATOM   12492 O OH   . TYR B 1 737  ? 145.119 167.291 155.238 1.00 31.35 ?  737  TYR B OH   1 
ATOM   12493 N N    . VAL B 1 738  ? 141.937 164.818 147.551 1.00 25.41 ?  738  VAL B N    1 
ATOM   12494 C CA   . VAL B 1 738  ? 141.797 164.469 146.139 1.00 28.40 ?  738  VAL B CA   1 
ATOM   12495 C C    . VAL B 1 738  ? 140.798 165.395 145.452 1.00 27.53 ?  738  VAL B C    1 
ATOM   12496 O O    . VAL B 1 738  ? 140.934 165.680 144.255 1.00 23.40 ?  738  VAL B O    1 
ATOM   12497 C CB   . VAL B 1 738  ? 141.432 162.979 145.962 1.00 30.77 ?  738  VAL B CB   1 
ATOM   12498 C CG1  . VAL B 1 738  ? 142.492 162.094 146.604 1.00 28.82 ?  738  VAL B CG1  1 
ATOM   12499 C CG2  . VAL B 1 738  ? 140.056 162.664 146.523 1.00 24.96 ?  738  VAL B CG2  1 
ATOM   12500 N N    . PHE B 1 739  ? 139.806 165.907 146.192 1.00 24.06 ?  739  PHE B N    1 
ATOM   12501 C CA   . PHE B 1 739  ? 138.913 166.922 145.644 1.00 26.41 ?  739  PHE B CA   1 
ATOM   12502 C C    . PHE B 1 739  ? 139.678 168.184 145.278 1.00 26.51 ?  739  PHE B C    1 
ATOM   12503 O O    . PHE B 1 739  ? 139.470 168.754 144.202 1.00 22.25 ?  739  PHE B O    1 
ATOM   12504 C CB   . PHE B 1 739  ? 137.811 167.248 146.654 1.00 24.35 ?  739  PHE B CB   1 
ATOM   12505 C CG   . PHE B 1 739  ? 136.533 166.491 146.431 1.00 27.26 ?  739  PHE B CG   1 
ATOM   12506 C CD1  . PHE B 1 739  ? 136.463 165.473 145.494 1.00 27.14 ?  739  PHE B CD1  1 
ATOM   12507 C CD2  . PHE B 1 739  ? 135.400 166.796 147.168 1.00 27.09 ?  739  PHE B CD2  1 
ATOM   12508 C CE1  . PHE B 1 739  ? 135.285 164.779 145.294 1.00 26.34 ?  739  PHE B CE1  1 
ATOM   12509 C CE2  . PHE B 1 739  ? 134.220 166.104 146.973 1.00 24.49 ?  739  PHE B CE2  1 
ATOM   12510 C CZ   . PHE B 1 739  ? 134.163 165.094 146.035 1.00 21.68 ?  739  PHE B CZ   1 
ATOM   12511 N N    . PHE B 1 740  ? 140.578 168.628 146.159 1.00 26.30 ?  740  PHE B N    1 
ATOM   12512 C CA   . PHE B 1 740  ? 141.389 169.809 145.873 1.00 28.97 ?  740  PHE B CA   1 
ATOM   12513 C C    . PHE B 1 740  ? 142.324 169.567 144.694 1.00 27.46 ?  740  PHE B C    1 
ATOM   12514 O O    . PHE B 1 740  ? 142.530 170.462 143.866 1.00 23.69 ?  740  PHE B O    1 
ATOM   12515 C CB   . PHE B 1 740  ? 142.183 170.216 147.114 1.00 26.69 ?  740  PHE B CB   1 
ATOM   12516 C CG   . PHE B 1 740  ? 141.331 170.737 148.236 1.00 27.15 ?  740  PHE B CG   1 
ATOM   12517 C CD1  . PHE B 1 740  ? 140.159 171.428 147.972 1.00 25.98 ?  740  PHE B CD1  1 
ATOM   12518 C CD2  . PHE B 1 740  ? 141.703 170.538 149.556 1.00 27.82 ?  740  PHE B CD2  1 
ATOM   12519 C CE1  . PHE B 1 740  ? 139.373 171.909 149.003 1.00 25.54 ?  740  PHE B CE1  1 
ATOM   12520 C CE2  . PHE B 1 740  ? 140.922 171.017 150.592 1.00 26.23 ?  740  PHE B CE2  1 
ATOM   12521 C CZ   . PHE B 1 740  ? 139.755 171.703 150.314 1.00 25.25 ?  740  PHE B CZ   1 
ATOM   12522 N N    . VAL B 1 741  ? 142.896 168.363 144.601 1.00 27.49 ?  741  VAL B N    1 
ATOM   12523 C CA   . VAL B 1 741  ? 143.797 168.043 143.493 1.00 26.81 ?  741  VAL B CA   1 
ATOM   12524 C C    . VAL B 1 741  ? 143.044 168.071 142.164 1.00 29.24 ?  741  VAL B C    1 
ATOM   12525 O O    . VAL B 1 741  ? 143.503 168.667 141.180 1.00 27.11 ?  741  VAL B O    1 
ATOM   12526 C CB   . VAL B 1 741  ? 144.477 166.682 143.733 1.00 26.79 ?  741  VAL B CB   1 
ATOM   12527 C CG1  . VAL B 1 741  ? 145.113 166.161 142.451 1.00 23.72 ?  741  VAL B CG1  1 
ATOM   12528 C CG2  . VAL B 1 741  ? 145.518 166.799 144.835 1.00 27.81 ?  741  VAL B CG2  1 
ATOM   12529 N N    . ILE B 1 742  ? 141.867 167.440 142.122 1.00 28.21 ?  742  ILE B N    1 
ATOM   12530 C CA   . ILE B 1 742  ? 141.076 167.414 140.894 1.00 28.13 ?  742  ILE B CA   1 
ATOM   12531 C C    . ILE B 1 742  ? 140.566 168.813 140.554 1.00 26.23 ?  742  ILE B C    1 
ATOM   12532 O O    . ILE B 1 742  ? 140.489 169.191 139.377 1.00 19.51 ?  742  ILE B O    1 
ATOM   12533 C CB   . ILE B 1 742  ? 139.934 166.387 141.028 1.00 27.11 ?  742  ILE B CB   1 
ATOM   12534 C CG1  . ILE B 1 742  ? 140.517 164.973 141.118 1.00 25.25 ?  742  ILE B CG1  1 
ATOM   12535 C CG2  . ILE B 1 742  ? 138.962 166.483 139.859 1.00 25.93 ?  742  ILE B CG2  1 
ATOM   12536 C CD1  . ILE B 1 742  ? 139.510 163.860 140.906 1.00 24.26 ?  742  ILE B CD1  1 
ATOM   12537 N N    . TYR B 1 743  ? 140.228 169.609 141.573 1.00 26.02 ?  743  TYR B N    1 
ATOM   12538 C CA   . TYR B 1 743  ? 139.794 170.981 141.332 1.00 26.46 ?  743  TYR B CA   1 
ATOM   12539 C C    . TYR B 1 743  ? 140.923 171.826 140.756 1.00 27.74 ?  743  TYR B C    1 
ATOM   12540 O O    . TYR B 1 743  ? 140.692 172.642 139.861 1.00 27.22 ?  743  TYR B O    1 
ATOM   12541 C CB   . TYR B 1 743  ? 139.257 171.599 142.623 1.00 26.66 ?  743  TYR B CB   1 
ATOM   12542 C CG   . TYR B 1 743  ? 137.872 171.121 143.002 1.00 27.08 ?  743  TYR B CG   1 
ATOM   12543 C CD1  . TYR B 1 743  ? 137.118 170.346 142.127 1.00 23.82 ?  743  TYR B CD1  1 
ATOM   12544 C CD2  . TYR B 1 743  ? 137.318 171.441 144.235 1.00 29.17 ?  743  TYR B CD2  1 
ATOM   12545 C CE1  . TYR B 1 743  ? 135.854 169.904 142.469 1.00 27.20 ?  743  TYR B CE1  1 
ATOM   12546 C CE2  . TYR B 1 743  ? 136.053 171.005 144.586 1.00 28.58 ?  743  TYR B CE2  1 
ATOM   12547 C CZ   . TYR B 1 743  ? 135.326 170.237 143.699 1.00 29.22 ?  743  TYR B CZ   1 
ATOM   12548 O OH   . TYR B 1 743  ? 134.067 169.800 144.042 1.00 27.20 ?  743  TYR B OH   1 
ATOM   12549 N N    . ALA B 1 744  ? 142.151 171.638 141.246 1.00 26.78 ?  744  ALA B N    1 
ATOM   12550 C CA   . ALA B 1 744  ? 143.295 172.336 140.663 1.00 24.82 ?  744  ALA B CA   1 
ATOM   12551 C C    . ALA B 1 744  ? 143.551 171.880 139.230 1.00 25.08 ?  744  ALA B C    1 
ATOM   12552 O O    . ALA B 1 744  ? 143.900 172.696 138.365 1.00 20.29 ?  744  ALA B O    1 
ATOM   12553 C CB   . ALA B 1 744  ? 144.537 172.120 141.527 1.00 22.16 ?  744  ALA B CB   1 
ATOM   12554 N N    . ILE B 1 745  ? 143.385 170.581 138.964 1.00 25.15 ?  745  ILE B N    1 
ATOM   12555 C CA   . ILE B 1 745  ? 143.591 170.056 137.614 1.00 25.56 ?  745  ILE B CA   1 
ATOM   12556 C C    . ILE B 1 745  ? 142.585 170.668 136.643 1.00 27.12 ?  745  ILE B C    1 
ATOM   12557 O O    . ILE B 1 745  ? 142.949 171.155 135.566 1.00 24.87 ?  745  ILE B O    1 
ATOM   12558 C CB   . ILE B 1 745  ? 143.510 168.518 137.621 1.00 24.64 ?  745  ILE B CB   1 
ATOM   12559 C CG1  . ILE B 1 745  ? 144.791 167.918 138.206 1.00 23.62 ?  745  ILE B CG1  1 
ATOM   12560 C CG2  . ILE B 1 745  ? 143.267 167.978 136.218 1.00 22.33 ?  745  ILE B CG2  1 
ATOM   12561 C CD1  . ILE B 1 745  ? 146.048 168.319 137.466 1.00 23.66 ?  745  ILE B CD1  1 
ATOM   12562 N N    . GLU B 1 746  ? 141.305 170.681 137.023 1.00 27.50 ?  746  GLU B N    1 
ATOM   12563 C CA   . GLU B 1 746  ? 140.301 171.278 136.150 1.00 24.07 ?  746  GLU B CA   1 
ATOM   12564 C C    . GLU B 1 746  ? 140.410 172.798 136.101 1.00 23.16 ?  746  GLU B C    1 
ATOM   12565 O O    . GLU B 1 746  ? 140.017 173.401 135.098 1.00 22.83 ?  746  GLU B O    1 
ATOM   12566 C CB   . GLU B 1 746  ? 138.893 170.848 136.575 1.00 25.55 ?  746  GLU B CB   1 
ATOM   12567 C CG   . GLU B 1 746  ? 138.427 171.383 137.914 1.00 26.48 ?  746  GLU B CG   1 
ATOM   12568 C CD   . GLU B 1 746  ? 137.014 170.947 138.250 1.00 29.36 ?  746  GLU B CD   1 
ATOM   12569 O OE1  . GLU B 1 746  ? 136.527 169.978 137.631 1.00 27.51 ?  746  GLU B OE1  1 
ATOM   12570 O OE2  . GLU B 1 746  ? 136.390 171.574 139.132 1.00 28.70 ?  746  GLU B OE2  1 
ATOM   12571 N N    . ALA B 1 747  ? 140.966 173.428 137.140 1.00 21.90 ?  747  ALA B N    1 
ATOM   12572 C CA   . ALA B 1 747  ? 141.225 174.862 137.086 1.00 26.92 ?  747  ALA B CA   1 
ATOM   12573 C C    . ALA B 1 747  ? 142.304 175.189 136.064 1.00 28.81 ?  747  ALA B C    1 
ATOM   12574 O O    . ALA B 1 747  ? 142.165 176.146 135.296 1.00 31.16 ?  747  ALA B O    1 
ATOM   12575 C CB   . ALA B 1 747  ? 141.620 175.377 138.470 1.00 23.21 ?  747  ALA B CB   1 
ATOM   12576 N N    . ILE B 1 748  ? 143.383 174.402 136.029 1.00 24.52 ?  748  ILE B N    1 
ATOM   12577 C CA   . ILE B 1 748  ? 144.402 174.642 135.010 1.00 24.25 ?  748  ILE B CA   1 
ATOM   12578 C C    . ILE B 1 748  ? 143.881 174.244 133.630 1.00 22.64 ?  748  ILE B C    1 
ATOM   12579 O O    . ILE B 1 748  ? 144.286 174.826 132.615 1.00 23.99 ?  748  ILE B O    1 
ATOM   12580 C CB   . ILE B 1 748  ? 145.727 173.935 135.373 1.00 26.52 ?  748  ILE B CB   1 
ATOM   12581 C CG1  . ILE B 1 748  ? 146.915 174.733 134.834 1.00 24.13 ?  748  ILE B CG1  1 
ATOM   12582 C CG2  . ILE B 1 748  ? 145.786 172.509 134.841 1.00 23.10 ?  748  ILE B CG2  1 
ATOM   12583 C CD1  . ILE B 1 748  ? 148.168 174.604 135.672 1.00 20.69 ?  748  ILE B CD1  1 
ATOM   12584 N N    . VAL B 1 749  ? 142.945 173.288 133.569 1.00 20.42 ?  749  VAL B N    1 
ATOM   12585 C CA   . VAL B 1 749  ? 142.304 172.949 132.300 1.00 23.93 ?  749  VAL B CA   1 
ATOM   12586 C C    . VAL B 1 749  ? 141.490 174.130 131.782 1.00 25.43 ?  749  VAL B C    1 
ATOM   12587 O O    . VAL B 1 749  ? 141.558 174.480 130.597 1.00 24.59 ?  749  VAL B O    1 
ATOM   12588 C CB   . VAL B 1 749  ? 141.442 171.681 132.464 1.00 26.28 ?  749  VAL B CB   1 
ATOM   12589 C CG1  . VAL B 1 749  ? 140.335 171.627 131.417 1.00 23.21 ?  749  VAL B CG1  1 
ATOM   12590 C CG2  . VAL B 1 749  ? 142.313 170.436 132.384 1.00 26.76 ?  749  VAL B CG2  1 
ATOM   12591 N N    . LYS B 1 750  ? 140.726 174.778 132.665 1.00 26.90 ?  750  LYS B N    1 
ATOM   12592 C CA   . LYS B 1 750  ? 139.965 175.960 132.268 1.00 28.52 ?  750  LYS B CA   1 
ATOM   12593 C C    . LYS B 1 750  ? 140.876 177.141 131.953 1.00 28.08 ?  750  LYS B C    1 
ATOM   12594 O O    . LYS B 1 750  ? 140.548 177.960 131.088 1.00 28.28 ?  750  LYS B O    1 
ATOM   12595 C CB   . LYS B 1 750  ? 138.967 176.335 133.362 1.00 24.92 ?  750  LYS B CB   1 
ATOM   12596 C CG   . LYS B 1 750  ? 137.760 175.416 133.440 1.00 24.35 ?  750  LYS B CG   1 
ATOM   12597 C CD   . LYS B 1 750  ? 136.723 175.784 132.392 1.00 26.03 ?  750  LYS B CD   1 
ATOM   12598 C CE   . LYS B 1 750  ? 136.130 177.156 132.664 1.00 30.05 ?  750  LYS B CE   1 
ATOM   12599 N NZ   . LYS B 1 750  ? 135.121 177.539 131.638 1.00 29.85 ?  750  LYS B NZ   1 
ATOM   12600 N N    . ILE B 1 751  ? 142.015 177.248 132.641 1.00 24.09 ?  751  ILE B N    1 
ATOM   12601 C CA   . ILE B 1 751  ? 142.991 178.287 132.319 1.00 25.25 ?  751  ILE B CA   1 
ATOM   12602 C C    . ILE B 1 751  ? 143.530 178.086 130.907 1.00 26.20 ?  751  ILE B C    1 
ATOM   12603 O O    . ILE B 1 751  ? 143.663 179.044 130.133 1.00 22.54 ?  751  ILE B O    1 
ATOM   12604 C CB   . ILE B 1 751  ? 144.118 178.301 133.371 1.00 25.69 ?  751  ILE B CB   1 
ATOM   12605 C CG1  . ILE B 1 751  ? 143.646 178.999 134.648 1.00 24.17 ?  751  ILE B CG1  1 
ATOM   12606 C CG2  . ILE B 1 751  ? 145.371 178.981 132.833 1.00 25.50 ?  751  ILE B CG2  1 
ATOM   12607 C CD1  . ILE B 1 751  ? 143.180 180.422 134.432 1.00 23.56 ?  751  ILE B CD1  1 
ATOM   12608 N N    . LEU B 1 752  ? 143.832 176.836 130.545 1.00 24.18 ?  752  LEU B N    1 
ATOM   12609 C CA   . LEU B 1 752  ? 144.242 176.536 129.176 1.00 25.43 ?  752  LEU B CA   1 
ATOM   12610 C C    . LEU B 1 752  ? 143.113 176.808 128.186 1.00 29.30 ?  752  LEU B C    1 
ATOM   12611 O O    . LEU B 1 752  ? 143.353 177.309 127.081 1.00 26.79 ?  752  LEU B O    1 
ATOM   12612 C CB   . LEU B 1 752  ? 144.704 175.082 129.076 1.00 24.43 ?  752  LEU B CB   1 
ATOM   12613 C CG   . LEU B 1 752  ? 145.346 174.669 127.752 1.00 25.62 ?  752  LEU B CG   1 
ATOM   12614 C CD1  . LEU B 1 752  ? 146.512 175.587 127.421 1.00 23.90 ?  752  LEU B CD1  1 
ATOM   12615 C CD2  . LEU B 1 752  ? 145.796 173.217 127.799 1.00 23.58 ?  752  LEU B CD2  1 
ATOM   12616 N N    . GLY B 1 753  ? 141.876 176.488 128.568 1.00 26.64 ?  753  GLY B N    1 
ATOM   12617 C CA   . GLY B 1 753  ? 140.721 176.705 127.712 1.00 25.35 ?  753  GLY B CA   1 
ATOM   12618 C C    . GLY B 1 753  ? 140.295 178.151 127.578 1.00 26.89 ?  753  GLY B C    1 
ATOM   12619 O O    . GLY B 1 753  ? 139.459 178.453 126.720 1.00 24.27 ?  753  GLY B O    1 
ATOM   12620 N N    . LEU B 1 754  ? 140.827 179.040 128.422 1.00 26.25 ?  754  LEU B N    1 
ATOM   12621 C CA   . LEU B 1 754  ? 140.583 180.470 128.247 1.00 27.73 ?  754  LEU B CA   1 
ATOM   12622 C C    . LEU B 1 754  ? 141.109 180.971 126.907 1.00 32.42 ?  754  LEU B C    1 
ATOM   12623 O O    . LEU B 1 754  ? 140.601 181.965 126.375 1.00 32.53 ?  754  LEU B O    1 
ATOM   12624 C CB   . LEU B 1 754  ? 141.221 181.261 129.390 1.00 25.60 ?  754  LEU B CB   1 
ATOM   12625 C CG   . LEU B 1 754  ? 140.530 181.218 130.754 1.00 28.42 ?  754  LEU B CG   1 
ATOM   12626 C CD1  . LEU B 1 754  ? 141.193 182.187 131.721 1.00 26.91 ?  754  LEU B CD1  1 
ATOM   12627 C CD2  . LEU B 1 754  ? 139.047 181.526 130.616 1.00 27.80 ?  754  LEU B CD2  1 
ATOM   12628 N N    . GLY B 1 755  ? 142.117 180.303 126.349 1.00 26.49 ?  755  GLY B N    1 
ATOM   12629 C CA   . GLY B 1 755  ? 142.638 180.621 125.038 1.00 24.41 ?  755  GLY B CA   1 
ATOM   12630 C C    . GLY B 1 755  ? 141.857 180.056 123.875 1.00 22.96 ?  755  GLY B C    1 
ATOM   12631 O O    . GLY B 1 755  ? 142.246 180.262 122.723 1.00 21.80 ?  755  GLY B O    1 
ATOM   12632 N N    . ARG B 1 756  ? 140.760 179.345 124.139 1.00 20.44 ?  756  ARG B N    1 
ATOM   12633 C CA   . ARG B 1 756  ? 139.913 178.789 123.090 1.00 24.51 ?  756  ARG B CA   1 
ATOM   12634 C C    . ARG B 1 756  ? 138.910 179.797 122.539 1.00 28.15 ?  756  ARG B C    1 
ATOM   12635 O O    . ARG B 1 756  ? 137.962 179.389 121.859 1.00 27.40 ?  756  ARG B O    1 
ATOM   12636 C CB   . ARG B 1 756  ? 139.172 177.553 123.608 1.00 23.12 ?  756  ARG B CB   1 
ATOM   12637 N N    . HIS B 1 757  ? 139.091 181.085 122.844 1.00 32.15 ?  757  HIS B N    1 
ATOM   12638 C CA   . HIS B 1 757  ? 138.326 182.200 122.283 1.00 33.06 ?  757  HIS B CA   1 
ATOM   12639 C C    . HIS B 1 757  ? 136.841 182.149 122.640 1.00 31.56 ?  757  HIS B C    1 
ATOM   12640 O O    . HIS B 1 757  ? 136.030 182.809 121.980 1.00 28.87 ?  757  HIS B O    1 
ATOM   12641 C CB   . HIS B 1 757  ? 138.501 182.286 120.761 1.00 30.10 ?  757  HIS B CB   1 
ATOM   12642 C CG   . HIS B 1 757  ? 139.895 182.001 120.296 1.00 32.23 ?  757  HIS B CG   1 
ATOM   12643 N ND1  . HIS B 1 757  ? 140.950 182.856 120.533 1.00 34.06 ?  757  HIS B ND1  1 
ATOM   12644 C CD2  . HIS B 1 757  ? 140.410 180.950 119.613 1.00 29.42 ?  757  HIS B CD2  1 
ATOM   12645 C CE1  . HIS B 1 757  ? 142.053 182.347 120.013 1.00 35.70 ?  757  HIS B CE1  1 
ATOM   12646 N NE2  . HIS B 1 757  ? 141.752 181.191 119.450 1.00 35.08 ?  757  HIS B NE2  1 
ATOM   12647 N N    . TYR B 1 758  ? 136.483 181.387 123.681 1.00 30.88 ?  758  TYR B N    1 
ATOM   12648 C CA   . TYR B 1 758  ? 135.114 181.316 124.209 1.00 29.27 ?  758  TYR B CA   1 
ATOM   12649 C C    . TYR B 1 758  ? 134.108 180.923 123.127 1.00 31.23 ?  758  TYR B C    1 
ATOM   12650 O O    . TYR B 1 758  ? 133.008 181.475 123.045 1.00 30.09 ?  758  TYR B O    1 
ATOM   12651 C CB   . TYR B 1 758  ? 134.716 182.638 124.873 1.00 28.68 ?  758  TYR B CB   1 
ATOM   12652 C CG   . TYR B 1 758  ? 133.604 182.520 125.891 1.00 30.59 ?  758  TYR B CG   1 
ATOM   12653 C CD1  . TYR B 1 758  ? 133.705 181.640 126.961 1.00 29.73 ?  758  TYR B CD1  1 
ATOM   12654 C CD2  . TYR B 1 758  ? 132.456 183.295 125.786 1.00 30.99 ?  758  TYR B CD2  1 
ATOM   12655 C CE1  . TYR B 1 758  ? 132.693 181.533 127.896 1.00 31.11 ?  758  TYR B CE1  1 
ATOM   12656 C CE2  . TYR B 1 758  ? 131.438 183.195 126.715 1.00 30.74 ?  758  TYR B CE2  1 
ATOM   12657 C CZ   . TYR B 1 758  ? 131.562 182.313 127.767 1.00 31.94 ?  758  TYR B CZ   1 
ATOM   12658 O OH   . TYR B 1 758  ? 130.552 182.211 128.694 1.00 29.18 ?  758  TYR B OH   1 
ATOM   12659 N N    . ILE B 1 759  ? 134.494 179.964 122.282 1.00 29.59 ?  759  ILE B N    1 
ATOM   12660 C CA   . ILE B 1 759  ? 133.644 179.575 121.160 1.00 30.87 ?  759  ILE B CA   1 
ATOM   12661 C C    . ILE B 1 759  ? 132.402 178.827 121.629 1.00 29.94 ?  759  ILE B C    1 
ATOM   12662 O O    . ILE B 1 759  ? 131.312 179.018 121.078 1.00 25.37 ?  759  ILE B O    1 
ATOM   12663 C CB   . ILE B 1 759  ? 134.435 178.707 120.162 1.00 30.00 ?  759  ILE B CB   1 
ATOM   12664 N N    . VAL B 1 760  ? 132.545 177.970 122.641 1.00 26.38 ?  760  VAL B N    1 
ATOM   12665 C CA   . VAL B 1 760  ? 131.418 177.179 123.118 1.00 24.78 ?  760  VAL B CA   1 
ATOM   12666 C C    . VAL B 1 760  ? 130.457 178.065 123.898 1.00 25.50 ?  760  VAL B C    1 
ATOM   12667 O O    . VAL B 1 760  ? 130.873 178.928 124.684 1.00 22.76 ?  760  VAL B O    1 
ATOM   12668 C CB   . VAL B 1 760  ? 131.912 176.002 123.976 1.00 24.74 ?  760  VAL B CB   1 
ATOM   12669 C CG1  . VAL B 1 760  ? 130.853 174.917 124.043 1.00 22.42 ?  760  VAL B CG1  1 
ATOM   12670 C CG2  . VAL B 1 760  ? 133.216 175.450 123.419 1.00 24.72 ?  760  VAL B CG2  1 
ATOM   12671 N N    . SER B 1 761  ? 129.159 177.859 123.680 1.00 26.14 ?  761  SER B N    1 
ATOM   12672 C CA   . SER B 1 761  ? 128.118 178.650 124.326 1.00 23.19 ?  761  SER B CA   1 
ATOM   12673 C C    . SER B 1 761  ? 127.549 177.975 125.568 1.00 22.81 ?  761  SER B C    1 
ATOM   12674 O O    . SER B 1 761  ? 127.408 178.618 126.611 1.00 25.71 ?  761  SER B O    1 
ATOM   12675 C CB   . SER B 1 761  ? 126.988 178.942 123.331 1.00 23.29 ?  761  SER B CB   1 
ATOM   12676 O OG   . SER B 1 761  ? 127.441 179.762 122.268 1.00 26.00 ?  761  SER B OG   1 
ATOM   12677 N N    . HIS B 1 762  ? 127.220 176.688 125.478 1.00 28.34 ?  762  HIS B N    1 
ATOM   12678 C CA   . HIS B 1 762  ? 126.598 175.970 126.584 1.00 32.99 ?  762  HIS B CA   1 
ATOM   12679 C C    . HIS B 1 762  ? 127.626 175.300 127.491 1.00 33.03 ?  762  HIS B C    1 
ATOM   12680 O O    . HIS B 1 762  ? 127.625 175.521 128.708 1.00 31.16 ?  762  HIS B O    1 
ATOM   12681 C CB   . HIS B 1 762  ? 125.617 174.928 126.035 1.00 31.46 ?  762  HIS B CB   1 
ATOM   12682 C CG   . HIS B 1 762  ? 124.754 174.294 127.082 1.00 32.79 ?  762  HIS B CG   1 
ATOM   12683 N ND1  . HIS B 1 762  ? 125.190 173.256 127.877 1.00 31.82 ?  762  HIS B ND1  1 
ATOM   12684 C CD2  . HIS B 1 762  ? 123.479 174.549 127.461 1.00 31.62 ?  762  HIS B CD2  1 
ATOM   12685 C CE1  . HIS B 1 762  ? 124.222 172.899 128.701 1.00 31.66 ?  762  HIS B CE1  1 
ATOM   12686 N NE2  . HIS B 1 762  ? 123.173 173.668 128.470 1.00 32.77 ?  762  HIS B NE2  1 
ATOM   12687 N N    . TRP B 1 763  ? 128.504 174.479 126.909 1.00 29.38 ?  763  TRP B N    1 
ATOM   12688 C CA   . TRP B 1 763  ? 129.432 173.692 127.713 1.00 30.14 ?  763  TRP B CA   1 
ATOM   12689 C C    . TRP B 1 763  ? 130.481 174.572 128.381 1.00 28.45 ?  763  TRP B C    1 
ATOM   12690 O O    . TRP B 1 763  ? 130.889 174.299 129.515 1.00 25.77 ?  763  TRP B O    1 
ATOM   12691 C CB   . TRP B 1 763  ? 130.086 172.615 126.848 1.00 29.84 ?  763  TRP B CB   1 
ATOM   12692 C CG   . TRP B 1 763  ? 129.111 171.907 125.948 1.00 31.27 ?  763  TRP B CG   1 
ATOM   12693 C CD1  . TRP B 1 763  ? 129.126 171.881 124.584 1.00 27.80 ?  763  TRP B CD1  1 
ATOM   12694 C CD2  . TRP B 1 763  ? 127.973 171.129 126.350 1.00 30.59 ?  763  TRP B CD2  1 
ATOM   12695 N NE1  . TRP B 1 763  ? 128.074 171.136 124.112 1.00 27.58 ?  763  TRP B NE1  1 
ATOM   12696 C CE2  . TRP B 1 763  ? 127.351 170.664 125.175 1.00 26.70 ?  763  TRP B CE2  1 
ATOM   12697 C CE3  . TRP B 1 763  ? 127.424 170.780 127.588 1.00 28.28 ?  763  TRP B CE3  1 
ATOM   12698 C CZ2  . TRP B 1 763  ? 126.207 169.868 125.201 1.00 24.64 ?  763  TRP B CZ2  1 
ATOM   12699 C CZ3  . TRP B 1 763  ? 126.287 169.992 127.611 1.00 26.94 ?  763  TRP B CZ3  1 
ATOM   12700 C CH2  . TRP B 1 763  ? 125.692 169.544 126.426 1.00 25.29 ?  763  TRP B CH2  1 
ATOM   12701 N N    . ASN B 1 764  ? 130.925 175.635 127.703 1.00 24.12 ?  764  ASN B N    1 
ATOM   12702 C CA   . ASN B 1 764  ? 131.870 176.560 128.324 1.00 26.75 ?  764  ASN B CA   1 
ATOM   12703 C C    . ASN B 1 764  ? 131.244 177.280 129.513 1.00 24.80 ?  764  ASN B C    1 
ATOM   12704 O O    . ASN B 1 764  ? 131.885 177.426 130.562 1.00 24.45 ?  764  ASN B O    1 
ATOM   12705 C CB   . ASN B 1 764  ? 132.379 177.568 127.296 1.00 28.32 ?  764  ASN B CB   1 
ATOM   12706 C CG   . ASN B 1 764  ? 133.782 177.251 126.815 1.00 26.55 ?  764  ASN B CG   1 
ATOM   12707 O OD1  . ASN B 1 764  ? 134.324 176.185 127.107 1.00 25.17 ?  764  ASN B OD1  1 
ATOM   12708 N ND2  . ASN B 1 764  ? 134.378 178.179 126.076 1.00 22.88 ?  764  ASN B ND2  1 
ATOM   12709 N N    . LYS B 1 765  ? 129.993 177.729 129.372 1.00 22.59 ?  765  LYS B N    1 
ATOM   12710 C CA   . LYS B 1 765  ? 129.301 178.373 130.486 1.00 28.83 ?  765  LYS B CA   1 
ATOM   12711 C C    . LYS B 1 765  ? 129.111 177.409 131.650 1.00 29.46 ?  765  LYS B C    1 
ATOM   12712 O O    . LYS B 1 765  ? 129.308 177.781 132.814 1.00 28.71 ?  765  LYS B O    1 
ATOM   12713 C CB   . LYS B 1 765  ? 127.947 178.914 130.026 1.00 25.93 ?  765  LYS B CB   1 
ATOM   12714 C CG   . LYS B 1 765  ? 127.993 180.288 129.382 1.00 24.73 ?  765  LYS B CG   1 
ATOM   12715 C CD   . LYS B 1 765  ? 126.602 180.730 128.949 1.00 24.41 ?  765  LYS B CD   1 
ATOM   12716 C CE   . LYS B 1 765  ? 126.663 181.665 127.752 1.00 25.78 ?  765  LYS B CE   1 
ATOM   12717 N NZ   . LYS B 1 765  ? 125.306 181.969 127.216 1.00 24.15 ?  765  LYS B NZ   1 
ATOM   12718 N N    . PHE B 1 766  ? 128.728 176.165 131.353 1.00 26.87 ?  766  PHE B N    1 
ATOM   12719 C CA   . PHE B 1 766  ? 128.509 175.189 132.416 1.00 26.25 ?  766  PHE B CA   1 
ATOM   12720 C C    . PHE B 1 766  ? 129.816 174.824 133.114 1.00 29.30 ?  766  PHE B C    1 
ATOM   12721 O O    . PHE B 1 766  ? 129.846 174.666 134.340 1.00 28.95 ?  766  PHE B O    1 
ATOM   12722 C CB   . PHE B 1 766  ? 127.818 173.949 131.851 1.00 28.58 ?  766  PHE B CB   1 
ATOM   12723 C CG   . PHE B 1 766  ? 126.313 174.032 131.875 1.00 29.24 ?  766  PHE B CG   1 
ATOM   12724 C CD1  . PHE B 1 766  ? 125.669 175.246 131.698 1.00 27.31 ?  766  PHE B CD1  1 
ATOM   12725 C CD2  . PHE B 1 766  ? 125.545 172.896 132.068 1.00 27.62 ?  766  PHE B CD2  1 
ATOM   12726 C CE1  . PHE B 1 766  ? 124.288 175.326 131.719 1.00 27.82 ?  766  PHE B CE1  1 
ATOM   12727 C CE2  . PHE B 1 766  ? 124.164 172.969 132.092 1.00 27.95 ?  766  PHE B CE2  1 
ATOM   12728 C CZ   . PHE B 1 766  ? 123.535 174.186 131.915 1.00 28.32 ?  766  PHE B CZ   1 
ATOM   12729 N N    . ASP B 1 767  ? 130.911 174.709 132.357 1.00 29.33 ?  767  ASP B N    1 
ATOM   12730 C CA   . ASP B 1 767  ? 132.210 174.432 132.963 1.00 29.82 ?  767  ASP B CA   1 
ATOM   12731 C C    . ASP B 1 767  ? 132.694 175.608 133.803 1.00 28.81 ?  767  ASP B C    1 
ATOM   12732 O O    . ASP B 1 767  ? 133.309 175.411 134.858 1.00 27.85 ?  767  ASP B O    1 
ATOM   12733 C CB   . ASP B 1 767  ? 133.231 174.087 131.879 1.00 28.19 ?  767  ASP B CB   1 
ATOM   12734 C CG   . ASP B 1 767  ? 134.183 172.984 132.303 1.00 31.21 ?  767  ASP B CG   1 
ATOM   12735 O OD1  . ASP B 1 767  ? 134.687 173.037 133.444 1.00 31.20 ?  767  ASP B OD1  1 
ATOM   12736 O OD2  . ASP B 1 767  ? 134.426 172.064 131.494 1.00 31.59 ?  767  ASP B OD2  1 
ATOM   12737 N N    . ALA B 1 768  ? 132.432 176.839 133.351 1.00 23.50 ?  768  ALA B N    1 
ATOM   12738 C CA   . ALA B 1 768  ? 132.790 178.011 134.146 1.00 25.41 ?  768  ALA B CA   1 
ATOM   12739 C C    . ALA B 1 768  ? 131.997 178.059 135.446 1.00 29.76 ?  768  ALA B C    1 
ATOM   12740 O O    . ALA B 1 768  ? 132.547 178.385 136.505 1.00 29.57 ?  768  ALA B O    1 
ATOM   12741 C CB   . ALA B 1 768  ? 132.569 179.285 133.332 1.00 23.35 ?  768  ALA B CB   1 
ATOM   12742 N N    . PHE B 1 769  ? 130.703 177.733 135.385 1.00 27.80 ?  769  PHE B N    1 
ATOM   12743 C CA   . PHE B 1 769  ? 129.894 177.664 136.599 1.00 27.53 ?  769  PHE B CA   1 
ATOM   12744 C C    . PHE B 1 769  ? 130.392 176.564 137.532 1.00 26.15 ?  769  PHE B C    1 
ATOM   12745 O O    . PHE B 1 769  ? 130.417 176.740 138.757 1.00 22.59 ?  769  PHE B O    1 
ATOM   12746 C CB   . PHE B 1 769  ? 128.425 177.443 136.233 1.00 27.18 ?  769  PHE B CB   1 
ATOM   12747 C CG   . PHE B 1 769  ? 127.548 177.102 137.404 1.00 30.83 ?  769  PHE B CG   1 
ATOM   12748 C CD1  . PHE B 1 769  ? 127.170 178.079 138.310 1.00 29.33 ?  769  PHE B CD1  1 
ATOM   12749 C CD2  . PHE B 1 769  ? 127.088 175.807 137.591 1.00 28.75 ?  769  PHE B CD2  1 
ATOM   12750 C CE1  . PHE B 1 769  ? 126.359 177.771 139.387 1.00 29.57 ?  769  PHE B CE1  1 
ATOM   12751 C CE2  . PHE B 1 769  ? 126.277 175.492 138.666 1.00 26.62 ?  769  PHE B CE2  1 
ATOM   12752 C CZ   . PHE B 1 769  ? 125.912 176.476 139.564 1.00 27.01 ?  769  PHE B CZ   1 
ATOM   12753 N N    . ILE B 1 770  ? 130.798 175.426 136.963 1.00 23.82 ?  770  ILE B N    1 
ATOM   12754 C CA   . ILE B 1 770  ? 131.343 174.328 137.757 1.00 26.46 ?  770  ILE B CA   1 
ATOM   12755 C C    . ILE B 1 770  ? 132.624 174.762 138.460 1.00 27.33 ?  770  ILE B C    1 
ATOM   12756 O O    . ILE B 1 770  ? 132.827 174.474 139.645 1.00 25.37 ?  770  ILE B O    1 
ATOM   12757 C CB   . ILE B 1 770  ? 131.565 173.093 136.859 1.00 27.15 ?  770  ILE B CB   1 
ATOM   12758 C CG1  . ILE B 1 770  ? 130.285 172.258 136.777 1.00 27.04 ?  770  ILE B CG1  1 
ATOM   12759 C CG2  . ILE B 1 770  ? 132.728 172.240 137.354 1.00 27.19 ?  770  ILE B CG2  1 
ATOM   12760 C CD1  . ILE B 1 770  ? 130.397 171.062 135.856 1.00 27.40 ?  770  ILE B CD1  1 
ATOM   12761 N N    . LEU B 1 771  ? 133.501 175.472 137.744 1.00 24.42 ?  771  LEU B N    1 
ATOM   12762 C CA   . LEU B 1 771  ? 134.739 175.959 138.346 1.00 25.50 ?  771  LEU B CA   1 
ATOM   12763 C C    . LEU B 1 771  ? 134.464 176.996 139.429 1.00 25.88 ?  771  LEU B C    1 
ATOM   12764 O O    . LEU B 1 771  ? 135.150 177.022 140.458 1.00 24.03 ?  771  LEU B O    1 
ATOM   12765 C CB   . LEU B 1 771  ? 135.654 176.542 137.271 1.00 25.04 ?  771  LEU B CB   1 
ATOM   12766 C CG   . LEU B 1 771  ? 137.146 176.314 137.517 1.00 28.16 ?  771  LEU B CG   1 
ATOM   12767 C CD1  . LEU B 1 771  ? 137.530 174.900 137.119 1.00 25.41 ?  771  LEU B CD1  1 
ATOM   12768 C CD2  . LEU B 1 771  ? 137.986 177.341 136.775 1.00 25.36 ?  771  LEU B CD2  1 
ATOM   12769 N N    . VAL B 1 772  ? 133.473 177.865 139.208 1.00 24.74 ?  772  VAL B N    1 
ATOM   12770 C CA   . VAL B 1 772  ? 133.108 178.864 140.210 1.00 26.64 ?  772  VAL B CA   1 
ATOM   12771 C C    . VAL B 1 772  ? 132.605 178.187 141.479 1.00 25.75 ?  772  VAL B C    1 
ATOM   12772 O O    . VAL B 1 772  ? 132.976 178.572 142.596 1.00 23.13 ?  772  VAL B O    1 
ATOM   12773 C CB   . VAL B 1 772  ? 132.067 179.841 139.627 1.00 25.34 ?  772  VAL B CB   1 
ATOM   12774 C CG1  . VAL B 1 772  ? 131.304 180.559 140.734 1.00 23.08 ?  772  VAL B CG1  1 
ATOM   12775 C CG2  . VAL B 1 772  ? 132.743 180.847 138.708 1.00 23.65 ?  772  VAL B CG2  1 
ATOM   12776 N N    . VAL B 1 773  ? 131.766 177.159 141.328 1.00 22.42 ?  773  VAL B N    1 
ATOM   12777 C CA   . VAL B 1 773  ? 131.269 176.422 142.488 1.00 20.51 ?  773  VAL B CA   1 
ATOM   12778 C C    . VAL B 1 773  ? 132.409 175.690 143.193 1.00 22.75 ?  773  VAL B C    1 
ATOM   12779 O O    . VAL B 1 773  ? 132.506 175.708 144.427 1.00 24.53 ?  773  VAL B O    1 
ATOM   12780 C CB   . VAL B 1 773  ? 130.146 175.458 142.060 1.00 20.42 ?  773  VAL B CB   1 
ATOM   12781 C CG1  . VAL B 1 773  ? 129.827 174.466 143.169 1.00 19.45 ?  773  VAL B CG1  1 
ATOM   12782 C CG2  . VAL B 1 773  ? 128.902 176.240 141.670 1.00 21.68 ?  773  VAL B CG2  1 
ATOM   12783 N N    . ALA B 1 774  ? 133.299 175.055 142.425 1.00 21.74 ?  774  ALA B N    1 
ATOM   12784 C CA   . ALA B 1 774  ? 134.360 174.247 143.018 1.00 25.80 ?  774  ALA B CA   1 
ATOM   12785 C C    . ALA B 1 774  ? 135.423 175.100 143.700 1.00 25.18 ?  774  ALA B C    1 
ATOM   12786 O O    . ALA B 1 774  ? 136.073 174.634 144.643 1.00 20.04 ?  774  ALA B O    1 
ATOM   12787 C CB   . ALA B 1 774  ? 135.000 173.362 141.950 1.00 23.64 ?  774  ALA B CB   1 
ATOM   12788 N N    . LEU B 1 775  ? 135.621 176.338 143.241 1.00 27.54 ?  775  LEU B N    1 
ATOM   12789 C CA   . LEU B 1 775  ? 136.625 177.201 143.855 1.00 27.38 ?  775  LEU B CA   1 
ATOM   12790 C C    . LEU B 1 775  ? 136.208 177.691 145.236 1.00 25.84 ?  775  LEU B C    1 
ATOM   12791 O O    . LEU B 1 775  ? 137.063 178.154 145.998 1.00 21.94 ?  775  LEU B O    1 
ATOM   12792 C CB   . LEU B 1 775  ? 136.922 178.394 142.946 1.00 24.00 ?  775  LEU B CB   1 
ATOM   12793 C CG   . LEU B 1 775  ? 138.259 178.360 142.202 1.00 24.76 ?  775  LEU B CG   1 
ATOM   12794 C CD1  . LEU B 1 775  ? 139.418 178.532 143.173 1.00 20.71 ?  775  LEU B CD1  1 
ATOM   12795 C CD2  . LEU B 1 775  ? 138.409 177.071 141.408 1.00 25.71 ?  775  LEU B CD2  1 
ATOM   12796 N N    . VAL B 1 776  ? 134.926 177.602 145.574 1.00 24.78 ?  776  VAL B N    1 
ATOM   12797 C CA   . VAL B 1 776  ? 134.449 178.021 146.885 1.00 24.67 ?  776  VAL B CA   1 
ATOM   12798 C C    . VAL B 1 776  ? 134.396 176.828 147.832 1.00 25.67 ?  776  VAL B C    1 
ATOM   12799 O O    . VAL B 1 776  ? 134.660 175.694 147.433 1.00 22.36 ?  776  VAL B O    1 
ATOM   12800 C CB   . VAL B 1 776  ? 133.071 178.699 146.786 1.00 23.15 ?  776  VAL B CB   1 
ATOM   12801 C CG1  . VAL B 1 776  ? 132.482 178.910 148.172 1.00 19.23 ?  776  VAL B CG1  1 
ATOM   12802 C CG2  . VAL B 1 776  ? 133.183 180.020 146.040 1.00 23.47 ?  776  VAL B CG2  1 
ATOM   12803 N N    . LYS B 1 797  ? 122.897 176.691 158.356 1.00 23.86 ?  797  LYS B N    1 
ATOM   12804 C CA   . LYS B 1 797  ? 123.366 175.360 157.987 1.00 29.24 ?  797  LYS B CA   1 
ATOM   12805 C C    . LYS B 1 797  ? 123.661 175.275 156.493 1.00 29.73 ?  797  LYS B C    1 
ATOM   12806 O O    . LYS B 1 797  ? 123.311 174.293 155.839 1.00 31.66 ?  797  LYS B O    1 
ATOM   12807 C CB   . LYS B 1 797  ? 122.335 174.300 158.379 1.00 30.57 ?  797  LYS B CB   1 
ATOM   12808 C CG   . LYS B 1 797  ? 121.941 174.322 159.847 1.00 31.30 ?  797  LYS B CG   1 
ATOM   12809 C CD   . LYS B 1 797  ? 120.831 173.323 160.133 1.00 29.01 ?  797  LYS B CD   1 
ATOM   12810 C CE   . LYS B 1 797  ? 120.524 173.246 161.620 1.00 28.35 ?  797  LYS B CE   1 
ATOM   12811 N NZ   . LYS B 1 797  ? 119.538 172.173 161.926 1.00 27.11 ?  797  LYS B NZ   1 
ATOM   12812 N N    . VAL B 1 798  ? 124.310 176.312 155.956 1.00 27.56 ?  798  VAL B N    1 
ATOM   12813 C CA   . VAL B 1 798  ? 124.646 176.332 154.533 1.00 28.01 ?  798  VAL B CA   1 
ATOM   12814 C C    . VAL B 1 798  ? 125.836 175.448 154.196 1.00 28.95 ?  798  VAL B C    1 
ATOM   12815 O O    . VAL B 1 798  ? 126.057 175.151 153.015 1.00 22.23 ?  798  VAL B O    1 
ATOM   12816 C CB   . VAL B 1 798  ? 124.915 177.772 154.056 1.00 26.27 ?  798  VAL B CB   1 
ATOM   12817 C CG1  . VAL B 1 798  ? 123.843 178.713 154.586 1.00 24.20 ?  798  VAL B CG1  1 
ATOM   12818 C CG2  . VAL B 1 798  ? 126.298 178.239 154.489 1.00 23.12 ?  798  VAL B CG2  1 
ATOM   12819 N N    . VAL B 1 799  ? 126.605 175.014 155.198 1.00 29.20 ?  799  VAL B N    1 
ATOM   12820 C CA   . VAL B 1 799  ? 127.735 174.127 154.939 1.00 27.66 ?  799  VAL B CA   1 
ATOM   12821 C C    . VAL B 1 799  ? 127.246 172.756 154.491 1.00 25.64 ?  799  VAL B C    1 
ATOM   12822 O O    . VAL B 1 799  ? 127.838 172.130 153.604 1.00 22.60 ?  799  VAL B O    1 
ATOM   12823 C CB   . VAL B 1 799  ? 128.636 174.030 156.183 1.00 25.08 ?  799  VAL B CB   1 
ATOM   12824 C CG1  . VAL B 1 799  ? 130.018 173.525 155.798 1.00 26.01 ?  799  VAL B CG1  1 
ATOM   12825 C CG2  . VAL B 1 799  ? 128.730 175.381 156.876 1.00 20.95 ?  799  VAL B CG2  1 
ATOM   12826 N N    . LYS B 1 800  ? 126.158 172.270 155.094 1.00 26.87 ?  800  LYS B N    1 
ATOM   12827 C CA   . LYS B 1 800  ? 125.586 170.992 154.681 1.00 30.41 ?  800  LYS B CA   1 
ATOM   12828 C C    . LYS B 1 800  ? 125.055 171.059 153.254 1.00 29.96 ?  800  LYS B C    1 
ATOM   12829 O O    . LYS B 1 800  ? 125.165 170.087 152.498 1.00 27.31 ?  800  LYS B O    1 
ATOM   12830 C CB   . LYS B 1 800  ? 124.481 170.577 155.652 1.00 29.27 ?  800  LYS B CB   1 
ATOM   12831 C CG   . LYS B 1 800  ? 124.899 170.618 157.114 1.00 28.96 ?  800  LYS B CG   1 
ATOM   12832 C CD   . LYS B 1 800  ? 124.433 169.379 157.861 1.00 28.34 ?  800  LYS B CD   1 
ATOM   12833 C CE   . LYS B 1 800  ? 122.926 169.385 158.057 1.00 26.96 ?  800  LYS B CE   1 
ATOM   12834 N NZ   . LYS B 1 800  ? 122.499 170.414 159.045 1.00 25.97 ?  800  LYS B NZ   1 
ATOM   12835 N N    . LEU B 1 801  ? 124.466 172.196 152.872 1.00 26.64 ?  801  LEU B N    1 
ATOM   12836 C CA   . LEU B 1 801  ? 124.018 172.374 151.494 1.00 28.84 ?  801  LEU B CA   1 
ATOM   12837 C C    . LEU B 1 801  ? 125.198 172.446 150.531 1.00 27.37 ?  801  LEU B C    1 
ATOM   12838 O O    . LEU B 1 801  ? 125.151 171.867 149.440 1.00 26.65 ?  801  LEU B O    1 
ATOM   12839 C CB   . LEU B 1 801  ? 123.154 173.629 151.381 1.00 28.92 ?  801  LEU B CB   1 
ATOM   12840 C CG   . LEU B 1 801  ? 121.644 173.427 151.521 1.00 27.17 ?  801  LEU B CG   1 
ATOM   12841 C CD1  . LEU B 1 801  ? 121.239 173.391 152.987 1.00 24.00 ?  801  LEU B CD1  1 
ATOM   12842 C CD2  . LEU B 1 801  ? 120.885 174.516 150.779 1.00 24.32 ?  801  LEU B CD2  1 
ATOM   12843 N N    . PHE B 1 802  ? 126.267 173.149 150.918 1.00 26.11 ?  802  PHE B N    1 
ATOM   12844 C CA   . PHE B 1 802  ? 127.445 173.250 150.062 1.00 27.29 ?  802  PHE B CA   1 
ATOM   12845 C C    . PHE B 1 802  ? 128.211 171.937 149.967 1.00 26.69 ?  802  PHE B C    1 
ATOM   12846 O O    . PHE B 1 802  ? 128.993 171.759 149.027 1.00 24.74 ?  802  PHE B O    1 
ATOM   12847 C CB   . PHE B 1 802  ? 128.371 174.357 150.566 1.00 27.49 ?  802  PHE B CB   1 
ATOM   12848 C CG   . PHE B 1 802  ? 128.222 175.656 149.826 1.00 29.47 ?  802  PHE B CG   1 
ATOM   12849 C CD1  . PHE B 1 802  ? 128.684 175.784 148.526 1.00 28.06 ?  802  PHE B CD1  1 
ATOM   12850 C CD2  . PHE B 1 802  ? 127.623 176.750 150.430 1.00 25.84 ?  802  PHE B CD2  1 
ATOM   12851 C CE1  . PHE B 1 802  ? 128.549 176.977 147.840 1.00 27.85 ?  802  PHE B CE1  1 
ATOM   12852 C CE2  . PHE B 1 802  ? 127.485 177.947 149.750 1.00 26.97 ?  802  PHE B CE2  1 
ATOM   12853 C CZ   . PHE B 1 802  ? 127.949 178.060 148.454 1.00 26.34 ?  802  PHE B CZ   1 
ATOM   12854 N N    . ARG B 1 803  ? 128.019 171.028 150.927 1.00 27.91 ?  803  ARG B N    1 
ATOM   12855 C CA   . ARG B 1 803  ? 128.639 169.709 150.838 1.00 30.13 ?  803  ARG B CA   1 
ATOM   12856 C C    . ARG B 1 803  ? 128.131 168.927 149.632 1.00 29.26 ?  803  ARG B C    1 
ATOM   12857 O O    . ARG B 1 803  ? 128.874 168.127 149.053 1.00 27.31 ?  803  ARG B O    1 
ATOM   12858 C CB   . ARG B 1 803  ? 128.388 168.922 152.125 1.00 26.88 ?  803  ARG B CB   1 
ATOM   12859 C CG   . ARG B 1 803  ? 129.348 169.254 153.256 1.00 27.01 ?  803  ARG B CG   1 
ATOM   12860 C CD   . ARG B 1 803  ? 129.099 168.377 154.475 1.00 29.88 ?  803  ARG B CD   1 
ATOM   12861 N NE   . ARG B 1 803  ? 127.681 168.104 154.673 1.00 26.13 ?  803  ARG B NE   1 
ATOM   12862 C CZ   . ARG B 1 803  ? 127.191 167.347 155.645 1.00 28.22 ?  803  ARG B CZ   1 
ATOM   12863 N NH1  . ARG B 1 803  ? 127.981 166.774 156.539 1.00 26.77 ?  803  ARG B NH1  1 
ATOM   12864 N NH2  . ARG B 1 803  ? 125.877 167.160 155.723 1.00 27.40 ?  803  ARG B NH2  1 
ATOM   12865 N N    . LEU B 1 804  ? 126.875 169.142 149.240 1.00 21.46 ?  804  LEU B N    1 
ATOM   12866 C CA   . LEU B 1 804  ? 126.305 168.502 148.063 1.00 20.11 ?  804  LEU B CA   1 
ATOM   12867 C C    . LEU B 1 804  ? 126.219 169.432 146.859 1.00 22.17 ?  804  LEU B C    1 
ATOM   12868 O O    . LEU B 1 804  ? 126.006 168.949 145.741 1.00 19.33 ?  804  LEU B O    1 
ATOM   12869 C CB   . LEU B 1 804  ? 124.908 167.954 148.380 1.00 18.98 ?  804  LEU B CB   1 
ATOM   12870 C CG   . LEU B 1 804  ? 124.781 167.093 149.637 1.00 21.42 ?  804  LEU B CG   1 
ATOM   12871 C CD1  . LEU B 1 804  ? 123.320 166.813 149.951 1.00 22.02 ?  804  LEU B CD1  1 
ATOM   12872 C CD2  . LEU B 1 804  ? 125.553 165.794 149.473 1.00 20.15 ?  804  LEU B CD2  1 
ATOM   12873 N N    . LEU B 1 805  ? 126.367 170.745 147.059 1.00 25.54 ?  805  LEU B N    1 
ATOM   12874 C CA   . LEU B 1 805  ? 126.326 171.678 145.937 1.00 25.92 ?  805  LEU B CA   1 
ATOM   12875 C C    . LEU B 1 805  ? 127.525 171.493 145.016 1.00 26.91 ?  805  LEU B C    1 
ATOM   12876 O O    . LEU B 1 805  ? 127.399 171.611 143.792 1.00 26.75 ?  805  LEU B O    1 
ATOM   12877 C CB   . LEU B 1 805  ? 126.261 173.116 146.451 1.00 23.32 ?  805  LEU B CB   1 
ATOM   12878 C CG   . LEU B 1 805  ? 124.860 173.696 146.649 1.00 24.29 ?  805  LEU B CG   1 
ATOM   12879 C CD1  . LEU B 1 805  ? 124.935 175.077 147.281 1.00 23.52 ?  805  LEU B CD1  1 
ATOM   12880 C CD2  . LEU B 1 805  ? 124.108 173.745 145.327 1.00 24.34 ?  805  LEU B CD2  1 
ATOM   12881 N N    . ARG B 1 806  ? 128.697 171.202 145.585 1.00 27.43 ?  806  ARG B N    1 
ATOM   12882 C CA   . ARG B 1 806  ? 129.868 170.918 144.766 1.00 27.45 ?  806  ARG B CA   1 
ATOM   12883 C C    . ARG B 1 806  ? 129.760 169.577 144.049 1.00 28.17 ?  806  ARG B C    1 
ATOM   12884 O O    . ARG B 1 806  ? 130.536 169.322 143.122 1.00 29.17 ?  806  ARG B O    1 
ATOM   12885 C CB   . ARG B 1 806  ? 131.132 170.952 145.627 1.00 26.20 ?  806  ARG B CB   1 
ATOM   12886 C CG   . ARG B 1 806  ? 131.568 172.351 146.035 1.00 26.61 ?  806  ARG B CG   1 
ATOM   12887 C CD   . ARG B 1 806  ? 132.973 172.347 146.613 1.00 26.62 ?  806  ARG B CD   1 
ATOM   12888 N NE   . ARG B 1 806  ? 133.042 171.609 147.868 1.00 30.07 ?  806  ARG B NE   1 
ATOM   12889 C CZ   . ARG B 1 806  ? 132.764 172.125 149.058 1.00 27.17 ?  806  ARG B CZ   1 
ATOM   12890 N NH1  . ARG B 1 806  ? 132.389 173.386 149.194 1.00 22.28 ?  806  ARG B NH1  1 
ATOM   12891 N NH2  . ARG B 1 806  ? 132.865 171.355 150.138 1.00 25.75 ?  806  ARG B NH2  1 
ATOM   12892 N N    . GLY B 1 807  ? 128.822 168.719 144.457 1.00 24.86 ?  807  GLY B N    1 
ATOM   12893 C CA   . GLY B 1 807  ? 128.625 167.429 143.822 1.00 24.37 ?  807  GLY B CA   1 
ATOM   12894 C C    . GLY B 1 807  ? 127.874 167.468 142.514 1.00 25.68 ?  807  GLY B C    1 
ATOM   12895 O O    . GLY B 1 807  ? 127.811 166.451 141.816 1.00 25.21 ?  807  GLY B O    1 
ATOM   12896 N N    . LEU B 1 808  ? 127.303 168.620 142.163 1.00 24.21 ?  808  LEU B N    1 
ATOM   12897 C CA   . LEU B 1 808  ? 126.619 168.790 140.884 1.00 24.70 ?  808  LEU B CA   1 
ATOM   12898 C C    . LEU B 1 808  ? 127.689 169.110 139.839 1.00 26.58 ?  808  LEU B C    1 
ATOM   12899 O O    . LEU B 1 808  ? 127.960 170.261 139.492 1.00 29.10 ?  808  LEU B O    1 
ATOM   12900 C CB   . LEU B 1 808  ? 125.545 169.869 140.988 1.00 23.74 ?  808  LEU B CB   1 
ATOM   12901 C CG   . LEU B 1 808  ? 124.490 170.075 139.887 1.00 23.71 ?  808  LEU B CG   1 
ATOM   12902 C CD1  . LEU B 1 808  ? 123.234 170.676 140.499 1.00 22.67 ?  808  LEU B CD1  1 
ATOM   12903 C CD2  . LEU B 1 808  ? 124.947 170.946 138.724 1.00 23.68 ?  808  LEU B CD2  1 
ATOM   12904 N N    . ARG B 1 809  ? 128.362 168.048 139.391 1.00 25.03 ?  809  ARG B N    1 
ATOM   12905 C CA   . ARG B 1 809  ? 129.425 168.144 138.396 1.00 23.91 ?  809  ARG B CA   1 
ATOM   12906 C C    . ARG B 1 809  ? 129.218 167.128 137.281 1.00 24.54 ?  809  ARG B C    1 
ATOM   12907 O O    . ARG B 1 809  ? 130.184 166.622 136.704 1.00 22.59 ?  809  ARG B O    1 
ATOM   12908 C CB   . ARG B 1 809  ? 130.800 167.960 139.037 1.00 26.24 ?  809  ARG B CB   1 
ATOM   12909 C CG   . ARG B 1 809  ? 131.880 168.848 138.437 1.00 24.85 ?  809  ARG B CG   1 
ATOM   12910 C CD   . ARG B 1 809  ? 133.234 168.623 139.093 1.00 25.40 ?  809  ARG B CD   1 
ATOM   12911 N NE   . ARG B 1 809  ? 133.924 167.452 138.564 1.00 21.81 ?  809  ARG B NE   1 
ATOM   12912 C CZ   . ARG B 1 809  ? 135.162 167.107 138.888 1.00 24.79 ?  809  ARG B CZ   1 
ATOM   12913 N NH1  . ARG B 1 809  ? 135.879 167.824 139.738 1.00 26.71 ?  809  ARG B NH1  1 
ATOM   12914 N NH2  . ARG B 1 809  ? 135.693 166.012 138.351 1.00 24.32 ?  809  ARG B NH2  1 
ATOM   12915 N N    . MET B 1 810  ? 127.960 166.815 136.979 1.00 31.83 ?  810  MET B N    1 
ATOM   12916 C CA   . MET B 1 810  ? 127.599 165.893 135.914 1.00 32.56 ?  810  MET B CA   1 
ATOM   12917 C C    . MET B 1 810  ? 127.131 166.619 134.662 1.00 31.70 ?  810  MET B C    1 
ATOM   12918 O O    . MET B 1 810  ? 126.502 166.008 133.791 1.00 29.70 ?  810  MET B O    1 
ATOM   12919 C CB   . MET B 1 810  ? 126.529 164.919 136.405 1.00 28.72 ?  810  MET B CB   1 
ATOM   12920 C CG   . MET B 1 810  ? 127.035 163.953 137.458 1.00 29.10 ?  810  MET B CG   1 
ATOM   12921 S SD   . MET B 1 810  ? 125.699 162.897 138.050 1.00 41.37 ?  810  MET B SD   1 
ATOM   12922 C CE   . MET B 1 810  ? 125.452 161.832 136.638 1.00 28.01 ?  810  MET B CE   1 
ATOM   12923 N N    . LEU B 1 811  ? 127.420 167.916 134.562 1.00 27.69 ?  811  LEU B N    1 
ATOM   12924 C CA   . LEU B 1 811  ? 127.110 168.687 133.368 1.00 29.17 ?  811  LEU B CA   1 
ATOM   12925 C C    . LEU B 1 811  ? 128.039 168.365 132.206 1.00 29.90 ?  811  LEU B C    1 
ATOM   12926 O O    . LEU B 1 811  ? 127.787 168.826 131.088 1.00 26.92 ?  811  LEU B O    1 
ATOM   12927 C CB   . LEU B 1 811  ? 127.177 170.181 133.687 1.00 25.69 ?  811  LEU B CB   1 
ATOM   12928 C CG   . LEU B 1 811  ? 126.433 170.630 134.948 1.00 30.24 ?  811  LEU B CG   1 
ATOM   12929 C CD1  . LEU B 1 811  ? 126.803 172.059 135.319 1.00 30.88 ?  811  LEU B CD1  1 
ATOM   12930 C CD2  . LEU B 1 811  ? 124.930 170.492 134.761 1.00 27.22 ?  811  LEU B CD2  1 
ATOM   12931 N N    . ARG B 1 812  ? 129.105 167.599 132.440 1.00 30.86 ?  812  ARG B N    1 
ATOM   12932 C CA   . ARG B 1 812  ? 130.046 167.249 131.386 1.00 31.80 ?  812  ARG B CA   1 
ATOM   12933 C C    . ARG B 1 812  ? 129.739 165.908 130.732 1.00 33.47 ?  812  ARG B C    1 
ATOM   12934 O O    . ARG B 1 812  ? 130.258 165.633 129.645 1.00 34.74 ?  812  ARG B O    1 
ATOM   12935 C CB   . ARG B 1 812  ? 131.473 167.230 131.942 1.00 30.68 ?  812  ARG B CB   1 
ATOM   12936 C CG   . ARG B 1 812  ? 132.018 168.607 132.281 1.00 27.92 ?  812  ARG B CG   1 
ATOM   12937 C CD   . ARG B 1 812  ? 133.520 168.568 132.493 1.00 31.45 ?  812  ARG B CD   1 
ATOM   12938 N NE   . ARG B 1 812  ? 134.192 167.819 131.438 1.00 32.69 ?  812  ARG B NE   1 
ATOM   12939 C CZ   . ARG B 1 812  ? 134.615 168.347 130.298 1.00 32.17 ?  812  ARG B CZ   1 
ATOM   12940 N NH1  . ARG B 1 812  ? 134.454 169.633 130.031 1.00 31.32 ?  812  ARG B NH1  1 
ATOM   12941 N NH2  . ARG B 1 812  ? 135.212 167.566 129.403 1.00 30.30 ?  812  ARG B NH2  1 
ATOM   12942 N N    . LEU B 1 813  ? 128.918 165.068 131.368 1.00 26.01 ?  813  LEU B N    1 
ATOM   12943 C CA   . LEU B 1 813  ? 128.550 163.793 130.761 1.00 27.20 ?  813  LEU B CA   1 
ATOM   12944 C C    . LEU B 1 813  ? 127.547 163.985 129.629 1.00 29.50 ?  813  LEU B C    1 
ATOM   12945 O O    . LEU B 1 813  ? 127.593 163.266 128.623 1.00 30.77 ?  813  LEU B O    1 
ATOM   12946 C CB   . LEU B 1 813  ? 127.988 162.847 131.822 1.00 25.21 ?  813  LEU B CB   1 
ATOM   12947 C CG   . LEU B 1 813  ? 128.938 162.441 132.951 1.00 30.71 ?  813  LEU B CG   1 
ATOM   12948 C CD1  . LEU B 1 813  ? 128.200 161.632 134.006 1.00 31.04 ?  813  LEU B CD1  1 
ATOM   12949 C CD2  . LEU B 1 813  ? 130.121 161.659 132.401 1.00 25.15 ?  813  LEU B CD2  1 
ATOM   12950 N N    . THR B 1 814  ? 126.632 164.946 129.776 1.00 25.34 ?  814  THR B N    1 
ATOM   12951 C CA   . THR B 1 814  ? 125.635 165.188 128.739 1.00 26.54 ?  814  THR B CA   1 
ATOM   12952 C C    . THR B 1 814  ? 126.240 165.797 127.480 1.00 25.04 ?  814  THR B C    1 
ATOM   12953 O O    . THR B 1 814  ? 125.589 165.784 126.431 1.00 24.58 ?  814  THR B O    1 
ATOM   12954 C CB   . THR B 1 814  ? 124.523 166.094 129.271 1.00 24.97 ?  814  THR B CB   1 
ATOM   12955 O OG1  . THR B 1 814  ? 123.641 166.450 128.199 1.00 23.39 ?  814  THR B OG1  1 
ATOM   12956 C CG2  . THR B 1 814  ? 125.107 167.355 129.879 1.00 23.16 ?  814  THR B CG2  1 
ATOM   12957 N N    . LYS B 1 815  ? 127.459 166.335 127.559 1.00 21.44 ?  815  LYS B N    1 
ATOM   12958 C CA   . LYS B 1 815  ? 128.133 166.806 126.354 1.00 21.74 ?  815  LYS B CA   1 
ATOM   12959 C C    . LYS B 1 815  ? 128.551 165.638 125.470 1.00 22.35 ?  815  LYS B C    1 
ATOM   12960 O O    . LYS B 1 815  ? 128.447 165.714 124.240 1.00 23.21 ?  815  LYS B O    1 
ATOM   12961 C CB   . LYS B 1 815  ? 129.345 167.661 126.727 1.00 22.86 ?  815  LYS B CB   1 
ATOM   12962 C CG   . LYS B 1 815  ? 130.013 168.342 125.541 1.00 22.95 ?  815  LYS B CG   1 
ATOM   12963 C CD   . LYS B 1 815  ? 131.447 167.873 125.360 1.00 24.46 ?  815  LYS B CD   1 
ATOM   12964 C CE   . LYS B 1 815  ? 132.395 168.621 126.284 1.00 22.77 ?  815  LYS B CE   1 
ATOM   12965 N NZ   . LYS B 1 815  ? 133.819 168.283 126.011 1.00 22.35 ?  815  LYS B NZ   1 
ATOM   12966 N N    . ALA B 1 816  ? 129.020 164.550 126.076 1.00 21.88 ?  816  ALA B N    1 
ATOM   12967 C CA   . ALA B 1 816  ? 129.417 163.357 125.342 1.00 25.78 ?  816  ALA B CA   1 
ATOM   12968 C C    . ALA B 1 816  ? 128.294 162.337 125.207 1.00 22.98 ?  816  ALA B C    1 
ATOM   12969 O O    . ALA B 1 816  ? 128.485 161.314 124.543 1.00 19.22 ?  816  ALA B O    1 
ATOM   12970 C CB   . ALA B 1 816  ? 130.627 162.702 126.016 1.00 23.84 ?  816  ALA B CB   1 
ATOM   12971 N N    . LEU B 1 817  ? 127.135 162.582 125.822 1.00 21.05 ?  817  LEU B N    1 
ATOM   12972 C CA   . LEU B 1 817  ? 126.006 161.670 125.696 1.00 19.76 ?  817  LEU B CA   1 
ATOM   12973 C C    . LEU B 1 817  ? 125.129 161.969 124.486 1.00 21.67 ?  817  LEU B C    1 
ATOM   12974 O O    . LEU B 1 817  ? 124.394 161.081 124.038 1.00 25.65 ?  817  LEU B O    1 
ATOM   12975 C CB   . LEU B 1 817  ? 125.153 161.710 126.969 1.00 19.47 ?  817  LEU B CB   1 
ATOM   12976 C CG   . LEU B 1 817  ? 124.249 160.508 127.252 1.00 18.88 ?  817  LEU B CG   1 
ATOM   12977 C CD1  . LEU B 1 817  ? 125.077 159.313 127.699 1.00 20.02 ?  817  LEU B CD1  1 
ATOM   12978 C CD2  . LEU B 1 817  ? 123.197 160.856 128.293 1.00 18.78 ?  817  LEU B CD2  1 
ATOM   12979 N N    . ILE B 1 818  ? 125.185 163.196 123.956 1.00 18.38 ?  818  ILE B N    1 
ATOM   12980 C CA   . ILE B 1 818  ? 124.402 163.537 122.762 1.00 17.63 ?  818  ILE B CA   1 
ATOM   12981 C C    . ILE B 1 818  ? 124.770 162.682 121.547 1.00 19.84 ?  818  ILE B C    1 
ATOM   12982 O O    . ILE B 1 818  ? 123.852 162.221 120.848 1.00 19.80 ?  818  ILE B O    1 
ATOM   12983 C CB   . ILE B 1 818  ? 124.493 165.044 122.483 1.00 17.67 ?  818  ILE B CB   1 
ATOM   12984 C CG1  . ILE B 1 818  ? 123.906 165.851 123.645 1.00 18.92 ?  818  ILE B CG1  1 
ATOM   12985 C CG2  . ILE B 1 818  ? 123.784 165.407 121.186 1.00 17.75 ?  818  ILE B CG2  1 
ATOM   12986 C CD1  . ILE B 1 818  ? 122.544 165.376 124.102 1.00 18.29 ?  818  ILE B CD1  1 
ATOM   12987 N N    . PRO B 1 819  ? 126.057 162.447 121.224 1.00 17.15 ?  819  PRO B N    1 
ATOM   12988 C CA   . PRO B 1 819  ? 126.350 161.539 120.100 1.00 14.99 ?  819  PRO B CA   1 
ATOM   12989 C C    . PRO B 1 819  ? 125.803 160.133 120.277 1.00 16.27 ?  819  PRO B C    1 
ATOM   12990 O O    . PRO B 1 819  ? 125.401 159.516 119.286 1.00 25.60 ?  819  PRO B O    1 
ATOM   12991 C CB   . PRO B 1 819  ? 127.883 161.538 120.043 1.00 17.13 ?  819  PRO B CB   1 
ATOM   12992 C CG   . PRO B 1 819  ? 128.262 162.851 120.568 1.00 20.07 ?  819  PRO B CG   1 
ATOM   12993 C CD   . PRO B 1 819  ? 127.301 163.101 121.686 1.00 17.76 ?  819  PRO B CD   1 
ATOM   12994 N N    . LYS B 1 820  ? 125.760 159.611 121.504 1.00 11.42 ?  820  LYS B N    1 
ATOM   12995 C CA   . LYS B 1 820  ? 125.223 158.268 121.712 1.00 11.37 ?  820  LYS B CA   1 
ATOM   12996 C C    . LYS B 1 820  ? 123.721 158.220 121.449 1.00 11.04 ?  820  LYS B C    1 
ATOM   12997 O O    . LYS B 1 820  ? 123.217 157.252 120.866 1.00 18.20 ?  820  LYS B O    1 
ATOM   12998 C CB   . LYS B 1 820  ? 125.545 157.789 123.126 1.00 12.77 ?  820  LYS B CB   1 
ATOM   12999 C CG   . LYS B 1 820  ? 127.030 157.808 123.466 1.00 16.06 ?  820  LYS B CG   1 
ATOM   13000 C CD   . LYS B 1 820  ? 127.856 157.126 122.385 1.00 14.98 ?  820  LYS B CD   1 
ATOM   13001 C CE   . LYS B 1 820  ? 129.346 157.278 122.640 1.00 13.22 ?  820  LYS B CE   1 
ATOM   13002 N NZ   . LYS B 1 820  ? 130.147 156.338 121.807 1.00 14.94 ?  820  LYS B NZ   1 
ATOM   13003 N N    . LEU B 1 821  ? 122.991 159.258 121.863 1.00 12.64 ?  821  LEU B N    1 
ATOM   13004 C CA   . LEU B 1 821  ? 121.558 159.308 121.586 1.00 15.83 ?  821  LEU B CA   1 
ATOM   13005 C C    . LEU B 1 821  ? 121.292 159.498 120.096 1.00 17.53 ?  821  LEU B C    1 
ATOM   13006 O O    . LEU B 1 821  ? 120.341 158.920 119.548 1.00 16.10 ?  821  LEU B O    1 
ATOM   13007 C CB   . LEU B 1 821  ? 120.911 160.425 122.404 1.00 15.54 ?  821  LEU B CB   1 
ATOM   13008 C CG   . LEU B 1 821  ? 120.821 160.218 123.919 1.00 17.52 ?  821  LEU B CG   1 
ATOM   13009 C CD1  . LEU B 1 821  ? 119.780 161.144 124.527 1.00 22.13 ?  821  LEU B CD1  1 
ATOM   13010 C CD2  . LEU B 1 821  ? 120.512 158.768 124.261 1.00 16.70 ?  821  LEU B CD2  1 
ATOM   13011 N N    . ILE B 1 822  ? 122.127 160.294 119.423 1.00 18.96 ?  822  ILE B N    1 
ATOM   13012 C CA   . ILE B 1 822  ? 122.021 160.426 117.972 1.00 10.58 ?  822  ILE B CA   1 
ATOM   13013 C C    . ILE B 1 822  ? 122.271 159.081 117.298 1.00 10.58 ?  822  ILE B C    1 
ATOM   13014 O O    . ILE B 1 822  ? 121.566 158.699 116.356 1.00 17.31 ?  822  ILE B O    1 
ATOM   13015 C CB   . ILE B 1 822  ? 122.986 161.517 117.466 1.00 11.58 ?  822  ILE B CB   1 
ATOM   13016 C CG1  . ILE B 1 822  ? 122.395 162.905 117.718 1.00 14.79 ?  822  ILE B CG1  1 
ATOM   13017 C CG2  . ILE B 1 822  ? 123.302 161.338 115.989 1.00 13.07 ?  822  ILE B CG2  1 
ATOM   13018 C CD1  . ILE B 1 822  ? 123.277 164.038 117.247 1.00 18.23 ?  822  ILE B CD1  1 
ATOM   13019 N N    . LEU B 1 823  ? 123.256 158.328 117.795 1.00 6.80  ?  823  LEU B N    1 
ATOM   13020 C CA   . LEU B 1 823  ? 123.544 157.006 117.249 1.00 4.48  ?  823  LEU B CA   1 
ATOM   13021 C C    . LEU B 1 823  ? 122.379 156.043 117.456 1.00 8.54  ?  823  LEU B C    1 
ATOM   13022 O O    . LEU B 1 823  ? 122.050 155.257 116.561 1.00 12.61 ?  823  LEU B O    1 
ATOM   13023 C CB   . LEU B 1 823  ? 124.817 156.447 117.883 1.00 4.82  ?  823  LEU B CB   1 
ATOM   13024 C CG   . LEU B 1 823  ? 126.087 156.444 117.030 1.00 10.75 ?  823  LEU B CG   1 
ATOM   13025 C CD1  . LEU B 1 823  ? 126.488 157.858 116.646 1.00 12.17 ?  823  LEU B CD1  1 
ATOM   13026 C CD2  . LEU B 1 823  ? 127.218 155.744 117.766 1.00 12.61 ?  823  LEU B CD2  1 
ATOM   13027 N N    . VAL B 1 824  ? 121.744 156.079 118.631 1.00 10.03 ?  824  VAL B N    1 
ATOM   13028 C CA   . VAL B 1 824  ? 120.652 155.138 118.876 1.00 7.98  ?  824  VAL B CA   1 
ATOM   13029 C C    . VAL B 1 824  ? 119.415 155.503 118.050 1.00 7.76  ?  824  VAL B C    1 
ATOM   13030 O O    . VAL B 1 824  ? 118.705 154.610 117.558 1.00 13.22 ?  824  VAL B O    1 
ATOM   13031 C CB   . VAL B 1 824  ? 120.354 155.018 120.389 1.00 8.57  ?  824  VAL B CB   1 
ATOM   13032 C CG1  . VAL B 1 824  ? 119.488 156.154 120.917 1.00 11.69 ?  824  VAL B CG1  1 
ATOM   13033 C CG2  . VAL B 1 824  ? 119.710 153.674 120.695 1.00 13.12 ?  824  VAL B CG2  1 
ATOM   13034 N N    . VAL B 1 825  ? 119.155 156.798 117.833 1.00 7.82  ?  825  VAL B N    1 
ATOM   13035 C CA   . VAL B 1 825  ? 118.023 157.154 116.980 1.00 5.67  ?  825  VAL B CA   1 
ATOM   13036 C C    . VAL B 1 825  ? 118.336 156.839 115.516 1.00 10.06 ?  825  VAL B C    1 
ATOM   13037 O O    . VAL B 1 825  ? 117.438 156.453 114.750 1.00 13.46 ?  825  VAL B O    1 
ATOM   13038 C CB   . VAL B 1 825  ? 117.605 158.623 117.212 1.00 8.76  ?  825  VAL B CB   1 
ATOM   13039 C CG1  . VAL B 1 825  ? 118.463 159.602 116.430 1.00 14.41 ?  825  VAL B CG1  1 
ATOM   13040 C CG2  . VAL B 1 825  ? 116.137 158.813 116.870 1.00 12.15 ?  825  VAL B CG2  1 
ATOM   13041 N N    . ASN B 1 826  ? 119.611 156.940 115.117 1.00 10.71 ?  826  ASN B N    1 
ATOM   13042 C CA   . ASN B 1 826  ? 120.021 156.488 113.792 1.00 5.25  ?  826  ASN B CA   1 
ATOM   13043 C C    . ASN B 1 826  ? 119.801 154.992 113.635 1.00 5.78  ?  826  ASN B C    1 
ATOM   13044 O O    . ASN B 1 826  ? 119.365 154.529 112.576 1.00 9.23  ?  826  ASN B O    1 
ATOM   13045 C CB   . ASN B 1 826  ? 121.492 156.830 113.555 1.00 4.74  ?  826  ASN B CB   1 
ATOM   13046 C CG   . ASN B 1 826  ? 121.680 158.185 112.918 1.00 4.22  ?  826  ASN B CG   1 
ATOM   13047 O OD1  . ASN B 1 826  ? 120.714 158.841 112.538 1.00 6.12  ?  826  ASN B OD1  1 
ATOM   13048 N ND2  . ASN B 1 826  ? 122.930 158.613 112.798 1.00 9.05  ?  826  ASN B ND2  1 
ATOM   13049 N N    . GLY B 1 827  ? 120.107 154.224 114.681 1.00 10.01 ?  827  GLY B N    1 
ATOM   13050 C CA   . GLY B 1 827  ? 119.874 152.791 114.634 1.00 8.56  ?  827  GLY B CA   1 
ATOM   13051 C C    . GLY B 1 827  ? 118.405 152.437 114.498 1.00 11.64 ?  827  GLY B C    1 
ATOM   13052 O O    . GLY B 1 827  ? 118.047 151.529 113.747 1.00 17.93 ?  827  GLY B O    1 
ATOM   13053 N N    . LYS B 1 828  ? 117.535 153.151 115.220 1.00 9.42  ?  828  LYS B N    1 
ATOM   13054 C CA   . LYS B 1 828  ? 116.098 152.901 115.095 1.00 7.83  ?  828  LYS B CA   1 
ATOM   13055 C C    . LYS B 1 828  ? 115.590 153.235 113.692 1.00 9.12  ?  828  LYS B C    1 
ATOM   13056 O O    . LYS B 1 828  ? 114.823 152.461 113.092 1.00 13.23 ?  828  LYS B O    1 
ATOM   13057 C CB   . LYS B 1 828  ? 115.331 153.706 116.144 1.00 7.00  ?  828  LYS B CB   1 
ATOM   13058 C CG   . LYS B 1 828  ? 115.710 153.385 117.582 1.00 12.75 ?  828  LYS B CG   1 
ATOM   13059 C CD   . LYS B 1 828  ? 114.826 152.304 118.181 1.00 14.96 ?  828  LYS B CD   1 
ATOM   13060 C CE   . LYS B 1 828  ? 113.390 152.779 118.324 1.00 15.01 ?  828  LYS B CE   1 
ATOM   13061 N NZ   . LYS B 1 828  ? 112.496 151.698 118.826 1.00 14.58 ?  828  LYS B NZ   1 
ATOM   13062 N N    . ILE B 1 829  ? 116.021 154.379 113.147 1.00 8.48  ?  829  ILE B N    1 
ATOM   13063 C CA   . ILE B 1 829  ? 115.608 154.771 111.800 1.00 8.30  ?  829  ILE B CA   1 
ATOM   13064 C C    . ILE B 1 829  ? 116.106 153.762 110.770 1.00 6.21  ?  829  ILE B C    1 
ATOM   13065 O O    . ILE B 1 829  ? 115.375 153.386 109.845 1.00 8.95  ?  829  ILE B O    1 
ATOM   13066 C CB   . ILE B 1 829  ? 116.094 156.200 111.492 1.00 7.17  ?  829  ILE B CB   1 
ATOM   13067 C CG1  . ILE B 1 829  ? 115.340 157.212 112.356 1.00 9.13  ?  829  ILE B CG1  1 
ATOM   13068 C CG2  . ILE B 1 829  ? 115.929 156.533 110.019 1.00 9.24  ?  829  ILE B CG2  1 
ATOM   13069 C CD1  . ILE B 1 829  ? 115.866 158.619 112.239 1.00 12.03 ?  829  ILE B CD1  1 
ATOM   13070 N N    . ASN B 1 830  ? 117.348 153.293 110.924 1.00 7.64  ?  830  ASN B N    1 
ATOM   13071 C CA   . ASN B 1 830  ? 117.893 152.293 110.012 1.00 0.87  ?  830  ASN B CA   1 
ATOM   13072 C C    . ASN B 1 830  ? 117.149 150.968 110.119 1.00 8.07  ?  830  ASN B C    1 
ATOM   13073 O O    . ASN B 1 830  ? 116.922 150.297 109.105 1.00 21.25 ?  830  ASN B O    1 
ATOM   13074 C CB   . ASN B 1 830  ? 119.382 152.095 110.289 1.00 3.84  ?  830  ASN B CB   1 
ATOM   13075 C CG   . ASN B 1 830  ? 120.093 151.369 109.166 1.00 5.40  ?  830  ASN B CG   1 
ATOM   13076 O OD1  . ASN B 1 830  ? 120.976 150.548 109.406 1.00 8.53  ?  830  ASN B OD1  1 
ATOM   13077 N ND2  . ASN B 1 830  ? 119.710 151.667 107.932 1.00 12.85 ?  830  ASN B ND2  1 
ATOM   13078 N N    . ASN B 1 831  ? 116.770 150.571 111.337 1.00 10.65 ?  831  ASN B N    1 
ATOM   13079 C CA   . ASN B 1 831  ? 116.043 149.319 111.516 1.00 11.09 ?  831  ASN B CA   1 
ATOM   13080 C C    . ASN B 1 831  ? 114.675 149.374 110.851 1.00 7.94  ?  831  ASN B C    1 
ATOM   13081 O O    . ASN B 1 831  ? 114.185 148.361 110.341 1.00 10.48 ?  831  ASN B O    1 
ATOM   13082 C CB   . ASN B 1 831  ? 115.905 148.998 113.004 1.00 11.75 ?  831  ASN B CB   1 
ATOM   13083 C CG   . ASN B 1 831  ? 117.196 148.495 113.611 1.00 16.08 ?  831  ASN B CG   1 
ATOM   13084 O OD1  . ASN B 1 831  ? 117.998 147.845 112.942 1.00 18.26 ?  831  ASN B OD1  1 
ATOM   13085 N ND2  . ASN B 1 831  ? 117.408 148.798 114.886 1.00 18.74 ?  831  ASN B ND2  1 
ATOM   13086 N N    . GLN B 1 832  ? 114.037 150.546 110.854 1.00 3.57  ?  832  GLN B N    1 
ATOM   13087 C CA   . GLN B 1 832  ? 112.777 150.667 110.121 1.00 6.03  ?  832  GLN B CA   1 
ATOM   13088 C C    . GLN B 1 832  ? 113.008 150.689 108.609 1.00 10.68 ?  832  GLN B C    1 
ATOM   13089 O O    . GLN B 1 832  ? 112.281 150.030 107.843 1.00 19.41 ?  832  GLN B O    1 
ATOM   13090 C CB   . GLN B 1 832  ? 112.028 151.921 110.563 1.00 11.07 ?  832  GLN B CB   1 
ATOM   13091 C CG   . GLN B 1 832  ? 110.662 152.064 109.923 1.00 12.47 ?  832  GLN B CG   1 
ATOM   13092 C CD   . GLN B 1 832  ? 109.846 150.791 110.026 1.00 16.03 ?  832  GLN B CD   1 
ATOM   13093 O OE1  . GLN B 1 832  ? 109.449 150.384 111.117 1.00 15.95 ?  832  GLN B OE1  1 
ATOM   13094 N NE2  . GLN B 1 832  ? 109.595 150.154 108.890 1.00 17.68 ?  832  GLN B NE2  1 
ATOM   13095 N N    . LEU B 1 833  ? 114.022 151.438 108.163 1.00 12.24 ?  833  LEU B N    1 
ATOM   13096 C CA   . LEU B 1 833  ? 114.230 151.643 106.735 1.00 2.07  ?  833  LEU B CA   1 
ATOM   13097 C C    . LEU B 1 833  ? 114.676 150.369 106.034 1.00 1.23  ?  833  LEU B C    1 
ATOM   13098 O O    . LEU B 1 833  ? 114.353 150.173 104.858 1.00 9.18  ?  833  LEU B O    1 
ATOM   13099 C CB   . LEU B 1 833  ? 115.260 152.744 106.500 1.00 4.54  ?  833  LEU B CB   1 
ATOM   13100 C CG   . LEU B 1 833  ? 114.864 153.797 105.467 1.00 8.23  ?  833  LEU B CG   1 
ATOM   13101 C CD1  . LEU B 1 833  ? 113.479 154.356 105.770 1.00 12.05 ?  833  LEU B CD1  1 
ATOM   13102 C CD2  . LEU B 1 833  ? 115.902 154.891 105.392 1.00 9.04  ?  833  LEU B CD2  1 
ATOM   13103 N N    . SER B 1 834  ? 115.429 149.506 106.721 1.00 1.74  ?  834  SER B N    1 
ATOM   13104 C CA   . SER B 1 834  ? 115.850 148.250 106.107 1.00 0.00  ?  834  SER B CA   1 
ATOM   13105 C C    . SER B 1 834  ? 114.655 147.361 105.793 1.00 3.04  ?  834  SER B C    1 
ATOM   13106 O O    . SER B 1 834  ? 114.575 146.777 104.704 1.00 11.23 ?  834  SER B O    1 
ATOM   13107 C CB   . SER B 1 834  ? 116.831 147.521 107.021 1.00 1.13  ?  834  SER B CB   1 
ATOM   13108 O OG   . SER B 1 834  ? 116.159 146.570 107.826 1.00 7.99  ?  834  SER B OG   1 
ATOM   13109 N N    . LEU B 1 835  ? 113.711 147.256 106.732 1.00 6.97  ?  835  LEU B N    1 
ATOM   13110 C CA   . LEU B 1 835  ? 112.497 146.484 106.490 1.00 3.75  ?  835  LEU B CA   1 
ATOM   13111 C C    . LEU B 1 835  ? 111.673 147.090 105.363 1.00 0.00  ?  835  LEU B C    1 
ATOM   13112 O O    . LEU B 1 835  ? 111.151 146.363 104.505 1.00 1.85  ?  835  LEU B O    1 
ATOM   13113 C CB   . LEU B 1 835  ? 111.670 146.396 107.773 1.00 2.49  ?  835  LEU B CB   1 
ATOM   13114 C CG   . LEU B 1 835  ? 110.291 145.746 107.658 1.00 11.79 ?  835  LEU B CG   1 
ATOM   13115 C CD1  . LEU B 1 835  ? 110.341 144.296 108.105 1.00 11.28 ?  835  LEU B CD1  1 
ATOM   13116 C CD2  . LEU B 1 835  ? 109.266 146.525 108.465 1.00 11.88 ?  835  LEU B CD2  1 
ATOM   13117 N N    . GLY B 1 836  ? 111.551 148.423 105.342 1.00 2.57  ?  836  GLY B N    1 
ATOM   13118 C CA   . GLY B 1 836  ? 110.810 149.061 104.261 1.00 4.58  ?  836  GLY B CA   1 
ATOM   13119 C C    . GLY B 1 836  ? 111.423 148.811 102.894 1.00 4.32  ?  836  GLY B C    1 
ATOM   13120 O O    . GLY B 1 836  ? 110.715 148.487 101.931 1.00 14.40 ?  836  GLY B O    1 
ATOM   13121 N N    . TYR B 1 837  ? 112.750 148.934 102.797 1.00 6.54  ?  837  TYR B N    1 
ATOM   13122 C CA   . TYR B 1 837  ? 113.442 148.688 101.536 1.00 0.00  ?  837  TYR B CA   1 
ATOM   13123 C C    . TYR B 1 837  ? 113.320 147.235 101.101 1.00 1.86  ?  837  TYR B C    1 
ATOM   13124 O O    . TYR B 1 837  ? 113.135 146.956 99.911  1.00 12.63 ?  837  TYR B O    1 
ATOM   13125 C CB   . TYR B 1 837  ? 114.912 149.080 101.659 1.00 0.00  ?  837  TYR B CB   1 
ATOM   13126 C CG   . TYR B 1 837  ? 115.241 150.390 100.996 1.00 3.23  ?  837  TYR B CG   1 
ATOM   13127 C CD1  . TYR B 1 837  ? 115.166 150.523 99.618  1.00 7.53  ?  837  TYR B CD1  1 
ATOM   13128 C CD2  . TYR B 1 837  ? 115.625 151.494 101.743 1.00 3.54  ?  837  TYR B CD2  1 
ATOM   13129 C CE1  . TYR B 1 837  ? 115.463 151.714 99.002  1.00 7.46  ?  837  TYR B CE1  1 
ATOM   13130 C CE2  . TYR B 1 837  ? 115.924 152.693 101.135 1.00 2.46  ?  837  TYR B CE2  1 
ATOM   13131 C CZ   . TYR B 1 837  ? 115.841 152.795 99.765  1.00 8.29  ?  837  TYR B CZ   1 
ATOM   13132 O OH   . TYR B 1 837  ? 116.138 153.982 99.150  1.00 13.25 ?  837  TYR B OH   1 
ATOM   13133 N N    . ASP B 1 838  ? 113.437 146.296 102.045 1.00 1.84  ?  838  ASP B N    1 
ATOM   13134 C CA   . ASP B 1 838  ? 113.298 144.885 101.699 1.00 0.00  ?  838  ASP B CA   1 
ATOM   13135 C C    . ASP B 1 838  ? 111.902 144.576 101.175 1.00 1.88  ?  838  ASP B C    1 
ATOM   13136 O O    . ASP B 1 838  ? 111.753 143.855 100.180 1.00 1.88  ?  838  ASP B O    1 
ATOM   13137 C CB   . ASP B 1 838  ? 113.620 144.010 102.909 1.00 3.95  ?  838  ASP B CB   1 
ATOM   13138 C CG   . ASP B 1 838  ? 115.106 143.903 103.173 1.00 9.77  ?  838  ASP B CG   1 
ATOM   13139 O OD1  . ASP B 1 838  ? 115.834 144.877 102.890 1.00 8.50  ?  838  ASP B OD1  1 
ATOM   13140 O OD2  . ASP B 1 838  ? 115.546 142.844 103.668 1.00 16.27 ?  838  ASP B OD2  1 
ATOM   13141 N N    . VAL B 1 839  ? 110.867 145.128 101.818 1.00 1.90  ?  839  VAL B N    1 
ATOM   13142 C CA   . VAL B 1 839  ? 109.496 144.885 101.369 1.00 0.54  ?  839  VAL B CA   1 
ATOM   13143 C C    . VAL B 1 839  ? 109.283 145.453 99.969  1.00 0.56  ?  839  VAL B C    1 
ATOM   13144 O O    . VAL B 1 839  ? 108.729 144.783 99.085  1.00 13.03 ?  839  VAL B O    1 
ATOM   13145 C CB   . VAL B 1 839  ? 108.490 145.469 102.378 1.00 4.51  ?  839  VAL B CB   1 
ATOM   13146 C CG1  . VAL B 1 839  ? 107.100 145.538 101.771 1.00 4.76  ?  839  VAL B CG1  1 
ATOM   13147 C CG2  . VAL B 1 839  ? 108.473 144.638 103.647 1.00 5.17  ?  839  VAL B CG2  1 
ATOM   13148 N N    . GLY B 1 840  ? 109.742 146.688 99.740  1.00 0.69  ?  840  GLY B N    1 
ATOM   13149 C CA   . GLY B 1 840  ? 109.570 147.294 98.428  1.00 0.00  ?  840  GLY B CA   1 
ATOM   13150 C C    . GLY B 1 840  ? 110.311 146.555 97.329  1.00 3.50  ?  840  GLY B C    1 
ATOM   13151 O O    . GLY B 1 840  ? 109.756 146.300 96.254  1.00 7.93  ?  840  GLY B O    1 
ATOM   13152 N N    . LYS B 1 841  ? 111.569 146.184 97.589  1.00 4.78  ?  841  LYS B N    1 
ATOM   13153 C CA   . LYS B 1 841  ? 112.365 145.466 96.600  1.00 0.00  ?  841  LYS B CA   1 
ATOM   13154 C C    . LYS B 1 841  ? 111.765 144.102 96.287  1.00 0.00  ?  841  LYS B C    1 
ATOM   13155 O O    . LYS B 1 841  ? 111.695 143.700 95.117  1.00 9.07  ?  841  LYS B O    1 
ATOM   13156 C CB   . LYS B 1 841  ? 113.798 145.315 97.106  1.00 0.45  ?  841  LYS B CB   1 
ATOM   13157 C CG   . LYS B 1 841  ? 114.861 145.437 96.036  1.00 8.70  ?  841  LYS B CG   1 
ATOM   13158 C CD   . LYS B 1 841  ? 116.160 145.971 96.619  1.00 11.10 ?  841  LYS B CD   1 
ATOM   13159 C CE   . LYS B 1 841  ? 115.951 147.326 97.281  1.00 6.78  ?  841  LYS B CE   1 
ATOM   13160 N NZ   . LYS B 1 841  ? 117.105 147.725 98.130  1.00 7.07  ?  841  LYS B NZ   1 
ATOM   13161 N N    . GLY B 1 842  ? 111.329 143.375 97.321  1.00 0.00  ?  842  GLY B N    1 
ATOM   13162 C CA   . GLY B 1 842  ? 110.713 142.079 97.095  1.00 0.00  ?  842  GLY B CA   1 
ATOM   13163 C C    . GLY B 1 842  ? 109.433 142.172 96.292  1.00 0.00  ?  842  GLY B C    1 
ATOM   13164 O O    . GLY B 1 842  ? 109.192 141.354 95.401  1.00 5.65  ?  842  GLY B O    1 
ATOM   13165 N N    . TYR B 1 843  ? 108.599 143.177 96.584  1.00 0.43  ?  843  TYR B N    1 
ATOM   13166 C CA   . TYR B 1 843  ? 107.380 143.360 95.803  1.00 0.00  ?  843  TYR B CA   1 
ATOM   13167 C C    . TYR B 1 843  ? 107.694 143.680 94.346  1.00 0.63  ?  843  TYR B C    1 
ATOM   13168 O O    . TYR B 1 843  ? 107.056 143.136 93.436  1.00 8.06  ?  843  TYR B O    1 
ATOM   13169 C CB   . TYR B 1 843  ? 106.514 144.459 96.417  1.00 0.00  ?  843  TYR B CB   1 
ATOM   13170 C CG   . TYR B 1 843  ? 105.281 144.783 95.602  1.00 0.39  ?  843  TYR B CG   1 
ATOM   13171 C CD1  . TYR B 1 843  ? 104.155 143.976 95.663  1.00 6.05  ?  843  TYR B CD1  1 
ATOM   13172 C CD2  . TYR B 1 843  ? 105.241 145.901 94.779  1.00 6.48  ?  843  TYR B CD2  1 
ATOM   13173 C CE1  . TYR B 1 843  ? 103.027 144.267 94.922  1.00 10.20 ?  843  TYR B CE1  1 
ATOM   13174 C CE2  . TYR B 1 843  ? 104.117 146.200 94.035  1.00 10.99 ?  843  TYR B CE2  1 
ATOM   13175 C CZ   . TYR B 1 843  ? 103.013 145.381 94.111  1.00 14.39 ?  843  TYR B CZ   1 
ATOM   13176 O OH   . TYR B 1 843  ? 101.891 145.676 93.372  1.00 13.64 ?  843  TYR B OH   1 
ATOM   13177 N N    . ILE B 1 844  ? 108.677 144.555 94.107  1.00 6.37  ?  844  ILE B N    1 
ATOM   13178 C CA   . ILE B 1 844  ? 109.028 144.934 92.738  1.00 1.07  ?  844  ILE B CA   1 
ATOM   13179 C C    . ILE B 1 844  ? 109.515 143.718 91.956  1.00 2.32  ?  844  ILE B C    1 
ATOM   13180 O O    . ILE B 1 844  ? 109.084 143.472 90.820  1.00 10.29 ?  844  ILE B O    1 
ATOM   13181 C CB   . ILE B 1 844  ? 110.081 146.057 92.747  1.00 4.17  ?  844  ILE B CB   1 
ATOM   13182 C CG1  . ILE B 1 844  ? 109.467 147.370 93.245  1.00 4.59  ?  844  ILE B CG1  1 
ATOM   13183 C CG2  . ILE B 1 844  ? 110.722 146.212 91.371  1.00 5.18  ?  844  ILE B CG2  1 
ATOM   13184 C CD1  . ILE B 1 844  ? 108.966 148.288 92.159  1.00 4.24  ?  844  ILE B CD1  1 
ATOM   13185 N N    . ILE B 1 845  ? 110.405 142.928 92.564  1.00 6.03  ?  845  ILE B N    1 
ATOM   13186 C CA   . ILE B 1 845  ? 110.950 141.753 91.887  1.00 4.88  ?  845  ILE B CA   1 
ATOM   13187 C C    . ILE B 1 845  ? 109.858 140.715 91.639  1.00 7.49  ?  845  ILE B C    1 
ATOM   13188 O O    . ILE B 1 845  ? 109.802 140.097 90.565  1.00 8.43  ?  845  ILE B O    1 
ATOM   13189 C CB   . ILE B 1 845  ? 112.123 141.175 92.698  1.00 4.35  ?  845  ILE B CB   1 
ATOM   13190 C CG1  . ILE B 1 845  ? 113.284 142.169 92.731  1.00 3.91  ?  845  ILE B CG1  1 
ATOM   13191 C CG2  . ILE B 1 845  ? 112.598 139.859 92.111  1.00 6.94  ?  845  ILE B CG2  1 
ATOM   13192 C CD1  . ILE B 1 845  ? 114.368 141.801 93.714  1.00 4.58  ?  845  ILE B CD1  1 
ATOM   13193 N N    . GLY B 1 846  ? 108.966 140.517 92.616  1.00 6.77  ?  846  GLY B N    1 
ATOM   13194 C CA   . GLY B 1 846  ? 107.882 139.565 92.436  1.00 2.23  ?  846  GLY B CA   1 
ATOM   13195 C C    . GLY B 1 846  ? 106.937 139.949 91.314  1.00 6.19  ?  846  GLY B C    1 
ATOM   13196 O O    . GLY B 1 846  ? 106.551 139.102 90.505  1.00 15.02 ?  846  GLY B O    1 
ATOM   13197 N N    . GLU B 1 847  ? 106.561 141.231 91.240  1.00 7.79  ?  847  GLU B N    1 
ATOM   13198 C CA   . GLU B 1 847  ? 105.711 141.681 90.139  1.00 6.11  ?  847  GLU B CA   1 
ATOM   13199 C C    . GLU B 1 847  ? 106.418 141.548 88.797  1.00 7.70  ?  847  GLU B C    1 
ATOM   13200 O O    . GLU B 1 847  ? 105.800 141.148 87.802  1.00 17.23 ?  847  GLU B O    1 
ATOM   13201 C CB   . GLU B 1 847  ? 105.257 143.125 90.360  1.00 7.59  ?  847  GLU B CB   1 
ATOM   13202 C CG   . GLU B 1 847  ? 104.467 143.362 91.636  1.00 10.64 ?  847  GLU B CG   1 
ATOM   13203 C CD   . GLU B 1 847  ? 103.433 142.286 91.898  1.00 17.74 ?  847  GLU B CD   1 
ATOM   13204 O OE1  . GLU B 1 847  ? 102.345 142.347 91.287  1.00 22.02 ?  847  GLU B OE1  1 
ATOM   13205 O OE2  . GLU B 1 847  ? 103.703 141.383 92.718  1.00 16.56 ?  847  GLU B OE2  1 
ATOM   13206 N N    . GLU B 1 848  ? 107.715 141.873 88.748  1.00 11.36 ?  848  GLU B N    1 
ATOM   13207 C CA   . GLU B 1 848  ? 108.445 141.790 87.486  1.00 11.99 ?  848  GLU B CA   1 
ATOM   13208 C C    . GLU B 1 848  ? 108.557 140.351 86.994  1.00 9.65  ?  848  GLU B C    1 
ATOM   13209 O O    . GLU B 1 848  ? 108.500 140.100 85.784  1.00 10.78 ?  848  GLU B O    1 
ATOM   13210 C CB   . GLU B 1 848  ? 109.829 142.419 87.638  1.00 12.17 ?  848  GLU B CB   1 
ATOM   13211 C CG   . GLU B 1 848  ? 109.913 143.843 87.113  1.00 13.54 ?  848  GLU B CG   1 
ATOM   13212 C CD   . GLU B 1 848  ? 111.070 144.621 87.707  1.00 17.64 ?  848  GLU B CD   1 
ATOM   13213 O OE1  . GLU B 1 848  ? 111.909 144.007 88.399  1.00 13.99 ?  848  GLU B OE1  1 
ATOM   13214 O OE2  . GLU B 1 848  ? 111.142 145.847 87.480  1.00 18.10 ?  848  GLU B OE2  1 
ATOM   13215 N N    . GLU B 1 849  ? 108.719 139.392 87.909  1.00 9.34  ?  849  GLU B N    1 
ATOM   13216 C CA   . GLU B 1 849  ? 108.773 137.992 87.493  1.00 13.24 ?  849  GLU B CA   1 
ATOM   13217 C C    . GLU B 1 849  ? 107.390 137.461 87.123  1.00 15.53 ?  849  GLU B C    1 
ATOM   13218 O O    . GLU B 1 849  ? 107.246 136.698 86.157  1.00 12.63 ?  849  GLU B O    1 
ATOM   13219 C CB   . GLU B 1 849  ? 109.399 137.138 88.596  1.00 11.23 ?  849  GLU B CB   1 
ATOM   13220 C CG   . GLU B 1 849  ? 110.914 137.228 88.660  1.00 12.35 ?  849  GLU B CG   1 
ATOM   13221 C CD   . GLU B 1 849  ? 111.475 136.727 89.975  1.00 17.28 ?  849  GLU B CD   1 
ATOM   13222 O OE1  . GLU B 1 849  ? 110.736 136.048 90.719  1.00 17.92 ?  849  GLU B OE1  1 
ATOM   13223 O OE2  . GLU B 1 849  ? 112.657 137.009 90.264  1.00 16.28 ?  849  GLU B OE2  1 
ATOM   13224 N N    . VAL B 1 850  ? 106.362 137.845 87.885  1.00 15.18 ?  850  VAL B N    1 
ATOM   13225 C CA   . VAL B 1 850  ? 105.014 137.337 87.649  1.00 12.34 ?  850  VAL B CA   1 
ATOM   13226 C C    . VAL B 1 850  ? 104.447 137.867 86.337  1.00 10.19 ?  850  VAL B C    1 
ATOM   13227 O O    . VAL B 1 850  ? 103.711 137.155 85.641  1.00 13.02 ?  850  VAL B O    1 
ATOM   13228 C CB   . VAL B 1 850  ? 104.129 137.675 88.865  1.00 13.35 ?  850  VAL B CB   1 
ATOM   13229 C CG1  . VAL B 1 850  ? 102.648 137.692 88.511  1.00 12.20 ?  850  VAL B CG1  1 
ATOM   13230 C CG2  . VAL B 1 850  ? 104.398 136.678 89.973  1.00 12.03 ?  850  VAL B CG2  1 
ATOM   13231 N N    . GLY B 1 851  ? 104.780 139.107 85.966  1.00 14.45 ?  851  GLY B N    1 
ATOM   13232 C CA   . GLY B 1 851  ? 104.345 139.624 84.678  1.00 12.94 ?  851  GLY B CA   1 
ATOM   13233 C C    . GLY B 1 851  ? 104.880 138.828 83.504  1.00 14.63 ?  851  GLY B C    1 
ATOM   13234 O O    . GLY B 1 851  ? 104.199 138.683 82.486  1.00 21.98 ?  851  GLY B O    1 
ATOM   13235 N N    . LYS B 1 852  ? 106.101 138.304 83.625  1.00 12.63 ?  852  LYS B N    1 
ATOM   13236 C CA   . LYS B 1 852  ? 106.646 137.438 82.586  1.00 17.46 ?  852  LYS B CA   1 
ATOM   13237 C C    . LYS B 1 852  ? 106.051 136.036 82.653  1.00 19.27 ?  852  LYS B C    1 
ATOM   13238 O O    . LYS B 1 852  ? 105.835 135.403 81.613  1.00 15.51 ?  852  LYS B O    1 
ATOM   13239 C CB   . LYS B 1 852  ? 108.169 137.374 82.703  1.00 16.78 ?  852  LYS B CB   1 
ATOM   13240 C CG   . LYS B 1 852  ? 108.860 138.716 82.537  1.00 16.76 ?  852  LYS B CG   1 
ATOM   13241 C CD   . LYS B 1 852  ? 108.532 139.341 81.193  1.00 16.75 ?  852  LYS B CD   1 
ATOM   13242 C CE   . LYS B 1 852  ? 108.820 140.833 81.190  1.00 18.40 ?  852  LYS B CE   1 
ATOM   13243 N NZ   . LYS B 1 852  ? 108.213 141.511 80.011  1.00 15.29 ?  852  LYS B NZ   1 
ATOM   13244 N N    . ILE B 1 853  ? 105.794 135.533 83.863  1.00 22.78 ?  853  ILE B N    1 
ATOM   13245 C CA   . ILE B 1 853  ? 105.279 134.173 84.014  1.00 18.48 ?  853  ILE B CA   1 
ATOM   13246 C C    . ILE B 1 853  ? 103.855 134.069 83.471  1.00 16.82 ?  853  ILE B C    1 
ATOM   13247 O O    . ILE B 1 853  ? 103.529 133.151 82.710  1.00 19.90 ?  853  ILE B O    1 
ATOM   13248 C CB   . ILE B 1 853  ? 105.360 133.731 85.487  1.00 13.16 ?  853  ILE B CB   1 
ATOM   13249 C CG1  . ILE B 1 853  ? 106.774 133.257 85.823  1.00 17.70 ?  853  ILE B CG1  1 
ATOM   13250 C CG2  . ILE B 1 853  ? 104.352 132.628 85.788  1.00 9.45  ?  853  ILE B CG2  1 
ATOM   13251 C CD1  . ILE B 1 853  ? 106.947 132.833 87.264  1.00 17.80 ?  853  ILE B CD1  1 
ATOM   13252 N N    . ILE B 1 854  ? 102.994 135.024 83.834  1.00 18.50 ?  854  ILE B N    1 
ATOM   13253 C CA   . ILE B 1 854  ? 101.570 134.946 83.506  1.00 17.50 ?  854  ILE B CA   1 
ATOM   13254 C C    . ILE B 1 854  ? 101.262 135.239 82.046  1.00 17.53 ?  854  ILE B C    1 
ATOM   13255 O O    . ILE B 1 854  ? 100.110 135.069 81.623  1.00 20.75 ?  854  ILE B O    1 
ATOM   13256 C CB   . ILE B 1 854  ? 100.788 135.899 84.435  1.00 18.37 ?  854  ILE B CB   1 
ATOM   13257 C CG1  . ILE B 1 854  ? 99.435  135.295 84.821  1.00 21.59 ?  854  ILE B CG1  1 
ATOM   13258 C CG2  . ILE B 1 854  ? 100.649 137.296 83.821  1.00 14.27 ?  854  ILE B CG2  1 
ATOM   13259 C CD1  . ILE B 1 854  ? 99.523  134.246 85.906  1.00 20.05 ?  854  ILE B CD1  1 
ATOM   13260 N N    . ASP B 1 855  ? 102.260 135.653 81.259  1.00 17.00 ?  855  ASP B N    1 
ATOM   13261 C CA   . ASP B 1 855  ? 102.016 136.030 79.868  1.00 21.68 ?  855  ASP B CA   1 
ATOM   13262 C C    . ASP B 1 855  ? 101.541 134.844 79.035  1.00 22.91 ?  855  ASP B C    1 
ATOM   13263 O O    . ASP B 1 855  ? 100.654 134.990 78.186  1.00 24.76 ?  855  ASP B O    1 
ATOM   13264 C CB   . ASP B 1 855  ? 103.284 136.635 79.265  1.00 22.44 ?  855  ASP B CB   1 
ATOM   13265 C CG   . ASP B 1 855  ? 102.986 137.652 78.181  1.00 22.94 ?  855  ASP B CG   1 
ATOM   13266 O OD1  . ASP B 1 855  ? 101.800 137.826 77.833  1.00 21.81 ?  855  ASP B OD1  1 
ATOM   13267 O OD2  . ASP B 1 855  ? 103.942 138.280 77.678  1.00 21.52 ?  855  ASP B OD2  1 
ATOM   13268 N N    . ARG B 1 856  ? 102.119 133.665 79.257  1.00 22.21 ?  856  ARG B N    1 
ATOM   13269 C CA   . ARG B 1 856  ? 101.771 132.473 78.495  1.00 26.01 ?  856  ARG B CA   1 
ATOM   13270 C C    . ARG B 1 856  ? 100.786 131.567 79.224  1.00 26.56 ?  856  ARG B C    1 
ATOM   13271 O O    . ARG B 1 856  ? 100.506 130.464 78.745  1.00 27.27 ?  856  ARG B O    1 
ATOM   13272 C CB   . ARG B 1 856  ? 103.037 131.691 78.136  1.00 25.17 ?  856  ARG B CB   1 
ATOM   13273 C CG   . ARG B 1 856  ? 103.818 131.172 79.332  1.00 21.35 ?  856  ARG B CG   1 
ATOM   13274 C CD   . ARG B 1 856  ? 105.255 130.851 78.948  1.00 24.59 ?  856  ARG B CD   1 
ATOM   13275 N NE   . ARG B 1 856  ? 105.669 129.531 79.407  1.00 26.38 ?  856  ARG B NE   1 
ATOM   13276 C CZ   . ARG B 1 856  ? 106.157 129.276 80.613  1.00 27.37 ?  856  ARG B CZ   1 
ATOM   13277 N NH1  . ARG B 1 856  ? 106.305 130.232 81.515  1.00 23.75 ?  856  ARG B NH1  1 
ATOM   13278 N NH2  . ARG B 1 856  ? 106.505 128.030 80.922  1.00 27.46 ?  856  ARG B NH2  1 
ATOM   13279 N N    . MET B 1 857  ? 100.250 132.004 80.365  1.00 22.78 ?  857  MET B N    1 
ATOM   13280 C CA   . MET B 1 857  ? 99.313  131.207 81.148  1.00 21.81 ?  857  MET B CA   1 
ATOM   13281 C C    . MET B 1 857  ? 97.921  131.829 81.207  1.00 24.52 ?  857  MET B C    1 
ATOM   13282 O O    . MET B 1 857  ? 97.111  131.446 82.057  1.00 25.10 ?  857  MET B O    1 
ATOM   13283 C CB   . MET B 1 857  ? 99.854  130.990 82.562  1.00 22.36 ?  857  MET B CB   1 
ATOM   13284 C CG   . MET B 1 857  ? 101.168 130.226 82.624  1.00 25.89 ?  857  MET B CG   1 
ATOM   13285 S SD   . MET B 1 857  ? 101.233 128.843 81.469  1.00 31.42 ?  857  MET B SD   1 
ATOM   13286 C CE   . MET B 1 857  ? 102.581 127.885 82.158  1.00 23.91 ?  857  MET B CE   1 
ATOM   13287 N N    . VAL B 1 858  ? 97.625  132.782 80.325  1.00 27.73 ?  858  VAL B N    1 
ATOM   13288 C CA   . VAL B 1 858  ? 96.329  133.448 80.279  1.00 27.31 ?  858  VAL B CA   1 
ATOM   13289 C C    . VAL B 1 858  ? 95.804  133.369 78.852  1.00 26.22 ?  858  VAL B C    1 
ATOM   13290 O O    . VAL B 1 858  ? 96.526  133.695 77.904  1.00 27.16 ?  858  VAL B O    1 
ATOM   13291 C CB   . VAL B 1 858  ? 96.423  134.914 80.748  1.00 26.72 ?  858  VAL B CB   1 
ATOM   13292 C CG1  . VAL B 1 858  ? 95.134  135.664 80.446  1.00 24.21 ?  858  VAL B CG1  1 
ATOM   13293 C CG2  . VAL B 1 858  ? 96.738  134.977 82.235  1.00 25.34 ?  858  VAL B CG2  1 
ATOM   13294 N N    . ASP B 1 859  ? 94.553  132.936 78.701  1.00 26.15 ?  859  ASP B N    1 
ATOM   13295 C CA   . ASP B 1 859  ? 93.933  132.732 77.395  1.00 25.92 ?  859  ASP B CA   1 
ATOM   13296 C C    . ASP B 1 859  ? 92.881  133.795 77.087  1.00 25.90 ?  859  ASP B C    1 
ATOM   13297 O O    . ASP B 1 859  ? 91.858  133.512 76.460  1.00 29.47 ?  859  ASP B O    1 
ATOM   13298 C CB   . ASP B 1 859  ? 93.319  131.338 77.306  1.00 27.99 ?  859  ASP B CB   1 
ATOM   13299 C CG   . ASP B 1 859  ? 94.364  130.242 77.271  1.00 31.43 ?  859  ASP B CG   1 
ATOM   13300 O OD1  . ASP B 1 859  ? 95.518  130.531 76.892  1.00 29.52 ?  859  ASP B OD1  1 
ATOM   13301 O OD2  . ASP B 1 859  ? 94.031  129.090 77.621  1.00 29.85 ?  859  ASP B OD2  1 
ATOM   13302 N N    . ASN B 1 860  ? 93.118  135.031 77.521  1.00 23.09 ?  860  ASN B N    1 
ATOM   13303 C CA   . ASN B 1 860  ? 92.221  136.136 77.209  1.00 27.25 ?  860  ASN B CA   1 
ATOM   13304 C C    . ASN B 1 860  ? 93.028  137.422 77.149  1.00 27.10 ?  860  ASN B C    1 
ATOM   13305 O O    . ASN B 1 860  ? 93.747  137.746 78.098  1.00 27.82 ?  860  ASN B O    1 
ATOM   13306 C CB   . ASN B 1 860  ? 91.103  136.265 78.247  1.00 26.56 ?  860  ASN B CB   1 
ATOM   13307 C CG   . ASN B 1 860  ? 90.183  137.438 77.968  1.00 28.43 ?  860  ASN B CG   1 
ATOM   13308 O OD1  . ASN B 1 860  ? 90.125  138.395 78.740  1.00 25.88 ?  860  ASN B OD1  1 
ATOM   13309 N ND2  . ASN B 1 860  ? 89.455  137.369 76.859  1.00 27.47 ?  860  ASN B ND2  1 
ATOM   13310 N N    . LYS B 1 861  ? 92.899  138.149 76.035  1.00 21.99 ?  861  LYS B N    1 
ATOM   13311 C CA   . LYS B 1 861  ? 93.666  139.378 75.851  1.00 24.83 ?  861  LYS B CA   1 
ATOM   13312 C C    . LYS B 1 861  ? 93.253  140.454 76.848  1.00 25.33 ?  861  LYS B C    1 
ATOM   13313 O O    . LYS B 1 861  ? 94.108  141.163 77.392  1.00 25.15 ?  861  LYS B O    1 
ATOM   13314 C CB   . LYS B 1 861  ? 93.505  139.884 74.417  1.00 25.43 ?  861  LYS B CB   1 
ATOM   13315 C CG   . LYS B 1 861  ? 94.398  139.183 73.405  1.00 24.03 ?  861  LYS B CG   1 
ATOM   13316 C CD   . LYS B 1 861  ? 93.686  138.008 72.748  1.00 23.78 ?  861  LYS B CD   1 
ATOM   13317 C CE   . LYS B 1 861  ? 92.406  138.449 72.054  1.00 23.91 ?  861  LYS B CE   1 
ATOM   13318 N NZ   . LYS B 1 861  ? 91.710  137.307 71.396  1.00 25.49 ?  861  LYS B NZ   1 
ATOM   13319 N N    . LYS B 1 862  ? 91.947  140.591 77.098  1.00 21.24 ?  862  LYS B N    1 
ATOM   13320 C CA   . LYS B 1 862  ? 91.463  141.623 78.011  1.00 25.71 ?  862  LYS B CA   1 
ATOM   13321 C C    . LYS B 1 862  ? 91.929  141.368 79.439  1.00 26.36 ?  862  LYS B C    1 
ATOM   13322 O O    . LYS B 1 862  ? 92.357  142.299 80.136  1.00 28.06 ?  862  LYS B O    1 
ATOM   13323 C CB   . LYS B 1 862  ? 89.937  141.698 77.954  1.00 23.58 ?  862  LYS B CB   1 
ATOM   13324 C CG   . LYS B 1 862  ? 89.391  142.655 76.905  1.00 24.07 ?  862  LYS B CG   1 
ATOM   13325 C CD   . LYS B 1 862  ? 89.347  142.014 75.524  1.00 23.92 ?  862  LYS B CD   1 
ATOM   13326 C CE   . LYS B 1 862  ? 88.578  140.701 75.543  1.00 24.16 ?  862  LYS B CE   1 
ATOM   13327 N NZ   . LYS B 1 862  ? 88.691  139.966 74.252  1.00 20.75 ?  862  LYS B NZ   1 
ATOM   13328 N N    . ILE B 1 863  ? 91.861  140.112 79.887  1.00 20.04 ?  863  ILE B N    1 
ATOM   13329 C CA   . ILE B 1 863  ? 92.256  139.780 81.252  1.00 24.36 ?  863  ILE B CA   1 
ATOM   13330 C C    . ILE B 1 863  ? 93.749  140.025 81.449  1.00 25.14 ?  863  ILE B C    1 
ATOM   13331 O O    . ILE B 1 863  ? 94.163  140.650 82.433  1.00 25.17 ?  863  ILE B O    1 
ATOM   13332 C CB   . ILE B 1 863  ? 91.861  138.329 81.584  1.00 24.38 ?  863  ILE B CB   1 
ATOM   13333 C CG1  . ILE B 1 863  ? 90.395  138.269 82.020  1.00 25.32 ?  863  ILE B CG1  1 
ATOM   13334 C CG2  . ILE B 1 863  ? 92.752  137.748 82.675  1.00 22.65 ?  863  ILE B CG2  1 
ATOM   13335 C CD1  . ILE B 1 863  ? 89.874  136.865 82.232  1.00 25.84 ?  863  ILE B CD1  1 
ATOM   13336 N N    . LEU B 1 864  ? 94.574  139.567 80.501  1.00 22.94 ?  864  LEU B N    1 
ATOM   13337 C CA   . LEU B 1 864  ? 96.016  139.763 80.629  1.00 25.74 ?  864  LEU B CA   1 
ATOM   13338 C C    . LEU B 1 864  ? 96.383  141.239 80.532  1.00 26.64 ?  864  LEU B C    1 
ATOM   13339 O O    . LEU B 1 864  ? 97.305  141.698 81.216  1.00 29.28 ?  864  LEU B O    1 
ATOM   13340 C CB   . LEU B 1 864  ? 96.769  138.931 79.583  1.00 24.84 ?  864  LEU B CB   1 
ATOM   13341 C CG   . LEU B 1 864  ? 96.853  139.307 78.098  1.00 22.86 ?  864  LEU B CG   1 
ATOM   13342 C CD1  . LEU B 1 864  ? 98.094  140.138 77.794  1.00 20.67 ?  864  LEU B CD1  1 
ATOM   13343 C CD2  . LEU B 1 864  ? 96.854  138.051 77.241  1.00 24.04 ?  864  LEU B CD2  1 
ATOM   13344 N N    . ARG B 1 865  ? 95.663  142.001 79.700  1.00 22.86 ?  865  ARG B N    1 
ATOM   13345 C CA   . ARG B 1 865  ? 95.899  143.439 79.618  1.00 25.13 ?  865  ARG B CA   1 
ATOM   13346 C C    . ARG B 1 865  ? 95.586  144.128 80.941  1.00 22.91 ?  865  ARG B C    1 
ATOM   13347 O O    . ARG B 1 865  ? 96.357  144.979 81.404  1.00 21.70 ?  865  ARG B O    1 
ATOM   13348 C CB   . ARG B 1 865  ? 95.065  144.039 78.487  1.00 22.03 ?  865  ARG B CB   1 
ATOM   13349 C CG   . ARG B 1 865  ? 95.551  145.394 78.003  1.00 21.21 ?  865  ARG B CG   1 
ATOM   13350 C CD   . ARG B 1 865  ? 94.438  146.161 77.305  1.00 21.58 ?  865  ARG B CD   1 
ATOM   13351 N NE   . ARG B 1 865  ? 93.160  146.031 77.995  1.00 22.16 ?  865  ARG B NE   1 
ATOM   13352 C CZ   . ARG B 1 865  ? 92.765  146.807 78.995  1.00 24.89 ?  865  ARG B CZ   1 
ATOM   13353 N NH1  . ARG B 1 865  ? 93.528  147.786 79.453  1.00 21.95 ?  865  ARG B NH1  1 
ATOM   13354 N NH2  . ARG B 1 865  ? 91.574  146.597 79.548  1.00 27.47 ?  865  ARG B NH2  1 
ATOM   13355 N N    . GLU B 1 866  ? 94.467  143.759 81.572  1.00 18.97 ?  866  GLU B N    1 
ATOM   13356 C CA   . GLU B 1 866  ? 94.112  144.341 82.864  1.00 22.34 ?  866  GLU B CA   1 
ATOM   13357 C C    . GLU B 1 866  ? 95.138  143.983 83.936  1.00 26.70 ?  866  GLU B C    1 
ATOM   13358 O O    . GLU B 1 866  ? 95.526  144.835 84.750  1.00 26.10 ?  866  GLU B O    1 
ATOM   13359 C CB   . GLU B 1 866  ? 92.720  143.868 83.281  1.00 21.39 ?  866  GLU B CB   1 
ATOM   13360 C CG   . GLU B 1 866  ? 92.026  144.773 84.283  1.00 26.90 ?  866  GLU B CG   1 
ATOM   13361 C CD   . GLU B 1 866  ? 92.232  146.242 83.978  1.00 28.35 ?  866  GLU B CD   1 
ATOM   13362 O OE1  . GLU B 1 866  ? 91.708  146.713 82.946  1.00 25.35 ?  866  GLU B OE1  1 
ATOM   13363 O OE2  . GLU B 1 866  ? 92.917  146.926 84.767  1.00 29.70 ?  866  GLU B OE2  1 
ATOM   13364 N N    . LEU B 1 867  ? 95.583  142.722 83.951  1.00 24.94 ?  867  LEU B N    1 
ATOM   13365 C CA   . LEU B 1 867  ? 96.566  142.289 84.941  1.00 23.43 ?  867  LEU B CA   1 
ATOM   13366 C C    . LEU B 1 867  ? 97.897  143.010 84.750  1.00 23.17 ?  867  LEU B C    1 
ATOM   13367 O O    . LEU B 1 867  ? 98.524  143.447 85.726  1.00 23.62 ?  867  LEU B O    1 
ATOM   13368 C CB   . LEU B 1 867  ? 96.748  140.772 84.863  1.00 19.85 ?  867  LEU B CB   1 
ATOM   13369 C CG   . LEU B 1 867  ? 95.501  139.940 85.191  1.00 22.94 ?  867  LEU B CG   1 
ATOM   13370 C CD1  . LEU B 1 867  ? 95.759  138.446 85.032  1.00 23.41 ?  867  LEU B CD1  1 
ATOM   13371 C CD2  . LEU B 1 867  ? 94.953  140.260 86.573  1.00 22.87 ?  867  LEU B CD2  1 
ATOM   13372 N N    . LYS B 1 868  ? 98.332  143.163 83.496  1.00 21.54 ?  868  LYS B N    1 
ATOM   13373 C CA   . LYS B 1 868  ? 99.557  143.903 83.217  1.00 23.90 ?  868  LYS B CA   1 
ATOM   13374 C C    . LYS B 1 868  ? 99.426  145.362 83.635  1.00 27.66 ?  868  LYS B C    1 
ATOM   13375 O O    . LYS B 1 868  ? 100.369 145.943 84.186  1.00 31.69 ?  868  LYS B O    1 
ATOM   13376 C CB   . LYS B 1 868  ? 99.904  143.794 81.732  1.00 22.85 ?  868  LYS B CB   1 
ATOM   13377 C CG   . LYS B 1 868  ? 100.550 142.473 81.341  1.00 25.45 ?  868  LYS B CG   1 
ATOM   13378 C CD   . LYS B 1 868  ? 100.924 142.451 79.867  1.00 27.35 ?  868  LYS B CD   1 
ATOM   13379 C CE   . LYS B 1 868  ? 101.590 141.137 79.485  1.00 27.62 ?  868  LYS B CE   1 
ATOM   13380 N NZ   . LYS B 1 868  ? 101.913 141.071 78.032  1.00 27.39 ?  868  LYS B NZ   1 
ATOM   13381 N N    . HIS B 1 869  ? 98.257  145.965 83.396  1.00 21.57 ?  869  HIS B N    1 
ATOM   13382 C CA   . HIS B 1 869  ? 98.042  147.361 83.766  1.00 21.17 ?  869  HIS B CA   1 
ATOM   13383 C C    . HIS B 1 869  ? 98.132  147.560 85.276  1.00 21.98 ?  869  HIS B C    1 
ATOM   13384 O O    . HIS B 1 869  ? 98.820  148.475 85.752  1.00 24.93 ?  869  HIS B O    1 
ATOM   13385 C CB   . HIS B 1 869  ? 96.687  147.833 83.238  1.00 22.62 ?  869  HIS B CB   1 
ATOM   13386 C CG   . HIS B 1 869  ? 96.290  149.196 83.714  1.00 25.91 ?  869  HIS B CG   1 
ATOM   13387 N ND1  . HIS B 1 869  ? 95.498  149.395 84.823  1.00 24.19 ?  869  HIS B ND1  1 
ATOM   13388 C CD2  . HIS B 1 869  ? 96.572  150.428 83.227  1.00 27.73 ?  869  HIS B CD2  1 
ATOM   13389 C CE1  . HIS B 1 869  ? 95.311  150.691 85.001  1.00 25.73 ?  869  HIS B CE1  1 
ATOM   13390 N NE2  . HIS B 1 869  ? 95.952  151.340 84.046  1.00 29.41 ?  869  HIS B NE2  1 
ATOM   13391 N N    . ILE B 1 870  ? 97.453  146.705 86.050  1.00 18.47 ?  870  ILE B N    1 
ATOM   13392 C CA   . ILE B 1 870  ? 97.462  146.893 87.501  1.00 23.00 ?  870  ILE B CA   1 
ATOM   13393 C C    . ILE B 1 870  ? 98.848  146.597 88.073  1.00 22.54 ?  870  ILE B C    1 
ATOM   13394 O O    . ILE B 1 870  ? 99.319  147.294 88.986  1.00 22.09 ?  870  ILE B O    1 
ATOM   13395 C CB   . ILE B 1 870  ? 96.354  146.058 88.179  1.00 24.88 ?  870  ILE B CB   1 
ATOM   13396 C CG1  . ILE B 1 870  ? 96.394  146.231 89.699  1.00 21.95 ?  870  ILE B CG1  1 
ATOM   13397 C CG2  . ILE B 1 870  ? 96.463  144.586 87.846  1.00 24.06 ?  870  ILE B CG2  1 
ATOM   13398 C CD1  . ILE B 1 870  ? 95.582  147.404 90.198  1.00 21.16 ?  870  ILE B CD1  1 
ATOM   13399 N N    . SER B 1 871  ? 99.542  145.590 87.522  1.00 20.54 ?  871  SER B N    1 
ATOM   13400 C CA   . SER B 1 871  ? 100.896 145.289 87.978  1.00 19.65 ?  871  SER B CA   1 
ATOM   13401 C C    . SER B 1 871  ? 101.849 146.447 87.697  1.00 19.59 ?  871  SER B C    1 
ATOM   13402 O O    . SER B 1 871  ? 102.658 146.818 88.559  1.00 19.40 ?  871  SER B O    1 
ATOM   13403 C CB   . SER B 1 871  ? 101.395 144.008 87.311  1.00 18.92 ?  871  SER B CB   1 
ATOM   13404 O OG   . SER B 1 871  ? 102.367 143.358 88.110  1.00 17.43 ?  871  SER B OG   1 
ATOM   13405 N N    . GLU B 1 872  ? 101.757 147.037 86.500  1.00 18.74 ?  872  GLU B N    1 
ATOM   13406 C CA   . GLU B 1 872  ? 102.608 148.172 86.156  1.00 16.70 ?  872  GLU B CA   1 
ATOM   13407 C C    . GLU B 1 872  ? 102.325 149.370 87.053  1.00 18.06 ?  872  GLU B C    1 
ATOM   13408 O O    . GLU B 1 872  ? 103.257 150.051 87.500  1.00 21.89 ?  872  GLU B O    1 
ATOM   13409 C CB   . GLU B 1 872  ? 102.410 148.545 84.687  1.00 14.14 ?  872  GLU B CB   1 
ATOM   13410 C CG   . GLU B 1 872  ? 103.473 149.474 84.127  1.00 21.23 ?  872  GLU B CG   1 
ATOM   13411 C CD   . GLU B 1 872  ? 104.424 148.767 83.181  1.00 26.02 ?  872  GLU B CD   1 
ATOM   13412 O OE1  . GLU B 1 872  ? 104.013 147.763 82.562  1.00 22.65 ?  872  GLU B OE1  1 
ATOM   13413 O OE2  . GLU B 1 872  ? 105.583 149.215 83.056  1.00 26.17 ?  872  GLU B OE2  1 
ATOM   13414 N N    . THR B 1 873  ? 101.044 149.638 87.330  1.00 18.66 ?  873  THR B N    1 
ATOM   13415 C CA   . THR B 1 873  ? 100.688 150.766 88.188  1.00 17.79 ?  873  THR B CA   1 
ATOM   13416 C C    . THR B 1 873  ? 101.249 150.586 89.597  1.00 19.08 ?  873  THR B C    1 
ATOM   13417 O O    . THR B 1 873  ? 101.853 151.511 90.164  1.00 22.67 ?  873  THR B O    1 
ATOM   13418 C CB   . THR B 1 873  ? 99.165  150.928 88.219  1.00 19.81 ?  873  THR B CB   1 
ATOM   13419 O OG1  . THR B 1 873  ? 98.735  151.631 87.047  1.00 20.92 ?  873  THR B OG1  1 
ATOM   13420 C CG2  . THR B 1 873  ? 98.715  151.702 89.453  1.00 18.25 ?  873  THR B CG2  1 
ATOM   13421 N N    . GLY B 1 874  ? 101.086 149.386 90.164  1.00 16.98 ?  874  GLY B N    1 
ATOM   13422 C CA   . GLY B 1 874  ? 101.616 149.131 91.495  1.00 15.95 ?  874  GLY B CA   1 
ATOM   13423 C C    . GLY B 1 874  ? 103.129 149.224 91.557  1.00 17.72 ?  874  GLY B C    1 
ATOM   13424 O O    . GLY B 1 874  ? 103.688 149.810 92.492  1.00 16.98 ?  874  GLY B O    1 
ATOM   13425 N N    . ARG B 1 875  ? 103.812 148.660 90.554  1.00 17.14 ?  875  ARG B N    1 
ATOM   13426 C CA   . ARG B 1 875  ? 105.271 148.713 90.524  1.00 12.46 ?  875  ARG B CA   1 
ATOM   13427 C C    . ARG B 1 875  ? 105.772 150.149 90.415  1.00 14.84 ?  875  ARG B C    1 
ATOM   13428 O O    . ARG B 1 875  ? 106.726 150.534 91.105  1.00 24.47 ?  875  ARG B O    1 
ATOM   13429 C CB   . ARG B 1 875  ? 105.795 147.866 89.364  1.00 12.98 ?  875  ARG B CB   1 
ATOM   13430 C CG   . ARG B 1 875  ? 107.221 148.179 88.949  1.00 13.95 ?  875  ARG B CG   1 
ATOM   13431 C CD   . ARG B 1 875  ? 107.667 147.314 87.783  1.00 13.55 ?  875  ARG B CD   1 
ATOM   13432 N NE   . ARG B 1 875  ? 107.304 147.898 86.497  1.00 18.39 ?  875  ARG B NE   1 
ATOM   13433 C CZ   . ARG B 1 875  ? 107.960 148.890 85.910  1.00 23.16 ?  875  ARG B CZ   1 
ATOM   13434 N NH1  . ARG B 1 875  ? 109.035 149.430 86.461  1.00 20.90 ?  875  ARG B NH1  1 
ATOM   13435 N NH2  . ARG B 1 875  ? 107.529 149.349 84.739  1.00 23.58 ?  875  ARG B NH2  1 
ATOM   13436 N N    . LEU B 1 876  ? 105.134 150.959 89.563  1.00 12.60 ?  876  LEU B N    1 
ATOM   13437 C CA   . LEU B 1 876  ? 105.545 152.352 89.413  1.00 11.79 ?  876  LEU B CA   1 
ATOM   13438 C C    . LEU B 1 876  ? 105.337 153.138 90.701  1.00 16.69 ?  876  LEU B C    1 
ATOM   13439 O O    . LEU B 1 876  ? 106.201 153.933 91.098  1.00 18.45 ?  876  LEU B O    1 
ATOM   13440 C CB   . LEU B 1 876  ? 104.782 153.002 88.259  1.00 13.37 ?  876  LEU B CB   1 
ATOM   13441 C CG   . LEU B 1 876  ? 105.410 152.890 86.869  1.00 18.68 ?  876  LEU B CG   1 
ATOM   13442 C CD1  . LEU B 1 876  ? 104.802 153.917 85.927  1.00 18.90 ?  876  LEU B CD1  1 
ATOM   13443 C CD2  . LEU B 1 876  ? 106.920 153.052 86.940  1.00 18.31 ?  876  LEU B CD2  1 
ATOM   13444 N N    . GLN B 1 877  ? 104.199 152.926 91.373  1.00 16.76 ?  877  GLN B N    1 
ATOM   13445 C CA   . GLN B 1 877  ? 103.958 153.619 92.637  1.00 15.71 ?  877  GLN B CA   1 
ATOM   13446 C C    . GLN B 1 877  ? 104.998 153.237 93.685  1.00 12.13 ?  877  GLN B C    1 
ATOM   13447 O O    . GLN B 1 877  ? 105.536 154.108 94.386  1.00 20.39 ?  877  GLN B O    1 
ATOM   13448 C CB   . GLN B 1 877  ? 102.550 153.310 93.145  1.00 21.15 ?  877  GLN B CB   1 
ATOM   13449 C CG   . GLN B 1 877  ? 102.137 154.109 94.372  1.00 20.97 ?  877  GLN B CG   1 
ATOM   13450 C CD   . GLN B 1 877  ? 102.064 155.600 94.101  1.00 23.03 ?  877  GLN B CD   1 
ATOM   13451 O OE1  . GLN B 1 877  ? 102.511 156.413 94.910  1.00 27.08 ?  877  GLN B OE1  1 
ATOM   13452 N NE2  . GLN B 1 877  ? 101.490 155.966 92.960  1.00 19.67 ?  877  GLN B NE2  1 
ATOM   13453 N N    . VAL B 1 878  ? 105.314 151.942 93.785  1.00 2.22  ?  878  VAL B N    1 
ATOM   13454 C CA   . VAL B 1 878  ? 106.276 151.486 94.786  1.00 1.34  ?  878  VAL B CA   1 
ATOM   13455 C C    . VAL B 1 878  ? 107.662 152.053 94.500  1.00 5.24  ?  878  VAL B C    1 
ATOM   13456 O O    . VAL B 1 878  ? 108.362 152.508 95.415  1.00 9.25  ?  878  VAL B O    1 
ATOM   13457 C CB   . VAL B 1 878  ? 106.288 149.947 94.850  1.00 11.77 ?  878  VAL B CB   1 
ATOM   13458 C CG1  . VAL B 1 878  ? 107.496 149.445 95.624  1.00 7.01  ?  878  VAL B CG1  1 
ATOM   13459 C CG2  . VAL B 1 878  ? 105.008 149.441 95.487  1.00 17.09 ?  878  VAL B CG2  1 
ATOM   13460 N N    . VAL B 1 879  ? 108.075 152.057 93.229  1.00 11.46 ?  879  VAL B N    1 
ATOM   13461 C CA   . VAL B 1 879  ? 109.416 152.541 92.912  1.00 8.57  ?  879  VAL B CA   1 
ATOM   13462 C C    . VAL B 1 879  ? 109.520 154.054 93.110  1.00 11.09 ?  879  VAL B C    1 
ATOM   13463 O O    . VAL B 1 879  ? 110.562 154.551 93.560  1.00 12.11 ?  879  VAL B O    1 
ATOM   13464 C CB   . VAL B 1 879  ? 109.840 152.085 91.497  1.00 2.57  ?  879  VAL B CB   1 
ATOM   13465 C CG1  . VAL B 1 879  ? 109.209 152.924 90.398  1.00 7.47  ?  879  VAL B CG1  1 
ATOM   13466 C CG2  . VAL B 1 879  ? 111.352 152.102 91.373  1.00 7.73  ?  879  VAL B CG2  1 
ATOM   13467 N N    . LYS B 1 880  ? 108.446 154.809 92.834  1.00 13.80 ?  880  LYS B N    1 
ATOM   13468 C CA   . LYS B 1 880  ? 108.480 156.246 93.098  1.00 8.41  ?  880  LYS B CA   1 
ATOM   13469 C C    . LYS B 1 880  ? 108.569 156.534 94.591  1.00 6.20  ?  880  LYS B C    1 
ATOM   13470 O O    . LYS B 1 880  ? 109.334 157.412 95.019  1.00 14.93 ?  880  LYS B O    1 
ATOM   13471 C CB   . LYS B 1 880  ? 107.249 156.924 92.499  1.00 13.22 ?  880  LYS B CB   1 
ATOM   13472 C CG   . LYS B 1 880  ? 107.240 158.435 92.672  1.00 14.46 ?  880  LYS B CG   1 
ATOM   13473 C CD   . LYS B 1 880  ? 106.099 159.082 91.907  1.00 12.92 ?  880  LYS B CD   1 
ATOM   13474 C CE   . LYS B 1 880  ? 105.576 160.310 92.635  1.00 13.06 ?  880  LYS B CE   1 
ATOM   13475 N NZ   . LYS B 1 880  ? 105.377 160.057 94.089  1.00 17.78 ?  880  LYS B NZ   1 
ATOM   13476 N N    . GLU B 1 881  ? 107.796 155.799 95.400  1.00 10.20 ?  881  GLU B N    1 
ATOM   13477 C CA   . GLU B 1 881  ? 107.855 155.994 96.846  1.00 11.63 ?  881  GLU B CA   1 
ATOM   13478 C C    . GLU B 1 881  ? 109.231 155.638 97.399  1.00 12.31 ?  881  GLU B C    1 
ATOM   13479 O O    . GLU B 1 881  ? 109.751 156.334 98.279  1.00 18.25 ?  881  GLU B O    1 
ATOM   13480 C CB   . GLU B 1 881  ? 106.764 155.171 97.529  1.00 13.51 ?  881  GLU B CB   1 
ATOM   13481 C CG   . GLU B 1 881  ? 105.356 155.664 97.236  1.00 15.34 ?  881  GLU B CG   1 
ATOM   13482 C CD   . GLU B 1 881  ? 104.399 155.428 98.387  1.00 20.65 ?  881  GLU B CD   1 
ATOM   13483 O OE1  . GLU B 1 881  ? 103.923 154.284 98.540  1.00 17.84 ?  881  GLU B OE1  1 
ATOM   13484 O OE2  . GLU B 1 881  ? 104.116 156.389 99.133  1.00 23.64 ?  881  GLU B OE2  1 
ATOM   13485 N N    . LEU B 1 882  ? 109.842 154.565 96.886  1.00 8.08  ?  882  LEU B N    1 
ATOM   13486 C CA   . LEU B 1 882  ? 111.180 154.188 97.338  1.00 5.68  ?  882  LEU B CA   1 
ATOM   13487 C C    . LEU B 1 882  ? 112.219 155.234 96.947  1.00 7.11  ?  882  LEU B C    1 
ATOM   13488 O O    . LEU B 1 882  ? 113.131 155.534 97.729  1.00 10.57 ?  882  LEU B O    1 
ATOM   13489 C CB   . LEU B 1 882  ? 111.558 152.820 96.775  1.00 8.81  ?  882  LEU B CB   1 
ATOM   13490 C CG   . LEU B 1 882  ? 111.628 151.671 97.783  1.00 6.09  ?  882  LEU B CG   1 
ATOM   13491 C CD1  . LEU B 1 882  ? 110.342 151.582 98.585  1.00 7.93  ?  882  LEU B CD1  1 
ATOM   13492 C CD2  . LEU B 1 882  ? 111.919 150.356 97.078  1.00 6.94  ?  882  LEU B CD2  1 
ATOM   13493 N N    . GLY B 1 883  ? 112.100 155.800 95.742  1.00 9.39  ?  883  GLY B N    1 
ATOM   13494 C CA   . GLY B 1 883  ? 113.016 156.859 95.343  1.00 10.76 ?  883  GLY B CA   1 
ATOM   13495 C C    . GLY B 1 883  ? 112.900 158.097 96.213  1.00 9.18  ?  883  GLY B C    1 
ATOM   13496 O O    . GLY B 1 883  ? 113.910 158.692 96.604  1.00 11.43 ?  883  GLY B O    1 
ATOM   13497 N N    . LEU B 1 884  ? 111.668 158.498 96.540  1.00 6.44  ?  884  LEU B N    1 
ATOM   13498 C CA   . LEU B 1 884  ? 111.491 159.646 97.427  1.00 7.03  ?  884  LEU B CA   1 
ATOM   13499 C C    . LEU B 1 884  ? 112.009 159.351 98.833  1.00 12.31 ?  884  LEU B C    1 
ATOM   13500 O O    . LEU B 1 884  ? 112.585 160.232 99.488  1.00 17.79 ?  884  LEU B O    1 
ATOM   13501 C CB   . LEU B 1 884  ? 110.022 160.060 97.465  1.00 11.56 ?  884  LEU B CB   1 
ATOM   13502 C CG   . LEU B 1 884  ? 109.497 160.755 96.206  1.00 13.44 ?  884  LEU B CG   1 
ATOM   13503 C CD1  . LEU B 1 884  ? 108.140 161.387 96.470  1.00 12.79 ?  884  LEU B CD1  1 
ATOM   13504 C CD2  . LEU B 1 884  ? 110.487 161.797 95.706  1.00 10.45 ?  884  LEU B CD2  1 
ATOM   13505 N N    . LEU B 1 885  ? 111.817 158.115 99.308  1.00 13.69 ?  885  LEU B N    1 
ATOM   13506 C CA   . LEU B 1 885  ? 112.346 157.719 100.610 1.00 11.26 ?  885  LEU B CA   1 
ATOM   13507 C C    . LEU B 1 885  ? 113.868 157.784 100.633 1.00 14.00 ?  885  LEU B C    1 
ATOM   13508 O O    . LEU B 1 885  ? 114.465 158.159 101.649 1.00 14.45 ?  885  LEU B O    1 
ATOM   13509 C CB   . LEU B 1 885  ? 111.861 156.312 100.957 1.00 10.40 ?  885  LEU B CB   1 
ATOM   13510 C CG   . LEU B 1 885  ? 112.146 155.766 102.355 1.00 8.33  ?  885  LEU B CG   1 
ATOM   13511 C CD1  . LEU B 1 885  ? 111.090 156.234 103.341 1.00 10.44 ?  885  LEU B CD1  1 
ATOM   13512 C CD2  . LEU B 1 885  ? 112.208 154.249 102.312 1.00 9.98  ?  885  LEU B CD2  1 
ATOM   13513 N N    . GLN B 1 886  ? 114.513 157.404 99.527  1.00 15.14 ?  886  GLN B N    1 
ATOM   13514 C CA   . GLN B 1 886  ? 115.957 157.593 99.417  1.00 10.56 ?  886  GLN B CA   1 
ATOM   13515 C C    . GLN B 1 886  ? 116.322 159.070 99.432  1.00 8.33  ?  886  GLN B C    1 
ATOM   13516 O O    . GLN B 1 886  ? 117.318 159.467 100.049 1.00 8.83  ?  886  GLN B O    1 
ATOM   13517 C CB   . GLN B 1 886  ? 116.488 156.947 98.140  1.00 12.16 ?  886  GLN B CB   1 
ATOM   13518 C CG   . GLN B 1 886  ? 117.993 156.741 98.152  1.00 10.44 ?  886  GLN B CG   1 
ATOM   13519 C CD   . GLN B 1 886  ? 118.722 157.673 97.205  1.00 14.65 ?  886  GLN B CD   1 
ATOM   13520 O OE1  . GLN B 1 886  ? 118.138 158.195 96.257  1.00 14.66 ?  886  GLN B OE1  1 
ATOM   13521 N NE2  . GLN B 1 886  ? 120.007 157.889 97.460  1.00 13.40 ?  886  GLN B NE2  1 
ATOM   13522 N N    . ARG B 1 887  ? 115.535 159.895 98.738  1.00 12.22 ?  887  ARG B N    1 
ATOM   13523 C CA   . ARG B 1 887  ? 115.838 161.320 98.634  1.00 16.66 ?  887  ARG B CA   1 
ATOM   13524 C C    . ARG B 1 887  ? 115.752 162.024 99.985  1.00 18.10 ?  887  ARG B C    1 
ATOM   13525 O O    . ARG B 1 887  ? 116.524 162.954 100.245 1.00 14.55 ?  887  ARG B O    1 
ATOM   13526 C CB   . ARG B 1 887  ? 114.894 161.970 97.618  1.00 14.99 ?  887  ARG B CB   1 
ATOM   13527 C CG   . ARG B 1 887  ? 114.929 163.490 97.569  1.00 15.31 ?  887  ARG B CG   1 
ATOM   13528 C CD   . ARG B 1 887  ? 116.217 164.003 96.946  1.00 15.92 ?  887  ARG B CD   1 
ATOM   13529 N NE   . ARG B 1 887  ? 116.024 165.282 96.272  1.00 18.97 ?  887  ARG B NE   1 
ATOM   13530 C CZ   . ARG B 1 887  ? 117.009 166.042 95.812  1.00 18.76 ?  887  ARG B CZ   1 
ATOM   13531 N NH1  . ARG B 1 887  ? 118.276 165.680 95.933  1.00 18.37 ?  887  ARG B NH1  1 
ATOM   13532 N NH2  . ARG B 1 887  ? 116.715 167.195 95.217  1.00 19.93 ?  887  ARG B NH2  1 
ATOM   13533 N N    . GLU B 1 888  ? 114.844 161.580 100.860 1.00 21.92 ?  888  GLU B N    1 
ATOM   13534 C CA   . GLU B 1 888  ? 114.583 162.312 102.100 1.00 17.70 ?  888  GLU B CA   1 
ATOM   13535 C C    . GLU B 1 888  ? 115.794 162.321 103.037 1.00 18.07 ?  888  GLU B C    1 
ATOM   13536 O O    . GLU B 1 888  ? 116.101 163.352 103.647 1.00 19.13 ?  888  GLU B O    1 
ATOM   13537 C CB   . GLU B 1 888  ? 113.358 161.725 102.801 1.00 17.03 ?  888  GLU B CB   1 
ATOM   13538 C CG   . GLU B 1 888  ? 112.875 162.536 103.992 1.00 20.29 ?  888  GLU B CG   1 
ATOM   13539 C CD   . GLU B 1 888  ? 111.459 162.180 104.406 1.00 23.06 ?  888  GLU B CD   1 
ATOM   13540 O OE1  . GLU B 1 888  ? 111.139 160.974 104.462 1.00 18.32 ?  888  GLU B OE1  1 
ATOM   13541 O OE2  . GLU B 1 888  ? 110.665 163.107 104.670 1.00 23.41 ?  888  GLU B OE2  1 
ATOM   13542 N N    . HIS B 1 889  ? 116.502 161.189 103.164 1.00 20.82 ?  889  HIS B N    1 
ATOM   13543 C CA   . HIS B 1 889  ? 117.652 161.106 104.066 1.00 15.41 ?  889  HIS B CA   1 
ATOM   13544 C C    . HIS B 1 889  ? 118.736 160.209 103.475 1.00 13.02 ?  889  HIS B C    1 
ATOM   13545 O O    . HIS B 1 889  ? 118.589 158.980 103.471 1.00 12.81 ?  889  HIS B O    1 
ATOM   13546 C CB   . HIS B 1 889  ? 117.233 160.577 105.438 1.00 11.94 ?  889  HIS B CB   1 
ATOM   13547 C CG   . HIS B 1 889  ? 116.045 159.671 105.395 1.00 14.38 ?  889  HIS B CG   1 
ATOM   13548 N ND1  . HIS B 1 889  ? 114.751 160.140 105.340 1.00 12.44 ?  889  HIS B ND1  1 
ATOM   13549 C CD2  . HIS B 1 889  ? 115.955 158.321 105.397 1.00 17.28 ?  889  HIS B CD2  1 
ATOM   13550 C CE1  . HIS B 1 889  ? 113.915 159.118 105.297 1.00 18.76 ?  889  HIS B CE1  1 
ATOM   13551 N NE2  . HIS B 1 889  ? 114.620 158.003 105.339 1.00 17.02 ?  889  HIS B NE2  1 
ATOM   13552 N N    . PRO B 1 890  ? 119.842 160.778 102.985 1.00 11.17 ?  890  PRO B N    1 
ATOM   13553 C CA   . PRO B 1 890  ? 120.807 159.980 102.212 1.00 15.35 ?  890  PRO B CA   1 
ATOM   13554 C C    . PRO B 1 890  ? 121.681 159.033 103.026 1.00 12.03 ?  890  PRO B C    1 
ATOM   13555 O O    . PRO B 1 890  ? 122.039 157.962 102.527 1.00 14.26 ?  890  PRO B O    1 
ATOM   13556 C CB   . PRO B 1 890  ? 121.667 161.048 101.523 1.00 13.77 ?  890  PRO B CB   1 
ATOM   13557 C CG   . PRO B 1 890  ? 121.544 162.252 102.384 1.00 11.49 ?  890  PRO B CG   1 
ATOM   13558 C CD   . PRO B 1 890  ? 120.176 162.213 102.990 1.00 8.14  ?  890  PRO B CD   1 
ATOM   13559 N N    . GLY B 1 891  ? 122.048 159.412 104.252 1.00 7.74  ?  891  GLY B N    1 
ATOM   13560 C CA   . GLY B 1 891  ? 122.999 158.608 105.010 1.00 4.63  ?  891  GLY B CA   1 
ATOM   13561 C C    . GLY B 1 891  ? 122.465 157.233 105.369 1.00 6.27  ?  891  GLY B C    1 
ATOM   13562 O O    . GLY B 1 891  ? 123.144 156.215 105.182 1.00 12.45 ?  891  GLY B O    1 
ATOM   13563 N N    . ILE B 1 892  ? 121.230 157.184 105.871 1.00 11.67 ?  892  ILE B N    1 
ATOM   13564 C CA   . ILE B 1 892  ? 120.613 155.916 106.240 1.00 10.23 ?  892  ILE B CA   1 
ATOM   13565 C C    . ILE B 1 892  ? 120.403 155.044 105.007 1.00 7.48  ?  892  ILE B C    1 
ATOM   13566 O O    . ILE B 1 892  ? 120.590 153.821 105.054 1.00 14.94 ?  892  ILE B O    1 
ATOM   13567 C CB   . ILE B 1 892  ? 119.293 156.176 106.985 1.00 9.35  ?  892  ILE B CB   1 
ATOM   13568 C CG1  . ILE B 1 892  ? 119.462 157.320 107.991 1.00 9.12  ?  892  ILE B CG1  1 
ATOM   13569 C CG2  . ILE B 1 892  ? 118.813 154.919 107.667 1.00 7.66  ?  892  ILE B CG2  1 
ATOM   13570 C CD1  . ILE B 1 892  ? 120.135 156.919 109.283 1.00 9.12  ?  892  ILE B CD1  1 
ATOM   13571 N N    . ALA B 1 893  ? 120.013 155.661 103.887 1.00 0.00  ?  893  ALA B N    1 
ATOM   13572 C CA   . ALA B 1 893  ? 119.806 154.914 102.651 1.00 0.00  ?  893  ALA B CA   1 
ATOM   13573 C C    . ALA B 1 893  ? 121.108 154.310 102.139 1.00 1.39  ?  893  ALA B C    1 
ATOM   13574 O O    . ALA B 1 893  ? 121.135 153.151 101.703 1.00 11.53 ?  893  ALA B O    1 
ATOM   13575 C CB   . ALA B 1 893  ? 119.183 155.822 101.593 1.00 6.70  ?  893  ALA B CB   1 
ATOM   13576 N N    . VAL B 1 894  ? 122.199 155.079 102.187 1.00 5.90  ?  894  VAL B N    1 
ATOM   13577 C CA   . VAL B 1 894  ? 123.495 154.559 101.759 1.00 2.61  ?  894  VAL B CA   1 
ATOM   13578 C C    . VAL B 1 894  ? 123.929 153.412 102.661 1.00 1.07  ?  894  VAL B C    1 
ATOM   13579 O O    . VAL B 1 894  ? 124.435 152.386 102.186 1.00 7.80  ?  894  VAL B O    1 
ATOM   13580 C CB   . VAL B 1 894  ? 124.540 155.691 101.726 1.00 0.17  ?  894  VAL B CB   1 
ATOM   13581 C CG1  . VAL B 1 894  ? 125.944 155.128 101.621 1.00 3.13  ?  894  VAL B CG1  1 
ATOM   13582 C CG2  . VAL B 1 894  ? 124.267 156.621 100.562 1.00 3.91  ?  894  VAL B CG2  1 
ATOM   13583 N N    . SER B 1 895  ? 123.702 153.551 103.971 1.00 2.97  ?  895  SER B N    1 
ATOM   13584 C CA   . SER B 1 895  ? 124.072 152.493 104.907 1.00 0.96  ?  895  SER B CA   1 
ATOM   13585 C C    . SER B 1 895  ? 123.308 151.201 104.630 1.00 1.00  ?  895  SER B C    1 
ATOM   13586 O O    . SER B 1 895  ? 123.900 150.112 104.577 1.00 7.26  ?  895  SER B O    1 
ATOM   13587 C CB   . SER B 1 895  ? 123.828 152.961 106.340 1.00 4.71  ?  895  SER B CB   1 
ATOM   13588 O OG   . SER B 1 895  ? 123.934 151.881 107.247 1.00 9.11  ?  895  SER B OG   1 
ATOM   13589 N N    . VAL B 1 896  ? 121.990 151.299 104.431 1.00 0.00  ?  896  VAL B N    1 
ATOM   13590 C CA   . VAL B 1 896  ? 121.199 150.084 104.242 1.00 0.41  ?  896  VAL B CA   1 
ATOM   13591 C C    . VAL B 1 896  ? 121.508 149.438 102.893 1.00 3.54  ?  896  VAL B C    1 
ATOM   13592 O O    . VAL B 1 896  ? 121.567 148.205 102.782 1.00 7.61  ?  896  VAL B O    1 
ATOM   13593 C CB   . VAL B 1 896  ? 119.692 150.364 104.429 1.00 0.00  ?  896  VAL B CB   1 
ATOM   13594 C CG1  . VAL B 1 896  ? 119.173 151.387 103.450 1.00 1.84  ?  896  VAL B CG1  1 
ATOM   13595 C CG2  . VAL B 1 896  ? 118.902 149.081 104.298 1.00 7.15  ?  896  VAL B CG2  1 
ATOM   13596 N N    . LYS B 1 897  ? 121.745 150.246 101.853 1.00 2.10  ?  897  LYS B N    1 
ATOM   13597 C CA   . LYS B 1 897  ? 122.070 149.670 100.551 1.00 0.00  ?  897  LYS B CA   1 
ATOM   13598 C C    . LYS B 1 897  ? 123.441 148.998 100.567 1.00 0.00  ?  897  LYS B C    1 
ATOM   13599 O O    . LYS B 1 897  ? 123.630 147.940 99.948  1.00 9.65  ?  897  LYS B O    1 
ATOM   13600 C CB   . LYS B 1 897  ? 121.998 150.751 99.477  1.00 0.00  ?  897  LYS B CB   1 
ATOM   13601 C CG   . LYS B 1 897  ? 120.662 150.797 98.754  1.00 0.00  ?  897  LYS B CG   1 
ATOM   13602 C CD   . LYS B 1 897  ? 120.255 152.227 98.452  1.00 0.00  ?  897  LYS B CD   1 
ATOM   13603 C CE   . LYS B 1 897  ? 118.910 152.289 97.755  1.00 3.13  ?  897  LYS B CE   1 
ATOM   13604 N NZ   . LYS B 1 897  ? 118.645 153.634 97.181  1.00 10.92 ?  897  LYS B NZ   1 
ATOM   13605 N N    . THR B 1 898  ? 124.406 149.589 101.282 1.00 3.59  ?  898  THR B N    1 
ATOM   13606 C CA   . THR B 1 898  ? 125.711 148.954 101.437 1.00 0.00  ?  898  THR B CA   1 
ATOM   13607 C C    . THR B 1 898  ? 125.594 147.626 102.176 1.00 0.76  ?  898  THR B C    1 
ATOM   13608 O O    . THR B 1 898  ? 126.233 146.636 101.795 1.00 2.41  ?  898  THR B O    1 
ATOM   13609 C CB   . THR B 1 898  ? 126.665 149.893 102.176 1.00 0.00  ?  898  THR B CB   1 
ATOM   13610 O OG1  . THR B 1 898  ? 126.776 151.127 101.458 1.00 0.32  ?  898  THR B OG1  1 
ATOM   13611 C CG2  . THR B 1 898  ? 128.040 149.270 102.298 1.00 4.24  ?  898  THR B CG2  1 
ATOM   13612 N N    . ARG B 1 899  ? 124.775 147.586 103.233 1.00 0.00  ?  899  ARG B N    1 
ATOM   13613 C CA   . ARG B 1 899  ? 124.563 146.332 103.953 1.00 4.28  ?  899  ARG B CA   1 
ATOM   13614 C C    . ARG B 1 899  ? 123.926 145.275 103.059 1.00 0.65  ?  899  ARG B C    1 
ATOM   13615 O O    . ARG B 1 899  ? 124.305 144.097 103.114 1.00 6.54  ?  899  ARG B O    1 
ATOM   13616 C CB   . ARG B 1 899  ? 123.704 146.576 105.192 1.00 0.00  ?  899  ARG B CB   1 
ATOM   13617 C CG   . ARG B 1 899  ? 123.623 145.385 106.132 1.00 2.44  ?  899  ARG B CG   1 
ATOM   13618 C CD   . ARG B 1 899  ? 123.182 145.804 107.524 1.00 3.74  ?  899  ARG B CD   1 
ATOM   13619 N NE   . ARG B 1 899  ? 121.784 146.215 107.561 1.00 8.12  ?  899  ARG B NE   1 
ATOM   13620 C CZ   . ARG B 1 899  ? 121.375 147.443 107.850 1.00 9.52  ?  899  ARG B CZ   1 
ATOM   13621 N NH1  . ARG B 1 899  ? 122.234 148.409 108.129 1.00 7.95  ?  899  ARG B NH1  1 
ATOM   13622 N NH2  . ARG B 1 899  ? 120.072 147.708 107.861 1.00 4.00  ?  899  ARG B NH2  1 
ATOM   13623 N N    . GLN B 1 900  ? 122.964 145.679 102.222 1.00 0.00  ?  900  GLN B N    1 
ATOM   13624 C CA   . GLN B 1 900  ? 122.337 144.748 101.285 1.00 5.29  ?  900  GLN B CA   1 
ATOM   13625 C C    . GLN B 1 900  ? 123.360 144.161 100.317 1.00 0.71  ?  900  GLN B C    1 
ATOM   13626 O O    . GLN B 1 900  ? 123.390 142.944 100.082 1.00 7.07  ?  900  GLN B O    1 
ATOM   13627 C CB   . GLN B 1 900  ? 121.226 145.459 100.511 1.00 2.32  ?  900  GLN B CB   1 
ATOM   13628 C CG   . GLN B 1 900  ? 119.847 145.376 101.140 1.00 3.44  ?  900  GLN B CG   1 
ATOM   13629 C CD   . GLN B 1 900  ? 118.744 145.762 100.169 1.00 2.19  ?  900  GLN B CD   1 
ATOM   13630 O OE1  . GLN B 1 900  ? 118.745 146.861 99.615  1.00 1.07  ?  900  GLN B OE1  1 
ATOM   13631 N NE2  . GLN B 1 900  ? 117.800 144.853 99.952  1.00 2.96  ?  900  GLN B NE2  1 
ATOM   13632 N N    . ALA B 1 901  ? 124.215 145.019 99.749  1.00 0.00  ?  901  ALA B N    1 
ATOM   13633 C CA   . ALA B 1 901  ? 125.213 144.548 98.791  1.00 0.00  ?  901  ALA B CA   1 
ATOM   13634 C C    . ALA B 1 901  ? 126.214 143.598 99.442  1.00 0.00  ?  901  ALA B C    1 
ATOM   13635 O O    . ALA B 1 901  ? 126.560 142.554 98.867  1.00 9.91  ?  901  ALA B O    1 
ATOM   13636 C CB   . ALA B 1 901  ? 125.935 145.737 98.162  1.00 0.00  ?  901  ALA B CB   1 
ATOM   13637 N N    . ILE B 1 902  ? 126.685 143.938 100.645 1.00 0.16  ?  902  ILE B N    1 
ATOM   13638 C CA   . ILE B 1 902  ? 127.649 143.081 101.332 1.00 0.00  ?  902  ILE B CA   1 
ATOM   13639 C C    . ILE B 1 902  ? 127.023 141.736 101.684 1.00 0.77  ?  902  ILE B C    1 
ATOM   13640 O O    . ILE B 1 902  ? 127.666 140.686 101.554 1.00 6.09  ?  902  ILE B O    1 
ATOM   13641 C CB   . ILE B 1 902  ? 128.211 143.797 102.574 1.00 0.00  ?  902  ILE B CB   1 
ATOM   13642 C CG1  . ILE B 1 902  ? 128.991 145.043 102.159 1.00 0.00  ?  902  ILE B CG1  1 
ATOM   13643 C CG2  . ILE B 1 902  ? 129.118 142.874 103.368 1.00 3.62  ?  902  ILE B CG2  1 
ATOM   13644 C CD1  . ILE B 1 902  ? 129.515 145.846 103.323 1.00 4.69  ?  902  ILE B CD1  1 
ATOM   13645 N N    . ARG B 1 903  ? 125.759 141.741 102.121 1.00 0.18  ?  903  ARG B N    1 
ATOM   13646 C CA   . ARG B 1 903  ? 125.074 140.490 102.429 1.00 3.08  ?  903  ARG B CA   1 
ATOM   13647 C C    . ARG B 1 903  ? 124.932 139.612 101.190 1.00 0.00  ?  903  ARG B C    1 
ATOM   13648 O O    . ARG B 1 903  ? 125.122 138.390 101.262 1.00 7.98  ?  903  ARG B O    1 
ATOM   13649 C CB   . ARG B 1 903  ? 123.707 140.788 103.042 1.00 0.00  ?  903  ARG B CB   1 
ATOM   13650 C CG   . ARG B 1 903  ? 122.868 139.566 103.357 1.00 1.13  ?  903  ARG B CG   1 
ATOM   13651 C CD   . ARG B 1 903  ? 121.519 139.965 103.939 1.00 3.24  ?  903  ARG B CD   1 
ATOM   13652 N NE   . ARG B 1 903  ? 120.553 140.323 102.907 1.00 6.97  ?  903  ARG B NE   1 
ATOM   13653 C CZ   . ARG B 1 903  ? 119.704 141.338 102.994 1.00 8.35  ?  903  ARG B CZ   1 
ATOM   13654 N NH1  . ARG B 1 903  ? 119.674 142.125 104.057 1.00 6.66  ?  903  ARG B NH1  1 
ATOM   13655 N NH2  . ARG B 1 903  ? 118.864 141.570 101.989 1.00 8.61  ?  903  ARG B NH2  1 
ATOM   13656 N N    . THR B 1 904  ? 124.611 140.220 100.043 1.00 0.00  ?  904  THR B N    1 
ATOM   13657 C CA   . THR B 1 904  ? 124.516 139.460 98.797  1.00 0.17  ?  904  THR B CA   1 
ATOM   13658 C C    . THR B 1 904  ? 125.852 138.815 98.438  1.00 0.00  ?  904  THR B C    1 
ATOM   13659 O O    . THR B 1 904  ? 125.912 137.622 98.098  1.00 7.96  ?  904  THR B O    1 
ATOM   13660 C CB   . THR B 1 904  ? 124.043 140.376 97.667  1.00 0.00  ?  904  THR B CB   1 
ATOM   13661 O OG1  . THR B 1 904  ? 122.679 140.750 97.893  1.00 8.62  ?  904  THR B OG1  1 
ATOM   13662 C CG2  . THR B 1 904  ? 124.155 139.680 96.321  1.00 0.00  ?  904  THR B CG2  1 
ATOM   13663 N N    . ILE B 1 905  ? 126.940 139.588 98.530  1.00 0.00  ?  905  ILE B N    1 
ATOM   13664 C CA   . ILE B 1 905  ? 128.259 139.060 98.178  1.00 0.00  ?  905  ILE B CA   1 
ATOM   13665 C C    . ILE B 1 905  ? 128.656 137.921 99.111  1.00 0.00  ?  905  ILE B C    1 
ATOM   13666 O O    . ILE B 1 905  ? 129.179 136.889 98.668  1.00 4.08  ?  905  ILE B O    1 
ATOM   13667 C CB   . ILE B 1 905  ? 129.310 140.185 98.183  1.00 0.00  ?  905  ILE B CB   1 
ATOM   13668 C CG1  . ILE B 1 905  ? 128.979 141.234 97.128  1.00 0.00  ?  905  ILE B CG1  1 
ATOM   13669 C CG2  . ILE B 1 905  ? 130.694 139.624 97.921  1.00 1.36  ?  905  ILE B CG2  1 
ATOM   13670 C CD1  . ILE B 1 905  ? 129.929 142.401 97.122  1.00 0.28  ?  905  ILE B CD1  1 
ATOM   13671 N N    . LEU B 1 906  ? 128.414 138.086 100.416 1.00 1.99  ?  906  LEU B N    1 
ATOM   13672 C CA   . LEU B 1 906  ? 128.782 137.045 101.372 1.00 0.61  ?  906  LEU B CA   1 
ATOM   13673 C C    . LEU B 1 906  ? 127.970 135.773 101.161 1.00 0.00  ?  906  LEU B C    1 
ATOM   13674 O O    . LEU B 1 906  ? 128.513 134.664 101.256 1.00 6.14  ?  906  LEU B O    1 
ATOM   13675 C CB   . LEU B 1 906  ? 128.617 137.558 102.801 1.00 0.93  ?  906  LEU B CB   1 
ATOM   13676 C CG   . LEU B 1 906  ? 129.597 138.649 103.235 1.00 0.00  ?  906  LEU B CG   1 
ATOM   13677 C CD1  . LEU B 1 906  ? 129.193 139.225 104.579 1.00 5.45  ?  906  LEU B CD1  1 
ATOM   13678 C CD2  . LEU B 1 906  ? 131.013 138.104 103.283 1.00 5.17  ?  906  LEU B CD2  1 
ATOM   13679 N N    . ASN B 1 907  ? 126.672 135.909 100.863 1.00 1.18  ?  907  ASN B N    1 
ATOM   13680 C CA   . ASN B 1 907  ? 125.852 134.733 100.584 1.00 0.64  ?  907  ASN B CA   1 
ATOM   13681 C C    . ASN B 1 907  ? 126.347 133.990 99.349  1.00 3.23  ?  907  ASN B C    1 
ATOM   13682 O O    . ASN B 1 907  ? 126.415 132.753 99.340  1.00 9.90  ?  907  ASN B O    1 
ATOM   13683 C CB   . ASN B 1 907  ? 124.391 135.144 100.405 1.00 4.61  ?  907  ASN B CB   1 
ATOM   13684 C CG   . ASN B 1 907  ? 123.738 135.558 101.707 1.00 10.87 ?  907  ASN B CG   1 
ATOM   13685 O OD1  . ASN B 1 907  ? 124.072 135.047 102.774 1.00 15.16 ?  907  ASN B OD1  1 
ATOM   13686 N ND2  . ASN B 1 907  ? 122.797 136.490 101.624 1.00 7.57  ?  907  ASN B ND2  1 
ATOM   13687 N N    . HIS B 1 908  ? 126.713 134.728 98.298  1.00 5.00  ?  908  HIS B N    1 
ATOM   13688 C CA   . HIS B 1 908  ? 127.185 134.066 97.085  1.00 0.78  ?  908  HIS B CA   1 
ATOM   13689 C C    . HIS B 1 908  ? 128.542 133.401 97.298  1.00 1.51  ?  908  HIS B C    1 
ATOM   13690 O O    . HIS B 1 908  ? 128.808 132.328 96.741  1.00 6.75  ?  908  HIS B O    1 
ATOM   13691 C CB   . HIS B 1 908  ? 127.230 135.062 95.932  1.00 0.85  ?  908  HIS B CB   1 
ATOM   13692 C CG   . HIS B 1 908  ? 125.901 135.274 95.279  1.00 0.27  ?  908  HIS B CG   1 
ATOM   13693 N ND1  . HIS B 1 908  ? 124.740 135.451 96.000  1.00 2.77  ?  908  HIS B ND1  1 
ATOM   13694 C CD2  . HIS B 1 908  ? 125.544 135.324 93.974  1.00 6.85  ?  908  HIS B CD2  1 
ATOM   13695 C CE1  . HIS B 1 908  ? 123.726 135.607 95.168  1.00 5.25  ?  908  HIS B CE1  1 
ATOM   13696 N NE2  . HIS B 1 908  ? 124.187 135.534 93.933  1.00 9.60  ?  908  HIS B NE2  1 
ATOM   13697 N N    . SER B 1 909  ? 129.409 134.007 98.116  1.00 4.29  ?  909  SER B N    1 
ATOM   13698 C CA   . SER B 1 909  ? 130.689 133.370 98.423  1.00 2.95  ?  909  SER B CA   1 
ATOM   13699 C C    . SER B 1 909  ? 130.496 132.103 99.251  1.00 1.96  ?  909  SER B C    1 
ATOM   13700 O O    . SER B 1 909  ? 131.219 131.115 99.066  1.00 7.36  ?  909  SER B O    1 
ATOM   13701 C CB   . SER B 1 909  ? 131.605 134.352 99.149  1.00 2.79  ?  909  SER B CB   1 
ATOM   13702 O OG   . SER B 1 909  ? 131.518 134.184 100.550 1.00 7.48  ?  909  SER B OG   1 
ATOM   13703 N N    . ARG B 1 910  ? 129.523 132.111 100.168 1.00 0.82  ?  910  ARG B N    1 
ATOM   13704 C CA   . ARG B 1 910  ? 129.195 130.899 100.914 1.00 0.00  ?  910  ARG B CA   1 
ATOM   13705 C C    . ARG B 1 910  ? 128.680 129.802 99.987  1.00 5.49  ?  910  ARG B C    1 
ATOM   13706 O O    . ARG B 1 910  ? 129.019 128.621 100.154 1.00 12.00 ?  910  ARG B O    1 
ATOM   13707 C CB   . ARG B 1 910  ? 128.164 131.220 101.993 1.00 1.86  ?  910  ARG B CB   1 
ATOM   13708 C CG   . ARG B 1 910  ? 127.823 130.060 102.908 1.00 7.53  ?  910  ARG B CG   1 
ATOM   13709 C CD   . ARG B 1 910  ? 126.658 130.413 103.818 1.00 11.95 ?  910  ARG B CD   1 
ATOM   13710 N NE   . ARG B 1 910  ? 126.514 131.854 103.989 1.00 16.14 ?  910  ARG B NE   1 
ATOM   13711 C CZ   . ARG B 1 910  ? 126.763 132.504 105.118 1.00 11.44 ?  910  ARG B CZ   1 
ATOM   13712 N NH1  . ARG B 1 910  ? 127.167 131.869 106.206 1.00 13.82 ?  910  ARG B NH1  1 
ATOM   13713 N NH2  . ARG B 1 910  ? 126.601 133.823 105.156 1.00 6.97  ?  910  ARG B NH2  1 
ATOM   13714 N N    . GLU B 1 911  ? 127.854 130.176 99.004  1.00 8.29  ?  911  GLU B N    1 
ATOM   13715 C CA   . GLU B 1 911  ? 127.392 129.207 98.012  1.00 6.77  ?  911  GLU B CA   1 
ATOM   13716 C C    . GLU B 1 911  ? 128.557 128.635 97.210  1.00 4.90  ?  911  GLU B C    1 
ATOM   13717 O O    . GLU B 1 911  ? 128.580 127.437 96.902  1.00 11.03 ?  911  GLU B O    1 
ATOM   13718 C CB   . GLU B 1 911  ? 126.375 129.855 97.074  1.00 9.90  ?  911  GLU B CB   1 
ATOM   13719 C CG   . GLU B 1 911  ? 124.936 129.759 97.545  1.00 10.98 ?  911  GLU B CG   1 
ATOM   13720 C CD   . GLU B 1 911  ? 123.996 130.602 96.706  1.00 12.96 ?  911  GLU B CD   1 
ATOM   13721 O OE1  . GLU B 1 911  ? 124.192 130.664 95.474  1.00 9.65  ?  911  GLU B OE1  1 
ATOM   13722 O OE2  . GLU B 1 911  ? 123.063 131.203 97.278  1.00 13.33 ?  911  GLU B OE2  1 
ATOM   13723 N N    . THR B 1 912  ? 129.525 129.483 96.853  1.00 6.52  ?  912  THR B N    1 
ATOM   13724 C CA   . THR B 1 912  ? 130.711 129.010 96.140  1.00 6.24  ?  912  THR B CA   1 
ATOM   13725 C C    . THR B 1 912  ? 131.513 128.028 96.989  1.00 7.31  ?  912  THR B C    1 
ATOM   13726 O O    . THR B 1 912  ? 132.002 127.010 96.481  1.00 12.14 ?  912  THR B O    1 
ATOM   13727 C CB   . THR B 1 912  ? 131.576 130.202 95.727  1.00 2.85  ?  912  THR B CB   1 
ATOM   13728 O OG1  . THR B 1 912  ? 130.877 130.983 94.751  1.00 3.61  ?  912  THR B OG1  1 
ATOM   13729 C CG2  . THR B 1 912  ? 132.896 129.740 95.130  1.00 1.78  ?  912  THR B CG2  1 
ATOM   13730 N N    . ILE B 1 913  ? 131.649 128.313 98.288  1.00 12.90 ?  913  ILE B N    1 
ATOM   13731 C CA   . ILE B 1 913  ? 132.351 127.401 99.192  1.00 11.54 ?  913  ILE B CA   1 
ATOM   13732 C C    . ILE B 1 913  ? 131.644 126.051 99.250  1.00 7.03  ?  913  ILE B C    1 
ATOM   13733 O O    . ILE B 1 913  ? 132.284 124.992 99.175  1.00 7.62  ?  913  ILE B O    1 
ATOM   13734 C CB   . ILE B 1 913  ? 132.481 128.030 100.593 1.00 10.71 ?  913  ILE B CB   1 
ATOM   13735 C CG1  . ILE B 1 913  ? 133.620 129.046 100.625 1.00 7.25  ?  913  ILE B CG1  1 
ATOM   13736 C CG2  . ILE B 1 913  ? 132.710 126.966 101.657 1.00 8.44  ?  913  ILE B CG2  1 
ATOM   13737 C CD1  . ILE B 1 913  ? 133.418 130.148 101.634 1.00 9.77  ?  913  ILE B CD1  1 
ATOM   13738 N N    . HIS B 1 914  ? 130.314 126.066 99.374  1.00 9.13  ?  914  HIS B N    1 
ATOM   13739 C CA   . HIS B 1 914  ? 129.564 124.813 99.436  1.00 11.18 ?  914  HIS B CA   1 
ATOM   13740 C C    . HIS B 1 914  ? 129.659 124.030 98.130  1.00 9.63  ?  914  HIS B C    1 
ATOM   13741 O O    . HIS B 1 914  ? 129.747 122.796 98.147  1.00 13.93 ?  914  HIS B O    1 
ATOM   13742 C CB   . HIS B 1 914  ? 128.105 125.087 99.796  1.00 17.03 ?  914  HIS B CB   1 
ATOM   13743 C CG   . HIS B 1 914  ? 127.894 125.403 101.242 1.00 12.68 ?  914  HIS B CG   1 
ATOM   13744 N ND1  . HIS B 1 914  ? 128.730 124.937 102.233 1.00 14.56 ?  914  HIS B ND1  1 
ATOM   13745 C CD2  . HIS B 1 914  ? 126.945 126.140 101.867 1.00 16.93 ?  914  HIS B CD2  1 
ATOM   13746 C CE1  . HIS B 1 914  ? 128.304 125.370 103.406 1.00 18.10 ?  914  HIS B CE1  1 
ATOM   13747 N NE2  . HIS B 1 914  ? 127.223 126.103 103.212 1.00 21.49 ?  914  HIS B NE2  1 
ATOM   13748 N N    . GLU B 1 915  ? 129.641 124.724 96.989  1.00 10.40 ?  915  GLU B N    1 
ATOM   13749 C CA   . GLU B 1 915  ? 129.779 124.035 95.709  1.00 8.99  ?  915  GLU B CA   1 
ATOM   13750 C C    . GLU B 1 915  ? 131.174 123.450 95.529  1.00 13.75 ?  915  GLU B C    1 
ATOM   13751 O O    . GLU B 1 915  ? 131.321 122.380 94.929  1.00 18.31 ?  915  GLU B O    1 
ATOM   13752 C CB   . GLU B 1 915  ? 129.447 124.984 94.560  1.00 13.59 ?  915  GLU B CB   1 
ATOM   13753 C CG   . GLU B 1 915  ? 127.983 124.966 94.158  1.00 17.22 ?  915  GLU B CG   1 
ATOM   13754 C CD   . GLU B 1 915  ? 127.486 126.321 93.698  1.00 16.46 ?  915  GLU B CD   1 
ATOM   13755 O OE1  . GLU B 1 915  ? 128.281 127.078 93.103  1.00 16.31 ?  915  GLU B OE1  1 
ATOM   13756 O OE2  . GLU B 1 915  ? 126.299 126.630 93.934  1.00 13.40 ?  915  GLU B OE2  1 
ATOM   13757 N N    . LEU B 1 916  ? 132.206 124.136 96.027  1.00 16.51 ?  916  LEU B N    1 
ATOM   13758 C CA   . LEU B 1 916  ? 133.551 123.568 96.007  1.00 10.40 ?  916  LEU B CA   1 
ATOM   13759 C C    . LEU B 1 916  ? 133.640 122.336 96.898  1.00 7.72  ?  916  LEU B C    1 
ATOM   13760 O O    . LEU B 1 916  ? 134.301 121.353 96.544  1.00 8.89  ?  916  LEU B O    1 
ATOM   13761 C CB   . LEU B 1 916  ? 134.571 124.615 96.450  1.00 10.93 ?  916  LEU B CB   1 
ATOM   13762 C CG   . LEU B 1 916  ? 135.378 125.314 95.359  1.00 7.34  ?  916  LEU B CG   1 
ATOM   13763 C CD1  . LEU B 1 916  ? 136.443 126.197 95.981  1.00 6.61  ?  916  LEU B CD1  1 
ATOM   13764 C CD2  . LEU B 1 916  ? 136.003 124.300 94.420  1.00 10.47 ?  916  LEU B CD2  1 
ATOM   13765 N N    . GLN B 1 917  ? 132.987 122.377 98.061  1.00 13.53 ?  917  GLN B N    1 
ATOM   13766 C CA   . GLN B 1 917  ? 133.014 121.236 98.972  1.00 12.28 ?  917  GLN B CA   1 
ATOM   13767 C C    . GLN B 1 917  ? 132.270 120.040 98.388  1.00 12.13 ?  917  GLN B C    1 
ATOM   13768 O O    . GLN B 1 917  ? 132.691 118.892 98.571  1.00 16.38 ?  917  GLN B O    1 
ATOM   13769 C CB   . GLN B 1 917  ? 132.421 121.636 100.323 1.00 11.56 ?  917  GLN B CB   1 
ATOM   13770 C CG   . GLN B 1 917  ? 132.614 120.612 101.426 1.00 8.86  ?  917  GLN B CG   1 
ATOM   13771 C CD   . GLN B 1 917  ? 131.936 121.019 102.718 1.00 15.76 ?  917  GLN B CD   1 
ATOM   13772 O OE1  . GLN B 1 917  ? 131.248 122.038 102.777 1.00 17.84 ?  917  GLN B OE1  1 
ATOM   13773 N NE2  . GLN B 1 917  ? 132.130 120.225 103.765 1.00 18.64 ?  917  GLN B NE2  1 
ATOM   13774 N N    . GLY B 1 918  ? 131.161 120.290 97.688  1.00 14.72 ?  918  GLY B N    1 
ATOM   13775 C CA   . GLY B 1 918  ? 130.405 119.203 97.088  1.00 10.28 ?  918  GLY B CA   1 
ATOM   13776 C C    . GLY B 1 918  ? 131.141 118.486 95.973  1.00 12.31 ?  918  GLY B C    1 
ATOM   13777 O O    . GLY B 1 918  ? 130.991 117.272 95.808  1.00 16.50 ?  918  GLY B O    1 
ATOM   13778 N N    . ALA B 1 919  ? 131.942 119.215 95.197  1.00 10.02 ?  919  ALA B N    1 
ATOM   13779 C CA   . ALA B 1 919  ? 132.671 118.635 94.076  1.00 10.18 ?  919  ALA B CA   1 
ATOM   13780 C C    . ALA B 1 919  ? 133.928 117.888 94.501  1.00 12.52 ?  919  ALA B C    1 
ATOM   13781 O O    . ALA B 1 919  ? 134.661 117.403 93.633  1.00 14.65 ?  919  ALA B O    1 
ATOM   13782 C CB   . ALA B 1 919  ? 133.040 119.726 93.068  1.00 8.33  ?  919  ALA B CB   1 
ATOM   13783 N N    . GLY B 1 920  ? 134.201 117.793 95.802  1.00 11.59 ?  920  GLY B N    1 
ATOM   13784 C CA   . GLY B 1 920  ? 135.342 117.060 96.303  1.00 8.92  ?  920  GLY B CA   1 
ATOM   13785 C C    . GLY B 1 920  ? 136.646 117.821 96.313  1.00 10.87 ?  920  GLY B C    1 
ATOM   13786 O O    . GLY B 1 920  ? 137.604 117.362 96.947  1.00 8.73  ?  920  GLY B O    1 
ATOM   13787 N N    . LEU B 1 921  ? 136.712 118.982 95.659  1.00 16.92 ?  921  LEU B N    1 
ATOM   13788 C CA   . LEU B 1 921  ? 137.954 119.739 95.554  1.00 14.89 ?  921  LEU B CA   1 
ATOM   13789 C C    . LEU B 1 921  ? 138.364 120.399 96.864  1.00 16.99 ?  921  LEU B C    1 
ATOM   13790 O O    . LEU B 1 921  ? 139.486 120.909 96.953  1.00 10.81 ?  921  LEU B O    1 
ATOM   13791 C CB   . LEU B 1 921  ? 137.818 120.797 94.459  1.00 10.66 ?  921  LEU B CB   1 
ATOM   13792 C CG   . LEU B 1 921  ? 137.377 120.263 93.095  1.00 14.51 ?  921  LEU B CG   1 
ATOM   13793 C CD1  . LEU B 1 921  ? 136.777 121.371 92.244  1.00 17.49 ?  921  LEU B CD1  1 
ATOM   13794 C CD2  . LEU B 1 921  ? 138.538 119.596 92.374  1.00 15.84 ?  921  LEU B CD2  1 
ATOM   13795 N N    . LEU B 1 922  ? 137.497 120.402 97.874  1.00 16.92 ?  922  LEU B N    1 
ATOM   13796 C CA   . LEU B 1 922  ? 137.793 121.004 99.166  1.00 15.21 ?  922  LEU B CA   1 
ATOM   13797 C C    . LEU B 1 922  ? 137.555 119.982 100.267 1.00 20.16 ?  922  LEU B C    1 
ATOM   13798 O O    . LEU B 1 922  ? 136.520 119.308 100.279 1.00 19.15 ?  922  LEU B O    1 
ATOM   13799 C CB   . LEU B 1 922  ? 136.930 122.247 99.403  1.00 14.99 ?  922  LEU B CB   1 
ATOM   13800 C CG   . LEU B 1 922  ? 137.549 123.365 100.240 1.00 14.28 ?  922  LEU B CG   1 
ATOM   13801 C CD1  . LEU B 1 922  ? 138.763 123.939 99.538  1.00 14.13 ?  922  LEU B CD1  1 
ATOM   13802 C CD2  . LEU B 1 922  ? 136.522 124.448 100.506 1.00 12.62 ?  922  LEU B CD2  1 
ATOM   13803 N N    . ASP B 1 923  ? 138.509 119.873 101.188 1.00 19.77 ?  923  ASP B N    1 
ATOM   13804 C CA   . ASP B 1 923  ? 138.339 119.011 102.346 1.00 19.86 ?  923  ASP B CA   1 
ATOM   13805 C C    . ASP B 1 923  ? 137.321 119.619 103.310 1.00 21.51 ?  923  ASP B C    1 
ATOM   13806 O O    . ASP B 1 923  ? 136.915 120.778 103.184 1.00 25.68 ?  923  ASP B O    1 
ATOM   13807 C CB   . ASP B 1 923  ? 139.676 118.788 103.053 1.00 24.41 ?  923  ASP B CB   1 
ATOM   13808 C CG   . ASP B 1 923  ? 140.838 118.680 102.085 1.00 29.14 ?  923  ASP B CG   1 
ATOM   13809 O OD1  . ASP B 1 923  ? 140.704 117.970 101.067 1.00 29.59 ?  923  ASP B OD1  1 
ATOM   13810 O OD2  . ASP B 1 923  ? 141.888 119.304 102.345 1.00 26.54 ?  923  ASP B OD2  1 
ATOM   13811 N N    . GLU B 1 924  ? 136.903 118.812 104.288 1.00 21.56 ?  924  GLU B N    1 
ATOM   13812 C CA   . GLU B 1 924  ? 135.896 119.271 105.240 1.00 20.91 ?  924  GLU B CA   1 
ATOM   13813 C C    . GLU B 1 924  ? 136.450 120.350 106.163 1.00 24.10 ?  924  GLU B C    1 
ATOM   13814 O O    . GLU B 1 924  ? 135.765 121.338 106.448 1.00 27.79 ?  924  GLU B O    1 
ATOM   13815 C CB   . GLU B 1 924  ? 135.363 118.090 106.051 1.00 17.94 ?  924  GLU B CB   1 
ATOM   13816 C CG   . GLU B 1 924  ? 134.023 117.565 105.560 1.00 20.90 ?  924  GLU B CG   1 
ATOM   13817 C CD   . GLU B 1 924  ? 133.182 116.959 106.667 1.00 27.49 ?  924  GLU B CD   1 
ATOM   13818 O OE1  . GLU B 1 924  ? 133.634 116.957 107.831 1.00 29.52 ?  924  GLU B OE1  1 
ATOM   13819 O OE2  . GLU B 1 924  ? 132.066 116.485 106.370 1.00 27.63 ?  924  GLU B OE2  1 
ATOM   13820 N N    . MET B 1 925  ? 137.689 120.182 106.635 1.00 20.81 ?  925  MET B N    1 
ATOM   13821 C CA   . MET B 1 925  ? 138.277 121.155 107.553 1.00 21.18 ?  925  MET B CA   1 
ATOM   13822 C C    . MET B 1 925  ? 138.566 122.480 106.852 1.00 21.66 ?  925  MET B C    1 
ATOM   13823 O O    . MET B 1 925  ? 138.384 123.554 107.441 1.00 28.31 ?  925  MET B O    1 
ATOM   13824 C CB   . MET B 1 925  ? 139.555 120.586 108.170 1.00 21.28 ?  925  MET B CB   1 
ATOM   13825 C CG   . MET B 1 925  ? 139.433 119.399 109.165 1.00 25.07 ?  925  MET B CG   1 
ATOM   13826 S SD   . MET B 1 925  ? 138.191 119.348 110.494 1.00 27.78 ?  925  MET B SD   1 
ATOM   13827 C CE   . MET B 1 925  ? 136.666 118.876 109.669 1.00 22.28 ?  925  MET B CE   1 
ATOM   13828 N N    . GLU B 1 926  ? 139.026 122.421 105.599 1.00 18.80 ?  926  GLU B N    1 
ATOM   13829 C CA   . GLU B 1 926  ? 139.267 123.639 104.830 1.00 20.73 ?  926  GLU B CA   1 
ATOM   13830 C C    . GLU B 1 926  ? 137.967 124.401 104.595 1.00 19.39 ?  926  GLU B C    1 
ATOM   13831 O O    . GLU B 1 926  ? 137.920 125.636 104.713 1.00 23.38 ?  926  GLU B O    1 
ATOM   13832 C CB   . GLU B 1 926  ? 139.926 123.284 103.497 1.00 20.78 ?  926  GLU B CB   1 
ATOM   13833 C CG   . GLU B 1 926  ? 141.446 123.276 103.520 1.00 22.21 ?  926  GLU B CG   1 
ATOM   13834 C CD   . GLU B 1 926  ? 142.013 122.349 104.571 1.00 26.86 ?  926  GLU B CD   1 
ATOM   13835 O OE1  . GLU B 1 926  ? 141.585 121.177 104.622 1.00 24.18 ?  926  GLU B OE1  1 
ATOM   13836 O OE2  . GLU B 1 926  ? 142.886 122.790 105.346 1.00 26.03 ?  926  GLU B OE2  1 
ATOM   13837 N N    . ALA B 1 927  ? 136.899 123.670 104.266 1.00 15.10 ?  927  ALA B N    1 
ATOM   13838 C CA   . ALA B 1 927  ? 135.587 124.282 104.103 1.00 14.62 ?  927  ALA B CA   1 
ATOM   13839 C C    . ALA B 1 927  ? 135.093 124.883 105.410 1.00 16.74 ?  927  ALA B C    1 
ATOM   13840 O O    . ALA B 1 927  ? 134.488 125.959 105.413 1.00 23.94 ?  927  ALA B O    1 
ATOM   13841 C CB   . ALA B 1 927  ? 134.590 123.252 103.575 1.00 14.22 ?  927  ALA B CB   1 
ATOM   13842 N N    . HIS B 1 928  ? 135.338 124.197 106.532 1.00 16.11 ?  928  HIS B N    1 
ATOM   13843 C CA   . HIS B 1 928  ? 134.947 124.734 107.833 1.00 17.18 ?  928  HIS B CA   1 
ATOM   13844 C C    . HIS B 1 928  ? 135.681 126.033 108.139 1.00 13.32 ?  928  HIS B C    1 
ATOM   13845 O O    . HIS B 1 928  ? 135.083 126.980 108.659 1.00 19.08 ?  928  HIS B O    1 
ATOM   13846 C CB   . HIS B 1 928  ? 135.204 123.703 108.933 1.00 15.81 ?  928  HIS B CB   1 
ATOM   13847 C CG   . HIS B 1 928  ? 134.226 122.569 108.947 1.00 15.59 ?  928  HIS B CG   1 
ATOM   13848 N ND1  . HIS B 1 928  ? 133.978 121.781 107.843 1.00 14.26 ?  928  HIS B ND1  1 
ATOM   13849 C CD2  . HIS B 1 928  ? 133.436 122.088 109.936 1.00 20.18 ?  928  HIS B CD2  1 
ATOM   13850 C CE1  . HIS B 1 928  ? 133.077 120.865 108.151 1.00 17.46 ?  928  HIS B CE1  1 
ATOM   13851 N NE2  . HIS B 1 928  ? 132.731 121.030 109.415 1.00 18.92 ?  928  HIS B NE2  1 
ATOM   13852 N N    . LYS B 1 929  ? 136.975 126.101 107.814 1.00 6.59  ?  929  LYS B N    1 
ATOM   13853 C CA   . LYS B 1 929  ? 137.730 127.333 108.036 1.00 8.23  ?  929  LYS B CA   1 
ATOM   13854 C C    . LYS B 1 929  ? 137.203 128.480 107.176 1.00 14.54 ?  929  LYS B C    1 
ATOM   13855 O O    . LYS B 1 929  ? 137.038 129.611 107.662 1.00 19.42 ?  929  LYS B O    1 
ATOM   13856 C CB   . LYS B 1 929  ? 139.214 127.094 107.756 1.00 10.86 ?  929  LYS B CB   1 
ATOM   13857 C CG   . LYS B 1 929  ? 139.931 126.290 108.829 1.00 14.81 ?  929  LYS B CG   1 
ATOM   13858 C CD   . LYS B 1 929  ? 141.430 126.241 108.568 1.00 17.56 ?  929  LYS B CD   1 
ATOM   13859 C CE   . LYS B 1 929  ? 141.878 124.854 108.134 1.00 15.21 ?  929  LYS B CE   1 
ATOM   13860 N NZ   . LYS B 1 929  ? 141.847 123.876 109.257 1.00 16.31 ?  929  LYS B NZ   1 
ATOM   13861 N N    . LEU B 1 930  ? 136.931 128.210 105.893 1.00 13.87 ?  930  LEU B N    1 
ATOM   13862 C CA   . LEU B 1 930  ? 136.413 129.260 105.016 1.00 10.12 ?  930  LEU B CA   1 
ATOM   13863 C C    . LEU B 1 930  ? 135.027 129.727 105.462 1.00 6.48  ?  930  LEU B C    1 
ATOM   13864 O O    . LEU B 1 930  ? 134.736 130.933 105.459 1.00 10.15 ?  930  LEU B O    1 
ATOM   13865 C CB   . LEU B 1 930  ? 136.386 128.766 103.571 1.00 12.77 ?  930  LEU B CB   1 
ATOM   13866 C CG   . LEU B 1 930  ? 137.757 128.538 102.928 1.00 9.74  ?  930  LEU B CG   1 
ATOM   13867 C CD1  . LEU B 1 930  ? 137.618 127.922 101.546 1.00 11.37 ?  930  LEU B CD1  1 
ATOM   13868 C CD2  . LEU B 1 930  ? 138.545 129.837 102.858 1.00 11.23 ?  930  LEU B CD2  1 
ATOM   13869 N N    . GLU B 1 931  ? 134.168 128.787 105.869 1.00 6.41  ?  931  GLU B N    1 
ATOM   13870 C CA   . GLU B 1 931  ? 132.856 129.144 106.398 1.00 8.69  ?  931  GLU B CA   1 
ATOM   13871 C C    . GLU B 1 931  ? 132.979 129.949 107.683 1.00 12.79 ?  931  GLU B C    1 
ATOM   13872 O O    . GLU B 1 931  ? 132.169 130.846 107.937 1.00 15.42 ?  931  GLU B O    1 
ATOM   13873 C CB   . GLU B 1 931  ? 132.026 127.884 106.645 1.00 14.53 ?  931  GLU B CB   1 
ATOM   13874 C CG   . GLU B 1 931  ? 131.540 127.171 105.396 1.00 16.43 ?  931  GLU B CG   1 
ATOM   13875 C CD   . GLU B 1 931  ? 130.380 127.875 104.731 1.00 21.10 ?  931  GLU B CD   1 
ATOM   13876 O OE1  . GLU B 1 931  ? 129.243 127.753 105.233 1.00 20.70 ?  931  GLU B OE1  1 
ATOM   13877 O OE2  . GLU B 1 931  ? 130.604 128.537 103.697 1.00 25.04 ?  931  GLU B OE2  1 
ATOM   13878 N N    . LEU B 1 932  ? 133.974 129.628 108.515 1.00 15.82 ?  932  LEU B N    1 
ATOM   13879 C CA   . LEU B 1 932  ? 134.206 130.387 109.738 1.00 11.79 ?  932  LEU B CA   1 
ATOM   13880 C C    . LEU B 1 932  ? 134.571 131.830 109.426 1.00 11.91 ?  932  LEU B C    1 
ATOM   13881 O O    . LEU B 1 932  ? 134.064 132.760 110.066 1.00 15.27 ?  932  LEU B O    1 
ATOM   13882 C CB   . LEU B 1 932  ? 135.314 129.725 110.555 1.00 9.11  ?  932  LEU B CB   1 
ATOM   13883 C CG   . LEU B 1 932  ? 135.272 129.875 112.073 1.00 9.59  ?  932  LEU B CG   1 
ATOM   13884 C CD1  . LEU B 1 932  ? 134.044 129.187 112.646 1.00 11.80 ?  932  LEU B CD1  1 
ATOM   13885 C CD2  . LEU B 1 932  ? 136.546 129.321 112.684 1.00 13.27 ?  932  LEU B CD2  1 
ATOM   13886 N N    . THR B 1 933  ? 135.445 132.033 108.435 1.00 9.67  ?  933  THR B N    1 
ATOM   13887 C CA   . THR B 1 933  ? 135.779 133.395 108.022 1.00 6.13  ?  933  THR B CA   1 
ATOM   13888 C C    . THR B 1 933  ? 134.547 134.126 107.498 1.00 8.49  ?  933  THR B C    1 
ATOM   13889 O O    . THR B 1 933  ? 134.338 135.309 107.803 1.00 13.65 ?  933  THR B O    1 
ATOM   13890 C CB   . THR B 1 933  ? 136.878 133.378 106.960 1.00 7.74  ?  933  THR B CB   1 
ATOM   13891 O OG1  . THR B 1 933  ? 136.428 132.649 105.812 1.00 13.99 ?  933  THR B OG1  1 
ATOM   13892 C CG2  . THR B 1 933  ? 138.140 132.730 107.505 1.00 9.04  ?  933  THR B CG2  1 
ATOM   13893 N N    . VAL B 1 934  ? 133.705 133.426 106.732 1.00 12.58 ?  934  VAL B N    1 
ATOM   13894 C CA   . VAL B 1 934  ? 132.495 134.047 106.193 1.00 7.39  ?  934  VAL B CA   1 
ATOM   13895 C C    . VAL B 1 934  ? 131.536 134.443 107.317 1.00 7.97  ?  934  VAL B C    1 
ATOM   13896 O O    . VAL B 1 934  ? 130.966 135.543 107.301 1.00 9.58  ?  934  VAL B O    1 
ATOM   13897 C CB   . VAL B 1 934  ? 131.830 133.113 105.161 1.00 9.06  ?  934  VAL B CB   1 
ATOM   13898 C CG1  . VAL B 1 934  ? 130.333 133.367 105.065 1.00 9.46  ?  934  VAL B CG1  1 
ATOM   13899 C CG2  . VAL B 1 934  ? 132.485 133.283 103.794 1.00 4.41  ?  934  VAL B CG2  1 
ATOM   13900 N N    . GLU B 1 935  ? 131.351 133.571 108.319 1.00 10.34 ?  935  GLU B N    1 
ATOM   13901 C CA   . GLU B 1 935  ? 130.447 133.921 109.417 1.00 7.85  ?  935  GLU B CA   1 
ATOM   13902 C C    . GLU B 1 935  ? 131.004 135.049 110.279 1.00 9.35  ?  935  GLU B C    1 
ATOM   13903 O O    . GLU B 1 935  ? 130.230 135.872 110.784 1.00 13.69 ?  935  GLU B O    1 
ATOM   13904 C CB   . GLU B 1 935  ? 130.108 132.721 110.315 1.00 9.71  ?  935  GLU B CB   1 
ATOM   13905 C CG   . GLU B 1 935  ? 129.444 131.517 109.647 1.00 13.90 ?  935  GLU B CG   1 
ATOM   13906 C CD   . GLU B 1 935  ? 129.852 130.188 110.273 1.00 16.34 ?  935  GLU B CD   1 
ATOM   13907 O OE1  . GLU B 1 935  ? 128.994 129.568 110.936 1.00 13.51 ?  935  GLU B OE1  1 
ATOM   13908 O OE2  . GLU B 1 935  ? 131.014 129.764 110.136 1.00 15.49 ?  935  GLU B OE2  1 
ATOM   13909 N N    . ILE B 1 936  ? 132.326 135.105 110.467 1.00 10.83 ?  936  ILE B N    1 
ATOM   13910 C CA   . ILE B 1 936  ? 132.919 136.235 111.182 1.00 5.64  ?  936  ILE B CA   1 
ATOM   13911 C C    . ILE B 1 936  ? 132.661 137.534 110.430 1.00 2.80  ?  936  ILE B C    1 
ATOM   13912 O O    . ILE B 1 936  ? 132.309 138.558 111.032 1.00 12.21 ?  936  ILE B O    1 
ATOM   13913 C CB   . ILE B 1 936  ? 134.425 136.000 111.417 1.00 11.39 ?  936  ILE B CB   1 
ATOM   13914 C CG1  . ILE B 1 936  ? 134.655 134.846 112.398 1.00 9.54  ?  936  ILE B CG1  1 
ATOM   13915 C CG2  . ILE B 1 936  ? 135.105 137.266 111.920 1.00 12.49 ?  936  ILE B CG2  1 
ATOM   13916 C CD1  . ILE B 1 936  ? 133.733 134.854 113.599 1.00 9.21  ?  936  ILE B CD1  1 
ATOM   13917 N N    . LYS B 1 937  ? 132.808 137.509 109.101 1.00 4.27  ?  937  LYS B N    1 
ATOM   13918 C CA   . LYS B 1 937  ? 132.533 138.706 108.309 1.00 10.16 ?  937  LYS B CA   1 
ATOM   13919 C C    . LYS B 1 937  ? 131.063 139.107 108.388 1.00 7.11  ?  937  LYS B C    1 
ATOM   13920 O O    . LYS B 1 937  ? 130.742 140.298 108.445 1.00 3.14  ?  937  LYS B O    1 
ATOM   13921 C CB   . LYS B 1 937  ? 132.953 138.486 106.857 1.00 8.40  ?  937  LYS B CB   1 
ATOM   13922 C CG   . LYS B 1 937  ? 134.451 138.366 106.668 1.00 6.96  ?  937  LYS B CG   1 
ATOM   13923 C CD   . LYS B 1 937  ? 134.807 138.115 105.219 1.00 11.84 ?  937  LYS B CD   1 
ATOM   13924 C CE   . LYS B 1 937  ? 135.352 139.372 104.573 1.00 14.54 ?  937  LYS B CE   1 
ATOM   13925 N NZ   . LYS B 1 937  ? 136.817 139.525 104.788 1.00 14.06 ?  937  LYS B NZ   1 
ATOM   13926 N N    . MET B 1 938  ? 130.156 138.126 108.396 1.00 5.24  ?  938  MET B N    1 
ATOM   13927 C CA   . MET B 1 938  ? 128.731 138.436 108.511 1.00 4.59  ?  938  MET B CA   1 
ATOM   13928 C C    . MET B 1 938  ? 128.399 139.056 109.865 1.00 9.34  ?  938  MET B C    1 
ATOM   13929 O O    . MET B 1 938  ? 127.628 140.024 109.942 1.00 13.08 ?  938  MET B O    1 
ATOM   13930 C CB   . MET B 1 938  ? 127.901 137.173 108.286 1.00 11.24 ?  938  MET B CB   1 
ATOM   13931 C CG   . MET B 1 938  ? 126.402 137.422 108.199 1.00 13.52 ?  938  MET B CG   1 
ATOM   13932 S SD   . MET B 1 938  ? 125.936 138.458 106.798 1.00 22.14 ?  938  MET B SD   1 
ATOM   13933 C CE   . MET B 1 938  ? 126.011 137.269 105.462 1.00 8.15  ?  938  MET B CE   1 
ATOM   13934 N N    . LYS B 1 939  ? 128.967 138.508 110.944 1.00 9.43  ?  939  LYS B N    1 
ATOM   13935 C CA   . LYS B 1 939  ? 128.724 139.063 112.273 1.00 4.22  ?  939  LYS B CA   1 
ATOM   13936 C C    . LYS B 1 939  ? 129.301 140.467 112.402 1.00 8.08  ?  939  LYS B C    1 
ATOM   13937 O O    . LYS B 1 939  ? 128.705 141.330 113.056 1.00 18.77 ?  939  LYS B O    1 
ATOM   13938 C CB   . LYS B 1 939  ? 129.302 138.141 113.346 1.00 7.08  ?  939  LYS B CB   1 
ATOM   13939 C CG   . LYS B 1 939  ? 128.888 138.512 114.762 1.00 11.19 ?  939  LYS B CG   1 
ATOM   13940 C CD   . LYS B 1 939  ? 129.124 137.371 115.739 1.00 10.30 ?  939  LYS B CD   1 
ATOM   13941 C CE   . LYS B 1 939  ? 128.261 137.523 116.982 1.00 5.55  ?  939  LYS B CE   1 
ATOM   13942 N NZ   . LYS B 1 939  ? 129.057 137.946 118.165 1.00 5.28  ?  939  LYS B NZ   1 
ATOM   13943 N N    . ARG B 1 940  ? 130.462 140.717 111.790 1.00 2.57  ?  940  ARG B N    1 
ATOM   13944 C CA   . ARG B 1 940  ? 131.013 142.069 111.795 1.00 2.97  ?  940  ARG B CA   1 
ATOM   13945 C C    . ARG B 1 940  ? 130.177 143.027 110.953 1.00 8.82  ?  940  ARG B C    1 
ATOM   13946 O O    . ARG B 1 940  ? 130.061 144.208 111.297 1.00 11.92 ?  940  ARG B O    1 
ATOM   13947 C CB   . ARG B 1 940  ? 132.459 142.051 111.304 1.00 4.45  ?  940  ARG B CB   1 
ATOM   13948 C CG   . ARG B 1 940  ? 133.427 141.380 112.263 1.00 7.56  ?  940  ARG B CG   1 
ATOM   13949 C CD   . ARG B 1 940  ? 134.866 141.558 111.815 1.00 8.72  ?  940  ARG B CD   1 
ATOM   13950 N NE   . ARG B 1 940  ? 135.792 140.769 112.620 1.00 10.61 ?  940  ARG B NE   1 
ATOM   13951 C CZ   . ARG B 1 940  ? 136.290 141.156 113.786 1.00 14.08 ?  940  ARG B CZ   1 
ATOM   13952 N NH1  . ARG B 1 940  ? 135.975 142.325 114.319 1.00 12.57 ?  940  ARG B NH1  1 
ATOM   13953 N NH2  . ARG B 1 940  ? 137.129 140.351 114.433 1.00 13.48 ?  940  ARG B NH2  1 
ATOM   13954 N N    . LEU B 1 941  ? 129.601 142.545 109.847 1.00 13.23 ?  941  LEU B N    1 
ATOM   13955 C CA   . LEU B 1 941  ? 128.734 143.385 109.025 1.00 10.94 ?  941  LEU B CA   1 
ATOM   13956 C C    . LEU B 1 941  ? 127.462 143.769 109.766 1.00 11.60 ?  941  LEU B C    1 
ATOM   13957 O O    . LEU B 1 941  ? 126.993 144.909 109.656 1.00 5.58  ?  941  LEU B O    1 
ATOM   13958 C CB   . LEU B 1 941  ? 128.394 142.671 107.716 1.00 10.55 ?  941  LEU B CB   1 
ATOM   13959 C CG   . LEU B 1 941  ? 127.123 143.135 106.995 1.00 4.90  ?  941  LEU B CG   1 
ATOM   13960 C CD1  . LEU B 1 941  ? 127.382 144.404 106.204 1.00 8.40  ?  941  LEU B CD1  1 
ATOM   13961 C CD2  . LEU B 1 941  ? 126.580 142.041 106.093 1.00 0.60  ?  941  LEU B CD2  1 
ATOM   13962 N N    . MET B 1 942  ? 126.893 142.836 110.532 1.00 14.65 ?  942  MET B N    1 
ATOM   13963 C CA   . MET B 1 942  ? 125.642 143.114 111.234 1.00 12.61 ?  942  MET B CA   1 
ATOM   13964 C C    . MET B 1 942  ? 125.777 144.187 112.312 1.00 14.24 ?  942  MET B C    1 
ATOM   13965 O O    . MET B 1 942  ? 124.753 144.687 112.788 1.00 14.73 ?  942  MET B O    1 
ATOM   13966 C CB   . MET B 1 942  ? 125.087 141.830 111.850 1.00 11.53 ?  942  MET B CB   1 
ATOM   13967 C CG   . MET B 1 942  ? 124.530 140.851 110.830 1.00 16.39 ?  942  MET B CG   1 
ATOM   13968 S SD   . MET B 1 942  ? 123.159 141.548 109.889 1.00 20.35 ?  942  MET B SD   1 
ATOM   13969 C CE   . MET B 1 942  ? 123.392 140.750 108.302 1.00 13.68 ?  942  MET B CE   1 
ATOM   13970 N N    . ASN B 1 943  ? 126.995 144.556 112.703 1.00 12.37 ?  943  ASN B N    1 
ATOM   13971 C CA   . ASN B 1 943  ? 127.239 145.614 113.677 1.00 12.91 ?  943  ASN B CA   1 
ATOM   13972 C C    . ASN B 1 943  ? 127.987 146.781 113.039 1.00 17.75 ?  943  ASN B C    1 
ATOM   13973 O O    . ASN B 1 943  ? 128.927 147.333 113.613 1.00 15.86 ?  943  ASN B O    1 
ATOM   13974 C CB   . ASN B 1 943  ? 127.999 145.074 114.886 1.00 14.99 ?  943  ASN B CB   1 
ATOM   13975 C CG   . ASN B 1 943  ? 127.180 144.086 115.694 1.00 20.04 ?  943  ASN B CG   1 
ATOM   13976 O OD1  . ASN B 1 943  ? 127.312 142.873 115.532 1.00 11.36 ?  943  ASN B OD1  1 
ATOM   13977 N ND2  . ASN B 1 943  ? 126.324 144.602 116.568 1.00 20.03 ?  943  ASN B ND2  1 
ATOM   13978 N N    . ALA B 1 944  ? 127.569 147.163 111.836 1.00 19.38 ?  944  ALA B N    1 
ATOM   13979 C CA   . ALA B 1 944  ? 128.162 148.262 111.092 1.00 16.28 ?  944  ALA B CA   1 
ATOM   13980 C C    . ALA B 1 944  ? 127.560 149.596 111.531 1.00 15.58 ?  944  ALA B C    1 
ATOM   13981 O O    . ALA B 1 944  ? 126.544 149.624 112.231 1.00 11.91 ?  944  ALA B O    1 
ATOM   13982 C CB   . ALA B 1 944  ? 127.943 148.044 109.596 1.00 16.30 ?  944  ALA B CB   1 
ATOM   13983 N N    . PRO B 1 945  ? 128.190 150.720 111.168 1.00 18.43 ?  945  PRO B N    1 
ATOM   13984 C CA   . PRO B 1 945  ? 127.554 152.024 111.402 1.00 16.48 ?  945  PRO B CA   1 
ATOM   13985 C C    . PRO B 1 945  ? 126.211 152.139 110.695 1.00 17.40 ?  945  PRO B C    1 
ATOM   13986 O O    . PRO B 1 945  ? 126.009 151.611 109.600 1.00 16.45 ?  945  PRO B O    1 
ATOM   13987 C CB   . PRO B 1 945  ? 128.567 153.019 110.829 1.00 12.34 ?  945  PRO B CB   1 
ATOM   13988 C CG   . PRO B 1 945  ? 129.870 152.345 110.988 1.00 13.25 ?  945  PRO B CG   1 
ATOM   13989 C CD   . PRO B 1 945  ? 129.617 150.869 110.824 1.00 17.10 ?  945  PRO B CD   1 
ATOM   13990 N N    . SER B 1 946  ? 125.287 152.846 111.343 1.00 14.07 ?  946  SER B N    1 
ATOM   13991 C CA   . SER B 1 946  ? 123.919 152.976 110.865 1.00 7.93  ?  946  SER B CA   1 
ATOM   13992 C C    . SER B 1 946  ? 123.685 154.246 110.057 1.00 9.58  ?  946  SER B C    1 
ATOM   13993 O O    . SER B 1 946  ? 122.535 154.552 109.729 1.00 11.32 ?  946  SER B O    1 
ATOM   13994 C CB   . SER B 1 946  ? 122.946 152.926 112.044 1.00 9.14  ?  946  SER B CB   1 
ATOM   13995 O OG   . SER B 1 946  ? 122.802 151.602 112.527 1.00 16.31 ?  946  SER B OG   1 
ATOM   13996 N N    . SER B 1 947  ? 124.741 154.994 109.736 1.00 8.73  ?  947  SER B N    1 
ATOM   13997 C CA   . SER B 1 947  ? 124.609 156.180 108.890 1.00 10.91 ?  947  SER B CA   1 
ATOM   13998 C C    . SER B 1 947  ? 125.953 156.412 108.207 1.00 15.41 ?  947  SER B C    1 
ATOM   13999 O O    . SER B 1 947  ? 126.876 156.957 108.819 1.00 17.85 ?  947  SER B O    1 
ATOM   14000 C CB   . SER B 1 947  ? 124.177 157.393 109.702 1.00 9.76  ?  947  SER B CB   1 
ATOM   14001 O OG   . SER B 1 947  ? 124.456 158.596 109.006 1.00 13.09 ?  947  SER B OG   1 
ATOM   14002 N N    . ILE B 1 948  ? 126.053 155.999 106.953 1.00 12.70 ?  948  ILE B N    1 
ATOM   14003 C CA   . ILE B 1 948  ? 127.245 156.213 106.134 1.00 11.55 ?  948  ILE B CA   1 
ATOM   14004 C C    . ILE B 1 948  ? 127.038 157.485 105.321 1.00 12.58 ?  948  ILE B C    1 
ATOM   14005 O O    . ILE B 1 948  ? 126.021 157.594 104.623 1.00 12.09 ?  948  ILE B O    1 
ATOM   14006 C CB   . ILE B 1 948  ? 127.520 155.013 105.210 1.00 12.66 ?  948  ILE B CB   1 
ATOM   14007 C CG1  . ILE B 1 948  ? 127.850 153.769 106.036 1.00 10.63 ?  948  ILE B CG1  1 
ATOM   14008 C CG2  . ILE B 1 948  ? 128.650 155.332 104.249 1.00 12.09 ?  948  ILE B CG2  1 
ATOM   14009 C CD1  . ILE B 1 948  ? 128.230 152.566 105.204 1.00 8.97  ?  948  ILE B CD1  1 
ATOM   14010 N N    . PRO B 1 949  ? 127.944 158.459 105.396 1.00 16.51 ?  949  PRO B N    1 
ATOM   14011 C CA   . PRO B 1 949  ? 127.759 159.726 104.666 1.00 16.41 ?  949  PRO B CA   1 
ATOM   14012 C C    . PRO B 1 949  ? 127.692 159.503 103.165 1.00 17.33 ?  949  PRO B C    1 
ATOM   14013 O O    . PRO B 1 949  ? 128.392 158.633 102.626 1.00 16.99 ?  949  PRO B O    1 
ATOM   14014 C CB   . PRO B 1 949  ? 129.004 160.540 105.049 1.00 16.82 ?  949  PRO B CB   1 
ATOM   14015 C CG   . PRO B 1 949  ? 129.480 159.931 106.326 1.00 19.52 ?  949  PRO B CG   1 
ATOM   14016 C CD   . PRO B 1 949  ? 129.157 158.473 106.229 1.00 18.90 ?  949  PRO B CD   1 
ATOM   14017 N N    . PRO B 1 950  ? 126.845 160.260 102.461 1.00 17.08 ?  950  PRO B N    1 
ATOM   14018 C CA   . PRO B 1 950  ? 126.753 160.093 101.011 1.00 16.00 ?  950  PRO B CA   1 
ATOM   14019 C C    . PRO B 1 950  ? 128.026 160.535 100.330 1.00 17.90 ?  950  PRO B C    1 
ATOM   14020 O O    . PRO B 1 950  ? 128.724 161.451 100.808 1.00 16.67 ?  950  PRO B O    1 
ATOM   14021 C CB   . PRO B 1 950  ? 125.564 160.995 100.628 1.00 14.38 ?  950  PRO B CB   1 
ATOM   14022 C CG   . PRO B 1 950  ? 125.459 161.979 101.736 1.00 13.65 ?  950  PRO B CG   1 
ATOM   14023 C CD   . PRO B 1 950  ? 125.890 161.256 102.973 1.00 14.47 ?  950  PRO B CD   1 
ATOM   14024 N N    . PRO B 1 951  ? 128.387 159.923 99.204  1.00 21.08 ?  951  PRO B N    1 
ATOM   14025 C CA   . PRO B 1 951  ? 129.655 160.245 98.548  1.00 20.39 ?  951  PRO B CA   1 
ATOM   14026 C C    . PRO B 1 951  ? 129.545 161.519 97.731  1.00 21.45 ?  951  PRO B C    1 
ATOM   14027 O O    . PRO B 1 951  ? 128.444 161.911 97.316  1.00 24.37 ?  951  PRO B O    1 
ATOM   14028 C CB   . PRO B 1 951  ? 129.912 159.025 97.644  1.00 21.01 ?  951  PRO B CB   1 
ATOM   14029 C CG   . PRO B 1 951  ? 128.778 158.055 97.908  1.00 20.86 ?  951  PRO B CG   1 
ATOM   14030 C CD   . PRO B 1 951  ? 127.667 158.846 98.507  1.00 20.94 ?  951  PRO B CD   1 
ATOM   14031 N N    . PRO B 1 952  ? 130.664 162.195 97.483  1.00 23.58 ?  952  PRO B N    1 
ATOM   14032 C CA   . PRO B 1 952  ? 130.659 163.350 96.577  1.00 23.33 ?  952  PRO B CA   1 
ATOM   14033 C C    . PRO B 1 952  ? 130.416 162.908 95.145  1.00 23.97 ?  952  PRO B C    1 
ATOM   14034 O O    . PRO B 1 952  ? 130.603 161.726 94.817  1.00 19.94 ?  952  PRO B O    1 
ATOM   14035 C CB   . PRO B 1 952  ? 132.067 163.944 96.750  1.00 23.87 ?  952  PRO B CB   1 
ATOM   14036 C CG   . PRO B 1 952  ? 132.586 163.364 98.028  1.00 23.48 ?  952  PRO B CG   1 
ATOM   14037 C CD   . PRO B 1 952  ? 131.974 162.006 98.126  1.00 22.98 ?  952  PRO B CD   1 
ATOM   14038 N N    . PRO B 1 953  ? 129.979 163.819 94.267  1.00 25.15 ?  953  PRO B N    1 
ATOM   14039 C CA   . PRO B 1 953  ? 129.711 163.430 92.869  1.00 24.25 ?  953  PRO B CA   1 
ATOM   14040 C C    . PRO B 1 953  ? 130.926 162.904 92.119  1.00 20.74 ?  953  PRO B C    1 
ATOM   14041 O O    . PRO B 1 953  ? 130.755 162.146 91.155  1.00 18.53 ?  953  PRO B O    1 
ATOM   14042 C CB   . PRO B 1 953  ? 129.190 164.729 92.240  1.00 21.12 ?  953  PRO B CB   1 
ATOM   14043 C CG   . PRO B 1 953  ? 128.659 165.519 93.386  1.00 22.17 ?  953  PRO B CG   1 
ATOM   14044 C CD   . PRO B 1 953  ? 129.553 165.202 94.545  1.00 20.09 ?  953  PRO B CD   1 
ATOM   14045 N N    . GLU B 1 954  ? 132.141 163.289 92.521  1.00 22.85 ?  954  GLU B N    1 
ATOM   14046 C CA   . GLU B 1 954  ? 133.339 162.753 91.882  1.00 25.73 ?  954  GLU B CA   1 
ATOM   14047 C C    . GLU B 1 954  ? 133.452 161.248 92.096  1.00 25.45 ?  954  GLU B C    1 
ATOM   14048 O O    . GLU B 1 954  ? 133.841 160.510 91.182  1.00 23.99 ?  954  GLU B O    1 
ATOM   14049 C CB   . GLU B 1 954  ? 134.582 163.466 92.415  1.00 24.18 ?  954  GLU B CB   1 
ATOM   14050 C CG   . GLU B 1 954  ? 134.401 164.961 92.626  1.00 23.41 ?  954  GLU B CG   1 
ATOM   14051 C CD   . GLU B 1 954  ? 134.912 165.781 91.457  1.00 26.02 ?  954  GLU B CD   1 
ATOM   14052 O OE1  . GLU B 1 954  ? 135.961 165.416 90.888  1.00 24.43 ?  954  GLU B OE1  1 
ATOM   14053 O OE2  . GLU B 1 954  ? 134.264 166.790 91.108  1.00 27.56 ?  954  GLU B OE2  1 
ATOM   14054 N N    . ASN B 1 955  ? 133.116 160.776 93.299  1.00 22.48 ?  955  ASN B N    1 
ATOM   14055 C CA   . ASN B 1 955  ? 133.132 159.342 93.566  1.00 19.63 ?  955  ASN B CA   1 
ATOM   14056 C C    . ASN B 1 955  ? 132.061 158.619 92.758  1.00 21.21 ?  955  ASN B C    1 
ATOM   14057 O O    . ASN B 1 955  ? 132.269 157.481 92.321  1.00 19.41 ?  955  ASN B O    1 
ATOM   14058 C CB   . ASN B 1 955  ? 132.944 159.086 95.061  1.00 19.15 ?  955  ASN B CB   1 
ATOM   14059 C CG   . ASN B 1 955  ? 133.626 157.814 95.526  1.00 22.55 ?  955  ASN B CG   1 
ATOM   14060 O OD1  . ASN B 1 955  ? 133.729 156.841 94.779  1.00 21.30 ?  955  ASN B OD1  1 
ATOM   14061 N ND2  . ASN B 1 955  ? 134.097 157.817 96.767  1.00 21.40 ?  955  ASN B ND2  1 
ATOM   14062 N N    . LEU B 1 956  ? 130.905 159.258 92.558  1.00 22.38 ?  956  LEU B N    1 
ATOM   14063 C CA   . LEU B 1 956  ? 129.864 158.665 91.725  1.00 18.21 ?  956  LEU B CA   1 
ATOM   14064 C C    . LEU B 1 956  ? 130.309 158.563 90.271  1.00 22.76 ?  956  LEU B C    1 
ATOM   14065 O O    . LEU B 1 956  ? 130.018 157.571 89.593  1.00 22.79 ?  956  LEU B O    1 
ATOM   14066 C CB   . LEU B 1 956  ? 128.573 159.475 91.836  1.00 14.60 ?  956  LEU B CB   1 
ATOM   14067 C CG   . LEU B 1 956  ? 127.736 159.254 93.097  1.00 16.38 ?  956  LEU B CG   1 
ATOM   14068 C CD1  . LEU B 1 956  ? 126.541 160.192 93.118  1.00 19.03 ?  956  LEU B CD1  1 
ATOM   14069 C CD2  . LEU B 1 956  ? 127.284 157.805 93.192  1.00 16.51 ?  956  LEU B CD2  1 
ATOM   14070 N N    . LEU B 1 957  ? 131.011 159.584 89.771  1.00 20.96 ?  957  LEU B N    1 
ATOM   14071 C CA   . LEU B 1 957  ? 131.514 159.528 88.401  1.00 17.75 ?  957  LEU B CA   1 
ATOM   14072 C C    . LEU B 1 957  ? 132.630 158.499 88.260  1.00 20.81 ?  957  LEU B C    1 
ATOM   14073 O O    . LEU B 1 957  ? 132.761 157.859 87.211  1.00 25.04 ?  957  LEU B O    1 
ATOM   14074 C CB   . LEU B 1 957  ? 131.998 160.911 87.959  1.00 21.62 ?  957  LEU B CB   1 
ATOM   14075 C CG   . LEU B 1 957  ? 131.922 161.257 86.467  1.00 23.19 ?  957  LEU B CG   1 
ATOM   14076 C CD1  . LEU B 1 957  ? 131.842 162.757 86.279  1.00 23.06 ?  957  LEU B CD1  1 
ATOM   14077 C CD2  . LEU B 1 957  ? 133.115 160.712 85.700  1.00 19.45 ?  957  LEU B CD2  1 
ATOM   14078 N N    . LYS B 1 958  ? 133.447 158.327 89.297  1.00 17.80 ?  958  LYS B N    1 
ATOM   14079 C CA   . LYS B 1 958  ? 134.571 157.406 89.208  1.00 19.17 ?  958  LYS B CA   1 
ATOM   14080 C C    . LYS B 1 958  ? 134.173 155.949 89.410  1.00 20.22 ?  958  LYS B C    1 
ATOM   14081 O O    . LYS B 1 958  ? 134.979 155.060 89.113  1.00 24.33 ?  958  LYS B O    1 
ATOM   14082 C CB   . LYS B 1 958  ? 135.650 157.800 90.223  1.00 18.59 ?  958  LYS B CB   1 
ATOM   14083 C CG   . LYS B 1 958  ? 135.567 157.078 91.559  1.00 19.42 ?  958  LYS B CG   1 
ATOM   14084 C CD   . LYS B 1 958  ? 136.937 156.972 92.208  1.00 23.25 ?  958  LYS B CD   1 
ATOM   14085 C CE   . LYS B 1 958  ? 136.998 155.815 93.191  1.00 20.86 ?  958  LYS B CE   1 
ATOM   14086 N NZ   . LYS B 1 958  ? 138.381 155.591 93.696  1.00 20.11 ?  958  LYS B NZ   1 
ATOM   14087 N N    . ASN B 1 959  ? 132.956 155.678 89.883  1.00 15.84 ?  959  ASN B N    1 
ATOM   14088 C CA   . ASN B 1 959  ? 132.530 154.324 90.213  1.00 17.92 ?  959  ASN B CA   1 
ATOM   14089 C C    . ASN B 1 959  ? 131.542 153.747 89.202  1.00 19.79 ?  959  ASN B C    1 
ATOM   14090 O O    . ASN B 1 959  ? 130.867 152.758 89.505  1.00 19.00 ?  959  ASN B O    1 
ATOM   14091 C CB   . ASN B 1 959  ? 131.924 154.293 91.617  1.00 17.87 ?  959  ASN B CB   1 
ATOM   14092 C CG   . ASN B 1 959  ? 132.601 153.281 92.520  1.00 22.85 ?  959  ASN B CG   1 
ATOM   14093 O OD1  . ASN B 1 959  ? 133.275 152.365 92.050  1.00 17.22 ?  959  ASN B OD1  1 
ATOM   14094 N ND2  . ASN B 1 959  ? 132.425 153.444 93.826  1.00 22.35 ?  959  ASN B ND2  1 
ATOM   14095 N N    . VAL B 1 960  ? 131.435 154.348 88.015  1.00 17.71 ?  960  VAL B N    1 
ATOM   14096 C CA   . VAL B 1 960  ? 130.582 153.791 86.972  1.00 12.65 ?  960  VAL B CA   1 
ATOM   14097 C C    . VAL B 1 960  ? 131.176 152.473 86.483  1.00 17.83 ?  960  VAL B C    1 
ATOM   14098 O O    . VAL B 1 960  ? 132.398 152.271 86.501  1.00 20.45 ?  960  VAL B O    1 
ATOM   14099 C CB   . VAL B 1 960  ? 130.407 154.800 85.820  1.00 14.05 ?  960  VAL B CB   1 
ATOM   14100 C CG1  . VAL B 1 960  ? 129.273 154.387 84.894  1.00 15.91 ?  960  VAL B CG1  1 
ATOM   14101 C CG2  . VAL B 1 960  ? 130.134 156.183 86.376  1.00 17.85 ?  960  VAL B CG2  1 
ATOM   14102 N N    . SER B 1 961  ? 130.298 151.557 86.060  1.00 21.02 ?  961  SER B N    1 
ATOM   14103 C CA   . SER B 1 961  ? 130.725 150.204 85.709  1.00 20.50 ?  961  SER B CA   1 
ATOM   14104 C C    . SER B 1 961  ? 131.657 150.197 84.503  1.00 19.95 ?  961  SER B C    1 
ATOM   14105 O O    . SER B 1 961  ? 132.605 149.405 84.449  1.00 24.92 ?  961  SER B O    1 
ATOM   14106 C CB   . SER B 1 961  ? 129.504 149.324 85.445  1.00 19.49 ?  961  SER B CB   1 
ATOM   14107 O OG   . SER B 1 961  ? 128.466 150.065 84.827  1.00 19.12 ?  961  SER B OG   1 
ATOM   14108 N N    . TRP B 1 962  ? 131.407 151.063 83.524  1.00 12.14 ?  962  TRP B N    1 
ATOM   14109 C CA   . TRP B 1 962  ? 132.238 151.124 82.330  1.00 15.27 ?  962  TRP B CA   1 
ATOM   14110 C C    . TRP B 1 962  ? 133.346 152.166 82.427  1.00 19.89 ?  962  TRP B C    1 
ATOM   14111 O O    . TRP B 1 962  ? 134.040 152.408 81.435  1.00 21.39 ?  962  TRP B O    1 
ATOM   14112 C CB   . TRP B 1 962  ? 131.379 151.386 81.089  1.00 17.41 ?  962  TRP B CB   1 
ATOM   14113 C CG   . TRP B 1 962  ? 130.337 152.450 81.251  1.00 19.40 ?  962  TRP B CG   1 
ATOM   14114 C CD1  . TRP B 1 962  ? 129.076 152.294 81.746  1.00 20.54 ?  962  TRP B CD1  1 
ATOM   14115 C CD2  . TRP B 1 962  ? 130.462 153.833 80.900  1.00 18.51 ?  962  TRP B CD2  1 
ATOM   14116 N NE1  . TRP B 1 962  ? 128.409 153.494 81.730  1.00 17.81 ?  962  TRP B NE1  1 
ATOM   14117 C CE2  . TRP B 1 962  ? 129.239 154.455 81.216  1.00 20.09 ?  962  TRP B CE2  1 
ATOM   14118 C CE3  . TRP B 1 962  ? 131.491 154.606 80.354  1.00 17.40 ?  962  TRP B CE3  1 
ATOM   14119 C CZ2  . TRP B 1 962  ? 129.017 155.813 81.003  1.00 21.14 ?  962  TRP B CZ2  1 
ATOM   14120 C CZ3  . TRP B 1 962  ? 131.267 155.953 80.142  1.00 18.93 ?  962  TRP B CZ3  1 
ATOM   14121 C CH2  . TRP B 1 962  ? 130.041 156.543 80.467  1.00 18.40 ?  962  TRP B CH2  1 
ATOM   14122 N N    . LEU B 1 963  ? 133.528 152.789 83.593  1.00 19.14 ?  963  LEU B N    1 
ATOM   14123 C CA   . LEU B 1 963  ? 134.620 153.727 83.809  1.00 18.53 ?  963  LEU B CA   1 
ATOM   14124 C C    . LEU B 1 963  ? 135.582 153.316 84.913  1.00 22.66 ?  963  LEU B C    1 
ATOM   14125 O O    . LEU B 1 963  ? 136.695 153.850 84.961  1.00 25.99 ?  963  LEU B O    1 
ATOM   14126 C CB   . LEU B 1 963  ? 134.077 155.127 84.138  1.00 19.88 ?  963  LEU B CB   1 
ATOM   14127 C CG   . LEU B 1 963  ? 133.527 155.953 82.974  1.00 21.23 ?  963  LEU B CG   1 
ATOM   14128 C CD1  . LEU B 1 963  ? 133.049 157.315 83.454  1.00 19.49 ?  963  LEU B CD1  1 
ATOM   14129 C CD2  . LEU B 1 963  ? 134.573 156.104 81.883  1.00 21.13 ?  963  LEU B CD2  1 
ATOM   14130 N N    . ALA B 1 964  ? 135.194 152.396 85.792  1.00 21.56 ?  964  ALA B N    1 
ATOM   14131 C CA   . ALA B 1 964  ? 136.054 152.011 86.902  1.00 22.03 ?  964  ALA B CA   1 
ATOM   14132 C C    . ALA B 1 964  ? 137.219 151.157 86.417  1.00 21.54 ?  964  ALA B C    1 
ATOM   14133 O O    . ALA B 1 964  ? 137.082 150.355 85.489  1.00 16.99 ?  964  ALA B O    1 
ATOM   14134 C CB   . ALA B 1 964  ? 135.250 151.251 87.956  1.00 19.31 ?  964  ALA B CB   1 
ATOM   14135 N N    . GLY B 1 965  ? 138.374 151.337 87.056  1.00 25.09 ?  965  GLY B N    1 
ATOM   14136 C CA   . GLY B 1 965  ? 139.562 150.568 86.768  1.00 25.72 ?  965  GLY B CA   1 
ATOM   14137 C C    . GLY B 1 965  ? 140.538 151.233 85.820  1.00 26.70 ?  965  GLY B C    1 
ATOM   14138 O O    . GLY B 1 965  ? 141.711 150.841 85.788  1.00 29.48 ?  965  GLY B O    1 
ATOM   14139 N N    . ASP B 1 966  ? 140.092 152.224 85.052  1.00 21.56 ?  966  ASP B N    1 
ATOM   14140 C CA   . ASP B 1 966  ? 140.938 152.938 84.102  1.00 24.51 ?  966  ASP B CA   1 
ATOM   14141 C C    . ASP B 1 966  ? 141.153 154.352 84.624  1.00 26.06 ?  966  ASP B C    1 
ATOM   14142 O O    . ASP B 1 966  ? 140.238 155.181 84.580  1.00 22.74 ?  966  ASP B O    1 
ATOM   14143 C CB   . ASP B 1 966  ? 140.306 152.955 82.711  1.00 24.93 ?  966  ASP B CB   1 
ATOM   14144 C CG   . ASP B 1 966  ? 140.182 151.570 82.106  1.00 26.74 ?  966  ASP B CG   1 
ATOM   14145 O OD1  . ASP B 1 966  ? 140.442 150.577 82.816  1.00 26.42 ?  966  ASP B OD1  1 
ATOM   14146 O OD2  . ASP B 1 966  ? 139.821 151.474 80.914  1.00 28.00 ?  966  ASP B OD2  1 
ATOM   14147 N N    . MET B 1 967  ? 142.364 154.626 85.118  1.00 23.98 ?  967  MET B N    1 
ATOM   14148 C CA   . MET B 1 967  ? 142.658 155.942 85.677  1.00 21.75 ?  967  MET B CA   1 
ATOM   14149 C C    . MET B 1 967  ? 142.741 157.006 84.589  1.00 21.20 ?  967  MET B C    1 
ATOM   14150 O O    . MET B 1 967  ? 142.276 158.136 84.783  1.00 22.82 ?  967  MET B O    1 
ATOM   14151 C CB   . MET B 1 967  ? 143.957 155.891 86.480  1.00 19.84 ?  967  MET B CB   1 
ATOM   14152 C CG   . MET B 1 967  ? 143.857 155.099 87.774  1.00 19.77 ?  967  MET B CG   1 
ATOM   14153 S SD   . MET B 1 967  ? 143.281 153.409 87.526  1.00 28.40 ?  967  MET B SD   1 
ATOM   14154 C CE   . MET B 1 967  ? 144.683 152.692 86.672  1.00 20.89 ?  967  MET B CE   1 
ATOM   14155 N N    . LYS B 1 968  ? 143.338 156.667 83.442  1.00 21.79 ?  968  LYS B N    1 
ATOM   14156 C CA   . LYS B 1 968  ? 143.429 157.622 82.341  1.00 27.39 ?  968  LYS B CA   1 
ATOM   14157 C C    . LYS B 1 968  ? 142.049 157.972 81.800  1.00 26.76 ?  968  LYS B C    1 
ATOM   14158 O O    . LYS B 1 968  ? 141.755 159.145 81.539  1.00 22.07 ?  968  LYS B O    1 
ATOM   14159 C CB   . LYS B 1 968  ? 144.312 157.057 81.228  1.00 24.48 ?  968  LYS B CB   1 
ATOM   14160 C CG   . LYS B 1 968  ? 145.804 157.161 81.499  1.00 22.49 ?  968  LYS B CG   1 
ATOM   14161 C CD   . LYS B 1 968  ? 146.356 155.858 82.057  1.00 20.82 ?  968  LYS B CD   1 
ATOM   14162 C CE   . LYS B 1 968  ? 146.201 154.722 81.059  1.00 22.61 ?  968  LYS B CE   1 
ATOM   14163 N NZ   . LYS B 1 968  ? 146.869 153.475 81.525  1.00 24.23 ?  968  LYS B NZ   1 
ATOM   14164 N N    . LEU B 1 969  ? 141.186 156.966 81.635  1.00 26.12 ?  969  LEU B N    1 
ATOM   14165 C CA   . LEU B 1 969  ? 139.822 157.218 81.181  1.00 27.06 ?  969  LEU B CA   1 
ATOM   14166 C C    . LEU B 1 969  ? 139.033 158.016 82.211  1.00 22.88 ?  969  LEU B C    1 
ATOM   14167 O O    . LEU B 1 969  ? 138.234 158.887 81.848  1.00 21.51 ?  969  LEU B O    1 
ATOM   14168 C CB   . LEU B 1 969  ? 139.122 155.896 80.872  1.00 23.26 ?  969  LEU B CB   1 
ATOM   14169 C CG   . LEU B 1 969  ? 137.861 155.932 80.005  1.00 21.21 ?  969  LEU B CG   1 
ATOM   14170 C CD1  . LEU B 1 969  ? 137.931 157.031 78.955  1.00 19.87 ?  969  LEU B CD1  1 
ATOM   14171 C CD2  . LEU B 1 969  ? 137.647 154.579 79.352  1.00 21.09 ?  969  LEU B CD2  1 
ATOM   14172 N N    . ILE B 1 970  ? 139.243 157.729 83.500  1.00 18.22 ?  970  ILE B N    1 
ATOM   14173 C CA   . ILE B 1 970  ? 138.564 158.476 84.555  1.00 20.75 ?  970  ILE B CA   1 
ATOM   14174 C C    . ILE B 1 970  ? 138.974 159.943 84.516  1.00 21.68 ?  970  ILE B C    1 
ATOM   14175 O O    . ILE B 1 970  ? 138.128 160.840 84.605  1.00 19.42 ?  970  ILE B O    1 
ATOM   14176 C CB   . ILE B 1 970  ? 138.845 157.834 85.929  1.00 22.08 ?  970  ILE B CB   1 
ATOM   14177 C CG1  . ILE B 1 970  ? 137.800 156.760 86.236  1.00 20.23 ?  970  ILE B CG1  1 
ATOM   14178 C CG2  . ILE B 1 970  ? 138.859 158.874 87.046  1.00 20.53 ?  970  ILE B CG2  1 
ATOM   14179 C CD1  . ILE B 1 970  ? 138.022 156.054 87.555  1.00 20.44 ?  970  ILE B CD1  1 
ATOM   14180 N N    . ASP B 1 971  ? 140.275 160.209 84.354  1.00 27.89 ?  971  ASP B N    1 
ATOM   14181 C CA   . ASP B 1 971  ? 140.748 161.588 84.265  1.00 29.21 ?  971  ASP B CA   1 
ATOM   14182 C C    . ASP B 1 971  ? 140.213 162.282 83.016  1.00 28.56 ?  971  ASP B C    1 
ATOM   14183 O O    . ASP B 1 971  ? 139.817 163.453 83.072  1.00 22.88 ?  971  ASP B O    1 
ATOM   14184 C CB   . ASP B 1 971  ? 142.276 161.619 84.285  1.00 25.44 ?  971  ASP B CB   1 
ATOM   14185 C CG   . ASP B 1 971  ? 142.833 162.033 85.633  1.00 25.86 ?  971  ASP B CG   1 
ATOM   14186 O OD1  . ASP B 1 971  ? 142.143 162.777 86.362  1.00 27.03 ?  971  ASP B OD1  1 
ATOM   14187 O OD2  . ASP B 1 971  ? 143.961 161.613 85.966  1.00 27.00 ?  971  ASP B OD2  1 
ATOM   14188 N N    . PHE B 1 972  ? 140.189 161.570 81.884  1.00 26.07 ?  972  PHE B N    1 
ATOM   14189 C CA   . PHE B 1 972  ? 139.690 162.150 80.640  1.00 27.61 ?  972  PHE B CA   1 
ATOM   14190 C C    . PHE B 1 972  ? 138.213 162.512 80.745  1.00 30.02 ?  972  PHE B C    1 
ATOM   14191 O O    . PHE B 1 972  ? 137.795 163.582 80.286  1.00 25.43 ?  972  PHE B O    1 
ATOM   14192 C CB   . PHE B 1 972  ? 139.922 161.173 79.484  1.00 26.14 ?  972  PHE B CB   1 
ATOM   14193 C CG   . PHE B 1 972  ? 139.718 161.775 78.120  1.00 26.59 ?  972  PHE B CG   1 
ATOM   14194 C CD1  . PHE B 1 972  ? 140.763 162.404 77.463  1.00 25.46 ?  972  PHE B CD1  1 
ATOM   14195 C CD2  . PHE B 1 972  ? 138.486 161.700 77.489  1.00 26.61 ?  972  PHE B CD2  1 
ATOM   14196 C CE1  . PHE B 1 972  ? 140.582 162.952 76.205  1.00 26.28 ?  972  PHE B CE1  1 
ATOM   14197 C CE2  . PHE B 1 972  ? 138.298 162.249 76.234  1.00 27.60 ?  972  PHE B CE2  1 
ATOM   14198 C CZ   . PHE B 1 972  ? 139.348 162.876 75.592  1.00 27.29 ?  972  PHE B CZ   1 
ATOM   14199 N N    . ILE B 1 973  ? 137.405 161.630 81.339  1.00 26.64 ?  973  ILE B N    1 
ATOM   14200 C CA   . ILE B 1 973  ? 135.977 161.903 81.465  1.00 24.14 ?  973  ILE B CA   1 
ATOM   14201 C C    . ILE B 1 973  ? 135.726 163.004 82.491  1.00 26.25 ?  973  ILE B C    1 
ATOM   14202 O O    . ILE B 1 973  ? 134.902 163.899 82.269  1.00 26.14 ?  973  ILE B O    1 
ATOM   14203 C CB   . ILE B 1 973  ? 135.215 160.609 81.808  1.00 21.61 ?  973  ILE B CB   1 
ATOM   14204 C CG1  . ILE B 1 973  ? 135.314 159.610 80.653  1.00 20.10 ?  973  ILE B CG1  1 
ATOM   14205 C CG2  . ILE B 1 973  ? 133.752 160.904 82.083  1.00 23.14 ?  973  ILE B CG2  1 
ATOM   14206 C CD1  . ILE B 1 973  ? 134.962 160.191 79.299  1.00 22.89 ?  973  ILE B CD1  1 
ATOM   14207 N N    . LYS B 1 974  ? 136.437 162.965 83.625  1.00 21.76 ?  974  LYS B N    1 
ATOM   14208 C CA   . LYS B 1 974  ? 136.241 163.962 84.672  1.00 22.16 ?  974  LYS B CA   1 
ATOM   14209 C C    . LYS B 1 974  ? 136.669 165.353 84.220  1.00 22.27 ?  974  LYS B C    1 
ATOM   14210 O O    . LYS B 1 974  ? 136.076 166.350 84.647  1.00 19.76 ?  974  LYS B O    1 
ATOM   14211 C CB   . LYS B 1 974  ? 137.008 163.549 85.930  1.00 22.72 ?  974  LYS B CB   1 
ATOM   14212 C CG   . LYS B 1 974  ? 136.730 164.406 87.156  1.00 23.63 ?  974  LYS B CG   1 
ATOM   14213 C CD   . LYS B 1 974  ? 137.582 163.972 88.341  1.00 19.93 ?  974  LYS B CD   1 
ATOM   14214 C CE   . LYS B 1 974  ? 137.378 162.501 88.669  1.00 21.00 ?  974  LYS B CE   1 
ATOM   14215 N NZ   . LYS B 1 974  ? 135.953 162.189 88.965  1.00 18.94 ?  974  LYS B NZ   1 
ATOM   14216 N N    . ALA B 1 975  ? 137.690 165.442 83.363  1.00 24.40 ?  975  ALA B N    1 
ATOM   14217 C CA   . ALA B 1 975  ? 138.113 166.745 82.862  1.00 25.58 ?  975  ALA B CA   1 
ATOM   14218 C C    . ALA B 1 975  ? 137.068 167.368 81.943  1.00 25.68 ?  975  ALA B C    1 
ATOM   14219 O O    . ALA B 1 975  ? 136.908 168.594 81.933  1.00 24.89 ?  975  ALA B O    1 
ATOM   14220 C CB   . ALA B 1 975  ? 139.451 166.620 82.135  1.00 26.43 ?  975  ALA B CB   1 
ATOM   14221 N N    . ARG B 1 976  ? 136.351 166.551 81.173  1.00 25.45 ?  976  ARG B N    1 
ATOM   14222 C CA   . ARG B 1 976  ? 135.410 167.041 80.175  1.00 25.54 ?  976  ARG B CA   1 
ATOM   14223 C C    . ARG B 1 976  ? 133.954 166.936 80.617  1.00 26.36 ?  976  ARG B C    1 
ATOM   14224 O O    . ARG B 1 976  ? 133.055 167.136 79.795  1.00 25.52 ?  976  ARG B O    1 
ATOM   14225 C CB   . ARG B 1 976  ? 135.610 166.288 78.859  1.00 29.38 ?  976  ARG B CB   1 
ATOM   14226 C CG   . ARG B 1 976  ? 136.756 166.821 78.018  1.00 28.23 ?  976  ARG B CG   1 
ATOM   14227 C CD   . ARG B 1 976  ? 137.517 165.694 77.344  1.00 26.79 ?  976  ARG B CD   1 
ATOM   14228 N NE   . ARG B 1 976  ? 138.896 166.069 77.060  1.00 30.10 ?  976  ARG B NE   1 
ATOM   14229 C CZ   . ARG B 1 976  ? 139.918 165.832 77.871  1.00 30.09 ?  976  ARG B CZ   1 
ATOM   14230 N NH1  . ARG B 1 976  ? 139.753 165.215 79.029  1.00 26.10 ?  976  ARG B NH1  1 
ATOM   14231 N NH2  . ARG B 1 976  ? 141.137 166.222 77.509  1.00 28.93 ?  976  ARG B NH2  1 
ATOM   14232 N N    . ALA B 1 977  ? 133.699 166.629 81.885  1.00 27.09 ?  977  ALA B N    1 
ATOM   14233 C CA   . ALA B 1 977  ? 132.338 166.535 82.390  1.00 24.47 ?  977  ALA B CA   1 
ATOM   14234 C C    . ALA B 1 977  ? 131.891 167.868 82.976  1.00 24.24 ?  977  ALA B C    1 
ATOM   14235 O O    . ALA B 1 977  ? 132.706 168.667 83.444  1.00 22.72 ?  977  ALA B O    1 
ATOM   14236 C CB   . ALA B 1 977  ? 132.226 165.439 83.450  1.00 19.67 ?  977  ALA B CB   1 
ATOM   14237 N N    . SER B 1 978  ? 130.581 168.102 82.947  1.00 20.92 ?  978  SER B N    1 
ATOM   14238 C CA   . SER B 1 978  ? 130.001 169.319 83.495  1.00 21.27 ?  978  SER B CA   1 
ATOM   14239 C C    . SER B 1 978  ? 128.866 168.963 84.444  1.00 23.10 ?  978  SER B C    1 
ATOM   14240 O O    . SER B 1 978  ? 128.272 167.888 84.356  1.00 27.26 ?  978  SER B O    1 
ATOM   14241 C CB   . SER B 1 978  ? 129.491 170.248 82.385  1.00 22.44 ?  978  SER B CB   1 
ATOM   14242 O OG   . SER B 1 978  ? 128.166 169.916 82.012  1.00 22.99 ?  978  SER B OG   1 
ATOM   14243 N N    . LEU B 1 979  ? 128.571 169.877 85.363  1.00 21.08 ?  979  LEU B N    1 
ATOM   14244 C CA   . LEU B 1 979  ? 127.485 169.703 86.320  1.00 19.44 ?  979  LEU B CA   1 
ATOM   14245 C C    . LEU B 1 979  ? 126.291 170.548 85.903  1.00 22.57 ?  979  LEU B C    1 
ATOM   14246 O O    . LEU B 1 979  ? 126.438 171.742 85.621  1.00 27.56 ?  979  LEU B O    1 
ATOM   14247 C CB   . LEU B 1 979  ? 127.929 170.089 87.732  1.00 23.17 ?  979  LEU B CB   1 
ATOM   14248 C CG   . LEU B 1 979  ? 127.432 169.196 88.870  1.00 25.50 ?  979  LEU B CG   1 
ATOM   14249 C CD1  . LEU B 1 979  ? 127.942 167.776 88.716  1.00 23.84 ?  979  LEU B CD1  1 
ATOM   14250 C CD2  . LEU B 1 979  ? 127.836 169.772 90.218  1.00 23.37 ?  979  LEU B CD2  1 
ATOM   14251 N N    . LEU B 1 980  ? 125.112 169.930 85.867  1.00 20.38 ?  980  LEU B N    1 
ATOM   14252 C CA   . LEU B 1 980  ? 123.878 170.621 85.522  1.00 22.03 ?  980  LEU B CA   1 
ATOM   14253 C C    . LEU B 1 980  ? 122.872 170.478 86.654  1.00 20.38 ?  980  LEU B C    1 
ATOM   14254 O O    . LEU B 1 980  ? 122.716 169.396 87.229  1.00 22.30 ?  980  LEU B O    1 
ATOM   14255 C CB   . LEU B 1 980  ? 123.276 170.079 84.220  1.00 24.14 ?  980  LEU B CB   1 
ATOM   14256 C CG   . LEU B 1 980  ? 123.561 170.838 82.920  1.00 21.19 ?  980  LEU B CG   1 
ATOM   14257 C CD1  . LEU B 1 980  ? 122.977 172.241 82.984  1.00 20.05 ?  980  LEU B CD1  1 
ATOM   14258 C CD2  . LEU B 1 980  ? 125.048 170.885 82.611  1.00 19.05 ?  980  LEU B CD2  1 
ATOM   14259 N N    . HIS B 1 981  ? 122.190 171.578 86.965  1.00 22.50 ?  981  HIS B N    1 
ATOM   14260 C CA   . HIS B 1 981  ? 121.170 171.623 88.002  1.00 26.21 ?  981  HIS B CA   1 
ATOM   14261 C C    . HIS B 1 981  ? 119.837 171.985 87.364  1.00 27.22 ?  981  HIS B C    1 
ATOM   14262 O O    . HIS B 1 981  ? 119.757 172.946 86.591  1.00 25.89 ?  981  HIS B O    1 
ATOM   14263 C CB   . HIS B 1 981  ? 121.537 172.640 89.088  1.00 22.52 ?  981  HIS B CB   1 
ATOM   14264 C CG   . HIS B 1 981  ? 120.739 172.501 90.348  1.00 25.29 ?  981  HIS B CG   1 
ATOM   14265 N ND1  . HIS B 1 981  ? 119.379 172.716 90.398  1.00 24.83 ?  981  HIS B ND1  1 
ATOM   14266 C CD2  . HIS B 1 981  ? 121.115 172.181 91.609  1.00 25.68 ?  981  HIS B CD2  1 
ATOM   14267 C CE1  . HIS B 1 981  ? 118.949 172.527 91.633  1.00 27.05 ?  981  HIS B CE1  1 
ATOM   14268 N NE2  . HIS B 1 981  ? 119.983 172.202 92.388  1.00 26.65 ?  981  HIS B NE2  1 
ATOM   14269 N N    . PHE B 1 982  ? 118.797 171.220 87.685  1.00 21.98 ?  982  PHE B N    1 
ATOM   14270 C CA   . PHE B 1 982  ? 117.465 171.453 87.152  1.00 21.50 ?  982  PHE B CA   1 
ATOM   14271 C C    . PHE B 1 982  ? 116.460 171.485 88.294  1.00 22.87 ?  982  PHE B C    1 
ATOM   14272 O O    . PHE B 1 982  ? 116.641 170.826 89.322  1.00 22.76 ?  982  PHE B O    1 
ATOM   14273 C CB   . PHE B 1 982  ? 117.066 170.374 86.137  1.00 17.80 ?  982  PHE B CB   1 
ATOM   14274 C CG   . PHE B 1 982  ? 117.790 170.473 84.825  1.00 22.93 ?  982  PHE B CG   1 
ATOM   14275 C CD1  . PHE B 1 982  ? 119.047 169.914 84.667  1.00 22.66 ?  982  PHE B CD1  1 
ATOM   14276 C CD2  . PHE B 1 982  ? 117.210 171.121 83.748  1.00 25.09 ?  982  PHE B CD2  1 
ATOM   14277 C CE1  . PHE B 1 982  ? 119.714 170.002 83.459  1.00 23.75 ?  982  PHE B CE1  1 
ATOM   14278 C CE2  . PHE B 1 982  ? 117.871 171.213 82.538  1.00 21.57 ?  982  PHE B CE2  1 
ATOM   14279 C CZ   . PHE B 1 982  ? 119.124 170.653 82.393  1.00 21.54 ?  982  PHE B CZ   1 
ATOM   14280 N N    . ASP B 1 983  ? 115.396 172.255 88.100  1.00 22.73 ?  983  ASP B N    1 
ATOM   14281 C CA   . ASP B 1 983  ? 114.354 172.421 89.098  1.00 21.08 ?  983  ASP B CA   1 
ATOM   14282 C C    . ASP B 1 983  ? 113.162 171.527 88.760  1.00 22.22 ?  983  ASP B C    1 
ATOM   14283 O O    . ASP B 1 983  ? 113.206 170.713 87.833  1.00 27.02 ?  983  ASP B O    1 
ATOM   14284 C CB   . ASP B 1 983  ? 113.955 173.895 89.194  1.00 23.15 ?  983  ASP B CB   1 
ATOM   14285 C CG   . ASP B 1 983  ? 115.135 174.832 89.022  1.00 25.65 ?  983  ASP B CG   1 
ATOM   14286 O OD1  . ASP B 1 983  ? 116.153 174.643 89.720  1.00 25.07 ?  983  ASP B OD1  1 
ATOM   14287 O OD2  . ASP B 1 983  ? 115.045 175.759 88.189  1.00 26.76 ?  983  ASP B OD2  1 
ATOM   14288 N N    . TYR B 1 984  ? 112.084 171.673 89.527  1.00 22.82 ?  984  TYR B N    1 
ATOM   14289 C CA   . TYR B 1 984  ? 110.887 170.869 89.319  1.00 23.19 ?  984  TYR B CA   1 
ATOM   14290 C C    . TYR B 1 984  ? 110.185 171.286 88.031  1.00 24.68 ?  984  TYR B C    1 
ATOM   14291 O O    . TYR B 1 984  ? 109.978 172.477 87.780  1.00 25.23 ?  984  TYR B O    1 
ATOM   14292 C CB   . TYR B 1 984  ? 109.944 171.025 90.514  1.00 23.61 ?  984  TYR B CB   1 
ATOM   14293 C CG   . TYR B 1 984  ? 108.748 170.091 90.529  1.00 23.28 ?  984  TYR B CG   1 
ATOM   14294 C CD1  . TYR B 1 984  ? 108.770 168.878 89.853  1.00 22.13 ?  984  TYR B CD1  1 
ATOM   14295 C CD2  . TYR B 1 984  ? 107.594 170.430 91.224  1.00 23.69 ?  984  TYR B CD2  1 
ATOM   14296 C CE1  . TYR B 1 984  ? 107.678 168.030 89.868  1.00 23.73 ?  984  TYR B CE1  1 
ATOM   14297 C CE2  . TYR B 1 984  ? 106.497 169.588 91.246  1.00 23.06 ?  984  TYR B CE2  1 
ATOM   14298 C CZ   . TYR B 1 984  ? 106.545 168.390 90.566  1.00 23.11 ?  984  TYR B CZ   1 
ATOM   14299 O OH   . TYR B 1 984  ? 105.457 167.548 90.584  1.00 21.06 ?  984  TYR B OH   1 
ATOM   14300 N N    . GLY B 1 985  ? 109.820 170.299 87.212  1.00 24.31 ?  985  GLY B N    1 
ATOM   14301 C CA   . GLY B 1 985  ? 109.025 170.524 86.025  1.00 22.45 ?  985  GLY B CA   1 
ATOM   14302 C C    . GLY B 1 985  ? 109.808 170.697 84.743  1.00 24.16 ?  985  GLY B C    1 
ATOM   14303 O O    . GLY B 1 985  ? 109.205 170.664 83.663  1.00 23.77 ?  985  GLY B O    1 
ATOM   14304 N N    . GLU B 1 986  ? 111.123 170.881 84.824  1.00 24.36 ?  986  GLU B N    1 
ATOM   14305 C CA   . GLU B 1 986  ? 111.924 171.066 83.624  1.00 22.98 ?  986  GLU B CA   1 
ATOM   14306 C C    . GLU B 1 986  ? 112.020 169.767 82.832  1.00 23.03 ?  986  GLU B C    1 
ATOM   14307 O O    . GLU B 1 986  ? 111.939 168.666 83.383  1.00 21.97 ?  986  GLU B O    1 
ATOM   14308 C CB   . GLU B 1 986  ? 113.323 171.565 83.987  1.00 25.75 ?  986  GLU B CB   1 
ATOM   14309 C CG   . GLU B 1 986  ? 113.337 172.630 85.071  1.00 26.46 ?  986  GLU B CG   1 
ATOM   14310 C CD   . GLU B 1 986  ? 114.327 173.742 84.786  1.00 28.27 ?  986  GLU B CD   1 
ATOM   14311 O OE1  . GLU B 1 986  ? 115.077 173.634 83.793  1.00 26.47 ?  986  GLU B OE1  1 
ATOM   14312 O OE2  . GLU B 1 986  ? 114.354 174.727 85.553  1.00 26.47 ?  986  GLU B OE2  1 
ATOM   14313 N N    . VAL B 1 987  ? 112.178 169.906 81.519  1.00 22.44 ?  987  VAL B N    1 
ATOM   14314 C CA   . VAL B 1 987  ? 112.343 168.778 80.611  1.00 20.39 ?  987  VAL B CA   1 
ATOM   14315 C C    . VAL B 1 987  ? 113.777 168.806 80.104  1.00 22.11 ?  987  VAL B C    1 
ATOM   14316 O O    . VAL B 1 987  ? 114.244 169.835 79.598  1.00 21.25 ?  987  VAL B O    1 
ATOM   14317 C CB   . VAL B 1 987  ? 111.330 168.831 79.452  1.00 18.91 ?  987  VAL B CB   1 
ATOM   14318 C CG1  . VAL B 1 987  ? 111.875 168.137 78.208  1.00 19.68 ?  987  VAL B CG1  1 
ATOM   14319 C CG2  . VAL B 1 987  ? 110.003 168.218 79.877  1.00 17.55 ?  987  VAL B CG2  1 
ATOM   14320 N N    . ILE B 1 988  ? 114.485 167.689 80.263  1.00 20.45 ?  988  ILE B N    1 
ATOM   14321 C CA   . ILE B 1 988  ? 115.904 167.662 79.930  1.00 19.71 ?  988  ILE B CA   1 
ATOM   14322 C C    . ILE B 1 988  ? 116.107 167.372 78.447  1.00 24.05 ?  988  ILE B C    1 
ATOM   14323 O O    . ILE B 1 988  ? 116.866 168.066 77.763  1.00 21.89 ?  988  ILE B O    1 
ATOM   14324 C CB   . ILE B 1 988  ? 116.639 166.641 80.815  1.00 19.37 ?  988  ILE B CB   1 
ATOM   14325 C CG1  . ILE B 1 988  ? 116.135 166.734 82.256  1.00 18.79 ?  988  ILE B CG1  1 
ATOM   14326 C CG2  . ILE B 1 988  ? 118.127 166.919 80.796  1.00 19.59 ?  988  ILE B CG2  1 
ATOM   14327 C CD1  . ILE B 1 988  ? 116.874 165.835 83.224  1.00 19.33 ?  988  ILE B CD1  1 
ATOM   14328 N N    . VAL B 1 989  ? 115.442 166.340 77.931  1.00 22.88 ?  989  VAL B N    1 
ATOM   14329 C CA   . VAL B 1 989  ? 115.536 165.980 76.519  1.00 23.10 ?  989  VAL B CA   1 
ATOM   14330 C C    . VAL B 1 989  ? 114.217 165.343 76.093  1.00 21.86 ?  989  VAL B C    1 
ATOM   14331 O O    . VAL B 1 989  ? 113.661 164.507 76.811  1.00 27.24 ?  989  VAL B O    1 
ATOM   14332 C CB   . VAL B 1 989  ? 116.739 165.045 76.252  1.00 21.38 ?  989  VAL B CB   1 
ATOM   14333 C CG1  . VAL B 1 989  ? 116.801 163.926 77.280  1.00 21.22 ?  989  VAL B CG1  1 
ATOM   14334 C CG2  . VAL B 1 989  ? 116.696 164.477 74.840  1.00 21.30 ?  989  VAL B CG2  1 
ATOM   14335 N N    . ARG B 1 990  ? 113.710 165.752 74.933  1.00 20.75 ?  990  ARG B N    1 
ATOM   14336 C CA   . ARG B 1 990  ? 112.457 165.247 74.392  1.00 25.27 ?  990  ARG B CA   1 
ATOM   14337 C C    . ARG B 1 990  ? 112.717 164.121 73.395  1.00 28.08 ?  990  ARG B C    1 
ATOM   14338 O O    . ARG B 1 990  ? 113.851 163.861 72.989  1.00 28.48 ?  990  ARG B O    1 
ATOM   14339 C CB   . ARG B 1 990  ? 111.666 166.378 73.727  1.00 25.48 ?  990  ARG B CB   1 
ATOM   14340 C CG   . ARG B 1 990  ? 110.834 167.207 74.692  1.00 25.05 ?  990  ARG B CG   1 
ATOM   14341 C CD   . ARG B 1 990  ? 111.062 168.695 74.474  1.00 24.50 ?  990  ARG B CD   1 
ATOM   14342 N NE   . ARG B 1 990  ? 110.349 169.507 75.453  1.00 27.35 ?  990  ARG B NE   1 
ATOM   14343 C CZ   . ARG B 1 990  ? 110.780 170.673 75.915  1.00 27.56 ?  990  ARG B CZ   1 
ATOM   14344 N NH1  . ARG B 1 990  ? 111.926 171.196 75.510  1.00 28.92 ?  990  ARG B NH1  1 
ATOM   14345 N NH2  . ARG B 1 990  ? 110.044 171.330 76.807  1.00 26.22 ?  990  ARG B NH2  1 
ATOM   14346 N N    . GLU B 1 991  ? 111.637 163.447 73.003  1.00 27.40 ?  991  GLU B N    1 
ATOM   14347 C CA   . GLU B 1 991  ? 111.739 162.353 72.048  1.00 26.21 ?  991  GLU B CA   1 
ATOM   14348 C C    . GLU B 1 991  ? 112.004 162.879 70.642  1.00 26.96 ?  991  GLU B C    1 
ATOM   14349 O O    . GLU B 1 991  ? 111.673 164.020 70.306  1.00 23.65 ?  991  GLU B O    1 
ATOM   14350 C CB   . GLU B 1 991  ? 110.460 161.514 72.050  1.00 24.55 ?  991  GLU B CB   1 
ATOM   14351 C CG   . GLU B 1 991  ? 109.922 161.197 73.431  1.00 27.09 ?  991  GLU B CG   1 
ATOM   14352 C CD   . GLU B 1 991  ? 108.622 160.418 73.387  1.00 31.37 ?  991  GLU B CD   1 
ATOM   14353 O OE1  . GLU B 1 991  ? 108.415 159.658 72.417  1.00 26.95 ?  991  GLU B OE1  1 
ATOM   14354 O OE2  . GLU B 1 991  ? 107.807 160.565 74.322  1.00 30.66 ?  991  GLU B OE2  1 
ATOM   14355 N N    . GLY B 1 992  ? 112.612 162.028 69.815  1.00 27.16 ?  992  GLY B N    1 
ATOM   14356 C CA   . GLY B 1 992  ? 112.885 162.352 68.432  1.00 26.85 ?  992  GLY B CA   1 
ATOM   14357 C C    . GLY B 1 992  ? 114.115 163.197 68.190  1.00 26.58 ?  992  GLY B C    1 
ATOM   14358 O O    . GLY B 1 992  ? 114.658 163.169 67.078  1.00 26.67 ?  992  GLY B O    1 
ATOM   14359 N N    . ASP B 1 993  ? 114.575 163.947 69.187  1.00 24.41 ?  993  ASP B N    1 
ATOM   14360 C CA   . ASP B 1 993  ? 115.745 164.792 69.021  1.00 25.57 ?  993  ASP B CA   1 
ATOM   14361 C C    . ASP B 1 993  ? 117.013 163.944 68.959  1.00 25.87 ?  993  ASP B C    1 
ATOM   14362 O O    . ASP B 1 993  ? 117.068 162.818 69.460  1.00 26.28 ?  993  ASP B O    1 
ATOM   14363 C CB   . ASP B 1 993  ? 115.843 165.798 70.167  1.00 26.95 ?  993  ASP B CB   1 
ATOM   14364 C CG   . ASP B 1 993  ? 114.524 166.492 70.446  1.00 27.94 ?  993  ASP B CG   1 
ATOM   14365 O OD1  . ASP B 1 993  ? 113.745 166.699 69.492  1.00 26.62 ?  993  ASP B OD1  1 
ATOM   14366 O OD2  . ASP B 1 993  ? 114.265 166.826 71.621  1.00 25.92 ?  993  ASP B OD2  1 
ATOM   14367 N N    . GLU B 1 994  ? 118.039 164.501 68.322  1.00 28.33 ?  994  GLU B N    1 
ATOM   14368 C CA   . GLU B 1 994  ? 119.327 163.827 68.245  1.00 28.83 ?  994  GLU B CA   1 
ATOM   14369 C C    . GLU B 1 994  ? 119.977 163.767 69.623  1.00 27.76 ?  994  GLU B C    1 
ATOM   14370 O O    . GLU B 1 994  ? 119.764 164.634 70.475  1.00 29.85 ?  994  GLU B O    1 
ATOM   14371 C CB   . GLU B 1 994  ? 120.248 164.544 67.257  1.00 27.41 ?  994  GLU B CB   1 
ATOM   14372 C CG   . GLU B 1 994  ? 121.017 163.609 66.336  1.00 27.39 ?  994  GLU B CG   1 
ATOM   14373 C CD   . GLU B 1 994  ? 122.242 163.010 66.998  1.00 31.85 ?  994  GLU B CD   1 
ATOM   14374 O OE1  . GLU B 1 994  ? 122.819 163.669 67.887  1.00 30.84 ?  994  GLU B OE1  1 
ATOM   14375 O OE2  . GLU B 1 994  ? 122.626 161.880 66.629  1.00 31.30 ?  994  GLU B OE2  1 
ATOM   14376 N N    . SER B 1 995  ? 120.773 162.722 69.837  1.00 22.80 ?  995  SER B N    1 
ATOM   14377 C CA   . SER B 1 995  ? 121.395 162.484 71.136  1.00 24.97 ?  995  SER B CA   1 
ATOM   14378 C C    . SER B 1 995  ? 122.487 163.518 71.382  1.00 24.66 ?  995  SER B C    1 
ATOM   14379 O O    . SER B 1 995  ? 123.547 163.477 70.748  1.00 24.44 ?  995  SER B O    1 
ATOM   14380 C CB   . SER B 1 995  ? 121.957 161.068 71.192  1.00 24.11 ?  995  SER B CB   1 
ATOM   14381 O OG   . SER B 1 995  ? 120.926 160.114 71.007  1.00 24.95 ?  995  SER B OG   1 
ATOM   14382 N N    . ASP B 1 996  ? 122.227 164.449 72.302  1.00 23.14 ?  996  ASP B N    1 
ATOM   14383 C CA   . ASP B 1 996  ? 123.212 165.477 72.620  1.00 23.90 ?  996  ASP B CA   1 
ATOM   14384 C C    . ASP B 1 996  ? 124.415 164.891 73.350  1.00 26.88 ?  996  ASP B C    1 
ATOM   14385 O O    . ASP B 1 996  ? 125.555 165.299 73.102  1.00 25.36 ?  996  ASP B O    1 
ATOM   14386 C CB   . ASP B 1 996  ? 122.565 166.582 73.454  1.00 22.31 ?  996  ASP B CB   1 
ATOM   14387 C CG   . ASP B 1 996  ? 123.435 167.820 73.559  1.00 28.35 ?  996  ASP B CG   1 
ATOM   14388 O OD1  . ASP B 1 996  ? 124.369 167.966 72.743  1.00 31.22 ?  996  ASP B OD1  1 
ATOM   14389 O OD2  . ASP B 1 996  ? 123.186 168.648 74.460  1.00 28.57 ?  996  ASP B OD2  1 
ATOM   14390 N N    . GLY B 1 997  ? 124.186 163.942 74.247  1.00 25.34 ?  997  GLY B N    1 
ATOM   14391 C CA   . GLY B 1 997  ? 125.281 163.380 75.011  1.00 22.16 ?  997  GLY B CA   1 
ATOM   14392 C C    . GLY B 1 997  ? 124.798 162.346 76.000  1.00 22.57 ?  997  GLY B C    1 
ATOM   14393 O O    . GLY B 1 997  ? 123.695 161.811 75.876  1.00 22.99 ?  997  GLY B O    1 
ATOM   14394 N N    . LEU B 1 998  ? 125.643 162.072 76.990  1.00 25.45 ?  998  LEU B N    1 
ATOM   14395 C CA   . LEU B 1 998  ? 125.391 161.044 77.990  1.00 22.26 ?  998  LEU B CA   1 
ATOM   14396 C C    . LEU B 1 998  ? 125.219 161.691 79.357  1.00 21.73 ?  998  LEU B C    1 
ATOM   14397 O O    . LEU B 1 998  ? 126.040 162.519 79.765  1.00 23.14 ?  998  LEU B O    1 
ATOM   14398 C CB   . LEU B 1 998  ? 126.537 160.028 78.017  1.00 17.23 ?  998  LEU B CB   1 
ATOM   14399 C CG   . LEU B 1 998  ? 126.451 158.867 79.007  1.00 16.24 ?  998  LEU B CG   1 
ATOM   14400 C CD1  . LEU B 1 998  ? 126.722 157.552 78.297  1.00 18.96 ?  998  LEU B CD1  1 
ATOM   14401 C CD2  . LEU B 1 998  ? 127.429 159.066 80.154  1.00 21.58 ?  998  LEU B CD2  1 
ATOM   14402 N N    . PHE B 1 999  ? 124.155 161.311 80.057  1.00 15.31 ?  999  PHE B N    1 
ATOM   14403 C CA   . PHE B 1 999  ? 123.831 161.843 81.371  1.00 12.41 ?  999  PHE B CA   1 
ATOM   14404 C C    . PHE B 1 999  ? 124.318 160.904 82.470  1.00 15.47 ?  999  PHE B C    1 
ATOM   14405 O O    . PHE B 1 999  ? 124.700 159.758 82.225  1.00 21.03 ?  999  PHE B O    1 
ATOM   14406 C CB   . PHE B 1 999  ? 122.320 162.058 81.502  1.00 15.66 ?  999  PHE B CB   1 
ATOM   14407 C CG   . PHE B 1 999  ? 121.782 163.161 80.639  1.00 22.54 ?  999  PHE B CG   1 
ATOM   14408 C CD1  . PHE B 1 999  ? 122.599 164.198 80.221  1.00 21.85 ?  999  PHE B CD1  1 
ATOM   14409 C CD2  . PHE B 1 999  ? 120.458 163.154 80.235  1.00 23.35 ?  999  PHE B CD2  1 
ATOM   14410 C CE1  . PHE B 1 999  ? 122.099 165.213 79.426  1.00 21.23 ?  999  PHE B CE1  1 
ATOM   14411 C CE2  . PHE B 1 999  ? 119.956 164.162 79.437  1.00 20.82 ?  999  PHE B CE2  1 
ATOM   14412 C CZ   . PHE B 1 999  ? 120.778 165.194 79.033  1.00 21.46 ?  999  PHE B CZ   1 
ATOM   14413 N N    . LEU B 1 1000 ? 124.296 161.412 83.700  1.00 10.96 ?  1000 LEU B N    1 
ATOM   14414 C CA   . LEU B 1 1000 ? 124.549 160.587 84.880  1.00 9.07  ?  1000 LEU B CA   1 
ATOM   14415 C C    . LEU B 1 1000 ? 123.901 161.296 86.061  1.00 17.69 ?  1000 LEU B C    1 
ATOM   14416 O O    . LEU B 1 1000 ? 124.357 162.371 86.461  1.00 25.52 ?  1000 LEU B O    1 
ATOM   14417 C CB   . LEU B 1 1000 ? 126.044 160.381 85.104  1.00 9.29  ?  1000 LEU B CB   1 
ATOM   14418 C CG   . LEU B 1 1000 ? 126.477 159.879 86.485  1.00 13.91 ?  1000 LEU B CG   1 
ATOM   14419 C CD1  . LEU B 1 1000 ? 126.000 158.455 86.707  1.00 17.59 ?  1000 LEU B CD1  1 
ATOM   14420 C CD2  . LEU B 1 1000 ? 127.985 159.968 86.648  1.00 20.26 ?  1000 LEU B CD2  1 
ATOM   14421 N N    . ILE B 1 1001 ? 122.839 160.705 86.605  1.00 17.97 ?  1001 ILE B N    1 
ATOM   14422 C CA   . ILE B 1 1001 ? 122.112 161.327 87.706  1.00 16.44 ?  1001 ILE B CA   1 
ATOM   14423 C C    . ILE B 1 1001 ? 122.914 161.164 88.989  1.00 12.58 ?  1001 ILE B C    1 
ATOM   14424 O O    . ILE B 1 1001 ? 123.227 160.043 89.406  1.00 15.15 ?  1001 ILE B O    1 
ATOM   14425 C CB   . ILE B 1 1001 ? 120.709 160.724 87.849  1.00 9.75  ?  1001 ILE B CB   1 
ATOM   14426 C CG1  . ILE B 1 1001 ? 120.108 160.437 86.473  1.00 10.11 ?  1001 ILE B CG1  1 
ATOM   14427 C CG2  . ILE B 1 1001 ? 119.814 161.645 88.658  1.00 11.96 ?  1001 ILE B CG2  1 
ATOM   14428 C CD1  . ILE B 1 1001 ? 119.694 161.680 85.723  1.00 14.92 ?  1001 ILE B CD1  1 
ATOM   14429 N N    . VAL B 1 1002 ? 123.253 162.285 89.621  1.00 8.88  ?  1002 VAL B N    1 
ATOM   14430 C CA   . VAL B 1 1002 ? 123.976 162.258 90.884  1.00 15.66 ?  1002 VAL B CA   1 
ATOM   14431 C C    . VAL B 1 1002 ? 123.149 162.785 92.050  1.00 18.65 ?  1002 VAL B C    1 
ATOM   14432 O O    . VAL B 1 1002 ? 123.531 162.552 93.208  1.00 19.55 ?  1002 VAL B O    1 
ATOM   14433 C CB   . VAL B 1 1002 ? 125.314 163.022 90.785  1.00 20.07 ?  1002 VAL B CB   1 
ATOM   14434 C CG1  . VAL B 1 1002 ? 126.019 162.686 89.484  1.00 19.49 ?  1002 VAL B CG1  1 
ATOM   14435 C CG2  . VAL B 1 1002 ? 125.100 164.521 90.911  1.00 19.48 ?  1002 VAL B CG2  1 
ATOM   14436 N N    . SER B 1 1003 ? 122.034 163.469 91.796  1.00 13.85 ?  1003 SER B N    1 
ATOM   14437 C CA   . SER B 1 1003 ? 121.151 163.884 92.883  1.00 14.32 ?  1003 SER B CA   1 
ATOM   14438 C C    . SER B 1 1003 ? 119.728 163.990 92.362  1.00 19.37 ?  1003 SER B C    1 
ATOM   14439 O O    . SER B 1 1003 ? 119.482 164.723 91.403  1.00 18.73 ?  1003 SER B O    1 
ATOM   14440 C CB   . SER B 1 1003 ? 121.601 165.221 93.479  1.00 22.14 ?  1003 SER B CB   1 
ATOM   14441 O OG   . SER B 1 1003 ? 120.657 165.708 94.419  1.00 23.24 ?  1003 SER B OG   1 
ATOM   14442 N N    . GLY B 1 1004 ? 118.803 163.278 92.986  1.00 19.73 ?  1004 GLY B N    1 
ATOM   14443 C CA   . GLY B 1 1004 ? 117.394 163.497 92.729  1.00 18.81 ?  1004 GLY B CA   1 
ATOM   14444 C C    . GLY B 1 1004 ? 116.769 162.439 91.835  1.00 11.61 ?  1004 GLY B C    1 
ATOM   14445 O O    . GLY B 1 1004 ? 117.438 161.786 91.027  1.00 13.15 ?  1004 GLY B O    1 
ATOM   14446 N N    . LEU B 1 1005 ? 115.457 162.270 91.985  1.00 10.34 ?  1005 LEU B N    1 
ATOM   14447 C CA   . LEU B 1 1005 ? 114.661 161.391 91.144  1.00 11.37 ?  1005 LEU B CA   1 
ATOM   14448 C C    . LEU B 1 1005 ? 114.322 162.076 89.824  1.00 11.22 ?  1005 LEU B C    1 
ATOM   14449 O O    . LEU B 1 1005 ? 114.309 163.305 89.717  1.00 20.80 ?  1005 LEU B O    1 
ATOM   14450 C CB   . LEU B 1 1005 ? 113.372 160.986 91.862  1.00 15.57 ?  1005 LEU B CB   1 
ATOM   14451 C CG   . LEU B 1 1005 ? 112.695 159.677 91.454  1.00 12.83 ?  1005 LEU B CG   1 
ATOM   14452 C CD1  . LEU B 1 1005 ? 113.410 158.484 92.053  1.00 12.69 ?  1005 LEU B CD1  1 
ATOM   14453 C CD2  . LEU B 1 1005 ? 111.229 159.685 91.855  1.00 15.23 ?  1005 LEU B CD2  1 
ATOM   14454 N N    . VAL B 1 1006 ? 114.037 161.261 88.809  1.00 6.67  ?  1006 VAL B N    1 
ATOM   14455 C CA   . VAL B 1 1006 ? 113.694 161.776 87.489  1.00 9.44  ?  1006 VAL B CA   1 
ATOM   14456 C C    . VAL B 1 1006 ? 112.829 160.732 86.790  1.00 14.71 ?  1006 VAL B C    1 
ATOM   14457 O O    . VAL B 1 1006 ? 112.938 159.535 87.064  1.00 21.47 ?  1006 VAL B O    1 
ATOM   14458 C CB   . VAL B 1 1006 ? 114.979 162.123 86.695  1.00 7.25  ?  1006 VAL B CB   1 
ATOM   14459 C CG1  . VAL B 1 1006 ? 115.789 160.872 86.375  1.00 10.79 ?  1006 VAL B CG1  1 
ATOM   14460 C CG2  . VAL B 1 1006 ? 114.672 162.945 85.466  1.00 11.19 ?  1006 VAL B CG2  1 
ATOM   14461 N N    . LYS B 1 1007 ? 111.938 161.187 85.909  1.00 11.98 ?  1007 LYS B N    1 
ATOM   14462 C CA   . LYS B 1 1007 ? 110.966 160.317 85.257  1.00 8.76  ?  1007 LYS B CA   1 
ATOM   14463 C C    . LYS B 1 1007 ? 111.267 160.222 83.769  1.00 15.25 ?  1007 LYS B C    1 
ATOM   14464 O O    . LYS B 1 1007 ? 111.351 161.243 83.080  1.00 18.02 ?  1007 LYS B O    1 
ATOM   14465 C CB   . LYS B 1 1007 ? 109.539 160.829 85.477  1.00 9.39  ?  1007 LYS B CB   1 
ATOM   14466 C CG   . LYS B 1 1007 ? 108.488 160.159 84.606  1.00 14.31 ?  1007 LYS B CG   1 
ATOM   14467 C CD   . LYS B 1 1007 ? 107.081 160.511 85.067  1.00 15.63 ?  1007 LYS B CD   1 
ATOM   14468 C CE   . LYS B 1 1007 ? 106.110 160.572 83.899  1.00 13.90 ?  1007 LYS B CE   1 
ATOM   14469 N NZ   . LYS B 1 1007 ? 106.591 161.488 82.829  1.00 11.04 ?  1007 LYS B NZ   1 
ATOM   14470 N N    . LEU B 1 1008 ? 111.416 158.993 83.277  1.00 15.75 ?  1008 LEU B N    1 
ATOM   14471 C CA   . LEU B 1 1008 ? 111.711 158.708 81.877  1.00 12.23 ?  1008 LEU B CA   1 
ATOM   14472 C C    . LEU B 1 1008 ? 110.475 158.053 81.272  1.00 15.59 ?  1008 LEU B C    1 
ATOM   14473 O O    . LEU B 1 1008 ? 110.166 156.899 81.586  1.00 19.12 ?  1008 LEU B O    1 
ATOM   14474 C CB   . LEU B 1 1008 ? 112.934 157.797 81.772  1.00 14.63 ?  1008 LEU B CB   1 
ATOM   14475 C CG   . LEU B 1 1008 ? 113.336 157.186 80.429  1.00 16.43 ?  1008 LEU B CG   1 
ATOM   14476 C CD1  . LEU B 1 1008 ? 114.260 158.124 79.675  1.00 16.92 ?  1008 LEU B CD1  1 
ATOM   14477 C CD2  . LEU B 1 1008 ? 113.995 155.829 80.632  1.00 14.66 ?  1008 LEU B CD2  1 
ATOM   14478 N N    . TYR B 1 1009 ? 109.760 158.785 80.417  1.00 15.84 ?  1009 TYR B N    1 
ATOM   14479 C CA   . TYR B 1 1009 ? 108.488 158.314 79.883  1.00 21.97 ?  1009 TYR B CA   1 
ATOM   14480 C C    . TYR B 1 1009 ? 108.467 158.481 78.372  1.00 23.92 ?  1009 TYR B C    1 
ATOM   14481 O O    . TYR B 1 1009 ? 108.881 159.518 77.851  1.00 19.79 ?  1009 TYR B O    1 
ATOM   14482 C CB   . TYR B 1 1009 ? 107.311 159.072 80.522  1.00 21.64 ?  1009 TYR B CB   1 
ATOM   14483 C CG   . TYR B 1 1009 ? 106.116 159.282 79.615  1.00 23.85 ?  1009 TYR B CG   1 
ATOM   14484 C CD1  . TYR B 1 1009 ? 105.227 158.247 79.352  1.00 21.94 ?  1009 TYR B CD1  1 
ATOM   14485 C CD2  . TYR B 1 1009 ? 105.867 160.521 79.037  1.00 22.12 ?  1009 TYR B CD2  1 
ATOM   14486 C CE1  . TYR B 1 1009 ? 104.131 158.437 78.529  1.00 24.59 ?  1009 TYR B CE1  1 
ATOM   14487 C CE2  . TYR B 1 1009 ? 104.775 160.720 78.213  1.00 23.19 ?  1009 TYR B CE2  1 
ATOM   14488 C CZ   . TYR B 1 1009 ? 103.911 159.675 77.963  1.00 25.96 ?  1009 TYR B CZ   1 
ATOM   14489 O OH   . TYR B 1 1009 ? 102.823 159.870 77.143  1.00 22.36 ?  1009 TYR B OH   1 
ATOM   14490 N N    . GLY B 1 1010 ? 107.974 157.467 77.672  1.00 26.44 ?  1010 GLY B N    1 
ATOM   14491 C CA   . GLY B 1 1010 ? 107.928 157.542 76.226  1.00 25.54 ?  1010 GLY B CA   1 
ATOM   14492 C C    . GLY B 1 1010 ? 107.349 156.288 75.617  1.00 25.34 ?  1010 GLY B C    1 
ATOM   14493 O O    . GLY B 1 1010 ? 106.594 155.558 76.261  1.00 24.54 ?  1010 GLY B O    1 
ATOM   14494 N N    . LYS B 1 1011 ? 107.702 156.056 74.357  1.00 25.37 ?  1011 LYS B N    1 
ATOM   14495 C CA   . LYS B 1 1011 ? 107.243 154.877 73.632  1.00 25.66 ?  1011 LYS B CA   1 
ATOM   14496 C C    . LYS B 1 1011 ? 108.403 153.934 73.332  1.00 25.83 ?  1011 LYS B C    1 
ATOM   14497 O O    . LYS B 1 1011 ? 109.532 154.374 73.115  1.00 25.42 ?  1011 LYS B O    1 
ATOM   14498 C CB   . LYS B 1 1011 ? 106.544 155.282 72.333  1.00 24.06 ?  1011 LYS B CB   1 
ATOM   14499 C CG   . LYS B 1 1011 ? 106.237 154.117 71.405  1.00 22.23 ?  1011 LYS B CG   1 
ATOM   14500 C CD   . LYS B 1 1011 ? 105.022 153.338 71.879  1.00 25.07 ?  1011 LYS B CD   1 
ATOM   14501 C CE   . LYS B 1 1011 ? 104.665 152.223 70.909  1.00 26.82 ?  1011 LYS B CE   1 
ATOM   14502 N NZ   . LYS B 1 1011 ? 103.236 151.820 71.028  1.00 28.13 ?  1011 LYS B NZ   1 
ATOM   14503 N N    . VAL B 1 1031 ? 104.508 154.528 75.622  1.00 24.74 ?  1031 VAL B N    1 
ATOM   14504 C CA   . VAL B 1 1031 ? 103.533 153.842 76.457  1.00 25.50 ?  1031 VAL B CA   1 
ATOM   14505 C C    . VAL B 1 1031 ? 104.154 153.468 77.797  1.00 26.85 ?  1031 VAL B C    1 
ATOM   14506 O O    . VAL B 1 1031 ? 103.444 153.243 78.777  1.00 25.96 ?  1031 VAL B O    1 
ATOM   14507 C CB   . VAL B 1 1031 ? 102.976 152.593 75.752  1.00 23.74 ?  1031 VAL B CB   1 
ATOM   14508 C CG1  . VAL B 1 1031 ? 101.966 152.989 74.685  1.00 23.75 ?  1031 VAL B CG1  1 
ATOM   14509 C CG2  . VAL B 1 1031 ? 104.107 151.771 75.153  1.00 24.15 ?  1031 VAL B CG2  1 
ATOM   14510 N N    . PHE B 1 1032 ? 105.480 153.405 77.837  1.00 24.07 ?  1032 PHE B N    1 
ATOM   14511 C CA   . PHE B 1 1032 ? 106.203 152.997 79.031  1.00 22.69 ?  1032 PHE B CA   1 
ATOM   14512 C C    . PHE B 1 1032 ? 106.675 154.211 79.826  1.00 22.52 ?  1032 PHE B C    1 
ATOM   14513 O O    . PHE B 1 1032 ? 106.840 155.314 79.296  1.00 20.16 ?  1032 PHE B O    1 
ATOM   14514 C CB   . PHE B 1 1032 ? 107.392 152.100 78.669  1.00 21.60 ?  1032 PHE B CB   1 
ATOM   14515 C CG   . PHE B 1 1032 ? 108.678 152.845 78.440  1.00 22.96 ?  1032 PHE B CG   1 
ATOM   14516 C CD1  . PHE B 1 1032 ? 108.864 153.605 77.297  1.00 23.68 ?  1032 PHE B CD1  1 
ATOM   14517 C CD2  . PHE B 1 1032 ? 109.708 152.774 79.366  1.00 21.05 ?  1032 PHE B CD2  1 
ATOM   14518 C CE1  . PHE B 1 1032 ? 110.048 154.288 77.085  1.00 23.09 ?  1032 PHE B CE1  1 
ATOM   14519 C CE2  . PHE B 1 1032 ? 110.893 153.454 79.161  1.00 21.44 ?  1032 PHE B CE2  1 
ATOM   14520 C CZ   . PHE B 1 1032 ? 111.064 154.211 78.019  1.00 20.13 ?  1032 PHE B CZ   1 
ATOM   14521 N N    . GLU B 1 1033 ? 106.882 153.985 81.121  1.00 24.56 ?  1033 GLU B N    1 
ATOM   14522 C CA   . GLU B 1 1033 ? 107.288 155.031 82.050  1.00 22.49 ?  1033 GLU B CA   1 
ATOM   14523 C C    . GLU B 1 1033 ? 108.068 154.390 83.187  1.00 22.41 ?  1033 GLU B C    1 
ATOM   14524 O O    . GLU B 1 1033 ? 107.636 153.373 83.737  1.00 24.44 ?  1033 GLU B O    1 
ATOM   14525 C CB   . GLU B 1 1033 ? 106.068 155.786 82.591  1.00 22.11 ?  1033 GLU B CB   1 
ATOM   14526 C CG   . GLU B 1 1033 ? 106.349 156.660 83.800  1.00 22.92 ?  1033 GLU B CG   1 
ATOM   14527 C CD   . GLU B 1 1033 ? 105.082 157.216 84.420  1.00 25.25 ?  1033 GLU B CD   1 
ATOM   14528 O OE1  . GLU B 1 1033 ? 104.008 157.088 83.797  1.00 26.48 ?  1033 GLU B OE1  1 
ATOM   14529 O OE2  . GLU B 1 1033 ? 105.160 157.778 85.533  1.00 22.61 ?  1033 GLU B OE2  1 
ATOM   14530 N N    . ASP B 1 1034 ? 109.212 154.979 83.531  1.00 16.31 ?  1034 ASP B N    1 
ATOM   14531 C CA   . ASP B 1 1034 ? 110.054 154.475 84.605  1.00 14.33 ?  1034 ASP B CA   1 
ATOM   14532 C C    . ASP B 1 1034 ? 110.627 155.651 85.381  1.00 15.09 ?  1034 ASP B C    1 
ATOM   14533 O O    . ASP B 1 1034 ? 110.547 156.805 84.956  1.00 20.00 ?  1034 ASP B O    1 
ATOM   14534 C CB   . ASP B 1 1034 ? 111.180 153.582 84.069  1.00 15.47 ?  1034 ASP B CB   1 
ATOM   14535 C CG   . ASP B 1 1034 ? 111.510 152.434 85.005  1.00 21.37 ?  1034 ASP B CG   1 
ATOM   14536 O OD1  . ASP B 1 1034 ? 110.668 152.106 85.868  1.00 18.22 ?  1034 ASP B OD1  1 
ATOM   14537 O OD2  . ASP B 1 1034 ? 112.611 151.858 84.879  1.00 21.59 ?  1034 ASP B OD2  1 
ATOM   14538 N N    . TYR B 1 1035 ? 111.202 155.347 86.540  1.00 10.51 ?  1035 TYR B N    1 
ATOM   14539 C CA   . TYR B 1 1035 ? 111.832 156.344 87.394  1.00 7.00  ?  1035 TYR B CA   1 
ATOM   14540 C C    . TYR B 1 1035 ? 113.296 155.986 87.596  1.00 11.25 ?  1035 TYR B C    1 
ATOM   14541 O O    . TYR B 1 1035 ? 113.617 154.852 87.966  1.00 18.31 ?  1035 TYR B O    1 
ATOM   14542 C CB   . TYR B 1 1035 ? 111.115 156.447 88.743  1.00 10.84 ?  1035 TYR B CB   1 
ATOM   14543 C CG   . TYR B 1 1035 ? 109.705 156.982 88.647  1.00 12.71 ?  1035 TYR B CG   1 
ATOM   14544 C CD1  . TYR B 1 1035 ? 109.464 158.275 88.205  1.00 14.42 ?  1035 TYR B CD1  1 
ATOM   14545 C CD2  . TYR B 1 1035 ? 108.616 156.195 88.994  1.00 14.53 ?  1035 TYR B CD2  1 
ATOM   14546 C CE1  . TYR B 1 1035 ? 108.178 158.772 88.115  1.00 16.50 ?  1035 TYR B CE1  1 
ATOM   14547 C CE2  . TYR B 1 1035 ? 107.325 156.682 88.906  1.00 12.22 ?  1035 TYR B CE2  1 
ATOM   14548 C CZ   . TYR B 1 1035 ? 107.113 157.971 88.466  1.00 15.58 ?  1035 TYR B CZ   1 
ATOM   14549 O OH   . TYR B 1 1035 ? 105.831 158.462 88.377  1.00 17.29 ?  1035 TYR B OH   1 
ATOM   14550 N N    . LEU B 1 1036 ? 114.175 156.951 87.353  1.00 10.69 ?  1036 LEU B N    1 
ATOM   14551 C CA   . LEU B 1 1036 ? 115.603 156.792 87.560  1.00 12.16 ?  1036 LEU B CA   1 
ATOM   14552 C C    . LEU B 1 1036 ? 116.049 157.647 88.739  1.00 13.81 ?  1036 LEU B C    1 
ATOM   14553 O O    . LEU B 1 1036 ? 115.511 158.731 88.983  1.00 13.95 ?  1036 LEU B O    1 
ATOM   14554 C CB   . LEU B 1 1036 ? 116.392 157.174 86.305  1.00 11.13 ?  1036 LEU B CB   1 
ATOM   14555 C CG   . LEU B 1 1036 ? 116.071 156.355 85.056  1.00 11.85 ?  1036 LEU B CG   1 
ATOM   14556 C CD1  . LEU B 1 1036 ? 116.305 157.176 83.801  1.00 11.71 ?  1036 LEU B CD1  1 
ATOM   14557 C CD2  . LEU B 1 1036 ? 116.893 155.080 85.029  1.00 13.96 ?  1036 LEU B CD2  1 
ATOM   14558 N N    . THR B 1 1037 ? 117.042 157.146 89.461  1.00 9.44  ?  1037 THR B N    1 
ATOM   14559 C CA   . THR B 1 1037 ? 117.524 157.750 90.693  1.00 6.99  ?  1037 THR B CA   1 
ATOM   14560 C C    . THR B 1 1037 ? 119.033 157.980 90.527  1.00 9.98  ?  1037 THR B C    1 
ATOM   14561 O O    . THR B 1 1037 ? 119.567 157.901 89.417  1.00 14.52 ?  1037 THR B O    1 
ATOM   14562 C CB   . THR B 1 1037 ? 117.160 156.855 91.885  1.00 12.84 ?  1037 THR B CB   1 
ATOM   14563 O OG1  . THR B 1 1037 ? 115.849 156.322 91.678  1.00 18.05 ?  1037 THR B OG1  1 
ATOM   14564 C CG2  . THR B 1 1037 ? 117.077 157.665 93.180  1.00 14.89 ?  1037 THR B CG2  1 
ATOM   14565 N N    . VAL B 1 1038 ? 119.716 158.291 91.631  1.00 10.46 ?  1038 VAL B N    1 
ATOM   14566 C CA   . VAL B 1 1038 ? 121.135 158.613 91.586  1.00 8.74  ?  1038 VAL B CA   1 
ATOM   14567 C C    . VAL B 1 1038 ? 121.944 157.399 91.140  1.00 12.26 ?  1038 VAL B C    1 
ATOM   14568 O O    . VAL B 1 1038 ? 121.541 156.243 91.331  1.00 13.73 ?  1038 VAL B O    1 
ATOM   14569 C CB   . VAL B 1 1038 ? 121.603 159.127 92.960  1.00 6.44  ?  1038 VAL B CB   1 
ATOM   14570 C CG1  . VAL B 1 1038 ? 120.754 160.296 93.395  1.00 13.96 ?  1038 VAL B CG1  1 
ATOM   14571 C CG2  . VAL B 1 1038 ? 121.500 158.039 93.992  1.00 8.80  ?  1038 VAL B CG2  1 
ATOM   14572 N N    . GLY B 1 1039 ? 123.085 157.664 90.508  1.00 15.82 ?  1039 GLY B N    1 
ATOM   14573 C CA   . GLY B 1 1039 ? 123.958 156.606 90.046  1.00 11.19 ?  1039 GLY B CA   1 
ATOM   14574 C C    . GLY B 1 1039 ? 123.541 155.934 88.759  1.00 10.86 ?  1039 GLY B C    1 
ATOM   14575 O O    . GLY B 1 1039 ? 124.171 154.947 88.364  1.00 16.52 ?  1039 GLY B O    1 
ATOM   14576 N N    . ASN B 1 1040 ? 122.500 156.426 88.095  1.00 9.53  ?  1040 ASN B N    1 
ATOM   14577 C CA   . ASN B 1 1040 ? 122.000 155.830 86.867  1.00 9.11  ?  1040 ASN B CA   1 
ATOM   14578 C C    . ASN B 1 1040 ? 122.450 156.642 85.660  1.00 11.75 ?  1040 ASN B C    1 
ATOM   14579 O O    . ASN B 1 1040 ? 122.687 157.849 85.752  1.00 15.87 ?  1040 ASN B O    1 
ATOM   14580 C CB   . ASN B 1 1040 ? 120.473 155.729 86.888  1.00 11.53 ?  1040 ASN B CB   1 
ATOM   14581 C CG   . ASN B 1 1040 ? 119.976 154.511 87.648  1.00 16.32 ?  1040 ASN B CG   1 
ATOM   14582 O OD1  . ASN B 1 1040 ? 119.037 153.843 87.220  1.00 22.09 ?  1040 ASN B OD1  1 
ATOM   14583 N ND2  . ASN B 1 1040 ? 120.606 154.218 88.778  1.00 13.84 ?  1040 ASN B ND2  1 
ATOM   14584 N N    . VAL B 1 1041 ? 122.566 155.963 84.521  1.00 11.37 ?  1041 VAL B N    1 
ATOM   14585 C CA   . VAL B 1 1041 ? 123.080 156.545 83.287  1.00 8.79  ?  1041 VAL B CA   1 
ATOM   14586 C C    . VAL B 1 1041 ? 121.981 156.498 82.236  1.00 11.98 ?  1041 VAL B C    1 
ATOM   14587 O O    . VAL B 1 1041 ? 121.294 155.480 82.095  1.00 16.27 ?  1041 VAL B O    1 
ATOM   14588 C CB   . VAL B 1 1041 ? 124.338 155.804 82.796  1.00 8.86  ?  1041 VAL B CB   1 
ATOM   14589 C CG1  . VAL B 1 1041 ? 124.976 156.543 81.634  1.00 15.48 ?  1041 VAL B CG1  1 
ATOM   14590 C CG2  . VAL B 1 1041 ? 125.333 155.632 83.933  1.00 9.17  ?  1041 VAL B CG2  1 
ATOM   14591 N N    . ILE B 1 1042 ? 121.815 157.598 81.504  1.00 15.08 ?  1042 ILE B N    1 
ATOM   14592 C CA   . ILE B 1 1042 ? 120.823 157.709 80.440  1.00 15.26 ?  1042 ILE B CA   1 
ATOM   14593 C C    . ILE B 1 1042 ? 121.537 158.054 79.141  1.00 17.60 ?  1042 ILE B C    1 
ATOM   14594 O O    . ILE B 1 1042 ? 122.470 158.864 79.132  1.00 21.95 ?  1042 ILE B O    1 
ATOM   14595 C CB   . ILE B 1 1042 ? 119.752 158.775 80.756  1.00 12.96 ?  1042 ILE B CB   1 
ATOM   14596 C CG1  . ILE B 1 1042 ? 119.323 158.708 82.220  1.00 15.99 ?  1042 ILE B CG1  1 
ATOM   14597 C CG2  . ILE B 1 1042 ? 118.543 158.608 79.847  1.00 18.55 ?  1042 ILE B CG2  1 
ATOM   14598 C CD1  . ILE B 1 1042 ? 118.551 159.923 82.669  1.00 16.39 ?  1042 ILE B CD1  1 
ATOM   14599 N N    . GLY B 1 1043 ? 121.099 157.437 78.047  1.00 20.22 ?  1043 GLY B N    1 
ATOM   14600 C CA   . GLY B 1 1043 ? 121.577 157.807 76.730  1.00 23.09 ?  1043 GLY B CA   1 
ATOM   14601 C C    . GLY B 1 1043 ? 122.753 157.021 76.200  1.00 24.61 ?  1043 GLY B C    1 
ATOM   14602 O O    . GLY B 1 1043 ? 123.401 157.479 75.252  1.00 25.68 ?  1043 GLY B O    1 
ATOM   14603 N N    . GLU B 1 1044 ? 123.063 155.861 76.786  1.00 20.49 ?  1044 GLU B N    1 
ATOM   14604 C CA   . GLU B 1 1044 ? 124.163 155.044 76.278  1.00 22.04 ?  1044 GLU B CA   1 
ATOM   14605 C C    . GLU B 1 1044 ? 123.867 154.528 74.874  1.00 21.36 ?  1044 GLU B C    1 
ATOM   14606 O O    . GLU B 1 1044 ? 124.750 154.521 74.007  1.00 20.10 ?  1044 GLU B O    1 
ATOM   14607 C CB   . GLU B 1 1044 ? 124.436 153.883 77.233  1.00 19.18 ?  1044 GLU B CB   1 
ATOM   14608 C CG   . GLU B 1 1044 ? 124.733 154.318 78.659  1.00 20.91 ?  1044 GLU B CG   1 
ATOM   14609 C CD   . GLU B 1 1044 ? 125.504 153.275 79.444  1.00 24.17 ?  1044 GLU B CD   1 
ATOM   14610 O OE1  . GLU B 1 1044 ? 126.686 153.038 79.119  1.00 20.85 ?  1044 GLU B OE1  1 
ATOM   14611 O OE2  . GLU B 1 1044 ? 124.927 152.695 80.388  1.00 25.93 ?  1044 GLU B OE2  1 
ATOM   14612 N N    . MET B 1 1045 ? 122.626 154.096 74.631  1.00 21.67 ?  1045 MET B N    1 
ATOM   14613 C CA   . MET B 1 1045 ? 122.228 153.667 73.293  1.00 23.50 ?  1045 MET B CA   1 
ATOM   14614 C C    . MET B 1 1045 ? 122.307 154.811 72.292  1.00 25.79 ?  1045 MET B C    1 
ATOM   14615 O O    . MET B 1 1045 ? 122.704 154.602 71.139  1.00 25.72 ?  1045 MET B O    1 
ATOM   14616 C CB   . MET B 1 1045 ? 120.812 153.093 73.329  1.00 23.88 ?  1045 MET B CB   1 
ATOM   14617 C CG   . MET B 1 1045 ? 120.745 151.576 73.398  1.00 23.55 ?  1045 MET B CG   1 
ATOM   14618 S SD   . MET B 1 1045 ? 121.663 150.774 72.071  1.00 34.87 ?  1045 MET B SD   1 
ATOM   14619 C CE   . MET B 1 1045 ? 120.372 150.582 70.844  1.00 25.11 ?  1045 MET B CE   1 
ATOM   14620 N N    . GLY B 1 1046 ? 121.930 156.020 72.713  1.00 23.91 ?  1046 GLY B N    1 
ATOM   14621 C CA   . GLY B 1 1046 ? 121.987 157.162 71.816  1.00 23.30 ?  1046 GLY B CA   1 
ATOM   14622 C C    . GLY B 1 1046 ? 123.403 157.538 71.423  1.00 23.16 ?  1046 GLY B C    1 
ATOM   14623 O O    . GLY B 1 1046 ? 123.650 157.958 70.290  1.00 21.70 ?  1046 GLY B O    1 
ATOM   14624 N N    . VAL B 1 1047 ? 124.353 157.405 72.353  1.00 19.81 ?  1047 VAL B N    1 
ATOM   14625 C CA   . VAL B 1 1047 ? 125.750 157.684 72.027  1.00 19.07 ?  1047 VAL B CA   1 
ATOM   14626 C C    . VAL B 1 1047 ? 126.433 156.505 71.354  1.00 24.55 ?  1047 VAL B C    1 
ATOM   14627 O O    . VAL B 1 1047 ? 127.503 156.678 70.757  1.00 25.11 ?  1047 VAL B O    1 
ATOM   14628 C CB   . VAL B 1 1047 ? 126.526 158.111 73.290  1.00 19.43 ?  1047 VAL B CB   1 
ATOM   14629 C CG1  . VAL B 1 1047 ? 127.030 156.900 74.063  1.00 19.87 ?  1047 VAL B CG1  1 
ATOM   14630 C CG2  . VAL B 1 1047 ? 127.674 159.048 72.929  1.00 21.00 ?  1047 VAL B CG2  1 
ATOM   14631 N N    . LEU B 1 1048 ? 125.841 155.311 71.415  1.00 24.98 ?  1048 LEU B N    1 
ATOM   14632 C CA   . LEU B 1 1048 ? 126.430 154.145 70.765  1.00 22.93 ?  1048 LEU B CA   1 
ATOM   14633 C C    . LEU B 1 1048 ? 125.978 154.015 69.312  1.00 21.81 ?  1048 LEU B C    1 
ATOM   14634 O O    . LEU B 1 1048 ? 126.810 153.971 68.400  1.00 24.35 ?  1048 LEU B O    1 
ATOM   14635 C CB   . LEU B 1 1048 ? 126.090 152.875 71.553  1.00 21.97 ?  1048 LEU B CB   1 
ATOM   14636 C CG   . LEU B 1 1048 ? 127.036 152.542 72.707  1.00 21.67 ?  1048 LEU B CG   1 
ATOM   14637 C CD1  . LEU B 1 1048 ? 126.598 151.267 73.405  1.00 23.15 ?  1048 LEU B CD1  1 
ATOM   14638 C CD2  . LEU B 1 1048 ? 128.465 152.417 72.205  1.00 22.19 ?  1048 LEU B CD2  1 
ATOM   14639 N N    . THR B 1 1049 ? 124.669 153.952 69.081  1.00 22.38 ?  1049 THR B N    1 
ATOM   14640 C CA   . THR B 1 1049 ? 124.137 153.732 67.742  1.00 26.88 ?  1049 THR B CA   1 
ATOM   14641 C C    . THR B 1 1049 ? 123.756 155.018 67.018  1.00 24.97 ?  1049 THR B C    1 
ATOM   14642 O O    . THR B 1 1049 ? 123.313 154.944 65.867  1.00 23.12 ?  1049 THR B O    1 
ATOM   14643 C CB   . THR B 1 1049 ? 122.919 152.805 67.802  1.00 26.34 ?  1049 THR B CB   1 
ATOM   14644 O OG1  . THR B 1 1049 ? 122.099 153.160 68.922  1.00 26.61 ?  1049 THR B OG1  1 
ATOM   14645 C CG2  . THR B 1 1049 ? 123.357 151.358 67.933  1.00 21.31 ?  1049 THR B CG2  1 
ATOM   14646 N N    . LYS B 1 1050 ? 123.922 156.179 67.661  1.00 22.81 ?  1050 LYS B N    1 
ATOM   14647 C CA   . LYS B 1 1050 ? 123.583 157.486 67.083  1.00 29.05 ?  1050 LYS B CA   1 
ATOM   14648 C C    . LYS B 1 1050 ? 122.125 157.545 66.626  1.00 29.36 ?  1050 LYS B C    1 
ATOM   14649 O O    . LYS B 1 1050 ? 121.803 158.120 65.584  1.00 25.94 ?  1050 LYS B O    1 
ATOM   14650 C CB   . LYS B 1 1050 ? 124.530 157.852 65.936  1.00 28.19 ?  1050 LYS B CB   1 
ATOM   14651 C CG   . LYS B 1 1050 ? 125.581 158.882 66.314  1.00 25.49 ?  1050 LYS B CG   1 
ATOM   14652 C CD   . LYS B 1 1050 ? 126.786 158.222 66.962  1.00 25.24 ?  1050 LYS B CD   1 
ATOM   14653 C CE   . LYS B 1 1050 ? 127.900 159.222 67.215  1.00 25.05 ?  1050 LYS B CE   1 
ATOM   14654 N NZ   . LYS B 1 1050 ? 129.078 158.576 67.856  1.00 28.76 ?  1050 LYS B NZ   1 
ATOM   14655 N N    . LYS B 1 1051 ? 121.229 156.941 67.421  1.00 29.63 ?  1051 LYS B N    1 
ATOM   14656 C CA   . LYS B 1 1051 ? 119.803 156.942 67.136  1.00 26.78 ?  1051 LYS B CA   1 
ATOM   14657 C C    . LYS B 1 1051 ? 119.116 158.108 67.843  1.00 29.19 ?  1051 LYS B C    1 
ATOM   14658 O O    . LYS B 1 1051 ? 119.596 158.584 68.877  1.00 30.83 ?  1051 LYS B O    1 
ATOM   14659 C CB   . LYS B 1 1051 ? 119.169 155.626 67.584  1.00 25.16 ?  1051 LYS B CB   1 
ATOM   14660 C CG   . LYS B 1 1051 ? 119.736 154.394 66.898  1.00 27.12 ?  1051 LYS B CG   1 
ATOM   14661 C CD   . LYS B 1 1051 ? 119.810 154.572 65.389  1.00 28.52 ?  1051 LYS B CD   1 
ATOM   14662 C CE   . LYS B 1 1051 ? 118.462 154.324 64.735  1.00 30.99 ?  1051 LYS B CE   1 
ATOM   14663 N NZ   . LYS B 1 1051 ? 118.564 154.313 63.249  1.00 29.67 ?  1051 LYS B NZ   1 
ATOM   14664 N N    . PRO B 1 1052 ? 118.002 158.597 67.297  1.00 28.29 ?  1052 PRO B N    1 
ATOM   14665 C CA   . PRO B 1 1052 ? 117.260 159.667 67.974  1.00 27.70 ?  1052 PRO B CA   1 
ATOM   14666 C C    . PRO B 1 1052 ? 116.672 159.200 69.296  1.00 25.38 ?  1052 PRO B C    1 
ATOM   14667 O O    . PRO B 1 1052 ? 116.400 158.014 69.500  1.00 23.65 ?  1052 PRO B O    1 
ATOM   14668 C CB   . PRO B 1 1052 ? 116.154 160.024 66.972  1.00 25.76 ?  1052 PRO B CB   1 
ATOM   14669 C CG   . PRO B 1 1052 ? 116.656 159.538 65.655  1.00 26.29 ?  1052 PRO B CG   1 
ATOM   14670 C CD   . PRO B 1 1052 ? 117.458 158.313 65.958  1.00 23.72 ?  1052 PRO B CD   1 
ATOM   14671 N N    . ARG B 1 1053 ? 116.490 160.157 70.203  1.00 24.19 ?  1053 ARG B N    1 
ATOM   14672 C CA   . ARG B 1 1053 ? 115.927 159.862 71.513  1.00 26.39 ?  1053 ARG B CA   1 
ATOM   14673 C C    . ARG B 1 1053 ? 114.472 159.422 71.389  1.00 26.47 ?  1053 ARG B C    1 
ATOM   14674 O O    . ARG B 1 1053 ? 113.741 159.854 70.495  1.00 27.71 ?  1053 ARG B O    1 
ATOM   14675 C CB   . ARG B 1 1053 ? 116.028 161.085 72.425  1.00 26.13 ?  1053 ARG B CB   1 
ATOM   14676 C CG   . ARG B 1 1053 ? 117.436 161.640 72.562  1.00 25.22 ?  1053 ARG B CG   1 
ATOM   14677 C CD   . ARG B 1 1053 ? 118.119 161.113 73.813  1.00 27.17 ?  1053 ARG B CD   1 
ATOM   14678 N NE   . ARG B 1 1053 ? 119.526 161.490 73.866  1.00 25.44 ?  1053 ARG B NE   1 
ATOM   14679 C CZ   . ARG B 1 1053 ? 120.258 161.498 74.971  1.00 22.88 ?  1053 ARG B CZ   1 
ATOM   14680 N NH1  . ARG B 1 1053 ? 119.746 161.154 76.141  1.00 23.20 ?  1053 ARG B NH1  1 
ATOM   14681 N NH2  . ARG B 1 1053 ? 121.535 161.861 74.900  1.00 22.77 ?  1053 ARG B NH2  1 
ATOM   14682 N N    . ASN B 1 1054 ? 114.055 158.547 72.306  1.00 24.56 ?  1054 ASN B N    1 
ATOM   14683 C CA   . ASN B 1 1054 ? 112.730 157.943 72.243  1.00 27.22 ?  1054 ASN B CA   1 
ATOM   14684 C C    . ASN B 1 1054 ? 111.949 158.065 73.546  1.00 28.03 ?  1054 ASN B C    1 
ATOM   14685 O O    . ASN B 1 1054 ? 110.907 157.414 73.688  1.00 27.38 ?  1054 ASN B O    1 
ATOM   14686 C CB   . ASN B 1 1054 ? 112.840 156.466 71.845  1.00 24.89 ?  1054 ASN B CB   1 
ATOM   14687 C CG   . ASN B 1 1054 ? 113.726 155.673 72.786  1.00 28.71 ?  1054 ASN B CG   1 
ATOM   14688 O OD1  . ASN B 1 1054 ? 114.524 156.240 73.532  1.00 26.55 ?  1054 ASN B OD1  1 
ATOM   14689 N ND2  . ASN B 1 1054 ? 113.590 154.352 72.754  1.00 27.40 ?  1054 ASN B ND2  1 
ATOM   14690 N N    . ALA B 1 1055 ? 112.410 158.876 74.497  1.00 23.52 ?  1055 ALA B N    1 
ATOM   14691 C CA   . ALA B 1 1055 ? 111.711 159.009 75.769  1.00 19.40 ?  1055 ALA B CA   1 
ATOM   14692 C C    . ALA B 1 1055 ? 112.021 160.368 76.378  1.00 19.34 ?  1055 ALA B C    1 
ATOM   14693 O O    . ALA B 1 1055 ? 113.192 160.725 76.537  1.00 19.68 ?  1055 ALA B O    1 
ATOM   14694 C CB   . ALA B 1 1055 ? 112.106 157.887 76.733  1.00 20.19 ?  1055 ALA B CB   1 
ATOM   14695 N N    . THR B 1 1056 ? 110.973 161.114 76.718  1.00 20.94 ?  1056 THR B N    1 
ATOM   14696 C CA   . THR B 1 1056 ? 111.147 162.395 77.386  1.00 21.68 ?  1056 THR B CA   1 
ATOM   14697 C C    . THR B 1 1056 ? 111.533 162.183 78.845  1.00 19.88 ?  1056 THR B C    1 
ATOM   14698 O O    . THR B 1 1056 ? 111.002 161.299 79.528  1.00 22.88 ?  1056 THR B O    1 
ATOM   14699 C CB   . THR B 1 1056 ? 109.866 163.225 77.299  1.00 21.01 ?  1056 THR B CB   1 
ATOM   14700 O OG1  . THR B 1 1056 ? 109.294 163.093 75.993  1.00 21.82 ?  1056 THR B OG1  1 
ATOM   14701 C CG2  . THR B 1 1056 ? 110.161 164.694 77.565  1.00 18.55 ?  1056 THR B CG2  1 
ATOM   14702 N N    . VAL B 1 1057 ? 112.463 163.006 79.320  1.00 12.41 ?  1057 VAL B N    1 
ATOM   14703 C CA   . VAL B 1 1057 ? 113.004 162.913 80.670  1.00 15.81 ?  1057 VAL B CA   1 
ATOM   14704 C C    . VAL B 1 1057 ? 112.617 164.183 81.416  1.00 18.39 ?  1057 VAL B C    1 
ATOM   14705 O O    . VAL B 1 1057 ? 113.057 165.281 81.055  1.00 19.47 ?  1057 VAL B O    1 
ATOM   14706 C CB   . VAL B 1 1057 ? 114.528 162.722 80.646  1.00 18.26 ?  1057 VAL B CB   1 
ATOM   14707 C CG1  . VAL B 1 1057 ? 115.026 162.238 81.982  1.00 18.02 ?  1057 VAL B CG1  1 
ATOM   14708 C CG2  . VAL B 1 1057 ? 114.922 161.744 79.555  1.00 17.12 ?  1057 VAL B CG2  1 
ATOM   14709 N N    . THR B 1 1058 ? 111.799 164.037 82.458  1.00 15.74 ?  1058 THR B N    1 
ATOM   14710 C CA   . THR B 1 1058 ? 111.275 165.166 83.216  1.00 16.41 ?  1058 THR B CA   1 
ATOM   14711 C C    . THR B 1 1058 ? 111.703 165.071 84.674  1.00 17.36 ?  1058 THR B C    1 
ATOM   14712 O O    . THR B 1 1058 ? 111.639 164.000 85.284  1.00 18.40 ?  1058 THR B O    1 
ATOM   14713 C CB   . THR B 1 1058 ? 109.743 165.240 83.139  1.00 16.31 ?  1058 THR B CB   1 
ATOM   14714 O OG1  . THR B 1 1058 ? 109.169 164.362 84.115  1.00 13.45 ?  1058 THR B OG1  1 
ATOM   14715 C CG2  . THR B 1 1058 ? 109.245 164.854 81.752  1.00 15.40 ?  1058 THR B CG2  1 
ATOM   14716 N N    . CYS B 1 1059 ? 112.115 166.205 85.234  1.00 20.51 ?  1059 CYS B N    1 
ATOM   14717 C CA   . CYS B 1 1059 ? 112.618 166.250 86.601  1.00 20.80 ?  1059 CYS B CA   1 
ATOM   14718 C C    . CYS B 1 1059 ? 111.462 166.162 87.590  1.00 23.00 ?  1059 CYS B C    1 
ATOM   14719 O O    . CYS B 1 1059 ? 110.607 167.051 87.635  1.00 25.84 ?  1059 CYS B O    1 
ATOM   14720 C CB   . CYS B 1 1059 ? 113.414 167.531 86.825  1.00 20.01 ?  1059 CYS B CB   1 
ATOM   14721 S SG   . CYS B 1 1059 ? 114.345 168.086 85.381  1.00 30.19 ?  1059 CYS B SG   1 
ATOM   14722 N N    . GLU B 1 1060 ? 111.437 165.089 88.384  1.00 21.23 ?  1060 GLU B N    1 
ATOM   14723 C CA   . GLU B 1 1060 ? 110.447 164.979 89.450  1.00 22.81 ?  1060 GLU B CA   1 
ATOM   14724 C C    . GLU B 1 1060 ? 110.820 165.843 90.648  1.00 25.29 ?  1060 GLU B C    1 
ATOM   14725 O O    . GLU B 1 1060 ? 109.938 166.361 91.342  1.00 27.12 ?  1060 GLU B O    1 
ATOM   14726 C CB   . GLU B 1 1060 ? 110.286 163.518 89.872  1.00 23.41 ?  1060 GLU B CB   1 
ATOM   14727 C CG   . GLU B 1 1060 ? 108.871 163.147 90.289  1.00 25.09 ?  1060 GLU B CG   1 
ATOM   14728 C CD   . GLU B 1 1060 ? 107.944 162.935 89.107  1.00 27.20 ?  1060 GLU B CD   1 
ATOM   14729 O OE1  . GLU B 1 1060 ? 108.441 162.838 87.965  1.00 26.03 ?  1060 GLU B OE1  1 
ATOM   14730 O OE2  . GLU B 1 1060 ? 106.716 162.865 89.320  1.00 28.77 ?  1060 GLU B OE2  1 
ATOM   14731 N N    . THR B 1 1061 ? 112.116 165.984 90.924  1.00 20.82 ?  1061 THR B N    1 
ATOM   14732 C CA   . THR B 1 1061 ? 112.602 166.886 91.961  1.00 22.81 ?  1061 THR B CA   1 
ATOM   14733 C C    . THR B 1 1061 ? 113.686 167.791 91.388  1.00 20.34 ?  1061 THR B C    1 
ATOM   14734 O O    . THR B 1 1061 ? 113.913 167.800 90.174  1.00 18.03 ?  1061 THR B O    1 
ATOM   14735 C CB   . THR B 1 1061 ? 113.152 166.109 93.162  1.00 22.03 ?  1061 THR B CB   1 
ATOM   14736 O OG1  . THR B 1 1061 ? 114.243 165.280 92.741  1.00 20.26 ?  1061 THR B OG1  1 
ATOM   14737 C CG2  . THR B 1 1061 ? 112.073 165.242 93.798  1.00 18.25 ?  1061 THR B CG2  1 
ATOM   14738 N N    . THR B 1 1062 ? 114.355 168.557 92.245  1.00 20.34 ?  1062 THR B N    1 
ATOM   14739 C CA   . THR B 1 1062 ? 115.540 169.291 91.821  1.00 20.70 ?  1062 THR B CA   1 
ATOM   14740 C C    . THR B 1 1062 ? 116.680 168.302 91.616  1.00 20.61 ?  1062 THR B C    1 
ATOM   14741 O O    . THR B 1 1062 ? 117.141 167.671 92.573  1.00 21.25 ?  1062 THR B O    1 
ATOM   14742 C CB   . THR B 1 1062 ? 115.920 170.344 92.858  1.00 20.01 ?  1062 THR B CB   1 
ATOM   14743 O OG1  . THR B 1 1062 ? 116.176 169.708 94.117  1.00 15.28 ?  1062 THR B OG1  1 
ATOM   14744 C CG2  . THR B 1 1062 ? 114.797 171.356 93.026  1.00 21.58 ?  1062 THR B CG2  1 
ATOM   14745 N N    . VAL B 1 1063 ? 117.135 168.162 90.374  1.00 20.35 ?  1063 VAL B N    1 
ATOM   14746 C CA   . VAL B 1 1063 ? 118.020 167.072 89.981  1.00 18.61 ?  1063 VAL B CA   1 
ATOM   14747 C C    . VAL B 1 1063 ? 119.363 167.646 89.543  1.00 19.09 ?  1063 VAL B C    1 
ATOM   14748 O O    . VAL B 1 1063 ? 119.423 168.612 88.772  1.00 18.86 ?  1063 VAL B O    1 
ATOM   14749 C CB   . VAL B 1 1063 ? 117.379 166.203 88.881  1.00 19.14 ?  1063 VAL B CB   1 
ATOM   14750 C CG1  . VAL B 1 1063 ? 116.907 167.047 87.712  1.00 19.18 ?  1063 VAL B CG1  1 
ATOM   14751 C CG2  . VAL B 1 1063 ? 118.324 165.109 88.418  1.00 18.21 ?  1063 VAL B CG2  1 
ATOM   14752 N N    . GLN B 1 1064 ? 120.436 167.069 90.072  1.00 20.47 ?  1064 GLN B N    1 
ATOM   14753 C CA   . GLN B 1 1064 ? 121.799 167.382 89.667  1.00 21.75 ?  1064 GLN B CA   1 
ATOM   14754 C C    . GLN B 1 1064 ? 122.346 166.219 88.853  1.00 19.86 ?  1064 GLN B C    1 
ATOM   14755 O O    . GLN B 1 1064 ? 122.350 165.076 89.325  1.00 20.45 ?  1064 GLN B O    1 
ATOM   14756 C CB   . GLN B 1 1064 ? 122.688 167.633 90.886  1.00 21.57 ?  1064 GLN B CB   1 
ATOM   14757 C CG   . GLN B 1 1064 ? 122.671 169.060 91.393  1.00 22.40 ?  1064 GLN B CG   1 
ATOM   14758 C CD   . GLN B 1 1064 ? 123.685 169.293 92.495  1.00 25.55 ?  1064 GLN B CD   1 
ATOM   14759 O OE1  . GLN B 1 1064 ? 124.188 168.348 93.101  1.00 21.66 ?  1064 GLN B OE1  1 
ATOM   14760 N NE2  . GLN B 1 1064 ? 123.991 170.558 92.759  1.00 26.09 ?  1064 GLN B NE2  1 
ATOM   14761 N N    . VAL B 1 1065 ? 122.808 166.518 87.635  1.00 19.73 ?  1065 VAL B N    1 
ATOM   14762 C CA   . VAL B 1 1065 ? 123.297 165.512 86.702  1.00 18.90 ?  1065 VAL B CA   1 
ATOM   14763 C C    . VAL B 1 1065 ? 124.699 165.884 86.234  1.00 22.41 ?  1065 VAL B C    1 
ATOM   14764 O O    . VAL B 1 1065 ? 125.137 167.033 86.332  1.00 27.48 ?  1065 VAL B O    1 
ATOM   14765 C CB   . VAL B 1 1065 ? 122.372 165.329 85.474  1.00 19.56 ?  1065 VAL B CB   1 
ATOM   14766 C CG1  . VAL B 1 1065 ? 120.924 165.195 85.891  1.00 21.35 ?  1065 VAL B CG1  1 
ATOM   14767 C CG2  . VAL B 1 1065 ? 122.538 166.479 84.494  1.00 17.78 ?  1065 VAL B CG2  1 
ATOM   14768 N N    . TYR B 1 1066 ? 125.400 164.875 85.724  1.00 17.24 ?  1066 TYR B N    1 
ATOM   14769 C CA   . TYR B 1 1066 ? 126.684 165.044 85.059  1.00 16.19 ?  1066 TYR B CA   1 
ATOM   14770 C C    . TYR B 1 1066 ? 126.480 164.899 83.557  1.00 18.68 ?  1066 TYR B C    1 
ATOM   14771 O O    . TYR B 1 1066 ? 125.875 163.925 83.100  1.00 24.60 ?  1066 TYR B O    1 
ATOM   14772 C CB   . TYR B 1 1066 ? 127.699 164.013 85.553  1.00 18.09 ?  1066 TYR B CB   1 
ATOM   14773 C CG   . TYR B 1 1066 ? 128.734 164.553 86.515  1.00 19.32 ?  1066 TYR B CG   1 
ATOM   14774 C CD1  . TYR B 1 1066 ? 129.607 165.563 86.132  1.00 20.86 ?  1066 TYR B CD1  1 
ATOM   14775 C CD2  . TYR B 1 1066 ? 128.847 164.044 87.802  1.00 19.25 ?  1066 TYR B CD2  1 
ATOM   14776 C CE1  . TYR B 1 1066 ? 130.560 166.054 87.006  1.00 20.91 ?  1066 TYR B CE1  1 
ATOM   14777 C CE2  . TYR B 1 1066 ? 129.795 164.529 88.684  1.00 23.72 ?  1066 TYR B CE2  1 
ATOM   14778 C CZ   . TYR B 1 1066 ? 130.649 165.534 88.280  1.00 23.88 ?  1066 TYR B CZ   1 
ATOM   14779 O OH   . TYR B 1 1066 ? 131.594 166.021 89.153  1.00 25.00 ?  1066 TYR B OH   1 
ATOM   14780 N N    . PHE B 1 1067 ? 126.984 165.865 82.797  1.00 20.15 ?  1067 PHE B N    1 
ATOM   14781 C CA   . PHE B 1 1067 ? 126.819 165.902 81.352  1.00 20.26 ?  1067 PHE B CA   1 
ATOM   14782 C C    . PHE B 1 1067 ? 128.172 165.717 80.682  1.00 20.54 ?  1067 PHE B C    1 
ATOM   14783 O O    . PHE B 1 1067 ? 129.146 166.394 81.036  1.00 20.40 ?  1067 PHE B O    1 
ATOM   14784 C CB   . PHE B 1 1067 ? 126.180 167.221 80.904  1.00 19.60 ?  1067 PHE B CB   1 
ATOM   14785 C CG   . PHE B 1 1067 ? 125.697 167.214 79.478  1.00 23.42 ?  1067 PHE B CG   1 
ATOM   14786 C CD1  . PHE B 1 1067 ? 125.391 166.026 78.835  1.00 21.12 ?  1067 PHE B CD1  1 
ATOM   14787 C CD2  . PHE B 1 1067 ? 125.547 168.403 78.782  1.00 23.88 ?  1067 PHE B CD2  1 
ATOM   14788 C CE1  . PHE B 1 1067 ? 124.948 166.023 77.525  1.00 21.86 ?  1067 PHE B CE1  1 
ATOM   14789 C CE2  . PHE B 1 1067 ? 125.104 168.406 77.472  1.00 23.47 ?  1067 PHE B CE2  1 
ATOM   14790 C CZ   . PHE B 1 1067 ? 124.804 167.214 76.844  1.00 23.13 ?  1067 PHE B CZ   1 
ATOM   14791 N N    . ILE B 1 1068 ? 128.223 164.792 79.726  1.00 18.49 ?  1068 ILE B N    1 
ATOM   14792 C CA   . ILE B 1 1068 ? 129.382 164.567 78.873  1.00 23.25 ?  1068 ILE B CA   1 
ATOM   14793 C C    . ILE B 1 1068 ? 128.926 164.721 77.429  1.00 20.83 ?  1068 ILE B C    1 
ATOM   14794 O O    . ILE B 1 1068 ? 127.950 164.085 77.014  1.00 22.28 ?  1068 ILE B O    1 
ATOM   14795 C CB   . ILE B 1 1068 ? 130.000 163.176 79.107  1.00 22.30 ?  1068 ILE B CB   1 
ATOM   14796 C CG1  . ILE B 1 1068 ? 130.552 163.068 80.529  1.00 21.93 ?  1068 ILE B CG1  1 
ATOM   14797 C CG2  . ILE B 1 1068 ? 131.089 162.892 78.085  1.00 20.99 ?  1068 ILE B CG2  1 
ATOM   14798 C CD1  . ILE B 1 1068 ? 129.822 162.062 81.390  1.00 18.25 ?  1068 ILE B CD1  1 
ATOM   14799 N N    . THR B 1 1069 ? 129.621 165.567 76.673  1.00 22.60 ?  1069 THR B N    1 
ATOM   14800 C CA   . THR B 1 1069 ? 129.249 165.809 75.287  1.00 23.87 ?  1069 THR B CA   1 
ATOM   14801 C C    . THR B 1 1069 ? 129.507 164.573 74.431  1.00 26.61 ?  1069 THR B C    1 
ATOM   14802 O O    . THR B 1 1069 ? 130.398 163.766 74.713  1.00 25.63 ?  1069 THR B O    1 
ATOM   14803 C CB   . THR B 1 1069 ? 130.020 167.003 74.723  1.00 23.90 ?  1069 THR B CB   1 
ATOM   14804 O OG1  . THR B 1 1069 ? 131.423 166.821 74.951  1.00 21.60 ?  1069 THR B OG1  1 
ATOM   14805 C CG2  . THR B 1 1069 ? 129.566 168.293 75.391  1.00 24.80 ?  1069 THR B CG2  1 
ATOM   14806 N N    . ALA B 1 1070 ? 128.701 164.427 73.376  1.00 25.55 ?  1070 ALA B N    1 
ATOM   14807 C CA   . ALA B 1 1070 ? 128.820 163.267 72.498  1.00 20.97 ?  1070 ALA B CA   1 
ATOM   14808 C C    . ALA B 1 1070 ? 130.124 163.280 71.712  1.00 19.68 ?  1070 ALA B C    1 
ATOM   14809 O O    . ALA B 1 1070 ? 130.683 162.215 71.428  1.00 19.29 ?  1070 ALA B O    1 
ATOM   14810 C CB   . ALA B 1 1070 ? 127.628 163.202 71.545  1.00 19.09 ?  1070 ALA B CB   1 
ATOM   14811 N N    . GLU B 1 1071 ? 130.612 164.466 71.338  1.00 20.23 ?  1071 GLU B N    1 
ATOM   14812 C CA   . GLU B 1 1071 ? 131.876 164.556 70.614  1.00 21.48 ?  1071 GLU B CA   1 
ATOM   14813 C C    . GLU B 1 1071 ? 133.040 164.085 71.477  1.00 20.30 ?  1071 GLU B C    1 
ATOM   14814 O O    . GLU B 1 1071 ? 133.946 163.396 70.991  1.00 20.29 ?  1071 GLU B O    1 
ATOM   14815 C CB   . GLU B 1 1071 ? 132.105 165.990 70.135  1.00 19.58 ?  1071 GLU B CB   1 
ATOM   14816 C CG   . GLU B 1 1071 ? 131.557 166.279 68.744  1.00 19.18 ?  1071 GLU B CG   1 
ATOM   14817 C CD   . GLU B 1 1071 ? 130.070 166.001 68.629  1.00 18.91 ?  1071 GLU B CD   1 
ATOM   14818 O OE1  . GLU B 1 1071 ? 129.306 166.476 69.496  1.00 16.92 ?  1071 GLU B OE1  1 
ATOM   14819 O OE2  . GLU B 1 1071 ? 129.665 165.307 67.673  1.00 22.06 ?  1071 GLU B OE2  1 
ATOM   14820 N N    . ASP B 1 1072 ? 133.031 164.444 72.763  1.00 19.30 ?  1072 ASP B N    1 
ATOM   14821 C CA   . ASP B 1 1072 ? 134.059 163.958 73.677  1.00 25.08 ?  1072 ASP B CA   1 
ATOM   14822 C C    . ASP B 1 1072 ? 133.961 162.449 73.864  1.00 22.85 ?  1072 ASP B C    1 
ATOM   14823 O O    . ASP B 1 1072 ? 134.984 161.768 74.000  1.00 20.51 ?  1072 ASP B O    1 
ATOM   14824 C CB   . ASP B 1 1072 ? 133.946 164.679 75.019  1.00 25.78 ?  1072 ASP B CB   1 
ATOM   14825 C CG   . ASP B 1 1072 ? 134.532 166.077 74.979  1.00 27.93 ?  1072 ASP B CG   1 
ATOM   14826 O OD1  . ASP B 1 1072 ? 135.273 166.384 74.021  1.00 29.63 ?  1072 ASP B OD1  1 
ATOM   14827 O OD2  . ASP B 1 1072 ? 134.243 166.872 75.897  1.00 25.07 ?  1072 ASP B OD2  1 
ATOM   14828 N N    . MET B 1 1073 ? 132.739 161.910 73.868  1.00 20.63 ?  1073 MET B N    1 
ATOM   14829 C CA   . MET B 1 1073 ? 132.566 160.462 73.942  1.00 23.24 ?  1073 MET B CA   1 
ATOM   14830 C C    . MET B 1 1073 ? 133.129 159.773 72.705  1.00 25.92 ?  1073 MET B C    1 
ATOM   14831 O O    . MET B 1 1073 ? 133.764 158.718 72.810  1.00 22.48 ?  1073 MET B O    1 
ATOM   14832 C CB   . MET B 1 1073 ? 131.087 160.119 74.123  1.00 23.33 ?  1073 MET B CB   1 
ATOM   14833 C CG   . MET B 1 1073 ? 130.836 158.917 75.018  1.00 23.94 ?  1073 MET B CG   1 
ATOM   14834 S SD   . MET B 1 1073 ? 131.313 159.216 76.730  1.00 29.79 ?  1073 MET B SD   1 
ATOM   14835 C CE   . MET B 1 1073 ? 132.528 157.924 76.972  1.00 21.62 ?  1073 MET B CE   1 
ATOM   14836 N N    . ASN B 1 1074 ? 132.909 160.358 71.524  1.00 28.21 ?  1074 ASN B N    1 
ATOM   14837 C CA   . ASN B 1 1074 ? 133.482 159.803 70.300  1.00 27.66 ?  1074 ASN B CA   1 
ATOM   14838 C C    . ASN B 1 1074 ? 135.004 159.874 70.321  1.00 26.51 ?  1074 ASN B C    1 
ATOM   14839 O O    . ASN B 1 1074 ? 135.684 158.943 69.871  1.00 24.02 ?  1074 ASN B O    1 
ATOM   14840 C CB   . ASN B 1 1074 ? 132.931 160.541 69.080  1.00 25.28 ?  1074 ASN B CB   1 
ATOM   14841 C CG   . ASN B 1 1074 ? 131.423 160.444 68.973  1.00 25.62 ?  1074 ASN B CG   1 
ATOM   14842 O OD1  . ASN B 1 1074 ? 130.777 159.741 69.750  1.00 19.93 ?  1074 ASN B OD1  1 
ATOM   14843 N ND2  . ASN B 1 1074 ? 130.852 161.154 68.007  1.00 22.89 ?  1074 ASN B ND2  1 
ATOM   14844 N N    . ILE B 1 1075 ? 135.553 160.976 70.839  1.00 26.71 ?  1075 ILE B N    1 
ATOM   14845 C CA   . ILE B 1 1075 ? 137.004 161.118 70.950  1.00 26.69 ?  1075 ILE B CA   1 
ATOM   14846 C C    . ILE B 1 1075 ? 137.573 160.061 71.889  1.00 24.75 ?  1075 ILE B C    1 
ATOM   14847 O O    . ILE B 1 1075 ? 138.596 159.430 71.593  1.00 22.64 ?  1075 ILE B O    1 
ATOM   14848 C CB   . ILE B 1 1075 ? 137.361 162.546 71.410  1.00 25.95 ?  1075 ILE B CB   1 
ATOM   14849 C CG1  . ILE B 1 1075 ? 137.197 163.533 70.253  1.00 23.48 ?  1075 ILE B CG1  1 
ATOM   14850 C CG2  . ILE B 1 1075 ? 138.779 162.610 71.959  1.00 24.93 ?  1075 ILE B CG2  1 
ATOM   14851 C CD1  . ILE B 1 1075 ? 136.951 164.957 70.697  1.00 22.51 ?  1075 ILE B CD1  1 
ATOM   14852 N N    . ALA B 1 1076 ? 136.908 159.835 73.026  1.00 25.28 ?  1076 ALA B N    1 
ATOM   14853 C CA   . ALA B 1 1076 ? 137.360 158.813 73.966  1.00 29.93 ?  1076 ALA B CA   1 
ATOM   14854 C C    . ALA B 1 1076 ? 137.225 157.409 73.389  1.00 27.73 ?  1076 ALA B C    1 
ATOM   14855 O O    . ALA B 1 1076 ? 138.052 156.539 73.684  1.00 22.84 ?  1076 ALA B O    1 
ATOM   14856 C CB   . ALA B 1 1076 ? 136.583 158.926 75.277  1.00 24.45 ?  1076 ALA B CB   1 
ATOM   14857 N N    . ILE B 1 1077 ? 136.187 157.166 72.585  1.00 26.43 ?  1077 ILE B N    1 
ATOM   14858 C CA   . ILE B 1 1077 ? 136.031 155.869 71.931  1.00 29.43 ?  1077 ILE B CA   1 
ATOM   14859 C C    . ILE B 1 1077 ? 137.161 155.638 70.933  1.00 32.11 ?  1077 ILE B C    1 
ATOM   14860 O O    . ILE B 1 1077 ? 137.773 154.564 70.899  1.00 31.59 ?  1077 ILE B O    1 
ATOM   14861 C CB   . ILE B 1 1077 ? 134.648 155.775 71.259  1.00 28.37 ?  1077 ILE B CB   1 
ATOM   14862 C CG1  . ILE B 1 1077 ? 133.570 155.459 72.297  1.00 28.47 ?  1077 ILE B CG1  1 
ATOM   14863 C CG2  . ILE B 1 1077 ? 134.642 154.725 70.156  1.00 25.76 ?  1077 ILE B CG2  1 
ATOM   14864 C CD1  . ILE B 1 1077 ? 132.162 155.712 71.806  1.00 28.28 ?  1077 ILE B CD1  1 
ATOM   14865 N N    . ASP B 1 1078 ? 137.470 156.651 70.123  1.00 28.72 ?  1078 ASP B N    1 
ATOM   14866 C CA   . ASP B 1 1078 ? 138.522 156.527 69.121  1.00 28.19 ?  1078 ASP B CA   1 
ATOM   14867 C C    . ASP B 1 1078 ? 139.925 156.615 69.709  1.00 29.64 ?  1078 ASP B C    1 
ATOM   14868 O O    . ASP B 1 1078 ? 140.893 156.318 69.001  1.00 30.91 ?  1078 ASP B O    1 
ATOM   14869 C CB   . ASP B 1 1078 ? 138.351 157.601 68.044  1.00 28.45 ?  1078 ASP B CB   1 
ATOM   14870 C CG   . ASP B 1 1078 ? 137.090 157.407 67.225  1.00 31.40 ?  1078 ASP B CG   1 
ATOM   14871 O OD1  . ASP B 1 1078 ? 136.465 156.332 67.340  1.00 28.61 ?  1078 ASP B OD1  1 
ATOM   14872 O OD2  . ASP B 1 1078 ? 136.724 158.329 66.466  1.00 33.11 ?  1078 ASP B OD2  1 
ATOM   14873 N N    . THR B 1 1079 ? 140.061 157.013 70.974  1.00 22.94 ?  1079 THR B N    1 
ATOM   14874 C CA   . THR B 1 1079 ? 141.370 157.122 71.607  1.00 24.22 ?  1079 THR B CA   1 
ATOM   14875 C C    . THR B 1 1079 ? 141.824 155.804 72.225  1.00 24.98 ?  1079 THR B C    1 
ATOM   14876 O O    . THR B 1 1079 ? 142.933 155.335 71.950  1.00 25.38 ?  1079 THR B O    1 
ATOM   14877 C CB   . THR B 1 1079 ? 141.347 158.220 72.676  1.00 22.79 ?  1079 THR B CB   1 
ATOM   14878 O OG1  . THR B 1 1079 ? 140.876 159.444 72.098  1.00 20.35 ?  1079 THR B OG1  1 
ATOM   14879 C CG2  . THR B 1 1079 ? 142.740 158.436 73.249  1.00 22.88 ?  1079 THR B CG2  1 
ATOM   14880 N N    . PHE B 1 1080 ? 140.984 155.196 73.059  1.00 24.42 ?  1080 PHE B N    1 
ATOM   14881 C CA   . PHE B 1 1080 ? 141.351 153.970 73.757  1.00 25.49 ?  1080 PHE B CA   1 
ATOM   14882 C C    . PHE B 1 1080 ? 141.127 152.773 72.841  1.00 25.58 ?  1080 PHE B C    1 
ATOM   14883 O O    . PHE B 1 1080 ? 140.023 152.581 72.319  1.00 24.89 ?  1080 PHE B O    1 
ATOM   14884 C CB   . PHE B 1 1080 ? 140.543 153.829 75.045  1.00 24.18 ?  1080 PHE B CB   1 
ATOM   14885 C CG   . PHE B 1 1080 ? 140.996 154.743 76.149  1.00 24.02 ?  1080 PHE B CG   1 
ATOM   14886 C CD1  . PHE B 1 1080 ? 140.663 156.089 76.137  1.00 24.40 ?  1080 PHE B CD1  1 
ATOM   14887 C CD2  . PHE B 1 1080 ? 141.758 154.257 77.200  1.00 22.98 ?  1080 PHE B CD2  1 
ATOM   14888 C CE1  . PHE B 1 1080 ? 141.080 156.932 77.150  1.00 24.70 ?  1080 PHE B CE1  1 
ATOM   14889 C CE2  . PHE B 1 1080 ? 142.177 155.095 78.217  1.00 22.70 ?  1080 PHE B CE2  1 
ATOM   14890 C CZ   . PHE B 1 1080 ? 141.837 156.434 78.191  1.00 22.03 ?  1080 PHE B CZ   1 
ATOM   14891 N N    . THR B 1 1081 ? 142.175 151.964 72.649  1.00 24.01 ?  1081 THR B N    1 
ATOM   14892 C CA   . THR B 1 1081 ? 142.117 150.819 71.747  1.00 24.78 ?  1081 THR B CA   1 
ATOM   14893 C C    . THR B 1 1081 ? 142.638 149.543 72.401  1.00 26.39 ?  1081 THR B C    1 
ATOM   14894 O O    . THR B 1 1081 ? 143.027 148.607 71.694  1.00 22.47 ?  1081 THR B O    1 
ATOM   14895 C CB   . THR B 1 1081 ? 142.899 151.100 70.460  1.00 24.90 ?  1081 THR B CB   1 
ATOM   14896 O OG1  . THR B 1 1081 ? 144.143 151.735 70.783  1.00 23.31 ?  1081 THR B OG1  1 
ATOM   14897 C CG2  . THR B 1 1081 ? 142.098 152.002 69.532  1.00 25.57 ?  1081 THR B CG2  1 
ATOM   14898 N N    . LEU B 1 1082 ? 142.656 149.482 73.730  1.00 28.91 ?  1082 LEU B N    1 
ATOM   14899 C CA   . LEU B 1 1082 ? 143.101 148.287 74.427  1.00 28.54 ?  1082 LEU B CA   1 
ATOM   14900 C C    . LEU B 1 1082 ? 142.023 147.205 74.366  1.00 27.76 ?  1082 LEU B C    1 
ATOM   14901 O O    . LEU B 1 1082 ? 140.918 147.419 73.858  1.00 25.19 ?  1082 LEU B O    1 
ATOM   14902 C CB   . LEU B 1 1082 ? 143.454 148.617 75.878  1.00 25.45 ?  1082 LEU B CB   1 
ATOM   14903 C CG   . LEU B 1 1082 ? 144.661 147.894 76.480  1.00 26.72 ?  1082 LEU B CG   1 
ATOM   14904 C CD1  . LEU B 1 1082 ? 145.930 148.240 75.717  1.00 25.43 ?  1082 LEU B CD1  1 
ATOM   14905 C CD2  . LEU B 1 1082 ? 144.808 148.230 77.956  1.00 25.89 ?  1082 LEU B CD2  1 
ATOM   14906 N N    . TYR B 1 1083 ? 142.364 146.019 74.877  1.00 24.15 ?  1083 TYR B N    1 
ATOM   14907 C CA   . TYR B 1 1083 ? 141.399 144.920 74.904  1.00 29.00 ?  1083 TYR B CA   1 
ATOM   14908 C C    . TYR B 1 1083 ? 140.164 145.236 75.744  1.00 27.67 ?  1083 TYR B C    1 
ATOM   14909 O O    . TYR B 1 1083 ? 139.046 144.959 75.276  1.00 24.82 ?  1083 TYR B O    1 
ATOM   14910 C CB   . TYR B 1 1083 ? 142.083 143.628 75.365  1.00 26.57 ?  1083 TYR B CB   1 
ATOM   14911 C CG   . TYR B 1 1083 ? 141.109 142.509 75.655  1.00 28.21 ?  1083 TYR B CG   1 
ATOM   14912 C CD1  . TYR B 1 1083 ? 140.360 141.936 74.635  1.00 25.55 ?  1083 TYR B CD1  1 
ATOM   14913 C CD2  . TYR B 1 1083 ? 140.930 142.033 76.948  1.00 27.54 ?  1083 TYR B CD2  1 
ATOM   14914 C CE1  . TYR B 1 1083 ? 139.464 140.915 74.893  1.00 28.11 ?  1083 TYR B CE1  1 
ATOM   14915 C CE2  . TYR B 1 1083 ? 140.035 141.012 77.215  1.00 27.01 ?  1083 TYR B CE2  1 
ATOM   14916 C CZ   . TYR B 1 1083 ? 139.306 140.457 76.184  1.00 29.05 ?  1083 TYR B CZ   1 
ATOM   14917 O OH   . TYR B 1 1083 ? 138.415 139.442 76.445  1.00 27.04 ?  1083 TYR B OH   1 
ATOM   14918 N N    . PRO B 1 1084 ? 140.267 145.805 76.970  1.00 26.44 ?  1084 PRO B N    1 
ATOM   14919 C CA   . PRO B 1 1084 ? 139.013 146.306 77.580  1.00 25.27 ?  1084 PRO B CA   1 
ATOM   14920 C C    . PRO B 1 1084 ? 138.604 147.637 76.953  1.00 23.85 ?  1084 PRO B C    1 
ATOM   14921 O O    . PRO B 1 1084 ? 138.765 148.721 77.513  1.00 21.06 ?  1084 PRO B O    1 
ATOM   14922 C CB   . PRO B 1 1084 ? 139.382 146.445 79.060  1.00 26.02 ?  1084 PRO B CB   1 
ATOM   14923 C CG   . PRO B 1 1084 ? 140.702 145.749 79.230  1.00 26.36 ?  1084 PRO B CG   1 
ATOM   14924 C CD   . PRO B 1 1084 ? 141.387 145.899 77.923  1.00 26.20 ?  1084 PRO B CD   1 
ATOM   14925 N N    . SER B 1 1085 ? 138.059 147.547 75.743  1.00 25.09 ?  1085 SER B N    1 
ATOM   14926 C CA   . SER B 1 1085 ? 137.755 148.733 74.958  1.00 27.84 ?  1085 SER B CA   1 
ATOM   14927 C C    . SER B 1 1085 ? 136.554 149.477 75.527  1.00 23.87 ?  1085 SER B C    1 
ATOM   14928 O O    . SER B 1 1085 ? 135.679 148.894 76.174  1.00 21.34 ?  1085 SER B O    1 
ATOM   14929 C CB   . SER B 1 1085 ? 137.487 148.350 73.502  1.00 23.93 ?  1085 SER B CB   1 
ATOM   14930 O OG   . SER B 1 1085 ? 136.534 149.218 72.913  1.00 22.49 ?  1085 SER B OG   1 
ATOM   14931 N N    . LEU B 1 1086 ? 136.531 150.791 75.291  1.00 18.88 ?  1086 LEU B N    1 
ATOM   14932 C CA   . LEU B 1 1086 ? 135.369 151.592 75.659  1.00 19.81 ?  1086 LEU B CA   1 
ATOM   14933 C C    . LEU B 1 1086 ? 134.137 151.153 74.879  1.00 23.86 ?  1086 LEU B C    1 
ATOM   14934 O O    . LEU B 1 1086 ? 133.042 151.039 75.444  1.00 29.02 ?  1086 LEU B O    1 
ATOM   14935 C CB   . LEU B 1 1086 ? 135.658 153.073 75.418  1.00 23.50 ?  1086 LEU B CB   1 
ATOM   14936 C CG   . LEU B 1 1086 ? 134.706 154.076 76.069  1.00 24.70 ?  1086 LEU B CG   1 
ATOM   14937 C CD1  . LEU B 1 1086 ? 134.534 153.777 77.548  1.00 21.30 ?  1086 LEU B CD1  1 
ATOM   14938 C CD2  . LEU B 1 1086 ? 135.210 155.492 75.859  1.00 24.19 ?  1086 LEU B CD2  1 
ATOM   14939 N N    . GLU B 1 1087 ? 134.304 150.897 73.579  1.00 21.35 ?  1087 GLU B N    1 
ATOM   14940 C CA   . GLU B 1 1087 ? 133.205 150.386 72.767  1.00 20.47 ?  1087 GLU B CA   1 
ATOM   14941 C C    . GLU B 1 1087 ? 132.751 149.018 73.257  1.00 24.59 ?  1087 GLU B C    1 
ATOM   14942 O O    . GLU B 1 1087 ? 131.547 148.742 73.322  1.00 23.59 ?  1087 GLU B O    1 
ATOM   14943 C CB   . GLU B 1 1087 ? 133.632 150.317 71.300  1.00 18.98 ?  1087 GLU B CB   1 
ATOM   14944 C CG   . GLU B 1 1087 ? 132.573 149.771 70.356  1.00 22.58 ?  1087 GLU B CG   1 
ATOM   14945 C CD   . GLU B 1 1087 ? 131.785 150.868 69.668  1.00 27.76 ?  1087 GLU B CD   1 
ATOM   14946 O OE1  . GLU B 1 1087 ? 132.159 152.051 69.814  1.00 27.17 ?  1087 GLU B OE1  1 
ATOM   14947 O OE2  . GLU B 1 1087 ? 130.795 150.548 68.977  1.00 28.32 ?  1087 GLU B OE2  1 
ATOM   14948 N N    . TYR B 1 1088 ? 133.704 148.158 73.627  1.00 24.44 ?  1088 TYR B N    1 
ATOM   14949 C CA   . TYR B 1 1088 ? 133.374 146.811 74.086  1.00 21.59 ?  1088 TYR B CA   1 
ATOM   14950 C C    . TYR B 1 1088 ? 132.548 146.845 75.367  1.00 22.48 ?  1088 TYR B C    1 
ATOM   14951 O O    . TYR B 1 1088 ? 131.507 146.187 75.462  1.00 24.35 ?  1088 TYR B O    1 
ATOM   14952 C CB   . TYR B 1 1088 ? 134.659 146.010 74.294  1.00 22.26 ?  1088 TYR B CB   1 
ATOM   14953 C CG   . TYR B 1 1088 ? 134.447 144.631 74.872  1.00 25.02 ?  1088 TYR B CG   1 
ATOM   14954 C CD1  . TYR B 1 1088 ? 133.547 143.745 74.294  1.00 21.27 ?  1088 TYR B CD1  1 
ATOM   14955 C CD2  . TYR B 1 1088 ? 135.147 144.214 75.996  1.00 25.85 ?  1088 TYR B CD2  1 
ATOM   14956 C CE1  . TYR B 1 1088 ? 133.352 142.483 74.821  1.00 21.86 ?  1088 TYR B CE1  1 
ATOM   14957 C CE2  . TYR B 1 1088 ? 134.958 142.955 76.530  1.00 22.33 ?  1088 TYR B CE2  1 
ATOM   14958 C CZ   . TYR B 1 1088 ? 134.059 142.094 75.937  1.00 26.50 ?  1088 TYR B CZ   1 
ATOM   14959 O OH   . TYR B 1 1088 ? 133.867 140.839 76.463  1.00 31.57 ?  1088 TYR B OH   1 
ATOM   14960 N N    . ARG B 1 1089 ? 132.994 147.616 76.362  1.00 18.04 ?  1089 ARG B N    1 
ATOM   14961 C CA   . ARG B 1 1089 ? 132.262 147.703 77.624  1.00 19.19 ?  1089 ARG B CA   1 
ATOM   14962 C C    . ARG B 1 1089 ? 130.918 148.399 77.444  1.00 16.79 ?  1089 ARG B C    1 
ATOM   14963 O O    . ARG B 1 1089 ? 129.907 147.976 78.027  1.00 17.86 ?  1089 ARG B O    1 
ATOM   14964 C CB   . ARG B 1 1089 ? 133.109 148.433 78.665  1.00 18.70 ?  1089 ARG B CB   1 
ATOM   14965 C CG   . ARG B 1 1089 ? 134.094 147.542 79.403  1.00 18.75 ?  1089 ARG B CG   1 
ATOM   14966 C CD   . ARG B 1 1089 ? 135.174 148.366 80.083  1.00 19.09 ?  1089 ARG B CD   1 
ATOM   14967 N NE   . ARG B 1 1089 ? 135.602 149.485 79.253  1.00 24.12 ?  1089 ARG B NE   1 
ATOM   14968 C CZ   . ARG B 1 1089 ? 136.584 150.319 79.566  1.00 24.28 ?  1089 ARG B CZ   1 
ATOM   14969 N NH1  . ARG B 1 1089 ? 137.266 150.192 80.692  1.00 20.24 ?  1089 ARG B NH1  1 
ATOM   14970 N NH2  . ARG B 1 1089 ? 136.890 151.306 78.728  1.00 20.27 ?  1089 ARG B NH2  1 
ATOM   14971 N N    . LEU B 1 1090 ? 130.890 149.470 76.641  1.00 16.84 ?  1090 LEU B N    1 
ATOM   14972 C CA   . LEU B 1 1090 ? 129.648 150.195 76.401  1.00 21.15 ?  1090 LEU B CA   1 
ATOM   14973 C C    . LEU B 1 1090 ? 128.620 149.311 75.711  1.00 22.16 ?  1090 LEU B C    1 
ATOM   14974 O O    . LEU B 1 1090 ? 127.423 149.387 76.011  1.00 23.01 ?  1090 LEU B O    1 
ATOM   14975 C CB   . LEU B 1 1090 ? 129.922 151.445 75.566  1.00 18.86 ?  1090 LEU B CB   1 
ATOM   14976 C CG   . LEU B 1 1090 ? 129.835 152.782 76.299  1.00 19.35 ?  1090 LEU B CG   1 
ATOM   14977 C CD1  . LEU B 1 1090 ? 130.940 152.871 77.328  1.00 18.56 ?  1090 LEU B CD1  1 
ATOM   14978 C CD2  . LEU B 1 1090 ? 129.913 153.946 75.324  1.00 24.29 ?  1090 LEU B CD2  1 
ATOM   14979 N N    . TRP B 1 1091 ? 129.067 148.462 74.785  1.00 18.51 ?  1091 TRP B N    1 
ATOM   14980 C CA   . TRP B 1 1091 ? 128.145 147.547 74.134  1.00 20.14 ?  1091 TRP B CA   1 
ATOM   14981 C C    . TRP B 1 1091 ? 127.759 146.386 75.038  1.00 20.42 ?  1091 TRP B C    1 
ATOM   14982 O O    . TRP B 1 1091 ? 126.621 145.918 74.969  1.00 22.27 ?  1091 TRP B O    1 
ATOM   14983 C CB   . TRP B 1 1091 ? 128.747 147.034 72.826  1.00 20.06 ?  1091 TRP B CB   1 
ATOM   14984 C CG   . TRP B 1 1091 ? 128.289 147.823 71.643  1.00 20.56 ?  1091 TRP B CG   1 
ATOM   14985 C CD1  . TRP B 1 1091 ? 129.053 148.618 70.840  1.00 20.77 ?  1091 TRP B CD1  1 
ATOM   14986 C CD2  . TRP B 1 1091 ? 126.950 147.917 71.143  1.00 23.28 ?  1091 TRP B CD2  1 
ATOM   14987 N NE1  . TRP B 1 1091 ? 128.275 149.191 69.863  1.00 24.06 ?  1091 TRP B NE1  1 
ATOM   14988 C CE2  . TRP B 1 1091 ? 126.980 148.776 70.028  1.00 27.01 ?  1091 TRP B CE2  1 
ATOM   14989 C CE3  . TRP B 1 1091 ? 125.730 147.351 71.526  1.00 18.58 ?  1091 TRP B CE3  1 
ATOM   14990 C CZ2  . TRP B 1 1091 ? 125.837 149.083 69.294  1.00 25.52 ?  1091 TRP B CZ2  1 
ATOM   14991 C CZ3  . TRP B 1 1091 ? 124.599 147.658 70.798  1.00 18.20 ?  1091 TRP B CZ3  1 
ATOM   14992 C CH2  . TRP B 1 1091 ? 124.659 148.515 69.694  1.00 21.58 ?  1091 TRP B CH2  1 
ATOM   14993 N N    . ARG B 1 1092 ? 128.671 145.922 75.897  1.00 14.66 ?  1092 ARG B N    1 
ATOM   14994 C CA   . ARG B 1 1092 ? 128.351 144.820 76.801  1.00 12.31 ?  1092 ARG B CA   1 
ATOM   14995 C C    . ARG B 1 1092 ? 127.281 145.216 77.811  1.00 16.29 ?  1092 ARG B C    1 
ATOM   14996 O O    . ARG B 1 1092 ? 126.389 144.416 78.127  1.00 16.30 ?  1092 ARG B O    1 
ATOM   14997 C CB   . ARG B 1 1092 ? 129.615 144.347 77.519  1.00 13.73 ?  1092 ARG B CB   1 
ATOM   14998 C CG   . ARG B 1 1092 ? 129.370 143.254 78.547  1.00 12.57 ?  1092 ARG B CG   1 
ATOM   14999 C CD   . ARG B 1 1092 ? 130.591 142.375 78.742  1.00 14.97 ?  1092 ARG B CD   1 
ATOM   15000 N NE   . ARG B 1 1092 ? 130.281 141.189 79.531  1.00 15.02 ?  1092 ARG B NE   1 
ATOM   15001 C CZ   . ARG B 1 1092 ? 130.637 141.019 80.797  1.00 17.14 ?  1092 ARG B CZ   1 
ATOM   15002 N NH1  . ARG B 1 1092 ? 131.321 141.942 81.453  1.00 17.28 ?  1092 ARG B NH1  1 
ATOM   15003 N NH2  . ARG B 1 1092 ? 130.300 139.893 81.420  1.00 15.10 ?  1092 ARG B NH2  1 
ATOM   15004 N N    . VAL B 1 1093 ? 127.354 146.447 78.330  1.00 19.59 ?  1093 VAL B N    1 
ATOM   15005 C CA   . VAL B 1 1093 ? 126.384 146.888 79.334  1.00 15.87 ?  1093 VAL B CA   1 
ATOM   15006 C C    . VAL B 1 1093 ? 124.975 146.910 78.745  1.00 15.74 ?  1093 VAL B C    1 
ATOM   15007 O O    . VAL B 1 1093 ? 124.038 146.309 79.294  1.00 18.81 ?  1093 VAL B O    1 
ATOM   15008 C CB   . VAL B 1 1093 ? 126.784 148.265 79.894  1.00 13.23 ?  1093 VAL B CB   1 
ATOM   15009 C CG1  . VAL B 1 1093 ? 125.623 148.897 80.642  1.00 11.74 ?  1093 VAL B CG1  1 
ATOM   15010 C CG2  . VAL B 1 1093 ? 127.997 148.136 80.797  1.00 15.27 ?  1093 VAL B CG2  1 
ATOM   15011 N N    . VAL B 1 1094 ? 124.816 147.566 77.592  1.00 13.74 ?  1094 VAL B N    1 
ATOM   15012 C CA   . VAL B 1 1094 ? 123.505 147.636 76.956  1.00 15.16 ?  1094 VAL B CA   1 
ATOM   15013 C C    . VAL B 1 1094 ? 123.086 146.270 76.429  1.00 15.37 ?  1094 VAL B C    1 
ATOM   15014 O O    . VAL B 1 1094 ? 121.889 145.976 76.346  1.00 17.66 ?  1094 VAL B O    1 
ATOM   15015 C CB   . VAL B 1 1094 ? 123.495 148.701 75.843  1.00 15.05 ?  1094 VAL B CB   1 
ATOM   15016 C CG1  . VAL B 1 1094 ? 123.750 150.079 76.428  1.00 17.74 ?  1094 VAL B CG1  1 
ATOM   15017 C CG2  . VAL B 1 1094 ? 124.515 148.379 74.769  1.00 12.43 ?  1094 VAL B CG2  1 
ATOM   15018 N N    . ALA B 1 1095 ? 124.050 145.404 76.102  1.00 14.52 ?  1095 ALA B N    1 
ATOM   15019 C CA   . ALA B 1 1095 ? 123.730 144.061 75.635  1.00 17.52 ?  1095 ALA B CA   1 
ATOM   15020 C C    . ALA B 1 1095 ? 123.087 143.237 76.738  1.00 12.40 ?  1095 ALA B C    1 
ATOM   15021 O O    . ALA B 1 1095 ? 122.055 142.594 76.521  1.00 16.84 ?  1095 ALA B O    1 
ATOM   15022 C CB   . ALA B 1 1095 ? 124.997 143.376 75.124  1.00 19.25 ?  1095 ALA B CB   1 
ATOM   15023 N N    . ILE B 1 1096 ? 123.683 143.250 77.932  1.00 6.07  ?  1096 ILE B N    1 
ATOM   15024 C CA   . ILE B 1 1096 ? 123.087 142.542 79.062  1.00 5.58  ?  1096 ILE B CA   1 
ATOM   15025 C C    . ILE B 1 1096 ? 121.739 143.156 79.421  1.00 8.47  ?  1096 ILE B C    1 
ATOM   15026 O O    . ILE B 1 1096 ? 120.767 142.438 79.708  1.00 12.99 ?  1096 ILE B O    1 
ATOM   15027 C CB   . ILE B 1 1096 ? 124.054 142.536 80.260  1.00 6.36  ?  1096 ILE B CB   1 
ATOM   15028 C CG1  . ILE B 1 1096 ? 125.345 141.805 79.892  1.00 7.27  ?  1096 ILE B CG1  1 
ATOM   15029 C CG2  . ILE B 1 1096 ? 123.408 141.888 81.474  1.00 8.56  ?  1096 ILE B CG2  1 
ATOM   15030 C CD1  . ILE B 1 1096 ? 126.294 141.617 81.052  1.00 7.85  ?  1096 ILE B CD1  1 
ATOM   15031 N N    . ARG B 1 1097 ? 121.647 144.493 79.373  1.00 11.45 ?  1097 ARG B N    1 
ATOM   15032 C CA   . ARG B 1 1097 ? 120.400 145.170 79.725  1.00 14.10 ?  1097 ARG B CA   1 
ATOM   15033 C C    . ARG B 1 1097 ? 119.264 144.805 78.772  1.00 15.75 ?  1097 ARG B C    1 
ATOM   15034 O O    . ARG B 1 1097 ? 118.116 144.639 79.202  1.00 12.60 ?  1097 ARG B O    1 
ATOM   15035 C CB   . ARG B 1 1097 ? 120.620 146.684 79.755  1.00 12.69 ?  1097 ARG B CB   1 
ATOM   15036 C CG   . ARG B 1 1097 ? 119.359 147.502 79.998  1.00 11.78 ?  1097 ARG B CG   1 
ATOM   15037 C CD   . ARG B 1 1097 ? 119.667 148.986 80.138  1.00 14.60 ?  1097 ARG B CD   1 
ATOM   15038 N NE   . ARG B 1 1097 ? 120.764 149.228 81.067  1.00 15.69 ?  1097 ARG B NE   1 
ATOM   15039 C CZ   . ARG B 1 1097 ? 121.700 150.153 80.901  1.00 14.89 ?  1097 ARG B CZ   1 
ATOM   15040 N NH1  . ARG B 1 1097 ? 121.707 150.948 79.844  1.00 11.15 ?  1097 ARG B NH1  1 
ATOM   15041 N NH2  . ARG B 1 1097 ? 122.652 150.284 81.820  1.00 14.45 ?  1097 ARG B NH2  1 
ATOM   15042 N N    . ILE B 1 1098 ? 119.558 144.667 77.479  1.00 17.56 ?  1098 ILE B N    1 
ATOM   15043 C CA   . ILE B 1 1098 ? 118.505 144.348 76.521  1.00 14.98 ?  1098 ILE B CA   1 
ATOM   15044 C C    . ILE B 1 1098 ? 118.275 142.840 76.423  1.00 13.15 ?  1098 ILE B C    1 
ATOM   15045 O O    . ILE B 1 1098 ? 117.187 142.410 76.011  1.00 16.50 ?  1098 ILE B O    1 
ATOM   15046 C CB   . ILE B 1 1098 ? 118.850 144.958 75.147  1.00 15.89 ?  1098 ILE B CB   1 
ATOM   15047 C CG1  . ILE B 1 1098 ? 117.672 144.883 74.180  1.00 16.25 ?  1098 ILE B CG1  1 
ATOM   15048 C CG2  . ILE B 1 1098 ? 120.002 144.207 74.500  1.00 13.89 ?  1098 ILE B CG2  1 
ATOM   15049 C CD1  . ILE B 1 1098 ? 117.955 145.555 72.859  1.00 22.02 ?  1098 ILE B CD1  1 
ATOM   15050 N N    . ALA B 1 1099 ? 119.245 142.025 76.848  1.00 9.46  ?  1099 ALA B N    1 
ATOM   15051 C CA   . ALA B 1 1099 ? 119.151 140.577 76.750  1.00 10.82 ?  1099 ALA B CA   1 
ATOM   15052 C C    . ALA B 1 1099 ? 118.467 139.930 77.943  1.00 13.11 ?  1099 ALA B C    1 
ATOM   15053 O O    . ALA B 1 1099 ? 117.914 138.836 77.793  1.00 14.75 ?  1099 ALA B O    1 
ATOM   15054 C CB   . ALA B 1 1099 ? 120.549 139.971 76.595  1.00 11.45 ?  1099 ALA B CB   1 
ATOM   15055 N N    . THR B 1 1100 ? 118.514 140.556 79.121  1.00 15.13 ?  1100 THR B N    1 
ATOM   15056 C CA   . THR B 1 1100 ? 117.814 139.992 80.276  1.00 8.86  ?  1100 THR B CA   1 
ATOM   15057 C C    . THR B 1 1100 ? 116.306 139.828 80.061  1.00 10.20 ?  1100 THR B C    1 
ATOM   15058 O O    . THR B 1 1100 ? 115.785 138.736 80.361  1.00 17.90 ?  1100 THR B O    1 
ATOM   15059 C CB   . THR B 1 1100 ? 118.125 140.825 81.526  1.00 13.61 ?  1100 THR B CB   1 
ATOM   15060 O OG1  . THR B 1 1100 ? 119.519 140.721 81.838  1.00 14.67 ?  1100 THR B OG1  1 
ATOM   15061 C CG2  . THR B 1 1100 ? 117.308 140.343 82.712  1.00 16.41 ?  1100 THR B CG2  1 
ATOM   15062 N N    . PRO B 1 1101 ? 115.549 140.824 79.561  1.00 9.24  ?  1101 PRO B N    1 
ATOM   15063 C CA   . PRO B 1 1101 ? 114.109 140.583 79.353  1.00 11.24 ?  1101 PRO B CA   1 
ATOM   15064 C C    . PRO B 1 1101 ? 113.800 139.499 78.334  1.00 18.55 ?  1101 PRO B C    1 
ATOM   15065 O O    . PRO B 1 1101 ? 112.787 138.807 78.481  1.00 16.66 ?  1101 PRO B O    1 
ATOM   15066 C CB   . PRO B 1 1101 ? 113.583 141.950 78.893  1.00 10.50 ?  1101 PRO B CB   1 
ATOM   15067 C CG   . PRO B 1 1101 ? 114.578 142.924 79.375  1.00 15.82 ?  1101 PRO B CG   1 
ATOM   15068 C CD   . PRO B 1 1101 ? 115.883 142.223 79.225  1.00 12.91 ?  1101 PRO B CD   1 
ATOM   15069 N N    . LEU B 1 1102 ? 114.634 139.327 77.305  1.00 19.74 ?  1102 LEU B N    1 
ATOM   15070 C CA   . LEU B 1 1102 ? 114.378 138.283 76.315  1.00 13.22 ?  1102 LEU B CA   1 
ATOM   15071 C C    . LEU B 1 1102 ? 114.527 136.891 76.920  1.00 14.19 ?  1102 LEU B C    1 
ATOM   15072 O O    . LEU B 1 1102 ? 113.701 136.005 76.664  1.00 21.52 ?  1102 LEU B O    1 
ATOM   15073 C CB   . LEU B 1 1102 ? 115.312 138.454 75.118  1.00 13.75 ?  1102 LEU B CB   1 
ATOM   15074 C CG   . LEU B 1 1102 ? 115.142 139.741 74.308  1.00 17.06 ?  1102 LEU B CG   1 
ATOM   15075 C CD1  . LEU B 1 1102 ? 115.941 139.674 73.017  1.00 20.44 ?  1102 LEU B CD1  1 
ATOM   15076 C CD2  . LEU B 1 1102 ? 113.673 140.007 74.017  1.00 14.68 ?  1102 LEU B CD2  1 
ATOM   15077 N N    . ILE B 1 1103 ? 115.569 136.681 77.726  1.00 10.80 ?  1103 ILE B N    1 
ATOM   15078 C CA   . ILE B 1 1103 ? 115.745 135.397 78.397  1.00 11.57 ?  1103 ILE B CA   1 
ATOM   15079 C C    . ILE B 1 1103 ? 114.638 135.175 79.422  1.00 14.79 ?  1103 ILE B C    1 
ATOM   15080 O O    . ILE B 1 1103 ? 114.181 134.043 79.623  1.00 20.64 ?  1103 ILE B O    1 
ATOM   15081 C CB   . ILE B 1 1103 ? 117.144 135.312 79.035  1.00 10.73 ?  1103 ILE B CB   1 
ATOM   15082 C CG1  . ILE B 1 1103 ? 118.220 135.623 77.996  1.00 10.02 ?  1103 ILE B CG1  1 
ATOM   15083 C CG2  . ILE B 1 1103 ? 117.384 133.937 79.640  1.00 11.86 ?  1103 ILE B CG2  1 
ATOM   15084 C CD1  . ILE B 1 1103 ? 118.330 134.589 76.902  1.00 18.47 ?  1103 ILE B CD1  1 
ATOM   15085 N N    . MET B 1 1104 ? 114.190 136.245 80.085  1.00 16.00 ?  1104 MET B N    1 
ATOM   15086 C CA   . MET B 1 1104 ? 113.074 136.109 81.020  1.00 19.53 ?  1104 MET B CA   1 
ATOM   15087 C C    . MET B 1 1104 ? 111.784 135.721 80.302  1.00 22.09 ?  1104 MET B C    1 
ATOM   15088 O O    . MET B 1 1104 ? 111.021 134.882 80.795  1.00 20.27 ?  1104 MET B O    1 
ATOM   15089 C CB   . MET B 1 1104 ? 112.882 137.408 81.801  1.00 21.03 ?  1104 MET B CB   1 
ATOM   15090 C CG   . MET B 1 1104 ? 113.648 137.460 83.108  1.00 23.93 ?  1104 MET B CG   1 
ATOM   15091 S SD   . MET B 1 1104 ? 113.595 135.894 83.992  1.00 23.74 ?  1104 MET B SD   1 
ATOM   15092 C CE   . MET B 1 1104 ? 112.137 136.125 85.003  1.00 20.55 ?  1104 MET B CE   1 
ATOM   15093 N N    . GLU B 1 1105 ? 111.524 136.323 79.140  1.00 24.58 ?  1105 GLU B N    1 
ATOM   15094 C CA   . GLU B 1 1105 ? 110.315 136.050 78.373  1.00 21.88 ?  1105 GLU B CA   1 
ATOM   15095 C C    . GLU B 1 1105 ? 110.354 134.692 77.680  1.00 21.37 ?  1105 GLU B C    1 
ATOM   15096 O O    . GLU B 1 1105 ? 109.291 134.124 77.404  1.00 24.75 ?  1105 GLU B O    1 
ATOM   15097 C CB   . GLU B 1 1105 ? 110.101 137.174 77.349  1.00 19.26 ?  1105 GLU B CB   1 
ATOM   15098 C CG   . GLU B 1 1105 ? 108.849 137.065 76.482  1.00 19.40 ?  1105 GLU B CG   1 
ATOM   15099 C CD   . GLU B 1 1105 ? 107.586 137.481 77.210  1.00 26.51 ?  1105 GLU B CD   1 
ATOM   15100 O OE1  . GLU B 1 1105 ? 107.692 138.071 78.304  1.00 27.66 ?  1105 GLU B OE1  1 
ATOM   15101 O OE2  . GLU B 1 1105 ? 106.484 137.218 76.685  1.00 25.29 ?  1105 GLU B OE2  1 
ATOM   15102 N N    . GLN B 1 1106 ? 111.553 134.164 77.408  1.00 22.42 ?  1106 GLN B N    1 
ATOM   15103 C CA   . GLN B 1 1106 ? 111.690 132.875 76.731  1.00 22.69 ?  1106 GLN B CA   1 
ATOM   15104 C C    . GLN B 1 1106 ? 110.979 131.762 77.494  1.00 24.16 ?  1106 GLN B C    1 
ATOM   15105 O O    . GLN B 1 1106 ? 110.036 131.147 76.982  1.00 22.63 ?  1106 GLN B O    1 
ATOM   15106 C CB   . GLN B 1 1106 ? 113.173 132.548 76.556  1.00 19.87 ?  1106 GLN B CB   1 
ATOM   15107 C CG   . GLN B 1 1106 ? 113.461 131.141 76.065  1.00 20.01 ?  1106 GLN B CG   1 
ATOM   15108 C CD   . GLN B 1 1106 ? 114.381 130.382 77.002  1.00 22.42 ?  1106 GLN B CD   1 
ATOM   15109 O OE1  . GLN B 1 1106 ? 114.289 130.513 78.223  1.00 20.80 ?  1106 GLN B OE1  1 
ATOM   15110 N NE2  . GLN B 1 1106 ? 115.283 129.592 76.432  1.00 25.37 ?  1106 GLN B NE2  1 
ATOM   15111 N N    . MET B 1 1107 ? 111.429 131.493 78.724  1.00 26.01 ?  1107 MET B N    1 
ATOM   15112 C CA   . MET B 1 1107 ? 110.785 130.550 79.644  1.00 27.24 ?  1107 MET B CA   1 
ATOM   15113 C C    . MET B 1 1107 ? 110.692 129.142 79.052  1.00 29.65 ?  1107 MET B C    1 
ATOM   15114 O O    . MET B 1 1107 ? 109.612 128.556 78.949  1.00 26.67 ?  1107 MET B O    1 
ATOM   15115 C CB   . MET B 1 1107 ? 109.404 131.056 80.073  1.00 26.04 ?  1107 MET B CB   1 
ATOM   15116 C CG   . MET B 1 1107 ? 109.309 131.787 81.428  1.00 25.42 ?  1107 MET B CG   1 
ATOM   15117 S SD   . MET B 1 1107 ? 110.061 131.058 82.906  1.00 34.58 ?  1107 MET B SD   1 
ATOM   15118 C CE   . MET B 1 1107 ? 111.732 131.696 82.849  1.00 25.93 ?  1107 MET B CE   1 
ATOM   15119 N N    . ALA B 1 1108 ? 111.841 128.599 78.654  1.00 25.46 ?  1108 ALA B N    1 
ATOM   15120 C CA   . ALA B 1 1108 ? 111.915 127.198 78.258  1.00 25.18 ?  1108 ALA B CA   1 
ATOM   15121 C C    . ALA B 1 1108 ? 112.125 126.273 79.448  1.00 27.43 ?  1108 ALA B C    1 
ATOM   15122 O O    . ALA B 1 1108 ? 112.203 125.053 79.265  1.00 25.30 ?  1108 ALA B O    1 
ATOM   15123 C CB   . ALA B 1 1108 ? 113.035 126.991 77.235  1.00 22.74 ?  1108 ALA B CB   1 
ATOM   15124 N N    . PHE B 1 1109 ? 112.231 126.831 80.648  1.00 29.80 ?  1109 PHE B N    1 
ATOM   15125 C CA   . PHE B 1 1109 ? 112.409 126.069 81.878  1.00 25.80 ?  1109 PHE B CA   1 
ATOM   15126 C C    . PHE B 1 1109 ? 111.570 126.763 82.946  1.00 24.58 ?  1109 PHE B C    1 
ATOM   15127 O O    . PHE B 1 1109 ? 110.687 127.574 82.644  1.00 19.80 ?  1109 PHE B O    1 
ATOM   15128 C CB   . PHE B 1 1109 ? 113.890 125.984 82.278  1.00 24.54 ?  1109 PHE B CB   1 
ATOM   15129 C CG   . PHE B 1 1109 ? 114.797 125.465 81.198  1.00 28.48 ?  1109 PHE B CG   1 
ATOM   15130 C CD1  . PHE B 1 1109 ? 115.018 124.108 81.033  1.00 28.79 ?  1109 PHE B CD1  1 
ATOM   15131 C CD2  . PHE B 1 1109 ? 115.448 126.352 80.355  1.00 23.67 ?  1109 PHE B CD2  1 
ATOM   15132 C CE1  . PHE B 1 1109 ? 115.868 123.648 80.036  1.00 25.22 ?  1109 PHE B CE1  1 
ATOM   15133 C CE2  . PHE B 1 1109 ? 116.294 125.902 79.363  1.00 23.40 ?  1109 PHE B CE2  1 
ATOM   15134 C CZ   . PHE B 1 1109 ? 116.505 124.550 79.201  1.00 24.94 ?  1109 PHE B CZ   1 
ATOM   15135 N N    . GLN B 1 1110 ? 111.834 126.449 84.214  1.00 24.95 ?  1110 GLN B N    1 
ATOM   15136 C CA   . GLN B 1 1110 ? 111.173 127.111 85.329  1.00 23.72 ?  1110 GLN B CA   1 
ATOM   15137 C C    . GLN B 1 1110 ? 112.190 127.384 86.428  1.00 23.68 ?  1110 GLN B C    1 
ATOM   15138 O O    . GLN B 1 1110 ? 113.220 126.712 86.521  1.00 22.36 ?  1110 GLN B O    1 
ATOM   15139 C CB   . GLN B 1 1110 ? 110.019 126.274 85.894  1.00 22.72 ?  1110 GLN B CB   1 
ATOM   15140 C CG   . GLN B 1 1110 ? 108.739 126.317 85.077  1.00 25.34 ?  1110 GLN B CG   1 
ATOM   15141 C CD   . GLN B 1 1110 ? 108.252 127.726 84.781  1.00 26.33 ?  1110 GLN B CD   1 
ATOM   15142 O OE1  . GLN B 1 1110 ? 107.973 128.057 83.630  1.00 23.90 ?  1110 GLN B OE1  1 
ATOM   15143 N NE2  . GLN B 1 1110 ? 108.130 128.553 85.815  1.00 26.42 ?  1110 GLN B NE2  1 
ATOM   15144 N N    . GLY B 1 1111 ? 111.889 128.378 87.262  1.00 19.41 ?  1111 GLY B N    1 
ATOM   15145 C CA   . GLY B 1 1111 ? 112.792 128.782 88.325  1.00 23.35 ?  1111 GLY B CA   1 
ATOM   15146 C C    . GLY B 1 1111 ? 113.906 129.726 87.920  1.00 26.89 ?  1111 GLY B C    1 
ATOM   15147 O O    . GLY B 1 1111 ? 114.743 130.062 88.768  1.00 28.21 ?  1111 GLY B O    1 
ATOM   15148 N N    . TRP B 1 1112 ? 113.929 130.172 86.659  1.00 21.56 ?  1112 TRP B N    1 
ATOM   15149 C CA   . TRP B 1 1112 ? 114.870 131.147 86.092  1.00 19.09 ?  1112 TRP B CA   1 
ATOM   15150 C C    . TRP B 1 1112 ? 114.543 132.561 86.580  1.00 22.24 ?  1112 TRP B C    1 
ATOM   15151 O O    . TRP B 1 1112 ? 113.886 133.352 85.894  1.00 23.92 ?  1112 TRP B O    1 
ATOM   15152 C CB   . TRP B 1 1112 ? 114.818 131.068 84.568  1.00 20.75 ?  1112 TRP B CB   1 
ATOM   15153 C CG   . TRP B 1 1112 ? 115.704 130.011 83.946  1.00 25.87 ?  1112 TRP B CG   1 
ATOM   15154 C CD1  . TRP B 1 1112 ? 115.305 128.927 83.220  1.00 26.14 ?  1112 TRP B CD1  1 
ATOM   15155 C CD2  . TRP B 1 1112 ? 117.145 130.023 83.875  1.00 25.76 ?  1112 TRP B CD2  1 
ATOM   15156 N NE1  . TRP B 1 1112 ? 116.398 128.224 82.778  1.00 22.62 ?  1112 TRP B NE1  1 
ATOM   15157 C CE2  . TRP B 1 1112 ? 117.541 128.876 83.153  1.00 25.82 ?  1112 TRP B CE2  1 
ATOM   15158 C CE3  . TRP B 1 1112 ? 118.137 130.879 84.378  1.00 21.88 ?  1112 TRP B CE3  1 
ATOM   15159 C CZ2  . TRP B 1 1112 ? 118.877 128.562 82.925  1.00 22.97 ?  1112 TRP B CZ2  1 
ATOM   15160 C CZ3  . TRP B 1 1112 ? 119.472 130.556 84.153  1.00 18.26 ?  1112 TRP B CZ3  1 
ATOM   15161 C CH2  . TRP B 1 1112 ? 119.826 129.416 83.428  1.00 19.45 ?  1112 TRP B CH2  1 
ATOM   15162 N N    . THR B 1 1113 ? 115.041 132.900 87.767  1.00 22.76 ?  1113 THR B N    1 
ATOM   15163 C CA   . THR B 1 1113 ? 114.806 134.209 88.353  1.00 20.18 ?  1113 THR B CA   1 
ATOM   15164 C C    . THR B 1 1113 ? 115.638 135.272 87.639  1.00 16.97 ?  1113 THR B C    1 
ATOM   15165 O O    . THR B 1 1113 ? 116.542 134.971 86.859  1.00 17.94 ?  1113 THR B O    1 
ATOM   15166 C CB   . THR B 1 1113 ? 115.148 134.203 89.839  1.00 18.36 ?  1113 THR B CB   1 
ATOM   15167 O OG1  . THR B 1 1113 ? 116.511 133.792 90.000  1.00 18.63 ?  1113 THR B OG1  1 
ATOM   15168 C CG2  . THR B 1 1113 ? 114.245 133.243 90.583  1.00 16.40 ?  1113 THR B CG2  1 
ATOM   15169 N N    . GLN B 1 1114 ? 115.309 136.540 87.912  1.00 17.91 ?  1114 GLN B N    1 
ATOM   15170 C CA   . GLN B 1 1114 ? 116.021 137.647 87.276  1.00 18.55 ?  1114 GLN B CA   1 
ATOM   15171 C C    . GLN B 1 1114 ? 117.480 137.685 87.705  1.00 15.71 ?  1114 GLN B C    1 
ATOM   15172 O O    . GLN B 1 1114 ? 118.367 137.954 86.888  1.00 22.01 ?  1114 GLN B O    1 
ATOM   15173 C CB   . GLN B 1 1114 ? 115.344 138.976 87.608  1.00 21.27 ?  1114 GLN B CB   1 
ATOM   15174 C CG   . GLN B 1 1114 ? 116.032 140.195 86.994  1.00 17.92 ?  1114 GLN B CG   1 
ATOM   15175 C CD   . GLN B 1 1114 ? 115.302 140.718 85.775  1.00 21.19 ?  1114 GLN B CD   1 
ATOM   15176 O OE1  . GLN B 1 1114 ? 114.858 139.941 84.932  1.00 19.57 ?  1114 GLN B OE1  1 
ATOM   15177 N NE2  . GLN B 1 1114 ? 115.186 142.038 85.664  1.00 20.81 ?  1114 GLN B NE2  1 
ATOM   15178 N N    . GLU B 1 1115 ? 117.745 137.434 88.987  1.00 13.74 ?  1115 GLU B N    1 
ATOM   15179 C CA   . GLU B 1 1115 ? 119.118 137.438 89.477  1.00 12.89 ?  1115 GLU B CA   1 
ATOM   15180 C C    . GLU B 1 1115 ? 119.953 136.342 88.828  1.00 11.05 ?  1115 GLU B C    1 
ATOM   15181 O O    . GLU B 1 1115 ? 121.104 136.570 88.447  1.00 17.98 ?  1115 GLU B O    1 
ATOM   15182 C CB   . GLU B 1 1115 ? 119.130 137.263 90.992  1.00 18.10 ?  1115 GLU B CB   1 
ATOM   15183 C CG   . GLU B 1 1115 ? 120.518 137.115 91.594  1.00 19.74 ?  1115 GLU B CG   1 
ATOM   15184 C CD   . GLU B 1 1115 ? 120.603 137.645 93.016  1.00 22.34 ?  1115 GLU B CD   1 
ATOM   15185 O OE1  . GLU B 1 1115 ? 120.284 136.891 93.961  1.00 18.19 ?  1115 GLU B OE1  1 
ATOM   15186 O OE2  . GLU B 1 1115 ? 120.993 138.817 93.192  1.00 19.78 ?  1115 GLU B OE2  1 
ATOM   15187 N N    . LYS B 1 1116 ? 119.403 135.134 88.721  1.00 11.04 ?  1116 LYS B N    1 
ATOM   15188 C CA   . LYS B 1 1116 ? 120.182 134.025 88.178  1.00 14.70 ?  1116 LYS B CA   1 
ATOM   15189 C C    . LYS B 1 1116 ? 120.252 134.060 86.657  1.00 13.06 ?  1116 LYS B C    1 
ATOM   15190 O O    . LYS B 1 1116 ? 121.237 133.584 86.075  1.00 15.63 ?  1116 LYS B O    1 
ATOM   15191 C CB   . LYS B 1 1116 ? 119.631 132.712 88.749  1.00 16.79 ?  1116 LYS B CB   1 
ATOM   15192 C CG   . LYS B 1 1116 ? 120.052 131.387 88.120  1.00 18.85 ?  1116 LYS B CG   1 
ATOM   15193 C CD   . LYS B 1 1116 ? 119.025 130.312 88.522  1.00 19.88 ?  1116 LYS B CD   1 
ATOM   15194 C CE   . LYS B 1 1116 ? 118.700 129.306 87.438  1.00 18.89 ?  1116 LYS B CE   1 
ATOM   15195 N NZ   . LYS B 1 1116 ? 119.885 128.645 86.816  1.00 19.37 ?  1116 LYS B NZ   1 
ATOM   15196 N N    . VAL B 1 1117 ? 119.259 134.667 86.005  1.00 8.66  ?  1117 VAL B N    1 
ATOM   15197 C CA   . VAL B 1 1117 ? 119.407 135.046 84.600  1.00 3.10  ?  1117 VAL B CA   1 
ATOM   15198 C C    . VAL B 1 1117 ? 120.543 136.045 84.419  1.00 8.30  ?  1117 VAL B C    1 
ATOM   15199 O O    . VAL B 1 1117 ? 121.355 135.914 83.497  1.00 16.04 ?  1117 VAL B O    1 
ATOM   15200 C CB   . VAL B 1 1117 ? 118.079 135.601 84.056  1.00 10.04 ?  1117 VAL B CB   1 
ATOM   15201 C CG1  . VAL B 1 1117 ? 118.314 136.420 82.793  1.00 11.02 ?  1117 VAL B CG1  1 
ATOM   15202 C CG2  . VAL B 1 1117 ? 117.133 134.459 83.740  1.00 15.12 ?  1117 VAL B CG2  1 
ATOM   15203 N N    . LYS B 1 1118 ? 120.611 137.069 85.279  1.00 12.52 ?  1118 LYS B N    1 
ATOM   15204 C CA   . LYS B 1 1118 ? 121.671 138.071 85.155  1.00 3.69  ?  1118 LYS B CA   1 
ATOM   15205 C C    . LYS B 1 1118 ? 123.044 137.465 85.414  1.00 4.69  ?  1118 LYS B C    1 
ATOM   15206 O O    . LYS B 1 1118 ? 124.012 137.785 84.715  1.00 10.08 ?  1118 LYS B O    1 
ATOM   15207 C CB   . LYS B 1 1118 ? 121.417 139.236 86.115  1.00 7.60  ?  1118 LYS B CB   1 
ATOM   15208 C CG   . LYS B 1 1118 ? 120.343 140.214 85.655  1.00 10.59 ?  1118 LYS B CG   1 
ATOM   15209 C CD   . LYS B 1 1118 ? 120.331 141.485 86.495  1.00 9.46  ?  1118 LYS B CD   1 
ATOM   15210 C CE   . LYS B 1 1118 ? 120.351 141.177 87.986  1.00 14.41 ?  1118 LYS B CE   1 
ATOM   15211 N NZ   . LYS B 1 1118 ? 119.476 142.105 88.756  1.00 14.18 ?  1118 LYS B NZ   1 
ATOM   15212 N N    . LEU B 1 1119 ? 123.145 136.586 86.409  1.00 11.76 ?  1119 LEU B N    1 
ATOM   15213 C CA   . LEU B 1 1119 ? 124.422 135.943 86.697  1.00 9.06  ?  1119 LEU B CA   1 
ATOM   15214 C C    . LEU B 1 1119 ? 124.804 134.938 85.617  1.00 14.39 ?  1119 LEU B C    1 
ATOM   15215 O O    . LEU B 1 1119 ? 125.994 134.671 85.416  1.00 16.12 ?  1119 LEU B O    1 
ATOM   15216 C CB   . LEU B 1 1119 ? 124.373 135.265 88.064  1.00 8.73  ?  1119 LEU B CB   1 
ATOM   15217 C CG   . LEU B 1 1119 ? 124.921 136.094 89.226  1.00 12.03 ?  1119 LEU B CG   1 
ATOM   15218 C CD1  . LEU B 1 1119 ? 124.787 135.344 90.539  1.00 14.30 ?  1119 LEU B CD1  1 
ATOM   15219 C CD2  . LEU B 1 1119 ? 126.363 136.499 88.976  1.00 13.00 ?  1119 LEU B CD2  1 
ATOM   15220 N N    . HIS B 1 1120 ? 123.820 134.370 84.913  1.00 14.08 ?  1120 HIS B N    1 
ATOM   15221 C CA   . HIS B 1 1120 ? 124.138 133.521 83.772  1.00 9.95  ?  1120 HIS B CA   1 
ATOM   15222 C C    . HIS B 1 1120 ? 124.605 134.351 82.579  1.00 10.85 ?  1120 HIS B C    1 
ATOM   15223 O O    . HIS B 1 1120 ? 125.532 133.954 81.866  1.00 15.50 ?  1120 HIS B O    1 
ATOM   15224 C CB   . HIS B 1 1120 ? 122.920 132.671 83.414  1.00 12.92 ?  1120 HIS B CB   1 
ATOM   15225 C CG   . HIS B 1 1120 ? 122.867 132.250 81.980  1.00 14.34 ?  1120 HIS B CG   1 
ATOM   15226 N ND1  . HIS B 1 1120 ? 121.896 132.696 81.111  1.00 13.23 ?  1120 HIS B ND1  1 
ATOM   15227 C CD2  . HIS B 1 1120 ? 123.649 131.404 81.269  1.00 17.62 ?  1120 HIS B CD2  1 
ATOM   15228 C CE1  . HIS B 1 1120 ? 122.089 132.155 79.922  1.00 13.13 ?  1120 HIS B CE1  1 
ATOM   15229 N NE2  . HIS B 1 1120 ? 123.146 131.365 79.991  1.00 16.88 ?  1120 HIS B NE2  1 
ATOM   15230 N N    . LEU B 1 1121 ? 123.977 135.508 82.349  1.00 8.94  ?  1121 LEU B N    1 
ATOM   15231 C CA   . LEU B 1 1121 ? 124.380 136.381 81.250  1.00 6.23  ?  1121 LEU B CA   1 
ATOM   15232 C C    . LEU B 1 1121 ? 125.711 137.073 81.516  1.00 9.78  ?  1121 LEU B C    1 
ATOM   15233 O O    . LEU B 1 1121 ? 126.380 137.487 80.563  1.00 16.82 ?  1121 LEU B O    1 
ATOM   15234 C CB   . LEU B 1 1121 ? 123.301 137.433 80.987  1.00 6.93  ?  1121 LEU B CB   1 
ATOM   15235 C CG   . LEU B 1 1121 ? 122.165 137.070 80.030  1.00 9.43  ?  1121 LEU B CG   1 
ATOM   15236 C CD1  . LEU B 1 1121 ? 121.140 138.189 79.981  1.00 9.96  ?  1121 LEU B CD1  1 
ATOM   15237 C CD2  . LEU B 1 1121 ? 122.697 136.772 78.640  1.00 11.54 ?  1121 LEU B CD2  1 
ATOM   15238 N N    . GLU B 1 1122 ? 126.096 137.218 82.786  1.00 11.90 ?  1122 GLU B N    1 
ATOM   15239 C CA   . GLU B 1 1122 ? 127.368 137.853 83.119  1.00 10.45 ?  1122 GLU B CA   1 
ATOM   15240 C C    . GLU B 1 1122 ? 128.548 137.034 82.611  1.00 15.66 ?  1122 GLU B C    1 
ATOM   15241 O O    . GLU B 1 1122 ? 129.549 137.596 82.150  1.00 19.85 ?  1122 GLU B O    1 
ATOM   15242 C CB   . GLU B 1 1122 ? 127.462 138.057 84.633  1.00 11.20 ?  1122 GLU B CB   1 
ATOM   15243 C CG   . GLU B 1 1122 ? 128.810 138.556 85.127  1.00 14.33 ?  1122 GLU B CG   1 
ATOM   15244 C CD   . GLU B 1 1122 ? 128.924 140.066 85.084  1.00 21.81 ?  1122 GLU B CD   1 
ATOM   15245 O OE1  . GLU B 1 1122 ? 127.934 140.730 84.709  1.00 25.43 ?  1122 GLU B OE1  1 
ATOM   15246 O OE2  . GLU B 1 1122 ? 130.005 140.591 85.421  1.00 22.98 ?  1122 GLU B OE2  1 
ATOM   15247 N N    . ARG B 1 1123 ? 128.444 135.704 82.680  1.00 20.82 ?  1123 ARG B N    1 
ATOM   15248 C CA   . ARG B 1 1123 ? 129.518 134.832 82.217  1.00 24.17 ?  1123 ARG B CA   1 
ATOM   15249 C C    . ARG B 1 1123 ? 129.729 134.908 80.711  1.00 18.31 ?  1123 ARG B C    1 
ATOM   15250 O O    . ARG B 1 1123 ? 130.833 134.618 80.239  1.00 16.36 ?  1123 ARG B O    1 
ATOM   15251 C CB   . ARG B 1 1123 ? 129.226 133.386 82.617  1.00 21.48 ?  1123 ARG B CB   1 
ATOM   15252 C CG   . ARG B 1 1123 ? 129.874 132.940 83.915  1.00 21.08 ?  1123 ARG B CG   1 
ATOM   15253 C CD   . ARG B 1 1123 ? 129.847 131.422 84.047  1.00 22.37 ?  1123 ARG B CD   1 
ATOM   15254 N NE   . ARG B 1 1123 ? 128.496 130.910 84.248  1.00 21.44 ?  1123 ARG B NE   1 
ATOM   15255 C CZ   . ARG B 1 1123 ? 127.763 130.332 83.305  1.00 21.84 ?  1123 ARG B CZ   1 
ATOM   15256 N NH1  . ARG B 1 1123 ? 128.221 130.170 82.075  1.00 24.34 ?  1123 ARG B NH1  1 
ATOM   15257 N NH2  . ARG B 1 1123 ? 126.538 129.909 83.604  1.00 19.54 ?  1123 ARG B NH2  1 
ATOM   15258 N N    . GLY B 1 1124 ? 128.701 135.278 79.947  1.00 16.04 ?  1124 GLY B N    1 
ATOM   15259 C CA   . GLY B 1 1124 ? 128.843 135.356 78.511  1.00 17.38 ?  1124 GLY B CA   1 
ATOM   15260 C C    . GLY B 1 1124 ? 129.579 136.602 78.058  1.00 21.62 ?  1124 GLY B C    1 
ATOM   15261 O O    . GLY B 1 1124 ? 129.681 137.598 78.771  1.00 24.00 ?  1124 GLY B O    1 
ATOM   15262 N N    . TYR B 1 1125 ? 130.101 136.533 76.835  1.00 27.74 ?  1125 TYR B N    1 
ATOM   15263 C CA   . TYR B 1 1125 ? 130.808 137.652 76.229  1.00 25.66 ?  1125 TYR B CA   1 
ATOM   15264 C C    . TYR B 1 1125 ? 130.549 137.640 74.730  1.00 22.80 ?  1125 TYR B C    1 
ATOM   15265 O O    . TYR B 1 1125 ? 130.158 136.621 74.156  1.00 23.66 ?  1125 TYR B O    1 
ATOM   15266 C CB   . TYR B 1 1125 ? 132.318 137.595 76.500  1.00 21.54 ?  1125 TYR B CB   1 
ATOM   15267 C CG   . TYR B 1 1125 ? 132.703 137.631 77.963  1.00 22.96 ?  1125 TYR B CG   1 
ATOM   15268 C CD1  . TYR B 1 1125 ? 132.795 138.835 78.648  1.00 22.10 ?  1125 TYR B CD1  1 
ATOM   15269 C CD2  . TYR B 1 1125 ? 132.990 136.461 78.655  1.00 27.17 ?  1125 TYR B CD2  1 
ATOM   15270 C CE1  . TYR B 1 1125 ? 133.154 138.873 79.982  1.00 26.08 ?  1125 TYR B CE1  1 
ATOM   15271 C CE2  . TYR B 1 1125 ? 133.351 136.490 79.990  1.00 27.41 ?  1125 TYR B CE2  1 
ATOM   15272 C CZ   . TYR B 1 1125 ? 133.429 137.699 80.648  1.00 29.65 ?  1125 TYR B CZ   1 
ATOM   15273 O OH   . TYR B 1 1125 ? 133.785 137.736 81.976  1.00 28.89 ?  1125 TYR B OH   1 
ATOM   15274 N N    . LEU B 1 1126 ? 130.773 138.789 74.099  1.00 20.31 ?  1126 LEU B N    1 
ATOM   15275 C CA   . LEU B 1 1126 ? 130.622 138.931 72.658  1.00 24.85 ?  1126 LEU B CA   1 
ATOM   15276 C C    . LEU B 1 1126 ? 131.996 139.012 72.006  1.00 28.65 ?  1126 LEU B C    1 
ATOM   15277 O O    . LEU B 1 1126 ? 132.926 139.602 72.564  1.00 26.58 ?  1126 LEU B O    1 
ATOM   15278 C CB   . LEU B 1 1126 ? 129.792 140.171 72.304  1.00 26.36 ?  1126 LEU B CB   1 
ATOM   15279 C CG   . LEU B 1 1126 ? 130.119 141.516 72.958  1.00 25.52 ?  1126 LEU B CG   1 
ATOM   15280 C CD1  . LEU B 1 1126 ? 131.042 142.346 72.074  1.00 22.87 ?  1126 LEU B CD1  1 
ATOM   15281 C CD2  . LEU B 1 1126 ? 128.845 142.285 73.275  1.00 23.12 ?  1126 LEU B CD2  1 
ATOM   15282 N N    . VAL B 1 1127 ? 132.116 138.415 70.823  1.00 27.02 ?  1127 VAL B N    1 
ATOM   15283 C CA   . VAL B 1 1127 ? 133.363 138.380 70.069  1.00 26.11 ?  1127 VAL B CA   1 
ATOM   15284 C C    . VAL B 1 1127 ? 133.133 139.095 68.745  1.00 27.90 ?  1127 VAL B C    1 
ATOM   15285 O O    . VAL B 1 1127 ? 132.126 138.850 68.071  1.00 27.21 ?  1127 VAL B O    1 
ATOM   15286 C CB   . VAL B 1 1127 ? 133.848 136.935 69.840  1.00 24.99 ?  1127 VAL B CB   1 
ATOM   15287 C CG1  . VAL B 1 1127 ? 135.145 136.922 69.042  1.00 25.78 ?  1127 VAL B CG1  1 
ATOM   15288 C CG2  . VAL B 1 1127 ? 134.027 136.218 71.169  1.00 21.31 ?  1127 VAL B CG2  1 
ATOM   15289 N N    . ASP B 1 1128 ? 134.056 139.987 68.388  1.00 28.55 ?  1128 ASP B N    1 
ATOM   15290 C CA   . ASP B 1 1128 ? 133.929 140.757 67.158  1.00 29.05 ?  1128 ASP B CA   1 
ATOM   15291 C C    . ASP B 1 1128 ? 134.000 139.849 65.937  1.00 26.27 ?  1128 ASP B C    1 
ATOM   15292 O O    . ASP B 1 1128 ? 134.758 138.875 65.907  1.00 23.47 ?  1128 ASP B O    1 
ATOM   15293 C CB   . ASP B 1 1128 ? 135.024 141.820 67.082  1.00 28.91 ?  1128 ASP B CB   1 
ATOM   15294 C CG   . ASP B 1 1128 ? 136.413 141.238 67.258  1.00 29.47 ?  1128 ASP B CG   1 
ATOM   15295 O OD1  . ASP B 1 1128 ? 136.533 140.160 67.876  1.00 31.66 ?  1128 ASP B OD1  1 
ATOM   15296 O OD2  . ASP B 1 1128 ? 137.384 141.858 66.775  1.00 26.55 ?  1128 ASP B OD2  1 
ATOM   15297 N N    . LEU B 1 1129 ? 133.197 140.174 64.924  1.00 27.13 ?  1129 LEU B N    1 
ATOM   15298 C CA   . LEU B 1 1129 ? 133.160 139.393 63.695  1.00 27.18 ?  1129 LEU B CA   1 
ATOM   15299 C C    . LEU B 1 1129 ? 134.298 139.731 62.741  1.00 29.76 ?  1129 LEU B C    1 
ATOM   15300 O O    . LEU B 1 1129 ? 134.491 139.009 61.757  1.00 25.08 ?  1129 LEU B O    1 
ATOM   15301 C CB   . LEU B 1 1129 ? 131.819 139.598 62.986  1.00 24.82 ?  1129 LEU B CB   1 
ATOM   15302 C CG   . LEU B 1 1129 ? 130.569 139.190 63.766  1.00 23.68 ?  1129 LEU B CG   1 
ATOM   15303 C CD1  . LEU B 1 1129 ? 129.413 140.127 63.453  1.00 25.37 ?  1129 LEU B CD1  1 
ATOM   15304 C CD2  . LEU B 1 1129 ? 130.193 137.749 63.460  1.00 24.76 ?  1129 LEU B CD2  1 
ATOM   15305 N N    . ALA B 1 1130 ? 135.044 140.809 63.002  1.00 30.49 ?  1130 ALA B N    1 
ATOM   15306 C CA   . ALA B 1 1130 ? 136.169 141.164 62.141  1.00 29.34 ?  1130 ALA B CA   1 
ATOM   15307 C C    . ALA B 1 1130 ? 137.271 140.114 62.204  1.00 27.96 ?  1130 ALA B C    1 
ATOM   15308 O O    . ALA B 1 1130 ? 137.882 139.786 61.180  1.00 23.52 ?  1130 ALA B O    1 
ATOM   15309 C CB   . ALA B 1 1130 ? 136.712 142.539 62.529  1.00 23.42 ?  1130 ALA B CB   1 
ATOM   15310 N N    . GLU B 1 1131 ? 137.543 139.582 63.398  1.00 26.41 ?  1131 GLU B N    1 
ATOM   15311 C CA   . GLU B 1 1131 ? 138.561 138.545 63.534  1.00 26.02 ?  1131 GLU B CA   1 
ATOM   15312 C C    . GLU B 1 1131 ? 138.119 137.244 62.877  1.00 26.55 ?  1131 GLU B C    1 
ATOM   15313 O O    . GLU B 1 1131 ? 138.941 136.527 62.293  1.00 24.74 ?  1131 GLU B O    1 
ATOM   15314 C CB   . GLU B 1 1131 ? 138.882 138.318 65.011  1.00 25.06 ?  1131 GLU B CB   1 
ATOM   15315 C CG   . GLU B 1 1131 ? 140.192 137.588 65.256  1.00 23.83 ?  1131 GLU B CG   1 
ATOM   15316 C CD   . GLU B 1 1131 ? 141.378 138.529 65.326  1.00 23.83 ?  1131 GLU B CD   1 
ATOM   15317 O OE1  . GLU B 1 1131 ? 141.172 139.728 65.607  1.00 23.56 ?  1131 GLU B OE1  1 
ATOM   15318 O OE2  . GLU B 1 1131 ? 142.517 138.069 65.102  1.00 23.80 ?  1131 GLU B OE2  1 
ATOM   15319 N N    . SER B 1 1132 ? 136.829 136.922 62.958  1.00 25.53 ?  1132 SER B N    1 
ATOM   15320 C CA   . SER B 1 1132 ? 136.295 135.680 62.419  1.00 26.58 ?  1132 SER B CA   1 
ATOM   15321 C C    . SER B 1 1132 ? 135.769 135.828 60.996  1.00 26.74 ?  1132 SER B C    1 
ATOM   15322 O O    . SER B 1 1132 ? 134.969 134.994 60.558  1.00 25.44 ?  1132 SER B O    1 
ATOM   15323 C CB   . SER B 1 1132 ? 135.191 135.142 63.332  1.00 25.12 ?  1132 SER B CB   1 
ATOM   15324 O OG   . SER B 1 1132 ? 135.708 134.783 64.601  1.00 27.32 ?  1132 SER B OG   1 
ATOM   15325 N N    . HIS B 1 1133 ? 136.200 136.871 60.277  1.00 26.68 ?  1133 HIS B N    1 
ATOM   15326 C CA   . HIS B 1 1133 ? 135.847 137.098 58.869  1.00 30.15 ?  1133 HIS B CA   1 
ATOM   15327 C C    . HIS B 1 1133 ? 134.336 137.187 58.660  1.00 29.55 ?  1133 HIS B C    1 
ATOM   15328 O O    . HIS B 1 1133 ? 133.807 136.716 57.650  1.00 30.13 ?  1133 HIS B O    1 
ATOM   15329 C CB   . HIS B 1 1133 ? 136.457 136.023 57.964  1.00 31.76 ?  1133 HIS B CB   1 
ATOM   15330 C CG   . HIS B 1 1133 ? 137.929 135.834 58.156  1.00 33.71 ?  1133 HIS B CG   1 
ATOM   15331 N ND1  . HIS B 1 1133 ? 138.869 136.561 57.459  1.00 32.65 ?  1133 HIS B ND1  1 
ATOM   15332 C CD2  . HIS B 1 1133 ? 138.623 135.001 58.967  1.00 31.75 ?  1133 HIS B CD2  1 
ATOM   15333 C CE1  . HIS B 1 1133 ? 140.079 136.184 57.831  1.00 28.55 ?  1133 HIS B CE1  1 
ATOM   15334 N NE2  . HIS B 1 1133 ? 139.958 135.239 58.746  1.00 34.48 ?  1133 HIS B NE2  1 
ATOM   15335 N N    . PHE B 1 1134 ? 133.644 137.802 59.626  1.00 26.42 ?  1134 PHE B N    1 
ATOM   15336 C CA   . PHE B 1 1134 ? 132.200 138.056 59.560  1.00 26.63 ?  1134 PHE B CA   1 
ATOM   15337 C C    . PHE B 1 1134 ? 131.395 136.772 59.361  1.00 25.82 ?  1134 PHE B C    1 
ATOM   15338 O O    . PHE B 1 1134 ? 130.401 136.750 58.632  1.00 25.33 ?  1134 PHE B O    1 
ATOM   15339 C CB   . PHE B 1 1134 ? 131.865 139.080 58.470  1.00 26.51 ?  1134 PHE B CB   1 
ATOM   15340 C CG   . PHE B 1 1134 ? 132.635 140.365 58.584  1.00 28.96 ?  1134 PHE B CG   1 
ATOM   15341 C CD1  . PHE B 1 1134 ? 132.775 140.998 59.808  1.00 27.48 ?  1134 PHE B CD1  1 
ATOM   15342 C CD2  . PHE B 1 1134 ? 133.218 140.941 57.467  1.00 27.51 ?  1134 PHE B CD2  1 
ATOM   15343 C CE1  . PHE B 1 1134 ? 133.481 142.182 59.917  1.00 26.03 ?  1134 PHE B CE1  1 
ATOM   15344 C CE2  . PHE B 1 1134 ? 133.927 142.125 57.568  1.00 25.47 ?  1134 PHE B CE2  1 
ATOM   15345 C CZ   . PHE B 1 1134 ? 134.058 142.745 58.796  1.00 26.81 ?  1134 PHE B CZ   1 
ATOM   15346 N N    . GLN B 1 1135 ? 131.825 135.693 60.011  1.00 21.89 ?  1135 GLN B N    1 
ATOM   15347 C CA   . GLN B 1 1135 ? 131.061 134.453 60.008  1.00 24.16 ?  1135 GLN B CA   1 
ATOM   15348 C C    . GLN B 1 1135 ? 131.251 133.756 61.345  1.00 23.86 ?  1135 GLN B C    1 
ATOM   15349 O O    . GLN B 1 1135 ? 132.368 133.687 61.866  1.00 22.52 ?  1135 GLN B O    1 
ATOM   15350 C CB   . GLN B 1 1135 ? 131.472 133.526 58.856  1.00 21.76 ?  1135 GLN B CB   1 
ATOM   15351 C CG   . GLN B 1 1135 ? 132.955 133.516 58.540  1.00 22.77 ?  1135 GLN B CG   1 
ATOM   15352 C CD   . GLN B 1 1135 ? 133.701 132.427 59.286  1.00 26.12 ?  1135 GLN B CD   1 
ATOM   15353 O OE1  . GLN B 1 1135 ? 133.173 131.337 59.507  1.00 27.81 ?  1135 GLN B OE1  1 
ATOM   15354 N NE2  . GLN B 1 1135 ? 134.936 132.717 59.678  1.00 27.47 ?  1135 GLN B NE2  1 
ATOM   15355 N N    . PHE B 1 1136 ? 130.153 133.244 61.895  1.00 25.42 ?  1136 PHE B N    1 
ATOM   15356 C CA   . PHE B 1 1136 ? 130.149 132.597 63.199  1.00 25.82 ?  1136 PHE B CA   1 
ATOM   15357 C C    . PHE B 1 1136 ? 129.701 131.150 63.056  1.00 26.45 ?  1136 PHE B C    1 
ATOM   15358 O O    . PHE B 1 1136 ? 128.708 130.860 62.382  1.00 26.49 ?  1136 PHE B O    1 
ATOM   15359 C CB   . PHE B 1 1136 ? 129.231 133.339 64.179  1.00 22.63 ?  1136 PHE B CB   1 
ATOM   15360 C CG   . PHE B 1 1136 ? 129.152 132.704 65.538  1.00 23.41 ?  1136 PHE B CG   1 
ATOM   15361 C CD1  . PHE B 1 1136 ? 130.268 132.647 66.358  1.00 26.33 ?  1136 PHE B CD1  1 
ATOM   15362 C CD2  . PHE B 1 1136 ? 127.960 132.167 65.998  1.00 23.07 ?  1136 PHE B CD2  1 
ATOM   15363 C CE1  . PHE B 1 1136 ? 130.198 132.064 67.609  1.00 24.27 ?  1136 PHE B CE1  1 
ATOM   15364 C CE2  . PHE B 1 1136 ? 127.884 131.582 67.249  1.00 25.88 ?  1136 PHE B CE2  1 
ATOM   15365 C CZ   . PHE B 1 1136 ? 129.004 131.531 68.055  1.00 24.44 ?  1136 PHE B CZ   1 
ATOM   15366 N N    . ASN B 1 1137 ? 130.438 130.247 63.696  1.00 26.22 ?  1137 ASN B N    1 
ATOM   15367 C CA   . ASN B 1 1137 ? 130.124 128.825 63.693  1.00 29.01 ?  1137 ASN B CA   1 
ATOM   15368 C C    . ASN B 1 1137 ? 129.471 128.468 65.022  1.00 25.62 ?  1137 ASN B C    1 
ATOM   15369 O O    . ASN B 1 1137 ? 130.049 128.714 66.087  1.00 26.41 ?  1137 ASN B O    1 
ATOM   15370 C CB   . ASN B 1 1137 ? 131.383 127.989 63.465  1.00 28.44 ?  1137 ASN B CB   1 
ATOM   15371 C CG   . ASN B 1 1137 ? 132.578 128.513 64.240  1.00 28.26 ?  1137 ASN B CG   1 
ATOM   15372 O OD1  . ASN B 1 1137 ? 132.639 129.692 64.587  1.00 27.89 ?  1137 ASN B OD1  1 
ATOM   15373 N ND2  . ASN B 1 1137 ? 133.537 127.636 64.513  1.00 25.19 ?  1137 ASN B ND2  1 
ATOM   15374 N N    . ILE B 1 1138 ? 128.276 127.892 64.961  1.00 26.31 ?  1138 ILE B N    1 
ATOM   15375 C CA   . ILE B 1 1138 ? 127.517 127.567 66.162  1.00 27.73 ?  1138 ILE B CA   1 
ATOM   15376 C C    . ILE B 1 1138 ? 127.929 126.186 66.655  1.00 29.68 ?  1138 ILE B C    1 
ATOM   15377 O O    . ILE B 1 1138 ? 127.907 125.204 65.901  1.00 29.29 ?  1138 ILE B O    1 
ATOM   15378 C CB   . ILE B 1 1138 ? 126.001 127.641 65.899  1.00 27.75 ?  1138 ILE B CB   1 
ATOM   15379 C CG1  . ILE B 1 1138 ? 125.214 127.033 67.059  1.00 23.62 ?  1138 ILE B CG1  1 
ATOM   15380 C CG2  . ILE B 1 1138 ? 125.630 126.927 64.624  1.00 27.84 ?  1138 ILE B CG2  1 
ATOM   15381 C CD1  . ILE B 1 1138 ? 123.745 127.400 67.061  1.00 26.63 ?  1138 ILE B CD1  1 
ATOM   15382 N N    . ASP B 1 1139 ? 128.347 126.118 67.912  1.00 26.87 ?  1139 ASP B N    1 
ATOM   15383 C CA   . ASP B 1 1139 ? 128.501 124.861 68.619  1.00 23.15 ?  1139 ASP B CA   1 
ATOM   15384 C C    . ASP B 1 1139 ? 127.278 124.661 69.508  1.00 23.73 ?  1139 ASP B C    1 
ATOM   15385 O O    . ASP B 1 1139 ? 126.416 125.531 69.622  1.00 28.75 ?  1139 ASP B O    1 
ATOM   15386 C CB   . ASP B 1 1139 ? 129.795 124.853 69.438  1.00 23.26 ?  1139 ASP B CB   1 
ATOM   15387 C CG   . ASP B 1 1139 ? 130.994 125.345 68.647  1.00 27.07 ?  1139 ASP B CG   1 
ATOM   15388 O OD1  . ASP B 1 1139 ? 130.850 125.610 67.436  1.00 27.70 ?  1139 ASP B OD1  1 
ATOM   15389 O OD2  . ASP B 1 1139 ? 132.085 125.469 69.242  1.00 27.79 ?  1139 ASP B OD2  1 
ATOM   15390 N N    . ALA B 1 1140 ? 127.189 123.500 70.140  1.00 21.39 ?  1140 ALA B N    1 
ATOM   15391 C CA   . ALA B 1 1140 ? 126.158 123.295 71.145  1.00 24.64 ?  1140 ALA B CA   1 
ATOM   15392 C C    . ALA B 1 1140 ? 126.660 123.593 72.549  1.00 26.14 ?  1140 ALA B C    1 
ATOM   15393 O O    . ALA B 1 1140 ? 125.935 123.352 73.520  1.00 27.57 ?  1140 ALA B O    1 
ATOM   15394 C CB   . ALA B 1 1140 ? 125.609 121.872 71.066  1.00 20.95 ?  1140 ALA B CB   1 
ATOM   15395 N N    . THR B 1 1141 ? 127.884 124.110 72.673  1.00 25.04 ?  1141 THR B N    1 
ATOM   15396 C CA   . THR B 1 1141 ? 128.394 124.584 73.952  1.00 27.50 ?  1141 THR B CA   1 
ATOM   15397 C C    . THR B 1 1141 ? 127.710 125.862 74.417  1.00 23.75 ?  1141 THR B C    1 
ATOM   15398 O O    . THR B 1 1141 ? 127.909 126.268 75.567  1.00 21.05 ?  1141 THR B O    1 
ATOM   15399 C CB   . THR B 1 1141 ? 129.904 124.813 73.867  1.00 26.61 ?  1141 THR B CB   1 
ATOM   15400 O OG1  . THR B 1 1141 ? 130.178 125.862 72.929  1.00 24.80 ?  1141 THR B OG1  1 
ATOM   15401 C CG2  . THR B 1 1141 ? 130.609 123.542 73.419  1.00 23.03 ?  1141 THR B CG2  1 
ATOM   15402 N N    . LEU B 1 1142 ? 126.928 126.508 73.559  1.00 19.95 ?  1142 LEU B N    1 
ATOM   15403 C CA   . LEU B 1 1142 ? 126.167 127.685 73.945  1.00 23.23 ?  1142 LEU B CA   1 
ATOM   15404 C C    . LEU B 1 1142 ? 124.862 127.287 74.620  1.00 24.95 ?  1142 LEU B C    1 
ATOM   15405 O O    . LEU B 1 1142 ? 124.219 126.304 74.240  1.00 21.62 ?  1142 LEU B O    1 
ATOM   15406 C CB   . LEU B 1 1142 ? 125.886 128.571 72.731  1.00 22.59 ?  1142 LEU B CB   1 
ATOM   15407 C CG   . LEU B 1 1142 ? 125.296 127.935 71.473  1.00 17.62 ?  1142 LEU B CG   1 
ATOM   15408 C CD1  . LEU B 1 1142 ? 123.774 128.017 71.433  1.00 18.87 ?  1142 LEU B CD1  1 
ATOM   15409 C CD2  . LEU B 1 1142 ? 125.911 128.613 70.257  1.00 18.08 ?  1142 LEU B CD2  1 
ATOM   15410 N N    . GLU B 1 1143 ? 124.485 128.057 75.637  1.00 27.16 ?  1143 GLU B N    1 
ATOM   15411 C CA   . GLU B 1 1143 ? 123.192 127.895 76.285  1.00 22.19 ?  1143 GLU B CA   1 
ATOM   15412 C C    . GLU B 1 1143 ? 122.130 128.801 75.681  1.00 23.80 ?  1143 GLU B C    1 
ATOM   15413 O O    . GLU B 1 1143 ? 120.953 128.426 75.647  1.00 27.29 ?  1143 GLU B O    1 
ATOM   15414 C CB   . GLU B 1 1143 ? 123.315 128.173 77.786  1.00 22.04 ?  1143 GLU B CB   1 
ATOM   15415 C CG   . GLU B 1 1143 ? 122.349 127.383 78.659  1.00 23.42 ?  1143 GLU B CG   1 
ATOM   15416 C CD   . GLU B 1 1143 ? 122.977 126.953 79.974  1.00 27.45 ?  1143 GLU B CD   1 
ATOM   15417 O OE1  . GLU B 1 1143 ? 124.199 127.150 80.140  1.00 26.06 ?  1143 GLU B OE1  1 
ATOM   15418 O OE2  . GLU B 1 1143 ? 122.252 126.425 80.844  1.00 27.08 ?  1143 GLU B OE2  1 
ATOM   15419 N N    . ASP B 1 1144 ? 122.522 129.980 75.198  1.00 21.02 ?  1144 ASP B N    1 
ATOM   15420 C CA   . ASP B 1 1144 ? 121.596 130.924 74.591  1.00 21.27 ?  1144 ASP B CA   1 
ATOM   15421 C C    . ASP B 1 1144 ? 122.364 131.850 73.660  1.00 21.84 ?  1144 ASP B C    1 
ATOM   15422 O O    . ASP B 1 1144 ? 123.505 132.228 73.938  1.00 24.96 ?  1144 ASP B O    1 
ATOM   15423 C CB   . ASP B 1 1144 ? 120.853 131.746 75.652  1.00 21.95 ?  1144 ASP B CB   1 
ATOM   15424 C CG   . ASP B 1 1144 ? 119.531 131.125 76.049  1.00 21.56 ?  1144 ASP B CG   1 
ATOM   15425 O OD1  . ASP B 1 1144 ? 118.597 131.136 75.221  1.00 20.27 ?  1144 ASP B OD1  1 
ATOM   15426 O OD2  . ASP B 1 1144 ? 119.429 130.618 77.186  1.00 16.23 ?  1144 ASP B OD2  1 
ATOM   15427 N N    . VAL B 1 1145 ? 121.726 132.208 72.546  1.00 18.01 ?  1145 VAL B N    1 
ATOM   15428 C CA   . VAL B 1 1145 ? 122.257 133.183 71.598  1.00 20.25 ?  1145 VAL B CA   1 
ATOM   15429 C C    . VAL B 1 1145 ? 121.198 134.252 71.355  1.00 19.70 ?  1145 VAL B C    1 
ATOM   15430 O O    . VAL B 1 1145 ? 120.032 133.934 71.087  1.00 21.25 ?  1145 VAL B O    1 
ATOM   15431 C CB   . VAL B 1 1145 ? 122.724 132.530 70.282  1.00 23.02 ?  1145 VAL B CB   1 
ATOM   15432 C CG1  . VAL B 1 1145 ? 123.868 131.593 70.553  1.00 21.78 ?  1145 VAL B CG1  1 
ATOM   15433 C CG2  . VAL B 1 1145 ? 121.611 131.713 69.640  1.00 22.08 ?  1145 VAL B CG2  1 
ATOM   15434 N N    . ILE B 1 1146 ? 121.569 135.539 71.439  1.00 19.23 ?  1146 ILE B N    1 
ATOM   15435 C CA   . ILE B 1 1146 ? 120.602 136.648 71.305  1.00 21.26 ?  1146 ILE B CA   1 
ATOM   15436 C C    . ILE B 1 1146 ? 121.069 137.654 70.294  1.00 19.10 ?  1146 ILE B C    1 
ATOM   15437 O O    . ILE B 1 1146 ? 122.250 137.975 70.239  1.00 14.50 ?  1146 ILE B O    1 
ATOM   15438 C CB   . ILE B 1 1146 ? 120.383 137.398 72.644  1.00 21.82 ?  1146 ILE B CB   1 
ATOM   15439 C CG1  . ILE B 1 1146 ? 120.207 136.429 73.815  1.00 20.93 ?  1146 ILE B CG1  1 
ATOM   15440 C CG2  . ILE B 1 1146 ? 119.179 138.316 72.551  1.00 14.81 ?  1146 ILE B CG2  1 
ATOM   15441 C CD1  . ILE B 1 1146 ? 121.487 136.102 74.549  1.00 18.77 ?  1146 ILE B CD1  1 
ATOM   15442 N N    . LEU B 1 1147 ? 120.148 138.163 69.501  1.00 20.21 ?  1147 LEU B N    1 
ATOM   15443 C CA   . LEU B 1 1147 ? 120.505 139.161 68.512  1.00 22.94 ?  1147 LEU B CA   1 
ATOM   15444 C C    . LEU B 1 1147 ? 120.291 140.601 69.006  1.00 26.37 ?  1147 LEU B C    1 
ATOM   15445 O O    . LEU B 1 1147 ? 119.189 141.123 68.903  1.00 28.22 ?  1147 LEU B O    1 
ATOM   15446 C CB   . LEU B 1 1147 ? 119.700 138.912 67.250  1.00 20.84 ?  1147 LEU B CB   1 
ATOM   15447 C CG   . LEU B 1 1147 ? 119.812 139.944 66.126  1.00 23.34 ?  1147 LEU B CG   1 
ATOM   15448 C CD1  . LEU B 1 1147 ? 121.129 139.790 65.392  1.00 24.23 ?  1147 LEU B CD1  1 
ATOM   15449 C CD2  . LEU B 1 1147 ? 118.655 139.799 65.153  1.00 21.45 ?  1147 LEU B CD2  1 
ATOM   15450 N N    . ILE B 1 1148 ? 121.335 141.272 69.486  1.00 20.58 ?  1148 ILE B N    1 
ATOM   15451 C CA   . ILE B 1 1148 ? 121.175 142.599 70.090  1.00 17.92 ?  1148 ILE B CA   1 
ATOM   15452 C C    . ILE B 1 1148 ? 121.291 143.757 69.134  1.00 20.16 ?  1148 ILE B C    1 
ATOM   15453 O O    . ILE B 1 1148 ? 121.033 144.886 69.509  1.00 24.40 ?  1148 ILE B O    1 
ATOM   15454 C CB   . ILE B 1 1148 ? 122.203 142.826 71.217  1.00 20.74 ?  1148 ILE B CB   1 
ATOM   15455 C CG1  . ILE B 1 1148 ? 123.616 142.937 70.653  1.00 21.84 ?  1148 ILE B CG1  1 
ATOM   15456 C CG2  . ILE B 1 1148 ? 122.132 141.710 72.246  1.00 18.21 ?  1148 ILE B CG2  1 
ATOM   15457 C CD1  . ILE B 1 1148 ? 124.684 142.931 71.723  1.00 20.17 ?  1148 ILE B CD1  1 
ATOM   15458 N N    . ASN B 1 1149 ? 121.659 143.489 67.893  1.00 21.78 ?  1149 ASN B N    1 
ATOM   15459 C CA   . ASN B 1 1149 ? 121.756 144.549 66.890  1.00 21.65 ?  1149 ASN B CA   1 
ATOM   15460 C C    . ASN B 1 1149 ? 121.696 144.029 65.458  1.00 23.51 ?  1149 ASN B C    1 
ATOM   15461 O O    . ASN B 1 1149 ? 121.876 142.840 65.227  1.00 21.71 ?  1149 ASN B O    1 
ATOM   15462 C CB   . ASN B 1 1149 ? 123.052 145.325 67.097  1.00 23.38 ?  1149 ASN B CB   1 
ATOM   15463 C CG   . ASN B 1 1149 ? 122.995 146.718 66.503  1.00 24.60 ?  1149 ASN B CG   1 
ATOM   15464 O OD1  . ASN B 1 1149 ? 121.975 147.127 65.947  1.00 21.87 ?  1149 ASN B OD1  1 
ATOM   15465 N ND2  . ASN B 1 1149 ? 124.090 147.459 66.626  1.00 21.84 ?  1149 ASN B ND2  1 
ATOM   15466 N N    . GLY B 1 1150 ? 121.423 144.903 64.495  1.00 28.09 ?  1150 GLY B N    1 
ATOM   15467 C CA   . GLY B 1 1150 ? 121.413 144.514 63.086  1.00 27.51 ?  1150 GLY B CA   1 
ATOM   15468 C C    . GLY B 1 1150 ? 120.377 143.540 62.565  1.00 25.96 ?  1150 GLY B C    1 
ATOM   15469 O O    . GLY B 1 1150 ? 119.393 143.255 63.245  1.00 24.66 ?  1150 GLY B O    1 
ATOM   15470 N N    . THR B 1 1151 ? 120.577 143.040 61.347  1.00 25.64 ?  1151 THR B N    1 
ATOM   15471 C CA   . THR B 1 1151 ? 119.680 142.036 60.775  1.00 26.36 ?  1151 THR B CA   1 
ATOM   15472 C C    . THR B 1 1151 ? 120.453 140.755 60.494  1.00 29.07 ?  1151 THR B C    1 
ATOM   15473 O O    . THR B 1 1151 ? 121.392 140.769 59.701  1.00 31.31 ?  1151 THR B O    1 
ATOM   15474 C CB   . THR B 1 1151 ? 119.087 142.510 59.451  1.00 28.86 ?  1151 THR B CB   1 
ATOM   15475 O OG1  . THR B 1 1151 ? 118.326 143.703 59.666  1.00 32.83 ?  1151 THR B OG1  1 
ATOM   15476 C CG2  . THR B 1 1151 ? 118.187 141.432 58.863  1.00 24.65 ?  1151 THR B CG2  1 
ATOM   15477 N N    . ALA B 1 1152 ? 120.078 139.646 61.121  1.00 22.08 ?  1152 ALA B N    1 
ATOM   15478 C CA   . ALA B 1 1152 ? 120.847 138.413 60.952  1.00 18.51 ?  1152 ALA B CA   1 
ATOM   15479 C C    . ALA B 1 1152 ? 120.788 137.841 59.541  1.00 24.52 ?  1152 ALA B C    1 
ATOM   15480 O O    . ALA B 1 1152 ? 119.848 138.114 58.792  1.00 23.10 ?  1152 ALA B O    1 
ATOM   15481 C CB   . ALA B 1 1152 ? 120.367 137.362 61.933  1.00 21.13 ?  1152 ALA B CB   1 
ATOM   15482 N N    . TYR B 1 1153 ? 121.759 137.003 59.180  1.00 27.94 ?  1153 TYR B N    1 
ATOM   15483 C CA   . TYR B 1 1153 ? 121.724 136.306 57.882  1.00 24.79 ?  1153 TYR B CA   1 
ATOM   15484 C C    . TYR B 1 1153 ? 122.437 134.963 58.015  1.00 22.96 ?  1153 TYR B C    1 
ATOM   15485 O O    . TYR B 1 1153 ? 123.657 134.882 57.868  1.00 18.09 ?  1153 TYR B O    1 
ATOM   15486 C CB   . TYR B 1 1153 ? 122.304 137.158 56.758  1.00 23.07 ?  1153 TYR B CB   1 
ATOM   15487 C CG   . TYR B 1 1153 ? 121.251 138.044 56.146  1.00 20.65 ?  1153 TYR B CG   1 
ATOM   15488 C CD1  . TYR B 1 1153 ? 120.231 137.501 55.383  1.00 21.18 ?  1153 TYR B CD1  1 
ATOM   15489 C CD2  . TYR B 1 1153 ? 121.256 139.414 56.353  1.00 22.55 ?  1153 TYR B CD2  1 
ATOM   15490 C CE1  . TYR B 1 1153 ? 119.252 138.296 54.825  1.00 25.80 ?  1153 TYR B CE1  1 
ATOM   15491 C CE2  . TYR B 1 1153 ? 120.281 140.219 55.798  1.00 24.84 ?  1153 TYR B CE2  1 
ATOM   15492 C CZ   . TYR B 1 1153 ? 119.283 139.653 55.035  1.00 26.06 ?  1153 TYR B CZ   1 
ATOM   15493 O OH   . TYR B 1 1153 ? 118.308 140.445 54.479  1.00 18.71 ?  1153 TYR B OH   1 
ATOM   15494 N N    . ASN B 1 1154 ? 121.675 133.916 58.322  1.00 25.10 ?  1154 ASN B N    1 
ATOM   15495 C CA   . ASN B 1 1154 ? 122.258 132.587 58.508  1.00 24.51 ?  1154 ASN B CA   1 
ATOM   15496 C C    . ASN B 1 1154 ? 122.811 132.066 57.192  1.00 25.80 ?  1154 ASN B C    1 
ATOM   15497 O O    . ASN B 1 1154 ? 122.520 132.613 56.133  1.00 29.24 ?  1154 ASN B O    1 
ATOM   15498 C CB   . ASN B 1 1154 ? 121.211 131.620 59.065  1.00 23.44 ?  1154 ASN B CB   1 
ATOM   15499 C CG   . ASN B 1 1154 ? 121.779 130.249 59.363  1.00 25.93 ?  1154 ASN B CG   1 
ATOM   15500 O OD1  . ASN B 1 1154 ? 122.949 130.114 59.697  1.00 25.57 ?  1154 ASN B OD1  1 
ATOM   15501 N ND2  . ASN B 1 1154 ? 120.944 129.223 59.256  1.00 26.75 ?  1154 ASN B ND2  1 
ATOM   15502 N N    . ALA B 1 1155 ? 123.618 131.014 57.251  1.00 25.91 ?  1155 ALA B N    1 
ATOM   15503 C CA   . ALA B 1 1155 ? 124.225 130.479 56.031  1.00 28.03 ?  1155 ALA B CA   1 
ATOM   15504 C C    . ALA B 1 1155 ? 123.276 129.549 55.260  1.00 28.55 ?  1155 ALA B C    1 
ATOM   15505 O O    . ALA B 1 1155 ? 123.651 129.000 54.227  1.00 28.67 ?  1155 ALA B O    1 
ATOM   15506 C CB   . ALA B 1 1155 ? 125.551 129.790 56.348  1.00 25.57 ?  1155 ALA B CB   1 
ATOM   15507 N N    . HIS B 1 1156 ? 122.059 129.362 55.761  1.00 28.08 ?  1156 HIS B N    1 
ATOM   15508 C CA   . HIS B 1 1156 ? 121.074 128.563 55.049  1.00 26.56 ?  1156 HIS B CA   1 
ATOM   15509 C C    . HIS B 1 1156 ? 119.968 129.502 54.661  1.00 29.46 ?  1156 HIS B C    1 
ATOM   15510 O O    . HIS B 1 1156 ? 119.329 130.093 55.528  1.00 27.44 ?  1156 HIS B O    1 
ATOM   15511 C CB   . HIS B 1 1156 ? 120.496 127.457 55.920  1.00 24.23 ?  1156 HIS B CB   1 
ATOM   15512 C CG   . HIS B 1 1156 ? 121.499 126.436 56.359  1.00 28.65 ?  1156 HIS B CG   1 
ATOM   15513 N ND1  . HIS B 1 1156 ? 122.678 126.771 56.988  1.00 32.74 ?  1156 HIS B ND1  1 
ATOM   15514 C CD2  . HIS B 1 1156 ? 121.485 125.084 56.281  1.00 29.67 ?  1156 HIS B CD2  1 
ATOM   15515 C CE1  . HIS B 1 1156 ? 123.355 125.671 57.265  1.00 32.99 ?  1156 HIS B CE1  1 
ATOM   15516 N NE2  . HIS B 1 1156 ? 122.651 124.634 56.848  1.00 31.66 ?  1156 HIS B NE2  1 
ATOM   15517 N N    . THR B 1 1157 ? 119.747 129.671 53.364  1.00 27.41 ?  1157 THR B N    1 
ATOM   15518 C CA   . THR B 1 1157 ? 118.667 130.522 52.903  1.00 24.81 ?  1157 THR B CA   1 
ATOM   15519 C C    . THR B 1 1157 ? 118.797 131.903 53.515  1.00 26.43 ?  1157 THR B C    1 
ATOM   15520 O O    . THR B 1 1157 ? 117.813 132.634 53.613  1.00 27.21 ?  1157 THR B O    1 
ATOM   15521 C CB   . THR B 1 1157 ? 117.280 129.946 53.264  1.00 26.69 ?  1157 THR B CB   1 
ATOM   15522 O OG1  . THR B 1 1157 ? 117.010 130.154 54.656  1.00 24.28 ?  1157 THR B OG1  1 
ATOM   15523 C CG2  . THR B 1 1157 ? 117.219 128.459 52.952  1.00 25.23 ?  1157 THR B CG2  1 
ATOM   15524 N N    . ARG B 1 1158 ? 120.018 132.258 53.898  1.00 28.18 ?  1158 ARG B N    1 
ATOM   15525 C CA   . ARG B 1 1158 ? 120.260 133.573 54.470  1.00 28.66 ?  1158 ARG B CA   1 
ATOM   15526 C C    . ARG B 1 1158 ? 119.249 133.927 55.536  1.00 28.87 ?  1158 ARG B C    1 
ATOM   15527 O O    . ARG B 1 1158 ? 118.669 135.011 55.505  1.00 28.19 ?  1158 ARG B O    1 
ATOM   15528 C CB   . ARG B 1 1158 ? 120.221 134.636 53.379  1.00 27.10 ?  1158 ARG B CB   1 
ATOM   15529 C CG   . ARG B 1 1158 ? 121.377 134.587 52.400  1.00 28.11 ?  1158 ARG B CG   1 
ATOM   15530 C CD   . ARG B 1 1158 ? 121.583 135.960 51.787  1.00 29.24 ?  1158 ARG B CD   1 
ATOM   15531 N NE   . ARG B 1 1158 ? 122.000 136.932 52.794  1.00 31.68 ?  1158 ARG B NE   1 
ATOM   15532 C CZ   . ARG B 1 1158 ? 122.116 138.236 52.573  1.00 32.22 ?  1158 ARG B CZ   1 
ATOM   15533 N NH1  . ARG B 1 1158 ? 121.833 138.735 51.378  1.00 28.85 ?  1158 ARG B NH1  1 
ATOM   15534 N NH2  . ARG B 1 1158 ? 122.509 139.044 53.548  1.00 28.43 ?  1158 ARG B NH2  1 
ATOM   15535 N N    . GLU B 1 1159 ? 119.042 133.034 56.492  1.00 28.47 ?  1159 GLU B N    1 
ATOM   15536 C CA   . GLU B 1 1159 ? 118.015 133.288 57.486  1.00 29.30 ?  1159 GLU B CA   1 
ATOM   15537 C C    . GLU B 1 1159 ? 118.109 134.728 57.949  1.00 28.75 ?  1159 GLU B C    1 
ATOM   15538 O O    . GLU B 1 1159 ? 119.142 135.156 58.449  1.00 26.36 ?  1159 GLU B O    1 
ATOM   15539 C CB   . GLU B 1 1159 ? 118.148 132.322 58.654  1.00 25.14 ?  1159 GLU B CB   1 
ATOM   15540 C CG   . GLU B 1 1159 ? 116.988 132.381 59.628  1.00 25.77 ?  1159 GLU B CG   1 
ATOM   15541 C CD   . GLU B 1 1159 ? 115.658 132.108 58.959  1.00 29.69 ?  1159 GLU B CD   1 
ATOM   15542 O OE1  . GLU B 1 1159 ? 115.057 133.059 58.418  1.00 30.65 ?  1159 GLU B OE1  1 
ATOM   15543 O OE2  . GLU B 1 1159 ? 115.213 130.943 58.976  1.00 30.07 ?  1159 GLU B OE2  1 
ATOM   15544 N N    . GLU B 1 1160 ? 117.031 135.481 57.773  1.00 26.89 ?  1160 GLU B N    1 
ATOM   15545 C CA   . GLU B 1 1160 ? 117.014 136.881 58.176  1.00 27.67 ?  1160 GLU B CA   1 
ATOM   15546 C C    . GLU B 1 1160 ? 116.133 137.116 59.391  1.00 28.83 ?  1160 GLU B C    1 
ATOM   15547 O O    . GLU B 1 1160 ? 114.953 136.766 59.382  1.00 28.60 ?  1160 GLU B O    1 
ATOM   15548 C CB   . GLU B 1 1160 ? 116.508 137.744 57.030  1.00 25.58 ?  1160 GLU B CB   1 
ATOM   15549 C CG   . GLU B 1 1160 ? 116.243 139.183 57.424  1.00 26.14 ?  1160 GLU B CG   1 
ATOM   15550 C CD   . GLU B 1 1160 ? 115.810 140.030 56.249  1.00 26.96 ?  1160 GLU B CD   1 
ATOM   15551 O OE1  . GLU B 1 1160 ? 115.583 139.464 55.160  1.00 27.04 ?  1160 GLU B OE1  1 
ATOM   15552 O OE2  . GLU B 1 1160 ? 115.698 141.262 56.413  1.00 26.34 ?  1160 GLU B OE2  1 
ATOM   15553 N N    . ILE B 1 1161 ? 116.699 137.706 60.440  1.00 26.68 ?  1161 ILE B N    1 
ATOM   15554 C CA   . ILE B 1 1161 ? 115.930 138.008 61.642  1.00 26.49 ?  1161 ILE B CA   1 
ATOM   15555 C C    . ILE B 1 1161 ? 116.246 139.443 62.052  1.00 26.25 ?  1161 ILE B C    1 
ATOM   15556 O O    . ILE B 1 1161 ? 117.294 139.970 61.686  1.00 26.49 ?  1161 ILE B O    1 
ATOM   15557 C CB   . ILE B 1 1161 ? 116.240 137.021 62.784  1.00 27.23 ?  1161 ILE B CB   1 
ATOM   15558 C CG1  . ILE B 1 1161 ? 116.354 135.591 62.251  1.00 23.84 ?  1161 ILE B CG1  1 
ATOM   15559 C CG2  . ILE B 1 1161 ? 115.178 137.101 63.869  1.00 27.28 ?  1161 ILE B CG2  1 
ATOM   15560 C CD1  . ILE B 1 1161 ? 117.731 135.232 61.737  1.00 21.94 ?  1161 ILE B CD1  1 
ATOM   15561 N N    . ARG B 1 1162 ? 115.354 140.069 62.811  1.00 25.52 ?  1162 ARG B N    1 
ATOM   15562 C CA   . ARG B 1 1162 ? 115.566 141.455 63.216  1.00 25.45 ?  1162 ARG B CA   1 
ATOM   15563 C C    . ARG B 1 1162 ? 115.825 141.579 64.711  1.00 26.13 ?  1162 ARG B C    1 
ATOM   15564 O O    . ARG B 1 1162 ? 115.329 140.776 65.499  1.00 26.71 ?  1162 ARG B O    1 
ATOM   15565 C CB   . ARG B 1 1162 ? 114.365 142.316 62.821  1.00 24.89 ?  1162 ARG B CB   1 
ATOM   15566 C CG   . ARG B 1 1162 ? 114.661 143.804 62.809  1.00 27.84 ?  1162 ARG B CG   1 
ATOM   15567 C CD   . ARG B 1 1162 ? 115.899 144.094 61.976  1.00 27.32 ?  1162 ARG B CD   1 
ATOM   15568 N NE   . ARG B 1 1162 ? 115.859 143.404 60.690  1.00 28.96 ?  1162 ARG B NE   1 
ATOM   15569 C CZ   . ARG B 1 1162 ? 115.309 143.903 59.589  1.00 30.79 ?  1162 ARG B CZ   1 
ATOM   15570 N NH1  . ARG B 1 1162 ? 114.749 145.105 59.611  1.00 28.91 ?  1162 ARG B NH1  1 
ATOM   15571 N NH2  . ARG B 1 1162 ? 115.320 143.201 58.465  1.00 25.64 ?  1162 ARG B NH2  1 
ATOM   15572 N N    . SER B 1 1163 ? 116.599 142.585 65.102  1.00 23.91 ?  1163 SER B N    1 
ATOM   15573 C CA   . SER B 1 1163 ? 116.924 142.778 66.513  1.00 23.96 ?  1163 SER B CA   1 
ATOM   15574 C C    . SER B 1 1163 ? 115.814 143.504 67.263  1.00 25.25 ?  1163 SER B C    1 
ATOM   15575 O O    . SER B 1 1163 ? 114.846 143.964 66.658  1.00 21.28 ?  1163 SER B O    1 
ATOM   15576 C CB   . SER B 1 1163 ? 118.233 143.552 66.647  1.00 20.77 ?  1163 SER B CB   1 
ATOM   15577 O OG   . SER B 1 1163 ? 119.273 142.875 65.973  1.00 22.12 ?  1163 SER B OG   1 
ATOM   15578 N N    . PRO B 1 1164 ? 115.956 143.606 68.592  1.00 26.32 ?  1164 PRO B N    1 
ATOM   15579 C CA   . PRO B 1 1164 ? 116.528 142.526 69.402  1.00 22.73 ?  1164 PRO B CA   1 
ATOM   15580 C C    . PRO B 1 1164 ? 115.630 141.301 69.393  1.00 20.91 ?  1164 PRO B C    1 
ATOM   15581 O O    . PRO B 1 1164 ? 114.423 141.429 69.596  1.00 21.50 ?  1164 PRO B O    1 
ATOM   15582 C CB   . PRO B 1 1164 ? 116.588 143.132 70.807  1.00 23.37 ?  1164 PRO B CB   1 
ATOM   15583 C CG   . PRO B 1 1164 ? 115.555 144.206 70.803  1.00 23.17 ?  1164 PRO B CG   1 
ATOM   15584 C CD   . PRO B 1 1164 ? 115.565 144.765 69.411  1.00 24.92 ?  1164 PRO B CD   1 
ATOM   15585 N N    . CYS B 1 1165 ? 116.207 140.129 69.157  1.00 25.32 ?  1165 CYS B N    1 
ATOM   15586 C CA   . CYS B 1 1165 ? 115.411 138.909 69.094  1.00 28.73 ?  1165 CYS B CA   1 
ATOM   15587 C C    . CYS B 1 1165 ? 116.189 137.690 69.550  1.00 26.19 ?  1165 CYS B C    1 
ATOM   15588 O O    . CYS B 1 1165 ? 117.380 137.563 69.266  1.00 24.33 ?  1165 CYS B O    1 
ATOM   15589 C CB   . CYS B 1 1165 ? 114.902 138.682 67.670  1.00 25.93 ?  1165 CYS B CB   1 
ATOM   15590 S SG   . CYS B 1 1165 ? 114.048 137.106 67.432  1.00 28.63 ?  1165 CYS B SG   1 
ATOM   15591 N N    . LEU B 1 1166 ? 115.518 136.788 70.257  1.00 20.33 ?  1166 LEU B N    1 
ATOM   15592 C CA   . LEU B 1 1166 ? 116.170 135.559 70.686  1.00 18.42 ?  1166 LEU B CA   1 
ATOM   15593 C C    . LEU B 1 1166 ? 116.168 134.588 69.522  1.00 24.72 ?  1166 LEU B C    1 
ATOM   15594 O O    . LEU B 1 1166 ? 115.105 134.215 69.027  1.00 24.63 ?  1166 LEU B O    1 
ATOM   15595 C CB   . LEU B 1 1166 ? 115.461 134.958 71.896  1.00 19.37 ?  1166 LEU B CB   1 
ATOM   15596 C CG   . LEU B 1 1166 ? 116.178 133.786 72.568  1.00 24.79 ?  1166 LEU B CG   1 
ATOM   15597 C CD1  . LEU B 1 1166 ? 117.580 134.196 72.991  1.00 20.61 ?  1166 LEU B CD1  1 
ATOM   15598 C CD2  . LEU B 1 1166 ? 115.383 133.288 73.764  1.00 22.72 ?  1166 LEU B CD2  1 
ATOM   15599 N N    . ILE B 1 1167 ? 117.347 134.175 69.077  1.00 23.84 ?  1167 ILE B N    1 
ATOM   15600 C CA   . ILE B 1 1167 ? 117.439 133.304 67.909  1.00 21.50 ?  1167 ILE B CA   1 
ATOM   15601 C C    . ILE B 1 1167 ? 116.691 132.003 68.170  1.00 21.25 ?  1167 ILE B C    1 
ATOM   15602 O O    . ILE B 1 1167 ? 116.741 131.444 69.275  1.00 16.28 ?  1167 ILE B O    1 
ATOM   15603 C CB   . ILE B 1 1167 ? 118.911 133.043 67.545  1.00 19.89 ?  1167 ILE B CB   1 
ATOM   15604 C CG1  . ILE B 1 1167 ? 119.676 134.366 67.482  1.00 20.20 ?  1167 ILE B CG1  1 
ATOM   15605 C CG2  . ILE B 1 1167 ? 119.019 132.320 66.208  1.00 20.40 ?  1167 ILE B CG2  1 
ATOM   15606 C CD1  . ILE B 1 1167 ? 121.098 134.247 66.973  1.00 16.53 ?  1167 ILE B CD1  1 
ATOM   15607 N N    . SER B 1 1168 ? 115.965 131.532 67.154  1.00 24.84 ?  1168 SER B N    1 
ATOM   15608 C CA   . SER B 1 1168 ? 115.199 130.301 67.281  1.00 28.62 ?  1168 SER B CA   1 
ATOM   15609 C C    . SER B 1 1168 ? 116.129 129.123 67.541  1.00 29.88 ?  1168 SER B C    1 
ATOM   15610 O O    . SER B 1 1168 ? 117.281 129.100 67.101  1.00 28.39 ?  1168 SER B O    1 
ATOM   15611 C CB   . SER B 1 1168 ? 114.369 130.050 66.021  1.00 22.20 ?  1168 SER B CB   1 
ATOM   15612 O OG   . SER B 1 1168 ? 113.446 131.101 65.796  1.00 21.97 ?  1168 SER B OG   1 
ATOM   15613 N N    . ARG B 1 1169 ? 115.694 128.179 68.368  1.00 23.79 ?  1169 ARG B N    1 
ATOM   15614 C CA   . ARG B 1 1169 ? 116.590 127.090 68.745  1.00 22.82 ?  1169 ARG B CA   1 
ATOM   15615 C C    . ARG B 1 1169 ? 117.111 126.284 67.551  1.00 26.64 ?  1169 ARG B C    1 
ATOM   15616 O O    . ARG B 1 1169 ? 118.214 125.742 67.614  1.00 24.92 ?  1169 ARG B O    1 
ATOM   15617 C CB   . ARG B 1 1169 ? 115.896 126.171 69.749  1.00 21.53 ?  1169 ARG B CB   1 
ATOM   15618 C CG   . ARG B 1 1169 ? 116.845 125.344 70.591  1.00 23.44 ?  1169 ARG B CG   1 
ATOM   15619 C CD   . ARG B 1 1169 ? 117.275 126.113 71.825  1.00 24.53 ?  1169 ARG B CD   1 
ATOM   15620 N NE   . ARG B 1 1169 ? 118.365 125.449 72.530  1.00 26.32 ?  1169 ARG B NE   1 
ATOM   15621 C CZ   . ARG B 1 1169 ? 118.767 125.770 73.754  1.00 26.03 ?  1169 ARG B CZ   1 
ATOM   15622 N NH1  . ARG B 1 1169 ? 118.155 126.740 74.418  1.00 25.75 ?  1169 ARG B NH1  1 
ATOM   15623 N NH2  . ARG B 1 1169 ? 119.770 125.113 74.317  1.00 24.26 ?  1169 ARG B NH2  1 
ATOM   15624 N N    . THR B 1 1170 ? 116.355 126.218 66.461  1.00 24.80 ?  1170 THR B N    1 
ATOM   15625 C CA   . THR B 1 1170 ? 116.746 125.406 65.309  1.00 25.81 ?  1170 THR B CA   1 
ATOM   15626 C C    . THR B 1 1170 ? 117.366 126.325 64.259  1.00 26.93 ?  1170 THR B C    1 
ATOM   15627 O O    . THR B 1 1170 ? 116.671 126.833 63.376  1.00 26.77 ?  1170 THR B O    1 
ATOM   15628 C CB   . THR B 1 1170 ? 115.542 124.647 64.740  1.00 25.48 ?  1170 THR B CB   1 
ATOM   15629 O OG1  . THR B 1 1170 ? 114.785 124.069 65.812  1.00 24.41 ?  1170 THR B OG1  1 
ATOM   15630 C CG2  . THR B 1 1170 ? 116.000 123.545 63.796  1.00 24.31 ?  1170 THR B CG2  1 
ATOM   15631 N N    . VAL B 1 1171 ? 118.679 126.536 64.354  1.00 29.70 ?  1171 VAL B N    1 
ATOM   15632 C CA   . VAL B 1 1171 ? 119.434 127.347 63.408  1.00 29.59 ?  1171 VAL B CA   1 
ATOM   15633 C C    . VAL B 1 1171 ? 120.767 126.659 63.135  1.00 28.83 ?  1171 VAL B C    1 
ATOM   15634 O O    . VAL B 1 1171 ? 121.063 125.592 63.678  1.00 30.61 ?  1171 VAL B O    1 
ATOM   15635 C CB   . VAL B 1 1171 ? 119.663 128.786 63.915  1.00 27.16 ?  1171 VAL B CB   1 
ATOM   15636 C CG1  . VAL B 1 1171 ? 118.423 129.639 63.686  1.00 27.39 ?  1171 VAL B CG1  1 
ATOM   15637 C CG2  . VAL B 1 1171 ? 120.061 128.774 65.383  1.00 25.61 ?  1171 VAL B CG2  1 
ATOM   15638 N N    . HIS B 1 1172 ? 121.576 127.281 62.284  1.00 25.49 ?  1172 HIS B N    1 
ATOM   15639 C CA   . HIS B 1 1172 ? 122.885 126.746 61.919  1.00 25.44 ?  1172 HIS B CA   1 
ATOM   15640 C C    . HIS B 1 1172 ? 123.874 127.908 61.896  1.00 26.38 ?  1172 HIS B C    1 
ATOM   15641 O O    . HIS B 1 1172 ? 123.576 129.013 62.363  1.00 28.40 ?  1172 HIS B O    1 
ATOM   15642 C CB   . HIS B 1 1172 ? 122.801 125.980 60.590  1.00 27.62 ?  1172 HIS B CB   1 
ATOM   15643 C CG   . HIS B 1 1172 ? 121.860 124.816 60.627  1.00 30.00 ?  1172 HIS B CG   1 
ATOM   15644 N ND1  . HIS B 1 1172 ? 121.771 123.966 61.709  1.00 31.55 ?  1172 HIS B ND1  1 
ATOM   15645 C CD2  . HIS B 1 1172 ? 120.962 124.364 59.720  1.00 27.36 ?  1172 HIS B CD2  1 
ATOM   15646 C CE1  . HIS B 1 1172 ? 120.860 123.041 61.466  1.00 28.30 ?  1172 HIS B CE1  1 
ATOM   15647 N NE2  . HIS B 1 1172 ? 120.355 123.258 60.265  1.00 29.20 ?  1172 HIS B NE2  1 
ATOM   15648 N N    . LYS B 1 1173 ? 125.076 127.656 61.375  1.00 28.87 ?  1173 LYS B N    1 
ATOM   15649 C CA   . LYS B 1 1173 ? 126.149 128.644 61.409  1.00 29.36 ?  1173 LYS B CA   1 
ATOM   15650 C C    . LYS B 1 1173 ? 125.819 129.822 60.502  1.00 27.64 ?  1173 LYS B C    1 
ATOM   15651 O O    . LYS B 1 1173 ? 125.429 129.637 59.346  1.00 26.47 ?  1173 LYS B O    1 
ATOM   15652 C CB   . LYS B 1 1173 ? 127.476 128.009 60.993  1.00 26.35 ?  1173 LYS B CB   1 
ATOM   15653 C CG   . LYS B 1 1173 ? 127.753 126.662 61.642  1.00 24.64 ?  1173 LYS B CG   1 
ATOM   15654 C CD   . LYS B 1 1173 ? 129.091 126.092 61.199  1.00 29.24 ?  1173 LYS B CD   1 
ATOM   15655 C CE   . LYS B 1 1173 ? 129.372 124.759 61.877  1.00 28.84 ?  1173 LYS B CE   1 
ATOM   15656 N NZ   . LYS B 1 1173 ? 130.605 124.110 61.351  1.00 31.31 ?  1173 LYS B NZ   1 
ATOM   15657 N N    . LEU B 1 1174 ? 125.989 131.033 61.027  1.00 24.90 ?  1174 LEU B N    1 
ATOM   15658 C CA   . LEU B 1 1174 ? 125.568 132.250 60.353  1.00 27.12 ?  1174 LEU B CA   1 
ATOM   15659 C C    . LEU B 1 1174 ? 126.763 133.151 60.072  1.00 25.21 ?  1174 LEU B C    1 
ATOM   15660 O O    . LEU B 1 1174 ? 127.741 133.174 60.827  1.00 21.87 ?  1174 LEU B O    1 
ATOM   15661 C CB   . LEU B 1 1174 ? 124.514 133.007 61.185  1.00 25.97 ?  1174 LEU B CB   1 
ATOM   15662 C CG   . LEU B 1 1174 ? 124.938 133.989 62.282  1.00 26.25 ?  1174 LEU B CG   1 
ATOM   15663 C CD1  . LEU B 1 1174 ? 123.743 134.812 62.738  1.00 25.04 ?  1174 LEU B CD1  1 
ATOM   15664 C CD2  . LEU B 1 1174 ? 125.562 133.264 63.465  1.00 22.64 ?  1174 LEU B CD2  1 
ATOM   15665 N N    . THR B 1 1175 ? 126.677 133.882 58.967  1.00 25.87 ?  1175 THR B N    1 
ATOM   15666 C CA   . THR B 1 1175 ? 127.688 134.839 58.543  1.00 24.21 ?  1175 THR B CA   1 
ATOM   15667 C C    . THR B 1 1175 ? 127.084 136.241 58.538  1.00 23.71 ?  1175 THR B C    1 
ATOM   15668 O O    . THR B 1 1175 ? 125.925 136.443 58.905  1.00 28.40 ?  1175 THR B O    1 
ATOM   15669 C CB   . THR B 1 1175 ? 128.246 134.475 57.163  1.00 25.48 ?  1175 THR B CB   1 
ATOM   15670 O OG1  . THR B 1 1175 ? 129.272 135.407 56.798  1.00 23.20 ?  1175 THR B OG1  1 
ATOM   15671 C CG2  . THR B 1 1175 ? 127.144 134.501 56.115  1.00 21.25 ?  1175 THR B CG2  1 
ATOM   15672 N N    . PHE B 1 1176 ? 127.885 137.220 58.124  1.00 23.30 ?  1176 PHE B N    1 
ATOM   15673 C CA   . PHE B 1 1176 ? 127.433 138.604 58.111  1.00 23.15 ?  1176 PHE B CA   1 
ATOM   15674 C C    . PHE B 1 1176 ? 128.118 139.360 56.984  1.00 24.73 ?  1176 PHE B C    1 
ATOM   15675 O O    . PHE B 1 1176 ? 129.187 138.974 56.505  1.00 23.85 ?  1176 PHE B O    1 
ATOM   15676 C CB   . PHE B 1 1176 ? 127.694 139.293 59.456  1.00 23.19 ?  1176 PHE B CB   1 
ATOM   15677 C CG   . PHE B 1 1176 ? 126.701 138.930 60.519  1.00 23.29 ?  1176 PHE B CG   1 
ATOM   15678 C CD1  . PHE B 1 1176 ? 125.402 139.403 60.456  1.00 23.51 ?  1176 PHE B CD1  1 
ATOM   15679 C CD2  . PHE B 1 1176 ? 127.059 138.100 61.568  1.00 20.53 ?  1176 PHE B CD2  1 
ATOM   15680 C CE1  . PHE B 1 1176 ? 124.481 139.068 61.426  1.00 21.94 ?  1176 PHE B CE1  1 
ATOM   15681 C CE2  . PHE B 1 1176 ? 126.141 137.761 62.542  1.00 21.36 ?  1176 PHE B CE2  1 
ATOM   15682 C CZ   . PHE B 1 1176 ? 124.851 138.245 62.468  1.00 23.80 ?  1176 PHE B CZ   1 
ATOM   15683 N N    . GLN B 1 1177 ? 127.481 140.450 56.568  1.00 26.94 ?  1177 GLN B N    1 
ATOM   15684 C CA   . GLN B 1 1177 ? 127.990 141.325 55.523  1.00 28.88 ?  1177 GLN B CA   1 
ATOM   15685 C C    . GLN B 1 1177 ? 128.335 142.684 56.116  1.00 29.81 ?  1177 GLN B C    1 
ATOM   15686 O O    . GLN B 1 1177 ? 127.570 143.237 56.912  1.00 27.41 ?  1177 GLN B O    1 
ATOM   15687 C CB   . GLN B 1 1177 ? 126.967 141.489 54.395  1.00 26.48 ?  1177 GLN B CB   1 
ATOM   15688 C CG   . GLN B 1 1177 ? 127.509 142.182 53.154  1.00 26.88 ?  1177 GLN B CG   1 
ATOM   15689 C CD   . GLN B 1 1177 ? 128.677 141.442 52.532  1.00 29.69 ?  1177 GLN B CD   1 
ATOM   15690 O OE1  . GLN B 1 1177 ? 129.837 141.781 52.767  1.00 30.54 ?  1177 GLN B OE1  1 
ATOM   15691 N NE2  . GLN B 1 1177 ? 128.376 140.425 51.733  1.00 29.10 ?  1177 GLN B NE2  1 
ATOM   15692 N N    . TYR B 1 1178 ? 129.492 143.215 55.727  1.00 31.02 ?  1178 TYR B N    1 
ATOM   15693 C CA   . TYR B 1 1178 ? 129.961 144.504 56.231  1.00 31.22 ?  1178 TYR B CA   1 
ATOM   15694 C C    . TYR B 1 1178 ? 129.103 145.614 55.638  1.00 30.41 ?  1178 TYR B C    1 
ATOM   15695 O O    . TYR B 1 1178 ? 129.257 145.982 54.471  1.00 29.32 ?  1178 TYR B O    1 
ATOM   15696 C CB   . TYR B 1 1178 ? 131.433 144.704 55.889  1.00 30.03 ?  1178 TYR B CB   1 
ATOM   15697 C CG   . TYR B 1 1178 ? 131.981 146.055 56.296  1.00 33.18 ?  1178 TYR B CG   1 
ATOM   15698 C CD1  . TYR B 1 1178 ? 132.294 146.329 57.621  1.00 32.24 ?  1178 TYR B CD1  1 
ATOM   15699 C CD2  . TYR B 1 1178 ? 132.191 147.055 55.353  1.00 30.70 ?  1178 TYR B CD2  1 
ATOM   15700 C CE1  . TYR B 1 1178 ? 132.796 147.561 57.998  1.00 30.68 ?  1178 TYR B CE1  1 
ATOM   15701 C CE2  . TYR B 1 1178 ? 132.693 148.291 55.721  1.00 32.04 ?  1178 TYR B CE2  1 
ATOM   15702 C CZ   . TYR B 1 1178 ? 132.993 148.537 57.044  1.00 32.48 ?  1178 TYR B CZ   1 
ATOM   15703 O OH   . TYR B 1 1178 ? 133.493 149.765 57.415  1.00 34.56 ?  1178 TYR B OH   1 
ATOM   15704 N N    . THR B 1 1179 ? 128.192 146.151 56.443  1.00 29.70 ?  1179 THR B N    1 
ATOM   15705 C CA   . THR B 1 1179 ? 127.351 147.273 56.053  1.00 34.52 ?  1179 THR B CA   1 
ATOM   15706 C C    . THR B 1 1179 ? 127.729 148.485 56.891  1.00 33.02 ?  1179 THR B C    1 
ATOM   15707 O O    . THR B 1 1179 ? 127.738 148.413 58.124  1.00 32.57 ?  1179 THR B O    1 
ATOM   15708 C CB   . THR B 1 1179 ? 125.866 146.943 56.231  1.00 32.84 ?  1179 THR B CB   1 
ATOM   15709 O OG1  . THR B 1 1179 ? 125.554 146.864 57.628  1.00 29.61 ?  1179 THR B OG1  1 
ATOM   15710 C CG2  . THR B 1 1179 ? 125.532 145.616 55.561  1.00 30.50 ?  1179 THR B CG2  1 
ATOM   15711 N N    . ALA B 1 1180 ? 128.044 149.593 56.219  1.00 26.96 ?  1180 ALA B N    1 
ATOM   15712 C CA   . ALA B 1 1180 ? 128.513 150.780 56.924  1.00 24.85 ?  1180 ALA B CA   1 
ATOM   15713 C C    . ALA B 1 1180 ? 127.398 151.512 57.654  1.00 24.79 ?  1180 ALA B C    1 
ATOM   15714 O O    . ALA B 1 1180 ? 127.682 152.267 58.590  1.00 25.32 ?  1180 ALA B O    1 
ATOM   15715 C CB   . ALA B 1 1180 ? 129.199 151.732 55.945  1.00 21.95 ?  1180 ALA B CB   1 
ATOM   15716 N N    . THR B 1 1181 ? 126.142 151.325 57.239  1.00 28.65 ?  1181 THR B N    1 
ATOM   15717 C CA   . THR B 1 1181 ? 125.043 152.030 57.891  1.00 28.93 ?  1181 THR B CA   1 
ATOM   15718 C C    . THR B 1 1181 ? 124.674 151.415 59.235  1.00 28.34 ?  1181 THR B C    1 
ATOM   15719 O O    . THR B 1 1181 ? 124.346 152.150 60.170  1.00 29.10 ?  1181 THR B O    1 
ATOM   15720 C CB   . THR B 1 1181 ? 123.825 152.113 56.954  1.00 31.08 ?  1181 THR B CB   1 
ATOM   15721 O OG1  . THR B 1 1181 ? 122.849 153.004 57.512  1.00 32.29 ?  1181 THR B OG1  1 
ATOM   15722 C CG2  . THR B 1 1181 ? 123.197 150.740 56.668  1.00 28.37 ?  1181 THR B CG2  1 
ATOM   15723 N N    . GLU B 1 1182 ? 124.754 150.094 59.372  1.00 27.90 ?  1182 GLU B N    1 
ATOM   15724 C CA   . GLU B 1 1182 ? 124.450 149.454 60.646  1.00 30.63 ?  1182 GLU B CA   1 
ATOM   15725 C C    . GLU B 1 1182 ? 125.374 148.263 60.826  1.00 28.30 ?  1182 GLU B C    1 
ATOM   15726 O O    . GLU B 1 1182 ? 125.511 147.442 59.918  1.00 30.11 ?  1182 GLU B O    1 
ATOM   15727 C CB   . GLU B 1 1182 ? 122.983 149.008 60.720  1.00 28.99 ?  1182 GLU B CB   1 
ATOM   15728 C CG   . GLU B 1 1182 ? 121.993 150.148 60.894  1.00 28.16 ?  1182 GLU B CG   1 
ATOM   15729 C CD   . GLU B 1 1182 ? 120.545 149.700 60.894  1.00 31.39 ?  1182 GLU B CD   1 
ATOM   15730 O OE1  . GLU B 1 1182 ? 120.260 148.532 60.558  1.00 31.32 ?  1182 GLU B OE1  1 
ATOM   15731 O OE2  . GLU B 1 1182 ? 119.692 150.498 61.333  1.00 33.30 ?  1182 GLU B OE2  1 
ATOM   15732 N N    . GLU B 1 1183 ? 126.002 148.176 61.992  1.00 25.16 ?  1183 GLU B N    1 
ATOM   15733 C CA   . GLU B 1 1183 ? 126.879 147.058 62.278  1.00 30.06 ?  1183 GLU B CA   1 
ATOM   15734 C C    . GLU B 1 1183 ? 126.249 146.180 63.334  1.00 30.17 ?  1183 GLU B C    1 
ATOM   15735 O O    . GLU B 1 1183 ? 126.219 146.542 64.503  1.00 26.99 ?  1183 GLU B O    1 
ATOM   15736 C CB   . GLU B 1 1183 ? 128.230 147.551 62.771  1.00 27.95 ?  1183 GLU B CB   1 
ATOM   15737 C CG   . GLU B 1 1183 ? 129.197 146.418 63.069  1.00 24.33 ?  1183 GLU B CG   1 
ATOM   15738 C CD   . GLU B 1 1183 ? 130.568 146.909 63.479  1.00 28.89 ?  1183 GLU B CD   1 
ATOM   15739 O OE1  . GLU B 1 1183 ? 130.743 148.136 63.622  1.00 26.46 ?  1183 GLU B OE1  1 
ATOM   15740 O OE2  . GLU B 1 1183 ? 131.470 146.064 63.658  1.00 30.57 ?  1183 GLU B OE2  1 
ATOM   15741 N N    . PRO B 1 1184 ? 125.744 145.017 62.933  1.00 30.09 ?  1184 PRO B N    1 
ATOM   15742 C CA   . PRO B 1 1184 ? 125.055 144.169 63.895  1.00 25.48 ?  1184 PRO B CA   1 
ATOM   15743 C C    . PRO B 1 1184 ? 126.044 143.561 64.837  1.00 23.69 ?  1184 PRO B C    1 
ATOM   15744 O O    . PRO B 1 1184 ? 127.214 143.465 64.484  1.00 23.96 ?  1184 PRO B O    1 
ATOM   15745 C CB   . PRO B 1 1184 ? 124.447 143.084 63.017  1.00 24.77 ?  1184 PRO B CB   1 
ATOM   15746 C CG   . PRO B 1 1184 ? 125.343 143.010 61.831  1.00 26.40 ?  1184 PRO B CG   1 
ATOM   15747 C CD   . PRO B 1 1184 ? 125.797 144.419 61.590  1.00 26.49 ?  1184 PRO B CD   1 
ATOM   15748 N N    . ARG B 1 1185 ? 125.596 143.162 66.018  1.00 25.98 ?  1185 ARG B N    1 
ATOM   15749 C CA   . ARG B 1 1185 ? 126.473 142.507 66.967  1.00 26.47 ?  1185 ARG B CA   1 
ATOM   15750 C C    . ARG B 1 1185 ? 125.628 141.528 67.746  1.00 29.28 ?  1185 ARG B C    1 
ATOM   15751 O O    . ARG B 1 1185 ? 124.422 141.715 67.843  1.00 30.94 ?  1185 ARG B O    1 
ATOM   15752 C CB   . ARG B 1 1185 ? 127.121 143.543 67.869  1.00 23.69 ?  1185 ARG B CB   1 
ATOM   15753 C CG   . ARG B 1 1185 ? 128.403 143.100 68.543  1.00 24.79 ?  1185 ARG B CG   1 
ATOM   15754 C CD   . ARG B 1 1185 ? 128.882 144.198 69.473  1.00 24.97 ?  1185 ARG B CD   1 
ATOM   15755 N NE   . ARG B 1 1185 ? 128.999 145.476 68.779  1.00 26.68 ?  1185 ARG B NE   1 
ATOM   15756 C CZ   . ARG B 1 1185 ? 130.151 146.026 68.412  1.00 23.48 ?  1185 ARG B CZ   1 
ATOM   15757 N NH1  . ARG B 1 1185 ? 131.296 145.418 68.687  1.00 23.88 ?  1185 ARG B NH1  1 
ATOM   15758 N NH2  . ARG B 1 1185 ? 130.159 147.191 67.781  1.00 20.63 ?  1185 ARG B NH2  1 
ATOM   15759 N N    . LEU B 1 1186 ? 126.227 140.473 68.289  1.00 23.62 ?  1186 LEU B N    1 
ATOM   15760 C CA   . LEU B 1 1186 ? 125.425 139.454 68.955  1.00 20.16 ?  1186 LEU B CA   1 
ATOM   15761 C C    . LEU B 1 1186 ? 126.042 138.970 70.227  1.00 22.26 ?  1186 LEU B C    1 
ATOM   15762 O O    . LEU B 1 1186 ? 127.254 139.050 70.405  1.00 22.19 ?  1186 LEU B O    1 
ATOM   15763 C CB   . LEU B 1 1186 ? 125.145 138.268 68.042  1.00 17.07 ?  1186 LEU B CB   1 
ATOM   15764 C CG   . LEU B 1 1186 ? 124.006 138.347 67.024  1.00 17.67 ?  1186 LEU B CG   1 
ATOM   15765 C CD1  . LEU B 1 1186 ? 124.323 139.313 65.897  1.00 17.61 ?  1186 LEU B CD1  1 
ATOM   15766 C CD2  . LEU B 1 1186 ? 123.748 136.962 66.459  1.00 22.15 ?  1186 LEU B CD2  1 
ATOM   15767 N N    . PHE B 1 1187 ? 125.222 138.442 71.099  1.00 21.70 ?  1187 PHE B N    1 
ATOM   15768 C CA   . PHE B 1 1187 ? 125.627 138.031 72.437  1.00 19.04 ?  1187 PHE B CA   1 
ATOM   15769 C C    . PHE B 1 1187 ? 125.475 136.520 72.534  1.00 17.74 ?  1187 PHE B C    1 
ATOM   15770 O O    . PHE B 1 1187 ? 124.384 135.987 72.302  1.00 18.00 ?  1187 PHE B O    1 
ATOM   15771 C CB   . PHE B 1 1187 ? 124.795 138.732 73.512  1.00 22.16 ?  1187 PHE B CB   1 
ATOM   15772 C CG   . PHE B 1 1187 ? 125.497 138.845 74.837  1.00 20.63 ?  1187 PHE B CG   1 
ATOM   15773 C CD1  . PHE B 1 1187 ? 126.748 139.430 74.919  1.00 19.55 ?  1187 PHE B CD1  1 
ATOM   15774 C CD2  . PHE B 1 1187 ? 124.913 138.362 75.995  1.00 18.55 ?  1187 PHE B CD2  1 
ATOM   15775 C CE1  . PHE B 1 1187 ? 127.406 139.534 76.130  1.00 15.37 ?  1187 PHE B CE1  1 
ATOM   15776 C CE2  . PHE B 1 1187 ? 125.567 138.463 77.212  1.00 15.59 ?  1187 PHE B CE2  1 
ATOM   15777 C CZ   . PHE B 1 1187 ? 126.816 139.051 77.278  1.00 11.94 ?  1187 PHE B CZ   1 
ATOM   15778 N N    . VAL B 1 1188 ? 126.566 135.840 72.873  1.00 21.43 ?  1188 VAL B N    1 
ATOM   15779 C CA   . VAL B 1 1188 ? 126.616 134.385 72.942  1.00 19.88 ?  1188 VAL B CA   1 
ATOM   15780 C C    . VAL B 1 1188 ? 127.089 133.993 74.334  1.00 17.26 ?  1188 VAL B C    1 
ATOM   15781 O O    . VAL B 1 1188 ? 128.048 134.572 74.856  1.00 18.72 ?  1188 VAL B O    1 
ATOM   15782 C CB   . VAL B 1 1188 ? 127.535 133.798 71.854  1.00 23.27 ?  1188 VAL B CB   1 
ATOM   15783 C CG1  . VAL B 1 1188 ? 126.823 133.788 70.513  1.00 17.52 ?  1188 VAL B CG1  1 
ATOM   15784 C CG2  . VAL B 1 1188 ? 128.828 134.597 71.748  1.00 22.45 ?  1188 VAL B CG2  1 
ATOM   15785 N N    . VAL B 1 1189 ? 126.404 133.028 74.941  1.00 12.21 ?  1189 VAL B N    1 
ATOM   15786 C CA   . VAL B 1 1189 ? 126.719 132.563 76.286  1.00 17.26 ?  1189 VAL B CA   1 
ATOM   15787 C C    . VAL B 1 1189 ? 127.084 131.088 76.212  1.00 21.56 ?  1189 VAL B C    1 
ATOM   15788 O O    . VAL B 1 1189 ? 126.311 130.280 75.686  1.00 17.49 ?  1189 VAL B O    1 
ATOM   15789 C CB   . VAL B 1 1189 ? 125.544 132.779 77.258  1.00 16.57 ?  1189 VAL B CB   1 
ATOM   15790 C CG1  . VAL B 1 1189 ? 125.998 132.546 78.687  1.00 14.34 ?  1189 VAL B CG1  1 
ATOM   15791 C CG2  . VAL B 1 1189 ? 124.961 134.173 77.096  1.00 20.98 ?  1189 VAL B CG2  1 
ATOM   15792 N N    . ARG B 1 1190 ? 128.255 130.741 76.740  1.00 25.40 ?  1190 ARG B N    1 
ATOM   15793 C CA   . ARG B 1 1190 ? 128.677 129.353 76.829  1.00 22.85 ?  1190 ARG B CA   1 
ATOM   15794 C C    . ARG B 1 1190 ? 127.962 128.660 77.990  1.00 21.28 ?  1190 ARG B C    1 
ATOM   15795 O O    . ARG B 1 1190 ? 127.308 129.294 78.822  1.00 26.04 ?  1190 ARG B O    1 
ATOM   15796 C CB   . ARG B 1 1190 ? 130.191 129.259 77.030  1.00 22.06 ?  1190 ARG B CB   1 
ATOM   15797 C CG   . ARG B 1 1190 ? 131.081 130.138 76.138  1.00 21.42 ?  1190 ARG B CG   1 
ATOM   15798 C CD   . ARG B 1 1190 ? 131.312 129.607 74.719  1.00 23.87 ?  1190 ARG B CD   1 
ATOM   15799 N NE   . ARG B 1 1190 ? 130.155 129.670 73.834  1.00 20.80 ?  1190 ARG B NE   1 
ATOM   15800 C CZ   . ARG B 1 1190 ? 130.162 129.247 72.577  1.00 23.05 ?  1190 ARG B CZ   1 
ATOM   15801 N NH1  . ARG B 1 1190 ? 131.217 128.639 72.059  1.00 26.82 ?  1190 ARG B NH1  1 
ATOM   15802 N NH2  . ARG B 1 1190 ? 129.086 129.445 71.819  1.00 20.93 ?  1190 ARG B NH2  1 
ATOM   15803 N N    . ASN B 1 1191 ? 128.096 127.336 78.048  1.00 19.28 ?  1191 ASN B N    1 
ATOM   15804 C CA   . ASN B 1 1191 ? 127.610 126.597 79.203  1.00 20.81 ?  1191 ASN B CA   1 
ATOM   15805 C C    . ASN B 1 1191 ? 128.620 126.692 80.345  1.00 21.89 ?  1191 ASN B C    1 
ATOM   15806 O O    . ASN B 1 1191 ? 129.716 127.241 80.199  1.00 20.17 ?  1191 ASN B O    1 
ATOM   15807 C CB   . ASN B 1 1191 ? 127.318 125.142 78.837  1.00 23.83 ?  1191 ASN B CB   1 
ATOM   15808 C CG   . ASN B 1 1191 ? 128.435 124.495 78.037  1.00 25.30 ?  1191 ASN B CG   1 
ATOM   15809 O OD1  . ASN B 1 1191 ? 129.617 124.754 78.262  1.00 24.09 ?  1191 ASN B OD1  1 
ATOM   15810 N ND2  . ASN B 1 1191 ? 128.060 123.622 77.110  1.00 18.52 ?  1191 ASN B ND2  1 
ATOM   15811 N N    . ALA B 1 1192 ? 128.251 126.145 81.503  1.00 21.89 ?  1192 ALA B N    1 
ATOM   15812 C CA   . ALA B 1 1192 ? 129.119 126.201 82.672  1.00 23.53 ?  1192 ALA B CA   1 
ATOM   15813 C C    . ALA B 1 1192 ? 130.302 125.257 82.507  1.00 26.13 ?  1192 ALA B C    1 
ATOM   15814 O O    . ALA B 1 1192 ? 130.200 124.070 82.835  1.00 26.85 ?  1192 ALA B O    1 
ATOM   15815 C CB   . ALA B 1 1192 ? 128.337 125.861 83.942  1.00 23.92 ?  1192 ALA B CB   1 
ATOM   15816 N N    . GLU B 1 1193 ? 131.417 125.795 82.007  1.00 27.25 ?  1193 GLU B N    1 
ATOM   15817 C CA   . GLU B 1 1193 ? 132.676 125.086 81.726  1.00 26.16 ?  1193 GLU B CA   1 
ATOM   15818 C C    . GLU B 1 1193 ? 132.489 123.713 81.079  1.00 26.55 ?  1193 GLU B C    1 
ATOM   15819 O O    . GLU B 1 1193 ? 132.456 123.593 79.854  1.00 26.48 ?  1193 GLU B O    1 
ATOM   15820 C CB   . GLU B 1 1193 ? 133.514 124.949 83.009  1.00 21.67 ?  1193 GLU B CB   1 
ATOM   15821 C CG   . GLU B 1 1193 ? 133.141 123.798 83.934  1.00 25.53 ?  1193 GLU B CG   1 
ATOM   15822 C CD   . GLU B 1 1193 ? 134.045 122.592 83.763  1.00 26.36 ?  1193 GLU B CD   1 
ATOM   15823 O OE1  . GLU B 1 1193 ? 135.113 122.733 83.132  1.00 26.23 ?  1193 GLU B OE1  1 
ATOM   15824 O OE2  . GLU B 1 1193 ? 133.686 121.504 84.260  1.00 28.70 ?  1193 GLU B OE2  1 
HETATM 15825 C C1   . POV C 2 .    ? 129.909 118.981 152.784 1.00 0.00  ?  1401 POV A C1   1 
HETATM 15826 C C2   . POV C 2 .    ? 129.114 119.244 151.501 1.00 2.51  ?  1401 POV A C2   1 
HETATM 15827 C C3   . POV C 2 .    ? 127.722 119.774 151.756 1.00 2.74  ?  1401 POV A C3   1 
HETATM 15828 C C210 . POV C 2 .    ? 127.495 115.611 140.223 1.00 0.63  ?  1401 POV A C210 1 
HETATM 15829 C C310 . POV C 2 .    ? 124.741 119.464 139.159 1.00 8.08  ?  1401 POV A C310 1 
HETATM 15830 O O11  . POV C 2 .    ? 129.095 118.285 153.700 1.00 1.33  ?  1401 POV A O11  1 
HETATM 15831 C C211 . POV C 2 .    ? 128.831 114.969 140.015 1.00 0.25  ?  1401 POV A C211 1 
HETATM 15832 C C311 . POV C 2 .    ? 125.282 119.776 137.771 1.00 8.11  ?  1401 POV A C311 1 
HETATM 15833 C C212 . POV C 2 .    ? 129.032 114.509 138.571 1.00 0.70  ?  1401 POV A C212 1 
HETATM 15834 C C312 . POV C 2 .    ? 124.380 119.261 136.657 1.00 3.90  ?  1401 POV A C312 1 
HETATM 15835 C C213 . POV C 2 .    ? 127.813 113.819 137.977 1.00 0.00  ?  1401 POV A C213 1 
HETATM 15836 C C313 . POV C 2 .    ? 124.310 117.741 136.579 1.00 0.58  ?  1401 POV A C313 1 
HETATM 15837 C C214 . POV C 2 .    ? 128.187 112.760 136.951 1.00 0.00  ?  1401 POV A C214 1 
HETATM 15838 C C314 . POV C 2 .    ? 123.684 117.242 135.283 1.00 2.12  ?  1401 POV A C314 1 
HETATM 15839 C C215 . POV C 2 .    ? 129.154 113.265 135.891 1.00 0.00  ?  1401 POV A C215 1 
HETATM 15840 C C315 . POV C 2 .    ? 123.446 115.737 135.257 1.00 0.25  ?  1401 POV A C315 1 
HETATM 15841 C C216 . POV C 2 .    ? 130.145 112.200 135.451 1.00 0.00  ?  1401 POV A C216 1 
HETATM 15842 C C316 . POV C 2 .    ? 124.732 114.927 135.317 1.00 0.87  ?  1401 POV A C316 1 
HETATM 15843 C C21  . POV C 2 .    ? 129.864 117.775 149.777 1.00 2.97  ?  1401 POV A C21  1 
HETATM 15844 O O21  . POV C 2 .    ? 128.964 118.062 150.714 1.00 3.47  ?  1401 POV A O21  1 
HETATM 15845 C C22  . POV C 2 .    ? 129.251 117.826 148.405 1.00 4.99  ?  1401 POV A C22  1 
HETATM 15846 O O22  . POV C 2 .    ? 131.014 117.508 150.018 1.00 4.57  ?  1401 POV A O22  1 
HETATM 15847 C C23  . POV C 2 .    ? 129.197 116.487 147.689 1.00 4.90  ?  1401 POV A C23  1 
HETATM 15848 C C24  . POV C 2 .    ? 128.179 116.504 146.558 1.00 3.13  ?  1401 POV A C24  1 
HETATM 15849 C C25  . POV C 2 .    ? 128.038 115.159 145.857 1.00 3.38  ?  1401 POV A C25  1 
HETATM 15850 C C26  . POV C 2 .    ? 126.708 114.997 145.135 1.00 1.67  ?  1401 POV A C26  1 
HETATM 15851 C C27  . POV C 2 .    ? 126.630 115.752 143.816 1.00 0.00  ?  1401 POV A C27  1 
HETATM 15852 C C28  . POV C 2 .    ? 127.016 114.890 142.616 1.00 0.00  ?  1401 POV A C28  1 
HETATM 15853 C C29  . POV C 2 .    ? 126.733 115.573 141.315 1.00 0.69  ?  1401 POV A C29  1 
HETATM 15854 C C31  . POV C 2 .    ? 125.894 120.372 150.376 1.00 2.41  ?  1401 POV A C31  1 
HETATM 15855 O O31  . POV C 2 .    ? 126.959 119.605 150.568 1.00 4.09  ?  1401 POV A O31  1 
HETATM 15856 C C32  . POV C 2 .    ? 125.180 119.972 149.119 1.00 1.91  ?  1401 POV A C32  1 
HETATM 15857 O O32  . POV C 2 .    ? 125.568 121.261 151.121 1.00 3.94  ?  1401 POV A O32  1 
HETATM 15858 C C33  . POV C 2 .    ? 126.082 119.810 147.910 1.00 0.12  ?  1401 POV A C33  1 
HETATM 15859 C C34  . POV C 2 .    ? 125.303 120.039 146.623 1.00 0.00  ?  1401 POV A C34  1 
HETATM 15860 C C35  . POV C 2 .    ? 126.160 120.063 145.367 1.00 0.00  ?  1401 POV A C35  1 
HETATM 15861 C C36  . POV C 2 .    ? 125.303 120.138 144.112 1.00 0.00  ?  1401 POV A C36  1 
HETATM 15862 C C37  . POV C 2 .    ? 126.047 119.834 142.821 1.00 0.47  ?  1401 POV A C37  1 
HETATM 15863 C C38  . POV C 2 .    ? 125.090 119.628 141.656 1.00 0.00  ?  1401 POV A C38  1 
HETATM 15864 C C39  . POV C 2 .    ? 125.744 119.696 140.283 1.00 0.70  ?  1401 POV A C39  1 
HETATM 15865 P P    . POV D 2 .    ? 123.618 121.647 157.020 1.00 24.06 ?  1402 POV A P    1 
HETATM 15866 C C1   . POV D 2 .    ? 123.502 120.889 154.490 1.00 5.45  ?  1402 POV A C1   1 
HETATM 15867 C C2   . POV D 2 .    ? 122.867 121.503 153.237 1.00 7.77  ?  1402 POV A C2   1 
HETATM 15868 C C3   . POV D 2 .    ? 122.746 123.008 153.294 1.00 3.58  ?  1402 POV A C3   1 
HETATM 15869 C C210 . POV D 2 .    ? 120.786 121.076 142.316 1.00 0.00  ?  1402 POV A C210 1 
HETATM 15870 C C310 . POV D 2 .    ? 124.145 124.656 141.360 1.00 0.00  ?  1402 POV A C310 1 
HETATM 15871 O O11  . POV D 2 .    ? 123.765 121.914 155.423 1.00 6.55  ?  1402 POV A O11  1 
HETATM 15872 C C211 . POV D 2 .    ? 121.065 119.881 141.462 1.00 0.00  ?  1402 POV A C211 1 
HETATM 15873 C C311 . POV D 2 .    ? 124.358 123.801 140.118 1.00 0.00  ?  1402 POV A C311 1 
HETATM 15874 O O12  . POV D 2 .    ? 122.065 122.201 157.190 1.00 6.82  ?  1402 POV A O12  1 
HETATM 15875 C C212 . POV D 2 .    ? 120.983 120.207 139.970 1.00 0.00  ?  1402 POV A C212 1 
HETATM 15876 C C312 . POV D 2 .    ? 124.278 124.604 138.826 1.00 0.00  ?  1402 POV A C312 1 
HETATM 15877 O O13  . POV D 2 .    ? 123.616 120.161 157.215 1.00 10.59 ?  1402 POV A O13  1 
HETATM 15878 C C213 . POV D 2 .    ? 119.781 121.058 139.589 1.00 0.22  ?  1402 POV A C213 1 
HETATM 15879 C C313 . POV D 2 .    ? 125.358 124.252 137.812 1.00 0.07  ?  1402 POV A C313 1 
HETATM 15880 O O14  . POV D 2 .    ? 124.534 122.530 157.807 1.00 8.67  ?  1402 POV A O14  1 
HETATM 15881 C C214 . POV D 2 .    ? 119.593 121.154 138.082 1.00 0.14  ?  1402 POV A C214 1 
HETATM 15882 C C314 . POV D 2 .    ? 125.179 124.958 136.474 1.00 3.57  ?  1402 POV A C314 1 
HETATM 15883 C C215 . POV D 2 .    ? 119.233 119.823 137.435 1.00 1.18  ?  1402 POV A C215 1 
HETATM 15884 C C315 . POV D 2 .    ? 124.019 124.417 135.647 1.00 2.59  ?  1402 POV A C315 1 
HETATM 15885 C C216 . POV D 2 .    ? 120.278 119.339 136.440 1.00 1.68  ?  1402 POV A C216 1 
HETATM 15886 C C316 . POV D 2 .    ? 123.929 125.055 134.269 1.00 0.00  ?  1402 POV A C316 1 
HETATM 15887 C C217 . POV D 2 .    ? 120.597 120.355 135.351 1.00 1.47  ?  1402 POV A C217 1 
HETATM 15888 C C218 . POV D 2 .    ? 120.833 119.699 134.000 1.00 0.00  ?  1402 POV A C218 1 
HETATM 15889 C C21  . POV D 2 .    ? 121.060 120.841 151.799 1.00 4.99  ?  1402 POV A C21  1 
HETATM 15890 O O21  . POV D 2 .    ? 121.546 121.004 153.027 1.00 6.44  ?  1402 POV A O21  1 
HETATM 15891 C C22  . POV D 2 .    ? 121.920 119.930 150.969 1.00 5.25  ?  1402 POV A C22  1 
HETATM 15892 O O22  . POV D 2 .    ? 120.046 121.365 151.417 1.00 8.45  ?  1402 POV A O22  1 
HETATM 15893 C C23  . POV D 2 .    ? 121.133 119.067 149.996 1.00 2.53  ?  1402 POV A C23  1 
HETATM 15894 C C24  . POV D 2 .    ? 121.369 119.474 148.549 1.00 0.88  ?  1402 POV A C24  1 
HETATM 15895 C C25  . POV D 2 .    ? 120.991 120.919 148.254 1.00 0.00  ?  1402 POV A C25  1 
HETATM 15896 C C26  . POV D 2 .    ? 120.997 121.226 146.763 1.00 0.00  ?  1402 POV A C26  1 
HETATM 15897 C C27  . POV D 2 .    ? 120.101 120.290 145.968 1.00 0.32  ?  1402 POV A C27  1 
HETATM 15898 C C28  . POV D 2 .    ? 120.647 119.948 144.582 1.00 0.00  ?  1402 POV A C28  1 
HETATM 15899 C C29  . POV D 2 .    ? 120.601 121.103 143.635 1.00 0.36  ?  1402 POV A C29  1 
HETATM 15900 C C31  . POV D 2 .    ? 123.349 124.359 151.449 1.00 5.70  ?  1402 POV A C31  1 
HETATM 15901 O O31  . POV D 2 .    ? 123.735 123.562 152.436 1.00 4.37  ?  1402 POV A O31  1 
HETATM 15902 C C32  . POV D 2 .    ? 124.422 124.463 150.404 1.00 4.98  ?  1402 POV A C32  1 
HETATM 15903 O O32  . POV D 2 .    ? 122.279 124.914 151.420 1.00 12.20 ?  1402 POV A O32  1 
HETATM 15904 C C33  . POV D 2 .    ? 124.121 125.418 149.264 1.00 3.19  ?  1402 POV A C33  1 
HETATM 15905 C C34  . POV D 2 .    ? 123.219 124.758 148.231 1.00 0.00  ?  1402 POV A C34  1 
HETATM 15906 C C35  . POV D 2 .    ? 123.828 123.527 147.579 1.00 0.23  ?  1402 POV A C35  1 
HETATM 15907 C C36  . POV D 2 .    ? 124.586 123.864 146.302 1.00 0.00  ?  1402 POV A C36  1 
HETATM 15908 C C37  . POV D 2 .    ? 123.684 124.271 145.146 1.00 0.00  ?  1402 POV A C37  1 
HETATM 15909 C C38  . POV D 2 .    ? 124.456 124.609 143.878 1.00 0.00  ?  1402 POV A C38  1 
HETATM 15910 C C39  . POV D 2 .    ? 123.975 123.855 142.645 1.00 0.00  ?  1402 POV A C39  1 
HETATM 15911 C C01  . AJP E 3 .    ? 129.650 120.808 138.058 1.00 0.00  ?  1403 AJP A C01  1 
HETATM 15912 C C02  . AJP E 3 .    ? 130.022 122.235 137.670 1.00 3.10  ?  1403 AJP A C02  1 
HETATM 15913 C C03  . AJP E 3 .    ? 131.244 122.734 138.426 1.00 0.00  ?  1403 AJP A C03  1 
HETATM 15914 C C04  . AJP E 3 .    ? 130.936 123.981 139.256 1.00 1.40  ?  1403 AJP A C04  1 
HETATM 15915 C C05  . AJP E 3 .    ? 129.692 123.802 140.103 1.00 4.28  ?  1403 AJP A C05  1 
HETATM 15916 C C06  . AJP E 3 .    ? 129.228 125.049 140.866 1.00 0.12  ?  1403 AJP A C06  1 
HETATM 15917 C C07  . AJP E 3 .    ? 128.631 124.468 142.163 1.00 0.00  ?  1403 AJP A C07  1 
HETATM 15918 C C08  . AJP E 3 .    ? 128.897 122.960 142.048 1.00 6.50  ?  1403 AJP A C08  1 
HETATM 15919 O O09  . AJP E 3 .    ? 129.979 122.854 141.124 1.00 4.91  ?  1403 AJP A O09  1 
HETATM 15920 C C10  . AJP E 3 .    ? 129.324 122.455 143.427 1.00 3.98  ?  1403 AJP A C10  1 
HETATM 15921 C C11  . AJP E 3 .    ? 128.918 123.598 144.363 1.00 0.00  ?  1403 AJP A C11  1 
HETATM 15922 C C12  . AJP E 3 .    ? 129.202 124.887 143.548 1.00 0.00  ?  1403 AJP A C12  1 
HETATM 15923 C C13  . AJP E 3 .    ? 128.458 126.035 144.245 1.00 0.00  ?  1403 AJP A C13  1 
HETATM 15924 C C14  . AJP E 3 .    ? 128.845 126.167 145.720 1.00 0.16  ?  1403 AJP A C14  1 
HETATM 15925 C C15  . AJP E 3 .    ? 128.714 124.859 146.514 1.00 0.00  ?  1403 AJP A C15  1 
HETATM 15926 C C16  . AJP E 3 .    ? 129.433 123.692 145.813 1.00 0.16  ?  1403 AJP A C16  1 
HETATM 15927 C C17  . AJP E 3 .    ? 129.222 122.385 146.579 1.00 6.03  ?  1403 AJP A C17  1 
HETATM 15928 C C18  . AJP E 3 .    ? 129.629 122.503 148.044 1.00 5.58  ?  1403 AJP A C18  1 
HETATM 15929 C C19  . AJP E 3 .    ? 128.865 123.635 148.716 1.00 1.31  ?  1403 AJP A C19  1 
HETATM 15930 C C20  . AJP E 3 .    ? 129.112 124.994 148.019 1.00 4.39  ?  1403 AJP A C20  1 
HETATM 15931 C C21  . AJP E 3 .    ? 128.217 126.032 148.718 1.00 1.11  ?  1403 AJP A C21  1 
HETATM 15932 C C22  . AJP E 3 .    ? 128.428 126.106 150.231 1.00 0.47  ?  1403 AJP A C22  1 
HETATM 15933 C C23  . AJP E 3 .    ? 128.245 124.744 150.888 1.00 2.33  ?  1403 AJP A C23  1 
HETATM 15934 C C24  . AJP E 3 .    ? 129.118 123.696 150.226 1.00 2.53  ?  1403 AJP A C24  1 
HETATM 15935 O O25  . AJP E 3 .    ? 128.601 124.855 152.285 1.00 2.04  ?  1403 AJP A O25  1 
HETATM 15936 C C26  . AJP E 3 .    ? 127.587 124.526 153.201 1.00 3.69  ?  1403 AJP A C26  1 
HETATM 15937 C C27  . AJP E 3 .    ? 128.252 124.057 154.491 1.00 4.34  ?  1403 AJP A C27  1 
HETATM 15938 C C28  . AJP E 3 .    ? 127.202 123.811 155.567 1.00 6.81  ?  1403 AJP A C28  1 
HETATM 15939 C C29  . AJP E 3 .    ? 126.317 125.038 155.725 1.00 4.11  ?  1403 AJP A C29  1 
HETATM 15940 C C30  . AJP E 3 .    ? 125.721 125.432 154.379 1.00 4.88  ?  1403 AJP A C30  1 
HETATM 15941 O O31  . AJP E 3 .    ? 126.783 125.667 153.442 1.00 4.46  ?  1403 AJP A O31  1 
HETATM 15942 C C32  . AJP E 3 .    ? 124.889 126.693 154.426 1.00 6.72  ?  1403 AJP A C32  1 
HETATM 15943 O O33  . AJP E 3 .    ? 123.841 126.585 155.381 1.00 9.82  ?  1403 AJP A O33  1 
HETATM 15944 O O34  . AJP E 3 .    ? 127.145 126.102 156.218 1.00 4.34  ?  1403 AJP A O34  1 
HETATM 15945 C C35  . AJP E 3 .    ? 126.876 126.590 157.511 1.00 5.32  ?  1403 AJP A C35  1 
HETATM 15946 C C36  . AJP E 3 .    ? 128.085 127.374 158.007 1.00 8.83  ?  1403 AJP A C36  1 
HETATM 15947 C C37  . AJP E 3 .    ? 127.780 128.091 159.319 1.00 8.81  ?  1403 AJP A C37  1 
HETATM 15948 C C38  . AJP E 3 .    ? 126.414 128.772 159.351 1.00 7.26  ?  1403 AJP A C38  1 
HETATM 15949 C C39  . AJP E 3 .    ? 125.339 127.842 158.797 1.00 4.81  ?  1403 AJP A C39  1 
HETATM 15950 O O40  . AJP E 3 .    ? 125.723 127.407 157.487 1.00 4.75  ?  1403 AJP A O40  1 
HETATM 15951 C C41  . AJP E 3 .    ? 123.991 128.512 158.661 1.00 6.45  ?  1403 AJP A C41  1 
HETATM 15952 O O42  . AJP E 3 .    ? 124.070 129.683 157.859 1.00 6.44  ?  1403 AJP A O42  1 
HETATM 15953 O O43  . AJP E 3 .    ? 126.054 129.128 160.681 1.00 7.53  ?  1403 AJP A O43  1 
HETATM 15954 O O44  . AJP E 3 .    ? 128.700 129.186 159.461 1.00 10.28 ?  1403 AJP A O44  1 
HETATM 15955 C C45  . AJP E 3 .    ? 129.227 129.456 160.739 1.00 5.17  ?  1403 AJP A C45  1 
HETATM 15956 O O54  . AJP E 3 .    ? 129.089 126.358 158.181 1.00 10.50 ?  1403 AJP A O54  1 
HETATM 15957 C C55  . AJP E 3 .    ? 130.368 126.690 158.679 1.00 6.02  ?  1403 AJP A C55  1 
HETATM 15958 C C56  . AJP E 3 .    ? 131.050 125.425 159.183 1.00 6.57  ?  1403 AJP A C56  1 
HETATM 15959 C C57  . AJP E 3 .    ? 132.463 125.342 158.640 1.00 5.47  ?  1403 AJP A C57  1 
HETATM 15960 C C58  . AJP E 3 .    ? 132.445 125.411 157.124 1.00 5.90  ?  1403 AJP A C58  1 
HETATM 15961 C C59  . AJP E 3 .    ? 131.805 126.724 156.679 1.00 3.65  ?  1403 AJP A C59  1 
HETATM 15962 O O60  . AJP E 3 .    ? 131.190 127.430 157.779 1.00 4.99  ?  1403 AJP A O60  1 
HETATM 15963 C C61  . AJP E 3 .    ? 130.779 126.565 155.578 1.00 4.15  ?  1403 AJP A C61  1 
HETATM 15964 O O62  . AJP E 3 .    ? 131.353 126.808 154.299 1.00 4.10  ?  1403 AJP A O62  1 
HETATM 15965 O O63  . AJP E 3 .    ? 131.701 124.322 156.591 1.00 5.89  ?  1403 AJP A O63  1 
HETATM 15966 O O64  . AJP E 3 .    ? 132.997 124.063 159.012 1.00 8.32  ?  1403 AJP A O64  1 
HETATM 15967 O O76  . AJP E 3 .    ? 131.069 125.420 160.606 1.00 9.89  ?  1403 AJP A O76  1 
HETATM 15968 O O77  . AJP E 3 .    ? 127.833 123.492 156.802 1.00 7.36  ?  1403 AJP A O77  1 
HETATM 15969 O O78  . AJP E 3 .    ? 128.989 122.864 154.251 1.00 4.17  ?  1403 AJP A O78  1 
HETATM 15970 O O79  . AJP E 3 .    ? 127.523 127.048 150.808 1.00 3.90  ?  1403 AJP A O79  1 
HETATM 15971 C C80  . AJP E 3 .    ? 130.582 125.423 148.160 1.00 3.27  ?  1403 AJP A C80  1 
HETATM 15972 C C81  . AJP E 3 .    ? 130.706 125.202 143.463 1.00 0.00  ?  1403 AJP A C81  1 
HETATM 15973 O O82  . AJP E 3 .    ? 130.685 122.038 143.437 1.00 5.47  ?  1403 AJP A O82  1 
HETATM 15974 C C83  . AJP E 3 .    ? 128.289 125.971 140.093 1.00 0.57  ?  1403 AJP A C83  1 
HETATM 15975 O O84  . AJP E 3 .    ? 128.592 123.352 139.318 1.00 5.89  ?  1403 AJP A O84  1 
HETATM 15976 C C85  . AJP E 3 .    ? 128.868 123.183 137.918 1.00 1.83  ?  1403 AJP A C85  1 
HETATM 15977 C C01  . AJP F 3 .    ? 119.846 116.132 134.515 1.00 2.09  ?  1404 AJP A C01  1 
HETATM 15978 C C02  . AJP F 3 .    ? 118.411 115.737 134.844 1.00 2.86  ?  1404 AJP A C02  1 
HETATM 15979 C C03  . AJP F 3 .    ? 117.819 116.602 135.946 1.00 1.28  ?  1404 AJP A C03  1 
HETATM 15980 C C04  . AJP F 3 .    ? 117.405 115.775 137.162 1.00 0.25  ?  1404 AJP A C04  1 
HETATM 15981 C C05  . AJP F 3 .    ? 118.514 114.843 137.606 1.00 1.90  ?  1404 AJP A C05  1 
HETATM 15982 C C06  . AJP F 3 .    ? 118.148 113.888 138.752 1.00 2.63  ?  1404 AJP A C06  1 
HETATM 15983 C C07  . AJP F 3 .    ? 119.405 113.891 139.645 1.00 4.83  ?  1404 AJP A C07  1 
HETATM 15984 C C08  . AJP F 3 .    ? 120.408 114.757 138.873 1.00 5.88  ?  1404 AJP A C08  1 
HETATM 15985 O O09  . AJP F 3 .    ? 119.580 115.635 138.118 1.00 2.19  ?  1404 AJP A O09  1 
HETATM 15986 C C10  . AJP F 3 .    ? 121.226 115.545 139.898 1.00 0.00  ?  1404 AJP A C10  1 
HETATM 15987 C C11  . AJP F 3 .    ? 120.849 114.905 141.238 1.00 2.42  ?  1404 AJP A C11  1 
HETATM 15988 C C12  . AJP F 3 .    ? 119.358 114.507 141.071 1.00 7.98  ?  1404 AJP A C12  1 
HETATM 15989 C C13  . AJP F 3 .    ? 119.023 113.521 142.199 1.00 0.00  ?  1404 AJP A C13  1 
HETATM 15990 C C14  . AJP F 3 .    ? 119.333 114.099 143.580 1.00 0.00  ?  1404 AJP A C14  1 
HETATM 15991 C C15  . AJP F 3 .    ? 120.772 114.613 143.714 1.00 0.57  ?  1404 AJP A C15  1 
HETATM 15992 C C16  . AJP F 3 .    ? 121.134 115.597 142.587 1.00 4.77  ?  1404 AJP A C16  1 
HETATM 15993 C C17  . AJP F 3 .    ? 122.594 116.042 142.698 1.00 1.77  ?  1404 AJP A C17  1 
HETATM 15994 C C18  . AJP F 3 .    ? 122.932 116.591 144.080 1.00 2.34  ?  1404 AJP A C18  1 
HETATM 15995 C C19  . AJP F 3 .    ? 122.611 115.558 145.151 1.00 0.00  ?  1404 AJP A C19  1 
HETATM 15996 C C20  . AJP F 3 .    ? 121.115 115.162 145.132 1.00 0.02  ?  1404 AJP A C20  1 
HETATM 15997 C C21  . AJP F 3 .    ? 120.923 114.055 146.185 1.00 2.20  ?  1404 AJP A C21  1 
HETATM 15998 C C22  . AJP F 3 .    ? 121.435 114.418 147.578 1.00 0.27  ?  1404 AJP A C22  1 
HETATM 15999 C C23  . AJP F 3 .    ? 122.894 114.850 147.531 1.00 5.36  ?  1404 AJP A C23  1 
HETATM 16000 C C24  . AJP F 3 .    ? 123.095 115.981 146.542 1.00 3.18  ?  1404 AJP A C24  1 
HETATM 16001 O O25  . AJP F 3 .    ? 123.306 115.269 148.852 1.00 0.41  ?  1404 AJP A O25  1 
HETATM 16002 C C26  . AJP F 3 .    ? 124.674 115.110 149.138 1.00 0.85  ?  1404 AJP A C26  1 
HETATM 16003 C C27  . AJP F 3 .    ? 124.910 115.528 150.584 1.00 7.79  ?  1404 AJP A C27  1 
HETATM 16004 C C28  . AJP F 3 .    ? 126.372 115.310 150.954 1.00 1.65  ?  1404 AJP A C28  1 
HETATM 16005 C C29  . AJP F 3 .    ? 126.798 113.883 150.631 1.00 2.71  ?  1404 AJP A C29  1 
HETATM 16006 C C30  . AJP F 3 .    ? 126.452 113.525 149.190 1.00 7.97  ?  1404 AJP A C30  1 
HETATM 16007 O O31  . AJP F 3 .    ? 125.054 113.760 148.953 1.00 3.56  ?  1404 AJP A O31  1 
HETATM 16008 C C32  . AJP F 3 .    ? 126.716 112.077 148.849 1.00 6.74  ?  1404 AJP A C32  1 
HETATM 16009 O O33  . AJP F 3 .    ? 128.056 111.713 149.153 1.00 6.40  ?  1404 AJP A O33  1 
HETATM 16010 O O34  . AJP F 3 .    ? 126.125 112.994 151.535 1.00 4.47  ?  1404 AJP A O34  1 
HETATM 16011 C C35  . AJP F 3 .    ? 126.912 112.326 152.493 1.00 4.76  ?  1404 AJP A C35  1 
HETATM 16012 C C36  . AJP F 3 .    ? 126.130 112.227 153.796 1.00 4.73  ?  1404 AJP A C36  1 
HETATM 16013 C C37  . AJP F 3 .    ? 126.888 111.388 154.818 1.00 4.60  ?  1404 AJP A C37  1 
HETATM 16014 C C38  . AJP F 3 .    ? 127.442 110.091 154.239 1.00 4.43  ?  1404 AJP A C38  1 
HETATM 16015 C C39  . AJP F 3 .    ? 128.169 110.367 152.928 1.00 4.41  ?  1404 AJP A C39  1 
HETATM 16016 O O40  . AJP F 3 .    ? 127.279 111.042 152.028 1.00 4.93  ?  1404 AJP A O40  1 
HETATM 16017 C C41  . AJP F 3 .    ? 128.632 109.109 152.230 1.00 3.69  ?  1404 AJP A C41  1 
HETATM 16018 O O42  . AJP F 3 .    ? 129.352 109.409 151.041 1.00 2.24  ?  1404 AJP A O42  1 
HETATM 16019 O O43  . AJP F 3 .    ? 128.348 109.491 155.158 1.00 5.97  ?  1404 AJP A O43  1 
HETATM 16020 O O44  . AJP F 3 .    ? 125.980 110.934 155.833 1.00 4.11  ?  1404 AJP A O44  1 
HETATM 16021 O O54  . AJP F 3 .    ? 126.011 113.596 154.221 1.00 6.18  ?  1404 AJP A O54  1 
HETATM 16022 C C55  . AJP F 3 .    ? 125.349 113.922 155.424 1.00 7.11  ?  1404 AJP A C55  1 
HETATM 16023 C C56  . AJP F 3 .    ? 125.510 115.413 155.691 1.00 5.24  ?  1404 AJP A C56  1 
HETATM 16024 C C57  . AJP F 3 .    ? 124.210 115.980 156.228 1.00 5.20  ?  1404 AJP A C57  1 
HETATM 16025 C C58  . AJP F 3 .    ? 123.097 115.784 155.217 1.00 6.02  ?  1404 AJP A C58  1 
HETATM 16026 C C59  . AJP F 3 .    ? 122.982 114.307 154.843 1.00 7.54  ?  1404 AJP A C59  1 
HETATM 16027 O O60  . AJP F 3 .    ? 123.989 113.499 155.493 1.00 10.29 ?  1404 AJP A O60  1 
HETATM 16028 C C61  . AJP F 3 .    ? 123.035 114.042 153.353 1.00 5.37  ?  1404 AJP A C61  1 
HETATM 16029 O O62  . AJP F 3 .    ? 122.186 112.962 152.986 1.00 3.94  ?  1404 AJP A O62  1 
HETATM 16030 O O63  . AJP F 3 .    ? 123.359 116.546 154.044 1.00 4.88  ?  1404 AJP A O63  1 
HETATM 16031 O O64  . AJP F 3 .    ? 124.392 117.392 156.408 1.00 14.01 ?  1404 AJP A O64  1 
HETATM 16032 O O76  . AJP F 3 .    ? 126.564 115.628 156.623 1.00 3.32  ?  1404 AJP A O76  1 
HETATM 16033 O O77  . AJP F 3 .    ? 126.569 115.588 152.335 1.00 2.99  ?  1404 AJP A O77  1 
HETATM 16034 O O78  . AJP F 3 .    ? 124.561 116.895 150.761 1.00 3.67  ?  1404 AJP A O78  1 
HETATM 16035 O O79  . AJP F 3 .    ? 121.283 113.304 148.458 1.00 4.14  ?  1404 AJP A O79  1 
HETATM 16036 C C80  . AJP F 3 .    ? 120.221 116.361 145.492 1.00 1.77  ?  1404 AJP A C80  1 
HETATM 16037 C C81  . AJP F 3 .    ? 118.424 115.727 141.137 1.00 2.74  ?  1404 AJP A C81  1 
HETATM 16038 O O82  . AJP F 3 .    ? 121.028 116.948 139.762 1.00 14.49 ?  1404 AJP A O82  1 
HETATM 16039 C C83  . AJP F 3 .    ? 117.687 112.500 138.316 1.00 1.69  ?  1404 AJP A C83  1 
HETATM 16040 O O84  . AJP F 3 .    ? 118.980 114.044 136.522 1.00 5.15  ?  1404 AJP A O84  1 
HETATM 16041 C C85  . AJP F 3 .    ? 118.331 114.284 135.263 1.00 5.06  ?  1404 AJP A C85  1 
HETATM 16042 C C1   . POV G 2 .    ? 114.782 125.541 152.778 1.00 1.02  ?  1401 POV B C1   1 
HETATM 16043 C C2   . POV G 2 .    ? 115.603 125.635 151.489 1.00 3.45  ?  1401 POV B C2   1 
HETATM 16044 C C3   . POV G 2 .    ? 117.023 125.145 151.652 1.00 4.66  ?  1401 POV B C3   1 
HETATM 16045 C C210 . POV G 2 .    ? 117.908 129.109 140.903 1.00 0.00  ?  1401 POV B C210 1 
HETATM 16046 C C310 . POV G 2 .    ? 119.981 125.569 139.013 1.00 10.53 ?  1401 POV B C310 1 
HETATM 16047 O O11  . POV G 2 .    ? 115.548 126.048 153.848 1.00 0.85  ?  1401 POV B O11  1 
HETATM 16048 C C211 . POV G 2 .    ? 116.645 129.643 140.303 1.00 5.05  ?  1401 POV B C211 1 
HETATM 16049 C C311 . POV G 2 .    ? 119.714 125.031 137.614 1.00 5.93  ?  1401 POV B C311 1 
HETATM 16050 C C212 . POV G 2 .    ? 116.872 130.070 138.851 1.00 1.35  ?  1401 POV B C212 1 
HETATM 16051 C C312 . POV G 2 .    ? 120.599 125.688 136.563 1.00 2.72  ?  1401 POV B C312 1 
HETATM 16052 C C213 . POV G 2 .    ? 115.706 130.829 138.234 1.00 1.34  ?  1401 POV B C213 1 
HETATM 16053 C C313 . POV G 2 .    ? 120.309 127.169 136.357 1.00 1.75  ?  1401 POV B C313 1 
HETATM 16054 C C214 . POV G 2 .    ? 116.090 131.520 136.933 1.00 0.00  ?  1401 POV B C214 1 
HETATM 16055 C C314 . POV G 2 .    ? 121.305 127.850 135.427 1.00 4.45  ?  1401 POV B C314 1 
HETATM 16056 C C215 . POV G 2 .    ? 115.021 132.470 136.415 1.00 0.00  ?  1401 POV B C215 1 
HETATM 16057 C C315 . POV G 2 .    ? 120.752 129.097 134.748 1.00 0.00  ?  1401 POV B C315 1 
HETATM 16058 C C216 . POV G 2 .    ? 115.035 132.603 134.901 1.00 0.32  ?  1401 POV B C216 1 
HETATM 16059 C C316 . POV G 2 .    ? 120.236 130.130 135.737 1.00 0.00  ?  1401 POV B C316 1 
HETATM 16060 C C21  . POV G 2 .    ? 114.849 127.394 150.072 1.00 3.87  ?  1401 POV B C21  1 
HETATM 16061 O O21  . POV G 2 .    ? 115.684 126.980 151.020 1.00 5.72  ?  1401 POV B O21  1 
HETATM 16062 C C22  . POV G 2 .    ? 115.104 126.676 148.776 1.00 1.37  ?  1401 POV B C22  1 
HETATM 16063 O O22  . POV G 2 .    ? 114.002 128.232 150.252 1.00 4.45  ?  1401 POV B O22  1 
HETATM 16064 C C23  . POV G 2 .    ? 116.129 127.342 147.875 1.00 3.51  ?  1401 POV B C23  1 
HETATM 16065 C C24  . POV G 2 .    ? 115.654 128.714 147.418 1.00 5.50  ?  1401 POV B C24  1 
HETATM 16066 C C25  . POV G 2 .    ? 116.069 129.044 145.992 1.00 4.59  ?  1401 POV B C25  1 
HETATM 16067 C C26  . POV G 2 .    ? 117.462 129.648 145.890 1.00 3.23  ?  1401 POV B C26  1 
HETATM 16068 C C27  . POV G 2 .    ? 118.220 129.200 144.649 1.00 1.32  ?  1401 POV B C27  1 
HETATM 16069 C C28  . POV G 2 .    ? 117.700 129.822 143.353 1.00 0.00  ?  1401 POV B C28  1 
HETATM 16070 C C29  . POV G 2 .    ? 118.345 129.192 142.160 1.00 2.93  ?  1401 POV B C29  1 
HETATM 16071 C C31  . POV G 2 .    ? 118.905 124.700 150.310 1.00 2.58  ?  1401 POV B C31  1 
HETATM 16072 O O31  . POV G 2 .    ? 117.638 125.087 150.372 1.00 9.01  ?  1401 POV B O31  1 
HETATM 16073 C C32  . POV G 2 .    ? 119.505 125.027 148.973 1.00 1.90  ?  1401 POV B C32  1 
HETATM 16074 O O32  . POV G 2 .    ? 119.474 124.164 151.226 1.00 0.94  ?  1401 POV B O32  1 
HETATM 16075 C C33  . POV G 2 .    ? 118.696 124.587 147.767 1.00 0.79  ?  1401 POV B C33  1 
HETATM 16076 C C34  . POV G 2 .    ? 119.419 124.971 146.484 1.00 0.00  ?  1401 POV B C34  1 
HETATM 16077 C C35  . POV G 2 .    ? 118.747 124.506 145.202 1.00 0.00  ?  1401 POV B C35  1 
HETATM 16078 C C36  . POV G 2 .    ? 119.484 125.037 143.981 1.00 0.00  ?  1401 POV B C36  1 
HETATM 16079 C C37  . POV G 2 .    ? 118.822 124.732 142.646 1.00 0.00  ?  1401 POV B C37  1 
HETATM 16080 C C38  . POV G 2 .    ? 119.588 125.367 141.493 1.00 0.00  ?  1401 POV B C38  1 
HETATM 16081 C C39  . POV G 2 .    ? 119.120 124.948 140.106 1.00 3.80  ?  1401 POV B C39  1 
HETATM 16082 C C01  . AJP H 3 .    ? 115.155 123.977 138.059 1.00 0.07  ?  1402 AJP B C01  1 
HETATM 16083 C C02  . AJP H 3 .    ? 114.777 122.546 137.693 1.00 1.73  ?  1402 AJP B C02  1 
HETATM 16084 C C03  . AJP H 3 .    ? 113.558 122.062 138.462 1.00 0.78  ?  1402 AJP B C03  1 
HETATM 16085 C C04  . AJP H 3 .    ? 113.862 120.815 139.295 1.00 5.03  ?  1402 AJP B C04  1 
HETATM 16086 C C05  . AJP H 3 .    ? 115.110 120.994 140.138 1.00 3.38  ?  1402 AJP B C05  1 
HETATM 16087 C C06  . AJP H 3 .    ? 115.574 119.746 140.900 1.00 0.33  ?  1402 AJP B C06  1 
HETATM 16088 C C07  . AJP H 3 .    ? 116.173 120.326 142.197 1.00 0.00  ?  1402 AJP B C07  1 
HETATM 16089 C C08  . AJP H 3 .    ? 115.909 121.835 142.082 1.00 7.48  ?  1402 AJP B C08  1 
HETATM 16090 O O09  . AJP H 3 .    ? 114.827 121.943 141.158 1.00 4.85  ?  1402 AJP B O09  1 
HETATM 16091 C C10  . AJP H 3 .    ? 115.482 122.339 143.462 1.00 4.40  ?  1402 AJP B C10  1 
HETATM 16092 C C11  . AJP H 3 .    ? 115.887 121.195 144.398 1.00 3.17  ?  1402 AJP B C11  1 
HETATM 16093 C C12  . AJP H 3 .    ? 115.601 119.906 143.582 1.00 2.22  ?  1402 AJP B C12  1 
HETATM 16094 C C13  . AJP H 3 .    ? 116.345 118.758 144.278 1.00 0.00  ?  1402 AJP B C13  1 
HETATM 16095 C C14  . AJP H 3 .    ? 115.958 118.624 145.752 1.00 0.54  ?  1402 AJP B C14  1 
HETATM 16096 C C15  . AJP H 3 .    ? 116.091 119.932 146.547 1.00 0.62  ?  1402 AJP B C15  1 
HETATM 16097 C C16  . AJP H 3 .    ? 115.372 121.100 145.848 1.00 0.00  ?  1402 AJP B C16  1 
HETATM 16098 C C17  . AJP H 3 .    ? 115.584 122.406 146.616 1.00 0.00  ?  1402 AJP B C17  1 
HETATM 16099 C C18  . AJP H 3 .    ? 115.182 122.286 148.082 1.00 0.04  ?  1402 AJP B C18  1 
HETATM 16100 C C19  . AJP H 3 .    ? 115.947 121.153 148.751 1.00 1.68  ?  1402 AJP B C19  1 
HETATM 16101 C C20  . AJP H 3 .    ? 115.696 119.796 148.052 1.00 2.22  ?  1402 AJP B C20  1 
HETATM 16102 C C21  . AJP H 3 .    ? 116.592 118.756 148.748 1.00 0.00  ?  1402 AJP B C21  1 
HETATM 16103 C C22  . AJP H 3 .    ? 116.384 118.679 150.262 1.00 0.72  ?  1402 AJP B C22  1 
HETATM 16104 C C23  . AJP H 3 .    ? 116.570 120.038 150.922 1.00 2.55  ?  1402 AJP B C23  1 
HETATM 16105 C C24  . AJP H 3 .    ? 115.700 121.091 150.262 1.00 3.89  ?  1402 AJP B C24  1 
HETATM 16106 O O25  . AJP H 3 .    ? 116.207 119.920 152.317 1.00 2.20  ?  1402 AJP B O25  1 
HETATM 16107 C C26  . AJP H 3 .    ? 117.204 120.279 153.242 1.00 3.16  ?  1402 AJP B C26  1 
HETATM 16108 C C27  . AJP H 3 .    ? 116.513 120.729 154.524 1.00 4.35  ?  1402 AJP B C27  1 
HETATM 16109 C C28  . AJP H 3 .    ? 117.544 121.007 155.611 1.00 5.74  ?  1402 AJP B C28  1 
HETATM 16110 C C29  . AJP H 3 .    ? 118.458 119.803 155.780 1.00 3.71  ?  1402 AJP B C29  1 
HETATM 16111 C C30  . AJP H 3 .    ? 119.081 119.424 154.444 1.00 4.73  ?  1402 AJP B C30  1 
HETATM 16112 O O31  . AJP H 3 .    ? 118.037 119.161 153.492 1.00 4.00  ?  1402 AJP B O31  1 
HETATM 16113 C C32  . AJP H 3 .    ? 119.940 118.182 154.509 1.00 6.04  ?  1402 AJP B C32  1 
HETATM 16114 O O33  . AJP H 3 .    ? 120.939 118.301 155.514 1.00 6.79  ?  1402 AJP B O33  1 
HETATM 16115 O O34  . AJP H 3 .    ? 117.647 118.714 156.242 1.00 4.86  ?  1402 AJP B O34  1 
HETATM 16116 C C35  . AJP H 3 .    ? 117.877 118.223 157.540 1.00 4.60  ?  1402 AJP B C35  1 
HETATM 16117 C C36  . AJP H 3 .    ? 116.571 117.660 158.078 1.00 8.77  ?  1402 AJP B C36  1 
HETATM 16118 C C37  . AJP H 3 .    ? 116.793 117.007 159.431 1.00 9.44  ?  1402 AJP B C37  1 
HETATM 16119 C C38  . AJP H 3 .    ? 117.926 115.992 159.376 1.00 7.98  ?  1402 AJP B C38  1 
HETATM 16120 C C39  . AJP H 3 .    ? 119.169 116.660 158.796 1.00 5.54  ?  1402 AJP B C39  1 
HETATM 16121 O O40  . AJP H 3 .    ? 118.865 117.209 157.503 1.00 5.82  ?  1402 AJP B O40  1 
HETATM 16122 C C41  . AJP H 3 .    ? 120.322 115.702 158.606 1.00 7.26  ?  1402 AJP B C41  1 
HETATM 16123 O O42  . AJP H 3 .    ? 121.466 116.370 158.090 1.00 7.70  ?  1402 AJP B O42  1 
HETATM 16124 O O43  . AJP H 3 .    ? 118.218 115.509 160.681 1.00 6.59  ?  1402 AJP B O43  1 
HETATM 16125 O O44  . AJP H 3 .    ? 115.595 116.300 159.782 1.00 9.20  ?  1402 AJP B O44  1 
HETATM 16126 O O54  . AJP H 3 .    ? 115.656 118.750 158.259 1.00 9.50  ?  1402 AJP B O54  1 
HETATM 16127 O O77  . AJP H 3 .    ? 116.891 121.310 156.838 1.00 6.59  ?  1402 AJP B O77  1 
HETATM 16128 O O78  . AJP H 3 .    ? 115.744 121.901 154.276 1.00 4.34  ?  1402 AJP B O78  1 
HETATM 16129 O O79  . AJP H 3 .    ? 117.290 117.734 150.833 1.00 4.17  ?  1402 AJP B O79  1 
HETATM 16130 C C80  . AJP H 3 .    ? 114.226 119.369 148.197 1.00 3.47  ?  1402 AJP B C80  1 
HETATM 16131 C C81  . AJP H 3 .    ? 114.097 119.592 143.496 1.00 0.00  ?  1402 AJP B C81  1 
HETATM 16132 O O82  . AJP H 3 .    ? 114.121 122.756 143.469 1.00 6.13  ?  1402 AJP B O82  1 
HETATM 16133 C C83  . AJP H 3 .    ? 116.512 118.823 140.126 1.00 0.00  ?  1402 AJP B C83  1 
HETATM 16134 O O84  . AJP H 3 .    ? 116.208 121.441 139.348 1.00 4.74  ?  1402 AJP B O84  1 
HETATM 16135 C C85  . AJP H 3 .    ? 115.930 121.598 137.947 1.00 1.46  ?  1402 AJP B C85  1 
HETATM 16136 C C01  . AJP I 3 .    ? 124.842 128.655 134.552 1.00 3.71  ?  1403 AJP B C01  1 
HETATM 16137 C C02  . AJP I 3 .    ? 126.282 129.056 134.850 1.00 1.97  ?  1403 AJP B C02  1 
HETATM 16138 C C03  . AJP I 3 .    ? 126.907 128.180 135.925 1.00 2.93  ?  1403 AJP B C03  1 
HETATM 16139 C C04  . AJP I 3 .    ? 127.339 128.992 137.145 1.00 1.48  ?  1403 AJP B C04  1 
HETATM 16140 C C05  . AJP I 3 .    ? 126.233 129.910 137.625 1.00 2.59  ?  1403 AJP B C05  1 
HETATM 16141 C C06  . AJP I 3 .    ? 126.616 130.852 138.776 1.00 2.20  ?  1403 AJP B C06  1 
HETATM 16142 C C07  . AJP I 3 .    ? 125.361 130.856 139.672 1.00 1.97  ?  1403 AJP B C07  1 
HETATM 16143 C C08  . AJP I 3 .    ? 124.359 129.978 138.914 1.00 2.43  ?  1403 AJP B C08  1 
HETATM 16144 O O09  . AJP I 3 .    ? 125.184 129.104 138.150 1.00 2.13  ?  1403 AJP B O09  1 
HETATM 16145 C C10  . AJP I 3 .    ? 123.555 129.187 139.949 1.00 0.16  ?  1403 AJP B C10  1 
HETATM 16146 C C11  . AJP I 3 .    ? 123.927 129.852 141.280 1.00 3.98  ?  1403 AJP B C11  1 
HETATM 16147 C C12  . AJP I 3 .    ? 125.415 130.258 141.105 1.00 6.52  ?  1403 AJP B C12  1 
HETATM 16148 C C13  . AJP I 3 .    ? 125.747 131.259 142.220 1.00 0.00  ?  1403 AJP B C13  1 
HETATM 16149 C C14  . AJP I 3 .    ? 125.444 130.696 143.608 1.00 0.00  ?  1403 AJP B C14  1 
HETATM 16150 C C15  . AJP I 3 .    ? 124.005 130.185 143.751 1.00 0.26  ?  1403 AJP B C15  1 
HETATM 16151 C C16  . AJP I 3 .    ? 123.642 129.183 142.640 1.00 7.38  ?  1403 AJP B C16  1 
HETATM 16152 C C17  . AJP I 3 .    ? 122.181 128.741 142.760 1.00 0.00  ?  1403 AJP B C17  1 
HETATM 16153 C C18  . AJP I 3 .    ? 121.840 128.221 144.153 1.00 0.00  ?  1403 AJP B C18  1 
HETATM 16154 C C19  . AJP I 3 .    ? 122.166 129.271 145.206 1.00 0.00  ?  1403 AJP B C19  1 
HETATM 16155 C C20  . AJP I 3 .    ? 123.663 129.660 145.177 1.00 0.00  ?  1403 AJP B C20  1 
HETATM 16156 C C21  . AJP I 3 .    ? 123.863 130.782 146.211 1.00 3.25  ?  1403 AJP B C21  1 
HETATM 16157 C C22  . AJP I 3 .    ? 123.363 130.437 147.614 1.00 0.03  ?  1403 AJP B C22  1 
HETATM 16158 C C23  . AJP I 3 .    ? 121.903 130.007 147.591 1.00 7.21  ?  1403 AJP B C23  1 
HETATM 16159 C C24  . AJP I 3 .    ? 121.684 128.875 146.606 1.00 0.41  ?  1403 AJP B C24  1 
HETATM 16160 O O25  . AJP I 3 .    ? 121.535 129.579 148.923 1.00 1.66  ?  1403 AJP B O25  1 
HETATM 16161 C C26  . AJP I 3 .    ? 120.161 129.607 149.222 1.00 1.40  ?  1403 AJP B C26  1 
HETATM 16162 C C27  . AJP I 3 .    ? 119.992 129.234 150.689 1.00 2.27  ?  1403 AJP B C27  1 
HETATM 16163 C C28  . AJP I 3 .    ? 118.524 129.328 151.087 1.00 0.75  ?  1403 AJP B C28  1 
HETATM 16164 C C29  . AJP I 3 .    ? 117.971 130.698 150.725 1.00 1.52  ?  1403 AJP B C29  1 
HETATM 16165 C C30  . AJP I 3 .    ? 118.227 130.999 149.253 1.00 0.86  ?  1403 AJP B C30  1 
HETATM 16166 O O31  . AJP I 3 .    ? 119.634 130.899 148.979 1.00 2.67  ?  1403 AJP B O31  1 
HETATM 16167 C C32  . AJP I 3 .    ? 117.788 132.382 148.824 1.00 2.34  ?  1403 AJP B C32  1 
HETATM 16168 O O33  . AJP I 3 .    ? 118.565 133.396 149.447 1.00 2.61  ?  1403 AJP B O33  1 
HETATM 16169 O O34  . AJP I 3 .    ? 118.650 131.663 151.542 1.00 4.15  ?  1403 AJP B O34  1 
HETATM 16170 C C35  . AJP I 3 .    ? 117.896 132.351 152.512 1.00 4.96  ?  1403 AJP B C35  1 
HETATM 16171 C C36  . AJP I 3 .    ? 118.758 132.536 153.755 1.00 4.89  ?  1403 AJP B C36  1 
HETATM 16172 C C37  . AJP I 3 .    ? 118.120 133.504 154.748 1.00 4.76  ?  1403 AJP B C37  1 
HETATM 16173 C C38  . AJP I 3 .    ? 117.478 134.730 154.110 1.00 3.95  ?  1403 AJP B C38  1 
HETATM 16174 C C39  . AJP I 3 .    ? 116.638 134.317 152.908 1.00 4.38  ?  1403 AJP B C39  1 
HETATM 16175 O O40  . AJP I 3 .    ? 117.466 133.592 151.990 1.00 5.44  ?  1403 AJP B O40  1 
HETATM 16176 C C41  . AJP I 3 .    ? 116.066 135.495 152.152 1.00 2.22  ?  1403 AJP B C41  1 
HETATM 16177 O O42  . AJP I 3 .    ? 115.253 135.069 151.066 1.00 1.81  ?  1403 AJP B O42  1 
HETATM 16178 O O43  . AJP I 3 .    ? 116.647 135.395 155.055 1.00 4.93  ?  1403 AJP B O43  1 
HETATM 16179 O O44  . AJP I 3 .    ? 119.159 134.075 155.558 1.00 3.55  ?  1403 AJP B O44  1 
HETATM 16180 O O54  . AJP I 3 .    ? 118.837 131.208 154.304 1.00 5.59  ?  1403 AJP B O54  1 
HETATM 16181 C C55  . AJP I 3 .    ? 119.307 130.998 155.618 1.00 6.46  ?  1403 AJP B C55  1 
HETATM 16182 C C56  . AJP I 3 .    ? 118.858 129.622 156.094 1.00 5.35  ?  1403 AJP B C56  1 
HETATM 16183 C C57  . AJP I 3 .    ? 120.020 128.896 156.745 1.00 4.14  ?  1403 AJP B C57  1 
HETATM 16184 C C58  . AJP I 3 .    ? 121.176 128.777 155.770 1.00 5.55  ?  1403 AJP B C58  1 
HETATM 16185 C C59  . AJP I 3 .    ? 121.605 130.167 155.307 1.00 6.68  ?  1403 AJP B C59  1 
HETATM 16186 O O60  . AJP I 3 .    ? 120.710 131.198 155.782 1.00 12.70 ?  1403 AJP B O60  1 
HETATM 16187 C C61  . AJP I 3 .    ? 121.743 130.302 153.805 1.00 4.57  ?  1403 AJP B C61  1 
HETATM 16188 O O63  . AJP I 3 .    ? 120.788 128.004 154.640 1.00 5.89  ?  1403 AJP B O63  1 
HETATM 16189 O O64  . AJP I 3 .    ? 119.581 127.567 157.064 1.00 6.96  ?  1403 AJP B O64  1 
HETATM 16190 O O76  . AJP I 3 .    ? 117.783 129.757 157.015 1.00 7.25  ?  1403 AJP B O76  1 
HETATM 16191 O O77  . AJP I 3 .    ? 118.382 129.086 152.482 1.00 3.45  ?  1403 AJP B O77  1 
HETATM 16192 O O78  . AJP I 3 .    ? 120.475 127.915 150.916 1.00 3.65  ?  1403 AJP B O78  1 
HETATM 16193 O O79  . AJP I 3 .    ? 123.527 131.563 148.477 1.00 4.80  ?  1403 AJP B O79  1 
HETATM 16194 C C80  . AJP I 3 .    ? 124.551 128.461 145.553 1.00 2.22  ?  1403 AJP B C80  1 
HETATM 16195 C C81  . AJP I 3 .    ? 126.358 129.044 141.182 1.00 1.98  ?  1403 AJP B C81  1 
HETATM 16196 O O82  . AJP I 3 .    ? 123.770 127.785 139.828 1.00 15.34 ?  1403 AJP B O82  1 
HETATM 16197 C C83  . AJP I 3 .    ? 127.090 132.238 138.348 1.00 1.58  ?  1403 AJP B C83  1 
HETATM 16198 O O84  . AJP I 3 .    ? 125.738 130.721 136.563 1.00 4.04  ?  1403 AJP B O84  1 
HETATM 16199 C C85  . AJP I 3 .    ? 126.362 130.503 135.287 1.00 6.90  ?  1403 AJP B C85  1 
# 
