data_1QWU
# 
_entry.id   1QWU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1QWU         
RCSB  RCSB020164   
WWPDB D_1000020164 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1QWN . unspecified 
PDB 1HTY . unspecified 
PDB 1HWW . unspecified 
PDB 1HXK . unspecified 
PDB 1PS3 . unspecified 
PDB 1QW9 . unspecified 
PDB 1QX1 . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1QWU 
_pdbx_database_status.recvd_initial_deposition_date   2003-09-03 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Numao, S.'     1 
'Kuntz, D.A.'   2 
'Withers, S.G.' 3 
'Rose, D.R.'    4 
# 
_citation.id                        primary 
_citation.title                     
;Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural analysis of covalent reaction intermediates.
;
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_volume            278 
_citation.page_first                48074 
_citation.page_last                 48083 
_citation.year                      2003 
_citation.journal_id_ASTM           JBCHA3 
_citation.country                   US 
_citation.journal_id_ISSN           0021-9258 
_citation.journal_id_CSD            0071 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   12960159 
_citation.pdbx_database_id_DOI      10.1074/jbc.M309249200 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Numao, S.'     1 
primary 'Kuntz, D.A.'   2 
primary 'Withers, S.G.' 3 
primary 'Rose, D.R.'    4 
# 
_cell.entry_id           1QWU 
_cell.length_a           68.850 
_cell.length_b           109.799 
_cell.length_c           138.765 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1QWU 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
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 'Alpha-mannosidase II'             119700.633 1    3.2.1.114 D341N 
'Family 38 catalytic domain (residues 94-1108)' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE             221.208    1    ?         ?     ? ? 
3 non-polymer syn 'ZINC ION'                         65.409     1    ?         ?     ? ? 
4 non-polymer syn '5-FLUORO-BETA-L-GULOSYL FLUORIDE' 200.137    1    ?         ?     ? ? 
5 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'    118.174    1    ?         ?     ? ? 
6 water       nat water                              18.015     1025 ?         ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase, MAN II, Golgi alpha-mannosidase II, AMAN II' 
# 
_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       
;RSSHHHHHHGEFDDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHK
LKVFVVPHSHNDPGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEF
VTGGWVMPDEANSHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQ
RQLEFLWRQIWDNKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVD
QWKKKAELYRTNVLLIPLGDNFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTL
SGDFFTYADRSDNYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKT
HVVVDYEQRMQEALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNT
LPHWREQLVDFYVSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSK
PEHTSYASNLLLRKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSH
GDRSGAYLFLPNGPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDS
GDIFYTDLNGLQFIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQ
GVLDNKPVLHIYRLVLEKVNNCVRPSKLHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVS
VMRRLTKSSAKTQRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYV
SSHSS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;RSSHHHHHHGEFDDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHK
LKVFVVPHSHNDPGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEF
VTGGWVMPDEANSHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQ
RQLEFLWRQIWDNKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVD
QWKKKAELYRTNVLLIPLGDNFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTL
SGDFFTYADRSDNYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKT
HVVVDYEQRMQEALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNT
LPHWREQLVDFYVSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSK
PEHTSYASNLLLRKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSH
GDRSGAYLFLPNGPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDS
GDIFYTDLNGLQFIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQ
GVLDNKPVLHIYRLVLEKVNNCVRPSKLHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVS
VMRRLTKSSAKTQRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYV
SSHSS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    ARG n 
1 2    SER n 
1 3    SER n 
1 4    HIS n 
1 5    HIS n 
1 6    HIS n 
1 7    HIS n 
1 8    HIS n 
1 9    HIS n 
1 10   GLY n 
1 11   GLU n 
1 12   PHE n 
1 13   ASP n 
1 14   ASP n 
1 15   PRO n 
1 16   ILE n 
1 17   ARG n 
1 18   PRO n 
1 19   PRO n 
1 20   LEU n 
1 21   LYS n 
1 22   VAL n 
1 23   ALA n 
1 24   ARG n 
1 25   SER n 
1 26   PRO n 
1 27   ARG n 
1 28   PRO n 
1 29   GLY n 
1 30   GLN n 
1 31   CYS n 
1 32   GLN n 
1 33   ASP n 
1 34   VAL n 
1 35   VAL n 
1 36   GLN n 
1 37   ASP n 
1 38   VAL n 
1 39   PRO n 
1 40   ASN n 
1 41   VAL n 
1 42   ASP n 
1 43   VAL n 
1 44   GLN n 
1 45   MET n 
1 46   LEU n 
1 47   GLU n 
1 48   LEU n 
1 49   TYR n 
1 50   ASP n 
1 51   ARG n 
1 52   MET n 
1 53   SER n 
1 54   PHE n 
1 55   LYS n 
1 56   ASP n 
1 57   ILE n 
1 58   ASP n 
1 59   GLY n 
1 60   GLY n 
1 61   VAL n 
1 62   TRP n 
1 63   LYS n 
1 64   GLN n 
1 65   GLY n 
1 66   TRP n 
1 67   ASN n 
1 68   ILE n 
1 69   LYS n 
1 70   TYR n 
1 71   ASP n 
1 72   PRO n 
1 73   LEU n 
1 74   LYS n 
1 75   TYR n 
1 76   ASN n 
1 77   ALA n 
1 78   HIS n 
1 79   HIS n 
1 80   LYS n 
1 81   LEU n 
1 82   LYS n 
1 83   VAL n 
1 84   PHE n 
1 85   VAL n 
1 86   VAL n 
1 87   PRO n 
1 88   HIS n 
1 89   SER n 
1 90   HIS n 
1 91   ASN n 
1 92   ASP n 
1 93   PRO n 
1 94   GLY n 
1 95   TRP n 
1 96   ILE n 
1 97   GLN n 
1 98   THR n 
1 99   PHE n 
1 100  GLU n 
1 101  GLU n 
1 102  TYR n 
1 103  TYR n 
1 104  GLN n 
1 105  HIS n 
1 106  ASP n 
1 107  THR n 
1 108  LYS n 
1 109  HIS n 
1 110  ILE n 
1 111  LEU n 
1 112  SER n 
1 113  ASN n 
1 114  ALA n 
1 115  LEU n 
1 116  ARG n 
1 117  HIS n 
1 118  LEU n 
1 119  HIS n 
1 120  ASP n 
1 121  ASN n 
1 122  PRO n 
1 123  GLU n 
1 124  MET n 
1 125  LYS n 
1 126  PHE n 
1 127  ILE n 
1 128  TRP n 
1 129  ALA n 
1 130  GLU n 
1 131  ILE n 
1 132  SER n 
1 133  TYR n 
1 134  PHE n 
1 135  ALA n 
1 136  ARG n 
1 137  PHE n 
1 138  TYR n 
1 139  HIS n 
1 140  ASP n 
1 141  LEU n 
1 142  GLY n 
1 143  GLU n 
1 144  ASN n 
1 145  LYS n 
1 146  LYS n 
1 147  LEU n 
1 148  GLN n 
1 149  MET n 
1 150  LYS n 
1 151  SER n 
1 152  ILE n 
1 153  VAL n 
1 154  LYS n 
1 155  ASN n 
1 156  GLY n 
1 157  GLN n 
1 158  LEU n 
1 159  GLU n 
1 160  PHE n 
1 161  VAL n 
1 162  THR n 
1 163  GLY n 
1 164  GLY n 
1 165  TRP n 
1 166  VAL n 
1 167  MET n 
1 168  PRO n 
1 169  ASP n 
1 170  GLU n 
1 171  ALA n 
1 172  ASN n 
1 173  SER n 
1 174  HIS n 
1 175  TRP n 
1 176  ARG n 
1 177  ASN n 
1 178  VAL n 
1 179  LEU n 
1 180  LEU n 
1 181  GLN n 
1 182  LEU n 
1 183  THR n 
1 184  GLU n 
1 185  GLY n 
1 186  GLN n 
1 187  THR n 
1 188  TRP n 
1 189  LEU n 
1 190  LYS n 
1 191  GLN n 
1 192  PHE n 
1 193  MET n 
1 194  ASN n 
1 195  VAL n 
1 196  THR n 
1 197  PRO n 
1 198  THR n 
1 199  ALA n 
1 200  SER n 
1 201  TRP n 
1 202  ALA n 
1 203  ILE n 
1 204  ASP n 
1 205  PRO n 
1 206  PHE n 
1 207  GLY n 
1 208  HIS n 
1 209  SER n 
1 210  PRO n 
1 211  THR n 
1 212  MET n 
1 213  PRO n 
1 214  TYR n 
1 215  ILE n 
1 216  LEU n 
1 217  GLN n 
1 218  LYS n 
1 219  SER n 
1 220  GLY n 
1 221  PHE n 
1 222  LYS n 
1 223  ASN n 
1 224  MET n 
1 225  LEU n 
1 226  ILE n 
1 227  GLN n 
1 228  ARG n 
1 229  THR n 
1 230  HIS n 
1 231  TYR n 
1 232  SER n 
1 233  VAL n 
1 234  LYS n 
1 235  LYS n 
1 236  GLU n 
1 237  LEU n 
1 238  ALA n 
1 239  GLN n 
1 240  GLN n 
1 241  ARG n 
1 242  GLN n 
1 243  LEU n 
1 244  GLU n 
1 245  PHE n 
1 246  LEU n 
1 247  TRP n 
1 248  ARG n 
1 249  GLN n 
1 250  ILE n 
1 251  TRP n 
1 252  ASP n 
1 253  ASN n 
1 254  LYS n 
1 255  GLY n 
1 256  ASP n 
1 257  THR n 
1 258  ALA n 
1 259  LEU n 
1 260  PHE n 
1 261  THR n 
1 262  HIS n 
1 263  MET n 
1 264  MET n 
1 265  PRO n 
1 266  PHE n 
1 267  TYR n 
1 268  SER n 
1 269  TYR n 
1 270  ASP n 
1 271  ILE n 
1 272  PRO n 
1 273  HIS n 
1 274  THR n 
1 275  CYS n 
1 276  GLY n 
1 277  PRO n 
1 278  ASP n 
1 279  PRO n 
1 280  LYS n 
1 281  VAL n 
1 282  CYS n 
1 283  CYS n 
1 284  GLN n 
1 285  PHE n 
1 286  ASP n 
1 287  PHE n 
1 288  LYS n 
1 289  ARG n 
1 290  MET n 
1 291  GLY n 
1 292  SER n 
1 293  PHE n 
1 294  GLY n 
1 295  LEU n 
1 296  SER n 
1 297  CYS n 
1 298  PRO n 
1 299  TRP n 
1 300  LYS n 
1 301  VAL n 
1 302  PRO n 
1 303  PRO n 
1 304  ARG n 
1 305  THR n 
1 306  ILE n 
1 307  SER n 
1 308  ASP n 
1 309  GLN n 
1 310  ASN n 
1 311  VAL n 
1 312  ALA n 
1 313  ALA n 
1 314  ARG n 
1 315  SER n 
1 316  ASP n 
1 317  LEU n 
1 318  LEU n 
1 319  VAL n 
1 320  ASP n 
1 321  GLN n 
1 322  TRP n 
1 323  LYS n 
1 324  LYS n 
1 325  LYS n 
1 326  ALA n 
1 327  GLU n 
1 328  LEU n 
1 329  TYR n 
1 330  ARG n 
1 331  THR n 
1 332  ASN n 
1 333  VAL n 
1 334  LEU n 
1 335  LEU n 
1 336  ILE n 
1 337  PRO n 
1 338  LEU n 
1 339  GLY n 
1 340  ASP n 
1 341  ASN n 
1 342  PHE n 
1 343  ARG n 
1 344  PHE n 
1 345  LYS n 
1 346  GLN n 
1 347  ASN n 
1 348  THR n 
1 349  GLU n 
1 350  TRP n 
1 351  ASP n 
1 352  VAL n 
1 353  GLN n 
1 354  ARG n 
1 355  VAL n 
1 356  ASN n 
1 357  TYR n 
1 358  GLU n 
1 359  ARG n 
1 360  LEU n 
1 361  PHE n 
1 362  GLU n 
1 363  HIS n 
1 364  ILE n 
1 365  ASN n 
1 366  SER n 
1 367  GLN n 
1 368  ALA n 
1 369  HIS n 
1 370  PHE n 
1 371  ASN n 
1 372  VAL n 
1 373  GLN n 
1 374  ALA n 
1 375  GLN n 
1 376  PHE n 
1 377  GLY n 
1 378  THR n 
1 379  LEU n 
1 380  GLN n 
1 381  GLU n 
1 382  TYR n 
1 383  PHE n 
1 384  ASP n 
1 385  ALA n 
1 386  VAL n 
1 387  HIS n 
1 388  GLN n 
1 389  ALA n 
1 390  GLU n 
1 391  ARG n 
1 392  ALA n 
1 393  GLY n 
1 394  GLN n 
1 395  ALA n 
1 396  GLU n 
1 397  PHE n 
1 398  PRO n 
1 399  THR n 
1 400  LEU n 
1 401  SER n 
1 402  GLY n 
1 403  ASP n 
1 404  PHE n 
1 405  PHE n 
1 406  THR n 
1 407  TYR n 
1 408  ALA n 
1 409  ASP n 
1 410  ARG n 
1 411  SER n 
1 412  ASP n 
1 413  ASN n 
1 414  TYR n 
1 415  TRP n 
1 416  SER n 
1 417  GLY n 
1 418  TYR n 
1 419  TYR n 
1 420  THR n 
1 421  SER n 
1 422  ARG n 
1 423  PRO n 
1 424  TYR n 
1 425  HIS n 
1 426  LYS n 
1 427  ARG n 
1 428  MET n 
1 429  ASP n 
1 430  ARG n 
1 431  VAL n 
1 432  LEU n 
1 433  MET n 
1 434  HIS n 
1 435  TYR n 
1 436  VAL n 
1 437  ARG n 
1 438  ALA n 
1 439  ALA n 
1 440  GLU n 
1 441  MET n 
1 442  LEU n 
1 443  SER n 
1 444  ALA n 
1 445  TRP n 
1 446  HIS n 
1 447  SER n 
1 448  TRP n 
1 449  ASP n 
1 450  GLY n 
1 451  MET n 
1 452  ALA n 
1 453  ARG n 
1 454  ILE n 
1 455  GLU n 
1 456  GLU n 
1 457  ARG n 
1 458  LEU n 
1 459  GLU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  ARG n 
1 464  GLU n 
1 465  LEU n 
1 466  SER n 
1 467  LEU n 
1 468  PHE n 
1 469  GLN n 
1 470  HIS n 
1 471  HIS n 
1 472  ASP n 
1 473  GLY n 
1 474  ILE n 
1 475  THR n 
1 476  GLY n 
1 477  THR n 
1 478  ALA n 
1 479  LYS n 
1 480  THR n 
1 481  HIS n 
1 482  VAL n 
1 483  VAL n 
1 484  VAL n 
1 485  ASP n 
1 486  TYR n 
1 487  GLU n 
1 488  GLN n 
1 489  ARG n 
1 490  MET n 
1 491  GLN n 
1 492  GLU n 
1 493  ALA n 
1 494  LEU n 
1 495  LYS n 
1 496  ALA n 
1 497  CYS n 
1 498  GLN n 
1 499  MET n 
1 500  VAL n 
1 501  MET n 
1 502  GLN n 
1 503  GLN n 
1 504  SER n 
1 505  VAL n 
1 506  TYR n 
1 507  ARG n 
1 508  LEU n 
1 509  LEU n 
1 510  THR n 
1 511  LYS n 
1 512  PRO n 
1 513  SER n 
1 514  ILE n 
1 515  TYR n 
1 516  SER n 
1 517  PRO n 
1 518  ASP n 
1 519  PHE n 
1 520  SER n 
1 521  PHE n 
1 522  SER n 
1 523  TYR n 
1 524  PHE n 
1 525  THR n 
1 526  LEU n 
1 527  ASP n 
1 528  ASP n 
1 529  SER n 
1 530  ARG n 
1 531  TRP n 
1 532  PRO n 
1 533  GLY n 
1 534  SER n 
1 535  GLY n 
1 536  VAL n 
1 537  GLU n 
1 538  ASP n 
1 539  SER n 
1 540  ARG n 
1 541  THR n 
1 542  THR n 
1 543  ILE n 
1 544  ILE n 
1 545  LEU n 
1 546  GLY n 
1 547  GLU n 
1 548  ASP n 
1 549  ILE n 
1 550  LEU n 
1 551  PRO n 
1 552  SER n 
1 553  LYS n 
1 554  HIS n 
1 555  VAL n 
1 556  VAL n 
1 557  MET n 
1 558  HIS n 
1 559  ASN n 
1 560  THR n 
1 561  LEU n 
1 562  PRO n 
1 563  HIS n 
1 564  TRP n 
1 565  ARG n 
1 566  GLU n 
1 567  GLN n 
1 568  LEU n 
1 569  VAL n 
1 570  ASP n 
1 571  PHE n 
1 572  TYR n 
1 573  VAL n 
1 574  SER n 
1 575  SER n 
1 576  PRO n 
1 577  PHE n 
1 578  VAL n 
1 579  SER n 
1 580  VAL n 
1 581  THR n 
1 582  ASP n 
1 583  LEU n 
1 584  ALA n 
1 585  ASN n 
1 586  ASN n 
1 587  PRO n 
1 588  VAL n 
1 589  GLU n 
1 590  ALA n 
1 591  GLN n 
1 592  VAL n 
1 593  SER n 
1 594  PRO n 
1 595  VAL n 
1 596  TRP n 
1 597  SER n 
1 598  TRP n 
1 599  HIS n 
1 600  HIS n 
1 601  ASP n 
1 602  THR n 
1 603  LEU n 
1 604  THR n 
1 605  LYS n 
1 606  THR n 
1 607  ILE n 
1 608  HIS n 
1 609  PRO n 
1 610  GLN n 
1 611  GLY n 
1 612  SER n 
1 613  THR n 
1 614  THR n 
1 615  LYS n 
1 616  TYR n 
1 617  ARG n 
1 618  ILE n 
1 619  ILE n 
1 620  PHE n 
1 621  LYS n 
1 622  ALA n 
1 623  ARG n 
1 624  VAL n 
1 625  PRO n 
1 626  PRO n 
1 627  MET n 
1 628  GLY n 
1 629  LEU n 
1 630  ALA n 
1 631  THR n 
1 632  TYR n 
1 633  VAL n 
1 634  LEU n 
1 635  THR n 
1 636  ILE n 
1 637  SER n 
1 638  ASP n 
1 639  SER n 
1 640  LYS n 
1 641  PRO n 
1 642  GLU n 
1 643  HIS n 
1 644  THR n 
1 645  SER n 
1 646  TYR n 
1 647  ALA n 
1 648  SER n 
1 649  ASN n 
1 650  LEU n 
1 651  LEU n 
1 652  LEU n 
1 653  ARG n 
1 654  LYS n 
1 655  ASN n 
1 656  PRO n 
1 657  THR n 
1 658  SER n 
1 659  LEU n 
1 660  PRO n 
1 661  LEU n 
1 662  GLY n 
1 663  GLN n 
1 664  TYR n 
1 665  PRO n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LYS n 
1 670  PHE n 
1 671  GLY n 
1 672  ASP n 
1 673  PRO n 
1 674  ARG n 
1 675  GLU n 
1 676  ILE n 
1 677  SER n 
1 678  LEU n 
1 679  ARG n 
1 680  VAL n 
1 681  GLY n 
1 682  ASN n 
1 683  GLY n 
1 684  PRO n 
1 685  THR n 
1 686  LEU n 
1 687  ALA n 
1 688  PHE n 
1 689  SER n 
1 690  GLU n 
1 691  GLN n 
1 692  GLY n 
1 693  LEU n 
1 694  LEU n 
1 695  LYS n 
1 696  SER n 
1 697  ILE n 
1 698  GLN n 
1 699  LEU n 
1 700  THR n 
1 701  GLN n 
1 702  ASP n 
1 703  SER n 
1 704  PRO n 
1 705  HIS n 
1 706  VAL n 
1 707  PRO n 
1 708  VAL n 
1 709  HIS n 
1 710  PHE n 
1 711  LYS n 
1 712  PHE n 
1 713  LEU n 
1 714  LYS n 
1 715  TYR n 
1 716  GLY n 
1 717  VAL n 
1 718  ARG n 
1 719  SER n 
1 720  HIS n 
1 721  GLY n 
1 722  ASP n 
1 723  ARG n 
1 724  SER n 
1 725  GLY n 
1 726  ALA n 
1 727  TYR n 
1 728  LEU n 
1 729  PHE n 
1 730  LEU n 
1 731  PRO n 
1 732  ASN n 
1 733  GLY n 
1 734  PRO n 
1 735  ALA n 
1 736  SER n 
1 737  PRO n 
1 738  VAL n 
1 739  GLU n 
1 740  LEU n 
1 741  GLY n 
1 742  GLN n 
1 743  PRO n 
1 744  VAL n 
1 745  VAL n 
1 746  LEU n 
1 747  VAL n 
1 748  THR n 
1 749  LYS n 
1 750  GLY n 
1 751  LYS n 
1 752  LEU n 
1 753  GLU n 
1 754  SER n 
1 755  SER n 
1 756  VAL n 
1 757  SER n 
1 758  VAL n 
1 759  GLY n 
1 760  LEU n 
1 761  PRO n 
1 762  SER n 
1 763  VAL n 
1 764  VAL n 
1 765  HIS n 
1 766  GLN n 
1 767  THR n 
1 768  ILE n 
1 769  MET n 
1 770  ARG n 
1 771  GLY n 
1 772  GLY n 
1 773  ALA n 
1 774  PRO n 
1 775  GLU n 
1 776  ILE n 
1 777  ARG n 
1 778  ASN n 
1 779  LEU n 
1 780  VAL n 
1 781  ASP n 
1 782  ILE n 
1 783  GLY n 
1 784  SER n 
1 785  LEU n 
1 786  ASP n 
1 787  ASN n 
1 788  THR n 
1 789  GLU n 
1 790  ILE n 
1 791  VAL n 
1 792  MET n 
1 793  ARG n 
1 794  LEU n 
1 795  GLU n 
1 796  THR n 
1 797  HIS n 
1 798  ILE n 
1 799  ASP n 
1 800  SER n 
1 801  GLY n 
1 802  ASP n 
1 803  ILE n 
1 804  PHE n 
1 805  TYR n 
1 806  THR n 
1 807  ASP n 
1 808  LEU n 
1 809  ASN n 
1 810  GLY n 
1 811  LEU n 
1 812  GLN n 
1 813  PHE n 
1 814  ILE n 
1 815  LYS n 
1 816  ARG n 
1 817  ARG n 
1 818  ARG n 
1 819  LEU n 
1 820  ASP n 
1 821  LYS n 
1 822  LEU n 
1 823  PRO n 
1 824  LEU n 
1 825  GLN n 
1 826  ALA n 
1 827  ASN n 
1 828  TYR n 
1 829  TYR n 
1 830  PRO n 
1 831  ILE n 
1 832  PRO n 
1 833  SER n 
1 834  GLY n 
1 835  MET n 
1 836  PHE n 
1 837  ILE n 
1 838  GLU n 
1 839  ASP n 
1 840  ALA n 
1 841  ASN n 
1 842  THR n 
1 843  ARG n 
1 844  LEU n 
1 845  THR n 
1 846  LEU n 
1 847  LEU n 
1 848  THR n 
1 849  GLY n 
1 850  GLN n 
1 851  PRO n 
1 852  LEU n 
1 853  GLY n 
1 854  GLY n 
1 855  SER n 
1 856  SER n 
1 857  LEU n 
1 858  ALA n 
1 859  SER n 
1 860  GLY n 
1 861  GLU n 
1 862  LEU n 
1 863  GLU n 
1 864  ILE n 
1 865  MET n 
1 866  GLN n 
1 867  ASP n 
1 868  ARG n 
1 869  ARG n 
1 870  LEU n 
1 871  ALA n 
1 872  SER n 
1 873  ASP n 
1 874  ASP n 
1 875  GLU n 
1 876  ARG n 
1 877  GLY n 
1 878  LEU n 
1 879  GLY n 
1 880  GLN n 
1 881  GLY n 
1 882  VAL n 
1 883  LEU n 
1 884  ASP n 
1 885  ASN n 
1 886  LYS n 
1 887  PRO n 
1 888  VAL n 
1 889  LEU n 
1 890  HIS n 
1 891  ILE n 
1 892  TYR n 
1 893  ARG n 
1 894  LEU n 
1 895  VAL n 
1 896  LEU n 
1 897  GLU n 
1 898  LYS n 
1 899  VAL n 
1 900  ASN n 
1 901  ASN n 
1 902  CYS n 
1 903  VAL n 
1 904  ARG n 
1 905  PRO n 
1 906  SER n 
1 907  LYS n 
1 908  LEU n 
1 909  HIS n 
1 910  PRO n 
1 911  ALA n 
1 912  GLY n 
1 913  TYR n 
1 914  LEU n 
1 915  THR n 
1 916  SER n 
1 917  ALA n 
1 918  ALA n 
1 919  HIS n 
1 920  LYS n 
1 921  ALA n 
1 922  SER n 
1 923  GLN n 
1 924  SER n 
1 925  LEU n 
1 926  LEU n 
1 927  ASP n 
1 928  PRO n 
1 929  LEU n 
1 930  ASP n 
1 931  LYS n 
1 932  PHE n 
1 933  ILE n 
1 934  PHE n 
1 935  ALA n 
1 936  GLU n 
1 937  ASN n 
1 938  GLU n 
1 939  TRP n 
1 940  ILE n 
1 941  GLY n 
1 942  ALA n 
1 943  GLN n 
1 944  GLY n 
1 945  GLN n 
1 946  PHE n 
1 947  GLY n 
1 948  GLY n 
1 949  ASP n 
1 950  HIS n 
1 951  PRO n 
1 952  SER n 
1 953  ALA n 
1 954  ARG n 
1 955  GLU n 
1 956  ASP n 
1 957  LEU n 
1 958  ASP n 
1 959  VAL n 
1 960  SER n 
1 961  VAL n 
1 962  MET n 
1 963  ARG n 
1 964  ARG n 
1 965  LEU n 
1 966  THR n 
1 967  LYS n 
1 968  SER n 
1 969  SER n 
1 970  ALA n 
1 971  LYS n 
1 972  THR n 
1 973  GLN n 
1 974  ARG n 
1 975  VAL n 
1 976  GLY n 
1 977  TYR n 
1 978  VAL n 
1 979  LEU n 
1 980  HIS n 
1 981  ARG n 
1 982  THR n 
1 983  ASN n 
1 984  LEU n 
1 985  MET n 
1 986  GLN n 
1 987  CYS n 
1 988  GLY n 
1 989  THR n 
1 990  PRO n 
1 991  GLU n 
1 992  GLU n 
1 993  HIS n 
1 994  THR n 
1 995  GLN n 
1 996  LYS n 
1 997  LEU n 
1 998  ASP n 
1 999  VAL n 
1 1000 CYS n 
1 1001 HIS n 
1 1002 LEU n 
1 1003 LEU n 
1 1004 PRO n 
1 1005 ASN n 
1 1006 VAL n 
1 1007 ALA n 
1 1008 ARG n 
1 1009 CYS n 
1 1010 GLU n 
1 1011 ARG n 
1 1012 THR n 
1 1013 THR n 
1 1014 LEU n 
1 1015 THR n 
1 1016 PHE n 
1 1017 LEU n 
1 1018 GLN n 
1 1019 ASN n 
1 1020 LEU n 
1 1021 GLU n 
1 1022 HIS n 
1 1023 LEU n 
1 1024 ASP n 
1 1025 GLY n 
1 1026 MET n 
1 1027 VAL n 
1 1028 ALA n 
1 1029 PRO n 
1 1030 GLU n 
1 1031 VAL n 
1 1032 CYS n 
1 1033 PRO n 
1 1034 MET n 
1 1035 GLU n 
1 1036 THR n 
1 1037 ALA n 
1 1038 ALA n 
1 1039 TYR n 
1 1040 VAL n 
1 1041 SER n 
1 1042 SER n 
1 1043 HIS n 
1 1044 SER n 
1 1045 SER 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               'fruit fly' 
_entity_src_gen.gene_src_genus                     Drosophila 
_entity_src_gen.pdbx_gene_src_gene                 'ALPHA-MAN-II OR GMII OR CG18474/CG18802/CG8139' 
_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      'Drosophila melanogaster' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     7227 
_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               'fruit fly' 
_entity_src_gen.pdbx_host_org_scientific_name      'Drosophila melanogaster' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7227 
_entity_src_gen.host_org_genus                     Drosophila 
_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               S2 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MAN2_DROME 
_struct_ref.pdbx_db_accession          Q24451 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHKLKVFVVPHSHND
PGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEFVTGGWVMPDEAN
SHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQRQLEFLWRQIWD
NKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVDQWKKKAELYRTN
VLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTLSGDFFTYADRSD
NYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKTHVVVDYEQRMQE
ALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNTLPHWREQLVDFY
VSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSKPEHTSYASNLLL
RKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSHGDRSGAYLFLPN
GPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDSGDIFYTDLNGLQ
FIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQGVLDNKPVLHIY
RLVLEKVNNCVRPSELHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVSVMRRLTKSSAKT
QRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYVSSHSS
;
_struct_ref.pdbx_align_begin           76 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              1QWU 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 13 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 1045 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q24451 
_struct_ref_seq.db_align_beg                  76 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1108 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       13 
_struct_ref_seq.pdbx_auth_seq_align_end       1045 
# 
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 1QWU ARG A 1   ? UNP Q24451 ?   ?   'CLONING ARTIFACT' 1   1  
1 1QWU SER A 2   ? UNP Q24451 ?   ?   'CLONING ARTIFACT' 2   2  
1 1QWU SER A 3   ? UNP Q24451 ?   ?   'CLONING ARTIFACT' 3   3  
1 1QWU HIS A 4   ? UNP Q24451 ?   ?   'EXPRESSION TAG'   4   4  
1 1QWU HIS A 5   ? UNP Q24451 ?   ?   'EXPRESSION TAG'   5   5  
1 1QWU HIS A 6   ? UNP Q24451 ?   ?   'EXPRESSION TAG'   6   6  
1 1QWU HIS A 7   ? UNP Q24451 ?   ?   'EXPRESSION TAG'   7   7  
1 1QWU HIS A 8   ? UNP Q24451 ?   ?   'EXPRESSION TAG'   8   8  
1 1QWU HIS A 9   ? UNP Q24451 ?   ?   'EXPRESSION TAG'   9   9  
1 1QWU GLY A 10  ? UNP Q24451 ?   ?   'CLONING ARTIFACT' 10  10 
1 1QWU GLU A 11  ? UNP Q24451 ?   ?   'CLONING ARTIFACT' 11  11 
1 1QWU PHE A 12  ? UNP Q24451 ?   ?   'CLONING ARTIFACT' 12  12 
1 1QWU ASN A 341 ? UNP Q24451 ASP 404 ENGINEERED         341 13 
1 1QWU LYS A 907 ? UNP Q24451 GLU 970 'SEE REMARK 999'   907 14 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                            ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                           ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                         ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                    ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                           ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                          ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                    ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                            ? 'C2 H5 N O2'     75.067  
GUL non-polymer         . '5-FLUORO-BETA-L-GULOSYL FLUORIDE' ? 'C6 H10 F2 O5'   200.137 
HIS 'L-peptide linking' y HISTIDINE                          ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                              ? 'H2 O'           18.015  
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 
MPD non-polymer         . '(4S)-2-METHYL-2,4-PENTANEDIOL'    ? 'C6 H14 O2'      118.174 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE             ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE                      ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                            ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                             ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                          ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                         ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                           ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                             ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'                         ? 'Zn 2'           65.409  
# 
_exptl.entry_id          1QWU 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.19 
_exptl_crystal.density_percent_sol   43.83 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7 
_exptl_crystal_grow.pdbx_details    'PEG 6000, MPD, Tris, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   ? 
_diffrn_detector.details                Osmic 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'focussing mirrors' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU RU200' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
# 
_reflns.entry_id                     1QWU 
_reflns.observed_criterion_sigma_I   2.0 
_reflns.observed_criterion_sigma_F   2.9 
_reflns.d_resolution_low             20 
_reflns.d_resolution_high            2.0 
_reflns.number_obs                   66355 
_reflns.number_all                   68690 
_reflns.percent_possible_obs         96.6 
_reflns.pdbx_Rmerge_I_obs            0.11 
_reflns.pdbx_Rsym_value              0.11 
_reflns.pdbx_netI_over_sigmaI        16.8 
_reflns.B_iso_Wilson_estimate        7.5 
_reflns.pdbx_redundancy              7 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.03 
_reflns_shell.d_res_low              2.16 
_reflns_shell.percent_possible_all   92.4 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      10064 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 1QWU 
_refine.ls_number_reflns_obs                     66355 
_refine.ls_number_reflns_all                     68690 
_refine.pdbx_ls_sigma_I                          0.0 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.84 
_refine.ls_d_res_high                            2.03 
_refine.ls_percent_reflns_obs                    96.6 
_refine.ls_R_factor_obs                          0.151 
_refine.ls_R_factor_all                          0.16 
_refine.ls_R_factor_R_work                       0.151 
_refine.ls_R_factor_R_free                       0.189 
_refine.ls_R_factor_R_free_error                 0.004 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 3.5 
_refine.ls_number_reflns_R_free                  2336 
_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                               16.9 
_refine.aniso_B[1][1]                            0.28 
_refine.aniso_B[2][2]                            0.97 
_refine.aniso_B[3][3]                            -1.25 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.338431 
_refine.solvent_model_param_bsol                 46.5168 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      1HTY 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        1QWU 
_refine_analyze.Luzzati_coordinate_error_obs    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   0.21 
_refine_analyze.Luzzati_sigma_a_free            0.16 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8181 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         35 
_refine_hist.number_atoms_solvent             1025 
_refine_hist.number_atoms_total               9241 
_refine_hist.d_res_high                       2.03 
_refine_hist.d_res_low                        19.84 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d                0.015 ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_na             ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_prot           ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d               ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_na            ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_prot          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg             1.7   ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      24.9  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      1.07  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             1.08  1.50 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            1.63  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             1.79  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            2.59  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       2.03 
_refine_ls_shell.d_res_low                        2.16 
_refine_ls_shell.number_reflns_R_work             10064 
_refine_ls_shell.R_factor_R_work                  0.181 
_refine_ls_shell.percent_reflns_obs               92.4 
_refine_ls_shell.R_factor_R_free                  0.206 
_refine_ls_shell.R_factor_R_free_error            0.011 
_refine_ls_shell.percent_reflns_R_free            3.5 
_refine_ls_shell.number_reflns_R_free             361 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_all                     ? 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 PROTEIN_REP.PRO    PROTEIN_REP.TOP  'X-RAY DIFFRACTION' 
2 CARBOHYDRATE.PARAM CARBOHYDRATE.TOP 'X-RAY DIFFRACTION' 
3 CIS_PEPTIDE.PARAM  CIS_PEPTIDE.TOP  'X-RAY DIFFRACTION' 
4 WATER_REP.PARAM    WATER_REP.TOP    'X-RAY DIFFRACTION' 
5 ION.PARAM          ION.TOP          'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  1QWU 
_struct.title                     'Golgi alpha-mannosidase II D341N mutant complex with 5-F-guloside' 
_struct.pdbx_descriptor           'Alpha-mannosidase II (E.C.3.2.1.114)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1QWU 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'glycosyl hydrolase family 38, covalent catalytic intermediate, HYDROLASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_biol.id   1 
# 
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  1  MET A 45   ? MET A 52   ? MET A 45   MET A 52   1 ? 8  
HELX_P HELX_P2  2  ASP A 71   ? TYR A 75   ? ASP A 71   TYR A 75   5 ? 5  
HELX_P HELX_P3  3  THR A 98   ? ASP A 106  ? THR A 98   ASP A 106  1 ? 9  
HELX_P HELX_P4  4  ASP A 106  ? ASN A 121  ? ASP A 106  ASN A 121  1 ? 16 
HELX_P HELX_P5  5  GLU A 130  ? LEU A 141  ? GLU A 130  LEU A 141  1 ? 12 
HELX_P HELX_P6  6  GLY A 142  ? ASN A 155  ? GLY A 142  ASN A 155  1 ? 14 
HELX_P HELX_P7  7  HIS A 174  ? ASN A 194  ? HIS A 174  ASN A 194  1 ? 21 
HELX_P HELX_P8  8  PRO A 210  ? LYS A 218  ? PRO A 210  LYS A 218  1 ? 9  
HELX_P HELX_P9  9  HIS A 230  ? GLN A 240  ? HIS A 230  GLN A 240  1 ? 11 
HELX_P HELX_P10 10 ASP A 270  ? THR A 274  ? ASP A 270  THR A 274  5 ? 5  
HELX_P HELX_P11 11 ASP A 278  ? CYS A 283  ? ASP A 278  CYS A 283  1 ? 6  
HELX_P HELX_P12 12 GLN A 284  ? ASP A 286  ? GLN A 284  ASP A 286  5 ? 3  
HELX_P HELX_P13 13 ASN A 310  ? GLU A 327  ? ASN A 310  GLU A 327  1 ? 18 
HELX_P HELX_P14 14 GLN A 346  ? GLN A 367  ? GLN A 346  GLN A 367  1 ? 22 
HELX_P HELX_P15 15 ALA A 368  ? PHE A 370  ? ALA A 368  PHE A 370  5 ? 3  
HELX_P HELX_P16 16 THR A 378  ? ALA A 392  ? THR A 378  ALA A 392  1 ? 15 
HELX_P HELX_P17 17 SER A 416  ? THR A 420  ? SER A 416  THR A 420  5 ? 5  
HELX_P HELX_P18 18 ARG A 422  ? TRP A 445  ? ARG A 422  TRP A 445  1 ? 24 
HELX_P HELX_P19 19 ASP A 449  ? ALA A 452  ? ASP A 449  ALA A 452  5 ? 4  
HELX_P HELX_P20 20 ARG A 453  ? GLN A 469  ? ARG A 453  GLN A 469  1 ? 17 
HELX_P HELX_P21 21 LYS A 479  ? LEU A 509  ? LYS A 479  LEU A 509  1 ? 31 
HELX_P HELX_P22 22 PRO A 823  ? TYR A 828  ? PRO A 823  TYR A 828  5 ? 6  
HELX_P HELX_P23 23 THR A 915  ? ASP A 927  ? THR A 915  ASP A 927  1 ? 13 
HELX_P HELX_P24 24 ASP A 998  ? LEU A 1002 ? ASP A 998  LEU A 1002 5 ? 5  
HELX_P HELX_P25 25 ASP A 1024 ? VAL A 1027 ? ASP A 1024 VAL A 1027 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1 disulf ? ? A CYS 31   SG  ? ? ? 1_555 A CYS 1032 SG  ? ? A CYS 31   A CYS 1032 1_555 ? ? ? ? ? ? ? 2.020 ? 
disulf2 disulf ? ? A CYS 275  SG  ? ? ? 1_555 A CYS 282  SG  ? ? A CYS 275  A CYS 282  1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf3 disulf ? ? A CYS 283  SG  ? ? ? 1_555 A CYS 297  SG  ? ? A CYS 283  A CYS 297  1_555 ? ? ? ? ? ? ? 2.051 ? 
disulf4 disulf ? ? A CYS 902  SG  ? ? ? 1_555 A CYS 987  SG  ? ? A CYS 902  A CYS 987  1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf5 disulf ? ? A CYS 1000 SG  ? ? ? 1_555 A CYS 1009 SG  ? ? A CYS 1000 A CYS 1009 1_555 ? ? ? ? ? ? ? 1.996 ? 
covale1 covale ? ? A ASN 194  ND2 ? ? ? 1_555 B NAG .    C1  ? ? A ASN 194  A NAG 2001 1_555 ? ? ? ? ? ? ? 1.458 ? 
covale2 covale ? ? A ASP 204  OD1 ? ? ? 1_555 D GUL .    C1  ? ? A ASP 204  A GUL 2003 1_555 ? ? ? ? ? ? ? 1.379 ? 
metalc1 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 A HIS 90   NE2 ? ? A ZN  2004 A HIS 90   1_555 ? ? ? ? ? ? ? 2.092 ? 
metalc2 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 D GUL .    O2  ? ? A ZN  2004 A GUL 2003 1_555 ? ? ? ? ? ? ? 2.340 ? 
metalc3 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 A ASP 92   OD1 ? ? A ZN  2004 A ASP 92   1_555 ? ? ? ? ? ? ? 2.014 ? 
metalc4 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 A HIS 471  NE2 ? ? A ZN  2004 A HIS 471  1_555 ? ? ? ? ? ? ? 2.181 ? 
metalc5 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 D GUL .    O3  ? ? A ZN  2004 A GUL 2003 1_555 ? ? ? ? ? ? ? 2.142 ? 
metalc6 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 A ASP 204  OD1 ? ? A ZN  2004 A ASP 204  1_555 ? ? ? ? ? ? ? 2.653 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 405 A . ? PHE 405 A THR 406 A ? THR 406 A 1 0.86 
2 TRP 531 A . ? TRP 531 A PRO 532 A ? PRO 532 A 1 0.47 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 6  ? 
B ? 3  ? 
C ? 2  ? 
D ? 2  ? 
E ? 6  ? 
F ? 5  ? 
G ? 5  ? 
H ? 12 ? 
I ? 5  ? 
J ? 8  ? 
K ? 5  ? 
# 
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 
A 1  2  ? parallel      
A 2  3  ? parallel      
A 3  4  ? anti-parallel 
A 4  5  ? parallel      
A 5  6  ? parallel      
B 1  2  ? parallel      
B 2  3  ? parallel      
C 1  2  ? parallel      
D 1  2  ? anti-parallel 
E 1  2  ? anti-parallel 
E 2  3  ? anti-parallel 
E 3  4  ? anti-parallel 
E 4  5  ? anti-parallel 
E 5  6  ? anti-parallel 
F 1  2  ? anti-parallel 
F 2  3  ? anti-parallel 
F 3  4  ? anti-parallel 
F 4  5  ? anti-parallel 
G 1  2  ? parallel      
G 2  3  ? anti-parallel 
G 3  4  ? anti-parallel 
G 4  5  ? parallel      
H 1  2  ? parallel      
H 2  3  ? anti-parallel 
H 3  4  ? anti-parallel 
H 4  5  ? anti-parallel 
H 5  6  ? anti-parallel 
H 6  7  ? anti-parallel 
H 7  8  ? anti-parallel 
H 8  9  ? anti-parallel 
H 9  10 ? anti-parallel 
H 10 11 ? anti-parallel 
H 11 12 ? anti-parallel 
I 1  2  ? anti-parallel 
I 2  3  ? anti-parallel 
I 3  4  ? anti-parallel 
I 4  5  ? anti-parallel 
J 1  2  ? anti-parallel 
J 2  3  ? anti-parallel 
J 3  4  ? anti-parallel 
J 4  5  ? anti-parallel 
J 5  6  ? anti-parallel 
J 6  7  ? anti-parallel 
J 7  8  ? anti-parallel 
K 1  2  ? anti-parallel 
K 2  3  ? anti-parallel 
K 3  4  ? anti-parallel 
K 4  5  ? 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 
A 1  VAL A 43   ? GLN A 44   ? VAL A 43   GLN A 44   
A 2  THR A 399  ? SER A 401  ? THR A 399  SER A 401  
A 3  GLU A 244  ? TRP A 247  ? GLU A 244  TRP A 247  
A 4  LEU A 259  ? MET A 263  ? LEU A 259  MET A 263  
A 5  ASN A 223  ? ILE A 226  ? ASN A 223  ILE A 226  
A 6  ALA A 199  ? ALA A 202  ? ALA A 199  ALA A 202  
B 1  VAL A 333  ? ASN A 341  ? VAL A 333  ASN A 341  
B 2  LEU A 81   ? HIS A 90   ? LEU A 81   HIS A 90   
B 3  VAL A 372  ? PHE A 376  ? VAL A 372  PHE A 376  
C 1  PHE A 126  ? TRP A 128  ? PHE A 126  TRP A 128  
C 2  LEU A 158  ? PHE A 160  ? LEU A 158  PHE A 160  
D 1  ALA A 408  ? ARG A 410  ? ALA A 408  ARG A 410  
D 2  ASN A 413  ? TYR A 414  ? ASN A 413  TYR A 414  
E 1  PHE A 524  ? ASP A 527  ? PHE A 524  ASP A 527  
E 2  ASP A 930  ? PHE A 934  ? ASP A 930  PHE A 934  
E 3  SER A 552  ? ASN A 559  ? SER A 552  ASN A 559  
E 4  GLY A 628  ? ILE A 636  ? GLY A 628  ILE A 636  
E 5  VAL A 578  ? ASP A 582  ? VAL A 578  ASP A 582  
E 6  PRO A 587  ? VAL A 588  ? PRO A 587  VAL A 588  
F 1  PHE A 524  ? ASP A 527  ? PHE A 524  ASP A 527  
F 2  ASP A 930  ? PHE A 934  ? ASP A 930  PHE A 934  
F 3  SER A 552  ? ASN A 559  ? SER A 552  ASN A 559  
F 4  GLY A 628  ? ILE A 636  ? GLY A 628  ILE A 636  
F 5  GLN A 945  ? PHE A 946  ? GLN A 945  PHE A 946  
G 1  THR A 542  ? ILE A 543  ? THR A 542  ILE A 543  
G 2  ARG A 565  ? VAL A 573  ? ARG A 565  VAL A 573  
G 3  THR A 606  ? VAL A 624  ? THR A 606  VAL A 624  
G 4  ALA A 590  ? ASP A 601  ? ALA A 590  ASP A 601  
G 5  THR A 644  ? TYR A 646  ? THR A 644  TYR A 646  
H 1  LYS A 669  ? GLY A 671  ? LYS A 669  GLY A 671  
H 2  SER A 648  ? LEU A 652  ? SER A 648  LEU A 652  
H 3  VAL A 745  ? LYS A 749  ? VAL A 745  LYS A 749  
H 4  SER A 754  ? LEU A 760  ? SER A 754  LEU A 760  
H 5  VAL A 763  ? MET A 769  ? VAL A 763  MET A 769  
H 6  GLU A 775  ? VAL A 780  ? GLU A 775  VAL A 780  
H 7  VAL A 888  ? LYS A 898  ? VAL A 888  LYS A 898  
H 8  THR A 842  ? THR A 848  ? THR A 842  THR A 848  
H 9  GLY A 834  ? GLU A 838  ? GLY A 834  GLU A 838  
H 10 ILE A 803  ? LEU A 808  ? ILE A 803  LEU A 808  
H 11 GLN A 812  ? ARG A 817  ? GLN A 812  ARG A 817  
H 12 ALA A 911  ? GLY A 912  ? ALA A 911  GLY A 912  
I 1  ILE A 676  ? ARG A 679  ? ILE A 676  ARG A 679  
I 2  THR A 685  ? PHE A 688  ? THR A 685  PHE A 688  
I 3  LEU A 694  ? GLN A 698  ? LEU A 694  GLN A 698  
I 4  VAL A 706  ? TYR A 715  ? VAL A 706  TYR A 715  
I 5  SER A 736  ? PRO A 737  ? SER A 736  PRO A 737  
J 1  ILE A 676  ? ARG A 679  ? ILE A 676  ARG A 679  
J 2  THR A 685  ? PHE A 688  ? THR A 685  PHE A 688  
J 3  LEU A 694  ? GLN A 698  ? LEU A 694  GLN A 698  
J 4  VAL A 706  ? TYR A 715  ? VAL A 706  TYR A 715  
J 5  THR A 788  ? THR A 796  ? THR A 788  THR A 796  
J 6  GLU A 861  ? ARG A 869  ? GLU A 861  ARG A 869  
J 7  LEU A 852  ? SER A 855  ? LEU A 852  SER A 855  
J 8  TYR A 829  ? ILE A 831  ? TYR A 829  ILE A 831  
K 1  LEU A 957  ? ARG A 964  ? LEU A 957  ARG A 964  
K 2  GLN A 973  ? ARG A 981  ? GLN A 973  ARG A 981  
K 3  THR A 1036 ? HIS A 1043 ? THR A 1036 HIS A 1043 
K 4  VAL A 1006 ? THR A 1012 ? VAL A 1006 THR A 1012 
K 5  ASN A 1019 ? HIS A 1022 ? ASN A 1019 HIS A 1022 
# 
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 
A 1  2  N VAL A 43   ? N VAL A 43   O THR A 399  ? O THR A 399  
A 2  3  O LEU A 400  ? O LEU A 400  N LEU A 246  ? N LEU A 246  
A 3  4  N PHE A 245  ? N PHE A 245  O THR A 261  ? O THR A 261  
A 4  5  O HIS A 262  ? O HIS A 262  N MET A 224  ? N MET A 224  
A 5  6  O ASN A 223  ? O ASN A 223  N SER A 200  ? N SER A 200  
B 1  2  O LEU A 334  ? O LEU A 334  N LYS A 82   ? N LYS A 82   
B 2  3  N VAL A 83   ? N VAL A 83   O GLN A 373  ? O GLN A 373  
C 1  2  N PHE A 126  ? N PHE A 126  O GLU A 159  ? O GLU A 159  
D 1  2  N ARG A 410  ? N ARG A 410  O ASN A 413  ? O ASN A 413  
E 1  2  N THR A 525  ? N THR A 525  O ILE A 933  ? O ILE A 933  
E 2  3  O PHE A 932  ? O PHE A 932  N VAL A 556  ? N VAL A 556  
E 3  4  N VAL A 555  ? N VAL A 555  O TYR A 632  ? O TYR A 632  
E 4  5  O VAL A 633  ? O VAL A 633  N THR A 581  ? N THR A 581  
E 5  6  N VAL A 580  ? N VAL A 580  O VAL A 588  ? O VAL A 588  
F 1  2  N THR A 525  ? N THR A 525  O ILE A 933  ? O ILE A 933  
F 2  3  O PHE A 932  ? O PHE A 932  N VAL A 556  ? N VAL A 556  
F 3  4  N VAL A 555  ? N VAL A 555  O TYR A 632  ? O TYR A 632  
F 4  5  N LEU A 629  ? N LEU A 629  O PHE A 946  ? O PHE A 946  
G 1  2  N ILE A 543  ? N ILE A 543  O TYR A 572  ? O TYR A 572  
G 2  3  N PHE A 571  ? N PHE A 571  O ILE A 618  ? O ILE A 618  
G 3  4  O ILE A 619  ? O ILE A 619  N GLN A 591  ? N GLN A 591  
G 4  5  N VAL A 592  ? N VAL A 592  O SER A 645  ? O SER A 645  
H 1  2  O LYS A 669  ? O LYS A 669  N LEU A 651  ? N LEU A 651  
H 2  3  N LEU A 652  ? N LEU A 652  O VAL A 745  ? O VAL A 745  
H 3  4  N LEU A 746  ? N LEU A 746  O SER A 757  ? O SER A 757  
H 4  5  N SER A 754  ? N SER A 754  O MET A 769  ? O MET A 769  
H 5  6  N ILE A 768  ? N ILE A 768  O GLU A 775  ? O GLU A 775  
H 6  7  N VAL A 780  ? N VAL A 780  O VAL A 888  ? O VAL A 888  
H 7  8  O VAL A 895  ? O VAL A 895  N THR A 845  ? N THR A 845  
H 8  9  O LEU A 846  ? O LEU A 846  N MET A 835  ? N MET A 835  
H 9  10 O PHE A 836  ? O PHE A 836  N TYR A 805  ? N TYR A 805  
H 10 11 N PHE A 804  ? N PHE A 804  O ARG A 816  ? O ARG A 816  
H 11 12 N PHE A 813  ? N PHE A 813  O GLY A 912  ? O GLY A 912  
I 1  2  N ILE A 676  ? N ILE A 676  O PHE A 688  ? O PHE A 688  
I 2  3  N ALA A 687  ? N ALA A 687  O LYS A 695  ? O LYS A 695  
I 3  4  N ILE A 697  ? N ILE A 697  O VAL A 706  ? O VAL A 706  
I 4  5  N LYS A 714  ? N LYS A 714  O SER A 736  ? O SER A 736  
J 1  2  N ILE A 676  ? N ILE A 676  O PHE A 688  ? O PHE A 688  
J 2  3  N ALA A 687  ? N ALA A 687  O LYS A 695  ? O LYS A 695  
J 3  4  N ILE A 697  ? N ILE A 697  O VAL A 706  ? O VAL A 706  
J 4  5  N LYS A 711  ? N LYS A 711  O ARG A 793  ? O ARG A 793  
J 5  6  N ILE A 790  ? N ILE A 790  O GLN A 866  ? O GLN A 866  
J 6  7  O GLU A 863  ? O GLU A 863  N SER A 855  ? N SER A 855  
J 7  8  O LEU A 852  ? O LEU A 852  N ILE A 831  ? N ILE A 831  
K 1  2  N ARG A 963  ? N ARG A 963  O GLY A 976  ? O GLY A 976  
K 2  3  N LEU A 979  ? N LEU A 979  O ALA A 1037 ? O ALA A 1037 
K 3  4  O SER A 1042 ? O SER A 1042 N ARG A 1008 ? N ARG A 1008 
K 4  5  N ARG A 1011 ? N ARG A 1011 O LEU A 1020 ? O LEU A 1020 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG A 2001' 
AC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN A 2004'  
AC3 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE GUL A 2003' 
AC4 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MPD A 2002' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 2  ASN A 194 ? ASN A 194  . ? 1_555 ? 
2  AC1 2  HOH F .   ? HOH A 2675 . ? 1_555 ? 
3  AC2 5  HIS A 90  ? HIS A 90   . ? 1_555 ? 
4  AC2 5  ASP A 92  ? ASP A 92   . ? 1_555 ? 
5  AC2 5  ASP A 204 ? ASP A 204  . ? 1_555 ? 
6  AC2 5  HIS A 471 ? HIS A 471  . ? 1_555 ? 
7  AC2 5  GUL D .   ? GUL A 2003 . ? 1_555 ? 
8  AC3 14 HIS A 90  ? HIS A 90   . ? 1_555 ? 
9  AC3 14 ASP A 92  ? ASP A 92   . ? 1_555 ? 
10 AC3 14 TRP A 95  ? TRP A 95   . ? 1_555 ? 
11 AC3 14 ASP A 204 ? ASP A 204  . ? 1_555 ? 
12 AC3 14 PHE A 206 ? PHE A 206  . ? 1_555 ? 
13 AC3 14 ARG A 228 ? ARG A 228  . ? 1_555 ? 
14 AC3 14 TYR A 269 ? TYR A 269  . ? 1_555 ? 
15 AC3 14 TRP A 415 ? TRP A 415  . ? 1_555 ? 
16 AC3 14 HIS A 471 ? HIS A 471  . ? 1_555 ? 
17 AC3 14 ASP A 472 ? ASP A 472  . ? 1_555 ? 
18 AC3 14 TYR A 727 ? TYR A 727  . ? 1_555 ? 
19 AC3 14 ARG A 876 ? ARG A 876  . ? 1_555 ? 
20 AC3 14 ZN  C .   ? ZN  A 2004 . ? 1_555 ? 
21 AC3 14 HOH F .   ? HOH A 2875 . ? 1_555 ? 
22 AC4 7  LYS A 63  ? LYS A 63   . ? 1_555 ? 
23 AC4 7  GLN A 64  ? GLN A 64   . ? 1_555 ? 
24 AC4 7  HIS A 273 ? HIS A 273  . ? 1_555 ? 
25 AC4 7  HOH F .   ? HOH A 2153 . ? 1_555 ? 
26 AC4 7  HOH F .   ? HOH A 2621 . ? 1_555 ? 
27 AC4 7  HOH F .   ? HOH A 2695 . ? 1_555 ? 
28 AC4 7  HOH F .   ? HOH A 2843 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1QWU 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1QWU 
_atom_sites.fract_transf_matrix[1][1]   0.014524 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009108 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.007206 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
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   . CYS A 1 31   ? 44.246 35.992  -18.713 1.00 21.89 ? 31   CYS A N   1 
ATOM   2    C  CA  . CYS A 1 31   ? 43.510 37.305  -18.531 1.00 21.32 ? 31   CYS A CA  1 
ATOM   3    C  C   . CYS A 1 31   ? 42.012 37.148  -18.688 1.00 21.56 ? 31   CYS A C   1 
ATOM   4    O  O   . CYS A 1 31   ? 41.563 36.676  -19.729 1.00 21.31 ? 31   CYS A O   1 
ATOM   5    C  CB  . CYS A 1 31   ? 43.900 38.359  -19.570 1.00 20.43 ? 31   CYS A CB  1 
ATOM   6    S  SG  . CYS A 1 31   ? 45.530 39.142  -19.483 1.00 21.58 ? 31   CYS A SG  1 
ATOM   7    N  N   . GLN A 1 32   ? 41.246 37.578  -17.683 1.00 21.32 ? 32   GLN A N   1 
ATOM   8    C  CA  . GLN A 1 32   ? 39.780 37.533  -17.756 1.00 21.89 ? 32   GLN A CA  1 
ATOM   9    C  C   . GLN A 1 32   ? 39.282 38.471  -18.870 1.00 20.75 ? 32   GLN A C   1 
ATOM   10   O  O   . GLN A 1 32   ? 39.916 39.484  -19.214 1.00 19.43 ? 32   GLN A O   1 
ATOM   11   C  CB  . GLN A 1 32   ? 39.127 38.037  -16.474 1.00 23.62 ? 32   GLN A CB  1 
ATOM   12   C  CG  . GLN A 1 32   ? 39.174 37.171  -15.253 1.00 28.28 ? 32   GLN A CG  1 
ATOM   13   C  CD  . GLN A 1 32   ? 38.170 37.677  -14.222 1.00 30.74 ? 32   GLN A CD  1 
ATOM   14   O  OE1 . GLN A 1 32   ? 36.978 37.354  -14.291 1.00 32.99 ? 32   GLN A OE1 1 
ATOM   15   N  NE2 . GLN A 1 32   ? 38.637 38.505  -13.284 1.00 31.66 ? 32   GLN A NE2 1 
ATOM   16   N  N   . ASP A 1 33   ? 38.112 38.153  -19.385 1.00 19.83 ? 33   ASP A N   1 
ATOM   17   C  CA  . ASP A 1 33   ? 37.492 38.934  -20.443 1.00 19.84 ? 33   ASP A CA  1 
ATOM   18   C  C   . ASP A 1 33   ? 36.602 39.916  -19.678 1.00 18.83 ? 33   ASP A C   1 
ATOM   19   O  O   . ASP A 1 33   ? 35.716 39.504  -18.946 1.00 20.74 ? 33   ASP A O   1 
ATOM   20   C  CB  . ASP A 1 33   ? 36.674 37.990  -21.328 1.00 20.39 ? 33   ASP A CB  1 
ATOM   21   C  CG  . ASP A 1 33   ? 36.030 38.690  -22.495 1.00 22.19 ? 33   ASP A CG  1 
ATOM   22   O  OD1 . ASP A 1 33   ? 35.911 38.056  -23.564 1.00 23.69 ? 33   ASP A OD1 1 
ATOM   23   O  OD2 . ASP A 1 33   ? 35.621 39.859  -22.354 1.00 22.31 ? 33   ASP A OD2 1 
ATOM   24   N  N   . VAL A 1 34   ? 36.828 41.212  -19.841 1.00 15.85 ? 34   VAL A N   1 
ATOM   25   C  CA  . VAL A 1 34   ? 36.067 42.175  -19.060 1.00 13.38 ? 34   VAL A CA  1 
ATOM   26   C  C   . VAL A 1 34   ? 34.877 42.741  -19.812 1.00 13.99 ? 34   VAL A C   1 
ATOM   27   O  O   . VAL A 1 34   ? 34.153 43.625  -19.315 1.00 11.91 ? 34   VAL A O   1 
ATOM   28   C  CB  . VAL A 1 34   ? 37.000 43.308  -18.585 1.00 13.49 ? 34   VAL A CB  1 
ATOM   29   C  CG1 . VAL A 1 34   ? 38.210 42.700  -17.876 1.00 12.07 ? 34   VAL A CG1 1 
ATOM   30   C  CG2 . VAL A 1 34   ? 37.496 44.136  -19.768 1.00 11.56 ? 34   VAL A CG2 1 
ATOM   31   N  N   . VAL A 1 35   ? 34.661 42.208  -21.010 1.00 12.04 ? 35   VAL A N   1 
ATOM   32   C  CA  . VAL A 1 35   ? 33.581 42.675  -21.854 1.00 12.15 ? 35   VAL A CA  1 
ATOM   33   C  C   . VAL A 1 35   ? 32.391 41.722  -22.026 1.00 12.74 ? 35   VAL A C   1 
ATOM   34   O  O   . VAL A 1 35   ? 31.245 42.087  -21.789 1.00 12.85 ? 35   VAL A O   1 
ATOM   35   C  CB  . VAL A 1 35   ? 34.126 42.993  -23.290 1.00 13.52 ? 35   VAL A CB  1 
ATOM   36   C  CG1 . VAL A 1 35   ? 32.966 43.426  -24.226 1.00 12.17 ? 35   VAL A CG1 1 
ATOM   37   C  CG2 . VAL A 1 35   ? 35.222 44.048  -23.218 1.00 10.31 ? 35   VAL A CG2 1 
ATOM   38   N  N   . GLN A 1 36   ? 32.689 40.494  -22.414 1.00 14.70 ? 36   GLN A N   1 
ATOM   39   C  CA  . GLN A 1 36   ? 31.685 39.487  -22.765 1.00 16.67 ? 36   GLN A CA  1 
ATOM   40   C  C   . GLN A 1 36   ? 31.021 38.597  -21.750 1.00 18.73 ? 36   GLN A C   1 
ATOM   41   O  O   . GLN A 1 36   ? 30.025 37.979  -22.067 1.00 21.00 ? 36   GLN A O   1 
ATOM   42   C  CB  . GLN A 1 36   ? 32.284 38.612  -23.853 1.00 16.76 ? 36   GLN A CB  1 
ATOM   43   C  CG  . GLN A 1 36   ? 32.946 39.472  -24.917 1.00 17.97 ? 36   GLN A CG  1 
ATOM   44   C  CD  . GLN A 1 36   ? 33.459 38.672  -26.102 1.00 18.26 ? 36   GLN A CD  1 
ATOM   45   O  OE1 . GLN A 1 36   ? 32.733 38.432  -27.052 1.00 18.35 ? 36   GLN A OE1 1 
ATOM   46   N  NE2 . GLN A 1 36   ? 34.718 38.254  -26.038 1.00 17.97 ? 36   GLN A NE2 1 
ATOM   47   N  N   . ASP A 1 37   ? 31.569 38.508  -20.548 1.00 20.46 ? 37   ASP A N   1 
ATOM   48   C  CA  . ASP A 1 37   ? 30.996 37.675  -19.498 1.00 20.39 ? 37   ASP A CA  1 
ATOM   49   C  C   . ASP A 1 37   ? 30.353 38.529  -18.410 1.00 19.60 ? 37   ASP A C   1 
ATOM   50   O  O   . ASP A 1 37   ? 31.064 39.172  -17.658 1.00 20.99 ? 37   ASP A O   1 
ATOM   51   C  CB  . ASP A 1 37   ? 32.100 36.842  -18.841 1.00 22.32 ? 37   ASP A CB  1 
ATOM   52   C  CG  . ASP A 1 37   ? 32.783 35.907  -19.812 1.00 24.17 ? 37   ASP A CG  1 
ATOM   53   O  OD1 . ASP A 1 37   ? 32.071 35.264  -20.608 1.00 24.80 ? 37   ASP A OD1 1 
ATOM   54   O  OD2 . ASP A 1 37   ? 34.027 35.824  -19.773 1.00 26.59 ? 37   ASP A OD2 1 
ATOM   55   N  N   . VAL A 1 38   ? 29.032 38.525  -18.311 1.00 18.84 ? 38   VAL A N   1 
ATOM   56   C  CA  . VAL A 1 38   ? 28.348 39.287  -17.268 1.00 18.46 ? 38   VAL A CA  1 
ATOM   57   C  C   . VAL A 1 38   ? 28.533 38.582  -15.896 1.00 17.92 ? 38   VAL A C   1 
ATOM   58   O  O   . VAL A 1 38   ? 28.058 37.463  -15.700 1.00 16.98 ? 38   VAL A O   1 
ATOM   59   C  CB  . VAL A 1 38   ? 26.837 39.379  -17.564 1.00 19.47 ? 38   VAL A CB  1 
ATOM   60   C  CG1 . VAL A 1 38   ? 26.105 40.126  -16.432 1.00 20.00 ? 38   VAL A CG1 1 
ATOM   61   C  CG2 . VAL A 1 38   ? 26.617 40.093  -18.922 1.00 19.53 ? 38   VAL A CG2 1 
ATOM   62   N  N   . PRO A 1 39   ? 29.241 39.227  -14.946 1.00 16.52 ? 39   PRO A N   1 
ATOM   63   C  CA  . PRO A 1 39   ? 29.410 38.571  -13.649 1.00 15.58 ? 39   PRO A CA  1 
ATOM   64   C  C   . PRO A 1 39   ? 28.083 38.218  -12.996 1.00 16.58 ? 39   PRO A C   1 
ATOM   65   O  O   . PRO A 1 39   ? 27.072 38.932  -13.106 1.00 15.22 ? 39   PRO A O   1 
ATOM   66   C  CB  . PRO A 1 39   ? 30.190 39.600  -12.829 1.00 16.45 ? 39   PRO A CB  1 
ATOM   67   C  CG  . PRO A 1 39   ? 31.074 40.285  -13.876 1.00 15.63 ? 39   PRO A CG  1 
ATOM   68   C  CD  . PRO A 1 39   ? 30.086 40.444  -15.047 1.00 16.34 ? 39   PRO A CD  1 
ATOM   69   N  N   . ASN A 1 40   ? 28.093 37.090  -12.302 1.00 18.11 ? 40   ASN A N   1 
ATOM   70   C  CA  . ASN A 1 40   ? 26.927 36.631  -11.589 1.00 19.04 ? 40   ASN A CA  1 
ATOM   71   C  C   . ASN A 1 40   ? 27.098 37.006  -10.100 1.00 17.60 ? 40   ASN A C   1 
ATOM   72   O  O   . ASN A 1 40   ? 27.925 36.421  -9.400  1.00 17.83 ? 40   ASN A O   1 
ATOM   73   C  CB  . ASN A 1 40   ? 26.812 35.119  -11.733 1.00 23.38 ? 40   ASN A CB  1 
ATOM   74   C  CG  . ASN A 1 40   ? 25.569 34.586  -11.075 1.00 28.15 ? 40   ASN A CG  1 
ATOM   75   O  OD1 . ASN A 1 40   ? 24.454 34.847  -11.528 1.00 32.63 ? 40   ASN A OD1 1 
ATOM   76   N  ND2 . ASN A 1 40   ? 25.744 33.856  -9.986  1.00 31.45 ? 40   ASN A ND2 1 
ATOM   77   N  N   . VAL A 1 41   ? 26.322 37.957  -9.601  1.00 15.25 ? 41   VAL A N   1 
ATOM   78   C  CA  . VAL A 1 41   ? 26.472 38.360  -8.193  1.00 14.16 ? 41   VAL A CA  1 
ATOM   79   C  C   . VAL A 1 41   ? 25.124 38.408  -7.493  1.00 13.07 ? 41   VAL A C   1 
ATOM   80   O  O   . VAL A 1 41   ? 24.105 38.588  -8.135  1.00 13.39 ? 41   VAL A O   1 
ATOM   81   C  CB  . VAL A 1 41   ? 27.137 39.755  -8.098  1.00 14.12 ? 41   VAL A CB  1 
ATOM   82   C  CG1 . VAL A 1 41   ? 28.595 39.672  -8.515  1.00 13.61 ? 41   VAL A CG1 1 
ATOM   83   C  CG2 . VAL A 1 41   ? 26.394 40.736  -9.015  1.00 13.39 ? 41   VAL A CG2 1 
ATOM   84   N  N   . ASP A 1 42   ? 25.111 38.235  -6.180  1.00 12.35 ? 42   ASP A N   1 
ATOM   85   C  CA  . ASP A 1 42   ? 23.864 38.287  -5.442  1.00 11.59 ? 42   ASP A CA  1 
ATOM   86   C  C   . ASP A 1 42   ? 23.210 39.671  -5.469  1.00 12.16 ? 42   ASP A C   1 
ATOM   87   O  O   . ASP A 1 42   ? 21.982 39.790  -5.498  1.00 11.77 ? 42   ASP A O   1 
ATOM   88   C  CB  . ASP A 1 42   ? 24.129 37.859  -3.999  1.00 14.12 ? 42   ASP A CB  1 
ATOM   89   C  CG  . ASP A 1 42   ? 24.729 36.473  -3.923  1.00 12.75 ? 42   ASP A CG  1 
ATOM   90   O  OD1 . ASP A 1 42   ? 24.118 35.558  -4.500  1.00 14.67 ? 42   ASP A OD1 1 
ATOM   91   O  OD2 . ASP A 1 42   ? 25.802 36.298  -3.326  1.00 13.34 ? 42   ASP A OD2 1 
ATOM   92   N  N   . VAL A 1 43   ? 24.015 40.730  -5.421  1.00 11.08 ? 43   VAL A N   1 
ATOM   93   C  CA  . VAL A 1 43   ? 23.465 42.096  -5.455  1.00 10.87 ? 43   VAL A CA  1 
ATOM   94   C  C   . VAL A 1 43   ? 24.206 42.886  -6.540  1.00 11.04 ? 43   VAL A C   1 
ATOM   95   O  O   . VAL A 1 43   ? 25.437 42.952  -6.503  1.00 9.91  ? 43   VAL A O   1 
ATOM   96   C  CB  . VAL A 1 43   ? 23.707 42.825  -4.094  1.00 12.87 ? 43   VAL A CB  1 
ATOM   97   C  CG1 . VAL A 1 43   ? 23.143 44.276  -4.132  1.00 10.96 ? 43   VAL A CG1 1 
ATOM   98   C  CG2 . VAL A 1 43   ? 23.100 41.994  -2.932  1.00 13.95 ? 43   VAL A CG2 1 
ATOM   99   N  N   . GLN A 1 44   ? 23.491 43.428  -7.523  1.00 10.11 ? 44   GLN A N   1 
ATOM   100  C  CA  . GLN A 1 44   ? 24.150 44.233  -8.557  1.00 10.43 ? 44   GLN A CA  1 
ATOM   101  C  C   . GLN A 1 44   ? 23.433 45.563  -8.395  1.00 10.12 ? 44   GLN A C   1 
ATOM   102  O  O   . GLN A 1 44   ? 22.233 45.657  -8.647  1.00 9.78  ? 44   GLN A O   1 
ATOM   103  C  CB  . GLN A 1 44   ? 23.962 43.608  -9.956  1.00 11.25 ? 44   GLN A CB  1 
ATOM   104  C  CG  . GLN A 1 44   ? 25.085 44.011  -10.967 1.00 9.69  ? 44   GLN A CG  1 
ATOM   105  C  CD  . GLN A 1 44   ? 25.204 45.534  -11.077 1.00 10.22 ? 44   GLN A CD  1 
ATOM   106  O  OE1 . GLN A 1 44   ? 24.234 46.204  -11.376 1.00 9.98  ? 44   GLN A OE1 1 
ATOM   107  N  NE2 . GLN A 1 44   ? 26.393 46.076  -10.811 1.00 8.26  ? 44   GLN A NE2 1 
ATOM   108  N  N   . MET A 1 45   ? 24.158 46.599  -7.966  1.00 9.39  ? 45   MET A N   1 
ATOM   109  C  CA  . MET A 1 45   ? 23.501 47.855  -7.650  1.00 9.67  ? 45   MET A CA  1 
ATOM   110  C  C   . MET A 1 45   ? 22.609 48.519  -8.678  1.00 9.38  ? 45   MET A C   1 
ATOM   111  O  O   . MET A 1 45   ? 21.611 49.117  -8.307  1.00 9.26  ? 45   MET A O   1 
ATOM   112  C  CB  . MET A 1 45   ? 24.507 48.857  -7.067  1.00 9.76  ? 45   MET A CB  1 
ATOM   113  C  CG  . MET A 1 45   ? 25.093 48.413  -5.732  1.00 9.75  ? 45   MET A CG  1 
ATOM   114  S  SD  . MET A 1 45   ? 23.897 48.100  -4.448  1.00 13.34 ? 45   MET A SD  1 
ATOM   115  C  CE  . MET A 1 45   ? 23.179 49.717  -4.262  1.00 10.79 ? 45   MET A CE  1 
ATOM   116  N  N   . LEU A 1 46   ? 22.938 48.429  -9.958  1.00 9.71  ? 46   LEU A N   1 
ATOM   117  C  CA  . LEU A 1 46   ? 22.064 49.039  -10.972 1.00 11.02 ? 46   LEU A CA  1 
ATOM   118  C  C   . LEU A 1 46   ? 20.724 48.256  -11.007 1.00 12.45 ? 46   LEU A C   1 
ATOM   119  O  O   . LEU A 1 46   ? 19.640 48.841  -11.135 1.00 12.28 ? 46   LEU A O   1 
ATOM   120  C  CB  . LEU A 1 46   ? 22.725 48.986  -12.370 1.00 9.00  ? 46   LEU A CB  1 
ATOM   121  C  CG  . LEU A 1 46   ? 21.923 49.672  -13.486 1.00 8.37  ? 46   LEU A CG  1 
ATOM   122  C  CD1 . LEU A 1 46   ? 21.961 51.196  -13.272 1.00 10.05 ? 46   LEU A CD1 1 
ATOM   123  C  CD2 . LEU A 1 46   ? 22.511 49.301  -14.851 1.00 8.35  ? 46   LEU A CD2 1 
ATOM   124  N  N   . GLU A 1 47   ? 20.829 46.929  -10.883 1.00 13.53 ? 47   GLU A N   1 
ATOM   125  C  CA  . GLU A 1 47   ? 19.662 46.063  -10.913 1.00 14.85 ? 47   GLU A CA  1 
ATOM   126  C  C   . GLU A 1 47   ? 18.819 46.345  -9.691  1.00 14.47 ? 47   GLU A C   1 
ATOM   127  O  O   . GLU A 1 47   ? 17.589 46.513  -9.794  1.00 14.96 ? 47   GLU A O   1 
ATOM   128  C  CB  . GLU A 1 47   ? 20.091 44.602  -10.962 1.00 17.74 ? 47   GLU A CB  1 
ATOM   129  C  CG  . GLU A 1 47   ? 18.970 43.579  -11.210 1.00 22.19 ? 47   GLU A CG  1 
ATOM   130  C  CD  . GLU A 1 47   ? 18.125 43.266  -9.974  1.00 24.52 ? 47   GLU A CD  1 
ATOM   131  O  OE1 . GLU A 1 47   ? 18.593 43.447  -8.831  1.00 24.82 ? 47   GLU A OE1 1 
ATOM   132  O  OE2 . GLU A 1 47   ? 16.979 42.806  -10.148 1.00 28.00 ? 47   GLU A OE2 1 
ATOM   133  N  N   . LEU A 1 48   ? 19.476 46.463  -8.541  1.00 13.44 ? 48   LEU A N   1 
ATOM   134  C  CA  . LEU A 1 48   ? 18.759 46.753  -7.309  1.00 12.87 ? 48   LEU A CA  1 
ATOM   135  C  C   . LEU A 1 48   ? 18.024 48.085  -7.441  1.00 12.29 ? 48   LEU A C   1 
ATOM   136  O  O   . LEU A 1 48   ? 16.842 48.198  -7.102  1.00 11.79 ? 48   LEU A O   1 
ATOM   137  C  CB  . LEU A 1 48   ? 19.726 46.785  -6.127  1.00 13.86 ? 48   LEU A CB  1 
ATOM   138  C  CG  . LEU A 1 48   ? 19.101 46.936  -4.725  1.00 16.55 ? 48   LEU A CG  1 
ATOM   139  C  CD1 . LEU A 1 48   ? 18.107 45.776  -4.456  1.00 16.84 ? 48   LEU A CD1 1 
ATOM   140  C  CD2 . LEU A 1 48   ? 20.176 46.972  -3.659  1.00 15.00 ? 48   LEU A CD2 1 
ATOM   141  N  N   . TYR A 1 49   ? 18.701 49.090  -7.981  1.00 11.49 ? 49   TYR A N   1 
ATOM   142  C  CA  . TYR A 1 49   ? 18.100 50.414  -8.137  1.00 11.63 ? 49   TYR A CA  1 
ATOM   143  C  C   . TYR A 1 49   ? 16.834 50.372  -9.007  1.00 12.96 ? 49   TYR A C   1 
ATOM   144  O  O   . TYR A 1 49   ? 15.859 51.076  -8.746  1.00 11.14 ? 49   TYR A O   1 
ATOM   145  C  CB  . TYR A 1 49   ? 19.133 51.378  -8.760  1.00 10.36 ? 49   TYR A CB  1 
ATOM   146  C  CG  . TYR A 1 49   ? 19.744 52.297  -7.733  1.00 10.69 ? 49   TYR A CG  1 
ATOM   147  C  CD1 . TYR A 1 49   ? 20.245 51.796  -6.512  1.00 9.23  ? 49   TYR A CD1 1 
ATOM   148  C  CD2 . TYR A 1 49   ? 19.723 53.673  -7.932  1.00 8.12  ? 49   TYR A CD2 1 
ATOM   149  C  CE1 . TYR A 1 49   ? 20.695 52.663  -5.514  1.00 10.62 ? 49   TYR A CE1 1 
ATOM   150  C  CE2 . TYR A 1 49   ? 20.160 54.542  -6.941  1.00 11.66 ? 49   TYR A CE2 1 
ATOM   151  C  CZ  . TYR A 1 49   ? 20.634 54.045  -5.741  1.00 9.37  ? 49   TYR A CZ  1 
ATOM   152  O  OH  . TYR A 1 49   ? 20.936 54.947  -4.759  1.00 11.25 ? 49   TYR A OH  1 
ATOM   153  N  N   . ASP A 1 50   ? 16.874 49.543  -10.039 1.00 14.94 ? 50   ASP A N   1 
ATOM   154  C  CA  . ASP A 1 50   ? 15.759 49.395  -10.964 1.00 17.41 ? 50   ASP A CA  1 
ATOM   155  C  C   . ASP A 1 50   ? 14.513 48.853  -10.222 1.00 19.10 ? 50   ASP A C   1 
ATOM   156  O  O   . ASP A 1 50   ? 13.389 49.308  -10.459 1.00 17.85 ? 50   ASP A O   1 
ATOM   157  C  CB  . ASP A 1 50   ? 16.174 48.421  -12.070 1.00 18.75 ? 50   ASP A CB  1 
ATOM   158  C  CG  . ASP A 1 50   ? 15.373 48.577  -13.336 1.00 22.13 ? 50   ASP A CG  1 
ATOM   159  O  OD1 . ASP A 1 50   ? 15.436 47.650  -14.181 1.00 22.95 ? 50   ASP A OD1 1 
ATOM   160  O  OD2 . ASP A 1 50   ? 14.703 49.615  -13.503 1.00 24.11 ? 50   ASP A OD2 1 
ATOM   161  N  N   . ARG A 1 51   ? 14.716 47.889  -9.326  1.00 20.06 ? 51   ARG A N   1 
ATOM   162  C  CA  . ARG A 1 51   ? 13.591 47.292  -8.602  1.00 22.60 ? 51   ARG A CA  1 
ATOM   163  C  C   . ARG A 1 51   ? 13.113 48.037  -7.354  1.00 22.33 ? 51   ARG A C   1 
ATOM   164  O  O   . ARG A 1 51   ? 11.925 48.001  -7.044  1.00 22.35 ? 51   ARG A O   1 
ATOM   165  C  CB  . ARG A 1 51   ? 13.888 45.843  -8.179  1.00 25.94 ? 51   ARG A CB  1 
ATOM   166  C  CG  . ARG A 1 51   ? 15.040 45.163  -8.857  1.00 30.31 ? 51   ARG A CG  1 
ATOM   167  C  CD  . ARG A 1 51   ? 15.006 43.672  -8.520  1.00 33.76 ? 51   ARG A CD  1 
ATOM   168  N  NE  . ARG A 1 51   ? 14.942 43.479  -7.085  1.00 35.54 ? 51   ARG A NE  1 
ATOM   169  C  CZ  . ARG A 1 51   ? 15.988 43.254  -6.296  1.00 35.95 ? 51   ARG A CZ  1 
ATOM   170  N  NH1 . ARG A 1 51   ? 17.211 43.174  -6.791  1.00 37.28 ? 51   ARG A NH1 1 
ATOM   171  N  NH2 . ARG A 1 51   ? 15.800 43.133  -4.990  1.00 36.96 ? 51   ARG A NH2 1 
ATOM   172  N  N   . MET A 1 52   ? 14.025 48.701  -6.648  1.00 21.62 ? 52   MET A N   1 
ATOM   173  C  CA  . MET A 1 52   ? 13.700 49.422  -5.421  1.00 22.09 ? 52   MET A CA  1 
ATOM   174  C  C   . MET A 1 52   ? 12.706 50.551  -5.613  1.00 22.07 ? 52   MET A C   1 
ATOM   175  O  O   . MET A 1 52   ? 12.739 51.258  -6.626  1.00 22.62 ? 52   MET A O   1 
ATOM   176  C  CB  . MET A 1 52   ? 14.969 50.022  -4.808  1.00 22.56 ? 52   MET A CB  1 
ATOM   177  C  CG  . MET A 1 52   ? 15.848 49.045  -4.089  1.00 23.79 ? 52   MET A CG  1 
ATOM   178  S  SD  . MET A 1 52   ? 17.385 49.899  -3.557  1.00 25.04 ? 52   MET A SD  1 
ATOM   179  C  CE  . MET A 1 52   ? 16.721 51.175  -2.486  1.00 24.21 ? 52   MET A CE  1 
ATOM   180  N  N   . SER A 1 53   ? 11.846 50.739  -4.620  1.00 21.53 ? 53   SER A N   1 
ATOM   181  C  CA  . SER A 1 53   ? 10.838 51.793  -4.678  1.00 21.79 ? 53   SER A CA  1 
ATOM   182  C  C   . SER A 1 53   ? 11.294 53.120  -4.091  1.00 20.91 ? 53   SER A C   1 
ATOM   183  O  O   . SER A 1 53   ? 10.747 54.163  -4.442  1.00 20.26 ? 53   SER A O   1 
ATOM   184  C  CB  . SER A 1 53   ? 9.565  51.349  -3.959  1.00 22.33 ? 53   SER A CB  1 
ATOM   185  O  OG  . SER A 1 53   ? 8.906  50.371  -4.744  1.00 24.56 ? 53   SER A OG  1 
ATOM   186  N  N   . PHE A 1 54   ? 12.265 53.073  -3.180  1.00 19.11 ? 54   PHE A N   1 
ATOM   187  C  CA  . PHE A 1 54   ? 12.771 54.286  -2.563  1.00 19.21 ? 54   PHE A CA  1 
ATOM   188  C  C   . PHE A 1 54   ? 11.724 55.058  -1.776  1.00 20.38 ? 54   PHE A C   1 
ATOM   189  O  O   . PHE A 1 54   ? 11.835 56.286  -1.655  1.00 20.35 ? 54   PHE A O   1 
ATOM   190  C  CB  . PHE A 1 54   ? 13.380 55.225  -3.633  1.00 17.10 ? 54   PHE A CB  1 
ATOM   191  C  CG  . PHE A 1 54   ? 14.643 54.692  -4.260  1.00 14.69 ? 54   PHE A CG  1 
ATOM   192  C  CD1 . PHE A 1 54   ? 14.585 53.783  -5.322  1.00 14.65 ? 54   PHE A CD1 1 
ATOM   193  C  CD2 . PHE A 1 54   ? 15.890 55.068  -3.760  1.00 13.78 ? 54   PHE A CD2 1 
ATOM   194  C  CE1 . PHE A 1 54   ? 15.758 53.256  -5.874  1.00 14.95 ? 54   PHE A CE1 1 
ATOM   195  C  CE2 . PHE A 1 54   ? 17.082 54.550  -4.300  1.00 12.75 ? 54   PHE A CE2 1 
ATOM   196  C  CZ  . PHE A 1 54   ? 17.025 53.645  -5.356  1.00 14.70 ? 54   PHE A CZ  1 
ATOM   197  N  N   . LYS A 1 55   ? 10.702 54.382  -1.235  1.00 20.01 ? 55   LYS A N   1 
ATOM   198  C  CA  . LYS A 1 55   ? 9.686  55.128  -0.477  1.00 20.10 ? 55   LYS A CA  1 
ATOM   199  C  C   . LYS A 1 55   ? 10.251 55.589  0.855   1.00 18.97 ? 55   LYS A C   1 
ATOM   200  O  O   . LYS A 1 55   ? 10.851 54.808  1.570   1.00 20.50 ? 55   LYS A O   1 
ATOM   201  C  CB  . LYS A 1 55   ? 8.432  54.267  -0.248  1.00 21.01 ? 55   LYS A CB  1 
ATOM   202  C  CG  . LYS A 1 55   ? 7.788  53.840  -1.530  1.00 21.06 ? 55   LYS A CG  1 
ATOM   203  C  CD  . LYS A 1 55   ? 7.487  55.026  -2.450  1.00 19.63 ? 55   LYS A CD  1 
ATOM   204  C  CE  . LYS A 1 55   ? 6.934  54.471  -3.758  1.00 20.44 ? 55   LYS A CE  1 
ATOM   205  N  NZ  . LYS A 1 55   ? 6.172  55.465  -4.568  1.00 19.21 ? 55   LYS A NZ  1 
ATOM   206  N  N   . ASP A 1 56   ? 10.048 56.851  1.194   1.00 18.09 ? 56   ASP A N   1 
ATOM   207  C  CA  . ASP A 1 56   ? 10.596 57.407  2.441   1.00 18.49 ? 56   ASP A CA  1 
ATOM   208  C  C   . ASP A 1 56   ? 9.533  57.383  3.562   1.00 19.36 ? 56   ASP A C   1 
ATOM   209  O  O   . ASP A 1 56   ? 8.978  58.413  3.924   1.00 19.09 ? 56   ASP A O   1 
ATOM   210  C  CB  . ASP A 1 56   ? 11.088 58.841  2.147   1.00 16.95 ? 56   ASP A CB  1 
ATOM   211  C  CG  . ASP A 1 56   ? 11.720 59.526  3.344   1.00 16.93 ? 56   ASP A CG  1 
ATOM   212  O  OD1 . ASP A 1 56   ? 12.234 58.858  4.260   1.00 17.09 ? 56   ASP A OD1 1 
ATOM   213  O  OD2 . ASP A 1 56   ? 11.717 60.763  3.366   1.00 18.77 ? 56   ASP A OD2 1 
ATOM   214  N  N   . ILE A 1 57   ? 9.251  56.214  4.116   1.00 20.01 ? 57   ILE A N   1 
ATOM   215  C  CA  . ILE A 1 57   ? 8.244  56.149  5.155   1.00 21.79 ? 57   ILE A CA  1 
ATOM   216  C  C   . ILE A 1 57   ? 8.852  56.152  6.540   1.00 21.46 ? 57   ILE A C   1 
ATOM   217  O  O   . ILE A 1 57   ? 10.000 55.748  6.736   1.00 21.75 ? 57   ILE A O   1 
ATOM   218  C  CB  . ILE A 1 57   ? 7.323  54.888  4.987   1.00 25.03 ? 57   ILE A CB  1 
ATOM   219  C  CG1 . ILE A 1 57   ? 8.063  53.639  5.391   1.00 25.11 ? 57   ILE A CG1 1 
ATOM   220  C  CG2 . ILE A 1 57   ? 6.864  54.697  3.527   1.00 23.63 ? 57   ILE A CG2 1 
ATOM   221  C  CD1 . ILE A 1 57   ? 7.512  53.118  6.649   1.00 29.03 ? 57   ILE A CD1 1 
ATOM   222  N  N   . ASP A 1 58   ? 8.072  56.627  7.503   1.00 21.82 ? 58   ASP A N   1 
ATOM   223  C  CA  . ASP A 1 58   ? 8.479  56.686  8.907   1.00 21.46 ? 58   ASP A CA  1 
ATOM   224  C  C   . ASP A 1 58   ? 8.503  55.272  9.460   1.00 20.96 ? 58   ASP A C   1 
ATOM   225  O  O   . ASP A 1 58   ? 7.451  54.638  9.585   1.00 22.16 ? 58   ASP A O   1 
ATOM   226  C  CB  . ASP A 1 58   ? 7.474  57.511  9.675   1.00 21.36 ? 58   ASP A CB  1 
ATOM   227  C  CG  . ASP A 1 58   ? 7.863  57.696  11.112  1.00 22.74 ? 58   ASP A CG  1 
ATOM   228  O  OD1 . ASP A 1 58   ? 7.274  58.601  11.749  1.00 25.60 ? 58   ASP A OD1 1 
ATOM   229  O  OD2 . ASP A 1 58   ? 8.742  56.959  11.610  1.00 22.14 ? 58   ASP A OD2 1 
ATOM   230  N  N   . GLY A 1 59   ? 9.687  54.758  9.774   1.00 19.13 ? 59   GLY A N   1 
ATOM   231  C  CA  . GLY A 1 59   ? 9.771  53.397  10.278  1.00 17.43 ? 59   GLY A CA  1 
ATOM   232  C  C   . GLY A 1 59   ? 9.777  53.291  11.795  1.00 16.35 ? 59   GLY A C   1 
ATOM   233  O  O   . GLY A 1 59   ? 10.061 52.223  12.324  1.00 16.19 ? 59   GLY A O   1 
ATOM   234  N  N   . GLY A 1 60   ? 9.459  54.391  12.479  1.00 16.56 ? 60   GLY A N   1 
ATOM   235  C  CA  . GLY A 1 60   ? 9.443  54.417  13.943  1.00 16.23 ? 60   GLY A CA  1 
ATOM   236  C  C   . GLY A 1 60   ? 10.699 55.027  14.540  1.00 16.20 ? 60   GLY A C   1 
ATOM   237  O  O   . GLY A 1 60   ? 11.253 55.979  13.997  1.00 15.33 ? 60   GLY A O   1 
ATOM   238  N  N   . VAL A 1 61   ? 11.160 54.502  15.672  1.00 16.33 ? 61   VAL A N   1 
ATOM   239  C  CA  . VAL A 1 61   ? 12.366 55.038  16.269  1.00 16.28 ? 61   VAL A CA  1 
ATOM   240  C  C   . VAL A 1 61   ? 13.495 54.908  15.233  1.00 16.42 ? 61   VAL A C   1 
ATOM   241  O  O   . VAL A 1 61   ? 14.352 55.801  15.134  1.00 16.21 ? 61   VAL A O   1 
ATOM   242  C  CB  . VAL A 1 61   ? 12.718 54.327  17.589  1.00 15.90 ? 61   VAL A CB  1 
ATOM   243  C  CG1 . VAL A 1 61   ? 11.679 54.728  18.682  1.00 15.97 ? 61   VAL A CG1 1 
ATOM   244  C  CG2 . VAL A 1 61   ? 12.734 52.806  17.402  1.00 16.29 ? 61   VAL A CG2 1 
ATOM   245  N  N   . TRP A 1 62   ? 13.513 53.810  14.468  1.00 15.15 ? 62   TRP A N   1 
ATOM   246  C  CA  . TRP A 1 62   ? 14.504 53.715  13.403  1.00 15.25 ? 62   TRP A CA  1 
ATOM   247  C  C   . TRP A 1 62   ? 13.723 54.370  12.270  1.00 16.82 ? 62   TRP A C   1 
ATOM   248  O  O   . TRP A 1 62   ? 13.016 53.712  11.498  1.00 15.83 ? 62   TRP A O   1 
ATOM   249  C  CB  . TRP A 1 62   ? 14.863 52.265  13.055  1.00 13.71 ? 62   TRP A CB  1 
ATOM   250  C  CG  . TRP A 1 62   ? 15.917 52.163  11.962  1.00 14.85 ? 62   TRP A CG  1 
ATOM   251  C  CD1 . TRP A 1 62   ? 16.593 53.209  11.364  1.00 15.32 ? 62   TRP A CD1 1 
ATOM   252  C  CD2 . TRP A 1 62   ? 16.313 50.981  11.259  1.00 14.85 ? 62   TRP A CD2 1 
ATOM   253  N  NE1 . TRP A 1 62   ? 17.364 52.742  10.320  1.00 16.57 ? 62   TRP A NE1 1 
ATOM   254  C  CE2 . TRP A 1 62   ? 17.218 51.381  10.235  1.00 15.25 ? 62   TRP A CE2 1 
ATOM   255  C  CE3 . TRP A 1 62   ? 15.991 49.624  11.388  1.00 13.62 ? 62   TRP A CE3 1 
ATOM   256  C  CZ2 . TRP A 1 62   ? 17.795 50.468  9.343   1.00 15.46 ? 62   TRP A CZ2 1 
ATOM   257  C  CZ3 . TRP A 1 62   ? 16.563 48.716  10.504  1.00 14.25 ? 62   TRP A CZ3 1 
ATOM   258  C  CH2 . TRP A 1 62   ? 17.456 49.141  9.492   1.00 15.82 ? 62   TRP A CH2 1 
ATOM   259  N  N   . LYS A 1 63   ? 13.840 55.696  12.192  1.00 17.65 ? 63   LYS A N   1 
ATOM   260  C  CA  . LYS A 1 63   ? 13.114 56.482  11.201  1.00 18.19 ? 63   LYS A CA  1 
ATOM   261  C  C   . LYS A 1 63   ? 13.144 55.977  9.756   1.00 17.26 ? 63   LYS A C   1 
ATOM   262  O  O   . LYS A 1 63   ? 12.148 56.068  9.030   1.00 17.94 ? 63   LYS A O   1 
ATOM   263  C  CB  . LYS A 1 63   ? 13.600 57.939  11.260  1.00 18.75 ? 63   LYS A CB  1 
ATOM   264  C  CG  . LYS A 1 63   ? 13.075 58.745  12.495  1.00 22.70 ? 63   LYS A CG  1 
ATOM   265  C  CD  . LYS A 1 63   ? 11.568 59.057  12.356  1.00 24.73 ? 63   LYS A CD  1 
ATOM   266  C  CE  . LYS A 1 63   ? 10.935 59.705  13.584  1.00 26.79 ? 63   LYS A CE  1 
ATOM   267  N  NZ  . LYS A 1 63   ? 11.126 59.003  14.922  1.00 29.35 ? 63   LYS A NZ  1 
ATOM   268  N  N   . GLN A 1 64   ? 14.278 55.446  9.323   1.00 15.67 ? 64   GLN A N   1 
ATOM   269  C  CA  . GLN A 1 64   ? 14.380 54.986  7.937   1.00 14.50 ? 64   GLN A CA  1 
ATOM   270  C  C   . GLN A 1 64   ? 14.398 53.477  7.768   1.00 13.54 ? 64   GLN A C   1 
ATOM   271  O  O   . GLN A 1 64   ? 14.683 52.968  6.683   1.00 12.04 ? 64   GLN A O   1 
ATOM   272  C  CB  . GLN A 1 64   ? 15.602 55.639  7.280   1.00 13.77 ? 64   GLN A CB  1 
ATOM   273  C  CG  . GLN A 1 64   ? 15.490 57.168  7.307   1.00 13.17 ? 64   GLN A CG  1 
ATOM   274  C  CD  . GLN A 1 64   ? 16.837 57.856  7.144   1.00 13.81 ? 64   GLN A CD  1 
ATOM   275  O  OE1 . GLN A 1 64   ? 17.817 57.507  7.829   1.00 13.33 ? 64   GLN A OE1 1 
ATOM   276  N  NE2 . GLN A 1 64   ? 16.898 58.826  6.228   1.00 12.59 ? 64   GLN A NE2 1 
ATOM   277  N  N   . GLY A 1 65   ? 14.056 52.772  8.838   1.00 13.57 ? 65   GLY A N   1 
ATOM   278  C  CA  . GLY A 1 65   ? 14.014 51.319  8.768   1.00 15.56 ? 65   GLY A CA  1 
ATOM   279  C  C   . GLY A 1 65   ? 12.639 50.774  9.165   1.00 17.04 ? 65   GLY A C   1 
ATOM   280  O  O   . GLY A 1 65   ? 11.623 51.121  8.531   1.00 18.36 ? 65   GLY A O   1 
ATOM   281  N  N   . TRP A 1 66   ? 12.605 49.940  10.208  1.00 17.21 ? 66   TRP A N   1 
ATOM   282  C  CA  . TRP A 1 66   ? 11.356 49.318  10.721  1.00 17.88 ? 66   TRP A CA  1 
ATOM   283  C  C   . TRP A 1 66   ? 11.665 48.894  12.156  1.00 18.53 ? 66   TRP A C   1 
ATOM   284  O  O   . TRP A 1 66   ? 12.834 48.977  12.557  1.00 18.86 ? 66   TRP A O   1 
ATOM   285  C  CB  . TRP A 1 66   ? 11.015 48.071  9.903   1.00 16.95 ? 66   TRP A CB  1 
ATOM   286  C  CG  . TRP A 1 66   ? 11.986 46.946  10.096  1.00 15.57 ? 66   TRP A CG  1 
ATOM   287  C  CD1 . TRP A 1 66   ? 11.871 45.897  10.962  1.00 15.09 ? 66   TRP A CD1 1 
ATOM   288  C  CD2 . TRP A 1 66   ? 13.207 46.730  9.369   1.00 15.94 ? 66   TRP A CD2 1 
ATOM   289  N  NE1 . TRP A 1 66   ? 12.933 45.032  10.815  1.00 13.68 ? 66   TRP A NE1 1 
ATOM   290  C  CE2 . TRP A 1 66   ? 13.771 45.520  9.849   1.00 15.46 ? 66   TRP A CE2 1 
ATOM   291  C  CE3 . TRP A 1 66   ? 13.877 47.440  8.355   1.00 16.10 ? 66   TRP A CE3 1 
ATOM   292  C  CZ2 . TRP A 1 66   ? 14.981 45.002  9.351   1.00 16.56 ? 66   TRP A CZ2 1 
ATOM   293  C  CZ3 . TRP A 1 66   ? 15.080 46.926  7.857   1.00 16.71 ? 66   TRP A CZ3 1 
ATOM   294  C  CH2 . TRP A 1 66   ? 15.621 45.722  8.356   1.00 16.46 ? 66   TRP A CH2 1 
ATOM   295  N  N   . ASN A 1 67   ? 10.653 48.458  12.925  1.00 19.46 ? 67   ASN A N   1 
ATOM   296  C  CA  . ASN A 1 67   ? 10.876 48.003  14.313  1.00 19.33 ? 67   ASN A CA  1 
ATOM   297  C  C   . ASN A 1 67   ? 11.484 46.613  14.305  1.00 18.41 ? 67   ASN A C   1 
ATOM   298  O  O   . ASN A 1 67   ? 10.811 45.608  13.997  1.00 16.24 ? 67   ASN A O   1 
ATOM   299  C  CB  . ASN A 1 67   ? 9.577  47.970  15.142  1.00 22.45 ? 67   ASN A CB  1 
ATOM   300  C  CG  . ASN A 1 67   ? 8.959  49.346  15.325  1.00 24.56 ? 67   ASN A CG  1 
ATOM   301  O  OD1 . ASN A 1 67   ? 9.657  50.351  15.501  1.00 26.09 ? 67   ASN A OD1 1 
ATOM   302  N  ND2 . ASN A 1 67   ? 7.638  49.394  15.300  1.00 27.27 ? 67   ASN A ND2 1 
ATOM   303  N  N   . ILE A 1 68   ? 12.760 46.544  14.653  1.00 16.81 ? 68   ILE A N   1 
ATOM   304  C  CA  . ILE A 1 68   ? 13.453 45.270  14.624  1.00 17.50 ? 68   ILE A CA  1 
ATOM   305  C  C   . ILE A 1 68   ? 12.986 44.373  15.757  1.00 19.40 ? 68   ILE A C   1 
ATOM   306  O  O   . ILE A 1 68   ? 12.845 44.813  16.891  1.00 18.16 ? 68   ILE A O   1 
ATOM   307  C  CB  . ILE A 1 68   ? 14.991 45.470  14.745  1.00 17.59 ? 68   ILE A CB  1 
ATOM   308  C  CG1 . ILE A 1 68   ? 15.502 46.357  13.582  1.00 18.19 ? 68   ILE A CG1 1 
ATOM   309  C  CG2 . ILE A 1 68   ? 15.710 44.080  14.734  1.00 18.12 ? 68   ILE A CG2 1 
ATOM   310  C  CD1 . ILE A 1 68   ? 16.932 46.862  13.728  1.00 17.68 ? 68   ILE A CD1 1 
ATOM   311  N  N   . LYS A 1 69   ? 12.741 43.107  15.451  1.00 21.03 ? 69   LYS A N   1 
ATOM   312  C  CA  . LYS A 1 69   ? 12.329 42.166  16.490  1.00 23.19 ? 69   LYS A CA  1 
ATOM   313  C  C   . LYS A 1 69   ? 13.352 41.047  16.455  1.00 22.37 ? 69   LYS A C   1 
ATOM   314  O  O   . LYS A 1 69   ? 13.960 40.800  15.425  1.00 22.07 ? 69   LYS A O   1 
ATOM   315  C  CB  . LYS A 1 69   ? 10.913 41.628  16.208  1.00 25.72 ? 69   LYS A CB  1 
ATOM   316  C  CG  . LYS A 1 69   ? 9.798  42.661  16.497  1.00 29.02 ? 69   LYS A CG  1 
ATOM   317  C  CD  . LYS A 1 69   ? 8.476  42.288  15.795  1.00 32.31 ? 69   LYS A CD  1 
ATOM   318  C  CE  . LYS A 1 69   ? 8.148  40.777  15.943  1.00 34.94 ? 69   LYS A CE  1 
ATOM   319  N  NZ  . LYS A 1 69   ? 6.884  40.336  15.216  1.00 36.49 ? 69   LYS A NZ  1 
ATOM   320  N  N   . TYR A 1 70   ? 13.598 40.420  17.598  1.00 21.64 ? 70   TYR A N   1 
ATOM   321  C  CA  . TYR A 1 70   ? 14.531 39.308  17.633  1.00 21.66 ? 70   TYR A CA  1 
ATOM   322  C  C   . TYR A 1 70   ? 13.970 38.244  18.567  1.00 22.34 ? 70   TYR A C   1 
ATOM   323  O  O   . TYR A 1 70   ? 13.105 38.531  19.402  1.00 21.96 ? 70   TYR A O   1 
ATOM   324  C  CB  . TYR A 1 70   ? 15.926 39.754  18.106  1.00 19.77 ? 70   TYR A CB  1 
ATOM   325  C  CG  . TYR A 1 70   ? 15.973 40.365  19.488  1.00 18.15 ? 70   TYR A CG  1 
ATOM   326  C  CD1 . TYR A 1 70   ? 16.198 39.589  20.613  1.00 19.06 ? 70   TYR A CD1 1 
ATOM   327  C  CD2 . TYR A 1 70   ? 15.802 41.721  19.660  1.00 17.74 ? 70   TYR A CD2 1 
ATOM   328  C  CE1 . TYR A 1 70   ? 16.258 40.168  21.880  1.00 18.47 ? 70   TYR A CE1 1 
ATOM   329  C  CE2 . TYR A 1 70   ? 15.848 42.305  20.907  1.00 18.10 ? 70   TYR A CE2 1 
ATOM   330  C  CZ  . TYR A 1 70   ? 16.073 41.532  22.006  1.00 17.60 ? 70   TYR A CZ  1 
ATOM   331  O  OH  . TYR A 1 70   ? 16.071 42.145  23.231  1.00 18.28 ? 70   TYR A OH  1 
ATOM   332  N  N   . ASP A 1 71   ? 14.455 37.024  18.407  1.00 23.06 ? 71   ASP A N   1 
ATOM   333  C  CA  . ASP A 1 71   ? 14.031 35.919  19.243  1.00 24.38 ? 71   ASP A CA  1 
ATOM   334  C  C   . ASP A 1 71   ? 15.034 35.849  20.378  1.00 25.04 ? 71   ASP A C   1 
ATOM   335  O  O   . ASP A 1 71   ? 16.197 35.526  20.172  1.00 25.21 ? 71   ASP A O   1 
ATOM   336  C  CB  . ASP A 1 71   ? 14.038 34.635  18.431  1.00 26.39 ? 71   ASP A CB  1 
ATOM   337  C  CG  . ASP A 1 71   ? 13.821 33.403  19.285  1.00 29.12 ? 71   ASP A CG  1 
ATOM   338  O  OD1 . ASP A 1 71   ? 13.284 33.522  20.417  1.00 30.00 ? 71   ASP A OD1 1 
ATOM   339  O  OD2 . ASP A 1 71   ? 14.195 32.314  18.809  1.00 30.41 ? 71   ASP A OD2 1 
ATOM   340  N  N   . PRO A 1 72   ? 14.593 36.164  21.609  1.00 26.29 ? 72   PRO A N   1 
ATOM   341  C  CA  . PRO A 1 72   ? 15.536 36.119  22.729  1.00 26.00 ? 72   PRO A CA  1 
ATOM   342  C  C   . PRO A 1 72   ? 16.284 34.808  22.896  1.00 26.05 ? 72   PRO A C   1 
ATOM   343  O  O   . PRO A 1 72   ? 17.387 34.790  23.440  1.00 26.99 ? 72   PRO A O   1 
ATOM   344  C  CB  . PRO A 1 72   ? 14.675 36.504  23.947  1.00 25.93 ? 72   PRO A CB  1 
ATOM   345  C  CG  . PRO A 1 72   ? 13.299 36.135  23.554  1.00 27.72 ? 72   PRO A CG  1 
ATOM   346  C  CD  . PRO A 1 72   ? 13.224 36.466  22.062  1.00 25.26 ? 72   PRO A CD  1 
ATOM   347  N  N   . LEU A 1 73   ? 15.718 33.719  22.398  1.00 25.40 ? 73   LEU A N   1 
ATOM   348  C  CA  . LEU A 1 73   ? 16.371 32.428  22.528  1.00 25.71 ? 73   LEU A CA  1 
ATOM   349  C  C   . LEU A 1 73   ? 17.458 32.221  21.508  1.00 25.63 ? 73   LEU A C   1 
ATOM   350  O  O   . LEU A 1 73   ? 18.113 31.188  21.506  1.00 24.84 ? 73   LEU A O   1 
ATOM   351  C  CB  . LEU A 1 73   ? 15.346 31.293  22.413  1.00 26.18 ? 73   LEU A CB  1 
ATOM   352  C  CG  . LEU A 1 73   ? 14.320 31.374  23.560  1.00 27.56 ? 73   LEU A CG  1 
ATOM   353  C  CD1 . LEU A 1 73   ? 13.326 30.202  23.457  1.00 28.28 ? 73   LEU A CD1 1 
ATOM   354  C  CD2 . LEU A 1 73   ? 15.062 31.367  24.923  1.00 26.80 ? 73   LEU A CD2 1 
ATOM   355  N  N   . LYS A 1 74   ? 17.663 33.198  20.630  1.00 25.10 ? 74   LYS A N   1 
ATOM   356  C  CA  . LYS A 1 74   ? 18.697 33.027  19.619  1.00 25.34 ? 74   LYS A CA  1 
ATOM   357  C  C   . LYS A 1 74   ? 20.070 32.840  20.266  1.00 25.26 ? 74   LYS A C   1 
ATOM   358  O  O   . LYS A 1 74   ? 20.886 32.048  19.792  1.00 24.72 ? 74   LYS A O   1 
ATOM   359  C  CB  . LYS A 1 74   ? 18.704 34.225  18.666  1.00 25.54 ? 74   LYS A CB  1 
ATOM   360  C  CG  . LYS A 1 74   ? 19.666 34.098  17.485  1.00 27.10 ? 74   LYS A CG  1 
ATOM   361  C  CD  . LYS A 1 74   ? 19.399 35.197  16.459  1.00 28.42 ? 74   LYS A CD  1 
ATOM   362  C  CE  . LYS A 1 74   ? 20.415 35.166  15.341  1.00 29.23 ? 74   LYS A CE  1 
ATOM   363  N  NZ  . LYS A 1 74   ? 20.006 36.131  14.283  1.00 30.12 ? 74   LYS A NZ  1 
ATOM   364  N  N   . TYR A 1 75   ? 20.331 33.562  21.352  1.00 25.89 ? 75   TYR A N   1 
ATOM   365  C  CA  . TYR A 1 75   ? 21.616 33.438  22.028  1.00 26.58 ? 75   TYR A CA  1 
ATOM   366  C  C   . TYR A 1 75   ? 21.466 32.659  23.311  1.00 26.90 ? 75   TYR A C   1 
ATOM   367  O  O   . TYR A 1 75   ? 20.463 32.789  23.996  1.00 27.17 ? 75   TYR A O   1 
ATOM   368  C  CB  . TYR A 1 75   ? 22.197 34.812  22.329  1.00 27.00 ? 75   TYR A CB  1 
ATOM   369  C  CG  . TYR A 1 75   ? 22.413 35.590  21.077  1.00 28.06 ? 75   TYR A CG  1 
ATOM   370  C  CD1 . TYR A 1 75   ? 21.504 36.564  20.687  1.00 29.23 ? 75   TYR A CD1 1 
ATOM   371  C  CD2 . TYR A 1 75   ? 23.480 35.303  20.237  1.00 28.15 ? 75   TYR A CD2 1 
ATOM   372  C  CE1 . TYR A 1 75   ? 21.643 37.236  19.499  1.00 29.33 ? 75   TYR A CE1 1 
ATOM   373  C  CE2 . TYR A 1 75   ? 23.626 35.969  19.035  1.00 30.82 ? 75   TYR A CE2 1 
ATOM   374  C  CZ  . TYR A 1 75   ? 22.692 36.938  18.685  1.00 29.49 ? 75   TYR A CZ  1 
ATOM   375  O  OH  . TYR A 1 75   ? 22.809 37.634  17.520  1.00 33.69 ? 75   TYR A OH  1 
ATOM   376  N  N   . ASN A 1 76   ? 22.471 31.855  23.628  1.00 26.55 ? 76   ASN A N   1 
ATOM   377  C  CA  . ASN A 1 76   ? 22.445 31.048  24.833  1.00 27.87 ? 76   ASN A CA  1 
ATOM   378  C  C   . ASN A 1 76   ? 23.878 30.755  25.231  1.00 28.67 ? 76   ASN A C   1 
ATOM   379  O  O   . ASN A 1 76   ? 24.807 31.187  24.557  1.00 29.25 ? 76   ASN A O   1 
ATOM   380  C  CB  . ASN A 1 76   ? 21.674 29.746  24.591  1.00 27.45 ? 76   ASN A CB  1 
ATOM   381  C  CG  . ASN A 1 76   ? 22.166 29.006  23.381  1.00 27.62 ? 76   ASN A CG  1 
ATOM   382  O  OD1 . ASN A 1 76   ? 23.344 28.660  23.282  1.00 28.38 ? 76   ASN A OD1 1 
ATOM   383  N  ND2 . ASN A 1 76   ? 21.262 28.761  22.436  1.00 29.84 ? 76   ASN A ND2 1 
ATOM   384  N  N   . ALA A 1 77   ? 24.063 30.018  26.321  1.00 29.68 ? 77   ALA A N   1 
ATOM   385  C  CA  . ALA A 1 77   ? 25.407 29.719  26.801  1.00 30.70 ? 77   ALA A CA  1 
ATOM   386  C  C   . ALA A 1 77   ? 26.317 29.105  25.737  1.00 31.24 ? 77   ALA A C   1 
ATOM   387  O  O   . ALA A 1 77   ? 27.528 29.269  25.777  1.00 31.88 ? 77   ALA A O   1 
ATOM   388  C  CB  . ALA A 1 77   ? 25.324 28.806  28.015  1.00 30.79 ? 77   ALA A CB  1 
ATOM   389  N  N   . HIS A 1 78   ? 25.737 28.416  24.767  1.00 32.65 ? 78   HIS A N   1 
ATOM   390  C  CA  . HIS A 1 78   ? 26.545 27.779  23.727  1.00 33.77 ? 78   HIS A CA  1 
ATOM   391  C  C   . HIS A 1 78   ? 26.648 28.600  22.453  1.00 32.69 ? 78   HIS A C   1 
ATOM   392  O  O   . HIS A 1 78   ? 27.307 28.196  21.491  1.00 33.21 ? 78   HIS A O   1 
ATOM   393  C  CB  . HIS A 1 78   ? 25.973 26.396  23.431  1.00 36.67 ? 78   HIS A CB  1 
ATOM   394  C  CG  . HIS A 1 78   ? 25.770 25.583  24.667  1.00 40.28 ? 78   HIS A CG  1 
ATOM   395  N  ND1 . HIS A 1 78   ? 26.822 25.174  25.462  1.00 42.03 ? 78   HIS A ND1 1 
ATOM   396  C  CD2 . HIS A 1 78   ? 24.638 25.219  25.319  1.00 41.53 ? 78   HIS A CD2 1 
ATOM   397  C  CE1 . HIS A 1 78   ? 26.346 24.598  26.554  1.00 42.60 ? 78   HIS A CE1 1 
ATOM   398  N  NE2 . HIS A 1 78   ? 25.024 24.614  26.492  1.00 42.85 ? 78   HIS A NE2 1 
ATOM   399  N  N   . HIS A 1 79   ? 26.004 29.763  22.463  1.00 30.64 ? 79   HIS A N   1 
ATOM   400  C  CA  . HIS A 1 79   ? 26.039 30.659  21.325  1.00 27.32 ? 79   HIS A CA  1 
ATOM   401  C  C   . HIS A 1 79   ? 25.804 32.066  21.832  1.00 24.52 ? 79   HIS A C   1 
ATOM   402  O  O   . HIS A 1 79   ? 24.673 32.527  21.890  1.00 23.68 ? 79   HIS A O   1 
ATOM   403  C  CB  . HIS A 1 79   ? 24.958 30.287  20.316  1.00 28.41 ? 79   HIS A CB  1 
ATOM   404  C  CG  . HIS A 1 79   ? 25.044 31.068  19.043  1.00 29.74 ? 79   HIS A CG  1 
ATOM   405  N  ND1 . HIS A 1 79   ? 24.185 32.103  18.744  1.00 30.07 ? 79   HIS A ND1 1 
ATOM   406  C  CD2 . HIS A 1 79   ? 25.928 31.002  18.021  1.00 28.79 ? 79   HIS A CD2 1 
ATOM   407  C  CE1 . HIS A 1 79   ? 24.540 32.645  17.593  1.00 29.82 ? 79   HIS A CE1 1 
ATOM   408  N  NE2 . HIS A 1 79   ? 25.595 31.994  17.135  1.00 28.91 ? 79   HIS A NE2 1 
ATOM   409  N  N   . LYS A 1 80   ? 26.878 32.737  22.205  1.00 20.98 ? 80   LYS A N   1 
ATOM   410  C  CA  . LYS A 1 80   ? 26.775 34.090  22.728  1.00 19.94 ? 80   LYS A CA  1 
ATOM   411  C  C   . LYS A 1 80   ? 27.025 35.169  21.666  1.00 18.53 ? 80   LYS A C   1 
ATOM   412  O  O   . LYS A 1 80   ? 27.649 34.911  20.646  1.00 16.54 ? 80   LYS A O   1 
ATOM   413  C  CB  . LYS A 1 80   ? 27.790 34.280  23.844  1.00 21.70 ? 80   LYS A CB  1 
ATOM   414  C  CG  . LYS A 1 80   ? 27.592 33.323  24.999  1.00 23.85 ? 80   LYS A CG  1 
ATOM   415  C  CD  . LYS A 1 80   ? 28.777 33.348  25.925  1.00 26.43 ? 80   LYS A CD  1 
ATOM   416  C  CE  . LYS A 1 80   ? 28.888 34.655  26.666  1.00 28.44 ? 80   LYS A CE  1 
ATOM   417  N  NZ  . LYS A 1 80   ? 29.712 34.444  27.909  1.00 30.51 ? 80   LYS A NZ  1 
ATOM   418  N  N   . LEU A 1 81   ? 26.537 36.371  21.946  1.00 16.69 ? 81   LEU A N   1 
ATOM   419  C  CA  . LEU A 1 81   ? 26.735 37.517  21.092  1.00 15.41 ? 81   LEU A CA  1 
ATOM   420  C  C   . LEU A 1 81   ? 28.045 38.163  21.595  1.00 16.46 ? 81   LEU A C   1 
ATOM   421  O  O   . LEU A 1 81   ? 28.155 38.601  22.758  1.00 14.99 ? 81   LEU A O   1 
ATOM   422  C  CB  . LEU A 1 81   ? 25.556 38.501  21.241  1.00 14.38 ? 81   LEU A CB  1 
ATOM   423  C  CG  . LEU A 1 81   ? 25.667 39.763  20.348  1.00 13.01 ? 81   LEU A CG  1 
ATOM   424  C  CD1 . LEU A 1 81   ? 25.587 39.339  18.886  1.00 12.32 ? 81   LEU A CD1 1 
ATOM   425  C  CD2 . LEU A 1 81   ? 24.511 40.742  20.637  1.00 12.20 ? 81   LEU A CD2 1 
ATOM   426  N  N   . LYS A 1 82   ? 29.044 38.188  20.730  1.00 15.65 ? 82   LYS A N   1 
ATOM   427  C  CA  . LYS A 1 82   ? 30.341 38.771  21.039  1.00 16.37 ? 82   LYS A CA  1 
ATOM   428  C  C   . LYS A 1 82   ? 30.249 40.229  20.569  1.00 16.33 ? 82   LYS A C   1 
ATOM   429  O  O   . LYS A 1 82   ? 30.079 40.488  19.374  1.00 15.15 ? 82   LYS A O   1 
ATOM   430  C  CB  . LYS A 1 82   ? 31.406 38.026  20.237  1.00 19.43 ? 82   LYS A CB  1 
ATOM   431  C  CG  . LYS A 1 82   ? 32.798 37.999  20.843  1.00 24.82 ? 82   LYS A CG  1 
ATOM   432  C  CD  . LYS A 1 82   ? 33.079 39.146  21.809  1.00 27.96 ? 82   LYS A CD  1 
ATOM   433  C  CE  . LYS A 1 82   ? 34.558 39.127  22.239  1.00 30.21 ? 82   LYS A CE  1 
ATOM   434  N  NZ  . LYS A 1 82   ? 35.011 37.822  22.798  1.00 31.59 ? 82   LYS A NZ  1 
ATOM   435  N  N   . VAL A 1 83   ? 30.398 41.180  21.492  1.00 14.58 ? 83   VAL A N   1 
ATOM   436  C  CA  . VAL A 1 83   ? 30.248 42.590  21.139  1.00 12.76 ? 83   VAL A CA  1 
ATOM   437  C  C   . VAL A 1 83   ? 31.572 43.341  21.260  1.00 13.60 ? 83   VAL A C   1 
ATOM   438  O  O   . VAL A 1 83   ? 32.230 43.284  22.309  1.00 12.31 ? 83   VAL A O   1 
ATOM   439  C  CB  . VAL A 1 83   ? 29.189 43.273  22.092  1.00 13.53 ? 83   VAL A CB  1 
ATOM   440  C  CG1 . VAL A 1 83   ? 28.973 44.759  21.725  1.00 12.80 ? 83   VAL A CG1 1 
ATOM   441  C  CG2 . VAL A 1 83   ? 27.858 42.527  22.002  1.00 12.83 ? 83   VAL A CG2 1 
ATOM   442  N  N   . PHE A 1 84   ? 31.962 44.039  20.191  1.00 12.61 ? 84   PHE A N   1 
ATOM   443  C  CA  . PHE A 1 84   ? 33.182 44.845  20.212  1.00 12.28 ? 84   PHE A CA  1 
ATOM   444  C  C   . PHE A 1 84   ? 32.815 46.331  20.145  1.00 11.94 ? 84   PHE A C   1 
ATOM   445  O  O   . PHE A 1 84   ? 32.278 46.804  19.145  1.00 10.95 ? 84   PHE A O   1 
ATOM   446  C  CB  . PHE A 1 84   ? 34.081 44.504  19.025  1.00 12.60 ? 84   PHE A CB  1 
ATOM   447  C  CG  . PHE A 1 84   ? 34.758 43.183  19.149  1.00 13.70 ? 84   PHE A CG  1 
ATOM   448  C  CD1 . PHE A 1 84   ? 34.358 42.118  18.378  1.00 14.41 ? 84   PHE A CD1 1 
ATOM   449  C  CD2 . PHE A 1 84   ? 35.794 43.006  20.076  1.00 13.53 ? 84   PHE A CD2 1 
ATOM   450  C  CE1 . PHE A 1 84   ? 34.977 40.874  18.513  1.00 15.05 ? 84   PHE A CE1 1 
ATOM   451  C  CE2 . PHE A 1 84   ? 36.422 41.779  20.230  1.00 13.87 ? 84   PHE A CE2 1 
ATOM   452  C  CZ  . PHE A 1 84   ? 36.015 40.697  19.443  1.00 14.59 ? 84   PHE A CZ  1 
ATOM   453  N  N   . VAL A 1 85   ? 33.107 47.059  21.208  1.00 10.80 ? 85   VAL A N   1 
ATOM   454  C  CA  . VAL A 1 85   ? 32.838 48.503  21.250  1.00 10.62 ? 85   VAL A CA  1 
ATOM   455  C  C   . VAL A 1 85   ? 34.146 49.133  20.815  1.00 9.97  ? 85   VAL A C   1 
ATOM   456  O  O   . VAL A 1 85   ? 35.159 48.982  21.494  1.00 10.64 ? 85   VAL A O   1 
ATOM   457  C  CB  . VAL A 1 85   ? 32.479 48.948  22.664  1.00 10.08 ? 85   VAL A CB  1 
ATOM   458  C  CG1 . VAL A 1 85   ? 32.335 50.481  22.730  1.00 9.10  ? 85   VAL A CG1 1 
ATOM   459  C  CG2 . VAL A 1 85   ? 31.175 48.209  23.088  1.00 9.29  ? 85   VAL A CG2 1 
ATOM   460  N  N   . VAL A 1 86   ? 34.111 49.836  19.690  1.00 8.94  ? 86   VAL A N   1 
ATOM   461  C  CA  . VAL A 1 86   ? 35.322 50.411  19.134  1.00 8.17  ? 86   VAL A CA  1 
ATOM   462  C  C   . VAL A 1 86   ? 35.411 51.943  19.218  1.00 7.85  ? 86   VAL A C   1 
ATOM   463  O  O   . VAL A 1 86   ? 34.817 52.653  18.445  1.00 8.26  ? 86   VAL A O   1 
ATOM   464  C  CB  . VAL A 1 86   ? 35.490 49.939  17.635  1.00 10.08 ? 86   VAL A CB  1 
ATOM   465  C  CG1 . VAL A 1 86   ? 36.850 50.407  17.069  1.00 8.17  ? 86   VAL A CG1 1 
ATOM   466  C  CG2 . VAL A 1 86   ? 35.371 48.418  17.528  1.00 8.06  ? 86   VAL A CG2 1 
ATOM   467  N  N   . PRO A 1 87   ? 36.179 52.458  20.177  1.00 8.19  ? 87   PRO A N   1 
ATOM   468  C  CA  . PRO A 1 87   ? 36.346 53.913  20.345  1.00 7.30  ? 87   PRO A CA  1 
ATOM   469  C  C   . PRO A 1 87   ? 37.035 54.533  19.125  1.00 8.70  ? 87   PRO A C   1 
ATOM   470  O  O   . PRO A 1 87   ? 38.004 53.962  18.583  1.00 8.00  ? 87   PRO A O   1 
ATOM   471  C  CB  . PRO A 1 87   ? 37.217 54.030  21.597  1.00 8.59  ? 87   PRO A CB  1 
ATOM   472  C  CG  . PRO A 1 87   ? 36.896 52.688  22.352  1.00 7.25  ? 87   PRO A CG  1 
ATOM   473  C  CD  . PRO A 1 87   ? 36.884 51.696  21.227  1.00 6.68  ? 87   PRO A CD  1 
ATOM   474  N  N   . HIS A 1 88   ? 36.572 55.714  18.729  1.00 8.68  ? 88   HIS A N   1 
ATOM   475  C  CA  . HIS A 1 88   ? 37.133 56.405  17.570  1.00 9.56  ? 88   HIS A CA  1 
ATOM   476  C  C   . HIS A 1 88   ? 36.840 57.899  17.647  1.00 9.29  ? 88   HIS A C   1 
ATOM   477  O  O   . HIS A 1 88   ? 35.994 58.348  18.429  1.00 8.41  ? 88   HIS A O   1 
ATOM   478  C  CB  . HIS A 1 88   ? 36.564 55.814  16.264  1.00 9.66  ? 88   HIS A CB  1 
ATOM   479  C  CG  . HIS A 1 88   ? 35.114 56.119  16.037  1.00 11.10 ? 88   HIS A CG  1 
ATOM   480  N  ND1 . HIS A 1 88   ? 34.687 57.212  15.311  1.00 11.47 ? 88   HIS A ND1 1 
ATOM   481  C  CD2 . HIS A 1 88   ? 33.992 55.469  16.434  1.00 11.93 ? 88   HIS A CD2 1 
ATOM   482  C  CE1 . HIS A 1 88   ? 33.367 57.217  15.261  1.00 11.21 ? 88   HIS A CE1 1 
ATOM   483  N  NE2 . HIS A 1 88   ? 32.918 56.170  15.935  1.00 12.41 ? 88   HIS A NE2 1 
ATOM   484  N  N   . SER A 1 89   ? 37.563 58.668  16.840  1.00 9.07  ? 89   SER A N   1 
ATOM   485  C  CA  . SER A 1 89   ? 37.413 60.122  16.819  1.00 8.99  ? 89   SER A CA  1 
ATOM   486  C  C   . SER A 1 89   ? 37.572 60.551  15.360  1.00 9.19  ? 89   SER A C   1 
ATOM   487  O  O   . SER A 1 89   ? 38.627 60.341  14.777  1.00 9.55  ? 89   SER A O   1 
ATOM   488  C  CB  . SER A 1 89   ? 38.523 60.725  17.684  1.00 8.09  ? 89   SER A CB  1 
ATOM   489  O  OG  . SER A 1 89   ? 38.491 62.127  17.658  1.00 10.10 ? 89   SER A OG  1 
ATOM   490  N  N   . HIS A 1 90   ? 36.526 61.124  14.767  1.00 9.04  ? 90   HIS A N   1 
ATOM   491  C  CA  . HIS A 1 90   ? 36.601 61.536  13.366  1.00 9.36  ? 90   HIS A CA  1 
ATOM   492  C  C   . HIS A 1 90   ? 37.249 62.911  13.274  1.00 10.76 ? 90   HIS A C   1 
ATOM   493  O  O   . HIS A 1 90   ? 36.671 63.928  13.702  1.00 10.65 ? 90   HIS A O   1 
ATOM   494  C  CB  . HIS A 1 90   ? 35.203 61.555  12.713  1.00 8.59  ? 90   HIS A CB  1 
ATOM   495  C  CG  . HIS A 1 90   ? 35.233 61.861  11.254  1.00 7.15  ? 90   HIS A CG  1 
ATOM   496  N  ND1 . HIS A 1 90   ? 35.813 61.019  10.331  1.00 8.88  ? 90   HIS A ND1 1 
ATOM   497  C  CD2 . HIS A 1 90   ? 34.811 62.946  10.562  1.00 6.58  ? 90   HIS A CD2 1 
ATOM   498  C  CE1 . HIS A 1 90   ? 35.747 61.566  9.129   1.00 9.10  ? 90   HIS A CE1 1 
ATOM   499  N  NE2 . HIS A 1 90   ? 35.143 62.736  9.243   1.00 7.56  ? 90   HIS A NE2 1 
ATOM   500  N  N   . ASN A 1 91   ? 38.462 62.933  12.734  1.00 9.55  ? 91   ASN A N   1 
ATOM   501  C  CA  . ASN A 1 91   ? 39.219 64.173  12.598  1.00 10.14 ? 91   ASN A CA  1 
ATOM   502  C  C   . ASN A 1 91   ? 39.344 64.584  11.137  1.00 10.94 ? 91   ASN A C   1 
ATOM   503  O  O   . ASN A 1 91   ? 39.820 63.794  10.305  1.00 11.20 ? 91   ASN A O   1 
ATOM   504  C  CB  . ASN A 1 91   ? 40.630 63.984  13.174  1.00 9.77  ? 91   ASN A CB  1 
ATOM   505  C  CG  . ASN A 1 91   ? 40.642 63.931  14.691  1.00 11.01 ? 91   ASN A CG  1 
ATOM   506  O  OD1 . ASN A 1 91   ? 41.188 64.818  15.336  1.00 10.98 ? 91   ASN A OD1 1 
ATOM   507  N  ND2 . ASN A 1 91   ? 40.037 62.896  15.264  1.00 10.32 ? 91   ASN A ND2 1 
ATOM   508  N  N   . ASP A 1 92   ? 38.943 65.817  10.854  1.00 9.72  ? 92   ASP A N   1 
ATOM   509  C  CA  . ASP A 1 92   ? 39.002 66.371  9.503   1.00 11.42 ? 92   ASP A CA  1 
ATOM   510  C  C   . ASP A 1 92   ? 40.263 67.228  9.260   1.00 10.38 ? 92   ASP A C   1 
ATOM   511  O  O   . ASP A 1 92   ? 40.465 68.214  9.955   1.00 10.91 ? 92   ASP A O   1 
ATOM   512  C  CB  . ASP A 1 92   ? 37.784 67.270  9.245   1.00 9.75  ? 92   ASP A CB  1 
ATOM   513  C  CG  . ASP A 1 92   ? 36.495 66.492  9.213   1.00 12.50 ? 92   ASP A CG  1 
ATOM   514  O  OD1 . ASP A 1 92   ? 36.480 65.454  8.540   1.00 13.17 ? 92   ASP A OD1 1 
ATOM   515  O  OD2 . ASP A 1 92   ? 35.515 66.896  9.858   1.00 12.88 ? 92   ASP A OD2 1 
ATOM   516  N  N   . PRO A 1 93   ? 41.110 66.854  8.280   1.00 11.20 ? 93   PRO A N   1 
ATOM   517  C  CA  . PRO A 1 93   ? 42.331 67.591  7.928   1.00 10.94 ? 93   PRO A CA  1 
ATOM   518  C  C   . PRO A 1 93   ? 41.845 68.852  7.186   1.00 11.41 ? 93   PRO A C   1 
ATOM   519  O  O   . PRO A 1 93   ? 42.063 69.020  5.980   1.00 10.81 ? 93   PRO A O   1 
ATOM   520  C  CB  . PRO A 1 93   ? 43.048 66.632  6.997   1.00 11.44 ? 93   PRO A CB  1 
ATOM   521  C  CG  . PRO A 1 93   ? 42.610 65.275  7.496   1.00 12.32 ? 93   PRO A CG  1 
ATOM   522  C  CD  . PRO A 1 93   ? 41.131 65.516  7.669   1.00 11.76 ? 93   PRO A CD  1 
ATOM   523  N  N   . GLY A 1 94   ? 41.137 69.695  7.941   1.00 10.94 ? 94   GLY A N   1 
ATOM   524  C  CA  . GLY A 1 94   ? 40.551 70.918  7.428   1.00 10.04 ? 94   GLY A CA  1 
ATOM   525  C  C   . GLY A 1 94   ? 39.082 70.672  7.130   1.00 10.75 ? 94   GLY A C   1 
ATOM   526  O  O   . GLY A 1 94   ? 38.732 69.598  6.612   1.00 10.09 ? 94   GLY A O   1 
ATOM   527  N  N   . TRP A 1 95   ? 38.226 71.630  7.496   1.00 9.23  ? 95   TRP A N   1 
ATOM   528  C  CA  . TRP A 1 95   ? 36.780 71.609  7.185   1.00 10.39 ? 95   TRP A CA  1 
ATOM   529  C  C   . TRP A 1 95   ? 36.257 73.012  7.588   1.00 12.09 ? 95   TRP A C   1 
ATOM   530  O  O   . TRP A 1 95   ? 36.178 73.937  6.754   1.00 10.64 ? 95   TRP A O   1 
ATOM   531  C  CB  . TRP A 1 95   ? 36.022 70.492  7.941   1.00 7.97  ? 95   TRP A CB  1 
ATOM   532  C  CG  . TRP A 1 95   ? 34.508 70.549  7.645   1.00 9.54  ? 95   TRP A CG  1 
ATOM   533  C  CD1 . TRP A 1 95   ? 33.916 70.995  6.478   1.00 7.89  ? 95   TRP A CD1 1 
ATOM   534  C  CD2 . TRP A 1 95   ? 33.431 70.186  8.518   1.00 7.99  ? 95   TRP A CD2 1 
ATOM   535  N  NE1 . TRP A 1 95   ? 32.549 70.946  6.586   1.00 10.16 ? 95   TRP A NE1 1 
ATOM   536  C  CE2 . TRP A 1 95   ? 32.219 70.448  7.822   1.00 8.25  ? 95   TRP A CE2 1 
ATOM   537  C  CE3 . TRP A 1 95   ? 33.367 69.664  9.825   1.00 8.23  ? 95   TRP A CE3 1 
ATOM   538  C  CZ2 . TRP A 1 95   ? 30.956 70.203  8.385   1.00 9.08  ? 95   TRP A CZ2 1 
ATOM   539  C  CZ3 . TRP A 1 95   ? 32.097 69.418  10.396  1.00 8.35  ? 95   TRP A CZ3 1 
ATOM   540  C  CH2 . TRP A 1 95   ? 30.912 69.687  9.671   1.00 8.13  ? 95   TRP A CH2 1 
ATOM   541  N  N   . ILE A 1 96   ? 35.968 73.161  8.884   1.00 12.98 ? 96   ILE A N   1 
ATOM   542  C  CA  . ILE A 1 96   ? 35.517 74.428  9.484   1.00 14.85 ? 96   ILE A CA  1 
ATOM   543  C  C   . ILE A 1 96   ? 36.737 75.252  9.917   1.00 14.95 ? 96   ILE A C   1 
ATOM   544  O  O   . ILE A 1 96   ? 36.668 76.466  9.970   1.00 15.39 ? 96   ILE A O   1 
ATOM   545  C  CB  . ILE A 1 96   ? 34.644 74.179  10.729  1.00 16.71 ? 96   ILE A CB  1 
ATOM   546  C  CG1 . ILE A 1 96   ? 33.427 73.366  10.314  1.00 17.75 ? 96   ILE A CG1 1 
ATOM   547  C  CG2 . ILE A 1 96   ? 34.186 75.516  11.348  1.00 19.66 ? 96   ILE A CG2 1 
ATOM   548  C  CD1 . ILE A 1 96   ? 32.857 73.846  8.991   1.00 15.97 ? 96   ILE A CD1 1 
ATOM   549  N  N   . GLN A 1 97   ? 37.840 74.574  10.235  1.00 14.38 ? 97   GLN A N   1 
ATOM   550  C  CA  . GLN A 1 97   ? 39.103 75.228  10.580  1.00 13.71 ? 97   GLN A CA  1 
ATOM   551  C  C   . GLN A 1 97   ? 40.130 74.637  9.585   1.00 12.34 ? 97   GLN A C   1 
ATOM   552  O  O   . GLN A 1 97   ? 39.852 73.642  8.909   1.00 11.59 ? 97   GLN A O   1 
ATOM   553  C  CB  . GLN A 1 97   ? 39.495 74.877  12.014  1.00 14.67 ? 97   GLN A CB  1 
ATOM   554  C  CG  . GLN A 1 97   ? 38.513 75.381  13.104  1.00 17.86 ? 97   GLN A CG  1 
ATOM   555  C  CD  . GLN A 1 97   ? 39.036 75.114  14.539  1.00 20.04 ? 97   GLN A CD  1 
ATOM   556  O  OE1 . GLN A 1 97   ? 40.151 75.515  14.888  1.00 21.78 ? 97   GLN A OE1 1 
ATOM   557  N  NE2 . GLN A 1 97   ? 38.234 74.422  15.365  1.00 20.13 ? 97   GLN A NE2 1 
ATOM   558  N  N   . THR A 1 98   ? 41.305 75.235  9.466   1.00 10.66 ? 98   THR A N   1 
ATOM   559  C  CA  . THR A 1 98   ? 42.314 74.661  8.588   1.00 10.47 ? 98   THR A CA  1 
ATOM   560  C  C   . THR A 1 98   ? 42.965 73.461  9.297   1.00 10.91 ? 98   THR A C   1 
ATOM   561  O  O   . THR A 1 98   ? 42.783 73.235  10.512  1.00 10.78 ? 98   THR A O   1 
ATOM   562  C  CB  . THR A 1 98   ? 43.449 75.628  8.324   1.00 11.07 ? 98   THR A CB  1 
ATOM   563  O  OG1 . THR A 1 98   ? 44.096 75.915  9.577   1.00 12.68 ? 98   THR A OG1 1 
ATOM   564  C  CG2 . THR A 1 98   ? 42.927 76.962  7.730   1.00 9.88  ? 98   THR A CG2 1 
ATOM   565  N  N   . PHE A 1 99   ? 43.704 72.674  8.531   1.00 9.25  ? 99   PHE A N   1 
ATOM   566  C  CA  . PHE A 1 99   ? 44.452 71.551  9.099   1.00 9.89  ? 99   PHE A CA  1 
ATOM   567  C  C   . PHE A 1 99   ? 45.220 71.986  10.367  1.00 10.26 ? 99   PHE A C   1 
ATOM   568  O  O   . PHE A 1 99   ? 45.083 71.382  11.425  1.00 10.04 ? 99   PHE A O   1 
ATOM   569  C  CB  . PHE A 1 99   ? 45.477 71.037  8.081   1.00 8.24  ? 99   PHE A CB  1 
ATOM   570  C  CG  . PHE A 1 99   ? 46.348 69.897  8.612   1.00 10.69 ? 99   PHE A CG  1 
ATOM   571  C  CD1 . PHE A 1 99   ? 45.948 68.561  8.473   1.00 8.53  ? 99   PHE A CD1 1 
ATOM   572  C  CD2 . PHE A 1 99   ? 47.547 70.168  9.257   1.00 9.33  ? 99   PHE A CD2 1 
ATOM   573  C  CE1 . PHE A 1 99   ? 46.733 67.521  8.972   1.00 11.04 ? 99   PHE A CE1 1 
ATOM   574  C  CE2 . PHE A 1 99   ? 48.337 69.136  9.758   1.00 12.54 ? 99   PHE A CE2 1 
ATOM   575  C  CZ  . PHE A 1 99   ? 47.922 67.797  9.611   1.00 10.18 ? 99   PHE A CZ  1 
ATOM   576  N  N   . GLU A 1 100  ? 46.037 73.034  10.257  1.00 10.75 ? 100  GLU A N   1 
ATOM   577  C  CA  . GLU A 1 100  ? 46.835 73.491  11.396  1.00 11.57 ? 100  GLU A CA  1 
ATOM   578  C  C   . GLU A 1 100  ? 46.007 74.028  12.553  1.00 10.86 ? 100  GLU A C   1 
ATOM   579  O  O   . GLU A 1 100  ? 46.360 73.820  13.707  1.00 10.65 ? 100  GLU A O   1 
ATOM   580  C  CB  . GLU A 1 100  ? 47.847 74.556  10.931  1.00 12.21 ? 100  GLU A CB  1 
ATOM   581  C  CG  . GLU A 1 100  ? 48.868 74.965  11.962  1.00 14.02 ? 100  GLU A CG  1 
ATOM   582  C  CD  . GLU A 1 100  ? 49.732 73.808  12.430  1.00 16.09 ? 100  GLU A CD  1 
ATOM   583  O  OE1 . GLU A 1 100  ? 49.843 72.790  11.686  1.00 13.49 ? 100  GLU A OE1 1 
ATOM   584  O  OE2 . GLU A 1 100  ? 50.309 73.927  13.542  1.00 16.34 ? 100  GLU A OE2 1 
ATOM   585  N  N   . GLU A 1 101  ? 44.908 74.718  12.258  1.00 11.54 ? 101  GLU A N   1 
ATOM   586  C  CA  . GLU A 1 101  ? 44.054 75.230  13.338  1.00 13.07 ? 101  GLU A CA  1 
ATOM   587  C  C   . GLU A 1 101  ? 43.462 74.033  14.123  1.00 12.64 ? 101  GLU A C   1 
ATOM   588  O  O   . GLU A 1 101  ? 43.492 73.995  15.359  1.00 10.67 ? 101  GLU A O   1 
ATOM   589  C  CB  . GLU A 1 101  ? 42.924 76.102  12.758  1.00 16.20 ? 101  GLU A CB  1 
ATOM   590  C  CG  . GLU A 1 101  ? 43.479 77.355  12.046  1.00 18.42 ? 101  GLU A CG  1 
ATOM   591  C  CD  . GLU A 1 101  ? 42.399 78.208  11.379  1.00 20.90 ? 101  GLU A CD  1 
ATOM   592  O  OE1 . GLU A 1 101  ? 41.420 77.661  10.823  1.00 17.36 ? 101  GLU A OE1 1 
ATOM   593  O  OE2 . GLU A 1 101  ? 42.552 79.443  11.404  1.00 21.22 ? 101  GLU A OE2 1 
ATOM   594  N  N   . TYR A 1 102  ? 42.925 73.060  13.392  1.00 11.58 ? 102  TYR A N   1 
ATOM   595  C  CA  . TYR A 1 102  ? 42.385 71.875  14.045  1.00 12.33 ? 102  TYR A CA  1 
ATOM   596  C  C   . TYR A 1 102  ? 43.486 71.153  14.835  1.00 12.53 ? 102  TYR A C   1 
ATOM   597  O  O   . TYR A 1 102  ? 43.266 70.698  15.962  1.00 12.18 ? 102  TYR A O   1 
ATOM   598  C  CB  . TYR A 1 102  ? 41.832 70.897  13.027  1.00 12.22 ? 102  TYR A CB  1 
ATOM   599  C  CG  . TYR A 1 102  ? 40.420 71.157  12.631  1.00 12.56 ? 102  TYR A CG  1 
ATOM   600  C  CD1 . TYR A 1 102  ? 39.430 71.402  13.600  1.00 13.11 ? 102  TYR A CD1 1 
ATOM   601  C  CD2 . TYR A 1 102  ? 40.032 71.018  11.296  1.00 11.86 ? 102  TYR A CD2 1 
ATOM   602  C  CE1 . TYR A 1 102  ? 38.067 71.478  13.231  1.00 13.21 ? 102  TYR A CE1 1 
ATOM   603  C  CE2 . TYR A 1 102  ? 38.714 71.100  10.921  1.00 12.46 ? 102  TYR A CE2 1 
ATOM   604  C  CZ  . TYR A 1 102  ? 37.725 71.323  11.877  1.00 12.25 ? 102  TYR A CZ  1 
ATOM   605  O  OH  . TYR A 1 102  ? 36.426 71.385  11.440  1.00 10.88 ? 102  TYR A OH  1 
ATOM   606  N  N   . TYR A 1 103  ? 44.669 71.031  14.235  1.00 11.84 ? 103  TYR A N   1 
ATOM   607  C  CA  . TYR A 1 103  ? 45.724 70.337  14.955  1.00 13.16 ? 103  TYR A CA  1 
ATOM   608  C  C   . TYR A 1 103  ? 46.034 71.029  16.289  1.00 13.72 ? 103  TYR A C   1 
ATOM   609  O  O   . TYR A 1 103  ? 46.179 70.359  17.320  1.00 12.37 ? 103  TYR A O   1 
ATOM   610  C  CB  . TYR A 1 103  ? 46.995 70.261  14.136  1.00 11.76 ? 103  TYR A CB  1 
ATOM   611  C  CG  . TYR A 1 103  ? 48.119 69.612  14.888  1.00 12.82 ? 103  TYR A CG  1 
ATOM   612  C  CD1 . TYR A 1 103  ? 48.091 68.236  15.172  1.00 11.66 ? 103  TYR A CD1 1 
ATOM   613  C  CD2 . TYR A 1 103  ? 49.215 70.377  15.356  1.00 13.10 ? 103  TYR A CD2 1 
ATOM   614  C  CE1 . TYR A 1 103  ? 49.118 67.646  15.901  1.00 13.68 ? 103  TYR A CE1 1 
ATOM   615  C  CE2 . TYR A 1 103  ? 50.252 69.793  16.097  1.00 11.86 ? 103  TYR A CE2 1 
ATOM   616  C  CZ  . TYR A 1 103  ? 50.194 68.429  16.367  1.00 13.28 ? 103  TYR A CZ  1 
ATOM   617  O  OH  . TYR A 1 103  ? 51.186 67.831  17.112  1.00 14.88 ? 103  TYR A OH  1 
ATOM   618  N  N   . GLN A 1 104  ? 46.139 72.357  16.272  1.00 14.24 ? 104  GLN A N   1 
ATOM   619  C  CA  . GLN A 1 104  ? 46.460 73.090  17.498  1.00 15.34 ? 104  GLN A CA  1 
ATOM   620  C  C   . GLN A 1 104  ? 45.310 73.111  18.461  1.00 16.41 ? 104  GLN A C   1 
ATOM   621  O  O   . GLN A 1 104  ? 45.509 73.010  19.672  1.00 17.58 ? 104  GLN A O   1 
ATOM   622  C  CB  . GLN A 1 104  ? 46.845 74.550  17.207  1.00 16.08 ? 104  GLN A CB  1 
ATOM   623  C  CG  . GLN A 1 104  ? 48.168 74.738  16.471  1.00 14.82 ? 104  GLN A CG  1 
ATOM   624  C  CD  . GLN A 1 104  ? 49.344 74.147  17.245  1.00 18.36 ? 104  GLN A CD  1 
ATOM   625  O  OE1 . GLN A 1 104  ? 49.376 74.193  18.487  1.00 17.47 ? 104  GLN A OE1 1 
ATOM   626  N  NE2 . GLN A 1 104  ? 50.328 73.603  16.518  1.00 16.54 ? 104  GLN A NE2 1 
ATOM   627  N  N   . HIS A 1 105  ? 44.094 73.240  17.949  1.00 16.79 ? 105  HIS A N   1 
ATOM   628  C  CA  . HIS A 1 105  ? 42.939 73.356  18.838  1.00 17.57 ? 105  HIS A CA  1 
ATOM   629  C  C   . HIS A 1 105  ? 42.318 72.075  19.372  1.00 17.47 ? 105  HIS A C   1 
ATOM   630  O  O   . HIS A 1 105  ? 41.755 72.090  20.459  1.00 16.89 ? 105  HIS A O   1 
ATOM   631  C  CB  . HIS A 1 105  ? 41.843 74.177  18.151  1.00 19.41 ? 105  HIS A CB  1 
ATOM   632  C  CG  . HIS A 1 105  ? 42.290 75.547  17.740  1.00 22.01 ? 105  HIS A CG  1 
ATOM   633  N  ND1 . HIS A 1 105  ? 41.615 76.304  16.802  1.00 23.37 ? 105  HIS A ND1 1 
ATOM   634  C  CD2 . HIS A 1 105  ? 43.350 76.293  18.136  1.00 22.97 ? 105  HIS A CD2 1 
ATOM   635  C  CE1 . HIS A 1 105  ? 42.243 77.456  16.641  1.00 23.71 ? 105  HIS A CE1 1 
ATOM   636  N  NE2 . HIS A 1 105  ? 43.298 77.474  17.437  1.00 23.54 ? 105  HIS A NE2 1 
ATOM   637  N  N   . ASP A 1 106  ? 42.420 70.984  18.611  1.00 15.89 ? 106  ASP A N   1 
ATOM   638  C  CA  . ASP A 1 106  ? 41.801 69.723  19.010  1.00 15.68 ? 106  ASP A CA  1 
ATOM   639  C  C   . ASP A 1 106  ? 42.628 68.464  18.879  1.00 14.08 ? 106  ASP A C   1 
ATOM   640  O  O   . ASP A 1 106  ? 42.858 67.734  19.858  1.00 14.14 ? 106  ASP A O   1 
ATOM   641  C  CB  . ASP A 1 106  ? 40.521 69.509  18.182  1.00 17.53 ? 106  ASP A CB  1 
ATOM   642  C  CG  . ASP A 1 106  ? 39.499 70.639  18.364  1.00 19.10 ? 106  ASP A CG  1 
ATOM   643  O  OD1 . ASP A 1 106  ? 38.766 70.630  19.360  1.00 21.25 ? 106  ASP A OD1 1 
ATOM   644  O  OD2 . ASP A 1 106  ? 39.449 71.544  17.519  1.00 20.41 ? 106  ASP A OD2 1 
ATOM   645  N  N   . THR A 1 107  ? 43.063 68.195  17.651  1.00 12.93 ? 107  THR A N   1 
ATOM   646  C  CA  . THR A 1 107  ? 43.768 66.955  17.369  1.00 11.45 ? 107  THR A CA  1 
ATOM   647  C  C   . THR A 1 107  ? 45.019 66.661  18.181  1.00 10.73 ? 107  THR A C   1 
ATOM   648  O  O   . THR A 1 107  ? 45.210 65.528  18.628  1.00 9.92  ? 107  THR A O   1 
ATOM   649  C  CB  . THR A 1 107  ? 44.098 66.856  15.882  1.00 11.51 ? 107  THR A CB  1 
ATOM   650  O  OG1 . THR A 1 107  ? 42.905 67.080  15.125  1.00 11.45 ? 107  THR A OG1 1 
ATOM   651  C  CG2 . THR A 1 107  ? 44.654 65.478  15.552  1.00 10.74 ? 107  THR A CG2 1 
ATOM   652  N  N   . LYS A 1 108  ? 45.895 67.636  18.377  1.00 10.70 ? 108  LYS A N   1 
ATOM   653  C  CA  . LYS A 1 108  ? 47.073 67.300  19.193  1.00 11.42 ? 108  LYS A CA  1 
ATOM   654  C  C   . LYS A 1 108  ? 46.640 66.923  20.614  1.00 10.95 ? 108  LYS A C   1 
ATOM   655  O  O   . LYS A 1 108  ? 47.286 66.096  21.250  1.00 11.19 ? 108  LYS A O   1 
ATOM   656  C  CB  . LYS A 1 108  ? 48.107 68.448  19.242  1.00 12.48 ? 108  LYS A CB  1 
ATOM   657  C  CG  . LYS A 1 108  ? 47.714 69.700  20.029  1.00 15.12 ? 108  LYS A CG  1 
ATOM   658  C  CD  . LYS A 1 108  ? 48.878 70.720  19.937  1.00 15.38 ? 108  LYS A CD  1 
ATOM   659  C  CE  . LYS A 1 108  ? 48.664 71.928  20.832  1.00 16.89 ? 108  LYS A CE  1 
ATOM   660  N  NZ  . LYS A 1 108  ? 49.860 72.801  20.800  1.00 16.78 ? 108  LYS A NZ  1 
ATOM   661  N  N   . HIS A 1 109  ? 45.534 67.498  21.096  1.00 10.71 ? 109  HIS A N   1 
ATOM   662  C  CA  . HIS A 1 109  ? 45.066 67.175  22.444  1.00 12.35 ? 109  HIS A CA  1 
ATOM   663  C  C   . HIS A 1 109  ? 44.447 65.793  22.441  1.00 12.26 ? 109  HIS A C   1 
ATOM   664  O  O   . HIS A 1 109  ? 44.625 65.024  23.386  1.00 12.45 ? 109  HIS A O   1 
ATOM   665  C  CB  . HIS A 1 109  ? 44.066 68.222  22.937  1.00 13.15 ? 109  HIS A CB  1 
ATOM   666  C  CG  . HIS A 1 109  ? 44.644 69.594  22.968  1.00 15.56 ? 109  HIS A CG  1 
ATOM   667  N  ND1 . HIS A 1 109  ? 45.713 69.929  23.781  1.00 18.09 ? 109  HIS A ND1 1 
ATOM   668  C  CD2 . HIS A 1 109  ? 44.418 70.671  22.181  1.00 16.18 ? 109  HIS A CD2 1 
ATOM   669  C  CE1 . HIS A 1 109  ? 46.120 71.153  23.486  1.00 17.26 ? 109  HIS A CE1 1 
ATOM   670  N  NE2 . HIS A 1 109  ? 45.353 71.622  22.515  1.00 16.81 ? 109  HIS A NE2 1 
ATOM   671  N  N   . ILE A 1 110  ? 43.724 65.470  21.367  1.00 12.52 ? 110  ILE A N   1 
ATOM   672  C  CA  . ILE A 1 110  ? 43.119 64.147  21.250  1.00 13.07 ? 110  ILE A CA  1 
ATOM   673  C  C   . ILE A 1 110  ? 44.211 63.078  21.244  1.00 13.29 ? 110  ILE A C   1 
ATOM   674  O  O   . ILE A 1 110  ? 44.136 62.059  21.953  1.00 14.13 ? 110  ILE A O   1 
ATOM   675  C  CB  . ILE A 1 110  ? 42.292 64.028  19.933  1.00 12.06 ? 110  ILE A CB  1 
ATOM   676  C  CG1 . ILE A 1 110  ? 41.057 64.945  20.017  1.00 11.11 ? 110  ILE A CG1 1 
ATOM   677  C  CG2 . ILE A 1 110  ? 41.890 62.550  19.684  1.00 12.10 ? 110  ILE A CG2 1 
ATOM   678  C  CD1 . ILE A 1 110  ? 40.270 65.079  18.682  1.00 11.22 ? 110  ILE A CD1 1 
ATOM   679  N  N   . LEU A 1 111  ? 45.240 63.293  20.436  1.00 12.75 ? 111  LEU A N   1 
ATOM   680  C  CA  . LEU A 1 111  ? 46.298 62.296  20.370  1.00 13.23 ? 111  LEU A CA  1 
ATOM   681  C  C   . LEU A 1 111  ? 47.145 62.226  21.649  1.00 13.37 ? 111  LEU A C   1 
ATOM   682  O  O   . LEU A 1 111  ? 47.524 61.140  22.088  1.00 13.33 ? 111  LEU A O   1 
ATOM   683  C  CB  . LEU A 1 111  ? 47.184 62.555  19.128  1.00 13.43 ? 111  LEU A CB  1 
ATOM   684  C  CG  . LEU A 1 111  ? 46.421 62.253  17.819  1.00 12.66 ? 111  LEU A CG  1 
ATOM   685  C  CD1 . LEU A 1 111  ? 47.261 62.653  16.584  1.00 10.13 ? 111  LEU A CD1 1 
ATOM   686  C  CD2 . LEU A 1 111  ? 46.067 60.763  17.810  1.00 12.26 ? 111  LEU A CD2 1 
ATOM   687  N  N   . SER A 1 112  ? 47.421 63.369  22.255  1.00 12.37 ? 112  SER A N   1 
ATOM   688  C  CA  . SER A 1 112  ? 48.199 63.388  23.484  1.00 13.34 ? 112  SER A CA  1 
ATOM   689  C  C   . SER A 1 112  ? 47.442 62.637  24.597  1.00 13.47 ? 112  SER A C   1 
ATOM   690  O  O   . SER A 1 112  ? 48.024 61.811  25.327  1.00 12.89 ? 112  SER A O   1 
ATOM   691  C  CB  . SER A 1 112  ? 48.476 64.838  23.912  1.00 14.71 ? 112  SER A CB  1 
ATOM   692  O  OG  . SER A 1 112  ? 49.172 64.802  25.148  1.00 18.22 ? 112  SER A OG  1 
ATOM   693  N  N   . ASN A 1 113  ? 46.148 62.918  24.726  1.00 11.29 ? 113  ASN A N   1 
ATOM   694  C  CA  . ASN A 1 113  ? 45.354 62.219  25.729  1.00 12.76 ? 113  ASN A CA  1 
ATOM   695  C  C   . ASN A 1 113  ? 45.110 60.742  25.401  1.00 12.26 ? 113  ASN A C   1 
ATOM   696  O  O   . ASN A 1 113  ? 44.976 59.924  26.307  1.00 12.02 ? 113  ASN A O   1 
ATOM   697  C  CB  . ASN A 1 113  ? 44.056 62.985  26.002  1.00 13.03 ? 113  ASN A CB  1 
ATOM   698  C  CG  . ASN A 1 113  ? 44.344 64.259  26.798  1.00 16.09 ? 113  ASN A CG  1 
ATOM   699  O  OD1 . ASN A 1 113  ? 45.208 64.237  27.671  1.00 20.70 ? 113  ASN A OD1 1 
ATOM   700  N  ND2 . ASN A 1 113  ? 43.689 65.356  26.482  1.00 15.99 ? 113  ASN A ND2 1 
ATOM   701  N  N   . ALA A 1 114  ? 45.060 60.400  24.115  1.00 10.57 ? 114  ALA A N   1 
ATOM   702  C  CA  . ALA A 1 114  ? 44.907 58.996  23.725  1.00 11.52 ? 114  ALA A CA  1 
ATOM   703  C  C   . ALA A 1 114  ? 46.175 58.259  24.196  1.00 11.27 ? 114  ALA A C   1 
ATOM   704  O  O   . ALA A 1 114  ? 46.106 57.142  24.714  1.00 10.01 ? 114  ALA A O   1 
ATOM   705  C  CB  . ALA A 1 114  ? 44.790 58.893  22.219  1.00 10.84 ? 114  ALA A CB  1 
ATOM   706  N  N   . LEU A 1 115  ? 47.344 58.876  24.007  1.00 10.15 ? 115  LEU A N   1 
ATOM   707  C  CA  . LEU A 1 115  ? 48.583 58.231  24.422  1.00 12.73 ? 115  LEU A CA  1 
ATOM   708  C  C   . LEU A 1 115  ? 48.571 57.994  25.954  1.00 14.15 ? 115  LEU A C   1 
ATOM   709  O  O   . LEU A 1 115  ? 48.826 56.884  26.438  1.00 14.68 ? 115  LEU A O   1 
ATOM   710  C  CB  . LEU A 1 115  ? 49.807 59.091  23.999  1.00 12.56 ? 115  LEU A CB  1 
ATOM   711  C  CG  . LEU A 1 115  ? 51.191 58.612  24.443  1.00 14.16 ? 115  LEU A CG  1 
ATOM   712  C  CD1 . LEU A 1 115  ? 51.406 57.165  23.984  1.00 13.76 ? 115  LEU A CD1 1 
ATOM   713  C  CD2 . LEU A 1 115  ? 52.287 59.513  23.911  1.00 14.02 ? 115  LEU A CD2 1 
ATOM   714  N  N   . ARG A 1 116  ? 48.229 59.030  26.705  1.00 15.27 ? 116  ARG A N   1 
ATOM   715  C  CA  . ARG A 1 116  ? 48.193 58.920  28.146  1.00 16.80 ? 116  ARG A CA  1 
ATOM   716  C  C   . ARG A 1 116  ? 47.162 57.880  28.601  1.00 16.55 ? 116  ARG A C   1 
ATOM   717  O  O   . ARG A 1 116  ? 47.488 56.945  29.344  1.00 17.37 ? 116  ARG A O   1 
ATOM   718  C  CB  . ARG A 1 116  ? 47.863 60.282  28.753  1.00 18.88 ? 116  ARG A CB  1 
ATOM   719  C  CG  . ARG A 1 116  ? 47.622 60.236  30.278  1.00 23.19 ? 116  ARG A CG  1 
ATOM   720  C  CD  . ARG A 1 116  ? 46.913 61.528  30.723  1.00 27.71 ? 116  ARG A CD  1 
ATOM   721  N  NE  . ARG A 1 116  ? 46.384 61.437  32.087  1.00 31.38 ? 116  ARG A NE  1 
ATOM   722  C  CZ  . ARG A 1 116  ? 45.907 62.476  32.775  1.00 33.56 ? 116  ARG A CZ  1 
ATOM   723  N  NH1 . ARG A 1 116  ? 45.889 63.694  32.226  1.00 33.70 ? 116  ARG A NH1 1 
ATOM   724  N  NH2 . ARG A 1 116  ? 45.456 62.299  34.018  1.00 34.79 ? 116  ARG A NH2 1 
ATOM   725  N  N   . HIS A 1 117  ? 45.922 58.034  28.147  1.00 16.21 ? 117  HIS A N   1 
ATOM   726  C  CA  . HIS A 1 117  ? 44.893 57.105  28.544  1.00 16.78 ? 117  HIS A CA  1 
ATOM   727  C  C   . HIS A 1 117  ? 45.063 55.659  28.170  1.00 16.33 ? 117  HIS A C   1 
ATOM   728  O  O   . HIS A 1 117  ? 44.763 54.810  29.008  1.00 15.91 ? 117  HIS A O   1 
ATOM   729  C  CB  . HIS A 1 117  ? 43.523 57.620  28.143  1.00 19.81 ? 117  HIS A CB  1 
ATOM   730  C  CG  . HIS A 1 117  ? 42.987 58.612  29.129  1.00 25.00 ? 117  HIS A CG  1 
ATOM   731  N  ND1 . HIS A 1 117  ? 42.270 58.229  30.245  1.00 24.95 ? 117  HIS A ND1 1 
ATOM   732  C  CD2 . HIS A 1 117  ? 43.250 59.937  29.287  1.00 26.51 ? 117  HIS A CD2 1 
ATOM   733  C  CE1 . HIS A 1 117  ? 42.132 59.267  31.056  1.00 27.93 ? 117  HIS A CE1 1 
ATOM   734  N  NE2 . HIS A 1 117  ? 42.720 60.315  30.502  1.00 28.84 ? 117  HIS A NE2 1 
ATOM   735  N  N   . LEU A 1 118  ? 45.552 55.356  26.963  1.00 13.80 ? 118  LEU A N   1 
ATOM   736  C  CA  . LEU A 1 118  ? 45.759 53.964  26.588  1.00 14.35 ? 118  LEU A CA  1 
ATOM   737  C  C   . LEU A 1 118  ? 46.963 53.417  27.356  1.00 14.67 ? 118  LEU A C   1 
ATOM   738  O  O   . LEU A 1 118  ? 46.998 52.257  27.747  1.00 15.00 ? 118  LEU A O   1 
ATOM   739  C  CB  . LEU A 1 118  ? 45.996 53.815  25.069  1.00 14.23 ? 118  LEU A CB  1 
ATOM   740  C  CG  . LEU A 1 118  ? 44.800 54.300  24.201  1.00 15.62 ? 118  LEU A CG  1 
ATOM   741  C  CD1 . LEU A 1 118  ? 45.121 54.190  22.720  1.00 14.82 ? 118  LEU A CD1 1 
ATOM   742  C  CD2 . LEU A 1 118  ? 43.585 53.492  24.526  1.00 14.76 ? 118  LEU A CD2 1 
ATOM   743  N  N   . HIS A 1 119  ? 47.974 54.246  27.551  1.00 15.08 ? 119  HIS A N   1 
ATOM   744  C  CA  . HIS A 1 119  ? 49.146 53.794  28.287  1.00 15.58 ? 119  HIS A CA  1 
ATOM   745  C  C   . HIS A 1 119  ? 48.719 53.346  29.698  1.00 16.12 ? 119  HIS A C   1 
ATOM   746  O  O   . HIS A 1 119  ? 49.122 52.281  30.156  1.00 15.64 ? 119  HIS A O   1 
ATOM   747  C  CB  . HIS A 1 119  ? 50.172 54.940  28.368  1.00 15.95 ? 119  HIS A CB  1 
ATOM   748  C  CG  . HIS A 1 119  ? 51.341 54.647  29.247  1.00 18.59 ? 119  HIS A CG  1 
ATOM   749  N  ND1 . HIS A 1 119  ? 51.364 54.973  30.588  1.00 19.95 ? 119  HIS A ND1 1 
ATOM   750  C  CD2 . HIS A 1 119  ? 52.521 54.032  28.988  1.00 19.68 ? 119  HIS A CD2 1 
ATOM   751  C  CE1 . HIS A 1 119  ? 52.507 54.570  31.115  1.00 20.90 ? 119  HIS A CE1 1 
ATOM   752  N  NE2 . HIS A 1 119  ? 53.226 53.993  30.166  1.00 21.08 ? 119  HIS A NE2 1 
ATOM   753  N  N   . ASP A 1 120  ? 47.876 54.148  30.350  1.00 16.01 ? 120  ASP A N   1 
ATOM   754  C  CA  . ASP A 1 120  ? 47.417 53.864  31.721  1.00 16.70 ? 120  ASP A CA  1 
ATOM   755  C  C   . ASP A 1 120  ? 46.273 52.867  31.907  1.00 17.04 ? 120  ASP A C   1 
ATOM   756  O  O   . ASP A 1 120  ? 46.035 52.416  33.007  1.00 17.79 ? 120  ASP A O   1 
ATOM   757  C  CB  . ASP A 1 120  ? 47.013 55.152  32.418  1.00 15.43 ? 120  ASP A CB  1 
ATOM   758  C  CG  . ASP A 1 120  ? 48.186 56.063  32.670  1.00 17.50 ? 120  ASP A CG  1 
ATOM   759  O  OD1 . ASP A 1 120  ? 49.321 55.570  32.743  1.00 18.70 ? 120  ASP A OD1 1 
ATOM   760  O  OD2 . ASP A 1 120  ? 47.967 57.282  32.791  1.00 19.44 ? 120  ASP A OD2 1 
ATOM   761  N  N   . ASN A 1 121  ? 45.552 52.545  30.841  1.00 17.49 ? 121  ASN A N   1 
ATOM   762  C  CA  . ASN A 1 121  ? 44.430 51.609  30.917  1.00 17.15 ? 121  ASN A CA  1 
ATOM   763  C  C   . ASN A 1 121  ? 44.646 50.562  29.828  1.00 17.96 ? 121  ASN A C   1 
ATOM   764  O  O   . ASN A 1 121  ? 44.136 50.674  28.715  1.00 17.54 ? 121  ASN A O   1 
ATOM   765  C  CB  . ASN A 1 121  ? 43.134 52.385  30.719  1.00 16.06 ? 121  ASN A CB  1 
ATOM   766  C  CG  . ASN A 1 121  ? 42.921 53.431  31.814  1.00 17.40 ? 121  ASN A CG  1 
ATOM   767  O  OD1 . ASN A 1 121  ? 42.430 53.102  32.899  1.00 16.55 ? 121  ASN A OD1 1 
ATOM   768  N  ND2 . ASN A 1 121  ? 43.318 54.692  31.547  1.00 13.26 ? 121  ASN A ND2 1 
ATOM   769  N  N   . PRO A 1 122  ? 45.394 49.505  30.157  1.00 18.20 ? 122  PRO A N   1 
ATOM   770  C  CA  . PRO A 1 122  ? 45.714 48.422  29.223  1.00 17.38 ? 122  PRO A CA  1 
ATOM   771  C  C   . PRO A 1 122  ? 44.592 47.847  28.377  1.00 16.81 ? 122  PRO A C   1 
ATOM   772  O  O   . PRO A 1 122  ? 44.835 47.454  27.234  1.00 16.36 ? 122  PRO A O   1 
ATOM   773  C  CB  . PRO A 1 122  ? 46.339 47.357  30.124  1.00 17.99 ? 122  PRO A CB  1 
ATOM   774  C  CG  . PRO A 1 122  ? 46.919 48.171  31.243  1.00 19.37 ? 122  PRO A CG  1 
ATOM   775  C  CD  . PRO A 1 122  ? 45.837 49.166  31.519  1.00 18.53 ? 122  PRO A CD  1 
ATOM   776  N  N   . GLU A 1 123  ? 43.377 47.799  28.915  1.00 16.14 ? 123  GLU A N   1 
ATOM   777  C  CA  . GLU A 1 123  ? 42.262 47.221  28.160  1.00 16.56 ? 123  GLU A CA  1 
ATOM   778  C  C   . GLU A 1 123  ? 41.521 48.174  27.230  1.00 15.42 ? 123  GLU A C   1 
ATOM   779  O  O   . GLU A 1 123  ? 40.706 47.723  26.420  1.00 14.11 ? 123  GLU A O   1 
ATOM   780  C  CB  . GLU A 1 123  ? 41.231 46.585  29.101  1.00 18.77 ? 123  GLU A CB  1 
ATOM   781  C  CG  . GLU A 1 123  ? 41.803 45.562  30.103  1.00 26.52 ? 123  GLU A CG  1 
ATOM   782  C  CD  . GLU A 1 123  ? 42.553 44.414  29.440  1.00 30.28 ? 123  GLU A CD  1 
ATOM   783  O  OE1 . GLU A 1 123  ? 41.953 43.670  28.604  1.00 33.16 ? 123  GLU A OE1 1 
ATOM   784  O  OE2 . GLU A 1 123  ? 43.766 44.255  29.764  1.00 34.73 ? 123  GLU A OE2 1 
ATOM   785  N  N   . MET A 1 124  ? 41.746 49.474  27.383  1.00 14.51 ? 124  MET A N   1 
ATOM   786  C  CA  . MET A 1 124  ? 41.113 50.467  26.537  1.00 14.40 ? 124  MET A CA  1 
ATOM   787  C  C   . MET A 1 124  ? 41.732 50.359  25.119  1.00 14.63 ? 124  MET A C   1 
ATOM   788  O  O   . MET A 1 124  ? 42.902 50.010  24.987  1.00 15.09 ? 124  MET A O   1 
ATOM   789  C  CB  . MET A 1 124  ? 41.346 51.867  27.118  1.00 15.56 ? 124  MET A CB  1 
ATOM   790  C  CG  . MET A 1 124  ? 40.569 52.971  26.410  1.00 15.62 ? 124  MET A CG  1 
ATOM   791  S  SD  . MET A 1 124  ? 38.818 52.609  26.346  1.00 16.73 ? 124  MET A SD  1 
ATOM   792  C  CE  . MET A 1 124  ? 38.155 54.120  25.450  1.00 15.27 ? 124  MET A CE  1 
ATOM   793  N  N   . LYS A 1 125  ? 40.930 50.632  24.087  1.00 13.69 ? 125  LYS A N   1 
ATOM   794  C  CA  . LYS A 1 125  ? 41.332 50.567  22.668  1.00 12.74 ? 125  LYS A CA  1 
ATOM   795  C  C   . LYS A 1 125  ? 40.928 51.866  21.937  1.00 12.44 ? 125  LYS A C   1 
ATOM   796  O  O   . LYS A 1 125  ? 40.086 52.625  22.426  1.00 11.03 ? 125  LYS A O   1 
ATOM   797  C  CB  . LYS A 1 125  ? 40.621 49.394  21.998  1.00 15.24 ? 125  LYS A CB  1 
ATOM   798  C  CG  . LYS A 1 125  ? 40.855 48.051  22.691  1.00 17.90 ? 125  LYS A CG  1 
ATOM   799  C  CD  . LYS A 1 125  ? 42.149 47.427  22.216  1.00 20.73 ? 125  LYS A CD  1 
ATOM   800  C  CE  . LYS A 1 125  ? 42.501 46.120  22.941  1.00 22.77 ? 125  LYS A CE  1 
ATOM   801  N  NZ  . LYS A 1 125  ? 41.553 45.016  22.679  1.00 24.79 ? 125  LYS A NZ  1 
ATOM   802  N  N   . PHE A 1 126  ? 41.499 52.099  20.752  1.00 10.01 ? 126  PHE A N   1 
ATOM   803  C  CA  . PHE A 1 126  ? 41.196 53.307  19.996  1.00 9.40  ? 126  PHE A CA  1 
ATOM   804  C  C   . PHE A 1 126  ? 41.684 53.070  18.568  1.00 9.26  ? 126  PHE A C   1 
ATOM   805  O  O   . PHE A 1 126  ? 42.724 52.445  18.376  1.00 9.14  ? 126  PHE A O   1 
ATOM   806  C  CB  . PHE A 1 126  ? 41.969 54.488  20.623  1.00 8.34  ? 126  PHE A CB  1 
ATOM   807  C  CG  . PHE A 1 126  ? 41.587 55.860  20.098  1.00 9.29  ? 126  PHE A CG  1 
ATOM   808  C  CD1 . PHE A 1 126  ? 40.249 56.286  20.096  1.00 8.18  ? 126  PHE A CD1 1 
ATOM   809  C  CD2 . PHE A 1 126  ? 42.586 56.769  19.729  1.00 9.47  ? 126  PHE A CD2 1 
ATOM   810  C  CE1 . PHE A 1 126  ? 39.916 57.612  19.749  1.00 9.59  ? 126  PHE A CE1 1 
ATOM   811  C  CE2 . PHE A 1 126  ? 42.266 58.098  19.374  1.00 10.54 ? 126  PHE A CE2 1 
ATOM   812  C  CZ  . PHE A 1 126  ? 40.926 58.520  19.389  1.00 8.47  ? 126  PHE A CZ  1 
ATOM   813  N  N   . ILE A 1 127  ? 40.934 53.536  17.567  1.00 9.75  ? 127  ILE A N   1 
ATOM   814  C  CA  . ILE A 1 127  ? 41.391 53.385  16.179  1.00 9.48  ? 127  ILE A CA  1 
ATOM   815  C  C   . ILE A 1 127  ? 41.663 54.778  15.602  1.00 9.70  ? 127  ILE A C   1 
ATOM   816  O  O   . ILE A 1 127  ? 41.011 55.765  16.009  1.00 7.93  ? 127  ILE A O   1 
ATOM   817  C  CB  . ILE A 1 127  ? 40.354 52.632  15.305  1.00 10.66 ? 127  ILE A CB  1 
ATOM   818  C  CG1 . ILE A 1 127  ? 39.012 53.370  15.300  1.00 10.78 ? 127  ILE A CG1 1 
ATOM   819  C  CG2 . ILE A 1 127  ? 40.165 51.215  15.859  1.00 11.70 ? 127  ILE A CG2 1 
ATOM   820  C  CD1 . ILE A 1 127  ? 37.999 52.716  14.350  1.00 9.04  ? 127  ILE A CD1 1 
ATOM   821  N  N   . TRP A 1 128  ? 42.629 54.866  14.681  1.00 8.62  ? 128  TRP A N   1 
ATOM   822  C  CA  . TRP A 1 128  ? 42.991 56.156  14.091  1.00 9.59  ? 128  TRP A CA  1 
ATOM   823  C  C   . TRP A 1 128  ? 43.116 56.016  12.570  1.00 9.18  ? 128  TRP A C   1 
ATOM   824  O  O   . TRP A 1 128  ? 43.778 55.105  12.082  1.00 6.50  ? 128  TRP A O   1 
ATOM   825  C  CB  . TRP A 1 128  ? 44.318 56.674  14.664  1.00 8.81  ? 128  TRP A CB  1 
ATOM   826  C  CG  . TRP A 1 128  ? 44.556 58.149  14.303  1.00 10.01 ? 128  TRP A CG  1 
ATOM   827  C  CD1 . TRP A 1 128  ? 45.309 58.658  13.267  1.00 10.56 ? 128  TRP A CD1 1 
ATOM   828  C  CD2 . TRP A 1 128  ? 43.937 59.267  14.936  1.00 9.56  ? 128  TRP A CD2 1 
ATOM   829  N  NE1 . TRP A 1 128  ? 45.186 60.040  13.224  1.00 9.27  ? 128  TRP A NE1 1 
ATOM   830  C  CE2 . TRP A 1 128  ? 44.349 60.434  14.237  1.00 10.03 ? 128  TRP A CE2 1 
ATOM   831  C  CE3 . TRP A 1 128  ? 43.064 59.398  16.045  1.00 9.40  ? 128  TRP A CE3 1 
ATOM   832  C  CZ2 . TRP A 1 128  ? 43.917 61.722  14.608  1.00 9.48  ? 128  TRP A CZ2 1 
ATOM   833  C  CZ3 . TRP A 1 128  ? 42.638 60.674  16.410  1.00 9.35  ? 128  TRP A CZ3 1 
ATOM   834  C  CH2 . TRP A 1 128  ? 43.067 61.822  15.687  1.00 9.79  ? 128  TRP A CH2 1 
ATOM   835  N  N   . ALA A 1 129  ? 42.499 56.940  11.839  1.00 8.83  ? 129  ALA A N   1 
ATOM   836  C  CA  . ALA A 1 129  ? 42.504 56.887  10.368  1.00 8.95  ? 129  ALA A CA  1 
ATOM   837  C  C   . ALA A 1 129  ? 43.436 57.839  9.609   1.00 10.07 ? 129  ALA A C   1 
ATOM   838  O  O   . ALA A 1 129  ? 44.058 57.447  8.639   1.00 10.13 ? 129  ALA A O   1 
ATOM   839  C  CB  . ALA A 1 129  ? 41.050 57.092  9.835   1.00 8.00  ? 129  ALA A CB  1 
ATOM   840  N  N   . GLU A 1 130  ? 43.531 59.090  10.055  1.00 11.58 ? 130  GLU A N   1 
ATOM   841  C  CA  . GLU A 1 130  ? 44.293 60.112  9.335   1.00 11.79 ? 130  GLU A CA  1 
ATOM   842  C  C   . GLU A 1 130  ? 45.771 60.279  9.669   1.00 12.31 ? 130  GLU A C   1 
ATOM   843  O  O   . GLU A 1 130  ? 46.131 60.970  10.648  1.00 10.18 ? 130  GLU A O   1 
ATOM   844  C  CB  . GLU A 1 130  ? 43.589 61.463  9.505   1.00 12.89 ? 130  GLU A CB  1 
ATOM   845  C  CG  . GLU A 1 130  ? 42.095 61.480  9.142   1.00 13.48 ? 130  GLU A CG  1 
ATOM   846  C  CD  . GLU A 1 130  ? 41.208 60.903  10.232  1.00 15.70 ? 130  GLU A CD  1 
ATOM   847  O  OE1 . GLU A 1 130  ? 41.667 60.829  11.404  1.00 17.68 ? 130  GLU A OE1 1 
ATOM   848  O  OE2 . GLU A 1 130  ? 40.044 60.525  9.937   1.00 15.21 ? 130  GLU A OE2 1 
ATOM   849  N  N   . ILE A 1 131  ? 46.619 59.704  8.817   1.00 10.60 ? 131  ILE A N   1 
ATOM   850  C  CA  . ILE A 1 131  ? 48.038 59.781  9.059   1.00 10.66 ? 131  ILE A CA  1 
ATOM   851  C  C   . ILE A 1 131  ? 48.609 61.189  8.927   1.00 10.35 ? 131  ILE A C   1 
ATOM   852  O  O   . ILE A 1 131  ? 49.621 61.500  9.573   1.00 12.19 ? 131  ILE A O   1 
ATOM   853  C  CB  . ILE A 1 131  ? 48.782 58.763  8.180   1.00 10.35 ? 131  ILE A CB  1 
ATOM   854  C  CG1 . ILE A 1 131  ? 48.184 57.360  8.433   1.00 10.90 ? 131  ILE A CG1 1 
ATOM   855  C  CG2 . ILE A 1 131  ? 50.274 58.766  8.494   1.00 11.48 ? 131  ILE A CG2 1 
ATOM   856  C  CD1 . ILE A 1 131  ? 47.971 56.976  9.941   1.00 9.91  ? 131  ILE A CD1 1 
ATOM   857  N  N   . SER A 1 132  ? 47.958 62.073  8.170   1.00 8.02  ? 132  SER A N   1 
ATOM   858  C  CA  . SER A 1 132  ? 48.486 63.448  8.058   1.00 7.20  ? 132  SER A CA  1 
ATOM   859  C  C   . SER A 1 132  ? 48.613 64.061  9.458   1.00 8.29  ? 132  SER A C   1 
ATOM   860  O  O   . SER A 1 132  ? 49.631 64.682  9.802   1.00 8.22  ? 132  SER A O   1 
ATOM   861  C  CB  . SER A 1 132  ? 47.591 64.335  7.163   1.00 5.98  ? 132  SER A CB  1 
ATOM   862  O  OG  . SER A 1 132  ? 46.226 64.328  7.549   1.00 5.91  ? 132  SER A OG  1 
ATOM   863  N  N   . TYR A 1 133  ? 47.583 63.865  10.271  1.00 9.58  ? 133  TYR A N   1 
ATOM   864  C  CA  . TYR A 1 133  ? 47.561 64.375  11.648  1.00 9.64  ? 133  TYR A CA  1 
ATOM   865  C  C   . TYR A 1 133  ? 48.502 63.566  12.545  1.00 10.64 ? 133  TYR A C   1 
ATOM   866  O  O   . TYR A 1 133  ? 49.227 64.137  13.379  1.00 11.75 ? 133  TYR A O   1 
ATOM   867  C  CB  . TYR A 1 133  ? 46.153 64.269  12.223  1.00 8.26  ? 133  TYR A CB  1 
ATOM   868  C  CG  . TYR A 1 133  ? 45.257 65.464  11.957  1.00 7.51  ? 133  TYR A CG  1 
ATOM   869  C  CD1 . TYR A 1 133  ? 43.976 65.279  11.453  1.00 7.01  ? 133  TYR A CD1 1 
ATOM   870  C  CD2 . TYR A 1 133  ? 45.696 66.761  12.210  1.00 7.11  ? 133  TYR A CD2 1 
ATOM   871  C  CE1 . TYR A 1 133  ? 43.149 66.343  11.195  1.00 7.83  ? 133  TYR A CE1 1 
ATOM   872  C  CE2 . TYR A 1 133  ? 44.865 67.869  11.966  1.00 10.39 ? 133  TYR A CE2 1 
ATOM   873  C  CZ  . TYR A 1 133  ? 43.592 67.637  11.459  1.00 9.63  ? 133  TYR A CZ  1 
ATOM   874  O  OH  . TYR A 1 133  ? 42.743 68.685  11.277  1.00 11.35 ? 133  TYR A OH  1 
ATOM   875  N  N   . PHE A 1 134  ? 48.487 62.244  12.391  1.00 10.37 ? 134  PHE A N   1 
ATOM   876  C  CA  . PHE A 1 134  ? 49.344 61.430  13.256  1.00 10.52 ? 134  PHE A CA  1 
ATOM   877  C  C   . PHE A 1 134  ? 50.828 61.710  13.049  1.00 11.02 ? 134  PHE A C   1 
ATOM   878  O  O   . PHE A 1 134  ? 51.598 61.792  14.028  1.00 10.68 ? 134  PHE A O   1 
ATOM   879  C  CB  . PHE A 1 134  ? 49.083 59.945  13.067  1.00 10.07 ? 134  PHE A CB  1 
ATOM   880  C  CG  . PHE A 1 134  ? 49.626 59.112  14.184  1.00 12.17 ? 134  PHE A CG  1 
ATOM   881  C  CD1 . PHE A 1 134  ? 48.888 58.927  15.356  1.00 12.02 ? 134  PHE A CD1 1 
ATOM   882  C  CD2 . PHE A 1 134  ? 50.888 58.574  14.109  1.00 9.58  ? 134  PHE A CD2 1 
ATOM   883  C  CE1 . PHE A 1 134  ? 49.423 58.211  16.439  1.00 13.99 ? 134  PHE A CE1 1 
ATOM   884  C  CE2 . PHE A 1 134  ? 51.425 57.864  15.176  1.00 12.04 ? 134  PHE A CE2 1 
ATOM   885  C  CZ  . PHE A 1 134  ? 50.680 57.685  16.353  1.00 11.74 ? 134  PHE A CZ  1 
ATOM   886  N  N   . ALA A 1 135  ? 51.232 61.838  11.785  1.00 10.32 ? 135  ALA A N   1 
ATOM   887  C  CA  . ALA A 1 135  ? 52.624 62.114  11.462  1.00 12.70 ? 135  ALA A CA  1 
ATOM   888  C  C   . ALA A 1 135  ? 53.041 63.480  12.060  1.00 14.81 ? 135  ALA A C   1 
ATOM   889  O  O   . ALA A 1 135  ? 54.152 63.622  12.594  1.00 16.08 ? 135  ALA A O   1 
ATOM   890  C  CB  . ALA A 1 135  ? 52.805 62.118  9.957   1.00 11.46 ? 135  ALA A CB  1 
ATOM   891  N  N   . ARG A 1 136  ? 52.154 64.472  11.963  1.00 14.51 ? 136  ARG A N   1 
ATOM   892  C  CA  . ARG A 1 136  ? 52.403 65.806  12.488  1.00 15.53 ? 136  ARG A CA  1 
ATOM   893  C  C   . ARG A 1 136  ? 52.631 65.724  14.013  1.00 16.57 ? 136  ARG A C   1 
ATOM   894  O  O   . ARG A 1 136  ? 53.568 66.313  14.558  1.00 16.28 ? 136  ARG A O   1 
ATOM   895  C  CB  . ARG A 1 136  ? 51.203 66.697  12.189  1.00 16.08 ? 136  ARG A CB  1 
ATOM   896  C  CG  . ARG A 1 136  ? 51.209 68.083  12.874  1.00 17.84 ? 136  ARG A CG  1 
ATOM   897  C  CD  . ARG A 1 136  ? 51.935 69.169  12.026  1.00 20.31 ? 136  ARG A CD  1 
ATOM   898  N  NE  . ARG A 1 136  ? 51.870 70.503  12.648  1.00 17.41 ? 136  ARG A NE  1 
ATOM   899  C  CZ  . ARG A 1 136  ? 52.607 70.816  13.709  1.00 19.91 ? 136  ARG A CZ  1 
ATOM   900  N  NH1 . ARG A 1 136  ? 53.444 69.892  14.194  1.00 16.16 ? 136  ARG A NH1 1 
ATOM   901  N  NH2 . ARG A 1 136  ? 52.472 72.001  14.317  1.00 17.19 ? 136  ARG A NH2 1 
ATOM   902  N  N   . PHE A 1 137  ? 51.770 64.966  14.683  1.00 15.26 ? 137  PHE A N   1 
ATOM   903  C  CA  . PHE A 1 137  ? 51.841 64.769  16.121  1.00 14.44 ? 137  PHE A CA  1 
ATOM   904  C  C   . PHE A 1 137  ? 53.106 64.023  16.556  1.00 15.33 ? 137  PHE A C   1 
ATOM   905  O  O   . PHE A 1 137  ? 53.875 64.494  17.393  1.00 14.56 ? 137  PHE A O   1 
ATOM   906  C  CB  . PHE A 1 137  ? 50.632 63.974  16.579  1.00 12.75 ? 137  PHE A CB  1 
ATOM   907  C  CG  . PHE A 1 137  ? 50.598 63.742  18.053  1.00 12.45 ? 137  PHE A CG  1 
ATOM   908  C  CD1 . PHE A 1 137  ? 50.274 64.787  18.926  1.00 11.08 ? 137  PHE A CD1 1 
ATOM   909  C  CD2 . PHE A 1 137  ? 50.894 62.484  18.574  1.00 12.05 ? 137  PHE A CD2 1 
ATOM   910  C  CE1 . PHE A 1 137  ? 50.240 64.583  20.283  1.00 10.81 ? 137  PHE A CE1 1 
ATOM   911  C  CE2 . PHE A 1 137  ? 50.861 62.260  19.952  1.00 12.73 ? 137  PHE A CE2 1 
ATOM   912  C  CZ  . PHE A 1 137  ? 50.526 63.323  20.814  1.00 11.33 ? 137  PHE A CZ  1 
ATOM   913  N  N   . TYR A 1 138  ? 53.309 62.849  15.976  1.00 15.04 ? 138  TYR A N   1 
ATOM   914  C  CA  . TYR A 1 138  ? 54.456 62.008  16.303  1.00 15.79 ? 138  TYR A CA  1 
ATOM   915  C  C   . TYR A 1 138  ? 55.803 62.722  16.172  1.00 16.71 ? 138  TYR A C   1 
ATOM   916  O  O   . TYR A 1 138  ? 56.674 62.570  17.029  1.00 14.94 ? 138  TYR A O   1 
ATOM   917  C  CB  . TYR A 1 138  ? 54.476 60.761  15.409  1.00 14.30 ? 138  TYR A CB  1 
ATOM   918  C  CG  . TYR A 1 138  ? 55.525 59.723  15.811  1.00 16.99 ? 138  TYR A CG  1 
ATOM   919  C  CD1 . TYR A 1 138  ? 55.251 58.782  16.804  1.00 15.74 ? 138  TYR A CD1 1 
ATOM   920  C  CD2 . TYR A 1 138  ? 56.787 59.678  15.182  1.00 16.06 ? 138  TYR A CD2 1 
ATOM   921  C  CE1 . TYR A 1 138  ? 56.201 57.819  17.162  1.00 17.50 ? 138  TYR A CE1 1 
ATOM   922  C  CE2 . TYR A 1 138  ? 57.749 58.702  15.535  1.00 16.90 ? 138  TYR A CE2 1 
ATOM   923  C  CZ  . TYR A 1 138  ? 57.445 57.786  16.520  1.00 17.14 ? 138  TYR A CZ  1 
ATOM   924  O  OH  . TYR A 1 138  ? 58.365 56.828  16.898  1.00 19.78 ? 138  TYR A OH  1 
ATOM   925  N  N   . HIS A 1 139  ? 55.997 63.475  15.098  1.00 17.92 ? 139  HIS A N   1 
ATOM   926  C  CA  . HIS A 1 139  ? 57.278 64.142  14.951  1.00 21.71 ? 139  HIS A CA  1 
ATOM   927  C  C   . HIS A 1 139  ? 57.521 65.202  15.995  1.00 21.04 ? 139  HIS A C   1 
ATOM   928  O  O   . HIS A 1 139  ? 58.665 65.556  16.246  1.00 22.27 ? 139  HIS A O   1 
ATOM   929  C  CB  . HIS A 1 139  ? 57.456 64.697  13.538  1.00 22.91 ? 139  HIS A CB  1 
ATOM   930  C  CG  . HIS A 1 139  ? 57.702 63.623  12.524  1.00 27.91 ? 139  HIS A CG  1 
ATOM   931  N  ND1 . HIS A 1 139  ? 58.795 62.776  12.592  1.00 29.43 ? 139  HIS A ND1 1 
ATOM   932  C  CD2 . HIS A 1 139  ? 56.955 63.192  11.475  1.00 28.62 ? 139  HIS A CD2 1 
ATOM   933  C  CE1 . HIS A 1 139  ? 58.703 61.871  11.631  1.00 31.29 ? 139  HIS A CE1 1 
ATOM   934  N  NE2 . HIS A 1 139  ? 57.598 62.103  10.938  1.00 29.79 ? 139  HIS A NE2 1 
ATOM   935  N  N   . ASP A 1 140  ? 56.453 65.706  16.597  1.00 19.62 ? 140  ASP A N   1 
ATOM   936  C  CA  . ASP A 1 140  ? 56.583 66.702  17.668  1.00 18.44 ? 140  ASP A CA  1 
ATOM   937  C  C   . ASP A 1 140  ? 56.801 66.067  19.060  1.00 16.76 ? 140  ASP A C   1 
ATOM   938  O  O   . ASP A 1 140  ? 57.139 66.760  20.019  1.00 16.00 ? 140  ASP A O   1 
ATOM   939  C  CB  . ASP A 1 140  ? 55.347 67.580  17.721  1.00 18.26 ? 140  ASP A CB  1 
ATOM   940  C  CG  . ASP A 1 140  ? 55.415 68.744  16.722  1.00 20.95 ? 140  ASP A CG  1 
ATOM   941  O  OD1 . ASP A 1 140  ? 56.347 68.742  15.895  1.00 22.68 ? 140  ASP A OD1 1 
ATOM   942  O  OD2 . ASP A 1 140  ? 54.540 69.642  16.773  1.00 20.35 ? 140  ASP A OD2 1 
ATOM   943  N  N   . LEU A 1 141  ? 56.614 64.761  19.172  1.00 15.69 ? 141  LEU A N   1 
ATOM   944  C  CA  . LEU A 1 141  ? 56.772 64.072  20.457  1.00 16.29 ? 141  LEU A CA  1 
ATOM   945  C  C   . LEU A 1 141  ? 58.205 63.904  20.890  1.00 16.29 ? 141  LEU A C   1 
ATOM   946  O  O   . LEU A 1 141  ? 59.085 63.720  20.062  1.00 15.72 ? 141  LEU A O   1 
ATOM   947  C  CB  . LEU A 1 141  ? 56.165 62.661  20.414  1.00 16.82 ? 141  LEU A CB  1 
ATOM   948  C  CG  . LEU A 1 141  ? 54.662 62.429  20.516  1.00 17.39 ? 141  LEU A CG  1 
ATOM   949  C  CD1 . LEU A 1 141  ? 54.402 60.897  20.502  1.00 16.09 ? 141  LEU A CD1 1 
ATOM   950  C  CD2 . LEU A 1 141  ? 54.118 63.098  21.797  1.00 16.26 ? 141  LEU A CD2 1 
ATOM   951  N  N   . GLY A 1 142  ? 58.442 63.956  22.195  1.00 18.05 ? 142  GLY A N   1 
ATOM   952  C  CA  . GLY A 1 142  ? 59.796 63.715  22.676  1.00 19.30 ? 142  GLY A CA  1 
ATOM   953  C  C   . GLY A 1 142  ? 60.054 62.212  22.521  1.00 19.50 ? 142  GLY A C   1 
ATOM   954  O  O   . GLY A 1 142  ? 59.114 61.423  22.399  1.00 19.50 ? 142  GLY A O   1 
ATOM   955  N  N   . GLU A 1 143  ? 61.316 61.816  22.522  1.00 20.15 ? 143  GLU A N   1 
ATOM   956  C  CA  . GLU A 1 143  ? 61.688 60.428  22.353  1.00 20.93 ? 143  GLU A CA  1 
ATOM   957  C  C   . GLU A 1 143  ? 61.027 59.507  23.374  1.00 21.62 ? 143  GLU A C   1 
ATOM   958  O  O   . GLU A 1 143  ? 60.637 58.383  23.057  1.00 20.95 ? 143  GLU A O   1 
ATOM   959  C  CB  . GLU A 1 143  ? 63.205 60.293  22.427  1.00 23.90 ? 143  GLU A CB  1 
ATOM   960  C  CG  . GLU A 1 143  ? 63.755 58.975  21.888  1.00 26.32 ? 143  GLU A CG  1 
ATOM   961  C  CD  . GLU A 1 143  ? 63.460 58.772  20.388  1.00 29.73 ? 143  GLU A CD  1 
ATOM   962  O  OE1 . GLU A 1 143  ? 63.474 59.754  19.595  1.00 30.41 ? 143  GLU A OE1 1 
ATOM   963  O  OE2 . GLU A 1 143  ? 63.222 57.613  20.003  1.00 31.02 ? 143  GLU A OE2 1 
ATOM   964  N  N   . ASN A 1 144  ? 60.859 59.969  24.598  1.00 22.10 ? 144  ASN A N   1 
ATOM   965  C  CA  . ASN A 1 144  ? 60.232 59.098  25.580  1.00 22.80 ? 144  ASN A CA  1 
ATOM   966  C  C   . ASN A 1 144  ? 58.774 58.755  25.175  1.00 21.67 ? 144  ASN A C   1 
ATOM   967  O  O   . ASN A 1 144  ? 58.365 57.601  25.261  1.00 19.56 ? 144  ASN A O   1 
ATOM   968  C  CB  . ASN A 1 144  ? 60.303 59.750  26.976  1.00 25.15 ? 144  ASN A CB  1 
ATOM   969  C  CG  . ASN A 1 144  ? 59.460 59.010  28.020  1.00 29.36 ? 144  ASN A CG  1 
ATOM   970  O  OD1 . ASN A 1 144  ? 58.244 59.257  28.156  1.00 31.59 ? 144  ASN A OD1 1 
ATOM   971  N  ND2 . ASN A 1 144  ? 60.098 58.092  28.759  1.00 28.94 ? 144  ASN A ND2 1 
ATOM   972  N  N   . LYS A 1 145  ? 58.011 59.753  24.719  1.00 21.10 ? 145  LYS A N   1 
ATOM   973  C  CA  . LYS A 1 145  ? 56.620 59.529  24.318  1.00 20.03 ? 145  LYS A CA  1 
ATOM   974  C  C   . LYS A 1 145  ? 56.522 58.758  23.001  1.00 19.23 ? 145  LYS A C   1 
ATOM   975  O  O   . LYS A 1 145  ? 55.564 58.015  22.793  1.00 18.45 ? 145  LYS A O   1 
ATOM   976  C  CB  . LYS A 1 145  ? 55.871 60.861  24.207  1.00 21.93 ? 145  LYS A CB  1 
ATOM   977  C  CG  . LYS A 1 145  ? 55.680 61.608  25.560  1.00 24.50 ? 145  LYS A CG  1 
ATOM   978  C  CD  . LYS A 1 145  ? 54.886 60.773  26.566  1.00 28.04 ? 145  LYS A CD  1 
ATOM   979  C  CE  . LYS A 1 145  ? 54.551 61.538  27.870  1.00 29.65 ? 145  LYS A CE  1 
ATOM   980  N  NZ  . LYS A 1 145  ? 55.755 61.944  28.667  1.00 33.13 ? 145  LYS A NZ  1 
ATOM   981  N  N   . LYS A 1 146  ? 57.491 58.955  22.101  1.00 18.12 ? 146  LYS A N   1 
ATOM   982  C  CA  . LYS A 1 146  ? 57.496 58.214  20.826  1.00 17.13 ? 146  LYS A CA  1 
ATOM   983  C  C   . LYS A 1 146  ? 57.579 56.734  21.146  1.00 16.17 ? 146  LYS A C   1 
ATOM   984  O  O   . LYS A 1 146  ? 56.946 55.920  20.493  1.00 15.86 ? 146  LYS A O   1 
ATOM   985  C  CB  . LYS A 1 146  ? 58.697 58.577  19.940  1.00 16.26 ? 146  LYS A CB  1 
ATOM   986  C  CG  . LYS A 1 146  ? 58.584 59.936  19.266  1.00 18.16 ? 146  LYS A CG  1 
ATOM   987  C  CD  . LYS A 1 146  ? 59.706 60.184  18.253  1.00 20.90 ? 146  LYS A CD  1 
ATOM   988  C  CE  . LYS A 1 146  ? 59.520 61.571  17.639  1.00 21.95 ? 146  LYS A CE  1 
ATOM   989  N  NZ  . LYS A 1 146  ? 60.629 61.833  16.753  1.00 25.66 ? 146  LYS A NZ  1 
ATOM   990  N  N   . LEU A 1 147  ? 58.354 56.385  22.165  1.00 15.79 ? 147  LEU A N   1 
ATOM   991  C  CA  . LEU A 1 147  ? 58.504 54.975  22.535  1.00 15.25 ? 147  LEU A CA  1 
ATOM   992  C  C   . LEU A 1 147  ? 57.209 54.477  23.182  1.00 15.14 ? 147  LEU A C   1 
ATOM   993  O  O   . LEU A 1 147  ? 56.789 53.345  22.949  1.00 13.16 ? 147  LEU A O   1 
ATOM   994  C  CB  . LEU A 1 147  ? 59.687 54.784  23.494  1.00 17.93 ? 147  LEU A CB  1 
ATOM   995  C  CG  . LEU A 1 147  ? 61.042 55.106  22.860  1.00 18.65 ? 147  LEU A CG  1 
ATOM   996  C  CD1 . LEU A 1 147  ? 62.151 54.983  23.884  1.00 21.46 ? 147  LEU A CD1 1 
ATOM   997  C  CD2 . LEU A 1 147  ? 61.308 54.149  21.724  1.00 21.19 ? 147  LEU A CD2 1 
ATOM   998  N  N   . GLN A 1 148  ? 56.579 55.310  24.005  1.00 13.79 ? 148  GLN A N   1 
ATOM   999  C  CA  . GLN A 1 148  ? 55.327 54.886  24.603  1.00 15.22 ? 148  GLN A CA  1 
ATOM   1000 C  C   . GLN A 1 148  ? 54.291 54.668  23.502  1.00 14.04 ? 148  GLN A C   1 
ATOM   1001 O  O   . GLN A 1 148  ? 53.519 53.714  23.563  1.00 12.90 ? 148  GLN A O   1 
ATOM   1002 C  CB  . GLN A 1 148  ? 54.778 55.930  25.560  1.00 18.09 ? 148  GLN A CB  1 
ATOM   1003 C  CG  . GLN A 1 148  ? 55.504 56.038  26.847  1.00 22.99 ? 148  GLN A CG  1 
ATOM   1004 C  CD  . GLN A 1 148  ? 54.760 56.913  27.842  1.00 26.86 ? 148  GLN A CD  1 
ATOM   1005 O  OE1 . GLN A 1 148  ? 53.707 57.498  27.526  1.00 28.68 ? 148  GLN A OE1 1 
ATOM   1006 N  NE2 . GLN A 1 148  ? 55.302 57.007  29.054  1.00 28.35 ? 148  GLN A NE2 1 
ATOM   1007 N  N   . MET A 1 149  ? 54.276 55.557  22.511  1.00 11.79 ? 149  MET A N   1 
ATOM   1008 C  CA  . MET A 1 149  ? 53.317 55.445  21.408  1.00 12.65 ? 149  MET A CA  1 
ATOM   1009 C  C   . MET A 1 149  ? 53.573 54.183  20.603  1.00 13.18 ? 149  MET A C   1 
ATOM   1010 O  O   . MET A 1 149  ? 52.646 53.443  20.290  1.00 13.32 ? 149  MET A O   1 
ATOM   1011 C  CB  . MET A 1 149  ? 53.395 56.668  20.481  1.00 12.74 ? 149  MET A CB  1 
ATOM   1012 C  CG  . MET A 1 149  ? 52.409 56.655  19.315  1.00 14.14 ? 149  MET A CG  1 
ATOM   1013 S  SD  . MET A 1 149  ? 50.700 56.799  19.886  1.00 16.70 ? 149  MET A SD  1 
ATOM   1014 C  CE  . MET A 1 149  ? 50.573 58.498  20.039  1.00 15.09 ? 149  MET A CE  1 
ATOM   1015 N  N   . LYS A 1 150  ? 54.823 53.935  20.254  1.00 13.20 ? 150  LYS A N   1 
ATOM   1016 C  CA  . LYS A 1 150  ? 55.120 52.729  19.500  1.00 15.49 ? 150  LYS A CA  1 
ATOM   1017 C  C   . LYS A 1 150  ? 54.677 51.495  20.276  1.00 14.78 ? 150  LYS A C   1 
ATOM   1018 O  O   . LYS A 1 150  ? 54.224 50.526  19.673  1.00 14.04 ? 150  LYS A O   1 
ATOM   1019 C  CB  . LYS A 1 150  ? 56.620 52.581  19.184  1.00 17.66 ? 150  LYS A CB  1 
ATOM   1020 C  CG  . LYS A 1 150  ? 57.151 53.465  18.099  1.00 21.92 ? 150  LYS A CG  1 
ATOM   1021 C  CD  . LYS A 1 150  ? 58.592 53.078  17.812  1.00 26.55 ? 150  LYS A CD  1 
ATOM   1022 C  CE  . LYS A 1 150  ? 59.253 54.081  16.913  1.00 30.60 ? 150  LYS A CE  1 
ATOM   1023 N  NZ  . LYS A 1 150  ? 60.472 53.495  16.288  1.00 33.25 ? 150  LYS A NZ  1 
ATOM   1024 N  N   . SER A 1 151  ? 54.799 51.508  21.599  1.00 14.61 ? 151  SER A N   1 
ATOM   1025 C  CA  . SER A 1 151  ? 54.403 50.305  22.320  1.00 16.02 ? 151  SER A CA  1 
ATOM   1026 C  C   . SER A 1 151  ? 52.883 50.096  22.407  1.00 15.32 ? 151  SER A C   1 
ATOM   1027 O  O   . SER A 1 151  ? 52.432 48.953  22.374  1.00 13.19 ? 151  SER A O   1 
ATOM   1028 C  CB  . SER A 1 151  ? 55.041 50.253  23.718  1.00 17.13 ? 151  SER A CB  1 
ATOM   1029 O  OG  . SER A 1 151  ? 54.288 51.011  24.620  1.00 25.86 ? 151  SER A OG  1 
ATOM   1030 N  N   . ILE A 1 152  ? 52.080 51.161  22.508  1.00 14.26 ? 152  ILE A N   1 
ATOM   1031 C  CA  . ILE A 1 152  ? 50.650 50.906  22.541  1.00 15.37 ? 152  ILE A CA  1 
ATOM   1032 C  C   . ILE A 1 152  ? 50.140 50.562  21.138  1.00 15.76 ? 152  ILE A C   1 
ATOM   1033 O  O   . ILE A 1 152  ? 49.037 50.078  20.991  1.00 18.00 ? 152  ILE A O   1 
ATOM   1034 C  CB  . ILE A 1 152  ? 49.809 52.068  23.132  1.00 14.53 ? 152  ILE A CB  1 
ATOM   1035 C  CG1 . ILE A 1 152  ? 49.979 53.337  22.319  1.00 14.51 ? 152  ILE A CG1 1 
ATOM   1036 C  CG2 . ILE A 1 152  ? 50.184 52.303  24.599  1.00 16.71 ? 152  ILE A CG2 1 
ATOM   1037 C  CD1 . ILE A 1 152  ? 48.973 54.406  22.739  1.00 13.23 ? 152  ILE A CD1 1 
ATOM   1038 N  N   . VAL A 1 153  ? 50.931 50.820  20.101  1.00 17.00 ? 153  VAL A N   1 
ATOM   1039 C  CA  . VAL A 1 153  ? 50.524 50.428  18.742  1.00 16.30 ? 153  VAL A CA  1 
ATOM   1040 C  C   . VAL A 1 153  ? 50.917 48.940  18.576  1.00 17.13 ? 153  VAL A C   1 
ATOM   1041 O  O   . VAL A 1 153  ? 50.102 48.099  18.171  1.00 16.33 ? 153  VAL A O   1 
ATOM   1042 C  CB  . VAL A 1 153  ? 51.232 51.282  17.679  1.00 16.57 ? 153  VAL A CB  1 
ATOM   1043 C  CG1 . VAL A 1 153  ? 51.082 50.630  16.283  1.00 15.11 ? 153  VAL A CG1 1 
ATOM   1044 C  CG2 . VAL A 1 153  ? 50.631 52.712  17.697  1.00 15.37 ? 153  VAL A CG2 1 
ATOM   1045 N  N   . LYS A 1 154  ? 52.158 48.624  18.946  1.00 18.22 ? 154  LYS A N   1 
ATOM   1046 C  CA  . LYS A 1 154  ? 52.682 47.267  18.849  1.00 20.37 ? 154  LYS A CA  1 
ATOM   1047 C  C   . LYS A 1 154  ? 51.835 46.264  19.638  1.00 20.11 ? 154  LYS A C   1 
ATOM   1048 O  O   . LYS A 1 154  ? 51.616 45.153  19.175  1.00 21.45 ? 154  LYS A O   1 
ATOM   1049 C  CB  . LYS A 1 154  ? 54.119 47.208  19.363  1.00 22.05 ? 154  LYS A CB  1 
ATOM   1050 C  CG  . LYS A 1 154  ? 54.700 45.818  19.264  1.00 26.59 ? 154  LYS A CG  1 
ATOM   1051 C  CD  . LYS A 1 154  ? 56.003 45.718  20.017  1.00 29.46 ? 154  LYS A CD  1 
ATOM   1052 C  CE  . LYS A 1 154  ? 57.165 46.025  19.107  1.00 31.88 ? 154  LYS A CE  1 
ATOM   1053 N  NZ  . LYS A 1 154  ? 57.126 45.105  17.936  1.00 33.98 ? 154  LYS A NZ  1 
ATOM   1054 N  N   . ASN A 1 155  ? 51.370 46.656  20.818  1.00 19.80 ? 155  ASN A N   1 
ATOM   1055 C  CA  . ASN A 1 155  ? 50.533 45.798  21.656  1.00 21.04 ? 155  ASN A CA  1 
ATOM   1056 C  C   . ASN A 1 155  ? 49.027 45.750  21.273  1.00 20.46 ? 155  ASN A C   1 
ATOM   1057 O  O   . ASN A 1 155  ? 48.243 45.096  21.947  1.00 20.58 ? 155  ASN A O   1 
ATOM   1058 C  CB  . ASN A 1 155  ? 50.681 46.200  23.147  1.00 23.56 ? 155  ASN A CB  1 
ATOM   1059 C  CG  . ASN A 1 155  ? 49.793 47.409  23.554  1.00 25.84 ? 155  ASN A CG  1 
ATOM   1060 O  OD1 . ASN A 1 155  ? 49.053 47.955  22.730  1.00 27.69 ? 155  ASN A OD1 1 
ATOM   1061 N  ND2 . ASN A 1 155  ? 49.870 47.818  24.833  1.00 23.52 ? 155  ASN A ND2 1 
ATOM   1062 N  N   . GLY A 1 156  ? 48.609 46.456  20.221  1.00 19.64 ? 156  GLY A N   1 
ATOM   1063 C  CA  . GLY A 1 156  ? 47.208 46.376  19.796  1.00 17.38 ? 156  GLY A CA  1 
ATOM   1064 C  C   . GLY A 1 156  ? 46.169 47.316  20.392  1.00 16.25 ? 156  GLY A C   1 
ATOM   1065 O  O   . GLY A 1 156  ? 44.991 47.245  20.019  1.00 14.59 ? 156  GLY A O   1 
ATOM   1066 N  N   . GLN A 1 157  ? 46.572 48.200  21.306  1.00 14.08 ? 157  GLN A N   1 
ATOM   1067 C  CA  . GLN A 1 157  ? 45.627 49.131  21.902  1.00 13.43 ? 157  GLN A CA  1 
ATOM   1068 C  C   . GLN A 1 157  ? 45.245 50.274  20.944  1.00 13.75 ? 157  GLN A C   1 
ATOM   1069 O  O   . GLN A 1 157  ? 44.091 50.644  20.831  1.00 14.86 ? 157  GLN A O   1 
ATOM   1070 C  CB  . GLN A 1 157  ? 46.213 49.736  23.179  1.00 14.31 ? 157  GLN A CB  1 
ATOM   1071 C  CG  . GLN A 1 157  ? 45.984 48.913  24.444  1.00 12.19 ? 157  GLN A CG  1 
ATOM   1072 C  CD  . GLN A 1 157  ? 46.439 49.689  25.651  1.00 12.66 ? 157  GLN A CD  1 
ATOM   1073 O  OE1 . GLN A 1 157  ? 47.613 49.672  25.997  1.00 12.96 ? 157  GLN A OE1 1 
ATOM   1074 N  NE2 . GLN A 1 157  ? 45.528 50.413  26.268  1.00 11.61 ? 157  GLN A NE2 1 
ATOM   1075 N  N   . LEU A 1 158  ? 46.221 50.836  20.252  1.00 13.49 ? 158  LEU A N   1 
ATOM   1076 C  CA  . LEU A 1 158  ? 45.930 51.927  19.313  1.00 12.79 ? 158  LEU A CA  1 
ATOM   1077 C  C   . LEU A 1 158  ? 46.146 51.284  17.942  1.00 12.33 ? 158  LEU A C   1 
ATOM   1078 O  O   . LEU A 1 158  ? 47.235 50.757  17.660  1.00 8.76  ? 158  LEU A O   1 
ATOM   1079 C  CB  . LEU A 1 158  ? 46.911 53.080  19.539  1.00 14.96 ? 158  LEU A CB  1 
ATOM   1080 C  CG  . LEU A 1 158  ? 46.759 54.459  18.881  1.00 18.91 ? 158  LEU A CG  1 
ATOM   1081 C  CD1 . LEU A 1 158  ? 48.178 55.009  18.596  1.00 19.70 ? 158  LEU A CD1 1 
ATOM   1082 C  CD2 . LEU A 1 158  ? 45.971 54.394  17.623  1.00 20.28 ? 158  LEU A CD2 1 
ATOM   1083 N  N   . GLU A 1 159  ? 45.104 51.308  17.108  1.00 9.59  ? 159  GLU A N   1 
ATOM   1084 C  CA  . GLU A 1 159  ? 45.194 50.671  15.801  1.00 10.24 ? 159  GLU A CA  1 
ATOM   1085 C  C   . GLU A 1 159  ? 44.843 51.584  14.654  1.00 10.46 ? 159  GLU A C   1 
ATOM   1086 O  O   . GLU A 1 159  ? 43.834 52.302  14.684  1.00 10.29 ? 159  GLU A O   1 
ATOM   1087 C  CB  . GLU A 1 159  ? 44.282 49.412  15.767  1.00 11.51 ? 159  GLU A CB  1 
ATOM   1088 C  CG  . GLU A 1 159  ? 44.165 48.702  14.425  1.00 11.91 ? 159  GLU A CG  1 
ATOM   1089 C  CD  . GLU A 1 159  ? 43.188 47.531  14.480  1.00 14.77 ? 159  GLU A CD  1 
ATOM   1090 O  OE1 . GLU A 1 159  ? 43.527 46.535  15.167  1.00 13.13 ? 159  GLU A OE1 1 
ATOM   1091 O  OE2 . GLU A 1 159  ? 42.091 47.620  13.855  1.00 13.42 ? 159  GLU A OE2 1 
ATOM   1092 N  N   . PHE A 1 160  ? 45.695 51.575  13.642  1.00 9.44  ? 160  PHE A N   1 
ATOM   1093 C  CA  . PHE A 1 160  ? 45.431 52.389  12.463  1.00 9.20  ? 160  PHE A CA  1 
ATOM   1094 C  C   . PHE A 1 160  ? 44.528 51.666  11.494  1.00 9.33  ? 160  PHE A C   1 
ATOM   1095 O  O   . PHE A 1 160  ? 44.741 50.496  11.175  1.00 7.58  ? 160  PHE A O   1 
ATOM   1096 C  CB  . PHE A 1 160  ? 46.742 52.732  11.780  1.00 9.66  ? 160  PHE A CB  1 
ATOM   1097 C  CG  . PHE A 1 160  ? 47.640 53.520  12.654  1.00 10.70 ? 160  PHE A CG  1 
ATOM   1098 C  CD1 . PHE A 1 160  ? 48.692 52.896  13.351  1.00 11.43 ? 160  PHE A CD1 1 
ATOM   1099 C  CD2 . PHE A 1 160  ? 47.406 54.869  12.851  1.00 10.67 ? 160  PHE A CD2 1 
ATOM   1100 C  CE1 . PHE A 1 160  ? 49.496 53.620  14.223  1.00 9.75  ? 160  PHE A CE1 1 
ATOM   1101 C  CE2 . PHE A 1 160  ? 48.204 55.609  13.733  1.00 11.76 ? 160  PHE A CE2 1 
ATOM   1102 C  CZ  . PHE A 1 160  ? 49.246 54.981  14.410  1.00 11.61 ? 160  PHE A CZ  1 
ATOM   1103 N  N   . VAL A 1 161  ? 43.518 52.383  11.034  1.00 9.19  ? 161  VAL A N   1 
ATOM   1104 C  CA  . VAL A 1 161  ? 42.560 51.848  10.096  1.00 8.76  ? 161  VAL A CA  1 
ATOM   1105 C  C   . VAL A 1 161  ? 42.820 52.636  8.810   1.00 10.06 ? 161  VAL A C   1 
ATOM   1106 O  O   . VAL A 1 161  ? 42.955 53.877  8.854   1.00 11.78 ? 161  VAL A O   1 
ATOM   1107 C  CB  . VAL A 1 161  ? 41.106 52.030  10.614  1.00 7.75  ? 161  VAL A CB  1 
ATOM   1108 C  CG1 . VAL A 1 161  ? 40.871 51.101  11.813  1.00 7.58  ? 161  VAL A CG1 1 
ATOM   1109 C  CG2 . VAL A 1 161  ? 40.844 53.487  11.038  1.00 6.16  ? 161  VAL A CG2 1 
ATOM   1110 N  N   . THR A 1 162  ? 42.890 51.901  7.695   1.00 9.36  ? 162  THR A N   1 
ATOM   1111 C  CA  . THR A 1 162  ? 43.198 52.420  6.358   1.00 10.15 ? 162  THR A CA  1 
ATOM   1112 C  C   . THR A 1 162  ? 44.661 52.909  6.338   1.00 10.20 ? 162  THR A C   1 
ATOM   1113 O  O   . THR A 1 162  ? 45.498 52.384  5.598   1.00 10.89 ? 162  THR A O   1 
ATOM   1114 C  CB  . THR A 1 162  ? 42.285 53.614  5.887   1.00 9.22  ? 162  THR A CB  1 
ATOM   1115 O  OG1 . THR A 1 162  ? 40.913 53.240  5.935   1.00 10.99 ? 162  THR A OG1 1 
ATOM   1116 C  CG2 . THR A 1 162  ? 42.602 53.966  4.423   1.00 10.40 ? 162  THR A CG2 1 
ATOM   1117 N  N   . GLY A 1 163  ? 44.986 53.903  7.143   1.00 9.79  ? 163  GLY A N   1 
ATOM   1118 C  CA  . GLY A 1 163  ? 46.371 54.371  7.132   1.00 10.45 ? 163  GLY A CA  1 
ATOM   1119 C  C   . GLY A 1 163  ? 46.733 55.308  5.983   1.00 10.98 ? 163  GLY A C   1 
ATOM   1120 O  O   . GLY A 1 163  ? 47.906 55.432  5.634   1.00 13.09 ? 163  GLY A O   1 
ATOM   1121 N  N   . GLY A 1 164  ? 45.742 55.962  5.384   1.00 10.52 ? 164  GLY A N   1 
ATOM   1122 C  CA  . GLY A 1 164  ? 46.014 56.911  4.314   1.00 9.94  ? 164  GLY A CA  1 
ATOM   1123 C  C   . GLY A 1 164  ? 46.356 58.290  4.879   1.00 10.51 ? 164  GLY A C   1 
ATOM   1124 O  O   . GLY A 1 164  ? 46.108 58.544  6.044   1.00 9.74  ? 164  GLY A O   1 
ATOM   1125 N  N   . TRP A 1 165  ? 46.935 59.182  4.077   1.00 9.81  ? 165  TRP A N   1 
ATOM   1126 C  CA  . TRP A 1 165  ? 47.259 60.515  4.580   1.00 8.96  ? 165  TRP A CA  1 
ATOM   1127 C  C   . TRP A 1 165  ? 45.932 61.131  5.069   1.00 8.52  ? 165  TRP A C   1 
ATOM   1128 O  O   . TRP A 1 165  ? 45.901 61.890  6.038   1.00 8.41  ? 165  TRP A O   1 
ATOM   1129 C  CB  . TRP A 1 165  ? 47.865 61.345  3.451   1.00 8.38  ? 165  TRP A CB  1 
ATOM   1130 C  CG  . TRP A 1 165  ? 48.676 62.512  3.918   1.00 8.98  ? 165  TRP A CG  1 
ATOM   1131 C  CD1 . TRP A 1 165  ? 48.455 63.839  3.637   1.00 8.96  ? 165  TRP A CD1 1 
ATOM   1132 C  CD2 . TRP A 1 165  ? 49.871 62.468  4.735   1.00 9.11  ? 165  TRP A CD2 1 
ATOM   1133 N  NE1 . TRP A 1 165  ? 49.433 64.616  4.233   1.00 8.61  ? 165  TRP A NE1 1 
ATOM   1134 C  CE2 . TRP A 1 165  ? 50.309 63.806  4.905   1.00 8.67  ? 165  TRP A CE2 1 
ATOM   1135 C  CE3 . TRP A 1 165  ? 50.611 61.425  5.327   1.00 10.00 ? 165  TRP A CE3 1 
ATOM   1136 C  CZ2 . TRP A 1 165  ? 51.453 64.135  5.647   1.00 9.14  ? 165  TRP A CZ2 1 
ATOM   1137 C  CZ3 . TRP A 1 165  ? 51.772 61.756  6.075   1.00 9.19  ? 165  TRP A CZ3 1 
ATOM   1138 C  CH2 . TRP A 1 165  ? 52.167 63.097  6.219   1.00 9.47  ? 165  TRP A CH2 1 
ATOM   1139 N  N   . VAL A 1 166  ? 44.838 60.770  4.405   1.00 7.10  ? 166  VAL A N   1 
ATOM   1140 C  CA  . VAL A 1 166  ? 43.504 61.252  4.764   1.00 7.41  ? 166  VAL A CA  1 
ATOM   1141 C  C   . VAL A 1 166  ? 42.497 60.109  4.540   1.00 7.25  ? 166  VAL A C   1 
ATOM   1142 O  O   . VAL A 1 166  ? 42.901 58.975  4.228   1.00 6.75  ? 166  VAL A O   1 
ATOM   1143 C  CB  . VAL A 1 166  ? 43.067 62.492  3.866   1.00 6.90  ? 166  VAL A CB  1 
ATOM   1144 C  CG1 . VAL A 1 166  ? 44.104 63.666  3.986   1.00 5.70  ? 166  VAL A CG1 1 
ATOM   1145 C  CG2 . VAL A 1 166  ? 42.943 62.061  2.387   1.00 8.41  ? 166  VAL A CG2 1 
ATOM   1146 N  N   . MET A 1 167  ? 41.206 60.412  4.735   1.00 7.85  ? 167  MET A N   1 
ATOM   1147 C  CA  . MET A 1 167  ? 40.070 59.502  4.433   1.00 7.23  ? 167  MET A CA  1 
ATOM   1148 C  C   . MET A 1 167  ? 39.543 60.315  3.237   1.00 7.59  ? 167  MET A C   1 
ATOM   1149 O  O   . MET A 1 167  ? 38.799 61.296  3.398   1.00 7.93  ? 167  MET A O   1 
ATOM   1150 C  CB  . MET A 1 167  ? 39.044 59.509  5.563   1.00 7.98  ? 167  MET A CB  1 
ATOM   1151 C  CG  . MET A 1 167  ? 37.769 58.731  5.252   1.00 9.00  ? 167  MET A CG  1 
ATOM   1152 S  SD  . MET A 1 167  ? 36.572 58.948  6.618   1.00 10.52 ? 167  MET A SD  1 
ATOM   1153 C  CE  . MET A 1 167  ? 37.570 58.077  7.995   1.00 7.24  ? 167  MET A CE  1 
ATOM   1154 N  N   . PRO A 1 168  ? 39.894 59.901  2.013   1.00 7.11  ? 168  PRO A N   1 
ATOM   1155 C  CA  . PRO A 1 168  ? 39.456 60.679  0.865   1.00 6.21  ? 168  PRO A CA  1 
ATOM   1156 C  C   . PRO A 1 168  ? 38.025 60.656  0.392   1.00 6.70  ? 168  PRO A C   1 
ATOM   1157 O  O   . PRO A 1 168  ? 37.285 59.736  0.673   1.00 5.33  ? 168  PRO A O   1 
ATOM   1158 C  CB  . PRO A 1 168  ? 40.387 60.178  -0.236  1.00 7.21  ? 168  PRO A CB  1 
ATOM   1159 C  CG  . PRO A 1 168  ? 40.427 58.674  0.076   1.00 6.03  ? 168  PRO A CG  1 
ATOM   1160 C  CD  . PRO A 1 168  ? 40.593 58.676  1.593   1.00 5.96  ? 168  PRO A CD  1 
ATOM   1161 N  N   . ASP A 1 169  ? 37.699 61.692  -0.372  1.00 5.50  ? 169  ASP A N   1 
ATOM   1162 C  CA  . ASP A 1 169  ? 36.432 61.792  -1.077  1.00 5.89  ? 169  ASP A CA  1 
ATOM   1163 C  C   . ASP A 1 169  ? 36.500 60.620  -2.055  1.00 6.94  ? 169  ASP A C   1 
ATOM   1164 O  O   . ASP A 1 169  ? 37.582 60.284  -2.516  1.00 5.59  ? 169  ASP A O   1 
ATOM   1165 C  CB  . ASP A 1 169  ? 36.421 63.078  -1.891  1.00 5.76  ? 169  ASP A CB  1 
ATOM   1166 C  CG  . ASP A 1 169  ? 35.268 63.138  -2.840  1.00 6.05  ? 169  ASP A CG  1 
ATOM   1167 O  OD1 . ASP A 1 169  ? 34.168 62.631  -2.508  1.00 4.74  ? 169  ASP A OD1 1 
ATOM   1168 O  OD2 . ASP A 1 169  ? 35.461 63.716  -3.913  1.00 7.92  ? 169  ASP A OD2 1 
ATOM   1169 N  N   . GLU A 1 170  ? 35.366 60.016  -2.402  1.00 7.21  ? 170  GLU A N   1 
ATOM   1170 C  CA  . GLU A 1 170  ? 35.397 58.890  -3.337  1.00 8.85  ? 170  GLU A CA  1 
ATOM   1171 C  C   . GLU A 1 170  ? 34.707 59.240  -4.653  1.00 8.79  ? 170  GLU A C   1 
ATOM   1172 O  O   . GLU A 1 170  ? 34.709 58.455  -5.611  1.00 9.99  ? 170  GLU A O   1 
ATOM   1173 C  CB  . GLU A 1 170  ? 34.757 57.647  -2.669  1.00 8.68  ? 170  GLU A CB  1 
ATOM   1174 C  CG  . GLU A 1 170  ? 35.638 57.173  -1.480  1.00 8.62  ? 170  GLU A CG  1 
ATOM   1175 C  CD  . GLU A 1 170  ? 35.100 55.977  -0.746  1.00 10.19 ? 170  GLU A CD  1 
ATOM   1176 O  OE1 . GLU A 1 170  ? 34.314 55.206  -1.348  1.00 7.64  ? 170  GLU A OE1 1 
ATOM   1177 O  OE2 . GLU A 1 170  ? 35.495 55.805  0.437   1.00 10.28 ? 170  GLU A OE2 1 
ATOM   1178 N  N   . ALA A 1 171  ? 34.164 60.447  -4.723  1.00 9.55  ? 171  ALA A N   1 
ATOM   1179 C  CA  . ALA A 1 171  ? 33.469 60.844  -5.936  1.00 9.38  ? 171  ALA A CA  1 
ATOM   1180 C  C   . ALA A 1 171  ? 34.288 61.587  -6.980  1.00 9.74  ? 171  ALA A C   1 
ATOM   1181 O  O   . ALA A 1 171  ? 34.316 61.238  -8.174  1.00 10.07 ? 171  ALA A O   1 
ATOM   1182 C  CB  . ALA A 1 171  ? 32.252 61.661  -5.575  1.00 9.23  ? 171  ALA A CB  1 
ATOM   1183 N  N   . ASN A 1 172  ? 34.953 62.629  -6.530  1.00 10.08 ? 172  ASN A N   1 
ATOM   1184 C  CA  . ASN A 1 172  ? 35.718 63.481  -7.416  1.00 8.17  ? 172  ASN A CA  1 
ATOM   1185 C  C   . ASN A 1 172  ? 37.171 63.053  -7.583  1.00 8.32  ? 172  ASN A C   1 
ATOM   1186 O  O   . ASN A 1 172  ? 37.833 63.415  -8.554  1.00 8.44  ? 172  ASN A O   1 
ATOM   1187 C  CB  . ASN A 1 172  ? 35.681 64.881  -6.824  1.00 7.97  ? 172  ASN A CB  1 
ATOM   1188 C  CG  . ASN A 1 172  ? 34.256 65.430  -6.675  1.00 8.20  ? 172  ASN A CG  1 
ATOM   1189 O  OD1 . ASN A 1 172  ? 33.555 65.680  -7.679  1.00 8.70  ? 172  ASN A OD1 1 
ATOM   1190 N  ND2 . ASN A 1 172  ? 33.827 65.643  -5.427  1.00 7.18  ? 172  ASN A ND2 1 
ATOM   1191 N  N   . SER A 1 173  ? 37.679 62.308  -6.610  1.00 8.08  ? 173  SER A N   1 
ATOM   1192 C  CA  . SER A 1 173  ? 39.077 61.931  -6.619  1.00 7.77  ? 173  SER A CA  1 
ATOM   1193 C  C   . SER A 1 173  ? 39.489 61.017  -7.737  1.00 8.14  ? 173  SER A C   1 
ATOM   1194 O  O   . SER A 1 173  ? 38.732 60.107  -8.114  1.00 7.64  ? 173  SER A O   1 
ATOM   1195 C  CB  . SER A 1 173  ? 39.445 61.279  -5.307  1.00 6.73  ? 173  SER A CB  1 
ATOM   1196 O  OG  . SER A 1 173  ? 38.542 60.226  -4.993  1.00 9.02  ? 173  SER A OG  1 
ATOM   1197 N  N   . HIS A 1 174  ? 40.686 61.260  -8.263  1.00 6.51  ? 174  HIS A N   1 
ATOM   1198 C  CA  . HIS A 1 174  ? 41.196 60.376  -9.319  1.00 7.00  ? 174  HIS A CA  1 
ATOM   1199 C  C   . HIS A 1 174  ? 41.851 59.177  -8.617  1.00 5.64  ? 174  HIS A C   1 
ATOM   1200 O  O   . HIS A 1 174  ? 42.496 59.346  -7.608  1.00 4.22  ? 174  HIS A O   1 
ATOM   1201 C  CB  . HIS A 1 174  ? 42.205 61.104  -10.186 1.00 7.18  ? 174  HIS A CB  1 
ATOM   1202 C  CG  . HIS A 1 174  ? 42.438 60.428  -11.492 1.00 6.79  ? 174  HIS A CG  1 
ATOM   1203 N  ND1 . HIS A 1 174  ? 43.119 59.232  -11.594 1.00 6.73  ? 174  HIS A ND1 1 
ATOM   1204 C  CD2 . HIS A 1 174  ? 41.987 60.717  -12.737 1.00 7.15  ? 174  HIS A CD2 1 
ATOM   1205 C  CE1 . HIS A 1 174  ? 43.074 58.812  -12.848 1.00 6.73  ? 174  HIS A CE1 1 
ATOM   1206 N  NE2 . HIS A 1 174  ? 42.393 59.693  -13.560 1.00 6.76  ? 174  HIS A NE2 1 
ATOM   1207 N  N   . TRP A 1 175  ? 41.682 57.968  -9.147  1.00 5.21  ? 175  TRP A N   1 
ATOM   1208 C  CA  . TRP A 1 175  ? 42.241 56.814  -8.487  1.00 5.70  ? 175  TRP A CA  1 
ATOM   1209 C  C   . TRP A 1 175  ? 43.721 56.990  -8.301  1.00 6.01  ? 175  TRP A C   1 
ATOM   1210 O  O   . TRP A 1 175  ? 44.288 56.491  -7.310  1.00 6.77  ? 175  TRP A O   1 
ATOM   1211 C  CB  . TRP A 1 175  ? 41.943 55.520  -9.264  1.00 6.30  ? 175  TRP A CB  1 
ATOM   1212 C  CG  . TRP A 1 175  ? 42.768 55.324  -10.536 1.00 6.95  ? 175  TRP A CG  1 
ATOM   1213 C  CD1 . TRP A 1 175  ? 42.427 55.685  -11.805 1.00 7.65  ? 175  TRP A CD1 1 
ATOM   1214 C  CD2 . TRP A 1 175  ? 44.080 54.722  -10.626 1.00 8.32  ? 175  TRP A CD2 1 
ATOM   1215 N  NE1 . TRP A 1 175  ? 43.453 55.347  -12.693 1.00 7.04  ? 175  TRP A NE1 1 
ATOM   1216 C  CE2 . TRP A 1 175  ? 44.470 54.756  -11.997 1.00 6.85  ? 175  TRP A CE2 1 
ATOM   1217 C  CE3 . TRP A 1 175  ? 44.961 54.150  -9.678  1.00 7.29  ? 175  TRP A CE3 1 
ATOM   1218 C  CZ2 . TRP A 1 175  ? 45.703 54.239  -12.451 1.00 6.90  ? 175  TRP A CZ2 1 
ATOM   1219 C  CZ3 . TRP A 1 175  ? 46.194 53.629  -10.139 1.00 8.55  ? 175  TRP A CZ3 1 
ATOM   1220 C  CH2 . TRP A 1 175  ? 46.544 53.683  -11.515 1.00 7.39  ? 175  TRP A CH2 1 
ATOM   1221 N  N   . ARG A 1 176  ? 44.377 57.706  -9.215  1.00 6.05  ? 176  ARG A N   1 
ATOM   1222 C  CA  . ARG A 1 176  ? 45.811 57.897  -9.042  1.00 6.20  ? 176  ARG A CA  1 
ATOM   1223 C  C   . ARG A 1 176  ? 46.159 58.639  -7.733  1.00 7.33  ? 176  ARG A C   1 
ATOM   1224 O  O   . ARG A 1 176  ? 47.170 58.305  -7.040  1.00 7.70  ? 176  ARG A O   1 
ATOM   1225 C  CB  . ARG A 1 176  ? 46.400 58.616  -10.274 1.00 6.79  ? 176  ARG A CB  1 
ATOM   1226 C  CG  . ARG A 1 176  ? 46.430 57.727  -11.533 1.00 7.64  ? 176  ARG A CG  1 
ATOM   1227 C  CD  . ARG A 1 176  ? 46.424 58.546  -12.818 1.00 9.48  ? 176  ARG A CD  1 
ATOM   1228 N  NE  . ARG A 1 176  ? 47.510 59.520  -12.899 1.00 10.39 ? 176  ARG A NE  1 
ATOM   1229 C  CZ  . ARG A 1 176  ? 47.681 60.367  -13.925 1.00 10.81 ? 176  ARG A CZ  1 
ATOM   1230 N  NH1 . ARG A 1 176  ? 46.845 60.352  -14.958 1.00 8.86  ? 176  ARG A NH1 1 
ATOM   1231 N  NH2 . ARG A 1 176  ? 48.667 61.258  -13.894 1.00 9.61  ? 176  ARG A NH2 1 
ATOM   1232 N  N   . ASN A 1 177  ? 45.362 59.642  -7.384  1.00 5.82  ? 177  ASN A N   1 
ATOM   1233 C  CA  . ASN A 1 177  ? 45.609 60.415  -6.154  1.00 6.28  ? 177  ASN A CA  1 
ATOM   1234 C  C   . ASN A 1 177  ? 45.119 59.687  -4.907  1.00 6.62  ? 177  ASN A C   1 
ATOM   1235 O  O   . ASN A 1 177  ? 45.608 59.930  -3.773  1.00 7.44  ? 177  ASN A O   1 
ATOM   1236 C  CB  . ASN A 1 177  ? 44.980 61.811  -6.266  1.00 4.90  ? 177  ASN A CB  1 
ATOM   1237 C  CG  . ASN A 1 177  ? 45.656 62.640  -7.331  1.00 7.27  ? 177  ASN A CG  1 
ATOM   1238 O  OD1 . ASN A 1 177  ? 46.815 62.398  -7.651  1.00 8.87  ? 177  ASN A OD1 1 
ATOM   1239 N  ND2 . ASN A 1 177  ? 44.939 63.594  -7.905  1.00 10.16 ? 177  ASN A ND2 1 
ATOM   1240 N  N   . VAL A 1 178  ? 44.137 58.808  -5.100  1.00 6.41  ? 178  VAL A N   1 
ATOM   1241 C  CA  . VAL A 1 178  ? 43.664 58.004  -3.978  1.00 5.88  ? 178  VAL A CA  1 
ATOM   1242 C  C   . VAL A 1 178  ? 44.854 57.061  -3.621  1.00 6.70  ? 178  VAL A C   1 
ATOM   1243 O  O   . VAL A 1 178  ? 45.161 56.841  -2.440  1.00 5.94  ? 178  VAL A O   1 
ATOM   1244 C  CB  . VAL A 1 178  ? 42.418 57.159  -4.367  1.00 6.62  ? 178  VAL A CB  1 
ATOM   1245 C  CG1 . VAL A 1 178  ? 42.144 56.108  -3.277  1.00 6.85  ? 178  VAL A CG1 1 
ATOM   1246 C  CG2 . VAL A 1 178  ? 41.176 58.092  -4.520  1.00 6.81  ? 178  VAL A CG2 1 
ATOM   1247 N  N   . LEU A 1 179  ? 45.504 56.482  -4.638  1.00 4.35  ? 179  LEU A N   1 
ATOM   1248 C  CA  . LEU A 1 179  ? 46.643 55.605  -4.383  1.00 6.57  ? 179  LEU A CA  1 
ATOM   1249 C  C   . LEU A 1 179  ? 47.788 56.442  -3.794  1.00 7.07  ? 179  LEU A C   1 
ATOM   1250 O  O   . LEU A 1 179  ? 48.454 56.039  -2.842  1.00 8.26  ? 179  LEU A O   1 
ATOM   1251 C  CB  . LEU A 1 179  ? 47.136 54.937  -5.691  1.00 7.26  ? 179  LEU A CB  1 
ATOM   1252 C  CG  . LEU A 1 179  ? 48.420 54.079  -5.519  1.00 6.82  ? 179  LEU A CG  1 
ATOM   1253 C  CD1 . LEU A 1 179  ? 48.197 52.971  -4.478  1.00 4.84  ? 179  LEU A CD1 1 
ATOM   1254 C  CD2 . LEU A 1 179  ? 48.815 53.471  -6.873  1.00 6.19  ? 179  LEU A CD2 1 
ATOM   1255 N  N   . LEU A 1 180  ? 48.013 57.631  -4.360  1.00 7.09  ? 180  LEU A N   1 
ATOM   1256 C  CA  . LEU A 1 180  ? 49.078 58.480  -3.872  1.00 8.01  ? 180  LEU A CA  1 
ATOM   1257 C  C   . LEU A 1 180  ? 48.939 58.738  -2.353  1.00 8.53  ? 180  LEU A C   1 
ATOM   1258 O  O   . LEU A 1 180  ? 49.902 58.544  -1.591  1.00 7.41  ? 180  LEU A O   1 
ATOM   1259 C  CB  . LEU A 1 180  ? 49.061 59.822  -4.597  1.00 7.77  ? 180  LEU A CB  1 
ATOM   1260 C  CG  . LEU A 1 180  ? 50.184 60.785  -4.212  1.00 8.24  ? 180  LEU A CG  1 
ATOM   1261 C  CD1 . LEU A 1 180  ? 51.477 60.232  -4.801  1.00 8.00  ? 180  LEU A CD1 1 
ATOM   1262 C  CD2 . LEU A 1 180  ? 49.906 62.187  -4.721  1.00 5.88  ? 180  LEU A CD2 1 
ATOM   1263 N  N   . GLN A 1 181  ? 47.752 59.163  -1.911  1.00 8.43  ? 181  GLN A N   1 
ATOM   1264 C  CA  . GLN A 1 181  ? 47.575 59.491  -0.489  1.00 7.67  ? 181  GLN A CA  1 
ATOM   1265 C  C   . GLN A 1 181  ? 47.616 58.270  0.392   1.00 7.52  ? 181  GLN A C   1 
ATOM   1266 O  O   . GLN A 1 181  ? 48.110 58.357  1.508   1.00 7.19  ? 181  GLN A O   1 
ATOM   1267 C  CB  . GLN A 1 181  ? 46.293 60.320  -0.251  1.00 7.38  ? 181  GLN A CB  1 
ATOM   1268 C  CG  . GLN A 1 181  ? 44.970 59.624  -0.484  1.00 7.53  ? 181  GLN A CG  1 
ATOM   1269 C  CD  . GLN A 1 181  ? 44.592 58.678  0.655   1.00 9.27  ? 181  GLN A CD  1 
ATOM   1270 O  OE1 . GLN A 1 181  ? 44.846 58.965  1.819   1.00 8.56  ? 181  GLN A OE1 1 
ATOM   1271 N  NE2 . GLN A 1 181  ? 43.968 57.562  0.317   1.00 7.53  ? 181  GLN A NE2 1 
ATOM   1272 N  N   . LEU A 1 182  ? 47.112 57.134  -0.105  1.00 5.60  ? 182  LEU A N   1 
ATOM   1273 C  CA  . LEU A 1 182  ? 47.166 55.893  0.651   1.00 5.63  ? 182  LEU A CA  1 
ATOM   1274 C  C   . LEU A 1 182  ? 48.638 55.518  0.871   1.00 5.65  ? 182  LEU A C   1 
ATOM   1275 O  O   . LEU A 1 182  ? 49.058 55.164  1.967   1.00 5.37  ? 182  LEU A O   1 
ATOM   1276 C  CB  . LEU A 1 182  ? 46.487 54.734  -0.120  1.00 3.63  ? 182  LEU A CB  1 
ATOM   1277 C  CG  . LEU A 1 182  ? 46.576 53.369  0.560   1.00 4.48  ? 182  LEU A CG  1 
ATOM   1278 C  CD1 . LEU A 1 182  ? 45.774 53.385  1.900   1.00 3.30  ? 182  LEU A CD1 1 
ATOM   1279 C  CD2 . LEU A 1 182  ? 46.003 52.260  -0.370  1.00 4.79  ? 182  LEU A CD2 1 
ATOM   1280 N  N   . THR A 1 183  ? 49.422 55.614  -0.197  1.00 6.51  ? 183  THR A N   1 
ATOM   1281 C  CA  . THR A 1 183  ? 50.829 55.267  -0.142  1.00 7.56  ? 183  THR A CA  1 
ATOM   1282 C  C   . THR A 1 183  ? 51.591 56.229  0.798   1.00 8.63  ? 183  THR A C   1 
ATOM   1283 O  O   . THR A 1 183  ? 52.507 55.810  1.520   1.00 10.21 ? 183  THR A O   1 
ATOM   1284 C  CB  . THR A 1 183  ? 51.505 55.315  -1.579  1.00 7.80  ? 183  THR A CB  1 
ATOM   1285 O  OG1 . THR A 1 183  ? 50.817 54.438  -2.479  1.00 7.56  ? 183  THR A OG1 1 
ATOM   1286 C  CG2 . THR A 1 183  ? 53.004 54.863  -1.506  1.00 6.66  ? 183  THR A CG2 1 
ATOM   1287 N  N   . GLU A 1 184  ? 51.237 57.503  0.776   1.00 8.23  ? 184  GLU A N   1 
ATOM   1288 C  CA  . GLU A 1 184  ? 51.939 58.472  1.613   1.00 9.54  ? 184  GLU A CA  1 
ATOM   1289 C  C   . GLU A 1 184  ? 51.747 58.126  3.105   1.00 8.64  ? 184  GLU A C   1 
ATOM   1290 O  O   . GLU A 1 184  ? 52.695 58.138  3.888   1.00 10.08 ? 184  GLU A O   1 
ATOM   1291 C  CB  . GLU A 1 184  ? 51.402 59.875  1.328   1.00 9.30  ? 184  GLU A CB  1 
ATOM   1292 C  CG  . GLU A 1 184  ? 52.254 61.005  1.856   1.00 11.95 ? 184  GLU A CG  1 
ATOM   1293 C  CD  . GLU A 1 184  ? 53.651 61.080  1.196   1.00 12.75 ? 184  GLU A CD  1 
ATOM   1294 O  OE1 . GLU A 1 184  ? 53.805 60.759  0.002   1.00 12.77 ? 184  GLU A OE1 1 
ATOM   1295 O  OE2 . GLU A 1 184  ? 54.595 61.467  1.890   1.00 14.83 ? 184  GLU A OE2 1 
ATOM   1296 N  N   . GLY A 1 185  ? 50.526 57.806  3.491   1.00 6.95  ? 185  GLY A N   1 
ATOM   1297 C  CA  . GLY A 1 185  ? 50.278 57.469  4.886   1.00 7.70  ? 185  GLY A CA  1 
ATOM   1298 C  C   . GLY A 1 185  ? 50.853 56.116  5.293   1.00 8.09  ? 185  GLY A C   1 
ATOM   1299 O  O   . GLY A 1 185  ? 51.436 55.966  6.385   1.00 7.61  ? 185  GLY A O   1 
ATOM   1300 N  N   . GLN A 1 186  ? 50.688 55.120  4.431   1.00 7.49  ? 186  GLN A N   1 
ATOM   1301 C  CA  . GLN A 1 186  ? 51.206 53.788  4.751   1.00 9.19  ? 186  GLN A CA  1 
ATOM   1302 C  C   . GLN A 1 186  ? 52.748 53.704  4.731   1.00 9.71  ? 186  GLN A C   1 
ATOM   1303 O  O   . GLN A 1 186  ? 53.331 52.915  5.471   1.00 9.49  ? 186  GLN A O   1 
ATOM   1304 C  CB  . GLN A 1 186  ? 50.592 52.716  3.819   1.00 9.76  ? 186  GLN A CB  1 
ATOM   1305 C  CG  . GLN A 1 186  ? 49.059 52.497  4.079   1.00 11.39 ? 186  GLN A CG  1 
ATOM   1306 C  CD  . GLN A 1 186  ? 48.619 51.097  3.727   1.00 11.00 ? 186  GLN A CD  1 
ATOM   1307 O  OE1 . GLN A 1 186  ? 49.275 50.434  2.938   1.00 13.74 ? 186  GLN A OE1 1 
ATOM   1308 N  NE2 . GLN A 1 186  ? 47.526 50.633  4.311   1.00 11.77 ? 186  GLN A NE2 1 
ATOM   1309 N  N   . THR A 1 187  ? 53.401 54.508  3.892   1.00 9.16  ? 187  THR A N   1 
ATOM   1310 C  CA  . THR A 1 187  ? 54.848 54.484  3.861   1.00 8.00  ? 187  THR A CA  1 
ATOM   1311 C  C   . THR A 1 187  ? 55.346 55.085  5.195   1.00 8.97  ? 187  THR A C   1 
ATOM   1312 O  O   . THR A 1 187  ? 56.278 54.580  5.803   1.00 8.83  ? 187  THR A O   1 
ATOM   1313 C  CB  . THR A 1 187  ? 55.366 55.249  2.650   1.00 9.01  ? 187  THR A CB  1 
ATOM   1314 O  OG1 . THR A 1 187  ? 54.897 54.585  1.455   1.00 7.14  ? 187  THR A OG1 1 
ATOM   1315 C  CG2 . THR A 1 187  ? 56.919 55.267  2.637   1.00 6.28  ? 187  THR A CG2 1 
ATOM   1316 N  N   . TRP A 1 188  ? 54.701 56.140  5.657   1.00 9.29  ? 188  TRP A N   1 
ATOM   1317 C  CA  . TRP A 1 188  ? 55.060 56.747  6.925   1.00 10.03 ? 188  TRP A CA  1 
ATOM   1318 C  C   . TRP A 1 188  ? 54.825 55.689  8.037   1.00 10.48 ? 188  TRP A C   1 
ATOM   1319 O  O   . TRP A 1 188  ? 55.694 55.450  8.880   1.00 9.94  ? 188  TRP A O   1 
ATOM   1320 C  CB  . TRP A 1 188  ? 54.182 57.992  7.195   1.00 11.14 ? 188  TRP A CB  1 
ATOM   1321 C  CG  . TRP A 1 188  ? 54.624 58.780  8.422   1.00 11.39 ? 188  TRP A CG  1 
ATOM   1322 C  CD1 . TRP A 1 188  ? 55.533 59.813  8.463   1.00 11.47 ? 188  TRP A CD1 1 
ATOM   1323 C  CD2 . TRP A 1 188  ? 54.287 58.490  9.790   1.00 11.15 ? 188  TRP A CD2 1 
ATOM   1324 N  NE1 . TRP A 1 188  ? 55.790 60.161  9.767   1.00 9.68  ? 188  TRP A NE1 1 
ATOM   1325 C  CE2 . TRP A 1 188  ? 55.044 59.374  10.603  1.00 10.62 ? 188  TRP A CE2 1 
ATOM   1326 C  CE3 . TRP A 1 188  ? 53.435 57.564  10.402  1.00 8.95  ? 188  TRP A CE3 1 
ATOM   1327 C  CZ2 . TRP A 1 188  ? 54.973 59.363  12.005  1.00 8.92  ? 188  TRP A CZ2 1 
ATOM   1328 C  CZ3 . TRP A 1 188  ? 53.364 57.542  11.824  1.00 12.44 ? 188  TRP A CZ3 1 
ATOM   1329 C  CH2 . TRP A 1 188  ? 54.137 58.448  12.597  1.00 11.44 ? 188  TRP A CH2 1 
ATOM   1330 N  N   . LEU A 1 189  ? 53.659 55.039  8.030   1.00 9.61  ? 189  LEU A N   1 
ATOM   1331 C  CA  . LEU A 1 189  ? 53.356 54.050  9.069   1.00 10.74 ? 189  LEU A CA  1 
ATOM   1332 C  C   . LEU A 1 189  ? 54.357 52.900  9.111   1.00 11.02 ? 189  LEU A C   1 
ATOM   1333 O  O   . LEU A 1 189  ? 54.779 52.474  10.196  1.00 12.24 ? 189  LEU A O   1 
ATOM   1334 C  CB  . LEU A 1 189  ? 51.934 53.474  8.892   1.00 10.64 ? 189  LEU A CB  1 
ATOM   1335 C  CG  . LEU A 1 189  ? 50.776 54.347  9.417   1.00 10.09 ? 189  LEU A CG  1 
ATOM   1336 C  CD1 . LEU A 1 189  ? 49.443 53.603  9.117   1.00 10.13 ? 189  LEU A CD1 1 
ATOM   1337 C  CD2 . LEU A 1 189  ? 50.930 54.550  10.984  1.00 8.04  ? 189  LEU A CD2 1 
ATOM   1338 N  N   . LYS A 1 190  ? 54.734 52.382  7.949   1.00 11.01 ? 190  LYS A N   1 
ATOM   1339 C  CA  . LYS A 1 190  ? 55.694 51.271  7.937   1.00 13.55 ? 190  LYS A CA  1 
ATOM   1340 C  C   . LYS A 1 190  ? 57.018 51.726  8.533   1.00 13.26 ? 190  LYS A C   1 
ATOM   1341 O  O   . LYS A 1 190  ? 57.625 51.054  9.346   1.00 12.19 ? 190  LYS A O   1 
ATOM   1342 C  CB  . LYS A 1 190  ? 55.997 50.777  6.509   1.00 15.43 ? 190  LYS A CB  1 
ATOM   1343 C  CG  . LYS A 1 190  ? 56.850 49.478  6.512   1.00 14.85 ? 190  LYS A CG  1 
ATOM   1344 C  CD  . LYS A 1 190  ? 56.984 48.926  5.136   1.00 18.30 ? 190  LYS A CD  1 
ATOM   1345 C  CE  . LYS A 1 190  ? 57.861 47.655  5.104   1.00 21.93 ? 190  LYS A CE  1 
ATOM   1346 N  NZ  . LYS A 1 190  ? 58.267 47.357  3.672   1.00 22.19 ? 190  LYS A NZ  1 
ATOM   1347 N  N   . GLN A 1 191  ? 57.446 52.897  8.115   1.00 13.23 ? 191  GLN A N   1 
ATOM   1348 C  CA  . GLN A 1 191  ? 58.713 53.412  8.558   1.00 15.34 ? 191  GLN A CA  1 
ATOM   1349 C  C   . GLN A 1 191  ? 58.808 53.704  10.048  1.00 14.72 ? 191  GLN A C   1 
ATOM   1350 O  O   . GLN A 1 191  ? 59.758 53.287  10.710  1.00 15.13 ? 191  GLN A O   1 
ATOM   1351 C  CB  . GLN A 1 191  ? 59.031 54.680  7.790   1.00 16.55 ? 191  GLN A CB  1 
ATOM   1352 C  CG  . GLN A 1 191  ? 60.477 55.085  7.883   1.00 22.90 ? 191  GLN A CG  1 
ATOM   1353 C  CD  . GLN A 1 191  ? 60.720 56.446  7.251   1.00 25.99 ? 191  GLN A CD  1 
ATOM   1354 O  OE1 . GLN A 1 191  ? 60.049 56.838  6.269   1.00 28.53 ? 191  GLN A OE1 1 
ATOM   1355 N  NE2 . GLN A 1 191  ? 61.678 57.183  7.811   1.00 28.37 ? 191  GLN A NE2 1 
ATOM   1356 N  N   . PHE A 1 192  ? 57.835 54.439  10.574  1.00 13.84 ? 192  PHE A N   1 
ATOM   1357 C  CA  . PHE A 1 192  ? 57.860 54.823  11.968  1.00 13.91 ? 192  PHE A CA  1 
ATOM   1358 C  C   . PHE A 1 192  ? 57.069 54.002  12.973  1.00 14.70 ? 192  PHE A C   1 
ATOM   1359 O  O   . PHE A 1 192  ? 57.381 54.040  14.165  1.00 14.60 ? 192  PHE A O   1 
ATOM   1360 C  CB  . PHE A 1 192  ? 57.423 56.279  12.092  1.00 12.43 ? 192  PHE A CB  1 
ATOM   1361 C  CG  . PHE A 1 192  ? 58.323 57.223  11.377  1.00 14.59 ? 192  PHE A CG  1 
ATOM   1362 C  CD1 . PHE A 1 192  ? 58.007 57.667  10.087  1.00 13.13 ? 192  PHE A CD1 1 
ATOM   1363 C  CD2 . PHE A 1 192  ? 59.519 57.656  11.974  1.00 14.60 ? 192  PHE A CD2 1 
ATOM   1364 C  CE1 . PHE A 1 192  ? 58.849 58.524  9.401   1.00 13.93 ? 192  PHE A CE1 1 
ATOM   1365 C  CE2 . PHE A 1 192  ? 60.382 58.527  11.276  1.00 15.06 ? 192  PHE A CE2 1 
ATOM   1366 C  CZ  . PHE A 1 192  ? 60.037 58.958  9.990   1.00 14.48 ? 192  PHE A CZ  1 
ATOM   1367 N  N   . MET A 1 193  ? 56.025 53.316  12.530  1.00 13.30 ? 193  MET A N   1 
ATOM   1368 C  CA  . MET A 1 193  ? 55.210 52.535  13.464  1.00 14.07 ? 193  MET A CA  1 
ATOM   1369 C  C   . MET A 1 193  ? 55.366 51.045  13.189  1.00 13.49 ? 193  MET A C   1 
ATOM   1370 O  O   . MET A 1 193  ? 54.858 50.207  13.948  1.00 13.81 ? 193  MET A O   1 
ATOM   1371 C  CB  . MET A 1 193  ? 53.723 52.925  13.337  1.00 14.96 ? 193  MET A CB  1 
ATOM   1372 C  CG  . MET A 1 193  ? 53.338 54.298  13.899  1.00 17.41 ? 193  MET A CG  1 
ATOM   1373 S  SD  . MET A 1 193  ? 53.618 54.427  15.730  1.00 24.09 ? 193  MET A SD  1 
ATOM   1374 C  CE  . MET A 1 193  ? 55.041 55.473  15.528  1.00 21.33 ? 193  MET A CE  1 
ATOM   1375 N  N   . ASN A 1 194  ? 56.030 50.717  12.082  1.00 13.75 ? 194  ASN A N   1 
ATOM   1376 C  CA  . ASN A 1 194  ? 56.272 49.326  11.707  1.00 15.81 ? 194  ASN A CA  1 
ATOM   1377 C  C   . ASN A 1 194  ? 54.955 48.515  11.573  1.00 15.75 ? 194  ASN A C   1 
ATOM   1378 O  O   . ASN A 1 194  ? 54.875 47.377  12.029  1.00 15.99 ? 194  ASN A O   1 
ATOM   1379 C  CB  . ASN A 1 194  ? 57.210 48.703  12.761  1.00 19.88 ? 194  ASN A CB  1 
ATOM   1380 C  CG  . ASN A 1 194  ? 57.541 47.249  12.482  1.00 25.90 ? 194  ASN A CG  1 
ATOM   1381 O  OD1 . ASN A 1 194  ? 57.777 46.864  11.342  1.00 25.29 ? 194  ASN A OD1 1 
ATOM   1382 N  ND2 . ASN A 1 194  ? 57.534 46.483  13.572  1.00 33.09 ? 194  ASN A ND2 1 
ATOM   1383 N  N   . VAL A 1 195  ? 53.926 49.123  10.980  1.00 14.20 ? 195  VAL A N   1 
ATOM   1384 C  CA  . VAL A 1 195  ? 52.631 48.468  10.764  1.00 13.18 ? 195  VAL A CA  1 
ATOM   1385 C  C   . VAL A 1 195  ? 52.027 48.909  9.434   1.00 12.26 ? 195  VAL A C   1 
ATOM   1386 O  O   . VAL A 1 195  ? 52.239 50.044  8.997   1.00 10.05 ? 195  VAL A O   1 
ATOM   1387 C  CB  . VAL A 1 195  ? 51.559 48.790  11.872  1.00 15.16 ? 195  VAL A CB  1 
ATOM   1388 C  CG1 . VAL A 1 195  ? 52.017 48.261  13.249  1.00 17.23 ? 195  VAL A CG1 1 
ATOM   1389 C  CG2 . VAL A 1 195  ? 51.260 50.280  11.922  1.00 14.45 ? 195  VAL A CG2 1 
ATOM   1390 N  N   . THR A 1 196  ? 51.270 48.000  8.825   1.00 10.47 ? 196  THR A N   1 
ATOM   1391 C  CA  . THR A 1 196  ? 50.561 48.228  7.578   1.00 11.25 ? 196  THR A CA  1 
ATOM   1392 C  C   . THR A 1 196  ? 49.099 47.765  7.764   1.00 11.45 ? 196  THR A C   1 
ATOM   1393 O  O   . THR A 1 196  ? 48.822 46.563  7.799   1.00 9.91  ? 196  THR A O   1 
ATOM   1394 C  CB  . THR A 1 196  ? 51.212 47.434  6.422   1.00 11.68 ? 196  THR A CB  1 
ATOM   1395 O  OG1 . THR A 1 196  ? 52.533 47.947  6.209   1.00 12.95 ? 196  THR A OG1 1 
ATOM   1396 C  CG2 . THR A 1 196  ? 50.410 47.591  5.149   1.00 11.61 ? 196  THR A CG2 1 
ATOM   1397 N  N   . PRO A 1 197  ? 48.157 48.712  7.914   1.00 11.05 ? 197  PRO A N   1 
ATOM   1398 C  CA  . PRO A 1 197  ? 46.734 48.373  8.096   1.00 12.11 ? 197  PRO A CA  1 
ATOM   1399 C  C   . PRO A 1 197  ? 46.206 47.469  6.982   1.00 12.33 ? 197  PRO A C   1 
ATOM   1400 O  O   . PRO A 1 197  ? 46.580 47.629  5.840   1.00 12.69 ? 197  PRO A O   1 
ATOM   1401 C  CB  . PRO A 1 197  ? 46.041 49.725  8.053   1.00 11.96 ? 197  PRO A CB  1 
ATOM   1402 C  CG  . PRO A 1 197  ? 47.090 50.651  8.656   1.00 11.86 ? 197  PRO A CG  1 
ATOM   1403 C  CD  . PRO A 1 197  ? 48.390 50.157  8.064   1.00 11.45 ? 197  PRO A CD  1 
ATOM   1404 N  N   . THR A 1 198  ? 45.371 46.492  7.326   1.00 11.84 ? 198  THR A N   1 
ATOM   1405 C  CA  . THR A 1 198  ? 44.776 45.654  6.299   1.00 10.40 ? 198  THR A CA  1 
ATOM   1406 C  C   . THR A 1 198  ? 43.264 45.812  6.386   1.00 9.11  ? 198  THR A C   1 
ATOM   1407 O  O   . THR A 1 198  ? 42.542 45.141  5.654   1.00 7.99  ? 198  THR A O   1 
ATOM   1408 C  CB  . THR A 1 198  ? 45.089 44.168  6.446   1.00 11.27 ? 198  THR A CB  1 
ATOM   1409 O  OG1 . THR A 1 198  ? 44.534 43.722  7.682   1.00 10.32 ? 198  THR A OG1 1 
ATOM   1410 C  CG2 . THR A 1 198  ? 46.619 43.900  6.359   1.00 10.79 ? 198  THR A CG2 1 
ATOM   1411 N  N   . ALA A 1 199  ? 42.790 46.678  7.294   1.00 9.01  ? 199  ALA A N   1 
ATOM   1412 C  CA  . ALA A 1 199  ? 41.364 46.973  7.388   1.00 8.15  ? 199  ALA A CA  1 
ATOM   1413 C  C   . ALA A 1 199  ? 41.159 48.488  7.131   1.00 8.77  ? 199  ALA A C   1 
ATOM   1414 O  O   . ALA A 1 199  ? 41.867 49.323  7.720   1.00 8.52  ? 199  ALA A O   1 
ATOM   1415 C  CB  . ALA A 1 199  ? 40.804 46.598  8.795   1.00 8.45  ? 199  ALA A CB  1 
ATOM   1416 N  N   . SER A 1 200  ? 40.171 48.839  6.307   1.00 7.32  ? 200  SER A N   1 
ATOM   1417 C  CA  . SER A 1 200  ? 39.907 50.247  5.991   1.00 8.97  ? 200  SER A CA  1 
ATOM   1418 C  C   . SER A 1 200  ? 38.656 50.730  6.697   1.00 9.37  ? 200  SER A C   1 
ATOM   1419 O  O   . SER A 1 200  ? 37.736 49.951  6.953   1.00 10.38 ? 200  SER A O   1 
ATOM   1420 C  CB  . SER A 1 200  ? 39.752 50.467  4.471   1.00 9.75  ? 200  SER A CB  1 
ATOM   1421 O  OG  . SER A 1 200  ? 39.568 51.841  4.191   1.00 11.17 ? 200  SER A OG  1 
ATOM   1422 N  N   . TRP A 1 201  ? 38.626 52.019  6.990   1.00 7.64  ? 201  TRP A N   1 
ATOM   1423 C  CA  . TRP A 1 201  ? 37.538 52.641  7.724   1.00 8.97  ? 201  TRP A CA  1 
ATOM   1424 C  C   . TRP A 1 201  ? 37.203 53.975  7.022   1.00 9.89  ? 201  TRP A C   1 
ATOM   1425 O  O   . TRP A 1 201  ? 38.004 54.905  7.059   1.00 10.50 ? 201  TRP A O   1 
ATOM   1426 C  CB  . TRP A 1 201  ? 38.038 52.887  9.155   1.00 8.60  ? 201  TRP A CB  1 
ATOM   1427 C  CG  . TRP A 1 201  ? 37.174 53.752  10.078  1.00 10.44 ? 201  TRP A CG  1 
ATOM   1428 C  CD1 . TRP A 1 201  ? 37.289 55.098  10.295  1.00 10.74 ? 201  TRP A CD1 1 
ATOM   1429 C  CD2 . TRP A 1 201  ? 36.214 53.278  11.029  1.00 10.46 ? 201  TRP A CD2 1 
ATOM   1430 N  NE1 . TRP A 1 201  ? 36.479 55.496  11.343  1.00 11.43 ? 201  TRP A NE1 1 
ATOM   1431 C  CE2 . TRP A 1 201  ? 35.807 54.396  11.811  1.00 11.74 ? 201  TRP A CE2 1 
ATOM   1432 C  CE3 . TRP A 1 201  ? 35.662 52.021  11.302  1.00 10.44 ? 201  TRP A CE3 1 
ATOM   1433 C  CZ2 . TRP A 1 201  ? 34.878 54.288  12.842  1.00 11.82 ? 201  TRP A CZ2 1 
ATOM   1434 C  CZ3 . TRP A 1 201  ? 34.728 51.915  12.344  1.00 10.47 ? 201  TRP A CZ3 1 
ATOM   1435 C  CH2 . TRP A 1 201  ? 34.349 53.043  13.096  1.00 11.47 ? 201  TRP A CH2 1 
ATOM   1436 N  N   . ALA A 1 202  ? 36.036 54.047  6.391   1.00 9.43  ? 202  ALA A N   1 
ATOM   1437 C  CA  . ALA A 1 202  ? 35.642 55.253  5.669   1.00 9.72  ? 202  ALA A CA  1 
ATOM   1438 C  C   . ALA A 1 202  ? 34.216 55.625  6.091   1.00 9.38  ? 202  ALA A C   1 
ATOM   1439 O  O   . ALA A 1 202  ? 33.236 55.197  5.500   1.00 8.77  ? 202  ALA A O   1 
ATOM   1440 C  CB  . ALA A 1 202  ? 35.738 55.010  4.136   1.00 8.68  ? 202  ALA A CB  1 
ATOM   1441 N  N   . ILE A 1 203  ? 34.114 56.454  7.126   1.00 9.89  ? 203  ILE A N   1 
ATOM   1442 C  CA  . ILE A 1 203  ? 32.815 56.780  7.664   1.00 9.26  ? 203  ILE A CA  1 
ATOM   1443 C  C   . ILE A 1 203  ? 32.190 58.088  7.274   1.00 10.07 ? 203  ILE A C   1 
ATOM   1444 O  O   . ILE A 1 203  ? 31.032 58.302  7.619   1.00 7.85  ? 203  ILE A O   1 
ATOM   1445 C  CB  . ILE A 1 203  ? 32.838 56.679  9.219   1.00 9.84  ? 203  ILE A CB  1 
ATOM   1446 C  CG1 . ILE A 1 203  ? 33.913 57.613  9.790   1.00 10.36 ? 203  ILE A CG1 1 
ATOM   1447 C  CG2 . ILE A 1 203  ? 33.121 55.196  9.634   1.00 9.47  ? 203  ILE A CG2 1 
ATOM   1448 C  CD1 . ILE A 1 203  ? 33.823 57.856  11.319  1.00 10.15 ? 203  ILE A CD1 1 
ATOM   1449 N  N   . ASP A 1 204  ? 32.921 58.971  6.581   1.00 9.60  ? 204  ASP A N   1 
ATOM   1450 C  CA  . ASP A 1 204  ? 32.315 60.257  6.222   1.00 10.45 ? 204  ASP A CA  1 
ATOM   1451 C  C   . ASP A 1 204  ? 32.210 60.671  4.750   1.00 10.42 ? 204  ASP A C   1 
ATOM   1452 O  O   . ASP A 1 204  ? 31.538 61.664  4.453   1.00 11.41 ? 204  ASP A O   1 
ATOM   1453 C  CB  . ASP A 1 204  ? 32.957 61.399  7.020   1.00 10.92 ? 204  ASP A CB  1 
ATOM   1454 C  CG  . ASP A 1 204  ? 31.933 62.494  7.410   1.00 12.99 ? 204  ASP A CG  1 
ATOM   1455 O  OD1 . ASP A 1 204  ? 32.344 63.663  7.603   1.00 11.89 ? 204  ASP A OD1 1 
ATOM   1456 O  OD2 . ASP A 1 204  ? 30.721 62.174  7.548   1.00 10.38 ? 204  ASP A OD2 1 
ATOM   1457 N  N   . PRO A 1 205  ? 32.899 59.976  3.809   1.00 11.29 ? 205  PRO A N   1 
ATOM   1458 C  CA  . PRO A 1 205  ? 32.758 60.382  2.387   1.00 10.22 ? 205  PRO A CA  1 
ATOM   1459 C  C   . PRO A 1 205  ? 31.261 60.290  2.046   1.00 10.66 ? 205  PRO A C   1 
ATOM   1460 O  O   . PRO A 1 205  ? 30.552 59.433  2.585   1.00 9.84  ? 205  PRO A O   1 
ATOM   1461 C  CB  . PRO A 1 205  ? 33.554 59.314  1.637   1.00 11.09 ? 205  PRO A CB  1 
ATOM   1462 C  CG  . PRO A 1 205  ? 34.609 58.939  2.624   1.00 13.55 ? 205  PRO A CG  1 
ATOM   1463 C  CD  . PRO A 1 205  ? 33.836 58.846  3.927   1.00 11.32 ? 205  PRO A CD  1 
ATOM   1464 N  N   . PHE A 1 206  ? 30.796 61.141  1.127   1.00 10.70 ? 206  PHE A N   1 
ATOM   1465 C  CA  . PHE A 1 206  ? 29.382 61.245  0.761   1.00 9.57  ? 206  PHE A CA  1 
ATOM   1466 C  C   . PHE A 1 206  ? 29.020 60.270  -0.381  1.00 10.82 ? 206  PHE A C   1 
ATOM   1467 O  O   . PHE A 1 206  ? 28.865 60.675  -1.526  1.00 10.44 ? 206  PHE A O   1 
ATOM   1468 C  CB  . PHE A 1 206  ? 29.126 62.707  0.363   1.00 10.72 ? 206  PHE A CB  1 
ATOM   1469 C  CG  . PHE A 1 206  ? 29.982 63.716  1.143   1.00 12.14 ? 206  PHE A CG  1 
ATOM   1470 C  CD1 . PHE A 1 206  ? 30.298 63.502  2.501   1.00 11.13 ? 206  PHE A CD1 1 
ATOM   1471 C  CD2 . PHE A 1 206  ? 30.492 64.866  0.508   1.00 12.74 ? 206  PHE A CD2 1 
ATOM   1472 C  CE1 . PHE A 1 206  ? 31.119 64.409  3.214   1.00 12.98 ? 206  PHE A CE1 1 
ATOM   1473 C  CE2 . PHE A 1 206  ? 31.316 65.780  1.217   1.00 12.19 ? 206  PHE A CE2 1 
ATOM   1474 C  CZ  . PHE A 1 206  ? 31.630 65.548  2.565   1.00 11.88 ? 206  PHE A CZ  1 
ATOM   1475 N  N   . GLY A 1 207  ? 28.864 58.989  -0.050  1.00 10.48 ? 207  GLY A N   1 
ATOM   1476 C  CA  . GLY A 1 207  ? 28.633 57.987  -1.072  1.00 9.26  ? 207  GLY A CA  1 
ATOM   1477 C  C   . GLY A 1 207  ? 29.993 57.298  -1.240  1.00 9.01  ? 207  GLY A C   1 
ATOM   1478 O  O   . GLY A 1 207  ? 31.040 57.870  -0.951  1.00 8.54  ? 207  GLY A O   1 
ATOM   1479 N  N   . HIS A 1 208  ? 29.986 56.075  -1.751  1.00 8.65  ? 208  HIS A N   1 
ATOM   1480 C  CA  . HIS A 1 208  ? 31.203 55.284  -1.877  1.00 8.59  ? 208  HIS A CA  1 
ATOM   1481 C  C   . HIS A 1 208  ? 31.405 54.696  -3.261  1.00 8.33  ? 208  HIS A C   1 
ATOM   1482 O  O   . HIS A 1 208  ? 30.435 54.368  -3.962  1.00 7.70  ? 208  HIS A O   1 
ATOM   1483 C  CB  . HIS A 1 208  ? 31.134 54.165  -0.840  1.00 9.27  ? 208  HIS A CB  1 
ATOM   1484 C  CG  . HIS A 1 208  ? 31.244 54.655  0.571   1.00 10.23 ? 208  HIS A CG  1 
ATOM   1485 N  ND1 . HIS A 1 208  ? 32.462 54.919  1.167   1.00 9.21  ? 208  HIS A ND1 1 
ATOM   1486 C  CD2 . HIS A 1 208  ? 30.295 54.957  1.493   1.00 10.55 ? 208  HIS A CD2 1 
ATOM   1487 C  CE1 . HIS A 1 208  ? 32.255 55.364  2.396   1.00 9.86  ? 208  HIS A CE1 1 
ATOM   1488 N  NE2 . HIS A 1 208  ? 30.952 55.394  2.618   1.00 9.44  ? 208  HIS A NE2 1 
ATOM   1489 N  N   . SER A 1 209  ? 32.670 54.562  -3.636  1.00 7.10  ? 209  SER A N   1 
ATOM   1490 C  CA  . SER A 1 209  ? 33.062 54.052  -4.946  1.00 7.36  ? 209  SER A CA  1 
ATOM   1491 C  C   . SER A 1 209  ? 33.794 52.725  -4.843  1.00 6.96  ? 209  SER A C   1 
ATOM   1492 O  O   . SER A 1 209  ? 34.570 52.540  -3.904  1.00 6.37  ? 209  SER A O   1 
ATOM   1493 C  CB  . SER A 1 209  ? 34.021 55.041  -5.591  1.00 6.08  ? 209  SER A CB  1 
ATOM   1494 O  OG  . SER A 1 209  ? 34.605 54.451  -6.741  1.00 9.29  ? 209  SER A OG  1 
ATOM   1495 N  N   . PRO A 1 210  ? 33.576 51.804  -5.820  1.00 6.71  ? 210  PRO A N   1 
ATOM   1496 C  CA  . PRO A 1 210  ? 34.229 50.487  -5.845  1.00 6.36  ? 210  PRO A CA  1 
ATOM   1497 C  C   . PRO A 1 210  ? 35.699 50.674  -6.205  1.00 7.86  ? 210  PRO A C   1 
ATOM   1498 O  O   . PRO A 1 210  ? 36.465 49.727  -6.162  1.00 7.74  ? 210  PRO A O   1 
ATOM   1499 C  CB  . PRO A 1 210  ? 33.466 49.706  -6.924  1.00 6.15  ? 210  PRO A CB  1 
ATOM   1500 C  CG  . PRO A 1 210  ? 32.951 50.763  -7.835  1.00 4.46  ? 210  PRO A CG  1 
ATOM   1501 C  CD  . PRO A 1 210  ? 32.568 51.906  -6.895  1.00 5.12  ? 210  PRO A CD  1 
ATOM   1502 N  N   . THR A 1 211  ? 36.092 51.891  -6.570  1.00 7.53  ? 211  THR A N   1 
ATOM   1503 C  CA  . THR A 1 211  ? 37.518 52.111  -6.822  1.00 8.93  ? 211  THR A CA  1 
ATOM   1504 C  C   . THR A 1 211  ? 38.315 51.861  -5.502  1.00 7.76  ? 211  THR A C   1 
ATOM   1505 O  O   . THR A 1 211  ? 39.500 51.461  -5.539  1.00 8.14  ? 211  THR A O   1 
ATOM   1506 C  CB  . THR A 1 211  ? 37.802 53.580  -7.319  1.00 9.37  ? 211  THR A CB  1 
ATOM   1507 O  OG1 . THR A 1 211  ? 37.202 53.764  -8.613  1.00 9.22  ? 211  THR A OG1 1 
ATOM   1508 C  CG2 . THR A 1 211  ? 39.328 53.835  -7.443  1.00 7.13  ? 211  THR A CG2 1 
ATOM   1509 N  N   . MET A 1 212  ? 37.674 52.072  -4.345  1.00 6.86  ? 212  MET A N   1 
ATOM   1510 C  CA  . MET A 1 212  ? 38.360 51.874  -3.056  1.00 7.17  ? 212  MET A CA  1 
ATOM   1511 C  C   . MET A 1 212  ? 38.716 50.397  -2.857  1.00 7.03  ? 212  MET A C   1 
ATOM   1512 O  O   . MET A 1 212  ? 39.885 50.084  -2.673  1.00 6.76  ? 212  MET A O   1 
ATOM   1513 C  CB  . MET A 1 212  ? 37.534 52.413  -1.883  1.00 8.18  ? 212  MET A CB  1 
ATOM   1514 C  CG  . MET A 1 212  ? 37.194 53.892  -2.010  1.00 11.08 ? 212  MET A CG  1 
ATOM   1515 S  SD  . MET A 1 212  ? 38.681 54.960  -2.303  1.00 14.23 ? 212  MET A SD  1 
ATOM   1516 C  CE  . MET A 1 212  ? 39.523 54.796  -0.696  1.00 10.64 ? 212  MET A CE  1 
ATOM   1517 N  N   . PRO A 1 213  ? 37.738 49.472  -2.878  1.00 8.02  ? 213  PRO A N   1 
ATOM   1518 C  CA  . PRO A 1 213  ? 38.177 48.081  -2.710  1.00 7.43  ? 213  PRO A CA  1 
ATOM   1519 C  C   . PRO A 1 213  ? 39.152 47.669  -3.831  1.00 8.81  ? 213  PRO A C   1 
ATOM   1520 O  O   . PRO A 1 213  ? 40.017 46.803  -3.638  1.00 8.23  ? 213  PRO A O   1 
ATOM   1521 C  CB  . PRO A 1 213  ? 36.872 47.287  -2.762  1.00 7.51  ? 213  PRO A CB  1 
ATOM   1522 C  CG  . PRO A 1 213  ? 35.917 48.224  -3.518  1.00 8.37  ? 213  PRO A CG  1 
ATOM   1523 C  CD  . PRO A 1 213  ? 36.261 49.538  -2.849  1.00 8.86  ? 213  PRO A CD  1 
ATOM   1524 N  N   . TYR A 1 214  ? 39.005 48.251  -5.022  1.00 8.68  ? 214  TYR A N   1 
ATOM   1525 C  CA  . TYR A 1 214  ? 39.921 47.905  -6.119  1.00 7.58  ? 214  TYR A CA  1 
ATOM   1526 C  C   . TYR A 1 214  ? 41.385 48.143  -5.711  1.00 8.53  ? 214  TYR A C   1 
ATOM   1527 O  O   . TYR A 1 214  ? 42.245 47.242  -5.823  1.00 7.70  ? 214  TYR A O   1 
ATOM   1528 C  CB  . TYR A 1 214  ? 39.646 48.742  -7.349  1.00 8.99  ? 214  TYR A CB  1 
ATOM   1529 C  CG  . TYR A 1 214  ? 40.588 48.439  -8.510  1.00 11.36 ? 214  TYR A CG  1 
ATOM   1530 C  CD1 . TYR A 1 214  ? 40.350 47.360  -9.367  1.00 12.25 ? 214  TYR A CD1 1 
ATOM   1531 C  CD2 . TYR A 1 214  ? 41.668 49.278  -8.799  1.00 10.40 ? 214  TYR A CD2 1 
ATOM   1532 C  CE1 . TYR A 1 214  ? 41.159 47.151  -10.501 1.00 14.27 ? 214  TYR A CE1 1 
ATOM   1533 C  CE2 . TYR A 1 214  ? 42.472 49.077  -9.913  1.00 10.73 ? 214  TYR A CE2 1 
ATOM   1534 C  CZ  . TYR A 1 214  ? 42.219 48.023  -10.772 1.00 13.64 ? 214  TYR A CZ  1 
ATOM   1535 O  OH  . TYR A 1 214  ? 43.007 47.850  -11.919 1.00 12.19 ? 214  TYR A OH  1 
ATOM   1536 N  N   . ILE A 1 215  ? 41.667 49.370  -5.268  1.00 7.83  ? 215  ILE A N   1 
ATOM   1537 C  CA  . ILE A 1 215  ? 43.008 49.769  -4.836  1.00 7.54  ? 215  ILE A CA  1 
ATOM   1538 C  C   . ILE A 1 215  ? 43.415 49.050  -3.532  1.00 7.90  ? 215  ILE A C   1 
ATOM   1539 O  O   . ILE A 1 215  ? 44.539 48.548  -3.387  1.00 6.89  ? 215  ILE A O   1 
ATOM   1540 C  CB  . ILE A 1 215  ? 43.062 51.336  -4.608  1.00 8.78  ? 215  ILE A CB  1 
ATOM   1541 C  CG1 . ILE A 1 215  ? 42.801 52.054  -5.935  1.00 7.96  ? 215  ILE A CG1 1 
ATOM   1542 C  CG2 . ILE A 1 215  ? 44.436 51.758  -3.995  1.00 8.24  ? 215  ILE A CG2 1 
ATOM   1543 C  CD1 . ILE A 1 215  ? 42.831 53.555  -5.843  1.00 11.46 ? 215  ILE A CD1 1 
ATOM   1544 N  N   . LEU A 1 216  ? 42.488 48.973  -2.590  1.00 6.40  ? 216  LEU A N   1 
ATOM   1545 C  CA  . LEU A 1 216  ? 42.810 48.355  -1.308  1.00 7.88  ? 216  LEU A CA  1 
ATOM   1546 C  C   . LEU A 1 216  ? 43.158 46.871  -1.452  1.00 8.86  ? 216  LEU A C   1 
ATOM   1547 O  O   . LEU A 1 216  ? 44.133 46.392  -0.852  1.00 9.70  ? 216  LEU A O   1 
ATOM   1548 C  CB  . LEU A 1 216  ? 41.622 48.523  -0.338  1.00 6.31  ? 216  LEU A CB  1 
ATOM   1549 C  CG  . LEU A 1 216  ? 41.265 50.000  0.024   1.00 7.79  ? 216  LEU A CG  1 
ATOM   1550 C  CD1 . LEU A 1 216  ? 39.960 50.001  0.858   1.00 5.12  ? 216  LEU A CD1 1 
ATOM   1551 C  CD2 . LEU A 1 216  ? 42.433 50.693  0.839   1.00 4.19  ? 216  LEU A CD2 1 
ATOM   1552 N  N   . GLN A 1 217  ? 42.370 46.146  -2.233  1.00 8.14  ? 217  GLN A N   1 
ATOM   1553 C  CA  . GLN A 1 217  ? 42.625 44.719  -2.384  1.00 9.33  ? 217  GLN A CA  1 
ATOM   1554 C  C   . GLN A 1 217  ? 43.980 44.489  -3.053  1.00 10.08 ? 217  GLN A C   1 
ATOM   1555 O  O   . GLN A 1 217  ? 44.624 43.451  -2.829  1.00 9.98  ? 217  GLN A O   1 
ATOM   1556 C  CB  . GLN A 1 217  ? 41.456 44.081  -3.157  1.00 10.14 ? 217  GLN A CB  1 
ATOM   1557 C  CG  . GLN A 1 217  ? 41.452 42.532  -3.244  1.00 14.09 ? 217  GLN A CG  1 
ATOM   1558 C  CD  . GLN A 1 217  ? 42.247 42.034  -4.418  1.00 14.92 ? 217  GLN A CD  1 
ATOM   1559 O  OE1 . GLN A 1 217  ? 42.319 42.711  -5.436  1.00 16.97 ? 217  GLN A OE1 1 
ATOM   1560 N  NE2 . GLN A 1 217  ? 42.848 40.853  -4.294  1.00 15.82 ? 217  GLN A NE2 1 
ATOM   1561 N  N   . LYS A 1 218  ? 44.446 45.465  -3.846  1.00 9.16  ? 218  LYS A N   1 
ATOM   1562 C  CA  . LYS A 1 218  ? 45.750 45.337  -4.536  1.00 9.25  ? 218  LYS A CA  1 
ATOM   1563 C  C   . LYS A 1 218  ? 46.876 45.985  -3.693  1.00 9.77  ? 218  LYS A C   1 
ATOM   1564 O  O   . LYS A 1 218  ? 48.019 46.169  -4.159  1.00 9.11  ? 218  LYS A O   1 
ATOM   1565 C  CB  . LYS A 1 218  ? 45.681 46.023  -5.910  1.00 8.69  ? 218  LYS A CB  1 
ATOM   1566 C  CG  . LYS A 1 218  ? 44.818 45.249  -6.975  1.00 11.27 ? 218  LYS A CG  1 
ATOM   1567 C  CD  . LYS A 1 218  ? 44.660 46.108  -8.269  1.00 10.82 ? 218  LYS A CD  1 
ATOM   1568 C  CE  . LYS A 1 218  ? 44.175 45.304  -9.454  1.00 12.12 ? 218  LYS A CE  1 
ATOM   1569 N  NZ  . LYS A 1 218  ? 43.109 44.296  -9.174  1.00 11.62 ? 218  LYS A NZ  1 
ATOM   1570 N  N   . SER A 1 219  ? 46.515 46.338  -2.458  1.00 8.72  ? 219  SER A N   1 
ATOM   1571 C  CA  . SER A 1 219  ? 47.420 46.957  -1.514  1.00 8.80  ? 219  SER A CA  1 
ATOM   1572 C  C   . SER A 1 219  ? 47.441 46.176  -0.194  1.00 9.29  ? 219  SER A C   1 
ATOM   1573 O  O   . SER A 1 219  ? 47.763 46.709  0.874   1.00 7.74  ? 219  SER A O   1 
ATOM   1574 C  CB  . SER A 1 219  ? 47.011 48.414  -1.280  1.00 8.74  ? 219  SER A CB  1 
ATOM   1575 O  OG  . SER A 1 219  ? 47.157 49.168  -2.470  1.00 8.39  ? 219  SER A OG  1 
ATOM   1576 N  N   . GLY A 1 220  ? 47.096 44.893  -0.283  1.00 9.12  ? 220  GLY A N   1 
ATOM   1577 C  CA  . GLY A 1 220  ? 47.142 44.032  0.885   1.00 7.91  ? 220  GLY A CA  1 
ATOM   1578 C  C   . GLY A 1 220  ? 45.937 44.000  1.804   1.00 9.53  ? 220  GLY A C   1 
ATOM   1579 O  O   . GLY A 1 220  ? 45.942 43.219  2.746   1.00 9.26  ? 220  GLY A O   1 
ATOM   1580 N  N   . PHE A 1 221  ? 44.902 44.792  1.541   1.00 8.35  ? 221  PHE A N   1 
ATOM   1581 C  CA  . PHE A 1 221  ? 43.773 44.819  2.462   1.00 9.40  ? 221  PHE A CA  1 
ATOM   1582 C  C   . PHE A 1 221  ? 42.938 43.572  2.404   1.00 9.22  ? 221  PHE A C   1 
ATOM   1583 O  O   . PHE A 1 221  ? 42.876 42.925  1.375   1.00 9.05  ? 221  PHE A O   1 
ATOM   1584 C  CB  . PHE A 1 221  ? 42.887 46.048  2.206   1.00 7.80  ? 221  PHE A CB  1 
ATOM   1585 C  CG  . PHE A 1 221  ? 43.465 47.328  2.758   1.00 8.92  ? 221  PHE A CG  1 
ATOM   1586 C  CD1 . PHE A 1 221  ? 44.572 47.932  2.158   1.00 7.50  ? 221  PHE A CD1 1 
ATOM   1587 C  CD2 . PHE A 1 221  ? 42.911 47.923  3.882   1.00 8.21  ? 221  PHE A CD2 1 
ATOM   1588 C  CE1 . PHE A 1 221  ? 45.113 49.115  2.688   1.00 9.48  ? 221  PHE A CE1 1 
ATOM   1589 C  CE2 . PHE A 1 221  ? 43.449 49.100  4.409   1.00 8.28  ? 221  PHE A CE2 1 
ATOM   1590 C  CZ  . PHE A 1 221  ? 44.544 49.699  3.825   1.00 7.55  ? 221  PHE A CZ  1 
ATOM   1591 N  N   . LYS A 1 222  ? 42.304 43.249  3.526   1.00 10.62 ? 222  LYS A N   1 
ATOM   1592 C  CA  . LYS A 1 222  ? 41.443 42.086  3.654   1.00 11.94 ? 222  LYS A CA  1 
ATOM   1593 C  C   . LYS A 1 222  ? 40.012 42.474  4.013   1.00 11.92 ? 222  LYS A C   1 
ATOM   1594 O  O   . LYS A 1 222  ? 39.089 41.676  3.853   1.00 11.90 ? 222  LYS A O   1 
ATOM   1595 C  CB  . LYS A 1 222  ? 42.012 41.161  4.728   1.00 15.68 ? 222  LYS A CB  1 
ATOM   1596 C  CG  . LYS A 1 222  ? 43.042 40.147  4.216   1.00 20.07 ? 222  LYS A CG  1 
ATOM   1597 C  CD  . LYS A 1 222  ? 43.799 40.610  2.976   1.00 26.35 ? 222  LYS A CD  1 
ATOM   1598 C  CE  . LYS A 1 222  ? 44.649 39.492  2.342   1.00 28.72 ? 222  LYS A CE  1 
ATOM   1599 N  NZ  . LYS A 1 222  ? 45.422 38.768  3.376   1.00 31.73 ? 222  LYS A NZ  1 
ATOM   1600 N  N   . ASN A 1 223  ? 39.822 43.700  4.497   1.00 10.31 ? 223  ASN A N   1 
ATOM   1601 C  CA  . ASN A 1 223  ? 38.502 44.148  4.904   1.00 9.97  ? 223  ASN A CA  1 
ATOM   1602 C  C   . ASN A 1 223  ? 38.329 45.669  4.782   1.00 9.13  ? 223  ASN A C   1 
ATOM   1603 O  O   . ASN A 1 223  ? 39.310 46.403  4.850   1.00 8.37  ? 223  ASN A O   1 
ATOM   1604 C  CB  . ASN A 1 223  ? 38.257 43.786  6.385   1.00 9.28  ? 223  ASN A CB  1 
ATOM   1605 C  CG  . ASN A 1 223  ? 38.344 42.302  6.652   1.00 12.11 ? 223  ASN A CG  1 
ATOM   1606 O  OD1 . ASN A 1 223  ? 39.390 41.785  7.112   1.00 14.20 ? 223  ASN A OD1 1 
ATOM   1607 N  ND2 . ASN A 1 223  ? 37.265 41.600  6.359   1.00 7.77  ? 223  ASN A ND2 1 
ATOM   1608 N  N   . MET A 1 224  ? 37.079 46.123  4.661   1.00 9.06  ? 224  MET A N   1 
ATOM   1609 C  CA  . MET A 1 224  ? 36.774 47.569  4.615   1.00 9.32  ? 224  MET A CA  1 
ATOM   1610 C  C   . MET A 1 224  ? 35.367 47.826  5.165   1.00 10.24 ? 224  MET A C   1 
ATOM   1611 O  O   . MET A 1 224  ? 34.515 46.932  5.164   1.00 9.48  ? 224  MET A O   1 
ATOM   1612 C  CB  . MET A 1 224  ? 36.861 48.144  3.198   1.00 9.78  ? 224  MET A CB  1 
ATOM   1613 C  CG  . MET A 1 224  ? 35.852 47.583  2.227   1.00 9.50  ? 224  MET A CG  1 
ATOM   1614 S  SD  . MET A 1 224  ? 36.040 48.400  0.621   1.00 11.50 ? 224  MET A SD  1 
ATOM   1615 C  CE  . MET A 1 224  ? 35.514 49.997  0.995   1.00 10.02 ? 224  MET A CE  1 
ATOM   1616 N  N   . LEU A 1 225  ? 35.165 49.053  5.645   1.00 7.92  ? 225  LEU A N   1 
ATOM   1617 C  CA  . LEU A 1 225  ? 33.924 49.474  6.236   1.00 7.79  ? 225  LEU A CA  1 
ATOM   1618 C  C   . LEU A 1 225  ? 33.511 50.801  5.628   1.00 8.26  ? 225  LEU A C   1 
ATOM   1619 O  O   . LEU A 1 225  ? 34.347 51.675  5.437   1.00 9.27  ? 225  LEU A O   1 
ATOM   1620 C  CB  . LEU A 1 225  ? 34.099 49.617  7.752   1.00 6.79  ? 225  LEU A CB  1 
ATOM   1621 C  CG  . LEU A 1 225  ? 32.873 50.198  8.480   1.00 8.10  ? 225  LEU A CG  1 
ATOM   1622 C  CD1 . LEU A 1 225  ? 32.751 49.569  9.891   1.00 6.55  ? 225  LEU A CD1 1 
ATOM   1623 C  CD2 . LEU A 1 225  ? 32.997 51.756  8.554   1.00 7.04  ? 225  LEU A CD2 1 
ATOM   1624 N  N   . ILE A 1 226  ? 32.224 50.929  5.310   1.00 9.40  ? 226  ILE A N   1 
ATOM   1625 C  CA  . ILE A 1 226  ? 31.678 52.156  4.717   1.00 10.15 ? 226  ILE A CA  1 
ATOM   1626 C  C   . ILE A 1 226  ? 30.420 52.577  5.489   1.00 10.70 ? 226  ILE A C   1 
ATOM   1627 O  O   . ILE A 1 226  ? 29.815 51.761  6.197   1.00 11.25 ? 226  ILE A O   1 
ATOM   1628 C  CB  . ILE A 1 226  ? 31.362 51.959  3.199   1.00 10.88 ? 226  ILE A CB  1 
ATOM   1629 C  CG1 . ILE A 1 226  ? 30.303 50.877  2.993   1.00 11.71 ? 226  ILE A CG1 1 
ATOM   1630 C  CG2 . ILE A 1 226  ? 32.659 51.555  2.428   1.00 10.58 ? 226  ILE A CG2 1 
ATOM   1631 C  CD1 . ILE A 1 226  ? 29.876 50.741  1.506   1.00 10.70 ? 226  ILE A CD1 1 
ATOM   1632 N  N   . GLN A 1 227  ? 30.039 53.842  5.386   1.00 9.52  ? 227  GLN A N   1 
ATOM   1633 C  CA  . GLN A 1 227  ? 28.884 54.308  6.130   1.00 9.73  ? 227  GLN A CA  1 
ATOM   1634 C  C   . GLN A 1 227  ? 27.871 55.154  5.358   1.00 10.67 ? 227  GLN A C   1 
ATOM   1635 O  O   . GLN A 1 227  ? 26.680 54.818  5.367   1.00 9.26  ? 227  GLN A O   1 
ATOM   1636 C  CB  . GLN A 1 227  ? 29.355 55.073  7.373   1.00 9.30  ? 227  GLN A CB  1 
ATOM   1637 C  CG  . GLN A 1 227  ? 28.421 56.231  7.838   1.00 10.99 ? 227  GLN A CG  1 
ATOM   1638 C  CD  . GLN A 1 227  ? 27.035 55.752  8.345   1.00 10.93 ? 227  GLN A CD  1 
ATOM   1639 O  OE1 . GLN A 1 227  ? 26.831 54.564  8.633   1.00 9.57  ? 227  GLN A OE1 1 
ATOM   1640 N  NE2 . GLN A 1 227  ? 26.097 56.686  8.472   1.00 10.31 ? 227  GLN A NE2 1 
ATOM   1641 N  N   . ARG A 1 228  ? 28.306 56.217  4.666   1.00 8.27  ? 228  ARG A N   1 
ATOM   1642 C  CA  . ARG A 1 228  ? 27.310 57.051  3.995   1.00 9.16  ? 228  ARG A CA  1 
ATOM   1643 C  C   . ARG A 1 228  ? 26.754 56.500  2.689   1.00 9.22  ? 228  ARG A C   1 
ATOM   1644 O  O   . ARG A 1 228  ? 27.308 56.740  1.623   1.00 8.40  ? 228  ARG A O   1 
ATOM   1645 C  CB  . ARG A 1 228  ? 27.856 58.470  3.758   1.00 8.31  ? 228  ARG A CB  1 
ATOM   1646 C  CG  . ARG A 1 228  ? 28.032 59.295  5.025   1.00 9.63  ? 228  ARG A CG  1 
ATOM   1647 C  CD  . ARG A 1 228  ? 28.373 60.759  4.634   1.00 11.55 ? 228  ARG A CD  1 
ATOM   1648 N  NE  . ARG A 1 228  ? 28.568 61.684  5.760   1.00 11.87 ? 228  ARG A NE  1 
ATOM   1649 C  CZ  . ARG A 1 228  ? 27.591 62.308  6.421   1.00 13.62 ? 228  ARG A CZ  1 
ATOM   1650 N  NH1 . ARG A 1 228  ? 26.306 62.106  6.107   1.00 13.15 ? 228  ARG A NH1 1 
ATOM   1651 N  NH2 . ARG A 1 228  ? 27.910 63.196  7.351   1.00 11.39 ? 228  ARG A NH2 1 
ATOM   1652 N  N   . THR A 1 229  ? 25.686 55.721  2.781   1.00 9.91  ? 229  THR A N   1 
ATOM   1653 C  CA  . THR A 1 229  ? 25.040 55.165  1.596   1.00 9.54  ? 229  THR A CA  1 
ATOM   1654 C  C   . THR A 1 229  ? 23.564 55.539  1.742   1.00 9.81  ? 229  THR A C   1 
ATOM   1655 O  O   . THR A 1 229  ? 23.073 55.795  2.866   1.00 11.81 ? 229  THR A O   1 
ATOM   1656 C  CB  . THR A 1 229  ? 25.225 53.609  1.503   1.00 11.46 ? 229  THR A CB  1 
ATOM   1657 O  OG1 . THR A 1 229  ? 24.558 52.952  2.600   1.00 11.71 ? 229  THR A OG1 1 
ATOM   1658 C  CG2 . THR A 1 229  ? 26.705 53.265  1.550   1.00 9.89  ? 229  THR A CG2 1 
ATOM   1659 N  N   . HIS A 1 230  ? 22.853 55.578  0.617   1.00 9.19  ? 230  HIS A N   1 
ATOM   1660 C  CA  . HIS A 1 230  ? 21.443 55.992  0.582   1.00 9.04  ? 230  HIS A CA  1 
ATOM   1661 C  C   . HIS A 1 230  ? 20.578 55.275  1.627   1.00 9.15  ? 230  HIS A C   1 
ATOM   1662 O  O   . HIS A 1 230  ? 20.675 54.069  1.751   1.00 9.06  ? 230  HIS A O   1 
ATOM   1663 C  CB  . HIS A 1 230  ? 20.906 55.739  -0.837  1.00 10.57 ? 230  HIS A CB  1 
ATOM   1664 C  CG  . HIS A 1 230  ? 19.618 56.448  -1.141  1.00 11.37 ? 230  HIS A CG  1 
ATOM   1665 N  ND1 . HIS A 1 230  ? 18.443 56.185  -0.466  1.00 10.99 ? 230  HIS A ND1 1 
ATOM   1666 C  CD2 . HIS A 1 230  ? 19.325 57.410  -2.054  1.00 11.84 ? 230  HIS A CD2 1 
ATOM   1667 C  CE1 . HIS A 1 230  ? 17.481 56.958  -0.945  1.00 11.36 ? 230  HIS A CE1 1 
ATOM   1668 N  NE2 . HIS A 1 230  ? 17.988 57.710  -1.913  1.00 11.02 ? 230  HIS A NE2 1 
ATOM   1669 N  N   . TYR A 1 231  ? 19.751 56.004  2.387   1.00 9.58  ? 231  TYR A N   1 
ATOM   1670 C  CA  . TYR A 1 231  ? 18.928 55.353  3.406   1.00 11.04 ? 231  TYR A CA  1 
ATOM   1671 C  C   . TYR A 1 231  ? 18.069 54.215  2.869   1.00 11.79 ? 231  TYR A C   1 
ATOM   1672 O  O   . TYR A 1 231  ? 17.799 53.267  3.599   1.00 13.60 ? 231  TYR A O   1 
ATOM   1673 C  CB  . TYR A 1 231  ? 18.040 56.352  4.172   1.00 11.27 ? 231  TYR A CB  1 
ATOM   1674 C  CG  . TYR A 1 231  ? 17.089 57.153  3.302   1.00 13.76 ? 231  TYR A CG  1 
ATOM   1675 C  CD1 . TYR A 1 231  ? 15.793 56.697  3.045   1.00 12.59 ? 231  TYR A CD1 1 
ATOM   1676 C  CD2 . TYR A 1 231  ? 17.492 58.381  2.739   1.00 13.51 ? 231  TYR A CD2 1 
ATOM   1677 C  CE1 . TYR A 1 231  ? 14.922 57.442  2.252   1.00 14.47 ? 231  TYR A CE1 1 
ATOM   1678 C  CE2 . TYR A 1 231  ? 16.617 59.135  1.943   1.00 13.59 ? 231  TYR A CE2 1 
ATOM   1679 C  CZ  . TYR A 1 231  ? 15.337 58.656  1.704   1.00 14.18 ? 231  TYR A CZ  1 
ATOM   1680 O  OH  . TYR A 1 231  ? 14.466 59.380  0.905   1.00 14.66 ? 231  TYR A OH  1 
ATOM   1681 N  N   . SER A 1 232  ? 17.633 54.299  1.611   1.00 12.14 ? 232  SER A N   1 
ATOM   1682 C  CA  . SER A 1 232  ? 16.823 53.222  1.036   1.00 12.31 ? 232  SER A CA  1 
ATOM   1683 C  C   . SER A 1 232  ? 17.668 51.976  0.827   1.00 11.94 ? 232  SER A C   1 
ATOM   1684 O  O   . SER A 1 232  ? 17.169 50.864  1.001   1.00 11.16 ? 232  SER A O   1 
ATOM   1685 C  CB  . SER A 1 232  ? 16.228 53.645  -0.312  1.00 12.60 ? 232  SER A CB  1 
ATOM   1686 O  OG  . SER A 1 232  ? 15.295 54.690  -0.116  1.00 15.79 ? 232  SER A OG  1 
ATOM   1687 N  N   . VAL A 1 233  ? 18.938 52.167  0.436   1.00 10.04 ? 233  VAL A N   1 
ATOM   1688 C  CA  . VAL A 1 233  ? 19.846 51.055  0.224   1.00 9.77  ? 233  VAL A CA  1 
ATOM   1689 C  C   . VAL A 1 233  ? 20.129 50.339  1.563   1.00 10.82 ? 233  VAL A C   1 
ATOM   1690 O  O   . VAL A 1 233  ? 20.094 49.108  1.652   1.00 10.09 ? 233  VAL A O   1 
ATOM   1691 C  CB  . VAL A 1 233  ? 21.173 51.529  -0.438  1.00 9.03  ? 233  VAL A CB  1 
ATOM   1692 C  CG1 . VAL A 1 233  ? 22.191 50.365  -0.457  1.00 7.77  ? 233  VAL A CG1 1 
ATOM   1693 C  CG2 . VAL A 1 233  ? 20.903 51.971  -1.899  1.00 9.88  ? 233  VAL A CG2 1 
ATOM   1694 N  N   . LYS A 1 234  ? 20.397 51.113  2.602   1.00 10.88 ? 234  LYS A N   1 
ATOM   1695 C  CA  . LYS A 1 234  ? 20.614 50.547  3.924   1.00 11.54 ? 234  LYS A CA  1 
ATOM   1696 C  C   . LYS A 1 234  ? 19.405 49.669  4.306   1.00 12.63 ? 234  LYS A C   1 
ATOM   1697 O  O   . LYS A 1 234  ? 19.561 48.517  4.713   1.00 12.49 ? 234  LYS A O   1 
ATOM   1698 C  CB  . LYS A 1 234  ? 20.783 51.684  4.956   1.00 11.03 ? 234  LYS A CB  1 
ATOM   1699 C  CG  . LYS A 1 234  ? 22.167 52.394  4.869   1.00 12.49 ? 234  LYS A CG  1 
ATOM   1700 C  CD  . LYS A 1 234  ? 22.253 53.603  5.796   1.00 9.71  ? 234  LYS A CD  1 
ATOM   1701 C  CE  . LYS A 1 234  ? 23.664 54.250  5.716   1.00 11.71 ? 234  LYS A CE  1 
ATOM   1702 N  NZ  . LYS A 1 234  ? 24.625 53.677  6.736   1.00 11.73 ? 234  LYS A NZ  1 
ATOM   1703 N  N   . LYS A 1 235  ? 18.199 50.221  4.181   1.00 14.14 ? 235  LYS A N   1 
ATOM   1704 C  CA  . LYS A 1 235  ? 16.986 49.475  4.529   1.00 14.47 ? 235  LYS A CA  1 
ATOM   1705 C  C   . LYS A 1 235  ? 16.883 48.180  3.755   1.00 15.21 ? 235  LYS A C   1 
ATOM   1706 O  O   . LYS A 1 235  ? 16.685 47.107  4.330   1.00 15.13 ? 235  LYS A O   1 
ATOM   1707 C  CB  . LYS A 1 235  ? 15.752 50.321  4.261   1.00 15.95 ? 235  LYS A CB  1 
ATOM   1708 C  CG  . LYS A 1 235  ? 14.452 49.701  4.798   1.00 17.48 ? 235  LYS A CG  1 
ATOM   1709 C  CD  . LYS A 1 235  ? 13.295 50.601  4.483   1.00 17.12 ? 235  LYS A CD  1 
ATOM   1710 C  CE  . LYS A 1 235  ? 12.012 49.981  4.974   1.00 20.68 ? 235  LYS A CE  1 
ATOM   1711 N  NZ  . LYS A 1 235  ? 10.887 50.957  4.812   1.00 22.70 ? 235  LYS A NZ  1 
ATOM   1712 N  N   . GLU A 1 236  ? 17.031 48.277  2.440   1.00 15.63 ? 236  GLU A N   1 
ATOM   1713 C  CA  . GLU A 1 236  ? 16.957 47.108  1.569   1.00 15.57 ? 236  GLU A CA  1 
ATOM   1714 C  C   . GLU A 1 236  ? 17.986 46.015  1.931   1.00 15.43 ? 236  GLU A C   1 
ATOM   1715 O  O   . GLU A 1 236  ? 17.637 44.837  2.118   1.00 15.55 ? 236  GLU A O   1 
ATOM   1716 C  CB  . GLU A 1 236  ? 17.172 47.562  0.130   1.00 18.02 ? 236  GLU A CB  1 
ATOM   1717 C  CG  . GLU A 1 236  ? 16.947 46.487  -0.851  1.00 23.29 ? 236  GLU A CG  1 
ATOM   1718 C  CD  . GLU A 1 236  ? 15.465 46.134  -0.995  1.00 25.67 ? 236  GLU A CD  1 
ATOM   1719 O  OE1 . GLU A 1 236  ? 15.207 45.131  -1.678  1.00 28.62 ? 236  GLU A OE1 1 
ATOM   1720 O  OE2 . GLU A 1 236  ? 14.574 46.852  -0.450  1.00 27.12 ? 236  GLU A OE2 1 
ATOM   1721 N  N   . LEU A 1 237  ? 19.265 46.381  2.022   1.00 13.47 ? 237  LEU A N   1 
ATOM   1722 C  CA  . LEU A 1 237  ? 20.267 45.383  2.361   1.00 13.07 ? 237  LEU A CA  1 
ATOM   1723 C  C   . LEU A 1 237  ? 20.065 44.848  3.791   1.00 13.21 ? 237  LEU A C   1 
ATOM   1724 O  O   . LEU A 1 237  ? 20.326 43.670  4.080   1.00 13.53 ? 237  LEU A O   1 
ATOM   1725 C  CB  . LEU A 1 237  ? 21.665 45.975  2.220   1.00 10.38 ? 237  LEU A CB  1 
ATOM   1726 C  CG  . LEU A 1 237  ? 22.027 46.418  0.807   1.00 11.40 ? 237  LEU A CG  1 
ATOM   1727 C  CD1 . LEU A 1 237  ? 23.452 47.004  0.833   1.00 12.07 ? 237  LEU A CD1 1 
ATOM   1728 C  CD2 . LEU A 1 237  ? 21.995 45.227  -0.160  1.00 10.90 ? 237  LEU A CD2 1 
ATOM   1729 N  N   . ALA A 1 238  ? 19.617 45.710  4.691   1.00 12.73 ? 238  ALA A N   1 
ATOM   1730 C  CA  . ALA A 1 238  ? 19.373 45.262  6.056   1.00 14.28 ? 238  ALA A CA  1 
ATOM   1731 C  C   . ALA A 1 238  ? 18.336 44.133  6.083   1.00 16.17 ? 238  ALA A C   1 
ATOM   1732 O  O   . ALA A 1 238  ? 18.519 43.121  6.766   1.00 15.85 ? 238  ALA A O   1 
ATOM   1733 C  CB  . ALA A 1 238  ? 18.882 46.423  6.911   1.00 12.86 ? 238  ALA A CB  1 
ATOM   1734 N  N   . GLN A 1 239  ? 17.252 44.299  5.334   1.00 16.43 ? 239  GLN A N   1 
ATOM   1735 C  CA  . GLN A 1 239  ? 16.198 43.292  5.361   1.00 18.33 ? 239  GLN A CA  1 
ATOM   1736 C  C   . GLN A 1 239  ? 16.690 41.935  4.865   1.00 18.43 ? 239  GLN A C   1 
ATOM   1737 O  O   . GLN A 1 239  ? 16.177 40.914  5.271   1.00 18.57 ? 239  GLN A O   1 
ATOM   1738 C  CB  . GLN A 1 239  ? 14.992 43.770  4.542   1.00 18.70 ? 239  GLN A CB  1 
ATOM   1739 C  CG  . GLN A 1 239  ? 14.335 45.003  5.159   1.00 22.93 ? 239  GLN A CG  1 
ATOM   1740 C  CD  . GLN A 1 239  ? 13.284 45.669  4.261   1.00 26.45 ? 239  GLN A CD  1 
ATOM   1741 O  OE1 . GLN A 1 239  ? 13.457 45.771  3.043   1.00 28.27 ? 239  GLN A OE1 1 
ATOM   1742 N  NE2 . GLN A 1 239  ? 12.206 46.157  4.871   1.00 27.99 ? 239  GLN A NE2 1 
ATOM   1743 N  N   . GLN A 1 240  ? 17.686 41.938  3.989   1.00 17.79 ? 240  GLN A N   1 
ATOM   1744 C  CA  . GLN A 1 240  ? 18.222 40.700  3.439   1.00 17.90 ? 240  GLN A CA  1 
ATOM   1745 C  C   . GLN A 1 240  ? 19.522 40.285  4.132   1.00 17.19 ? 240  GLN A C   1 
ATOM   1746 O  O   . GLN A 1 240  ? 20.158 39.297  3.738   1.00 15.44 ? 240  GLN A O   1 
ATOM   1747 C  CB  . GLN A 1 240  ? 18.498 40.913  1.955   1.00 20.13 ? 240  GLN A CB  1 
ATOM   1748 C  CG  . GLN A 1 240  ? 17.311 41.517  1.196   1.00 22.67 ? 240  GLN A CG  1 
ATOM   1749 C  CD  . GLN A 1 240  ? 16.107 40.605  1.275   1.00 24.24 ? 240  GLN A CD  1 
ATOM   1750 O  OE1 . GLN A 1 240  ? 16.252 39.388  1.227   1.00 25.67 ? 240  GLN A OE1 1 
ATOM   1751 N  NE2 . GLN A 1 240  ? 14.914 41.183  1.391   1.00 28.08 ? 240  GLN A NE2 1 
ATOM   1752 N  N   . ARG A 1 241  ? 19.900 41.032  5.173   1.00 15.74 ? 241  ARG A N   1 
ATOM   1753 C  CA  . ARG A 1 241  ? 21.153 40.781  5.876   1.00 14.68 ? 241  ARG A CA  1 
ATOM   1754 C  C   . ARG A 1 241  ? 22.283 40.743  4.836   1.00 14.02 ? 241  ARG A C   1 
ATOM   1755 O  O   . ARG A 1 241  ? 23.111 39.821  4.795   1.00 11.85 ? 241  ARG A O   1 
ATOM   1756 C  CB  . ARG A 1 241  ? 21.077 39.474  6.677   1.00 16.96 ? 241  ARG A CB  1 
ATOM   1757 C  CG  . ARG A 1 241  ? 20.012 39.557  7.810   1.00 19.71 ? 241  ARG A CG  1 
ATOM   1758 C  CD  . ARG A 1 241  ? 20.122 38.428  8.814   1.00 21.89 ? 241  ARG A CD  1 
ATOM   1759 N  NE  . ARG A 1 241  ? 20.245 37.145  8.130   1.00 24.68 ? 241  ARG A NE  1 
ATOM   1760 C  CZ  . ARG A 1 241  ? 20.580 36.001  8.736   1.00 26.97 ? 241  ARG A CZ  1 
ATOM   1761 N  NH1 . ARG A 1 241  ? 20.817 35.993  10.053  1.00 26.61 ? 241  ARG A NH1 1 
ATOM   1762 N  NH2 . ARG A 1 241  ? 20.719 34.874  8.027   1.00 25.26 ? 241  ARG A NH2 1 
ATOM   1763 N  N   . GLN A 1 242  ? 22.301 41.753  3.957   1.00 13.73 ? 242  GLN A N   1 
ATOM   1764 C  CA  . GLN A 1 242  ? 23.369 41.830  2.952   1.00 11.90 ? 242  GLN A CA  1 
ATOM   1765 C  C   . GLN A 1 242  ? 24.190 43.106  3.198   1.00 12.84 ? 242  GLN A C   1 
ATOM   1766 O  O   . GLN A 1 242  ? 24.685 43.715  2.238   1.00 11.16 ? 242  GLN A O   1 
ATOM   1767 C  CB  . GLN A 1 242  ? 22.774 41.832  1.530   1.00 13.11 ? 242  GLN A CB  1 
ATOM   1768 C  CG  . GLN A 1 242  ? 21.997 40.529  1.163   1.00 12.12 ? 242  GLN A CG  1 
ATOM   1769 C  CD  . GLN A 1 242  ? 21.195 40.669  -0.127  1.00 13.58 ? 242  GLN A CD  1 
ATOM   1770 O  OE1 . GLN A 1 242  ? 20.648 41.728  -0.401  1.00 14.84 ? 242  GLN A OE1 1 
ATOM   1771 N  NE2 . GLN A 1 242  ? 21.113 39.589  -0.912  1.00 13.16 ? 242  GLN A NE2 1 
ATOM   1772 N  N   . LEU A 1 243  ? 24.317 43.516  4.474   1.00 10.59 ? 243  LEU A N   1 
ATOM   1773 C  CA  . LEU A 1 243  ? 25.100 44.705  4.824   1.00 11.54 ? 243  LEU A CA  1 
ATOM   1774 C  C   . LEU A 1 243  ? 26.578 44.374  4.829   1.00 11.78 ? 243  LEU A C   1 
ATOM   1775 O  O   . LEU A 1 243  ? 27.427 45.271  4.828   1.00 12.49 ? 243  LEU A O   1 
ATOM   1776 C  CB  . LEU A 1 243  ? 24.674 45.270  6.194   1.00 9.86  ? 243  LEU A CB  1 
ATOM   1777 C  CG  . LEU A 1 243  ? 23.299 45.960  6.148   1.00 10.54 ? 243  LEU A CG  1 
ATOM   1778 C  CD1 . LEU A 1 243  ? 22.770 46.213  7.590   1.00 8.70  ? 243  LEU A CD1 1 
ATOM   1779 C  CD2 . LEU A 1 243  ? 23.399 47.274  5.340   1.00 8.35  ? 243  LEU A CD2 1 
ATOM   1780 N  N   . GLU A 1 244  ? 26.886 43.078  4.879   1.00 11.77 ? 244  GLU A N   1 
ATOM   1781 C  CA  . GLU A 1 244  ? 28.263 42.622  4.790   1.00 11.43 ? 244  GLU A CA  1 
ATOM   1782 C  C   . GLU A 1 244  ? 28.323 41.834  3.502   1.00 11.59 ? 244  GLU A C   1 
ATOM   1783 O  O   . GLU A 1 244  ? 27.501 40.949  3.282   1.00 11.98 ? 244  GLU A O   1 
ATOM   1784 C  CB  . GLU A 1 244  ? 28.657 41.771  6.018   1.00 10.79 ? 244  GLU A CB  1 
ATOM   1785 C  CG  . GLU A 1 244  ? 28.976 42.689  7.216   1.00 9.23  ? 244  GLU A CG  1 
ATOM   1786 C  CD  . GLU A 1 244  ? 29.346 41.964  8.490   1.00 10.19 ? 244  GLU A CD  1 
ATOM   1787 O  OE1 . GLU A 1 244  ? 28.789 40.880  8.741   1.00 9.17  ? 244  GLU A OE1 1 
ATOM   1788 O  OE2 . GLU A 1 244  ? 30.189 42.507  9.245   1.00 10.66 ? 244  GLU A OE2 1 
ATOM   1789 N  N   . PHE A 1 245  ? 29.287 42.156  2.640   1.00 11.53 ? 245  PHE A N   1 
ATOM   1790 C  CA  . PHE A 1 245  ? 29.366 41.493  1.342   1.00 11.09 ? 245  PHE A CA  1 
ATOM   1791 C  C   . PHE A 1 245  ? 30.775 41.492  0.769   1.00 10.23 ? 245  PHE A C   1 
ATOM   1792 O  O   . PHE A 1 245  ? 31.651 42.200  1.264   1.00 9.68  ? 245  PHE A O   1 
ATOM   1793 C  CB  . PHE A 1 245  ? 28.394 42.203  0.362   1.00 9.26  ? 245  PHE A CB  1 
ATOM   1794 C  CG  . PHE A 1 245  ? 28.519 43.719  0.370   1.00 10.76 ? 245  PHE A CG  1 
ATOM   1795 C  CD1 . PHE A 1 245  ? 29.435 44.367  -0.460  1.00 10.02 ? 245  PHE A CD1 1 
ATOM   1796 C  CD2 . PHE A 1 245  ? 27.733 44.499  1.242   1.00 11.30 ? 245  PHE A CD2 1 
ATOM   1797 C  CE1 . PHE A 1 245  ? 29.573 45.786  -0.430  1.00 10.35 ? 245  PHE A CE1 1 
ATOM   1798 C  CE2 . PHE A 1 245  ? 27.858 45.900  1.284   1.00 9.35  ? 245  PHE A CE2 1 
ATOM   1799 C  CZ  . PHE A 1 245  ? 28.781 46.540  0.442   1.00 9.37  ? 245  PHE A CZ  1 
ATOM   1800 N  N   . LEU A 1 246  ? 30.976 40.687  -0.275  1.00 9.43  ? 246  LEU A N   1 
ATOM   1801 C  CA  . LEU A 1 246  ? 32.248 40.577  -0.962  1.00 9.08  ? 246  LEU A CA  1 
ATOM   1802 C  C   . LEU A 1 246  ? 32.069 41.466  -2.186  1.00 9.68  ? 246  LEU A C   1 
ATOM   1803 O  O   . LEU A 1 246  ? 31.422 41.097  -3.177  1.00 9.76  ? 246  LEU A O   1 
ATOM   1804 C  CB  . LEU A 1 246  ? 32.508 39.109  -1.344  1.00 11.07 ? 246  LEU A CB  1 
ATOM   1805 C  CG  . LEU A 1 246  ? 32.711 38.194  -0.112  1.00 13.78 ? 246  LEU A CG  1 
ATOM   1806 C  CD1 . LEU A 1 246  ? 32.730 36.694  -0.483  1.00 14.90 ? 246  LEU A CD1 1 
ATOM   1807 C  CD2 . LEU A 1 246  ? 34.044 38.557  0.491   1.00 17.37 ? 246  LEU A CD2 1 
ATOM   1808 N  N   . TRP A 1 247  ? 32.620 42.667  -2.088  1.00 9.28  ? 247  TRP A N   1 
ATOM   1809 C  CA  . TRP A 1 247  ? 32.511 43.662  -3.141  1.00 8.56  ? 247  TRP A CA  1 
ATOM   1810 C  C   . TRP A 1 247  ? 33.548 43.443  -4.231  1.00 9.54  ? 247  TRP A C   1 
ATOM   1811 O  O   . TRP A 1 247  ? 34.774 43.613  -3.999  1.00 8.98  ? 247  TRP A O   1 
ATOM   1812 C  CB  . TRP A 1 247  ? 32.686 45.044  -2.505  1.00 10.35 ? 247  TRP A CB  1 
ATOM   1813 C  CG  . TRP A 1 247  ? 32.208 46.232  -3.283  1.00 8.28  ? 247  TRP A CG  1 
ATOM   1814 C  CD1 . TRP A 1 247  ? 31.626 46.250  -4.524  1.00 8.58  ? 247  TRP A CD1 1 
ATOM   1815 C  CD2 . TRP A 1 247  ? 32.235 47.592  -2.827  1.00 7.99  ? 247  TRP A CD2 1 
ATOM   1816 N  NE1 . TRP A 1 247  ? 31.284 47.561  -4.868  1.00 6.09  ? 247  TRP A NE1 1 
ATOM   1817 C  CE2 . TRP A 1 247  ? 31.649 48.393  -3.843  1.00 7.05  ? 247  TRP A CE2 1 
ATOM   1818 C  CE3 . TRP A 1 247  ? 32.695 48.211  -1.652  1.00 8.19  ? 247  TRP A CE3 1 
ATOM   1819 C  CZ2 . TRP A 1 247  ? 31.513 49.786  -3.718  1.00 8.13  ? 247  TRP A CZ2 1 
ATOM   1820 C  CZ3 . TRP A 1 247  ? 32.556 49.612  -1.530  1.00 6.86  ? 247  TRP A CZ3 1 
ATOM   1821 C  CH2 . TRP A 1 247  ? 31.973 50.377  -2.553  1.00 6.83  ? 247  TRP A CH2 1 
ATOM   1822 N  N   . ARG A 1 248  ? 33.073 43.057  -5.417  1.00 7.44  ? 248  ARG A N   1 
ATOM   1823 C  CA  . ARG A 1 248  ? 33.976 42.856  -6.540  1.00 8.46  ? 248  ARG A CA  1 
ATOM   1824 C  C   . ARG A 1 248  ? 33.650 43.910  -7.585  1.00 8.53  ? 248  ARG A C   1 
ATOM   1825 O  O   . ARG A 1 248  ? 32.568 44.518  -7.534  1.00 8.25  ? 248  ARG A O   1 
ATOM   1826 C  CB  . ARG A 1 248  ? 33.780 41.467  -7.169  1.00 8.50  ? 248  ARG A CB  1 
ATOM   1827 C  CG  . ARG A 1 248  ? 32.440 41.335  -7.895  1.00 10.16 ? 248  ARG A CG  1 
ATOM   1828 C  CD  . ARG A 1 248  ? 32.396 40.035  -8.716  1.00 11.37 ? 248  ARG A CD  1 
ATOM   1829 N  NE  . ARG A 1 248  ? 32.331 38.858  -7.838  1.00 12.82 ? 248  ARG A NE  1 
ATOM   1830 C  CZ  . ARG A 1 248  ? 32.286 37.601  -8.291  1.00 14.38 ? 248  ARG A CZ  1 
ATOM   1831 N  NH1 . ARG A 1 248  ? 32.316 37.348  -9.608  1.00 10.70 ? 248  ARG A NH1 1 
ATOM   1832 N  NH2 . ARG A 1 248  ? 32.167 36.599  -7.428  1.00 13.27 ? 248  ARG A NH2 1 
ATOM   1833 N  N   . GLN A 1 249  ? 34.576 44.108  -8.532  1.00 9.17  ? 249  GLN A N   1 
ATOM   1834 C  CA  . GLN A 1 249  ? 34.416 45.083  -9.599  1.00 10.03 ? 249  GLN A CA  1 
ATOM   1835 C  C   . GLN A 1 249  ? 33.317 44.612  -10.548 1.00 9.76  ? 249  GLN A C   1 
ATOM   1836 O  O   . GLN A 1 249  ? 33.099 43.407  -10.705 1.00 8.75  ? 249  GLN A O   1 
ATOM   1837 C  CB  . GLN A 1 249  ? 35.762 45.273  -10.329 1.00 9.40  ? 249  GLN A CB  1 
ATOM   1838 C  CG  . GLN A 1 249  ? 36.855 45.792  -9.390  1.00 10.04 ? 249  GLN A CG  1 
ATOM   1839 C  CD  . GLN A 1 249  ? 36.420 47.097  -8.692  1.00 10.51 ? 249  GLN A CD  1 
ATOM   1840 O  OE1 . GLN A 1 249  ? 36.057 48.067  -9.368  1.00 10.29 ? 249  GLN A OE1 1 
ATOM   1841 N  NE2 . GLN A 1 249  ? 36.446 47.120  -7.342  1.00 8.03  ? 249  GLN A NE2 1 
ATOM   1842 N  N   . ILE A 1 250  ? 32.620 45.560  -11.168 1.00 9.65  ? 250  ILE A N   1 
ATOM   1843 C  CA  . ILE A 1 250  ? 31.485 45.230  -12.044 1.00 9.90  ? 250  ILE A CA  1 
ATOM   1844 C  C   . ILE A 1 250  ? 31.791 44.311  -13.224 1.00 11.31 ? 250  ILE A C   1 
ATOM   1845 O  O   . ILE A 1 250  ? 30.885 43.598  -13.710 1.00 11.87 ? 250  ILE A O   1 
ATOM   1846 C  CB  . ILE A 1 250  ? 30.769 46.513  -12.585 1.00 10.02 ? 250  ILE A CB  1 
ATOM   1847 C  CG1 . ILE A 1 250  ? 31.774 47.402  -13.331 1.00 9.48  ? 250  ILE A CG1 1 
ATOM   1848 C  CG2 . ILE A 1 250  ? 30.113 47.278  -11.437 1.00 8.74  ? 250  ILE A CG2 1 
ATOM   1849 C  CD1 . ILE A 1 250  ? 31.187 48.737  -13.847 1.00 10.34 ? 250  ILE A CD1 1 
ATOM   1850 N  N   . TRP A 1 251  ? 33.040 44.316  -13.685 1.00 11.51 ? 251  TRP A N   1 
ATOM   1851 C  CA  . TRP A 1 251  ? 33.444 43.459  -14.807 1.00 14.37 ? 251  TRP A CA  1 
ATOM   1852 C  C   . TRP A 1 251  ? 34.099 42.136  -14.371 1.00 16.00 ? 251  TRP A C   1 
ATOM   1853 O  O   . TRP A 1 251  ? 34.381 41.277  -15.202 1.00 16.64 ? 251  TRP A O   1 
ATOM   1854 C  CB  . TRP A 1 251  ? 34.468 44.185  -15.666 1.00 14.26 ? 251  TRP A CB  1 
ATOM   1855 C  CG  . TRP A 1 251  ? 35.747 44.343  -14.922 1.00 16.10 ? 251  TRP A CG  1 
ATOM   1856 C  CD1 . TRP A 1 251  ? 36.721 43.400  -14.738 1.00 16.23 ? 251  TRP A CD1 1 
ATOM   1857 C  CD2 . TRP A 1 251  ? 36.160 45.492  -14.218 1.00 15.18 ? 251  TRP A CD2 1 
ATOM   1858 N  NE1 . TRP A 1 251  ? 37.722 43.910  -13.963 1.00 18.06 ? 251  TRP A NE1 1 
ATOM   1859 C  CE2 . TRP A 1 251  ? 37.398 45.196  -13.624 1.00 16.08 ? 251  TRP A CE2 1 
ATOM   1860 C  CE3 . TRP A 1 251  ? 35.595 46.754  -14.025 1.00 14.78 ? 251  TRP A CE3 1 
ATOM   1861 C  CZ2 . TRP A 1 251  ? 38.089 46.110  -12.854 1.00 15.72 ? 251  TRP A CZ2 1 
ATOM   1862 C  CZ3 . TRP A 1 251  ? 36.272 47.666  -13.263 1.00 16.08 ? 251  TRP A CZ3 1 
ATOM   1863 C  CH2 . TRP A 1 251  ? 37.511 47.347  -12.684 1.00 16.86 ? 251  TRP A CH2 1 
ATOM   1864 N  N   . ASP A 1 252  ? 34.337 41.987  -13.072 1.00 16.78 ? 252  ASP A N   1 
ATOM   1865 C  CA  . ASP A 1 252  ? 35.022 40.825  -12.505 1.00 17.31 ? 252  ASP A CA  1 
ATOM   1866 C  C   . ASP A 1 252  ? 34.183 39.558  -12.453 1.00 17.95 ? 252  ASP A C   1 
ATOM   1867 O  O   . ASP A 1 252  ? 33.420 39.308  -11.523 1.00 18.24 ? 252  ASP A O   1 
ATOM   1868 C  CB  . ASP A 1 252  ? 35.551 41.182  -11.103 1.00 16.89 ? 252  ASP A CB  1 
ATOM   1869 C  CG  . ASP A 1 252  ? 36.374 40.052  -10.481 1.00 18.33 ? 252  ASP A CG  1 
ATOM   1870 O  OD1 . ASP A 1 252  ? 36.626 39.035  -11.183 1.00 17.01 ? 252  ASP A OD1 1 
ATOM   1871 O  OD2 . ASP A 1 252  ? 36.759 40.194  -9.300  1.00 15.83 ? 252  ASP A OD2 1 
ATOM   1872 N  N   . ASN A 1 253  ? 34.340 38.732  -13.470 1.00 19.02 ? 253  ASN A N   1 
ATOM   1873 C  CA  . ASN A 1 253  ? 33.560 37.519  -13.524 1.00 20.49 ? 253  ASN A CA  1 
ATOM   1874 C  C   . ASN A 1 253  ? 34.036 36.447  -12.539 1.00 20.23 ? 253  ASN A C   1 
ATOM   1875 O  O   . ASN A 1 253  ? 33.227 35.730  -11.954 1.00 21.02 ? 253  ASN A O   1 
ATOM   1876 C  CB  . ASN A 1 253  ? 33.583 36.988  -14.954 1.00 23.65 ? 253  ASN A CB  1 
ATOM   1877 C  CG  . ASN A 1 253  ? 32.746 35.763  -15.107 1.00 26.53 ? 253  ASN A CG  1 
ATOM   1878 O  OD1 . ASN A 1 253  ? 33.270 34.643  -15.172 1.00 28.84 ? 253  ASN A OD1 1 
ATOM   1879 N  ND2 . ASN A 1 253  ? 31.424 35.951  -15.148 1.00 28.81 ? 253  ASN A ND2 1 
ATOM   1880 N  N   . LYS A 1 254  ? 35.338 36.363  -12.325 1.00 20.37 ? 254  LYS A N   1 
ATOM   1881 C  CA  . LYS A 1 254  ? 35.891 35.346  -11.426 1.00 22.26 ? 254  LYS A CA  1 
ATOM   1882 C  C   . LYS A 1 254  ? 35.746 35.683  -9.936  1.00 21.39 ? 254  LYS A C   1 
ATOM   1883 O  O   . LYS A 1 254  ? 35.495 34.807  -9.110  1.00 20.10 ? 254  LYS A O   1 
ATOM   1884 C  CB  . LYS A 1 254  ? 37.364 35.119  -11.776 1.00 25.50 ? 254  LYS A CB  1 
ATOM   1885 C  CG  . LYS A 1 254  ? 37.919 33.793  -11.245 1.00 29.96 ? 254  LYS A CG  1 
ATOM   1886 C  CD  . LYS A 1 254  ? 39.358 33.548  -11.705 1.00 31.31 ? 254  LYS A CD  1 
ATOM   1887 C  CE  . LYS A 1 254  ? 39.922 32.257  -11.062 1.00 33.05 ? 254  LYS A CE  1 
ATOM   1888 N  NZ  . LYS A 1 254  ? 39.926 32.289  -9.565  1.00 32.62 ? 254  LYS A NZ  1 
ATOM   1889 N  N   . GLY A 1 255  ? 35.911 36.958  -9.602  1.00 20.71 ? 255  GLY A N   1 
ATOM   1890 C  CA  . GLY A 1 255  ? 35.783 37.382  -8.225  1.00 20.25 ? 255  GLY A CA  1 
ATOM   1891 C  C   . GLY A 1 255  ? 37.100 37.608  -7.506  1.00 20.06 ? 255  GLY A C   1 
ATOM   1892 O  O   . GLY A 1 255  ? 37.106 37.769  -6.300  1.00 20.22 ? 255  GLY A O   1 
ATOM   1893 N  N   . ASP A 1 256  ? 38.217 37.626  -8.225  1.00 20.11 ? 256  ASP A N   1 
ATOM   1894 C  CA  . ASP A 1 256  ? 39.498 37.823  -7.561  1.00 21.28 ? 256  ASP A CA  1 
ATOM   1895 C  C   . ASP A 1 256  ? 39.706 39.248  -7.076  1.00 19.14 ? 256  ASP A C   1 
ATOM   1896 O  O   . ASP A 1 256  ? 40.659 39.496  -6.360  1.00 18.83 ? 256  ASP A O   1 
ATOM   1897 C  CB  . ASP A 1 256  ? 40.682 37.476  -8.472  1.00 25.75 ? 256  ASP A CB  1 
ATOM   1898 C  CG  . ASP A 1 256  ? 40.683 36.024  -8.923  1.00 29.82 ? 256  ASP A CG  1 
ATOM   1899 O  OD1 . ASP A 1 256  ? 40.351 35.124  -8.107  1.00 31.63 ? 256  ASP A OD1 1 
ATOM   1900 O  OD2 . ASP A 1 256  ? 41.036 35.796  -10.103 1.00 32.89 ? 256  ASP A OD2 1 
ATOM   1901 N  N   . THR A 1 257  ? 38.852 40.189  -7.486  1.00 17.11 ? 257  THR A N   1 
ATOM   1902 C  CA  . THR A 1 257  ? 38.999 41.574  -7.013  1.00 15.20 ? 257  THR A CA  1 
ATOM   1903 C  C   . THR A 1 257  ? 38.219 41.812  -5.695  1.00 14.67 ? 257  THR A C   1 
ATOM   1904 O  O   . THR A 1 257  ? 38.293 42.915  -5.105  1.00 14.01 ? 257  THR A O   1 
ATOM   1905 C  CB  . THR A 1 257  ? 38.460 42.593  -8.052  1.00 14.30 ? 257  THR A CB  1 
ATOM   1906 O  OG1 . THR A 1 257  ? 37.051 42.372  -8.243  1.00 13.14 ? 257  THR A OG1 1 
ATOM   1907 C  CG2 . THR A 1 257  ? 39.207 42.437  -9.402  1.00 14.48 ? 257  THR A CG2 1 
ATOM   1908 N  N   . ALA A 1 258  ? 37.494 40.782  -5.250  1.00 12.34 ? 258  ALA A N   1 
ATOM   1909 C  CA  . ALA A 1 258  ? 36.646 40.862  -4.079  1.00 11.80 ? 258  ALA A CA  1 
ATOM   1910 C  C   . ALA A 1 258  ? 37.315 41.284  -2.778  1.00 11.44 ? 258  ALA A C   1 
ATOM   1911 O  O   . ALA A 1 258  ? 38.420 40.850  -2.467  1.00 11.65 ? 258  ALA A O   1 
ATOM   1912 C  CB  . ALA A 1 258  ? 35.924 39.534  -3.874  1.00 11.87 ? 258  ALA A CB  1 
ATOM   1913 N  N   . LEU A 1 259  ? 36.636 42.143  -2.018  1.00 10.77 ? 259  LEU A N   1 
ATOM   1914 C  CA  . LEU A 1 259  ? 37.145 42.602  -0.730  1.00 9.89  ? 259  LEU A CA  1 
ATOM   1915 C  C   . LEU A 1 259  ? 35.951 42.604  0.220   1.00 9.66  ? 259  LEU A C   1 
ATOM   1916 O  O   . LEU A 1 259  ? 34.904 43.212  -0.082  1.00 8.43  ? 259  LEU A O   1 
ATOM   1917 C  CB  . LEU A 1 259  ? 37.719 44.021  -0.843  1.00 8.57  ? 259  LEU A CB  1 
ATOM   1918 C  CG  . LEU A 1 259  ? 38.421 44.478  0.429   1.00 8.84  ? 259  LEU A CG  1 
ATOM   1919 C  CD1 . LEU A 1 259  ? 39.573 43.511  0.664   1.00 8.75  ? 259  LEU A CD1 1 
ATOM   1920 C  CD2 . LEU A 1 259  ? 38.882 45.961  0.344   1.00 5.97  ? 259  LEU A CD2 1 
ATOM   1921 N  N   . PHE A 1 260  ? 36.094 41.926  1.356   1.00 9.50  ? 260  PHE A N   1 
ATOM   1922 C  CA  . PHE A 1 260  ? 35.001 41.864  2.332   1.00 8.31  ? 260  PHE A CA  1 
ATOM   1923 C  C   . PHE A 1 260  ? 34.642 43.283  2.778   1.00 8.88  ? 260  PHE A C   1 
ATOM   1924 O  O   . PHE A 1 260  ? 35.525 44.068  3.162   1.00 8.97  ? 260  PHE A O   1 
ATOM   1925 C  CB  . PHE A 1 260  ? 35.408 40.994  3.547   1.00 9.45  ? 260  PHE A CB  1 
ATOM   1926 C  CG  . PHE A 1 260  ? 34.286 40.806  4.547   1.00 10.32 ? 260  PHE A CG  1 
ATOM   1927 C  CD1 . PHE A 1 260  ? 33.289 39.858  4.314   1.00 10.85 ? 260  PHE A CD1 1 
ATOM   1928 C  CD2 . PHE A 1 260  ? 34.196 41.605  5.686   1.00 10.04 ? 260  PHE A CD2 1 
ATOM   1929 C  CE1 . PHE A 1 260  ? 32.235 39.707  5.179   1.00 10.78 ? 260  PHE A CE1 1 
ATOM   1930 C  CE2 . PHE A 1 260  ? 33.135 41.462  6.573   1.00 10.28 ? 260  PHE A CE2 1 
ATOM   1931 C  CZ  . PHE A 1 260  ? 32.150 40.511  6.319   1.00 12.11 ? 260  PHE A CZ  1 
ATOM   1932 N  N   . THR A 1 261  ? 33.350 43.614  2.751   1.00 8.58  ? 261  THR A N   1 
ATOM   1933 C  CA  . THR A 1 261  ? 32.922 44.946  3.090   1.00 8.35  ? 261  THR A CA  1 
ATOM   1934 C  C   . THR A 1 261  ? 31.778 44.964  4.116   1.00 9.23  ? 261  THR A C   1 
ATOM   1935 O  O   . THR A 1 261  ? 30.814 44.208  4.001   1.00 9.56  ? 261  THR A O   1 
ATOM   1936 C  CB  . THR A 1 261  ? 32.438 45.690  1.829   1.00 8.45  ? 261  THR A CB  1 
ATOM   1937 O  OG1 . THR A 1 261  ? 33.488 45.715  0.856   1.00 7.78  ? 261  THR A OG1 1 
ATOM   1938 C  CG2 . THR A 1 261  ? 32.011 47.128  2.166   1.00 6.71  ? 261  THR A CG2 1 
ATOM   1939 N  N   . HIS A 1 262  ? 31.891 45.837  5.114   1.00 8.52  ? 262  HIS A N   1 
ATOM   1940 C  CA  . HIS A 1 262  ? 30.841 45.999  6.120   1.00 8.32  ? 262  HIS A CA  1 
ATOM   1941 C  C   . HIS A 1 262  ? 30.217 47.386  5.950   1.00 9.75  ? 262  HIS A C   1 
ATOM   1942 O  O   . HIS A 1 262  ? 30.907 48.422  6.108   1.00 9.36  ? 262  HIS A O   1 
ATOM   1943 C  CB  . HIS A 1 262  ? 31.443 45.891  7.532   1.00 9.46  ? 262  HIS A CB  1 
ATOM   1944 C  CG  . HIS A 1 262  ? 30.489 46.225  8.641   1.00 9.96  ? 262  HIS A CG  1 
ATOM   1945 N  ND1 . HIS A 1 262  ? 29.904 45.259  9.433   1.00 10.15 ? 262  HIS A ND1 1 
ATOM   1946 C  CD2 . HIS A 1 262  ? 30.033 47.415  9.106   1.00 10.07 ? 262  HIS A CD2 1 
ATOM   1947 C  CE1 . HIS A 1 262  ? 29.131 45.840  10.338  1.00 9.37  ? 262  HIS A CE1 1 
ATOM   1948 N  NE2 . HIS A 1 262  ? 29.193 47.145  10.165  1.00 9.28  ? 262  HIS A NE2 1 
ATOM   1949 N  N   . MET A 1 263  ? 28.922 47.426  5.624   1.00 9.57  ? 263  MET A N   1 
ATOM   1950 C  CA  . MET A 1 263  ? 28.228 48.696  5.526   1.00 10.92 ? 263  MET A CA  1 
ATOM   1951 C  C   . MET A 1 263  ? 27.522 48.934  6.875   1.00 12.69 ? 263  MET A C   1 
ATOM   1952 O  O   . MET A 1 263  ? 26.761 48.057  7.336   1.00 12.32 ? 263  MET A O   1 
ATOM   1953 C  CB  . MET A 1 263  ? 27.172 48.666  4.413   1.00 11.40 ? 263  MET A CB  1 
ATOM   1954 C  CG  . MET A 1 263  ? 26.431 50.013  4.229   1.00 10.81 ? 263  MET A CG  1 
ATOM   1955 S  SD  . MET A 1 263  ? 25.071 49.883  3.034   1.00 12.96 ? 263  MET A SD  1 
ATOM   1956 C  CE  . MET A 1 263  ? 25.953 49.612  1.485   1.00 11.06 ? 263  MET A CE  1 
ATOM   1957 N  N   . MET A 1 264  ? 27.759 50.080  7.521   1.00 10.00 ? 264  MET A N   1 
ATOM   1958 C  CA  . MET A 1 264  ? 27.066 50.351  8.781   1.00 11.27 ? 264  MET A CA  1 
ATOM   1959 C  C   . MET A 1 264  ? 25.590 50.547  8.371   1.00 11.47 ? 264  MET A C   1 
ATOM   1960 O  O   . MET A 1 264  ? 25.296 51.013  7.265   1.00 11.12 ? 264  MET A O   1 
ATOM   1961 C  CB  . MET A 1 264  ? 27.669 51.567  9.472   1.00 11.18 ? 264  MET A CB  1 
ATOM   1962 C  CG  . MET A 1 264  ? 29.085 51.289  9.984   1.00 12.92 ? 264  MET A CG  1 
ATOM   1963 S  SD  . MET A 1 264  ? 29.962 52.862  10.517  1.00 16.63 ? 264  MET A SD  1 
ATOM   1964 C  CE  . MET A 1 264  ? 28.948 53.486  11.722  1.00 16.51 ? 264  MET A CE  1 
ATOM   1965 N  N   . PRO A 1 265  ? 24.641 50.189  9.256   1.00 12.14 ? 265  PRO A N   1 
ATOM   1966 C  CA  . PRO A 1 265  ? 23.210 50.289  8.935   1.00 11.70 ? 265  PRO A CA  1 
ATOM   1967 C  C   . PRO A 1 265  ? 22.412 51.563  9.145   1.00 13.75 ? 265  PRO A C   1 
ATOM   1968 O  O   . PRO A 1 265  ? 21.335 51.738  8.540   1.00 12.52 ? 265  PRO A O   1 
ATOM   1969 C  CB  . PRO A 1 265  ? 22.615 49.133  9.763   1.00 14.23 ? 265  PRO A CB  1 
ATOM   1970 C  CG  . PRO A 1 265  ? 23.408 49.240  11.052  1.00 14.23 ? 265  PRO A CG  1 
ATOM   1971 C  CD  . PRO A 1 265  ? 24.844 49.656  10.620  1.00 12.18 ? 265  PRO A CD  1 
ATOM   1972 N  N   . PHE A 1 266  ? 22.932 52.465  9.962   1.00 12.42 ? 266  PHE A N   1 
ATOM   1973 C  CA  . PHE A 1 266  ? 22.174 53.639  10.305  1.00 12.57 ? 266  PHE A CA  1 
ATOM   1974 C  C   . PHE A 1 266  ? 22.544 54.981  9.688   1.00 12.21 ? 266  PHE A C   1 
ATOM   1975 O  O   . PHE A 1 266  ? 23.456 55.090  8.865   1.00 12.99 ? 266  PHE A O   1 
ATOM   1976 C  CB  . PHE A 1 266  ? 22.111 53.684  11.839  1.00 12.21 ? 266  PHE A CB  1 
ATOM   1977 C  CG  . PHE A 1 266  ? 21.557 52.385  12.456  1.00 12.20 ? 266  PHE A CG  1 
ATOM   1978 C  CD1 . PHE A 1 266  ? 22.178 51.782  13.554  1.00 11.86 ? 266  PHE A CD1 1 
ATOM   1979 C  CD2 . PHE A 1 266  ? 20.419 51.772  11.916  1.00 12.01 ? 266  PHE A CD2 1 
ATOM   1980 C  CE1 . PHE A 1 266  ? 21.675 50.580  14.112  1.00 13.48 ? 266  PHE A CE1 1 
ATOM   1981 C  CE2 . PHE A 1 266  ? 19.909 50.592  12.446  1.00 11.45 ? 266  PHE A CE2 1 
ATOM   1982 C  CZ  . PHE A 1 266  ? 20.536 49.975  13.556  1.00 11.79 ? 266  PHE A CZ  1 
ATOM   1983 N  N   . TYR A 1 267  ? 21.807 56.002  10.117  1.00 12.52 ? 267  TYR A N   1 
ATOM   1984 C  CA  . TYR A 1 267  ? 21.905 57.354  9.601   1.00 12.05 ? 267  TYR A CA  1 
ATOM   1985 C  C   . TYR A 1 267  ? 23.236 58.065  9.828   1.00 12.06 ? 267  TYR A C   1 
ATOM   1986 O  O   . TYR A 1 267  ? 23.673 58.872  8.998   1.00 11.91 ? 267  TYR A O   1 
ATOM   1987 C  CB  . TYR A 1 267  ? 20.751 58.169  10.214  1.00 12.67 ? 267  TYR A CB  1 
ATOM   1988 C  CG  . TYR A 1 267  ? 20.870 59.677  10.086  1.00 13.97 ? 267  TYR A CG  1 
ATOM   1989 C  CD1 . TYR A 1 267  ? 20.567 60.327  8.875   1.00 16.09 ? 267  TYR A CD1 1 
ATOM   1990 C  CD2 . TYR A 1 267  ? 21.218 60.468  11.195  1.00 14.57 ? 267  TYR A CD2 1 
ATOM   1991 C  CE1 . TYR A 1 267  ? 20.594 61.745  8.779   1.00 15.26 ? 267  TYR A CE1 1 
ATOM   1992 C  CE2 . TYR A 1 267  ? 21.256 61.884  11.113  1.00 14.29 ? 267  TYR A CE2 1 
ATOM   1993 C  CZ  . TYR A 1 267  ? 20.938 62.501  9.901   1.00 15.79 ? 267  TYR A CZ  1 
ATOM   1994 O  OH  . TYR A 1 267  ? 20.953 63.874  9.804   1.00 17.24 ? 267  TYR A OH  1 
ATOM   1995 N  N   . SER A 1 268  ? 23.878 57.779  10.953  1.00 11.07 ? 268  SER A N   1 
ATOM   1996 C  CA  . SER A 1 268  ? 25.139 58.433  11.267  1.00 11.26 ? 268  SER A CA  1 
ATOM   1997 C  C   . SER A 1 268  ? 26.089 57.465  11.954  1.00 11.57 ? 268  SER A C   1 
ATOM   1998 O  O   . SER A 1 268  ? 25.689 56.351  12.323  1.00 12.27 ? 268  SER A O   1 
ATOM   1999 C  CB  . SER A 1 268  ? 24.860 59.616  12.191  1.00 10.28 ? 268  SER A CB  1 
ATOM   2000 O  OG  . SER A 1 268  ? 26.050 60.196  12.696  1.00 12.05 ? 268  SER A OG  1 
ATOM   2001 N  N   . TYR A 1 269  ? 27.356 57.870  12.089  1.00 11.66 ? 269  TYR A N   1 
ATOM   2002 C  CA  . TYR A 1 269  ? 28.326 57.055  12.816  1.00 9.91  ? 269  TYR A CA  1 
ATOM   2003 C  C   . TYR A 1 269  ? 28.431 57.606  14.255  1.00 9.84  ? 269  TYR A C   1 
ATOM   2004 O  O   . TYR A 1 269  ? 29.255 57.122  15.045  1.00 10.58 ? 269  TYR A O   1 
ATOM   2005 C  CB  . TYR A 1 269  ? 29.707 57.111  12.162  1.00 9.77  ? 269  TYR A CB  1 
ATOM   2006 C  CG  . TYR A 1 269  ? 30.188 58.510  11.894  1.00 9.80  ? 269  TYR A CG  1 
ATOM   2007 C  CD1 . TYR A 1 269  ? 30.606 59.354  12.930  1.00 8.21  ? 269  TYR A CD1 1 
ATOM   2008 C  CD2 . TYR A 1 269  ? 30.189 59.003  10.592  1.00 10.29 ? 269  TYR A CD2 1 
ATOM   2009 C  CE1 . TYR A 1 269  ? 31.025 60.691  12.666  1.00 10.15 ? 269  TYR A CE1 1 
ATOM   2010 C  CE2 . TYR A 1 269  ? 30.587 60.315  10.308  1.00 11.28 ? 269  TYR A CE2 1 
ATOM   2011 C  CZ  . TYR A 1 269  ? 31.007 61.157  11.350  1.00 12.06 ? 269  TYR A CZ  1 
ATOM   2012 O  OH  . TYR A 1 269  ? 31.388 62.442  11.034  1.00 12.53 ? 269  TYR A OH  1 
ATOM   2013 N  N   . ASP A 1 270  ? 27.628 58.615  14.602  1.00 9.44  ? 270  ASP A N   1 
ATOM   2014 C  CA  . ASP A 1 270  ? 27.723 59.151  15.962  1.00 10.28 ? 270  ASP A CA  1 
ATOM   2015 C  C   . ASP A 1 270  ? 27.167 58.111  16.962  1.00 11.61 ? 270  ASP A C   1 
ATOM   2016 O  O   . ASP A 1 270  ? 26.607 57.086  16.555  1.00 11.48 ? 270  ASP A O   1 
ATOM   2017 C  CB  . ASP A 1 270  ? 27.036 60.539  16.075  1.00 11.09 ? 270  ASP A CB  1 
ATOM   2018 C  CG  . ASP A 1 270  ? 25.516 60.489  15.896  1.00 12.05 ? 270  ASP A CG  1 
ATOM   2019 O  OD1 . ASP A 1 270  ? 24.931 59.374  15.850  1.00 12.18 ? 270  ASP A OD1 1 
ATOM   2020 O  OD2 . ASP A 1 270  ? 24.909 61.594  15.836  1.00 12.78 ? 270  ASP A OD2 1 
ATOM   2021 N  N   . ILE A 1 271  ? 27.363 58.334  18.256  1.00 11.04 ? 271  ILE A N   1 
ATOM   2022 C  CA  . ILE A 1 271  ? 26.915 57.342  19.218  1.00 11.32 ? 271  ILE A CA  1 
ATOM   2023 C  C   . ILE A 1 271  ? 25.405 57.070  19.192  1.00 10.73 ? 271  ILE A C   1 
ATOM   2024 O  O   . ILE A 1 271  ? 25.003 55.910  19.238  1.00 11.70 ? 271  ILE A O   1 
ATOM   2025 C  CB  . ILE A 1 271  ? 27.463 57.665  20.642  1.00 11.05 ? 271  ILE A CB  1 
ATOM   2026 C  CG1 . ILE A 1 271  ? 28.995 57.542  20.605  1.00 9.65  ? 271  ILE A CG1 1 
ATOM   2027 C  CG2 . ILE A 1 271  ? 26.921 56.620  21.692  1.00 9.82  ? 271  ILE A CG2 1 
ATOM   2028 C  CD1 . ILE A 1 271  ? 29.729 58.213  21.779  1.00 10.79 ? 271  ILE A CD1 1 
ATOM   2029 N  N   . PRO A 1 272  ? 24.557 58.107  19.076  1.00 11.36 ? 272  PRO A N   1 
ATOM   2030 C  CA  . PRO A 1 272  ? 23.100 57.857  19.033  1.00 11.95 ? 272  PRO A CA  1 
ATOM   2031 C  C   . PRO A 1 272  ? 22.687 56.899  17.899  1.00 12.45 ? 272  PRO A C   1 
ATOM   2032 O  O   . PRO A 1 272  ? 21.657 56.227  17.986  1.00 13.68 ? 272  PRO A O   1 
ATOM   2033 C  CB  . PRO A 1 272  ? 22.505 59.243  18.792  1.00 10.25 ? 272  PRO A CB  1 
ATOM   2034 C  CG  . PRO A 1 272  ? 23.452 60.125  19.552  1.00 11.95 ? 272  PRO A CG  1 
ATOM   2035 C  CD  . PRO A 1 272  ? 24.834 59.554  19.206  1.00 11.67 ? 272  PRO A CD  1 
ATOM   2036 N  N   . HIS A 1 273  ? 23.483 56.853  16.836  1.00 11.85 ? 273  HIS A N   1 
ATOM   2037 C  CA  . HIS A 1 273  ? 23.172 56.003  15.682  1.00 11.42 ? 273  HIS A CA  1 
ATOM   2038 C  C   . HIS A 1 273  ? 24.097 54.803  15.479  1.00 12.04 ? 273  HIS A C   1 
ATOM   2039 O  O   . HIS A 1 273  ? 24.184 54.230  14.360  1.00 11.50 ? 273  HIS A O   1 
ATOM   2040 C  CB  . HIS A 1 273  ? 23.131 56.870  14.411  1.00 10.57 ? 273  HIS A CB  1 
ATOM   2041 C  CG  . HIS A 1 273  ? 22.060 57.921  14.459  1.00 11.47 ? 273  HIS A CG  1 
ATOM   2042 N  ND1 . HIS A 1 273  ? 22.274 59.189  14.962  1.00 13.12 ? 273  HIS A ND1 1 
ATOM   2043 C  CD2 . HIS A 1 273  ? 20.746 57.862  14.134  1.00 12.47 ? 273  HIS A CD2 1 
ATOM   2044 C  CE1 . HIS A 1 273  ? 21.134 59.863  14.941  1.00 13.03 ? 273  HIS A CE1 1 
ATOM   2045 N  NE2 . HIS A 1 273  ? 20.194 59.077  14.445  1.00 12.21 ? 273  HIS A NE2 1 
ATOM   2046 N  N   . THR A 1 274  ? 24.778 54.405  16.548  1.00 11.46 ? 274  THR A N   1 
ATOM   2047 C  CA  . THR A 1 274  ? 25.663 53.264  16.447  1.00 11.77 ? 274  THR A CA  1 
ATOM   2048 C  C   . THR A 1 274  ? 25.454 52.156  17.498  1.00 12.24 ? 274  THR A C   1 
ATOM   2049 O  O   . THR A 1 274  ? 25.986 51.069  17.314  1.00 13.70 ? 274  THR A O   1 
ATOM   2050 C  CB  . THR A 1 274  ? 27.151 53.702  16.430  1.00 11.89 ? 274  THR A CB  1 
ATOM   2051 O  OG1 . THR A 1 274  ? 27.410 54.629  17.485  1.00 11.93 ? 274  THR A OG1 1 
ATOM   2052 C  CG2 . THR A 1 274  ? 27.494 54.317  15.083  1.00 10.63 ? 274  THR A CG2 1 
ATOM   2053 N  N   . CYS A 1 275  ? 24.657 52.385  18.551  1.00 12.44 ? 275  CYS A N   1 
ATOM   2054 C  CA  . CYS A 1 275  ? 24.454 51.312  19.537  1.00 12.97 ? 275  CYS A CA  1 
ATOM   2055 C  C   . CYS A 1 275  ? 23.298 50.396  19.150  1.00 13.10 ? 275  CYS A C   1 
ATOM   2056 O  O   . CYS A 1 275  ? 23.227 49.251  19.598  1.00 12.56 ? 275  CYS A O   1 
ATOM   2057 C  CB  . CYS A 1 275  ? 24.173 51.879  20.948  1.00 13.99 ? 275  CYS A CB  1 
ATOM   2058 S  SG  . CYS A 1 275  ? 22.397 51.992  21.429  1.00 14.25 ? 275  CYS A SG  1 
ATOM   2059 N  N   . GLY A 1 276  ? 22.394 50.912  18.320  1.00 13.70 ? 276  GLY A N   1 
ATOM   2060 C  CA  . GLY A 1 276  ? 21.226 50.153  17.900  1.00 13.31 ? 276  GLY A CA  1 
ATOM   2061 C  C   . GLY A 1 276  ? 20.262 51.051  17.136  1.00 12.66 ? 276  GLY A C   1 
ATOM   2062 O  O   . GLY A 1 276  ? 20.608 52.214  16.885  1.00 12.27 ? 276  GLY A O   1 
ATOM   2063 N  N   . PRO A 1 277  ? 19.034 50.572  16.812  1.00 10.72 ? 277  PRO A N   1 
ATOM   2064 C  CA  . PRO A 1 277  ? 18.027 51.330  16.059  1.00 11.78 ? 277  PRO A CA  1 
ATOM   2065 C  C   . PRO A 1 277  ? 17.382 52.570  16.645  1.00 12.17 ? 277  PRO A C   1 
ATOM   2066 O  O   . PRO A 1 277  ? 16.873 53.394  15.907  1.00 13.20 ? 277  PRO A O   1 
ATOM   2067 C  CB  . PRO A 1 277  ? 16.962 50.260  15.716  1.00 11.96 ? 277  PRO A CB  1 
ATOM   2068 C  CG  . PRO A 1 277  ? 17.008 49.342  16.890  1.00 9.87  ? 277  PRO A CG  1 
ATOM   2069 C  CD  . PRO A 1 277  ? 18.521 49.239  17.190  1.00 10.70 ? 277  PRO A CD  1 
ATOM   2070 N  N   . ASP A 1 278  ? 17.414 52.710  17.962  1.00 12.94 ? 278  ASP A N   1 
ATOM   2071 C  CA  . ASP A 1 278  ? 16.740 53.824  18.618  1.00 13.98 ? 278  ASP A CA  1 
ATOM   2072 C  C   . ASP A 1 278  ? 17.688 54.862  19.172  1.00 13.88 ? 278  ASP A C   1 
ATOM   2073 O  O   . ASP A 1 278  ? 18.249 54.684  20.248  1.00 14.68 ? 278  ASP A O   1 
ATOM   2074 C  CB  . ASP A 1 278  ? 15.857 53.297  19.754  1.00 15.29 ? 278  ASP A CB  1 
ATOM   2075 C  CG  . ASP A 1 278  ? 14.966 54.393  20.350  1.00 17.39 ? 278  ASP A CG  1 
ATOM   2076 O  OD1 . ASP A 1 278  ? 15.110 55.580  19.954  1.00 17.23 ? 278  ASP A OD1 1 
ATOM   2077 O  OD2 . ASP A 1 278  ? 14.138 54.051  21.212  1.00 19.09 ? 278  ASP A OD2 1 
ATOM   2078 N  N   . PRO A 1 279  ? 17.858 55.972  18.453  1.00 13.56 ? 279  PRO A N   1 
ATOM   2079 C  CA  . PRO A 1 279  ? 18.765 57.035  18.908  1.00 14.11 ? 279  PRO A CA  1 
ATOM   2080 C  C   . PRO A 1 279  ? 18.387 57.636  20.243  1.00 14.38 ? 279  PRO A C   1 
ATOM   2081 O  O   . PRO A 1 279  ? 19.244 58.148  20.932  1.00 14.85 ? 279  PRO A O   1 
ATOM   2082 C  CB  . PRO A 1 279  ? 18.712 58.055  17.768  1.00 12.69 ? 279  PRO A CB  1 
ATOM   2083 C  CG  . PRO A 1 279  ? 17.285 57.872  17.247  1.00 15.28 ? 279  PRO A CG  1 
ATOM   2084 C  CD  . PRO A 1 279  ? 17.150 56.365  17.222  1.00 13.43 ? 279  PRO A CD  1 
ATOM   2085 N  N   . LYS A 1 280  ? 17.112 57.578  20.621  1.00 15.30 ? 280  LYS A N   1 
ATOM   2086 C  CA  . LYS A 1 280  ? 16.694 58.158  21.905  1.00 16.51 ? 280  LYS A CA  1 
ATOM   2087 C  C   . LYS A 1 280  ? 17.310 57.342  23.020  1.00 16.04 ? 280  LYS A C   1 
ATOM   2088 O  O   . LYS A 1 280  ? 17.622 57.857  24.104  1.00 17.29 ? 280  LYS A O   1 
ATOM   2089 C  CB  . LYS A 1 280  ? 15.170 58.142  22.037  1.00 18.14 ? 280  LYS A CB  1 
ATOM   2090 C  CG  . LYS A 1 280  ? 14.647 58.588  23.396  1.00 20.71 ? 280  LYS A CG  1 
ATOM   2091 C  CD  . LYS A 1 280  ? 13.132 58.735  23.363  1.00 23.91 ? 280  LYS A CD  1 
ATOM   2092 C  CE  . LYS A 1 280  ? 12.374 57.401  23.493  1.00 27.96 ? 280  LYS A CE  1 
ATOM   2093 N  NZ  . LYS A 1 280  ? 12.489 56.292  22.416  1.00 31.28 ? 280  LYS A NZ  1 
ATOM   2094 N  N   . VAL A 1 281  ? 17.500 56.057  22.752  1.00 16.08 ? 281  VAL A N   1 
ATOM   2095 C  CA  . VAL A 1 281  ? 18.111 55.172  23.742  1.00 15.64 ? 281  VAL A CA  1 
ATOM   2096 C  C   . VAL A 1 281  ? 19.640 55.227  23.657  1.00 15.25 ? 281  VAL A C   1 
ATOM   2097 O  O   . VAL A 1 281  ? 20.322 55.420  24.670  1.00 14.12 ? 281  VAL A O   1 
ATOM   2098 C  CB  . VAL A 1 281  ? 17.649 53.715  23.547  1.00 16.78 ? 281  VAL A CB  1 
ATOM   2099 C  CG1 . VAL A 1 281  ? 18.477 52.785  24.467  1.00 15.39 ? 281  VAL A CG1 1 
ATOM   2100 C  CG2 . VAL A 1 281  ? 16.109 53.605  23.827  1.00 16.71 ? 281  VAL A CG2 1 
ATOM   2101 N  N   . CYS A 1 282  ? 20.183 55.070  22.448  1.00 14.91 ? 282  CYS A N   1 
ATOM   2102 C  CA  . CYS A 1 282  ? 21.636 55.109  22.279  1.00 14.29 ? 282  CYS A CA  1 
ATOM   2103 C  C   . CYS A 1 282  ? 22.263 56.418  22.786  1.00 14.19 ? 282  CYS A C   1 
ATOM   2104 O  O   . CYS A 1 282  ? 23.381 56.421  23.329  1.00 14.81 ? 282  CYS A O   1 
ATOM   2105 C  CB  . CYS A 1 282  ? 21.998 54.941  20.807  1.00 13.77 ? 282  CYS A CB  1 
ATOM   2106 S  SG  . CYS A 1 282  ? 21.589 53.317  20.114  1.00 14.67 ? 282  CYS A SG  1 
ATOM   2107 N  N   . CYS A 1 283  ? 21.557 57.530  22.613  1.00 13.05 ? 283  CYS A N   1 
ATOM   2108 C  CA  . CYS A 1 283  ? 22.098 58.803  23.062  1.00 13.71 ? 283  CYS A CA  1 
ATOM   2109 C  C   . CYS A 1 283  ? 22.407 58.769  24.560  1.00 14.21 ? 283  CYS A C   1 
ATOM   2110 O  O   . CYS A 1 283  ? 23.356 59.411  25.044  1.00 13.97 ? 283  CYS A O   1 
ATOM   2111 C  CB  . CYS A 1 283  ? 21.144 59.963  22.720  1.00 14.56 ? 283  CYS A CB  1 
ATOM   2112 S  SG  . CYS A 1 283  ? 22.016 61.578  22.856  1.00 13.60 ? 283  CYS A SG  1 
ATOM   2113 N  N   . GLN A 1 284  ? 21.630 57.990  25.296  1.00 13.37 ? 284  GLN A N   1 
ATOM   2114 C  CA  . GLN A 1 284  ? 21.850 57.911  26.721  1.00 15.05 ? 284  GLN A CA  1 
ATOM   2115 C  C   . GLN A 1 284  ? 23.133 57.173  27.044  1.00 14.70 ? 284  GLN A C   1 
ATOM   2116 O  O   . GLN A 1 284  ? 23.521 57.082  28.214  1.00 16.23 ? 284  GLN A O   1 
ATOM   2117 C  CB  . GLN A 1 284  ? 20.672 57.218  27.396  1.00 14.40 ? 284  GLN A CB  1 
ATOM   2118 C  CG  . GLN A 1 284  ? 19.353 57.934  27.199  1.00 14.73 ? 284  GLN A CG  1 
ATOM   2119 C  CD  . GLN A 1 284  ? 18.213 57.120  27.769  1.00 15.80 ? 284  GLN A CD  1 
ATOM   2120 O  OE1 . GLN A 1 284  ? 18.222 56.765  28.942  1.00 17.21 ? 284  GLN A OE1 1 
ATOM   2121 N  NE2 . GLN A 1 284  ? 17.237 56.802  26.932  1.00 19.41 ? 284  GLN A NE2 1 
ATOM   2122 N  N   . PHE A 1 285  ? 23.797 56.630  26.027  1.00 14.57 ? 285  PHE A N   1 
ATOM   2123 C  CA  . PHE A 1 285  ? 25.039 55.925  26.291  1.00 13.59 ? 285  PHE A CA  1 
ATOM   2124 C  C   . PHE A 1 285  ? 26.244 56.626  25.688  1.00 13.41 ? 285  PHE A C   1 
ATOM   2125 O  O   . PHE A 1 285  ? 27.287 56.026  25.444  1.00 14.30 ? 285  PHE A O   1 
ATOM   2126 C  CB  . PHE A 1 285  ? 24.916 54.458  25.857  1.00 13.78 ? 285  PHE A CB  1 
ATOM   2127 C  CG  . PHE A 1 285  ? 23.912 53.661  26.715  1.00 14.81 ? 285  PHE A CG  1 
ATOM   2128 C  CD1 . PHE A 1 285  ? 24.334 52.994  27.864  1.00 15.05 ? 285  PHE A CD1 1 
ATOM   2129 C  CD2 . PHE A 1 285  ? 22.557 53.653  26.398  1.00 15.58 ? 285  PHE A CD2 1 
ATOM   2130 C  CE1 . PHE A 1 285  ? 23.424 52.326  28.699  1.00 15.93 ? 285  PHE A CE1 1 
ATOM   2131 C  CE2 . PHE A 1 285  ? 21.619 52.991  27.218  1.00 16.40 ? 285  PHE A CE2 1 
ATOM   2132 C  CZ  . PHE A 1 285  ? 22.053 52.327  28.371  1.00 16.62 ? 285  PHE A CZ  1 
ATOM   2133 N  N   . ASP A 1 286  ? 26.065 57.910  25.428  1.00 13.33 ? 286  ASP A N   1 
ATOM   2134 C  CA  . ASP A 1 286  ? 27.150 58.758  24.970  1.00 12.65 ? 286  ASP A CA  1 
ATOM   2135 C  C   . ASP A 1 286  ? 27.359 59.562  26.260  1.00 13.02 ? 286  ASP A C   1 
ATOM   2136 O  O   . ASP A 1 286  ? 26.709 60.573  26.495  1.00 11.73 ? 286  ASP A O   1 
ATOM   2137 C  CB  . ASP A 1 286  ? 26.712 59.666  23.826  1.00 12.18 ? 286  ASP A CB  1 
ATOM   2138 C  CG  . ASP A 1 286  ? 27.856 60.515  23.314  1.00 13.15 ? 286  ASP A CG  1 
ATOM   2139 O  OD1 . ASP A 1 286  ? 28.845 60.630  24.051  1.00 11.61 ? 286  ASP A OD1 1 
ATOM   2140 O  OD2 . ASP A 1 286  ? 27.765 61.076  22.200  1.00 13.87 ? 286  ASP A OD2 1 
ATOM   2141 N  N   . PHE A 1 287  ? 28.280 59.107  27.103  1.00 12.96 ? 287  PHE A N   1 
ATOM   2142 C  CA  . PHE A 1 287  ? 28.467 59.760  28.366  1.00 13.61 ? 287  PHE A CA  1 
ATOM   2143 C  C   . PHE A 1 287  ? 29.060 61.153  28.375  1.00 14.73 ? 287  PHE A C   1 
ATOM   2144 O  O   . PHE A 1 287  ? 29.233 61.746  29.436  1.00 12.99 ? 287  PHE A O   1 
ATOM   2145 C  CB  . PHE A 1 287  ? 29.205 58.802  29.306  1.00 12.72 ? 287  PHE A CB  1 
ATOM   2146 C  CG  . PHE A 1 287  ? 28.412 57.525  29.580  1.00 13.13 ? 287  PHE A CG  1 
ATOM   2147 C  CD1 . PHE A 1 287  ? 28.591 56.395  28.791  1.00 11.56 ? 287  PHE A CD1 1 
ATOM   2148 C  CD2 . PHE A 1 287  ? 27.447 57.485  30.584  1.00 11.97 ? 287  PHE A CD2 1 
ATOM   2149 C  CE1 . PHE A 1 287  ? 27.830 55.252  28.989  1.00 12.02 ? 287  PHE A CE1 1 
ATOM   2150 C  CE2 . PHE A 1 287  ? 26.659 56.323  30.798  1.00 12.83 ? 287  PHE A CE2 1 
ATOM   2151 C  CZ  . PHE A 1 287  ? 26.857 55.202  29.992  1.00 10.18 ? 287  PHE A CZ  1 
ATOM   2152 N  N   . LYS A 1 288  ? 29.350 61.680  27.191  1.00 15.50 ? 288  LYS A N   1 
ATOM   2153 C  CA  . LYS A 1 288  ? 29.869 63.025  27.089  1.00 14.99 ? 288  LYS A CA  1 
ATOM   2154 C  C   . LYS A 1 288  ? 28.691 64.001  27.022  1.00 15.98 ? 288  LYS A C   1 
ATOM   2155 O  O   . LYS A 1 288  ? 28.884 65.216  27.012  1.00 16.88 ? 288  LYS A O   1 
ATOM   2156 C  CB  . LYS A 1 288  ? 30.738 63.183  25.814  1.00 15.80 ? 288  LYS A CB  1 
ATOM   2157 C  CG  . LYS A 1 288  ? 31.460 64.564  25.753  1.00 15.36 ? 288  LYS A CG  1 
ATOM   2158 C  CD  . LYS A 1 288  ? 32.426 64.717  24.570  1.00 14.36 ? 288  LYS A CD  1 
ATOM   2159 C  CE  . LYS A 1 288  ? 33.187 66.055  24.675  1.00 16.23 ? 288  LYS A CE  1 
ATOM   2160 N  NZ  . LYS A 1 288  ? 34.208 66.223  23.557  1.00 18.86 ? 288  LYS A NZ  1 
ATOM   2161 N  N   . ARG A 1 289  ? 27.460 63.496  26.999  1.00 16.09 ? 289  ARG A N   1 
ATOM   2162 C  CA  . ARG A 1 289  ? 26.326 64.404  26.878  1.00 17.95 ? 289  ARG A CA  1 
ATOM   2163 C  C   . ARG A 1 289  ? 25.554 64.682  28.156  1.00 19.52 ? 289  ARG A C   1 
ATOM   2164 O  O   . ARG A 1 289  ? 24.347 64.863  28.104  1.00 18.93 ? 289  ARG A O   1 
ATOM   2165 C  CB  . ARG A 1 289  ? 25.349 63.878  25.816  1.00 16.63 ? 289  ARG A CB  1 
ATOM   2166 C  CG  . ARG A 1 289  ? 26.012 63.628  24.431  1.00 14.92 ? 289  ARG A CG  1 
ATOM   2167 C  CD  . ARG A 1 289  ? 24.952 63.363  23.387  1.00 13.80 ? 289  ARG A CD  1 
ATOM   2168 N  NE  . ARG A 1 289  ? 25.478 62.958  22.080  1.00 12.97 ? 289  ARG A NE  1 
ATOM   2169 C  CZ  . ARG A 1 289  ? 25.073 63.486  20.924  1.00 13.36 ? 289  ARG A CZ  1 
ATOM   2170 N  NH1 . ARG A 1 289  ? 24.151 64.452  20.914  1.00 10.60 ? 289  ARG A NH1 1 
ATOM   2171 N  NH2 . ARG A 1 289  ? 25.540 63.004  19.773  1.00 12.41 ? 289  ARG A NH2 1 
ATOM   2172 N  N   . MET A 1 290  ? 26.226 64.749  29.297  1.00 22.03 ? 290  MET A N   1 
ATOM   2173 C  CA  . MET A 1 290  ? 25.468 64.983  30.530  1.00 24.42 ? 290  MET A CA  1 
ATOM   2174 C  C   . MET A 1 290  ? 25.347 66.453  30.972  1.00 25.46 ? 290  MET A C   1 
ATOM   2175 O  O   . MET A 1 290  ? 24.540 66.753  31.901  1.00 27.36 ? 290  MET A O   1 
ATOM   2176 C  CB  . MET A 1 290  ? 25.991 64.085  31.669  1.00 24.23 ? 290  MET A CB  1 
ATOM   2177 C  CG  . MET A 1 290  ? 25.746 62.599  31.414  1.00 25.68 ? 290  MET A CG  1 
ATOM   2178 S  SD  . MET A 1 290  ? 26.206 61.442  32.761  1.00 28.89 ? 290  MET A SD  1 
ATOM   2179 C  CE  . MET A 1 290  ? 28.031 61.443  32.571  1.00 26.75 ? 290  MET A CE  1 
ATOM   2180 N  N   . GLY A 1 291  ? 26.106 67.357  30.319  1.00 24.62 ? 291  GLY A N   1 
ATOM   2181 C  CA  . GLY A 1 291  ? 26.031 68.783  30.636  1.00 23.09 ? 291  GLY A CA  1 
ATOM   2182 C  C   . GLY A 1 291  ? 27.298 69.644  30.718  1.00 23.12 ? 291  GLY A C   1 
ATOM   2183 O  O   . GLY A 1 291  ? 27.394 70.714  30.072  1.00 21.92 ? 291  GLY A O   1 
ATOM   2184 N  N   . SER A 1 292  ? 28.273 69.190  31.511  1.00 20.36 ? 292  SER A N   1 
ATOM   2185 C  CA  . SER A 1 292  ? 29.511 69.922  31.712  1.00 19.13 ? 292  SER A CA  1 
ATOM   2186 C  C   . SER A 1 292  ? 30.329 70.114  30.438  1.00 18.83 ? 292  SER A C   1 
ATOM   2187 O  O   . SER A 1 292  ? 31.178 71.004  30.396  1.00 17.92 ? 292  SER A O   1 
ATOM   2188 C  CB  . SER A 1 292  ? 30.367 69.209  32.753  1.00 20.27 ? 292  SER A CB  1 
ATOM   2189 O  OG  . SER A 1 292  ? 30.813 67.953  32.247  1.00 21.51 ? 292  SER A OG  1 
ATOM   2190 N  N   . PHE A 1 293  ? 30.093 69.273  29.421  1.00 17.69 ? 293  PHE A N   1 
ATOM   2191 C  CA  . PHE A 1 293  ? 30.804 69.367  28.145  1.00 17.23 ? 293  PHE A CA  1 
ATOM   2192 C  C   . PHE A 1 293  ? 30.033 70.230  27.131  1.00 17.62 ? 293  PHE A C   1 
ATOM   2193 O  O   . PHE A 1 293  ? 30.468 70.399  26.004  1.00 16.92 ? 293  PHE A O   1 
ATOM   2194 C  CB  . PHE A 1 293  ? 31.041 67.967  27.526  1.00 16.76 ? 293  PHE A CB  1 
ATOM   2195 C  CG  . PHE A 1 293  ? 31.965 67.091  28.328  1.00 16.08 ? 293  PHE A CG  1 
ATOM   2196 C  CD1 . PHE A 1 293  ? 31.455 66.168  29.230  1.00 16.94 ? 293  PHE A CD1 1 
ATOM   2197 C  CD2 . PHE A 1 293  ? 33.337 67.189  28.171  1.00 15.54 ? 293  PHE A CD2 1 
ATOM   2198 C  CE1 . PHE A 1 293  ? 32.315 65.341  29.969  1.00 17.59 ? 293  PHE A CE1 1 
ATOM   2199 C  CE2 . PHE A 1 293  ? 34.218 66.372  28.896  1.00 16.67 ? 293  PHE A CE2 1 
ATOM   2200 C  CZ  . PHE A 1 293  ? 33.709 65.444  29.798  1.00 17.31 ? 293  PHE A CZ  1 
ATOM   2201 N  N   . GLY A 1 294  ? 28.875 70.753  27.526  1.00 18.17 ? 294  GLY A N   1 
ATOM   2202 C  CA  . GLY A 1 294  ? 28.106 71.576  26.604  1.00 19.03 ? 294  GLY A CA  1 
ATOM   2203 C  C   . GLY A 1 294  ? 27.384 70.779  25.521  1.00 19.40 ? 294  GLY A C   1 
ATOM   2204 O  O   . GLY A 1 294  ? 27.069 71.308  24.453  1.00 19.65 ? 294  GLY A O   1 
ATOM   2205 N  N   . LEU A 1 295  ? 27.127 69.501  25.779  1.00 18.50 ? 295  LEU A N   1 
ATOM   2206 C  CA  . LEU A 1 295  ? 26.425 68.659  24.809  1.00 18.69 ? 295  LEU A CA  1 
ATOM   2207 C  C   . LEU A 1 295  ? 25.192 68.066  25.493  1.00 18.42 ? 295  LEU A C   1 
ATOM   2208 O  O   . LEU A 1 295  ? 25.130 67.974  26.723  1.00 18.40 ? 295  LEU A O   1 
ATOM   2209 C  CB  . LEU A 1 295  ? 27.344 67.533  24.300  1.00 19.47 ? 295  LEU A CB  1 
ATOM   2210 C  CG  . LEU A 1 295  ? 28.623 67.943  23.528  1.00 21.06 ? 295  LEU A CG  1 
ATOM   2211 C  CD1 . LEU A 1 295  ? 29.570 66.744  23.373  1.00 19.19 ? 295  LEU A CD1 1 
ATOM   2212 C  CD2 . LEU A 1 295  ? 28.240 68.512  22.150  1.00 20.32 ? 295  LEU A CD2 1 
ATOM   2213 N  N   . SER A 1 296  ? 24.195 67.688  24.709  1.00 18.79 ? 296  SER A N   1 
ATOM   2214 C  CA  . SER A 1 296  ? 23.000 67.097  25.298  1.00 19.17 ? 296  SER A CA  1 
ATOM   2215 C  C   . SER A 1 296  ? 22.387 66.211  24.237  1.00 18.39 ? 296  SER A C   1 
ATOM   2216 O  O   . SER A 1 296  ? 22.873 66.194  23.114  1.00 17.11 ? 296  SER A O   1 
ATOM   2217 C  CB  . SER A 1 296  ? 22.013 68.198  25.744  1.00 18.52 ? 296  SER A CB  1 
ATOM   2218 O  OG  . SER A 1 296  ? 21.682 69.065  24.674  1.00 20.32 ? 296  SER A OG  1 
ATOM   2219 N  N   . CYS A 1 297  ? 21.334 65.485  24.614  1.00 18.22 ? 297  CYS A N   1 
ATOM   2220 C  CA  . CYS A 1 297  ? 20.624 64.569  23.728  1.00 18.57 ? 297  CYS A CA  1 
ATOM   2221 C  C   . CYS A 1 297  ? 19.403 65.240  23.140  1.00 19.56 ? 297  CYS A C   1 
ATOM   2222 O  O   . CYS A 1 297  ? 18.499 65.665  23.859  1.00 19.79 ? 297  CYS A O   1 
ATOM   2223 C  CB  . CYS A 1 297  ? 20.207 63.317  24.498  1.00 17.56 ? 297  CYS A CB  1 
ATOM   2224 S  SG  . CYS A 1 297  ? 21.632 62.224  24.764  1.00 17.58 ? 297  CYS A SG  1 
ATOM   2225 N  N   . PRO A 1 298  ? 19.357 65.348  21.815  1.00 20.34 ? 298  PRO A N   1 
ATOM   2226 C  CA  . PRO A 1 298  ? 18.182 65.998  21.231  1.00 20.69 ? 298  PRO A CA  1 
ATOM   2227 C  C   . PRO A 1 298  ? 16.861 65.248  21.467  1.00 20.91 ? 298  PRO A C   1 
ATOM   2228 O  O   . PRO A 1 298  ? 15.787 65.842  21.352  1.00 19.18 ? 298  PRO A O   1 
ATOM   2229 C  CB  . PRO A 1 298  ? 18.558 66.140  19.748  1.00 21.63 ? 298  PRO A CB  1 
ATOM   2230 C  CG  . PRO A 1 298  ? 19.580 65.037  19.524  1.00 21.77 ? 298  PRO A CG  1 
ATOM   2231 C  CD  . PRO A 1 298  ? 20.390 65.046  20.801  1.00 20.94 ? 298  PRO A CD  1 
ATOM   2232 N  N   . TRP A 1 299  ? 16.945 63.963  21.826  1.00 19.76 ? 299  TRP A N   1 
ATOM   2233 C  CA  . TRP A 1 299  ? 15.738 63.168  22.090  1.00 20.90 ? 299  TRP A CA  1 
ATOM   2234 C  C   . TRP A 1 299  ? 15.189 63.392  23.502  1.00 21.09 ? 299  TRP A C   1 
ATOM   2235 O  O   . TRP A 1 299  ? 14.280 62.699  23.921  1.00 21.69 ? 299  TRP A O   1 
ATOM   2236 C  CB  . TRP A 1 299  ? 16.010 61.670  21.827  1.00 18.90 ? 299  TRP A CB  1 
ATOM   2237 C  CG  . TRP A 1 299  ? 16.370 61.453  20.372  1.00 17.80 ? 299  TRP A CG  1 
ATOM   2238 C  CD1 . TRP A 1 299  ? 15.507 61.266  19.342  1.00 17.42 ? 299  TRP A CD1 1 
ATOM   2239 C  CD2 . TRP A 1 299  ? 17.684 61.531  19.785  1.00 18.66 ? 299  TRP A CD2 1 
ATOM   2240 N  NE1 . TRP A 1 299  ? 16.189 61.224  18.148  1.00 19.74 ? 299  TRP A NE1 1 
ATOM   2241 C  CE2 . TRP A 1 299  ? 17.525 61.386  18.389  1.00 18.43 ? 299  TRP A CE2 1 
ATOM   2242 C  CE3 . TRP A 1 299  ? 18.977 61.710  20.307  1.00 16.37 ? 299  TRP A CE3 1 
ATOM   2243 C  CZ2 . TRP A 1 299  ? 18.613 61.415  17.496  1.00 18.89 ? 299  TRP A CZ2 1 
ATOM   2244 C  CZ3 . TRP A 1 299  ? 20.054 61.734  19.425  1.00 17.53 ? 299  TRP A CZ3 1 
ATOM   2245 C  CH2 . TRP A 1 299  ? 19.866 61.588  18.032  1.00 16.99 ? 299  TRP A CH2 1 
ATOM   2246 N  N   . LYS A 1 300  ? 15.774 64.352  24.224  1.00 22.78 ? 300  LYS A N   1 
ATOM   2247 C  CA  . LYS A 1 300  ? 15.331 64.745  25.569  1.00 24.06 ? 300  LYS A CA  1 
ATOM   2248 C  C   . LYS A 1 300  ? 15.531 63.795  26.755  1.00 23.86 ? 300  LYS A C   1 
ATOM   2249 O  O   . LYS A 1 300  ? 15.027 64.055  27.847  1.00 24.58 ? 300  LYS A O   1 
ATOM   2250 C  CB  . LYS A 1 300  ? 13.862 65.190  25.503  1.00 24.49 ? 300  LYS A CB  1 
ATOM   2251 C  CG  . LYS A 1 300  ? 13.645 66.402  24.599  1.00 27.81 ? 300  LYS A CG  1 
ATOM   2252 C  CD  . LYS A 1 300  ? 12.155 66.693  24.432  1.00 30.45 ? 300  LYS A CD  1 
ATOM   2253 C  CE  . LYS A 1 300  ? 11.909 68.083  23.875  1.00 32.30 ? 300  LYS A CE  1 
ATOM   2254 N  NZ  . LYS A 1 300  ? 12.830 68.395  22.733  1.00 33.91 ? 300  LYS A NZ  1 
ATOM   2255 N  N   . VAL A 1 301  ? 16.234 62.685  26.556  1.00 22.86 ? 301  VAL A N   1 
ATOM   2256 C  CA  . VAL A 1 301  ? 16.527 61.787  27.659  1.00 22.43 ? 301  VAL A CA  1 
ATOM   2257 C  C   . VAL A 1 301  ? 18.053 61.806  27.678  1.00 22.87 ? 301  VAL A C   1 
ATOM   2258 O  O   . VAL A 1 301  ? 18.694 61.388  26.717  1.00 22.26 ? 301  VAL A O   1 
ATOM   2259 C  CB  . VAL A 1 301  ? 16.021 60.361  27.414  1.00 22.99 ? 301  VAL A CB  1 
ATOM   2260 C  CG1 . VAL A 1 301  ? 16.406 59.499  28.588  1.00 22.19 ? 301  VAL A CG1 1 
ATOM   2261 C  CG2 . VAL A 1 301  ? 14.474 60.360  27.239  1.00 22.83 ? 301  VAL A CG2 1 
ATOM   2262 N  N   . PRO A 1 302  ? 18.649 62.306  28.770  1.00 22.28 ? 302  PRO A N   1 
ATOM   2263 C  CA  . PRO A 1 302  ? 20.102 62.409  28.924  1.00 21.63 ? 302  PRO A CA  1 
ATOM   2264 C  C   . PRO A 1 302  ? 20.782 61.152  29.410  1.00 21.06 ? 302  PRO A C   1 
ATOM   2265 O  O   . PRO A 1 302  ? 20.132 60.232  29.888  1.00 19.78 ? 302  PRO A O   1 
ATOM   2266 C  CB  . PRO A 1 302  ? 20.244 63.542  29.931  1.00 22.14 ? 302  PRO A CB  1 
ATOM   2267 C  CG  . PRO A 1 302  ? 19.113 63.259  30.874  1.00 22.76 ? 302  PRO A CG  1 
ATOM   2268 C  CD  . PRO A 1 302  ? 17.956 62.851  29.956  1.00 22.89 ? 302  PRO A CD  1 
ATOM   2269 N  N   . PRO A 1 303  ? 22.113 61.073  29.240  1.00 20.64 ? 303  PRO A N   1 
ATOM   2270 C  CA  . PRO A 1 303  ? 22.734 59.843  29.750  1.00 20.27 ? 303  PRO A CA  1 
ATOM   2271 C  C   . PRO A 1 303  ? 22.805 59.979  31.281  1.00 20.16 ? 303  PRO A C   1 
ATOM   2272 O  O   . PRO A 1 303  ? 22.766 61.096  31.818  1.00 17.84 ? 303  PRO A O   1 
ATOM   2273 C  CB  . PRO A 1 303  ? 24.131 59.836  29.109  1.00 20.80 ? 303  PRO A CB  1 
ATOM   2274 C  CG  . PRO A 1 303  ? 24.380 61.298  28.701  1.00 21.51 ? 303  PRO A CG  1 
ATOM   2275 C  CD  . PRO A 1 303  ? 23.011 61.849  28.363  1.00 20.05 ? 303  PRO A CD  1 
ATOM   2276 N  N   . ARG A 1 304  ? 22.914 58.854  31.975  1.00 20.91 ? 304  ARG A N   1 
ATOM   2277 C  CA  . ARG A 1 304  ? 23.044 58.867  33.430  1.00 22.19 ? 304  ARG A CA  1 
ATOM   2278 C  C   . ARG A 1 304  ? 24.238 58.030  33.847  1.00 21.37 ? 304  ARG A C   1 
ATOM   2279 O  O   . ARG A 1 304  ? 24.459 56.950  33.314  1.00 20.71 ? 304  ARG A O   1 
ATOM   2280 C  CB  . ARG A 1 304  ? 21.770 58.324  34.091  1.00 25.28 ? 304  ARG A CB  1 
ATOM   2281 C  CG  . ARG A 1 304  ? 20.723 59.396  34.290  1.00 28.06 ? 304  ARG A CG  1 
ATOM   2282 C  CD  . ARG A 1 304  ? 19.523 58.867  35.059  1.00 31.69 ? 304  ARG A CD  1 
ATOM   2283 N  NE  . ARG A 1 304  ? 18.877 57.766  34.357  1.00 35.23 ? 304  ARG A NE  1 
ATOM   2284 C  CZ  . ARG A 1 304  ? 18.644 56.572  34.894  1.00 37.26 ? 304  ARG A CZ  1 
ATOM   2285 N  NH1 . ARG A 1 304  ? 19.002 56.303  36.153  1.00 37.24 ? 304  ARG A NH1 1 
ATOM   2286 N  NH2 . ARG A 1 304  ? 18.048 55.643  34.158  1.00 39.57 ? 304  ARG A NH2 1 
ATOM   2287 N  N   . THR A 1 305  ? 25.020 58.532  34.798  1.00 20.82 ? 305  THR A N   1 
ATOM   2288 C  CA  . THR A 1 305  ? 26.192 57.801  35.265  1.00 19.90 ? 305  THR A CA  1 
ATOM   2289 C  C   . THR A 1 305  ? 25.768 56.421  35.697  1.00 18.97 ? 305  THR A C   1 
ATOM   2290 O  O   . THR A 1 305  ? 24.736 56.288  36.345  1.00 19.91 ? 305  THR A O   1 
ATOM   2291 C  CB  . THR A 1 305  ? 26.848 58.547  36.427  1.00 20.25 ? 305  THR A CB  1 
ATOM   2292 O  OG1 . THR A 1 305  ? 27.337 59.792  35.925  1.00 21.85 ? 305  THR A OG1 1 
ATOM   2293 C  CG2 . THR A 1 305  ? 27.994 57.747  37.034  1.00 19.88 ? 305  THR A CG2 1 
ATOM   2294 N  N   . ILE A 1 306  ? 26.532 55.394  35.313  1.00 18.07 ? 306  ILE A N   1 
ATOM   2295 C  CA  . ILE A 1 306  ? 26.189 54.015  35.670  1.00 17.70 ? 306  ILE A CA  1 
ATOM   2296 C  C   . ILE A 1 306  ? 26.607 53.757  37.108  1.00 18.34 ? 306  ILE A C   1 
ATOM   2297 O  O   . ILE A 1 306  ? 27.685 54.176  37.531  1.00 16.70 ? 306  ILE A O   1 
ATOM   2298 C  CB  . ILE A 1 306  ? 26.896 52.983  34.767  1.00 16.64 ? 306  ILE A CB  1 
ATOM   2299 C  CG1 . ILE A 1 306  ? 26.655 53.308  33.285  1.00 15.94 ? 306  ILE A CG1 1 
ATOM   2300 C  CG2 . ILE A 1 306  ? 26.372 51.542  35.082  1.00 17.46 ? 306  ILE A CG2 1 
ATOM   2301 C  CD1 . ILE A 1 306  ? 25.216 53.216  32.853  1.00 14.91 ? 306  ILE A CD1 1 
ATOM   2302 N  N   . SER A 1 307  ? 25.752 53.063  37.858  1.00 19.35 ? 307  SER A N   1 
ATOM   2303 C  CA  . SER A 1 307  ? 26.030 52.745  39.260  1.00 20.41 ? 307  SER A CA  1 
ATOM   2304 C  C   . SER A 1 307  ? 25.532 51.350  39.517  1.00 21.56 ? 307  SER A C   1 
ATOM   2305 O  O   . SER A 1 307  ? 24.914 50.737  38.647  1.00 21.09 ? 307  SER A O   1 
ATOM   2306 C  CB  . SER A 1 307  ? 25.248 53.664  40.179  1.00 20.03 ? 307  SER A CB  1 
ATOM   2307 O  OG  . SER A 1 307  ? 23.857 53.453  39.972  1.00 17.28 ? 307  SER A OG  1 
ATOM   2308 N  N   . ASP A 1 308  ? 25.766 50.864  40.726  1.00 22.62 ? 308  ASP A N   1 
ATOM   2309 C  CA  . ASP A 1 308  ? 25.311 49.536  41.077  1.00 24.54 ? 308  ASP A CA  1 
ATOM   2310 C  C   . ASP A 1 308  ? 23.801 49.464  41.124  1.00 23.14 ? 308  ASP A C   1 
ATOM   2311 O  O   . ASP A 1 308  ? 23.265 48.407  40.899  1.00 23.70 ? 308  ASP A O   1 
ATOM   2312 C  CB  . ASP A 1 308  ? 25.888 49.087  42.418  1.00 27.35 ? 308  ASP A CB  1 
ATOM   2313 C  CG  . ASP A 1 308  ? 27.382 48.883  42.357  1.00 29.99 ? 308  ASP A CG  1 
ATOM   2314 O  OD1 . ASP A 1 308  ? 27.901 48.707  41.242  1.00 31.44 ? 308  ASP A OD1 1 
ATOM   2315 O  OD2 . ASP A 1 308  ? 28.044 48.885  43.415  1.00 33.63 ? 308  ASP A OD2 1 
ATOM   2316 N  N   . GLN A 1 309  ? 23.130 50.589  41.387  1.00 23.37 ? 309  GLN A N   1 
ATOM   2317 C  CA  . GLN A 1 309  ? 21.661 50.642  41.447  1.00 23.38 ? 309  GLN A CA  1 
ATOM   2318 C  C   . GLN A 1 309  ? 20.976 50.764  40.097  1.00 22.62 ? 309  GLN A C   1 
ATOM   2319 O  O   . GLN A 1 309  ? 19.761 50.551  39.995  1.00 23.02 ? 309  GLN A O   1 
ATOM   2320 C  CB  . GLN A 1 309  ? 21.159 51.833  42.282  1.00 24.64 ? 309  GLN A CB  1 
ATOM   2321 C  CG  . GLN A 1 309  ? 21.472 51.783  43.764  1.00 26.79 ? 309  GLN A CG  1 
ATOM   2322 C  CD  . GLN A 1 309  ? 22.961 51.887  44.029  1.00 28.05 ? 309  GLN A CD  1 
ATOM   2323 O  OE1 . GLN A 1 309  ? 23.631 52.776  43.494  1.00 27.95 ? 309  GLN A OE1 1 
ATOM   2324 N  NE2 . GLN A 1 309  ? 23.492 50.975  44.853  1.00 27.99 ? 309  GLN A NE2 1 
ATOM   2325 N  N   . ASN A 1 310  ? 21.694 51.162  39.051  1.00 20.87 ? 310  ASN A N   1 
ATOM   2326 C  CA  . ASN A 1 310  ? 20.972 51.279  37.788  1.00 19.63 ? 310  ASN A CA  1 
ATOM   2327 C  C   . ASN A 1 310  ? 21.551 50.466  36.672  1.00 19.04 ? 310  ASN A C   1 
ATOM   2328 O  O   . ASN A 1 310  ? 20.963 50.416  35.606  1.00 19.44 ? 310  ASN A O   1 
ATOM   2329 C  CB  . ASN A 1 310  ? 20.854 52.746  37.324  1.00 18.09 ? 310  ASN A CB  1 
ATOM   2330 C  CG  . ASN A 1 310  ? 22.202 53.371  36.926  1.00 18.25 ? 310  ASN A CG  1 
ATOM   2331 O  OD1 . ASN A 1 310  ? 23.193 52.658  36.654  1.00 15.78 ? 310  ASN A OD1 1 
ATOM   2332 N  ND2 . ASN A 1 310  ? 22.240 54.711  36.879  1.00 17.87 ? 310  ASN A ND2 1 
ATOM   2333 N  N   . VAL A 1 311  ? 22.693 49.827  36.921  1.00 20.13 ? 311  VAL A N   1 
ATOM   2334 C  CA  . VAL A 1 311  ? 23.385 49.059  35.874  1.00 18.12 ? 311  VAL A CA  1 
ATOM   2335 C  C   . VAL A 1 311  ? 22.559 47.932  35.260  1.00 18.50 ? 311  VAL A C   1 
ATOM   2336 O  O   . VAL A 1 311  ? 22.679 47.669  34.060  1.00 17.74 ? 311  VAL A O   1 
ATOM   2337 C  CB  . VAL A 1 311  ? 24.713 48.505  36.387  1.00 18.08 ? 311  VAL A CB  1 
ATOM   2338 C  CG1 . VAL A 1 311  ? 24.474 47.509  37.532  1.00 18.26 ? 311  VAL A CG1 1 
ATOM   2339 C  CG2 . VAL A 1 311  ? 25.507 47.881  35.225  1.00 17.80 ? 311  VAL A CG2 1 
ATOM   2340 N  N   . ALA A 1 312  ? 21.708 47.284  36.060  1.00 17.48 ? 312  ALA A N   1 
ATOM   2341 C  CA  . ALA A 1 312  ? 20.892 46.192  35.545  1.00 17.77 ? 312  ALA A CA  1 
ATOM   2342 C  C   . ALA A 1 312  ? 19.891 46.727  34.561  1.00 18.02 ? 312  ALA A C   1 
ATOM   2343 O  O   . ALA A 1 312  ? 19.712 46.154  33.506  1.00 18.41 ? 312  ALA A O   1 
ATOM   2344 C  CB  . ALA A 1 312  ? 20.163 45.433  36.695  1.00 19.46 ? 312  ALA A CB  1 
ATOM   2345 N  N   . ALA A 1 313  ? 19.248 47.837  34.899  1.00 17.88 ? 313  ALA A N   1 
ATOM   2346 C  CA  . ALA A 1 313  ? 18.260 48.454  34.024  1.00 18.44 ? 313  ALA A CA  1 
ATOM   2347 C  C   . ALA A 1 313  ? 18.924 49.114  32.789  1.00 18.53 ? 313  ALA A C   1 
ATOM   2348 O  O   . ALA A 1 313  ? 18.377 49.098  31.680  1.00 17.60 ? 313  ALA A O   1 
ATOM   2349 C  CB  . ALA A 1 313  ? 17.464 49.496  34.798  1.00 17.12 ? 313  ALA A CB  1 
ATOM   2350 N  N   . ARG A 1 314  ? 20.076 49.731  33.001  1.00 17.79 ? 314  ARG A N   1 
ATOM   2351 C  CA  . ARG A 1 314  ? 20.790 50.378  31.892  1.00 18.73 ? 314  ARG A CA  1 
ATOM   2352 C  C   . ARG A 1 314  ? 21.266 49.259  30.932  1.00 17.60 ? 314  ARG A C   1 
ATOM   2353 O  O   . ARG A 1 314  ? 21.147 49.376  29.718  1.00 17.66 ? 314  ARG A O   1 
ATOM   2354 C  CB  . ARG A 1 314  ? 21.983 51.142  32.445  1.00 18.64 ? 314  ARG A CB  1 
ATOM   2355 C  CG  . ARG A 1 314  ? 21.610 52.338  33.301  1.00 20.43 ? 314  ARG A CG  1 
ATOM   2356 C  CD  . ARG A 1 314  ? 21.271 53.573  32.460  1.00 21.79 ? 314  ARG A CD  1 
ATOM   2357 N  NE  . ARG A 1 314  ? 19.883 53.601  32.032  1.00 22.85 ? 314  ARG A NE  1 
ATOM   2358 C  CZ  . ARG A 1 314  ? 19.361 54.523  31.235  1.00 23.14 ? 314  ARG A CZ  1 
ATOM   2359 N  NH1 . ARG A 1 314  ? 20.115 55.506  30.752  1.00 24.02 ? 314  ARG A NH1 1 
ATOM   2360 N  NH2 . ARG A 1 314  ? 18.066 54.489  30.942  1.00 24.03 ? 314  ARG A NH2 1 
ATOM   2361 N  N   . SER A 1 315  ? 21.796 48.175  31.488  1.00 18.15 ? 315  SER A N   1 
ATOM   2362 C  CA  . SER A 1 315  ? 22.256 47.055  30.670  1.00 18.99 ? 315  SER A CA  1 
ATOM   2363 C  C   . SER A 1 315  ? 21.080 46.429  29.897  1.00 20.89 ? 315  SER A C   1 
ATOM   2364 O  O   . SER A 1 315  ? 21.243 46.024  28.751  1.00 21.95 ? 315  SER A O   1 
ATOM   2365 C  CB  . SER A 1 315  ? 22.943 46.003  31.549  1.00 17.98 ? 315  SER A CB  1 
ATOM   2366 O  OG  . SER A 1 315  ? 24.163 46.507  32.076  1.00 15.48 ? 315  SER A OG  1 
ATOM   2367 N  N   . ASP A 1 316  ? 19.903 46.350  30.519  1.00 21.63 ? 316  ASP A N   1 
ATOM   2368 C  CA  . ASP A 1 316  ? 18.708 45.800  29.856  1.00 22.85 ? 316  ASP A CA  1 
ATOM   2369 C  C   . ASP A 1 316  ? 18.456 46.577  28.580  1.00 21.37 ? 316  ASP A C   1 
ATOM   2370 O  O   . ASP A 1 316  ? 18.216 45.993  27.523  1.00 19.96 ? 316  ASP A O   1 
ATOM   2371 C  CB  . ASP A 1 316  ? 17.430 45.991  30.694  1.00 26.34 ? 316  ASP A CB  1 
ATOM   2372 C  CG  . ASP A 1 316  ? 17.341 45.072  31.898  1.00 29.19 ? 316  ASP A CG  1 
ATOM   2373 O  OD1 . ASP A 1 316  ? 16.514 45.381  32.798  1.00 30.88 ? 316  ASP A OD1 1 
ATOM   2374 O  OD2 . ASP A 1 316  ? 18.062 44.052  31.943  1.00 31.73 ? 316  ASP A OD2 1 
ATOM   2375 N  N   . LEU A 1 317  ? 18.459 47.903  28.699  1.00 20.56 ? 317  LEU A N   1 
ATOM   2376 C  CA  . LEU A 1 317  ? 18.202 48.763  27.539  1.00 20.01 ? 317  LEU A CA  1 
ATOM   2377 C  C   . LEU A 1 317  ? 19.260 48.619  26.454  1.00 18.15 ? 317  LEU A C   1 
ATOM   2378 O  O   . LEU A 1 317  ? 18.935 48.463  25.278  1.00 18.08 ? 317  LEU A O   1 
ATOM   2379 C  CB  . LEU A 1 317  ? 18.133 50.244  27.942  1.00 21.00 ? 317  LEU A CB  1 
ATOM   2380 C  CG  . LEU A 1 317  ? 16.798 50.899  28.297  1.00 22.48 ? 317  LEU A CG  1 
ATOM   2381 C  CD1 . LEU A 1 317  ? 17.066 52.388  28.613  1.00 23.61 ? 317  LEU A CD1 1 
ATOM   2382 C  CD2 . LEU A 1 317  ? 15.794 50.781  27.144  1.00 21.97 ? 317  LEU A CD2 1 
ATOM   2383 N  N   . LEU A 1 318  ? 20.517 48.657  26.871  1.00 16.98 ? 318  LEU A N   1 
ATOM   2384 C  CA  . LEU A 1 318  ? 21.631 48.591  25.952  1.00 16.23 ? 318  LEU A CA  1 
ATOM   2385 C  C   . LEU A 1 318  ? 21.711 47.256  25.266  1.00 16.40 ? 318  LEU A C   1 
ATOM   2386 O  O   . LEU A 1 318  ? 21.825 47.197  24.042  1.00 15.82 ? 318  LEU A O   1 
ATOM   2387 C  CB  . LEU A 1 318  ? 22.949 48.885  26.677  1.00 15.27 ? 318  LEU A CB  1 
ATOM   2388 C  CG  . LEU A 1 318  ? 24.210 48.972  25.783  1.00 15.35 ? 318  LEU A CG  1 
ATOM   2389 C  CD1 . LEU A 1 318  ? 24.033 50.100  24.743  1.00 15.24 ? 318  LEU A CD1 1 
ATOM   2390 C  CD2 . LEU A 1 318  ? 25.442 49.242  26.648  1.00 13.79 ? 318  LEU A CD2 1 
ATOM   2391 N  N   . VAL A 1 319  ? 21.653 46.177  26.034  1.00 15.25 ? 319  VAL A N   1 
ATOM   2392 C  CA  . VAL A 1 319  ? 21.724 44.865  25.413  1.00 15.92 ? 319  VAL A CA  1 
ATOM   2393 C  C   . VAL A 1 319  ? 20.575 44.687  24.409  1.00 16.28 ? 319  VAL A C   1 
ATOM   2394 O  O   . VAL A 1 319  ? 20.751 44.050  23.367  1.00 16.92 ? 319  VAL A O   1 
ATOM   2395 C  CB  . VAL A 1 319  ? 21.728 43.734  26.484  1.00 15.53 ? 319  VAL A CB  1 
ATOM   2396 C  CG1 . VAL A 1 319  ? 21.528 42.364  25.820  1.00 15.69 ? 319  VAL A CG1 1 
ATOM   2397 C  CG2 . VAL A 1 319  ? 23.069 43.766  27.258  1.00 16.36 ? 319  VAL A CG2 1 
ATOM   2398 N  N   . ASP A 1 320  ? 19.411 45.279  24.673  1.00 16.38 ? 320  ASP A N   1 
ATOM   2399 C  CA  . ASP A 1 320  ? 18.282 45.117  23.734  1.00 16.96 ? 320  ASP A CA  1 
ATOM   2400 C  C   . ASP A 1 320  ? 18.576 45.840  22.400  1.00 16.49 ? 320  ASP A C   1 
ATOM   2401 O  O   . ASP A 1 320  ? 18.238 45.339  21.319  1.00 15.77 ? 320  ASP A O   1 
ATOM   2402 C  CB  . ASP A 1 320  ? 16.999 45.654  24.375  1.00 18.63 ? 320  ASP A CB  1 
ATOM   2403 C  CG  . ASP A 1 320  ? 15.835 45.675  23.435  1.00 17.80 ? 320  ASP A CG  1 
ATOM   2404 O  OD1 . ASP A 1 320  ? 15.373 46.781  23.068  1.00 18.05 ? 320  ASP A OD1 1 
ATOM   2405 O  OD2 . ASP A 1 320  ? 15.371 44.581  23.080  1.00 20.42 ? 320  ASP A OD2 1 
ATOM   2406 N  N   . GLN A 1 321  ? 19.187 47.023  22.481  1.00 14.62 ? 321  GLN A N   1 
ATOM   2407 C  CA  . GLN A 1 321  ? 19.572 47.754  21.258  1.00 14.38 ? 321  GLN A CA  1 
ATOM   2408 C  C   . GLN A 1 321  ? 20.591 46.906  20.486  1.00 14.36 ? 321  GLN A C   1 
ATOM   2409 O  O   . GLN A 1 321  ? 20.476 46.726  19.261  1.00 13.40 ? 321  GLN A O   1 
ATOM   2410 C  CB  . GLN A 1 321  ? 20.221 49.094  21.603  1.00 14.64 ? 321  GLN A CB  1 
ATOM   2411 C  CG  . GLN A 1 321  ? 19.208 50.174  22.017  1.00 14.57 ? 321  GLN A CG  1 
ATOM   2412 C  CD  . GLN A 1 321  ? 18.135 50.348  20.969  1.00 15.61 ? 321  GLN A CD  1 
ATOM   2413 O  OE1 . GLN A 1 321  ? 18.411 50.751  19.842  1.00 15.96 ? 321  GLN A OE1 1 
ATOM   2414 N  NE2 . GLN A 1 321  ? 16.894 50.023  21.332  1.00 16.02 ? 321  GLN A NE2 1 
ATOM   2415 N  N   . TRP A 1 322  ? 21.580 46.375  21.210  1.00 13.32 ? 322  TRP A N   1 
ATOM   2416 C  CA  . TRP A 1 322  ? 22.621 45.550  20.579  1.00 13.27 ? 322  TRP A CA  1 
ATOM   2417 C  C   . TRP A 1 322  ? 22.022 44.340  19.862  1.00 13.42 ? 322  TRP A C   1 
ATOM   2418 O  O   . TRP A 1 322  ? 22.384 44.034  18.722  1.00 13.92 ? 322  TRP A O   1 
ATOM   2419 C  CB  . TRP A 1 322  ? 23.647 45.045  21.602  1.00 10.54 ? 322  TRP A CB  1 
ATOM   2420 C  CG  . TRP A 1 322  ? 24.605 46.079  22.129  1.00 10.54 ? 322  TRP A CG  1 
ATOM   2421 C  CD1 . TRP A 1 322  ? 24.795 47.346  21.663  1.00 11.01 ? 322  TRP A CD1 1 
ATOM   2422 C  CD2 . TRP A 1 322  ? 25.507 45.916  23.222  1.00 10.33 ? 322  TRP A CD2 1 
ATOM   2423 N  NE1 . TRP A 1 322  ? 25.768 47.988  22.404  1.00 11.97 ? 322  TRP A NE1 1 
ATOM   2424 C  CE2 . TRP A 1 322  ? 26.222 47.129  23.366  1.00 10.76 ? 322  TRP A CE2 1 
ATOM   2425 C  CE3 . TRP A 1 322  ? 25.783 44.861  24.098  1.00 11.62 ? 322  TRP A CE3 1 
ATOM   2426 C  CZ2 . TRP A 1 322  ? 27.199 47.314  24.358  1.00 11.02 ? 322  TRP A CZ2 1 
ATOM   2427 C  CZ3 . TRP A 1 322  ? 26.757 45.037  25.091  1.00 9.86  ? 322  TRP A CZ3 1 
ATOM   2428 C  CH2 . TRP A 1 322  ? 27.452 46.250  25.215  1.00 12.34 ? 322  TRP A CH2 1 
ATOM   2429 N  N   . LYS A 1 323  ? 21.112 43.647  20.530  1.00 13.21 ? 323  LYS A N   1 
ATOM   2430 C  CA  . LYS A 1 323  ? 20.533 42.453  19.897  1.00 14.90 ? 323  LYS A CA  1 
ATOM   2431 C  C   . LYS A 1 323  ? 19.691 42.811  18.692  1.00 13.90 ? 323  LYS A C   1 
ATOM   2432 O  O   . LYS A 1 323  ? 19.620 42.044  17.750  1.00 14.35 ? 323  LYS A O   1 
ATOM   2433 C  CB  . LYS A 1 323  ? 19.743 41.624  20.926  1.00 15.43 ? 323  LYS A CB  1 
ATOM   2434 C  CG  . LYS A 1 323  ? 20.712 40.781  21.791  1.00 16.23 ? 323  LYS A CG  1 
ATOM   2435 C  CD  . LYS A 1 323  ? 20.001 40.008  22.900  1.00 19.46 ? 323  LYS A CD  1 
ATOM   2436 C  CE  . LYS A 1 323  ? 21.021 39.179  23.714  1.00 19.59 ? 323  LYS A CE  1 
ATOM   2437 N  NZ  . LYS A 1 323  ? 20.305 38.289  24.661  1.00 23.98 ? 323  LYS A NZ  1 
ATOM   2438 N  N   . LYS A 1 324  ? 19.049 43.971  18.718  1.00 13.69 ? 324  LYS A N   1 
ATOM   2439 C  CA  . LYS A 1 324  ? 18.281 44.398  17.555  1.00 13.64 ? 324  LYS A CA  1 
ATOM   2440 C  C   . LYS A 1 324  ? 19.268 44.671  16.412  1.00 12.94 ? 324  LYS A C   1 
ATOM   2441 O  O   . LYS A 1 324  ? 19.072 44.199  15.297  1.00 14.17 ? 324  LYS A O   1 
ATOM   2442 C  CB  . LYS A 1 324  ? 17.454 45.650  17.891  1.00 13.97 ? 324  LYS A CB  1 
ATOM   2443 C  CG  . LYS A 1 324  ? 16.225 45.310  18.762  1.00 14.99 ? 324  LYS A CG  1 
ATOM   2444 C  CD  . LYS A 1 324  ? 15.505 46.546  19.283  1.00 14.79 ? 324  LYS A CD  1 
ATOM   2445 C  CE  . LYS A 1 324  ? 14.300 46.127  20.155  1.00 15.17 ? 324  LYS A CE  1 
ATOM   2446 N  NZ  . LYS A 1 324  ? 13.608 47.308  20.756  1.00 16.23 ? 324  LYS A NZ  1 
ATOM   2447 N  N   . LYS A 1 325  ? 20.340 45.417  16.690  1.00 11.70 ? 325  LYS A N   1 
ATOM   2448 C  CA  . LYS A 1 325  ? 21.335 45.694  15.647  1.00 11.11 ? 325  LYS A CA  1 
ATOM   2449 C  C   . LYS A 1 325  ? 21.893 44.368  15.106  1.00 11.90 ? 325  LYS A C   1 
ATOM   2450 O  O   . LYS A 1 325  ? 22.103 44.224  13.893  1.00 10.69 ? 325  LYS A O   1 
ATOM   2451 C  CB  . LYS A 1 325  ? 22.492 46.556  16.194  1.00 9.83  ? 325  LYS A CB  1 
ATOM   2452 C  CG  . LYS A 1 325  ? 23.413 47.164  15.100  1.00 9.46  ? 325  LYS A CG  1 
ATOM   2453 C  CD  . LYS A 1 325  ? 24.619 47.961  15.693  1.00 7.89  ? 325  LYS A CD  1 
ATOM   2454 C  CE  . LYS A 1 325  ? 25.376 48.742  14.592  1.00 9.66  ? 325  LYS A CE  1 
ATOM   2455 N  NZ  . LYS A 1 325  ? 26.588 49.392  15.137  1.00 9.35  ? 325  LYS A NZ  1 
ATOM   2456 N  N   . ALA A 1 326  ? 22.122 43.398  15.995  1.00 11.88 ? 326  ALA A N   1 
ATOM   2457 C  CA  . ALA A 1 326  ? 22.658 42.105  15.564  1.00 13.51 ? 326  ALA A CA  1 
ATOM   2458 C  C   . ALA A 1 326  ? 21.743 41.360  14.571  1.00 12.89 ? 326  ALA A C   1 
ATOM   2459 O  O   . ALA A 1 326  ? 22.206 40.551  13.780  1.00 14.46 ? 326  ALA A O   1 
ATOM   2460 C  CB  . ALA A 1 326  ? 22.953 41.211  16.790  1.00 12.65 ? 326  ALA A CB  1 
ATOM   2461 N  N   . GLU A 1 327  ? 20.444 41.620  14.602  1.00 14.55 ? 327  GLU A N   1 
ATOM   2462 C  CA  . GLU A 1 327  ? 19.546 40.937  13.664  1.00 14.33 ? 327  GLU A CA  1 
ATOM   2463 C  C   . GLU A 1 327  ? 19.808 41.298  12.209  1.00 13.98 ? 327  GLU A C   1 
ATOM   2464 O  O   . GLU A 1 327  ? 19.371 40.583  11.306  1.00 13.85 ? 327  GLU A O   1 
ATOM   2465 C  CB  . GLU A 1 327  ? 18.087 41.296  13.941  1.00 16.01 ? 327  GLU A CB  1 
ATOM   2466 C  CG  . GLU A 1 327  ? 17.500 40.529  15.072  1.00 18.10 ? 327  GLU A CG  1 
ATOM   2467 C  CD  . GLU A 1 327  ? 17.483 39.046  14.788  1.00 17.73 ? 327  GLU A CD  1 
ATOM   2468 O  OE1 . GLU A 1 327  ? 16.813 38.617  13.824  1.00 17.64 ? 327  GLU A OE1 1 
ATOM   2469 O  OE2 . GLU A 1 327  ? 18.158 38.326  15.531  1.00 19.21 ? 327  GLU A OE2 1 
ATOM   2470 N  N   . LEU A 1 328  ? 20.483 42.423  11.982  1.00 13.04 ? 328  LEU A N   1 
ATOM   2471 C  CA  . LEU A 1 328  ? 20.741 42.895  10.627  1.00 12.17 ? 328  LEU A CA  1 
ATOM   2472 C  C   . LEU A 1 328  ? 21.971 42.261  10.004  1.00 12.80 ? 328  LEU A C   1 
ATOM   2473 O  O   . LEU A 1 328  ? 22.263 42.498  8.816   1.00 12.98 ? 328  LEU A O   1 
ATOM   2474 C  CB  . LEU A 1 328  ? 20.894 44.420  10.650  1.00 12.69 ? 328  LEU A CB  1 
ATOM   2475 C  CG  . LEU A 1 328  ? 19.783 45.225  11.348  1.00 14.04 ? 328  LEU A CG  1 
ATOM   2476 C  CD1 . LEU A 1 328  ? 20.051 46.748  11.135  1.00 13.40 ? 328  LEU A CD1 1 
ATOM   2477 C  CD2 . LEU A 1 328  ? 18.378 44.858  10.767  1.00 14.48 ? 328  LEU A CD2 1 
ATOM   2478 N  N   . TYR A 1 329  ? 22.698 41.462  10.788  1.00 11.95 ? 329  TYR A N   1 
ATOM   2479 C  CA  . TYR A 1 329  ? 23.907 40.804  10.300  1.00 12.74 ? 329  TYR A CA  1 
ATOM   2480 C  C   . TYR A 1 329  ? 23.841 39.297  10.466  1.00 13.38 ? 329  TYR A C   1 
ATOM   2481 O  O   . TYR A 1 329  ? 22.954 38.793  11.154  1.00 14.03 ? 329  TYR A O   1 
ATOM   2482 C  CB  . TYR A 1 329  ? 25.149 41.378  10.976  1.00 11.30 ? 329  TYR A CB  1 
ATOM   2483 C  CG  . TYR A 1 329  ? 25.337 42.840  10.631  1.00 12.03 ? 329  TYR A CG  1 
ATOM   2484 C  CD1 . TYR A 1 329  ? 24.720 43.839  11.392  1.00 11.94 ? 329  TYR A CD1 1 
ATOM   2485 C  CD2 . TYR A 1 329  ? 26.096 43.218  9.521   1.00 10.81 ? 329  TYR A CD2 1 
ATOM   2486 C  CE1 . TYR A 1 329  ? 24.848 45.179  11.053  1.00 12.19 ? 329  TYR A CE1 1 
ATOM   2487 C  CE2 . TYR A 1 329  ? 26.237 44.541  9.168   1.00 11.33 ? 329  TYR A CE2 1 
ATOM   2488 C  CZ  . TYR A 1 329  ? 25.605 45.518  9.937   1.00 12.29 ? 329  TYR A CZ  1 
ATOM   2489 O  OH  . TYR A 1 329  ? 25.701 46.817  9.572   1.00 13.16 ? 329  TYR A OH  1 
ATOM   2490 N  N   . ARG A 1 330  ? 24.781 38.591  9.837   1.00 12.84 ? 330  ARG A N   1 
ATOM   2491 C  CA  . ARG A 1 330  ? 24.799 37.131  9.820   1.00 13.57 ? 330  ARG A CA  1 
ATOM   2492 C  C   . ARG A 1 330  ? 25.615 36.355  10.850  1.00 14.12 ? 330  ARG A C   1 
ATOM   2493 O  O   . ARG A 1 330  ? 25.392 35.161  11.016  1.00 12.99 ? 330  ARG A O   1 
ATOM   2494 C  CB  . ARG A 1 330  ? 25.212 36.655  8.416   1.00 14.14 ? 330  ARG A CB  1 
ATOM   2495 C  CG  . ARG A 1 330  ? 24.243 37.150  7.345   1.00 14.16 ? 330  ARG A CG  1 
ATOM   2496 C  CD  . ARG A 1 330  ? 24.535 36.587  5.963   1.00 14.12 ? 330  ARG A CD  1 
ATOM   2497 N  NE  . ARG A 1 330  ? 23.554 37.130  5.040   1.00 13.78 ? 330  ARG A NE  1 
ATOM   2498 C  CZ  . ARG A 1 330  ? 23.293 36.616  3.841   1.00 15.62 ? 330  ARG A CZ  1 
ATOM   2499 N  NH1 . ARG A 1 330  ? 23.952 35.542  3.437   1.00 13.02 ? 330  ARG A NH1 1 
ATOM   2500 N  NH2 . ARG A 1 330  ? 22.359 37.172  3.057   1.00 13.26 ? 330  ARG A NH2 1 
ATOM   2501 N  N   . THR A 1 331  ? 26.578 36.992  11.521  1.00 13.16 ? 331  THR A N   1 
ATOM   2502 C  CA  . THR A 1 331  ? 27.357 36.244  12.510  1.00 11.94 ? 331  THR A CA  1 
ATOM   2503 C  C   . THR A 1 331  ? 26.990 36.654  13.934  1.00 12.65 ? 331  THR A C   1 
ATOM   2504 O  O   . THR A 1 331  ? 26.150 37.540  14.147  1.00 12.21 ? 331  THR A O   1 
ATOM   2505 C  CB  . THR A 1 331  ? 28.862 36.473  12.324  1.00 12.57 ? 331  THR A CB  1 
ATOM   2506 O  OG1 . THR A 1 331  ? 29.195 37.781  12.784  1.00 10.29 ? 331  THR A OG1 1 
ATOM   2507 C  CG2 . THR A 1 331  ? 29.244 36.363  10.847  1.00 11.80 ? 331  THR A CG2 1 
ATOM   2508 N  N   . ASN A 1 332  ? 27.631 36.023  14.915  1.00 12.80 ? 332  ASN A N   1 
ATOM   2509 C  CA  . ASN A 1 332  ? 27.361 36.366  16.305  1.00 13.97 ? 332  ASN A CA  1 
ATOM   2510 C  C   . ASN A 1 332  ? 28.396 37.368  16.829  1.00 13.62 ? 332  ASN A C   1 
ATOM   2511 O  O   . ASN A 1 332  ? 28.569 37.519  18.046  1.00 12.29 ? 332  ASN A O   1 
ATOM   2512 C  CB  . ASN A 1 332  ? 27.332 35.099  17.186  1.00 16.08 ? 332  ASN A CB  1 
ATOM   2513 C  CG  . ASN A 1 332  ? 28.675 34.393  17.240  1.00 19.01 ? 332  ASN A CG  1 
ATOM   2514 O  OD1 . ASN A 1 332  ? 29.402 34.342  16.239  1.00 20.48 ? 332  ASN A OD1 1 
ATOM   2515 N  ND2 . ASN A 1 332  ? 29.015 33.844  18.405  1.00 19.25 ? 332  ASN A ND2 1 
ATOM   2516 N  N   . VAL A 1 333  ? 29.058 38.079  15.905  1.00 12.36 ? 333  VAL A N   1 
ATOM   2517 C  CA  . VAL A 1 333  ? 30.063 39.083  16.271  1.00 11.59 ? 333  VAL A CA  1 
ATOM   2518 C  C   . VAL A 1 333  ? 29.498 40.460  15.860  1.00 13.19 ? 333  VAL A C   1 
ATOM   2519 O  O   . VAL A 1 333  ? 29.233 40.722  14.666  1.00 13.25 ? 333  VAL A O   1 
ATOM   2520 C  CB  . VAL A 1 333  ? 31.415 38.809  15.548  1.00 12.85 ? 333  VAL A CB  1 
ATOM   2521 C  CG1 . VAL A 1 333  ? 32.441 39.898  15.902  1.00 11.70 ? 333  VAL A CG1 1 
ATOM   2522 C  CG2 . VAL A 1 333  ? 31.944 37.426  15.945  1.00 11.78 ? 333  VAL A CG2 1 
ATOM   2523 N  N   . LEU A 1 334  ? 29.344 41.341  16.845  1.00 10.54 ? 334  LEU A N   1 
ATOM   2524 C  CA  . LEU A 1 334  ? 28.735 42.644  16.643  1.00 10.79 ? 334  LEU A CA  1 
ATOM   2525 C  C   . LEU A 1 334  ? 29.677 43.842  16.765  1.00 9.74  ? 334  LEU A C   1 
ATOM   2526 O  O   . LEU A 1 334  ? 30.412 43.961  17.741  1.00 10.58 ? 334  LEU A O   1 
ATOM   2527 C  CB  . LEU A 1 334  ? 27.591 42.805  17.648  1.00 10.67 ? 334  LEU A CB  1 
ATOM   2528 C  CG  . LEU A 1 334  ? 26.731 44.061  17.474  1.00 8.59  ? 334  LEU A CG  1 
ATOM   2529 C  CD1 . LEU A 1 334  ? 26.022 43.985  16.075  1.00 8.55  ? 334  LEU A CD1 1 
ATOM   2530 C  CD2 . LEU A 1 334  ? 25.704 44.124  18.586  1.00 8.62  ? 334  LEU A CD2 1 
ATOM   2531 N  N   . LEU A 1 335  ? 29.645 44.734  15.782  1.00 9.94  ? 335  LEU A N   1 
ATOM   2532 C  CA  . LEU A 1 335  ? 30.510 45.924  15.800  1.00 9.46  ? 335  LEU A CA  1 
ATOM   2533 C  C   . LEU A 1 335  ? 29.724 47.102  16.336  1.00 9.56  ? 335  LEU A C   1 
ATOM   2534 O  O   . LEU A 1 335  ? 28.661 47.426  15.806  1.00 9.36  ? 335  LEU A O   1 
ATOM   2535 C  CB  . LEU A 1 335  ? 30.999 46.268  14.389  1.00 9.83  ? 335  LEU A CB  1 
ATOM   2536 C  CG  . LEU A 1 335  ? 31.769 47.587  14.311  1.00 10.35 ? 335  LEU A CG  1 
ATOM   2537 C  CD1 . LEU A 1 335  ? 33.102 47.432  15.064  1.00 9.69  ? 335  LEU A CD1 1 
ATOM   2538 C  CD2 . LEU A 1 335  ? 32.040 47.938  12.842  1.00 11.75 ? 335  LEU A CD2 1 
ATOM   2539 N  N   . ILE A 1 336  ? 30.246 47.735  17.388  1.00 9.92  ? 336  ILE A N   1 
ATOM   2540 C  CA  . ILE A 1 336  ? 29.609 48.896  17.991  1.00 9.38  ? 336  ILE A CA  1 
ATOM   2541 C  C   . ILE A 1 336  ? 30.630 50.052  18.036  1.00 9.88  ? 336  ILE A C   1 
ATOM   2542 O  O   . ILE A 1 336  ? 31.430 50.145  18.962  1.00 10.87 ? 336  ILE A O   1 
ATOM   2543 C  CB  . ILE A 1 336  ? 29.115 48.616  19.461  1.00 10.61 ? 336  ILE A CB  1 
ATOM   2544 C  CG1 . ILE A 1 336  ? 28.066 47.474  19.497  1.00 8.93  ? 336  ILE A CG1 1 
ATOM   2545 C  CG2 . ILE A 1 336  ? 28.497 49.921  20.061  1.00 8.78  ? 336  ILE A CG2 1 
ATOM   2546 C  CD1 . ILE A 1 336  ? 26.758 47.755  18.740  1.00 10.68 ? 336  ILE A CD1 1 
ATOM   2547 N  N   . PRO A 1 337  ? 30.639 50.915  17.008  1.00 9.85  ? 337  PRO A N   1 
ATOM   2548 C  CA  . PRO A 1 337  ? 31.572 52.042  17.005  1.00 9.58  ? 337  PRO A CA  1 
ATOM   2549 C  C   . PRO A 1 337  ? 31.182 52.962  18.179  1.00 10.23 ? 337  PRO A C   1 
ATOM   2550 O  O   . PRO A 1 337  ? 29.991 53.074  18.506  1.00 9.97  ? 337  PRO A O   1 
ATOM   2551 C  CB  . PRO A 1 337  ? 31.293 52.735  15.674  1.00 9.14  ? 337  PRO A CB  1 
ATOM   2552 C  CG  . PRO A 1 337  ? 30.711 51.642  14.794  1.00 9.94  ? 337  PRO A CG  1 
ATOM   2553 C  CD  . PRO A 1 337  ? 29.861 50.850  15.753  1.00 8.61  ? 337  PRO A CD  1 
ATOM   2554 N  N   . LEU A 1 338  ? 32.168 53.608  18.805  1.00 9.28  ? 338  LEU A N   1 
ATOM   2555 C  CA  . LEU A 1 338  ? 31.871 54.520  19.918  1.00 10.32 ? 338  LEU A CA  1 
ATOM   2556 C  C   . LEU A 1 338  ? 32.678 55.797  19.699  1.00 8.88  ? 338  LEU A C   1 
ATOM   2557 O  O   . LEU A 1 338  ? 33.843 55.892  20.110  1.00 7.90  ? 338  LEU A O   1 
ATOM   2558 C  CB  . LEU A 1 338  ? 32.251 53.899  21.268  1.00 10.43 ? 338  LEU A CB  1 
ATOM   2559 C  CG  . LEU A 1 338  ? 31.931 54.778  22.472  1.00 11.94 ? 338  LEU A CG  1 
ATOM   2560 C  CD1 . LEU A 1 338  ? 30.450 54.755  22.782  1.00 10.95 ? 338  LEU A CD1 1 
ATOM   2561 C  CD2 . LEU A 1 338  ? 32.734 54.252  23.686  1.00 11.73 ? 338  LEU A CD2 1 
ATOM   2562 N  N   . GLY A 1 339  ? 32.049 56.774  19.051  1.00 10.19 ? 339  GLY A N   1 
ATOM   2563 C  CA  . GLY A 1 339  ? 32.742 58.031  18.784  1.00 10.97 ? 339  GLY A CA  1 
ATOM   2564 C  C   . GLY A 1 339  ? 31.952 59.011  17.935  1.00 11.89 ? 339  GLY A C   1 
ATOM   2565 O  O   . GLY A 1 339  ? 30.791 58.740  17.583  1.00 11.86 ? 339  GLY A O   1 
ATOM   2566 N  N   . ASP A 1 340  ? 32.585 60.149  17.612  1.00 10.67 ? 340  ASP A N   1 
ATOM   2567 C  CA  . ASP A 1 340  ? 31.969 61.205  16.831  1.00 10.17 ? 340  ASP A CA  1 
ATOM   2568 C  C   . ASP A 1 340  ? 33.111 62.161  16.395  1.00 11.43 ? 340  ASP A C   1 
ATOM   2569 O  O   . ASP A 1 340  ? 34.298 61.882  16.598  1.00 11.15 ? 340  ASP A O   1 
ATOM   2570 C  CB  . ASP A 1 340  ? 30.974 61.941  17.729  1.00 11.26 ? 340  ASP A CB  1 
ATOM   2571 C  CG  . ASP A 1 340  ? 29.815 62.591  16.966  1.00 13.47 ? 340  ASP A CG  1 
ATOM   2572 O  OD1 . ASP A 1 340  ? 29.995 62.924  15.761  1.00 12.49 ? 340  ASP A OD1 1 
ATOM   2573 O  OD2 . ASP A 1 340  ? 28.726 62.787  17.594  1.00 11.58 ? 340  ASP A OD2 1 
ATOM   2574 N  N   . ASN A 1 341  ? 32.739 63.297  15.828  1.00 11.35 ? 341  ASN A N   1 
ATOM   2575 C  CA  . ASN A 1 341  ? 33.700 64.280  15.337  1.00 11.63 ? 341  ASN A CA  1 
ATOM   2576 C  C   . ASN A 1 341  ? 34.589 64.832  16.433  1.00 11.29 ? 341  ASN A C   1 
ATOM   2577 O  O   . ASN A 1 341  ? 34.100 65.299  17.468  1.00 10.92 ? 341  ASN A O   1 
ATOM   2578 C  CB  . ASN A 1 341  ? 32.962 65.450  14.661  1.00 11.32 ? 341  ASN A CB  1 
ATOM   2579 C  CG  . ASN A 1 341  ? 32.252 65.037  13.378  1.00 12.39 ? 341  ASN A CG  1 
ATOM   2580 O  OD1 . ASN A 1 341  ? 32.313 63.878  12.943  1.00 12.04 ? 341  ASN A OD1 1 
ATOM   2581 N  ND2 . ASN A 1 341  ? 31.582 65.989  12.761  1.00 13.13 ? 341  ASN A ND2 1 
ATOM   2582 N  N   . PHE A 1 342  ? 35.894 64.764  16.207  1.00 10.70 ? 342  PHE A N   1 
ATOM   2583 C  CA  . PHE A 1 342  ? 36.858 65.291  17.153  1.00 10.69 ? 342  PHE A CA  1 
ATOM   2584 C  C   . PHE A 1 342  ? 36.593 64.929  18.614  1.00 11.64 ? 342  PHE A C   1 
ATOM   2585 O  O   . PHE A 1 342  ? 36.756 65.757  19.517  1.00 10.34 ? 342  PHE A O   1 
ATOM   2586 C  CB  . PHE A 1 342  ? 36.962 66.811  16.987  1.00 9.99  ? 342  PHE A CB  1 
ATOM   2587 C  CG  . PHE A 1 342  ? 37.550 67.239  15.640  1.00 10.48 ? 342  PHE A CG  1 
ATOM   2588 C  CD1 . PHE A 1 342  ? 36.728 67.682  14.615  1.00 10.18 ? 342  PHE A CD1 1 
ATOM   2589 C  CD2 . PHE A 1 342  ? 38.912 67.182  15.413  1.00 10.26 ? 342  PHE A CD2 1 
ATOM   2590 C  CE1 . PHE A 1 342  ? 37.254 68.064  13.386  1.00 9.08  ? 342  PHE A CE1 1 
ATOM   2591 C  CE2 . PHE A 1 342  ? 39.457 67.562  14.195  1.00 10.18 ? 342  PHE A CE2 1 
ATOM   2592 C  CZ  . PHE A 1 342  ? 38.623 68.007  13.171  1.00 10.28 ? 342  PHE A CZ  1 
ATOM   2593 N  N   . ARG A 1 343  ? 36.207 63.677  18.846  1.00 11.32 ? 343  ARG A N   1 
ATOM   2594 C  CA  . ARG A 1 343  ? 35.981 63.200  20.201  1.00 12.31 ? 343  ARG A CA  1 
ATOM   2595 C  C   . ARG A 1 343  ? 37.307 62.755  20.879  1.00 13.55 ? 343  ARG A C   1 
ATOM   2596 O  O   . ARG A 1 343  ? 38.385 62.648  20.235  1.00 11.94 ? 343  ARG A O   1 
ATOM   2597 C  CB  . ARG A 1 343  ? 34.992 62.012  20.190  1.00 12.28 ? 343  ARG A CB  1 
ATOM   2598 C  CG  . ARG A 1 343  ? 33.531 62.414  19.994  1.00 12.29 ? 343  ARG A CG  1 
ATOM   2599 C  CD  . ARG A 1 343  ? 33.127 63.373  21.085  1.00 13.61 ? 343  ARG A CD  1 
ATOM   2600 N  NE  . ARG A 1 343  ? 31.701 63.696  21.033  1.00 13.09 ? 343  ARG A NE  1 
ATOM   2601 C  CZ  . ARG A 1 343  ? 30.742 63.008  21.654  1.00 13.79 ? 343  ARG A CZ  1 
ATOM   2602 N  NH1 . ARG A 1 343  ? 31.022 61.923  22.403  1.00 12.96 ? 343  ARG A NH1 1 
ATOM   2603 N  NH2 . ARG A 1 343  ? 29.485 63.421  21.538  1.00 12.47 ? 343  ARG A NH2 1 
ATOM   2604 N  N   . PHE A 1 344  ? 37.184 62.457  22.171  1.00 14.38 ? 344  PHE A N   1 
ATOM   2605 C  CA  . PHE A 1 344  ? 38.283 62.011  23.011  1.00 14.44 ? 344  PHE A CA  1 
ATOM   2606 C  C   . PHE A 1 344  ? 39.362 63.035  23.111  1.00 15.74 ? 344  PHE A C   1 
ATOM   2607 O  O   . PHE A 1 344  ? 40.558 62.727  23.056  1.00 16.60 ? 344  PHE A O   1 
ATOM   2608 C  CB  . PHE A 1 344  ? 38.819 60.689  22.518  1.00 13.12 ? 344  PHE A CB  1 
ATOM   2609 C  CG  . PHE A 1 344  ? 37.835 59.589  22.689  1.00 14.49 ? 344  PHE A CG  1 
ATOM   2610 C  CD1 . PHE A 1 344  ? 37.016 59.209  21.641  1.00 12.23 ? 344  PHE A CD1 1 
ATOM   2611 C  CD2 . PHE A 1 344  ? 37.632 59.006  23.957  1.00 13.98 ? 344  PHE A CD2 1 
ATOM   2612 C  CE1 . PHE A 1 344  ? 36.013 58.279  21.834  1.00 15.37 ? 344  PHE A CE1 1 
ATOM   2613 C  CE2 . PHE A 1 344  ? 36.613 58.063  24.147  1.00 15.32 ? 344  PHE A CE2 1 
ATOM   2614 C  CZ  . PHE A 1 344  ? 35.807 57.705  23.078  1.00 13.57 ? 344  PHE A CZ  1 
ATOM   2615 N  N   . LYS A 1 345  ? 38.911 64.271  23.260  1.00 16.37 ? 345  LYS A N   1 
ATOM   2616 C  CA  . LYS A 1 345  ? 39.809 65.389  23.377  1.00 18.39 ? 345  LYS A CA  1 
ATOM   2617 C  C   . LYS A 1 345  ? 40.296 65.630  24.797  1.00 19.08 ? 345  LYS A C   1 
ATOM   2618 O  O   . LYS A 1 345  ? 41.484 65.870  25.011  1.00 20.63 ? 345  LYS A O   1 
ATOM   2619 C  CB  . LYS A 1 345  ? 39.138 66.646  22.870  1.00 18.38 ? 345  LYS A CB  1 
ATOM   2620 C  CG  . LYS A 1 345  ? 40.007 67.837  23.007  1.00 20.23 ? 345  LYS A CG  1 
ATOM   2621 C  CD  . LYS A 1 345  ? 39.292 69.035  22.429  1.00 21.74 ? 345  LYS A CD  1 
ATOM   2622 C  CE  . LYS A 1 345  ? 40.028 70.302  22.773  1.00 22.41 ? 345  LYS A CE  1 
ATOM   2623 N  NZ  . LYS A 1 345  ? 39.329 71.452  22.126  1.00 25.60 ? 345  LYS A NZ  1 
ATOM   2624 N  N   . GLN A 1 346  ? 39.393 65.561  25.765  1.00 19.03 ? 346  GLN A N   1 
ATOM   2625 C  CA  . GLN A 1 346  ? 39.768 65.820  27.148  1.00 19.95 ? 346  GLN A CA  1 
ATOM   2626 C  C   . GLN A 1 346  ? 39.897 64.566  27.985  1.00 19.40 ? 346  GLN A C   1 
ATOM   2627 O  O   . GLN A 1 346  ? 39.153 63.601  27.768  1.00 16.34 ? 346  GLN A O   1 
ATOM   2628 C  CB  . GLN A 1 346  ? 38.720 66.717  27.780  1.00 22.72 ? 346  GLN A CB  1 
ATOM   2629 C  CG  . GLN A 1 346  ? 38.706 68.082  27.180  1.00 27.54 ? 346  GLN A CG  1 
ATOM   2630 C  CD  . GLN A 1 346  ? 37.560 68.886  27.702  1.00 31.11 ? 346  GLN A CD  1 
ATOM   2631 O  OE1 . GLN A 1 346  ? 36.437 68.790  27.191  1.00 32.63 ? 346  GLN A OE1 1 
ATOM   2632 N  NE2 . GLN A 1 346  ? 37.818 69.679  28.754  1.00 32.77 ? 346  GLN A NE2 1 
ATOM   2633 N  N   . ASN A 1 347  ? 40.827 64.592  28.946  1.00 18.90 ? 347  ASN A N   1 
ATOM   2634 C  CA  . ASN A 1 347  ? 41.021 63.450  29.839  1.00 21.24 ? 347  ASN A CA  1 
ATOM   2635 C  C   . ASN A 1 347  ? 39.721 63.098  30.522  1.00 19.29 ? 347  ASN A C   1 
ATOM   2636 O  O   . ASN A 1 347  ? 39.416 61.937  30.663  1.00 20.34 ? 347  ASN A O   1 
ATOM   2637 C  CB  . ASN A 1 347  ? 42.079 63.744  30.908  1.00 25.23 ? 347  ASN A CB  1 
ATOM   2638 C  CG  . ASN A 1 347  ? 43.379 64.145  30.298  1.00 29.91 ? 347  ASN A CG  1 
ATOM   2639 O  OD1 . ASN A 1 347  ? 43.704 65.347  30.210  1.00 34.33 ? 347  ASN A OD1 1 
ATOM   2640 N  ND2 . ASN A 1 347  ? 44.128 63.154  29.810  1.00 32.37 ? 347  ASN A ND2 1 
ATOM   2641 N  N   . THR A 1 348  ? 38.952 64.097  30.940  1.00 17.19 ? 348  THR A N   1 
ATOM   2642 C  CA  . THR A 1 348  ? 37.694 63.806  31.605  1.00 16.47 ? 348  THR A CA  1 
ATOM   2643 C  C   . THR A 1 348  ? 36.723 63.093  30.652  1.00 15.56 ? 348  THR A C   1 
ATOM   2644 O  O   . THR A 1 348  ? 35.842 62.340  31.084  1.00 14.28 ? 348  THR A O   1 
ATOM   2645 C  CB  . THR A 1 348  ? 37.063 65.085  32.127  1.00 16.17 ? 348  THR A CB  1 
ATOM   2646 O  OG1 . THR A 1 348  ? 36.953 66.007  31.047  1.00 17.16 ? 348  THR A OG1 1 
ATOM   2647 C  CG2 . THR A 1 348  ? 37.945 65.713  33.249  1.00 18.57 ? 348  THR A CG2 1 
ATOM   2648 N  N   . GLU A 1 349  ? 36.865 63.334  29.354  1.00 15.02 ? 349  GLU A N   1 
ATOM   2649 C  CA  . GLU A 1 349  ? 36.003 62.636  28.388  1.00 14.31 ? 349  GLU A CA  1 
ATOM   2650 C  C   . GLU A 1 349  ? 36.428 61.166  28.336  1.00 13.93 ? 349  GLU A C   1 
ATOM   2651 O  O   . GLU A 1 349  ? 35.590 60.284  28.305  1.00 14.02 ? 349  GLU A O   1 
ATOM   2652 C  CB  . GLU A 1 349  ? 36.134 63.211  26.983  1.00 14.04 ? 349  GLU A CB  1 
ATOM   2653 C  CG  . GLU A 1 349  ? 35.288 62.430  25.944  1.00 13.35 ? 349  GLU A CG  1 
ATOM   2654 C  CD  . GLU A 1 349  ? 35.352 63.055  24.556  1.00 13.05 ? 349  GLU A CD  1 
ATOM   2655 O  OE1 . GLU A 1 349  ? 34.799 62.478  23.613  1.00 14.24 ? 349  GLU A OE1 1 
ATOM   2656 O  OE2 . GLU A 1 349  ? 35.956 64.129  24.410  1.00 14.37 ? 349  GLU A OE2 1 
ATOM   2657 N  N   . TRP A 1 350  ? 37.734 60.909  28.294  1.00 12.76 ? 350  TRP A N   1 
ATOM   2658 C  CA  . TRP A 1 350  ? 38.217 59.531  28.261  1.00 13.25 ? 350  TRP A CA  1 
ATOM   2659 C  C   . TRP A 1 350  ? 37.698 58.755  29.469  1.00 13.82 ? 350  TRP A C   1 
ATOM   2660 O  O   . TRP A 1 350  ? 37.234 57.623  29.359  1.00 11.62 ? 350  TRP A O   1 
ATOM   2661 C  CB  . TRP A 1 350  ? 39.750 59.492  28.266  1.00 13.32 ? 350  TRP A CB  1 
ATOM   2662 C  CG  . TRP A 1 350  ? 40.358 59.759  26.917  1.00 12.41 ? 350  TRP A CG  1 
ATOM   2663 C  CD1 . TRP A 1 350  ? 40.728 60.976  26.387  1.00 12.10 ? 350  TRP A CD1 1 
ATOM   2664 C  CD2 . TRP A 1 350  ? 40.636 58.784  25.912  1.00 12.81 ? 350  TRP A CD2 1 
ATOM   2665 N  NE1 . TRP A 1 350  ? 41.215 60.801  25.120  1.00 11.50 ? 350  TRP A NE1 1 
ATOM   2666 C  CE2 . TRP A 1 350  ? 41.173 59.465  24.805  1.00 11.45 ? 350  TRP A CE2 1 
ATOM   2667 C  CE3 . TRP A 1 350  ? 40.480 57.385  25.837  1.00 12.32 ? 350  TRP A CE3 1 
ATOM   2668 C  CZ2 . TRP A 1 350  ? 41.558 58.798  23.639  1.00 12.34 ? 350  TRP A CZ2 1 
ATOM   2669 C  CZ3 . TRP A 1 350  ? 40.863 56.729  24.673  1.00 12.41 ? 350  TRP A CZ3 1 
ATOM   2670 C  CH2 . TRP A 1 350  ? 41.397 57.440  23.590  1.00 10.55 ? 350  TRP A CH2 1 
ATOM   2671 N  N   . ASP A 1 351  ? 37.792 59.377  30.636  1.00 14.64 ? 351  ASP A N   1 
ATOM   2672 C  CA  . ASP A 1 351  ? 37.327 58.748  31.855  1.00 16.54 ? 351  ASP A CA  1 
ATOM   2673 C  C   . ASP A 1 351  ? 35.817 58.460  31.860  1.00 16.67 ? 351  ASP A C   1 
ATOM   2674 O  O   . ASP A 1 351  ? 35.373 57.337  32.163  1.00 16.98 ? 351  ASP A O   1 
ATOM   2675 C  CB  . ASP A 1 351  ? 37.644 59.651  33.044  1.00 17.92 ? 351  ASP A CB  1 
ATOM   2676 C  CG  . ASP A 1 351  ? 39.102 59.628  33.423  1.00 20.51 ? 351  ASP A CG  1 
ATOM   2677 O  OD1 . ASP A 1 351  ? 39.794 58.605  33.212  1.00 21.94 ? 351  ASP A OD1 1 
ATOM   2678 O  OD2 . ASP A 1 351  ? 39.552 60.633  33.975  1.00 24.25 ? 351  ASP A OD2 1 
ATOM   2679 N  N   . VAL A 1 352  ? 35.032 59.472  31.521  1.00 16.13 ? 352  VAL A N   1 
ATOM   2680 C  CA  . VAL A 1 352  ? 33.597 59.295  31.575  1.00 16.67 ? 352  VAL A CA  1 
ATOM   2681 C  C   . VAL A 1 352  ? 33.119 58.198  30.619  1.00 15.89 ? 352  VAL A C   1 
ATOM   2682 O  O   . VAL A 1 352  ? 32.247 57.408  30.975  1.00 15.40 ? 352  VAL A O   1 
ATOM   2683 C  CB  . VAL A 1 352  ? 32.852 60.656  31.357  1.00 17.84 ? 352  VAL A CB  1 
ATOM   2684 C  CG1 . VAL A 1 352  ? 32.714 60.992  29.866  1.00 17.19 ? 352  VAL A CG1 1 
ATOM   2685 C  CG2 . VAL A 1 352  ? 31.516 60.613  32.060  1.00 17.99 ? 352  VAL A CG2 1 
ATOM   2686 N  N   . GLN A 1 353  ? 33.692 58.125  29.419  1.00 14.58 ? 353  GLN A N   1 
ATOM   2687 C  CA  . GLN A 1 353  ? 33.281 57.064  28.517  1.00 13.30 ? 353  GLN A CA  1 
ATOM   2688 C  C   . GLN A 1 353  ? 33.824 55.703  29.012  1.00 13.39 ? 353  GLN A C   1 
ATOM   2689 O  O   . GLN A 1 353  ? 33.075 54.741  29.130  1.00 14.14 ? 353  GLN A O   1 
ATOM   2690 C  CB  . GLN A 1 353  ? 33.763 57.345  27.081  1.00 12.49 ? 353  GLN A CB  1 
ATOM   2691 C  CG  . GLN A 1 353  ? 33.211 58.647  26.452  1.00 12.73 ? 353  GLN A CG  1 
ATOM   2692 C  CD  . GLN A 1 353  ? 31.739 58.554  26.031  1.00 13.93 ? 353  GLN A CD  1 
ATOM   2693 O  OE1 . GLN A 1 353  ? 30.931 57.883  26.679  1.00 13.04 ? 353  GLN A OE1 1 
ATOM   2694 N  NE2 . GLN A 1 353  ? 31.382 59.267  24.952  1.00 12.87 ? 353  GLN A NE2 1 
ATOM   2695 N  N   . ARG A 1 354  ? 35.118 55.622  29.317  1.00 12.58 ? 354  ARG A N   1 
ATOM   2696 C  CA  . ARG A 1 354  ? 35.685 54.359  29.753  1.00 13.10 ? 354  ARG A CA  1 
ATOM   2697 C  C   . ARG A 1 354  ? 35.071 53.749  31.020  1.00 13.81 ? 354  ARG A C   1 
ATOM   2698 O  O   . ARG A 1 354  ? 34.732 52.564  31.035  1.00 13.45 ? 354  ARG A O   1 
ATOM   2699 C  CB  . ARG A 1 354  ? 37.193 54.474  29.968  1.00 13.75 ? 354  ARG A CB  1 
ATOM   2700 C  CG  . ARG A 1 354  ? 37.808 53.185  30.550  1.00 14.30 ? 354  ARG A CG  1 
ATOM   2701 C  CD  . ARG A 1 354  ? 39.326 53.301  30.714  1.00 15.04 ? 354  ARG A CD  1 
ATOM   2702 N  NE  . ARG A 1 354  ? 39.670 54.343  31.684  1.00 16.34 ? 354  ARG A NE  1 
ATOM   2703 C  CZ  . ARG A 1 354  ? 39.519 54.239  33.004  1.00 16.44 ? 354  ARG A CZ  1 
ATOM   2704 N  NH1 . ARG A 1 354  ? 39.028 53.138  33.545  1.00 15.53 ? 354  ARG A NH1 1 
ATOM   2705 N  NH2 . ARG A 1 354  ? 39.865 55.243  33.785  1.00 15.36 ? 354  ARG A NH2 1 
ATOM   2706 N  N   . VAL A 1 355  ? 34.931 54.552  32.067  1.00 14.12 ? 355  VAL A N   1 
ATOM   2707 C  CA  . VAL A 1 355  ? 34.428 54.044  33.332  1.00 15.68 ? 355  VAL A CA  1 
ATOM   2708 C  C   . VAL A 1 355  ? 33.000 53.517  33.241  1.00 16.91 ? 355  VAL A C   1 
ATOM   2709 O  O   . VAL A 1 355  ? 32.708 52.395  33.692  1.00 17.32 ? 355  VAL A O   1 
ATOM   2710 C  CB  . VAL A 1 355  ? 34.561 55.143  34.431  1.00 17.43 ? 355  VAL A CB  1 
ATOM   2711 C  CG1 . VAL A 1 355  ? 33.913 54.679  35.736  1.00 19.78 ? 355  VAL A CG1 1 
ATOM   2712 C  CG2 . VAL A 1 355  ? 36.070 55.424  34.696  1.00 16.77 ? 355  VAL A CG2 1 
ATOM   2713 N  N   . ASN A 1 356  ? 32.110 54.309  32.652  1.00 14.92 ? 356  ASN A N   1 
ATOM   2714 C  CA  . ASN A 1 356  ? 30.741 53.869  32.529  1.00 14.40 ? 356  ASN A CA  1 
ATOM   2715 C  C   . ASN A 1 356  ? 30.632 52.592  31.699  1.00 15.06 ? 356  ASN A C   1 
ATOM   2716 O  O   . ASN A 1 356  ? 29.921 51.664  32.103  1.00 13.66 ? 356  ASN A O   1 
ATOM   2717 C  CB  . ASN A 1 356  ? 29.894 55.004  31.989  1.00 13.16 ? 356  ASN A CB  1 
ATOM   2718 C  CG  . ASN A 1 356  ? 29.609 56.045  33.072  1.00 14.87 ? 356  ASN A CG  1 
ATOM   2719 O  OD1 . ASN A 1 356  ? 28.975 55.720  34.093  1.00 14.73 ? 356  ASN A OD1 1 
ATOM   2720 N  ND2 . ASN A 1 356  ? 30.116 57.273  32.892  1.00 11.80 ? 356  ASN A ND2 1 
ATOM   2721 N  N   . TYR A 1 357  ? 31.366 52.510  30.581  1.00 13.77 ? 357  TYR A N   1 
ATOM   2722 C  CA  . TYR A 1 357  ? 31.320 51.289  29.780  1.00 14.81 ? 357  TYR A CA  1 
ATOM   2723 C  C   . TYR A 1 357  ? 31.928 50.094  30.513  1.00 15.19 ? 357  TYR A C   1 
ATOM   2724 O  O   . TYR A 1 357  ? 31.447 48.961  30.384  1.00 16.76 ? 357  TYR A O   1 
ATOM   2725 C  CB  . TYR A 1 357  ? 31.978 51.497  28.399  1.00 13.05 ? 357  TYR A CB  1 
ATOM   2726 C  CG  . TYR A 1 357  ? 30.965 52.016  27.387  1.00 12.08 ? 357  TYR A CG  1 
ATOM   2727 C  CD1 . TYR A 1 357  ? 30.801 53.386  27.154  1.00 11.97 ? 357  TYR A CD1 1 
ATOM   2728 C  CD2 . TYR A 1 357  ? 30.142 51.126  26.694  1.00 10.87 ? 357  TYR A CD2 1 
ATOM   2729 C  CE1 . TYR A 1 357  ? 29.830 53.866  26.235  1.00 11.67 ? 357  TYR A CE1 1 
ATOM   2730 C  CE2 . TYR A 1 357  ? 29.175 51.579  25.784  1.00 12.07 ? 357  TYR A CE2 1 
ATOM   2731 C  CZ  . TYR A 1 357  ? 29.016 52.946  25.556  1.00 13.52 ? 357  TYR A CZ  1 
ATOM   2732 O  OH  . TYR A 1 357  ? 28.021 53.374  24.690  1.00 11.83 ? 357  TYR A OH  1 
ATOM   2733 N  N   . GLU A 1 358  ? 32.974 50.319  31.294  1.00 15.37 ? 358  GLU A N   1 
ATOM   2734 C  CA  . GLU A 1 358  ? 33.544 49.189  32.037  1.00 16.86 ? 358  GLU A CA  1 
ATOM   2735 C  C   . GLU A 1 358  ? 32.488 48.656  33.023  1.00 16.19 ? 358  GLU A C   1 
ATOM   2736 O  O   . GLU A 1 358  ? 32.367 47.443  33.215  1.00 15.97 ? 358  GLU A O   1 
ATOM   2737 C  CB  . GLU A 1 358  ? 34.774 49.616  32.805  1.00 17.27 ? 358  GLU A CB  1 
ATOM   2738 C  CG  . GLU A 1 358  ? 36.054 49.636  31.988  1.00 22.01 ? 358  GLU A CG  1 
ATOM   2739 C  CD  . GLU A 1 358  ? 37.206 50.210  32.793  1.00 23.07 ? 358  GLU A CD  1 
ATOM   2740 O  OE1 . GLU A 1 358  ? 37.048 50.359  34.027  1.00 27.08 ? 358  GLU A OE1 1 
ATOM   2741 O  OE2 . GLU A 1 358  ? 38.263 50.528  32.218  1.00 26.50 ? 358  GLU A OE2 1 
ATOM   2742 N  N   . ARG A 1 359  ? 31.725 49.555  33.646  1.00 15.69 ? 359  ARG A N   1 
ATOM   2743 C  CA  . ARG A 1 359  ? 30.685 49.094  34.593  1.00 16.65 ? 359  ARG A CA  1 
ATOM   2744 C  C   . ARG A 1 359  ? 29.644 48.247  33.861  1.00 16.07 ? 359  ARG A C   1 
ATOM   2745 O  O   . ARG A 1 359  ? 29.206 47.216  34.381  1.00 15.34 ? 359  ARG A O   1 
ATOM   2746 C  CB  . ARG A 1 359  ? 29.976 50.269  35.261  1.00 17.33 ? 359  ARG A CB  1 
ATOM   2747 C  CG  . ARG A 1 359  ? 30.763 50.921  36.335  1.00 21.70 ? 359  ARG A CG  1 
ATOM   2748 C  CD  . ARG A 1 359  ? 30.041 52.172  36.838  1.00 24.46 ? 359  ARG A CD  1 
ATOM   2749 N  NE  . ARG A 1 359  ? 30.954 53.019  37.597  1.00 28.76 ? 359  ARG A NE  1 
ATOM   2750 C  CZ  . ARG A 1 359  ? 31.071 54.342  37.438  1.00 31.49 ? 359  ARG A CZ  1 
ATOM   2751 N  NH1 . ARG A 1 359  ? 30.326 54.995  36.528  1.00 30.65 ? 359  ARG A NH1 1 
ATOM   2752 N  NH2 . ARG A 1 359  ? 31.931 55.016  38.209  1.00 32.06 ? 359  ARG A NH2 1 
ATOM   2753 N  N   . LEU A 1 360  ? 29.249 48.691  32.662  1.00 13.77 ? 360  LEU A N   1 
ATOM   2754 C  CA  . LEU A 1 360  ? 28.273 47.951  31.879  1.00 15.56 ? 360  LEU A CA  1 
ATOM   2755 C  C   . LEU A 1 360  ? 28.829 46.595  31.480  1.00 15.69 ? 360  LEU A C   1 
ATOM   2756 O  O   . LEU A 1 360  ? 28.151 45.577  31.612  1.00 17.40 ? 360  LEU A O   1 
ATOM   2757 C  CB  . LEU A 1 360  ? 27.862 48.752  30.638  1.00 14.57 ? 360  LEU A CB  1 
ATOM   2758 C  CG  . LEU A 1 360  ? 27.066 50.044  30.891  1.00 15.68 ? 360  LEU A CG  1 
ATOM   2759 C  CD1 . LEU A 1 360  ? 27.055 50.906  29.651  1.00 15.61 ? 360  LEU A CD1 1 
ATOM   2760 C  CD2 . LEU A 1 360  ? 25.626 49.717  31.314  1.00 13.81 ? 360  LEU A CD2 1 
ATOM   2761 N  N   . PHE A 1 361  ? 30.068 46.558  30.999  1.00 15.91 ? 361  PHE A N   1 
ATOM   2762 C  CA  . PHE A 1 361  ? 30.652 45.280  30.611  1.00 15.97 ? 361  PHE A CA  1 
ATOM   2763 C  C   . PHE A 1 361  ? 30.742 44.318  31.815  1.00 16.85 ? 361  PHE A C   1 
ATOM   2764 O  O   . PHE A 1 361  ? 30.456 43.118  31.693  1.00 15.31 ? 361  PHE A O   1 
ATOM   2765 C  CB  . PHE A 1 361  ? 32.070 45.468  30.054  1.00 15.36 ? 361  PHE A CB  1 
ATOM   2766 C  CG  . PHE A 1 361  ? 32.152 46.292  28.803  1.00 15.41 ? 361  PHE A CG  1 
ATOM   2767 C  CD1 . PHE A 1 361  ? 33.360 46.917  28.467  1.00 16.33 ? 361  PHE A CD1 1 
ATOM   2768 C  CD2 . PHE A 1 361  ? 31.065 46.438  27.958  1.00 14.18 ? 361  PHE A CD2 1 
ATOM   2769 C  CE1 . PHE A 1 361  ? 33.474 47.679  27.293  1.00 15.50 ? 361  PHE A CE1 1 
ATOM   2770 C  CE2 . PHE A 1 361  ? 31.161 47.186  26.799  1.00 14.91 ? 361  PHE A CE2 1 
ATOM   2771 C  CZ  . PHE A 1 361  ? 32.368 47.810  26.461  1.00 16.38 ? 361  PHE A CZ  1 
ATOM   2772 N  N   . GLU A 1 362  ? 31.160 44.828  32.975  1.00 16.68 ? 362  GLU A N   1 
ATOM   2773 C  CA  . GLU A 1 362  ? 31.283 43.921  34.104  1.00 17.85 ? 362  GLU A CA  1 
ATOM   2774 C  C   . GLU A 1 362  ? 29.933 43.267  34.432  1.00 16.36 ? 362  GLU A C   1 
ATOM   2775 O  O   . GLU A 1 362  ? 29.858 42.059  34.620  1.00 16.02 ? 362  GLU A O   1 
ATOM   2776 C  CB  . GLU A 1 362  ? 31.853 44.621  35.355  1.00 20.10 ? 362  GLU A CB  1 
ATOM   2777 C  CG  . GLU A 1 362  ? 32.080 43.591  36.495  1.00 24.66 ? 362  GLU A CG  1 
ATOM   2778 C  CD  . GLU A 1 362  ? 32.582 44.189  37.804  1.00 27.11 ? 362  GLU A CD  1 
ATOM   2779 O  OE1 . GLU A 1 362  ? 33.167 45.297  37.782  1.00 30.49 ? 362  GLU A OE1 1 
ATOM   2780 O  OE2 . GLU A 1 362  ? 32.399 43.524  38.859  1.00 29.32 ? 362  GLU A OE2 1 
ATOM   2781 N  N   . HIS A 1 363  ? 28.870 44.059  34.488  1.00 15.66 ? 363  HIS A N   1 
ATOM   2782 C  CA  . HIS A 1 363  ? 27.566 43.499  34.774  1.00 16.24 ? 363  HIS A CA  1 
ATOM   2783 C  C   . HIS A 1 363  ? 27.079 42.561  33.644  1.00 16.13 ? 363  HIS A C   1 
ATOM   2784 O  O   . HIS A 1 363  ? 26.724 41.394  33.872  1.00 15.17 ? 363  HIS A O   1 
ATOM   2785 C  CB  . HIS A 1 363  ? 26.577 44.646  34.971  1.00 18.03 ? 363  HIS A CB  1 
ATOM   2786 C  CG  . HIS A 1 363  ? 25.148 44.212  35.102  1.00 20.36 ? 363  HIS A CG  1 
ATOM   2787 N  ND1 . HIS A 1 363  ? 24.625 43.710  36.275  1.00 22.62 ? 363  HIS A ND1 1 
ATOM   2788 C  CD2 . HIS A 1 363  ? 24.128 44.229  34.212  1.00 20.50 ? 363  HIS A CD2 1 
ATOM   2789 C  CE1 . HIS A 1 363  ? 23.343 43.437  36.102  1.00 21.28 ? 363  HIS A CE1 1 
ATOM   2790 N  NE2 . HIS A 1 363  ? 23.017 43.744  34.857  1.00 21.11 ? 363  HIS A NE2 1 
ATOM   2791 N  N   . ILE A 1 364  ? 27.053 43.073  32.422  1.00 14.94 ? 364  ILE A N   1 
ATOM   2792 C  CA  . ILE A 1 364  ? 26.566 42.283  31.305  1.00 14.85 ? 364  ILE A CA  1 
ATOM   2793 C  C   . ILE A 1 364  ? 27.263 40.939  31.132  1.00 15.75 ? 364  ILE A C   1 
ATOM   2794 O  O   . ILE A 1 364  ? 26.593 39.904  30.989  1.00 16.01 ? 364  ILE A O   1 
ATOM   2795 C  CB  . ILE A 1 364  ? 26.653 43.074  29.991  1.00 14.59 ? 364  ILE A CB  1 
ATOM   2796 C  CG1 . ILE A 1 364  ? 25.696 44.274  30.042  1.00 14.75 ? 364  ILE A CG1 1 
ATOM   2797 C  CG2 . ILE A 1 364  ? 26.322 42.137  28.798  1.00 12.97 ? 364  ILE A CG2 1 
ATOM   2798 C  CD1 . ILE A 1 364  ? 25.951 45.322  28.925  1.00 17.05 ? 364  ILE A CD1 1 
ATOM   2799 N  N   . ASN A 1 365  ? 28.589 40.941  31.175  1.00 15.33 ? 365  ASN A N   1 
ATOM   2800 C  CA  . ASN A 1 365  ? 29.353 39.711  30.985  1.00 17.34 ? 365  ASN A CA  1 
ATOM   2801 C  C   . ASN A 1 365  ? 29.196 38.719  32.140  1.00 19.75 ? 365  ASN A C   1 
ATOM   2802 O  O   . ASN A 1 365  ? 29.457 37.525  31.977  1.00 18.93 ? 365  ASN A O   1 
ATOM   2803 C  CB  . ASN A 1 365  ? 30.836 40.028  30.775  1.00 15.32 ? 365  ASN A CB  1 
ATOM   2804 C  CG  . ASN A 1 365  ? 31.077 40.928  29.553  1.00 16.05 ? 365  ASN A CG  1 
ATOM   2805 O  OD1 . ASN A 1 365  ? 30.170 41.164  28.751  1.00 14.21 ? 365  ASN A OD1 1 
ATOM   2806 N  ND2 . ASN A 1 365  ? 32.303 41.430  29.413  1.00 13.28 ? 365  ASN A ND2 1 
ATOM   2807 N  N   . SER A 1 366  ? 28.750 39.201  33.302  1.00 22.04 ? 366  SER A N   1 
ATOM   2808 C  CA  . SER A 1 366  ? 28.597 38.296  34.448  1.00 24.04 ? 366  SER A CA  1 
ATOM   2809 C  C   . SER A 1 366  ? 27.149 37.843  34.607  1.00 24.85 ? 366  SER A C   1 
ATOM   2810 O  O   . SER A 1 366  ? 26.856 37.044  35.465  1.00 26.41 ? 366  SER A O   1 
ATOM   2811 C  CB  . SER A 1 366  ? 29.060 38.991  35.730  1.00 24.86 ? 366  SER A CB  1 
ATOM   2812 O  OG  . SER A 1 366  ? 28.155 40.042  36.046  1.00 27.00 ? 366  SER A OG  1 
ATOM   2813 N  N   . GLN A 1 367  ? 26.254 38.361  33.778  1.00 25.16 ? 367  GLN A N   1 
ATOM   2814 C  CA  . GLN A 1 367  ? 24.841 38.006  33.804  1.00 26.34 ? 367  GLN A CA  1 
ATOM   2815 C  C   . GLN A 1 367  ? 24.558 37.026  32.663  1.00 26.12 ? 367  GLN A C   1 
ATOM   2816 O  O   . GLN A 1 367  ? 24.143 37.424  31.573  1.00 24.85 ? 367  GLN A O   1 
ATOM   2817 C  CB  . GLN A 1 367  ? 23.960 39.255  33.626  1.00 26.77 ? 367  GLN A CB  1 
ATOM   2818 C  CG  . GLN A 1 367  ? 24.058 40.258  34.770  1.00 30.24 ? 367  GLN A CG  1 
ATOM   2819 C  CD  . GLN A 1 367  ? 23.675 39.634  36.113  1.00 32.85 ? 367  GLN A CD  1 
ATOM   2820 O  OE1 . GLN A 1 367  ? 22.522 39.229  36.319  1.00 32.44 ? 367  GLN A OE1 1 
ATOM   2821 N  NE2 . GLN A 1 367  ? 24.648 39.535  37.026  1.00 33.66 ? 367  GLN A NE2 1 
ATOM   2822 N  N   . ALA A 1 368  ? 24.769 35.739  32.926  1.00 25.97 ? 368  ALA A N   1 
ATOM   2823 C  CA  . ALA A 1 368  ? 24.550 34.711  31.916  1.00 25.38 ? 368  ALA A CA  1 
ATOM   2824 C  C   . ALA A 1 368  ? 23.274 34.864  31.077  1.00 25.54 ? 368  ALA A C   1 
ATOM   2825 O  O   . ALA A 1 368  ? 23.274 34.578  29.858  1.00 24.77 ? 368  ALA A O   1 
ATOM   2826 C  CB  . ALA A 1 368  ? 24.565 33.335  32.575  1.00 25.18 ? 368  ALA A CB  1 
ATOM   2827 N  N   . HIS A 1 369  ? 22.184 35.292  31.700  1.00 24.40 ? 369  HIS A N   1 
ATOM   2828 C  CA  . HIS A 1 369  ? 20.943 35.417  30.941  1.00 24.21 ? 369  HIS A CA  1 
ATOM   2829 C  C   . HIS A 1 369  ? 21.026 36.355  29.730  1.00 23.33 ? 369  HIS A C   1 
ATOM   2830 O  O   . HIS A 1 369  ? 20.154 36.322  28.862  1.00 23.11 ? 369  HIS A O   1 
ATOM   2831 C  CB  . HIS A 1 369  ? 19.802 35.853  31.853  1.00 25.31 ? 369  HIS A CB  1 
ATOM   2832 C  CG  . HIS A 1 369  ? 19.866 37.291  32.275  1.00 27.68 ? 369  HIS A CG  1 
ATOM   2833 N  ND1 . HIS A 1 369  ? 19.339 38.316  31.514  1.00 26.98 ? 369  HIS A ND1 1 
ATOM   2834 C  CD2 . HIS A 1 369  ? 20.394 37.871  33.378  1.00 26.73 ? 369  HIS A CD2 1 
ATOM   2835 C  CE1 . HIS A 1 369  ? 19.540 39.466  32.133  1.00 27.02 ? 369  HIS A CE1 1 
ATOM   2836 N  NE2 . HIS A 1 369  ? 20.179 39.224  33.265  1.00 28.01 ? 369  HIS A NE2 1 
ATOM   2837 N  N   . PHE A 1 370  ? 22.057 37.196  29.648  1.00 22.43 ? 370  PHE A N   1 
ATOM   2838 C  CA  . PHE A 1 370  ? 22.150 38.079  28.468  1.00 20.03 ? 370  PHE A CA  1 
ATOM   2839 C  C   . PHE A 1 370  ? 22.814 37.299  27.341  1.00 18.95 ? 370  PHE A C   1 
ATOM   2840 O  O   . PHE A 1 370  ? 22.568 37.580  26.168  1.00 19.43 ? 370  PHE A O   1 
ATOM   2841 C  CB  . PHE A 1 370  ? 23.024 39.312  28.743  1.00 20.44 ? 370  PHE A CB  1 
ATOM   2842 C  CG  . PHE A 1 370  ? 22.321 40.424  29.502  1.00 19.60 ? 370  PHE A CG  1 
ATOM   2843 C  CD1 . PHE A 1 370  ? 22.850 40.906  30.691  1.00 19.40 ? 370  PHE A CD1 1 
ATOM   2844 C  CD2 . PHE A 1 370  ? 21.162 41.006  29.007  1.00 19.79 ? 370  PHE A CD2 1 
ATOM   2845 C  CE1 . PHE A 1 370  ? 22.231 41.965  31.385  1.00 16.98 ? 370  PHE A CE1 1 
ATOM   2846 C  CE2 . PHE A 1 370  ? 20.532 42.071  29.700  1.00 19.72 ? 370  PHE A CE2 1 
ATOM   2847 C  CZ  . PHE A 1 370  ? 21.089 42.537  30.895  1.00 18.32 ? 370  PHE A CZ  1 
ATOM   2848 N  N   . ASN A 1 371  ? 23.663 36.339  27.721  1.00 16.73 ? 371  ASN A N   1 
ATOM   2849 C  CA  . ASN A 1 371  ? 24.455 35.533  26.787  1.00 16.12 ? 371  ASN A CA  1 
ATOM   2850 C  C   . ASN A 1 371  ? 25.231 36.447  25.841  1.00 15.74 ? 371  ASN A C   1 
ATOM   2851 O  O   . ASN A 1 371  ? 25.254 36.242  24.624  1.00 14.84 ? 371  ASN A O   1 
ATOM   2852 C  CB  . ASN A 1 371  ? 23.566 34.587  26.002  1.00 16.93 ? 371  ASN A CB  1 
ATOM   2853 C  CG  . ASN A 1 371  ? 22.964 33.518  26.893  1.00 17.07 ? 371  ASN A CG  1 
ATOM   2854 O  OD1 . ASN A 1 371  ? 23.686 32.703  27.474  1.00 16.01 ? 371  ASN A OD1 1 
ATOM   2855 N  ND2 . ASN A 1 371  ? 21.654 33.533  27.021  1.00 15.78 ? 371  ASN A ND2 1 
ATOM   2856 N  N   . VAL A 1 372  ? 25.866 37.456  26.430  1.00 15.41 ? 372  VAL A N   1 
ATOM   2857 C  CA  . VAL A 1 372  ? 26.668 38.451  25.701  1.00 15.16 ? 372  VAL A CA  1 
ATOM   2858 C  C   . VAL A 1 372  ? 28.061 38.559  26.316  1.00 15.76 ? 372  VAL A C   1 
ATOM   2859 O  O   . VAL A 1 372  ? 28.213 38.430  27.525  1.00 15.61 ? 372  VAL A O   1 
ATOM   2860 C  CB  . VAL A 1 372  ? 26.046 39.867  25.825  1.00 15.63 ? 372  VAL A CB  1 
ATOM   2861 C  CG1 . VAL A 1 372  ? 27.043 40.927  25.290  1.00 14.05 ? 372  VAL A CG1 1 
ATOM   2862 C  CG2 . VAL A 1 372  ? 24.723 39.933  25.068  1.00 14.63 ? 372  VAL A CG2 1 
ATOM   2863 N  N   . GLN A 1 373  ? 29.076 38.758  25.488  1.00 15.86 ? 373  GLN A N   1 
ATOM   2864 C  CA  . GLN A 1 373  ? 30.440 38.981  25.997  1.00 17.01 ? 373  GLN A CA  1 
ATOM   2865 C  C   . GLN A 1 373  ? 30.861 40.282  25.278  1.00 16.46 ? 373  GLN A C   1 
ATOM   2866 O  O   . GLN A 1 373  ? 31.080 40.292  24.088  1.00 14.92 ? 373  GLN A O   1 
ATOM   2867 C  CB  . GLN A 1 373  ? 31.398 37.822  25.644  1.00 17.33 ? 373  GLN A CB  1 
ATOM   2868 C  CG  . GLN A 1 373  ? 32.879 38.116  25.996  1.00 17.79 ? 373  GLN A CG  1 
ATOM   2869 C  CD  . GLN A 1 373  ? 33.140 38.479  27.492  1.00 19.76 ? 373  GLN A CD  1 
ATOM   2870 O  OE1 . GLN A 1 373  ? 34.034 39.278  27.805  1.00 19.85 ? 373  GLN A OE1 1 
ATOM   2871 N  NE2 . GLN A 1 373  ? 32.393 37.871  28.396  1.00 16.96 ? 373  GLN A NE2 1 
ATOM   2872 N  N   . ALA A 1 374  ? 30.923 41.383  26.012  1.00 16.25 ? 374  ALA A N   1 
ATOM   2873 C  CA  . ALA A 1 374  ? 31.248 42.663  25.427  1.00 15.84 ? 374  ALA A CA  1 
ATOM   2874 C  C   . ALA A 1 374  ? 32.569 43.178  25.965  1.00 17.31 ? 374  ALA A C   1 
ATOM   2875 O  O   . ALA A 1 374  ? 32.905 42.931  27.138  1.00 15.25 ? 374  ALA A O   1 
ATOM   2876 C  CB  . ALA A 1 374  ? 30.157 43.657  25.754  1.00 15.41 ? 374  ALA A CB  1 
ATOM   2877 N  N   . GLN A 1 375  ? 33.293 43.912  25.112  1.00 16.44 ? 375  GLN A N   1 
ATOM   2878 C  CA  . GLN A 1 375  ? 34.575 44.497  25.492  1.00 17.40 ? 375  GLN A CA  1 
ATOM   2879 C  C   . GLN A 1 375  ? 35.013 45.538  24.477  1.00 16.25 ? 375  GLN A C   1 
ATOM   2880 O  O   . GLN A 1 375  ? 34.477 45.604  23.370  1.00 14.28 ? 375  GLN A O   1 
ATOM   2881 C  CB  . GLN A 1 375  ? 35.680 43.433  25.573  1.00 19.97 ? 375  GLN A CB  1 
ATOM   2882 C  CG  . GLN A 1 375  ? 35.958 42.715  24.266  1.00 24.66 ? 375  GLN A CG  1 
ATOM   2883 C  CD  . GLN A 1 375  ? 35.057 41.513  24.087  1.00 29.10 ? 375  GLN A CD  1 
ATOM   2884 O  OE1 . GLN A 1 375  ? 34.053 41.547  23.341  1.00 31.79 ? 375  GLN A OE1 1 
ATOM   2885 N  NE2 . GLN A 1 375  ? 35.388 40.438  24.788  1.00 29.24 ? 375  GLN A NE2 1 
ATOM   2886 N  N   . PHE A 1 376  ? 35.990 46.349  24.863  1.00 13.87 ? 376  PHE A N   1 
ATOM   2887 C  CA  . PHE A 1 376  ? 36.520 47.331  23.943  1.00 13.58 ? 376  PHE A CA  1 
ATOM   2888 C  C   . PHE A 1 376  ? 37.304 46.531  22.891  1.00 12.63 ? 376  PHE A C   1 
ATOM   2889 O  O   . PHE A 1 376  ? 37.873 45.480  23.183  1.00 12.42 ? 376  PHE A O   1 
ATOM   2890 C  CB  . PHE A 1 376  ? 37.456 48.310  24.674  1.00 12.68 ? 376  PHE A CB  1 
ATOM   2891 C  CG  . PHE A 1 376  ? 36.739 49.237  25.616  1.00 13.43 ? 376  PHE A CG  1 
ATOM   2892 C  CD1 . PHE A 1 376  ? 37.106 49.314  26.951  1.00 13.13 ? 376  PHE A CD1 1 
ATOM   2893 C  CD2 . PHE A 1 376  ? 35.695 50.054  25.155  1.00 11.99 ? 376  PHE A CD2 1 
ATOM   2894 C  CE1 . PHE A 1 376  ? 36.463 50.186  27.828  1.00 11.69 ? 376  PHE A CE1 1 
ATOM   2895 C  CE2 . PHE A 1 376  ? 35.042 50.940  26.041  1.00 12.57 ? 376  PHE A CE2 1 
ATOM   2896 C  CZ  . PHE A 1 376  ? 35.442 50.994  27.382  1.00 11.26 ? 376  PHE A CZ  1 
ATOM   2897 N  N   . GLY A 1 377  ? 37.312 47.004  21.661  1.00 11.90 ? 377  GLY A N   1 
ATOM   2898 C  CA  . GLY A 1 377  ? 38.069 46.281  20.640  1.00 11.33 ? 377  GLY A CA  1 
ATOM   2899 C  C   . GLY A 1 377  ? 38.492 47.219  19.526  1.00 12.20 ? 377  GLY A C   1 
ATOM   2900 O  O   . GLY A 1 377  ? 38.103 48.402  19.520  1.00 10.74 ? 377  GLY A O   1 
ATOM   2901 N  N   . THR A 1 378  ? 39.294 46.704  18.592  1.00 11.30 ? 378  THR A N   1 
ATOM   2902 C  CA  . THR A 1 378  ? 39.705 47.489  17.439  1.00 12.86 ? 378  THR A CA  1 
ATOM   2903 C  C   . THR A 1 378  ? 38.923 46.963  16.228  1.00 11.23 ? 378  THR A C   1 
ATOM   2904 O  O   . THR A 1 378  ? 38.203 45.951  16.305  1.00 10.78 ? 378  THR A O   1 
ATOM   2905 C  CB  . THR A 1 378  ? 41.215 47.350  17.134  1.00 12.60 ? 378  THR A CB  1 
ATOM   2906 O  OG1 . THR A 1 378  ? 41.493 45.998  16.794  1.00 14.91 ? 378  THR A OG1 1 
ATOM   2907 C  CG2 . THR A 1 378  ? 42.045 47.729  18.351  1.00 14.17 ? 378  THR A CG2 1 
ATOM   2908 N  N   . LEU A 1 379  ? 39.056 47.656  15.112  1.00 10.00 ? 379  LEU A N   1 
ATOM   2909 C  CA  . LEU A 1 379  ? 38.368 47.263  13.894  1.00 9.76  ? 379  LEU A CA  1 
ATOM   2910 C  C   . LEU A 1 379  ? 38.846 45.878  13.406  1.00 9.77  ? 379  LEU A C   1 
ATOM   2911 O  O   . LEU A 1 379  ? 38.037 45.025  13.060  1.00 9.56  ? 379  LEU A O   1 
ATOM   2912 C  CB  . LEU A 1 379  ? 38.631 48.329  12.832  1.00 10.11 ? 379  LEU A CB  1 
ATOM   2913 C  CG  . LEU A 1 379  ? 37.870 48.088  11.535  1.00 11.16 ? 379  LEU A CG  1 
ATOM   2914 C  CD1 . LEU A 1 379  ? 36.363 48.120  11.840  1.00 8.50  ? 379  LEU A CD1 1 
ATOM   2915 C  CD2 . LEU A 1 379  ? 38.288 49.188  10.479  1.00 7.97  ? 379  LEU A CD2 1 
ATOM   2916 N  N   . GLN A 1 380  ? 40.160 45.655  13.401  1.00 11.38 ? 380  GLN A N   1 
ATOM   2917 C  CA  . GLN A 1 380  ? 40.717 44.369  12.945  1.00 13.49 ? 380  GLN A CA  1 
ATOM   2918 C  C   . GLN A 1 380  ? 40.225 43.215  13.843  1.00 13.46 ? 380  GLN A C   1 
ATOM   2919 O  O   . GLN A 1 380  ? 40.010 42.093  13.371  1.00 13.28 ? 380  GLN A O   1 
ATOM   2920 C  CB  . GLN A 1 380  ? 42.244 44.412  12.965  1.00 15.51 ? 380  GLN A CB  1 
ATOM   2921 C  CG  . GLN A 1 380  ? 42.910 43.185  12.391  1.00 20.47 ? 380  GLN A CG  1 
ATOM   2922 C  CD  . GLN A 1 380  ? 42.561 42.969  10.927  1.00 25.46 ? 380  GLN A CD  1 
ATOM   2923 O  OE1 . GLN A 1 380  ? 42.643 43.902  10.104  1.00 26.61 ? 380  GLN A OE1 1 
ATOM   2924 N  NE2 . GLN A 1 380  ? 42.188 41.734  10.580  1.00 26.62 ? 380  GLN A NE2 1 
ATOM   2925 N  N   . GLU A 1 381  ? 40.080 43.484  15.135  1.00 12.66 ? 381  GLU A N   1 
ATOM   2926 C  CA  . GLU A 1 381  ? 39.593 42.447  16.040  1.00 13.98 ? 381  GLU A CA  1 
ATOM   2927 C  C   . GLU A 1 381  ? 38.199 42.011  15.605  1.00 12.20 ? 381  GLU A C   1 
ATOM   2928 O  O   . GLU A 1 381  ? 37.876 40.839  15.635  1.00 11.89 ? 381  GLU A O   1 
ATOM   2929 C  CB  . GLU A 1 381  ? 39.489 42.956  17.462  1.00 15.58 ? 381  GLU A CB  1 
ATOM   2930 C  CG  . GLU A 1 381  ? 40.774 42.932  18.261  1.00 20.27 ? 381  GLU A CG  1 
ATOM   2931 C  CD  . GLU A 1 381  ? 40.491 43.326  19.700  1.00 22.19 ? 381  GLU A CD  1 
ATOM   2932 O  OE1 . GLU A 1 381  ? 40.610 44.509  20.017  1.00 19.79 ? 381  GLU A OE1 1 
ATOM   2933 O  OE2 . GLU A 1 381  ? 40.096 42.445  20.511  1.00 27.97 ? 381  GLU A OE2 1 
ATOM   2934 N  N   . TYR A 1 382  ? 37.363 42.983  15.274  1.00 10.85 ? 382  TYR A N   1 
ATOM   2935 C  CA  . TYR A 1 382  ? 36.022 42.704  14.820  1.00 10.60 ? 382  TYR A CA  1 
ATOM   2936 C  C   . TYR A 1 382  ? 36.069 41.830  13.569  1.00 10.56 ? 382  TYR A C   1 
ATOM   2937 O  O   . TYR A 1 382  ? 35.470 40.760  13.526  1.00 10.86 ? 382  TYR A O   1 
ATOM   2938 C  CB  . TYR A 1 382  ? 35.289 44.001  14.479  1.00 10.67 ? 382  TYR A CB  1 
ATOM   2939 C  CG  . TYR A 1 382  ? 33.960 43.734  13.803  1.00 12.57 ? 382  TYR A CG  1 
ATOM   2940 C  CD1 . TYR A 1 382  ? 32.900 43.139  14.508  1.00 12.09 ? 382  TYR A CD1 1 
ATOM   2941 C  CD2 . TYR A 1 382  ? 33.805 43.958  12.429  1.00 11.00 ? 382  TYR A CD2 1 
ATOM   2942 C  CE1 . TYR A 1 382  ? 31.726 42.771  13.863  1.00 12.50 ? 382  TYR A CE1 1 
ATOM   2943 C  CE2 . TYR A 1 382  ? 32.648 43.590  11.778  1.00 12.57 ? 382  TYR A CE2 1 
ATOM   2944 C  CZ  . TYR A 1 382  ? 31.607 42.999  12.496  1.00 12.55 ? 382  TYR A CZ  1 
ATOM   2945 O  OH  . TYR A 1 382  ? 30.448 42.655  11.845  1.00 13.90 ? 382  TYR A OH  1 
ATOM   2946 N  N   . PHE A 1 383  ? 36.775 42.295  12.537  1.00 9.34  ? 383  PHE A N   1 
ATOM   2947 C  CA  . PHE A 1 383  ? 36.853 41.529  11.299  1.00 9.20  ? 383  PHE A CA  1 
ATOM   2948 C  C   . PHE A 1 383  ? 37.439 40.119  11.507  1.00 10.34 ? 383  PHE A C   1 
ATOM   2949 O  O   . PHE A 1 383  ? 36.919 39.148  10.930  1.00 9.72  ? 383  PHE A O   1 
ATOM   2950 C  CB  . PHE A 1 383  ? 37.656 42.304  10.259  1.00 9.58  ? 383  PHE A CB  1 
ATOM   2951 C  CG  . PHE A 1 383  ? 36.869 43.435  9.603   1.00 8.73  ? 383  PHE A CG  1 
ATOM   2952 C  CD1 . PHE A 1 383  ? 37.349 44.726  9.637   1.00 10.03 ? 383  PHE A CD1 1 
ATOM   2953 C  CD2 . PHE A 1 383  ? 35.646 43.179  8.970   1.00 10.76 ? 383  PHE A CD2 1 
ATOM   2954 C  CE1 . PHE A 1 383  ? 36.634 45.768  9.055   1.00 10.61 ? 383  PHE A CE1 1 
ATOM   2955 C  CE2 . PHE A 1 383  ? 34.900 44.210  8.368   1.00 12.42 ? 383  PHE A CE2 1 
ATOM   2956 C  CZ  . PHE A 1 383  ? 35.391 45.502  8.409   1.00 12.30 ? 383  PHE A CZ  1 
ATOM   2957 N  N   . ASP A 1 384  ? 38.475 39.982  12.340  1.00 10.22 ? 384  ASP A N   1 
ATOM   2958 C  CA  . ASP A 1 384  ? 39.051 38.642  12.555  1.00 11.92 ? 384  ASP A CA  1 
ATOM   2959 C  C   . ASP A 1 384  ? 38.011 37.708  13.163  1.00 11.96 ? 384  ASP A C   1 
ATOM   2960 O  O   . ASP A 1 384  ? 37.894 36.546  12.773  1.00 12.96 ? 384  ASP A O   1 
ATOM   2961 C  CB  . ASP A 1 384  ? 40.255 38.678  13.505  1.00 14.34 ? 384  ASP A CB  1 
ATOM   2962 C  CG  . ASP A 1 384  ? 41.451 39.358  12.905  1.00 15.12 ? 384  ASP A CG  1 
ATOM   2963 O  OD1 . ASP A 1 384  ? 41.544 39.462  11.658  1.00 15.73 ? 384  ASP A OD1 1 
ATOM   2964 O  OD2 . ASP A 1 384  ? 42.309 39.789  13.692  1.00 20.65 ? 384  ASP A OD2 1 
ATOM   2965 N  N   . ALA A 1 385  ? 37.229 38.220  14.100  1.00 11.79 ? 385  ALA A N   1 
ATOM   2966 C  CA  . ALA A 1 385  ? 36.229 37.387  14.757  1.00 12.57 ? 385  ALA A CA  1 
ATOM   2967 C  C   . ALA A 1 385  ? 35.140 37.006  13.745  1.00 13.09 ? 385  ALA A C   1 
ATOM   2968 O  O   . ALA A 1 385  ? 34.667 35.859  13.729  1.00 12.68 ? 385  ALA A O   1 
ATOM   2969 C  CB  . ALA A 1 385  ? 35.619 38.143  15.979  1.00 11.68 ? 385  ALA A CB  1 
ATOM   2970 N  N   . VAL A 1 386  ? 34.765 37.959  12.887  1.00 11.59 ? 386  VAL A N   1 
ATOM   2971 C  CA  . VAL A 1 386  ? 33.745 37.700  11.874  1.00 12.01 ? 386  VAL A CA  1 
ATOM   2972 C  C   . VAL A 1 386  ? 34.158 36.547  10.973  1.00 13.49 ? 386  VAL A C   1 
ATOM   2973 O  O   . VAL A 1 386  ? 33.366 35.629  10.696  1.00 13.38 ? 386  VAL A O   1 
ATOM   2974 C  CB  . VAL A 1 386  ? 33.514 38.938  10.976  1.00 11.96 ? 386  VAL A CB  1 
ATOM   2975 C  CG1 . VAL A 1 386  ? 32.714 38.562  9.726   1.00 11.19 ? 386  VAL A CG1 1 
ATOM   2976 C  CG2 . VAL A 1 386  ? 32.750 40.009  11.778  1.00 11.33 ? 386  VAL A CG2 1 
ATOM   2977 N  N   . HIS A 1 387  ? 35.402 36.580  10.524  1.00 12.57 ? 387  HIS A N   1 
ATOM   2978 C  CA  . HIS A 1 387  ? 35.877 35.549  9.618   1.00 13.74 ? 387  HIS A CA  1 
ATOM   2979 C  C   . HIS A 1 387  ? 36.054 34.220  10.327  1.00 14.03 ? 387  HIS A C   1 
ATOM   2980 O  O   . HIS A 1 387  ? 35.903 33.142  9.713   1.00 12.77 ? 387  HIS A O   1 
ATOM   2981 C  CB  . HIS A 1 387  ? 37.150 36.033  8.903   1.00 13.83 ? 387  HIS A CB  1 
ATOM   2982 C  CG  . HIS A 1 387  ? 36.884 37.162  7.951   1.00 16.27 ? 387  HIS A CG  1 
ATOM   2983 N  ND1 . HIS A 1 387  ? 36.030 37.034  6.873   1.00 15.74 ? 387  HIS A ND1 1 
ATOM   2984 C  CD2 . HIS A 1 387  ? 37.286 38.458  7.957   1.00 17.04 ? 387  HIS A CD2 1 
ATOM   2985 C  CE1 . HIS A 1 387  ? 35.912 38.202  6.261   1.00 16.98 ? 387  HIS A CE1 1 
ATOM   2986 N  NE2 . HIS A 1 387  ? 36.665 39.085  6.898   1.00 17.17 ? 387  HIS A NE2 1 
ATOM   2987 N  N   . GLN A 1 388  ? 36.369 34.289  11.616  1.00 15.48 ? 388  GLN A N   1 
ATOM   2988 C  CA  . GLN A 1 388  ? 36.475 33.065  12.397  1.00 18.17 ? 388  GLN A CA  1 
ATOM   2989 C  C   . GLN A 1 388  ? 35.059 32.451  12.408  1.00 17.86 ? 388  GLN A C   1 
ATOM   2990 O  O   . GLN A 1 388  ? 34.915 31.247  12.237  1.00 18.99 ? 388  GLN A O   1 
ATOM   2991 C  CB  . GLN A 1 388  ? 36.948 33.352  13.823  1.00 20.86 ? 388  GLN A CB  1 
ATOM   2992 C  CG  . GLN A 1 388  ? 38.445 33.690  13.907  1.00 26.70 ? 388  GLN A CG  1 
ATOM   2993 C  CD  . GLN A 1 388  ? 38.843 34.392  15.225  1.00 30.92 ? 388  GLN A CD  1 
ATOM   2994 O  OE1 . GLN A 1 388  ? 38.017 34.552  16.140  1.00 34.91 ? 388  GLN A OE1 1 
ATOM   2995 N  NE2 . GLN A 1 388  ? 40.113 34.813  15.322  1.00 31.40 ? 388  GLN A NE2 1 
ATOM   2996 N  N   . ALA A 1 389  ? 34.017 33.266  12.560  1.00 17.91 ? 389  ALA A N   1 
ATOM   2997 C  CA  . ALA A 1 389  ? 32.648 32.723  12.578  1.00 19.10 ? 389  ALA A CA  1 
ATOM   2998 C  C   . ALA A 1 389  ? 32.341 32.138  11.214  1.00 19.89 ? 389  ALA A C   1 
ATOM   2999 O  O   . ALA A 1 389  ? 31.757 31.044  11.087  1.00 20.36 ? 389  ALA A O   1 
ATOM   3000 C  CB  . ALA A 1 389  ? 31.629 33.810  12.950  1.00 17.96 ? 389  ALA A CB  1 
ATOM   3001 N  N   . GLU A 1 390  ? 32.768 32.863  10.188  1.00 21.85 ? 390  GLU A N   1 
ATOM   3002 C  CA  . GLU A 1 390  ? 32.597 32.447  8.803   1.00 22.72 ? 390  GLU A CA  1 
ATOM   3003 C  C   . GLU A 1 390  ? 33.232 31.072  8.572   1.00 24.02 ? 390  GLU A C   1 
ATOM   3004 O  O   . GLU A 1 390  ? 32.603 30.179  8.028   1.00 23.63 ? 390  GLU A O   1 
ATOM   3005 C  CB  . GLU A 1 390  ? 33.267 33.459  7.873   1.00 23.23 ? 390  GLU A CB  1 
ATOM   3006 C  CG  . GLU A 1 390  ? 33.200 33.077  6.395   1.00 22.55 ? 390  GLU A CG  1 
ATOM   3007 C  CD  . GLU A 1 390  ? 33.855 34.111  5.484   1.00 22.86 ? 390  GLU A CD  1 
ATOM   3008 O  OE1 . GLU A 1 390  ? 34.697 34.917  5.955   1.00 21.67 ? 390  GLU A OE1 1 
ATOM   3009 O  OE2 . GLU A 1 390  ? 33.530 34.106  4.284   1.00 23.36 ? 390  GLU A OE2 1 
ATOM   3010 N  N   . ARG A 1 391  ? 34.492 30.922  8.970   1.00 25.42 ? 391  ARG A N   1 
ATOM   3011 C  CA  . ARG A 1 391  ? 35.194 29.661  8.804   1.00 26.60 ? 391  ARG A CA  1 
ATOM   3012 C  C   . ARG A 1 391  ? 34.550 28.524  9.612   1.00 26.60 ? 391  ARG A C   1 
ATOM   3013 O  O   . ARG A 1 391  ? 34.631 27.366  9.225   1.00 27.34 ? 391  ARG A O   1 
ATOM   3014 C  CB  . ARG A 1 391  ? 36.678 29.812  9.198   1.00 28.04 ? 391  ARG A CB  1 
ATOM   3015 C  CG  . ARG A 1 391  ? 37.523 30.557  8.144   1.00 29.43 ? 391  ARG A CG  1 
ATOM   3016 C  CD  . ARG A 1 391  ? 39.020 30.406  8.390   1.00 30.36 ? 391  ARG A CD  1 
ATOM   3017 N  NE  . ARG A 1 391  ? 39.459 31.027  9.636   1.00 32.14 ? 391  ARG A NE  1 
ATOM   3018 C  CZ  . ARG A 1 391  ? 39.577 32.343  9.817   1.00 31.45 ? 391  ARG A CZ  1 
ATOM   3019 N  NH1 . ARG A 1 391  ? 39.287 33.186  8.828   1.00 31.43 ? 391  ARG A NH1 1 
ATOM   3020 N  NH2 . ARG A 1 391  ? 39.986 32.815  10.984  1.00 31.15 ? 391  ARG A NH2 1 
ATOM   3021 N  N   . ALA A 1 392  ? 33.901 28.848  10.724  1.00 26.72 ? 392  ALA A N   1 
ATOM   3022 C  CA  . ALA A 1 392  ? 33.270 27.820  11.546  1.00 27.25 ? 392  ALA A CA  1 
ATOM   3023 C  C   . ALA A 1 392  ? 31.969 27.394  10.882  1.00 28.03 ? 392  ALA A C   1 
ATOM   3024 O  O   . ALA A 1 392  ? 31.236 26.550  11.411  1.00 27.79 ? 392  ALA A O   1 
ATOM   3025 C  CB  . ALA A 1 392  ? 32.991 28.340  12.945  1.00 26.94 ? 392  ALA A CB  1 
ATOM   3026 N  N   . GLY A 1 393  ? 31.691 27.994  9.721   1.00 27.69 ? 393  GLY A N   1 
ATOM   3027 C  CA  . GLY A 1 393  ? 30.490 27.659  8.994   1.00 27.18 ? 393  GLY A CA  1 
ATOM   3028 C  C   . GLY A 1 393  ? 29.232 28.283  9.544   1.00 26.46 ? 393  GLY A C   1 
ATOM   3029 O  O   . GLY A 1 393  ? 28.141 27.794  9.283   1.00 26.52 ? 393  GLY A O   1 
ATOM   3030 N  N   . GLN A 1 394  ? 29.333 29.371  10.296  1.00 26.17 ? 394  GLN A N   1 
ATOM   3031 C  CA  . GLN A 1 394  ? 28.083 29.919  10.773  1.00 26.74 ? 394  GLN A CA  1 
ATOM   3032 C  C   . GLN A 1 394  ? 27.451 30.973  9.883   1.00 25.48 ? 394  GLN A C   1 
ATOM   3033 O  O   . GLN A 1 394  ? 26.342 31.411  10.145  1.00 26.98 ? 394  GLN A O   1 
ATOM   3034 C  CB  . GLN A 1 394  ? 28.199 30.399  12.227  1.00 28.56 ? 394  GLN A CB  1 
ATOM   3035 C  CG  . GLN A 1 394  ? 29.089 31.562  12.499  1.00 31.55 ? 394  GLN A CG  1 
ATOM   3036 C  CD  . GLN A 1 394  ? 28.749 32.226  13.841  1.00 32.05 ? 394  GLN A CD  1 
ATOM   3037 O  OE1 . GLN A 1 394  ? 27.959 33.183  13.902  1.00 31.26 ? 394  GLN A OE1 1 
ATOM   3038 N  NE2 . GLN A 1 394  ? 29.344 31.710  14.919  1.00 32.38 ? 394  GLN A NE2 1 
ATOM   3039 N  N   . ALA A 1 395  ? 28.130 31.350  8.803   1.00 24.47 ? 395  ALA A N   1 
ATOM   3040 C  CA  . ALA A 1 395  ? 27.609 32.333  7.874   1.00 23.05 ? 395  ALA A CA  1 
ATOM   3041 C  C   . ALA A 1 395  ? 28.315 32.249  6.532   1.00 23.06 ? 395  ALA A C   1 
ATOM   3042 O  O   . ALA A 1 395  ? 29.446 31.779  6.440   1.00 23.58 ? 395  ALA A O   1 
ATOM   3043 C  CB  . ALA A 1 395  ? 27.770 33.746  8.454   1.00 24.14 ? 395  ALA A CB  1 
ATOM   3044 N  N   . GLU A 1 396  ? 27.626 32.675  5.484   1.00 22.91 ? 396  GLU A N   1 
ATOM   3045 C  CA  . GLU A 1 396  ? 28.196 32.731  4.133   1.00 23.85 ? 396  GLU A CA  1 
ATOM   3046 C  C   . GLU A 1 396  ? 27.779 34.119  3.664   1.00 21.91 ? 396  GLU A C   1 
ATOM   3047 O  O   . GLU A 1 396  ? 26.647 34.574  3.926   1.00 21.99 ? 396  GLU A O   1 
ATOM   3048 C  CB  . GLU A 1 396  ? 27.590 31.662  3.231   1.00 28.01 ? 396  GLU A CB  1 
ATOM   3049 C  CG  . GLU A 1 396  ? 26.094 31.837  2.987   1.00 34.14 ? 396  GLU A CG  1 
ATOM   3050 C  CD  . GLU A 1 396  ? 25.466 30.594  2.351   1.00 38.19 ? 396  GLU A CD  1 
ATOM   3051 O  OE1 . GLU A 1 396  ? 26.055 30.047  1.383   1.00 40.41 ? 396  GLU A OE1 1 
ATOM   3052 O  OE2 . GLU A 1 396  ? 24.379 30.174  2.817   1.00 40.78 ? 396  GLU A OE2 1 
ATOM   3053 N  N   . PHE A 1 397  ? 28.669 34.808  2.982   1.00 18.43 ? 397  PHE A N   1 
ATOM   3054 C  CA  . PHE A 1 397  ? 28.344 36.160  2.584   1.00 15.40 ? 397  PHE A CA  1 
ATOM   3055 C  C   . PHE A 1 397  ? 27.994 36.335  1.120   1.00 14.30 ? 397  PHE A C   1 
ATOM   3056 O  O   . PHE A 1 397  ? 28.548 35.686  0.253   1.00 13.57 ? 397  PHE A O   1 
ATOM   3057 C  CB  . PHE A 1 397  ? 29.489 37.102  2.958   1.00 14.25 ? 397  PHE A CB  1 
ATOM   3058 C  CG  . PHE A 1 397  ? 29.766 37.154  4.442   1.00 14.32 ? 397  PHE A CG  1 
ATOM   3059 C  CD1 . PHE A 1 397  ? 30.864 36.475  4.991   1.00 13.45 ? 397  PHE A CD1 1 
ATOM   3060 C  CD2 . PHE A 1 397  ? 28.925 37.847  5.284   1.00 11.85 ? 397  PHE A CD2 1 
ATOM   3061 C  CE1 . PHE A 1 397  ? 31.106 36.497  6.381   1.00 13.37 ? 397  PHE A CE1 1 
ATOM   3062 C  CE2 . PHE A 1 397  ? 29.147 37.878  6.657   1.00 13.17 ? 397  PHE A CE2 1 
ATOM   3063 C  CZ  . PHE A 1 397  ? 30.249 37.197  7.211   1.00 12.63 ? 397  PHE A CZ  1 
ATOM   3064 N  N   . PRO A 1 398  ? 27.049 37.229  0.840   1.00 13.43 ? 398  PRO A N   1 
ATOM   3065 C  CA  . PRO A 1 398  ? 26.616 37.504  -0.526  1.00 13.50 ? 398  PRO A CA  1 
ATOM   3066 C  C   . PRO A 1 398  ? 27.707 38.270  -1.289  1.00 13.81 ? 398  PRO A C   1 
ATOM   3067 O  O   . PRO A 1 398  ? 28.570 38.936  -0.673  1.00 14.66 ? 398  PRO A O   1 
ATOM   3068 C  CB  . PRO A 1 398  ? 25.389 38.374  -0.307  1.00 12.17 ? 398  PRO A CB  1 
ATOM   3069 C  CG  . PRO A 1 398  ? 25.792 39.150  0.924   1.00 13.88 ? 398  PRO A CG  1 
ATOM   3070 C  CD  . PRO A 1 398  ? 26.311 38.063  1.801   1.00 13.21 ? 398  PRO A CD  1 
ATOM   3071 N  N   . THR A 1 399  ? 27.661 38.181  -2.615  1.00 11.44 ? 399  THR A N   1 
ATOM   3072 C  CA  . THR A 1 399  ? 28.593 38.908  -3.452  1.00 11.47 ? 399  THR A CA  1 
ATOM   3073 C  C   . THR A 1 399  ? 27.855 40.167  -3.957  1.00 11.35 ? 399  THR A C   1 
ATOM   3074 O  O   . THR A 1 399  ? 26.623 40.185  -4.070  1.00 11.19 ? 399  THR A O   1 
ATOM   3075 C  CB  . THR A 1 399  ? 29.027 38.074  -4.665  1.00 11.94 ? 399  THR A CB  1 
ATOM   3076 O  OG1 . THR A 1 399  ? 27.859 37.645  -5.369  1.00 12.06 ? 399  THR A OG1 1 
ATOM   3077 C  CG2 . THR A 1 399  ? 29.860 36.861  -4.207  1.00 11.59 ? 399  THR A CG2 1 
ATOM   3078 N  N   . LEU A 1 400  ? 28.610 41.208  -4.273  1.00 10.51 ? 400  LEU A N   1 
ATOM   3079 C  CA  . LEU A 1 400  ? 28.005 42.459  -4.738  1.00 9.40  ? 400  LEU A CA  1 
ATOM   3080 C  C   . LEU A 1 400  ? 28.936 43.204  -5.677  1.00 10.63 ? 400  LEU A C   1 
ATOM   3081 O  O   . LEU A 1 400  ? 30.173 43.101  -5.533  1.00 10.69 ? 400  LEU A O   1 
ATOM   3082 C  CB  . LEU A 1 400  ? 27.718 43.333  -3.528  1.00 9.42  ? 400  LEU A CB  1 
ATOM   3083 C  CG  . LEU A 1 400  ? 26.980 44.668  -3.763  1.00 10.56 ? 400  LEU A CG  1 
ATOM   3084 C  CD1 . LEU A 1 400  ? 26.227 44.997  -2.510  1.00 9.69  ? 400  LEU A CD1 1 
ATOM   3085 C  CD2 . LEU A 1 400  ? 27.967 45.821  -4.122  1.00 11.95 ? 400  LEU A CD2 1 
ATOM   3086 N  N   . SER A 1 401  ? 28.365 43.922  -6.652  1.00 10.64 ? 401  SER A N   1 
ATOM   3087 C  CA  . SER A 1 401  ? 29.137 44.770  -7.564  1.00 9.27  ? 401  SER A CA  1 
ATOM   3088 C  C   . SER A 1 401  ? 28.270 46.025  -7.732  1.00 10.08 ? 401  SER A C   1 
ATOM   3089 O  O   . SER A 1 401  ? 27.072 45.971  -7.513  1.00 7.78  ? 401  SER A O   1 
ATOM   3090 C  CB  . SER A 1 401  ? 29.402 44.098  -8.934  1.00 11.35 ? 401  SER A CB  1 
ATOM   3091 O  OG  . SER A 1 401  ? 28.308 44.193  -9.827  1.00 9.80  ? 401  SER A OG  1 
ATOM   3092 N  N   . GLY A 1 402  ? 28.891 47.150  -8.075  1.00 9.07  ? 402  GLY A N   1 
ATOM   3093 C  CA  . GLY A 1 402  ? 28.162 48.388  -8.243  1.00 8.36  ? 402  GLY A CA  1 
ATOM   3094 C  C   . GLY A 1 402  ? 28.781 49.478  -7.373  1.00 8.85  ? 402  GLY A C   1 
ATOM   3095 O  O   . GLY A 1 402  ? 29.826 49.253  -6.756  1.00 6.91  ? 402  GLY A O   1 
ATOM   3096 N  N   . ASP A 1 403  ? 28.161 50.659  -7.326  1.00 8.44  ? 403  ASP A N   1 
ATOM   3097 C  CA  . ASP A 1 403  ? 28.688 51.740  -6.490  1.00 8.57  ? 403  ASP A CA  1 
ATOM   3098 C  C   . ASP A 1 403  ? 27.577 52.232  -5.575  1.00 8.53  ? 403  ASP A C   1 
ATOM   3099 O  O   . ASP A 1 403  ? 26.470 51.675  -5.584  1.00 7.31  ? 403  ASP A O   1 
ATOM   3100 C  CB  . ASP A 1 403  ? 29.204 52.888  -7.356  1.00 8.78  ? 403  ASP A CB  1 
ATOM   3101 C  CG  . ASP A 1 403  ? 28.090 53.640  -8.078  1.00 10.26 ? 403  ASP A CG  1 
ATOM   3102 O  OD1 . ASP A 1 403  ? 26.957 53.144  -8.187  1.00 12.58 ? 403  ASP A OD1 1 
ATOM   3103 O  OD2 . ASP A 1 403  ? 28.360 54.748  -8.566  1.00 10.71 ? 403  ASP A OD2 1 
ATOM   3104 N  N   . PHE A 1 404  ? 27.874 53.254  -4.786  1.00 6.97  ? 404  PHE A N   1 
ATOM   3105 C  CA  . PHE A 1 404  ? 26.918 53.816  -3.859  1.00 7.37  ? 404  PHE A CA  1 
ATOM   3106 C  C   . PHE A 1 404  ? 26.784 55.310  -3.993  1.00 9.07  ? 404  PHE A C   1 
ATOM   3107 O  O   . PHE A 1 404  ? 26.982 56.055  -3.017  1.00 6.70  ? 404  PHE A O   1 
ATOM   3108 C  CB  . PHE A 1 404  ? 27.265 53.435  -2.407  1.00 7.57  ? 404  PHE A CB  1 
ATOM   3109 C  CG  . PHE A 1 404  ? 27.194 51.941  -2.165  1.00 7.94  ? 404  PHE A CG  1 
ATOM   3110 C  CD1 . PHE A 1 404  ? 28.355 51.161  -2.176  1.00 6.35  ? 404  PHE A CD1 1 
ATOM   3111 C  CD2 . PHE A 1 404  ? 25.958 51.306  -2.033  1.00 7.40  ? 404  PHE A CD2 1 
ATOM   3112 C  CE1 . PHE A 1 404  ? 28.290 49.758  -2.058  1.00 9.69  ? 404  PHE A CE1 1 
ATOM   3113 C  CE2 . PHE A 1 404  ? 25.874 49.897  -1.914  1.00 7.90  ? 404  PHE A CE2 1 
ATOM   3114 C  CZ  . PHE A 1 404  ? 27.037 49.122  -1.926  1.00 8.52  ? 404  PHE A CZ  1 
ATOM   3115 N  N   . PHE A 1 405  ? 26.446 55.719  -5.224  1.00 9.44  ? 405  PHE A N   1 
ATOM   3116 C  CA  . PHE A 1 405  ? 26.179 57.116  -5.564  1.00 10.52 ? 405  PHE A CA  1 
ATOM   3117 C  C   . PHE A 1 405  ? 24.819 57.069  -6.259  1.00 10.78 ? 405  PHE A C   1 
ATOM   3118 O  O   . PHE A 1 405  ? 24.533 56.097  -6.948  1.00 10.70 ? 405  PHE A O   1 
ATOM   3119 C  CB  . PHE A 1 405  ? 27.238 57.649  -6.534  1.00 11.54 ? 405  PHE A CB  1 
ATOM   3120 C  CG  . PHE A 1 405  ? 28.624 57.751  -5.933  1.00 12.78 ? 405  PHE A CG  1 
ATOM   3121 C  CD1 . PHE A 1 405  ? 29.689 57.034  -6.476  1.00 13.08 ? 405  PHE A CD1 1 
ATOM   3122 C  CD2 . PHE A 1 405  ? 28.868 58.593  -4.845  1.00 12.70 ? 405  PHE A CD2 1 
ATOM   3123 C  CE1 . PHE A 1 405  ? 30.973 57.153  -5.950  1.00 13.82 ? 405  PHE A CE1 1 
ATOM   3124 C  CE2 . PHE A 1 405  ? 30.159 58.725  -4.305  1.00 13.23 ? 405  PHE A CE2 1 
ATOM   3125 C  CZ  . PHE A 1 405  ? 31.213 58.007  -4.852  1.00 13.39 ? 405  PHE A CZ  1 
ATOM   3126 N  N   . THR A 1 406  ? 23.978 58.090  -6.124  1.00 10.30 ? 406  THR A N   1 
ATOM   3127 C  CA  . THR A 1 406  ? 24.245 59.292  -5.368  1.00 10.84 ? 406  THR A CA  1 
ATOM   3128 C  C   . THR A 1 406  ? 23.556 59.166  -4.015  1.00 11.57 ? 406  THR A C   1 
ATOM   3129 O  O   . THR A 1 406  ? 22.378 58.776  -3.904  1.00 9.04  ? 406  THR A O   1 
ATOM   3130 C  CB  . THR A 1 406  ? 23.725 60.558  -6.145  1.00 11.17 ? 406  THR A CB  1 
ATOM   3131 O  OG1 . THR A 1 406  ? 24.629 60.835  -7.228  1.00 12.01 ? 406  THR A OG1 1 
ATOM   3132 C  CG2 . THR A 1 406  ? 23.603 61.783  -5.239  1.00 9.90  ? 406  THR A CG2 1 
ATOM   3133 N  N   . TYR A 1 407  ? 24.342 59.473  -2.994  1.00 10.72 ? 407  TYR A N   1 
ATOM   3134 C  CA  . TYR A 1 407  ? 23.930 59.445  -1.613  1.00 10.92 ? 407  TYR A CA  1 
ATOM   3135 C  C   . TYR A 1 407  ? 22.840 60.470  -1.231  1.00 11.84 ? 407  TYR A C   1 
ATOM   3136 O  O   . TYR A 1 407  ? 22.835 61.612  -1.732  1.00 12.08 ? 407  TYR A O   1 
ATOM   3137 C  CB  . TYR A 1 407  ? 25.174 59.705  -0.748  1.00 9.76  ? 407  TYR A CB  1 
ATOM   3138 C  CG  . TYR A 1 407  ? 24.884 59.886  0.734   1.00 12.09 ? 407  TYR A CG  1 
ATOM   3139 C  CD1 . TYR A 1 407  ? 24.390 58.823  1.505   1.00 10.87 ? 407  TYR A CD1 1 
ATOM   3140 C  CD2 . TYR A 1 407  ? 25.212 61.073  1.381   1.00 11.10 ? 407  TYR A CD2 1 
ATOM   3141 C  CE1 . TYR A 1 407  ? 24.253 58.946  2.899   1.00 11.05 ? 407  TYR A CE1 1 
ATOM   3142 C  CE2 . TYR A 1 407  ? 25.088 61.200  2.757   1.00 9.97  ? 407  TYR A CE2 1 
ATOM   3143 C  CZ  . TYR A 1 407  ? 24.619 60.131  3.517   1.00 10.02 ? 407  TYR A CZ  1 
ATOM   3144 O  OH  . TYR A 1 407  ? 24.645 60.236  4.900   1.00 7.92  ? 407  TYR A OH  1 
ATOM   3145 N  N   . ALA A 1 408  ? 21.931 60.040  -0.344  1.00 11.79 ? 408  ALA A N   1 
ATOM   3146 C  CA  . ALA A 1 408  ? 20.895 60.900  0.238   1.00 12.66 ? 408  ALA A CA  1 
ATOM   3147 C  C   . ALA A 1 408  ? 20.834 60.432  1.678   1.00 12.66 ? 408  ALA A C   1 
ATOM   3148 O  O   . ALA A 1 408  ? 20.697 59.224  1.927   1.00 12.42 ? 408  ALA A O   1 
ATOM   3149 C  CB  . ALA A 1 408  ? 19.504 60.708  -0.438  1.00 12.33 ? 408  ALA A CB  1 
ATOM   3150 N  N   . ASP A 1 409  ? 20.962 61.354  2.634   1.00 12.97 ? 409  ASP A N   1 
ATOM   3151 C  CA  . ASP A 1 409  ? 20.891 60.966  4.047   1.00 13.68 ? 409  ASP A CA  1 
ATOM   3152 C  C   . ASP A 1 409  ? 19.451 61.033  4.575   1.00 14.29 ? 409  ASP A C   1 
ATOM   3153 O  O   . ASP A 1 409  ? 19.133 60.431  5.598   1.00 14.21 ? 409  ASP A O   1 
ATOM   3154 C  CB  . ASP A 1 409  ? 21.826 61.827  4.923   1.00 12.70 ? 409  ASP A CB  1 
ATOM   3155 C  CG  . ASP A 1 409  ? 21.532 63.311  4.841   1.00 14.13 ? 409  ASP A CG  1 
ATOM   3156 O  OD1 . ASP A 1 409  ? 20.899 63.735  3.857   1.00 14.26 ? 409  ASP A OD1 1 
ATOM   3157 O  OD2 . ASP A 1 409  ? 21.956 64.074  5.761   1.00 14.06 ? 409  ASP A OD2 1 
ATOM   3158 N  N   . ARG A 1 410  ? 18.578 61.756  3.875   1.00 14.02 ? 410  ARG A N   1 
ATOM   3159 C  CA  . ARG A 1 410  ? 17.159 61.854  4.285   1.00 14.43 ? 410  ARG A CA  1 
ATOM   3160 C  C   . ARG A 1 410  ? 16.324 62.458  3.166   1.00 15.32 ? 410  ARG A C   1 
ATOM   3161 O  O   . ARG A 1 410  ? 16.851 63.202  2.329   1.00 15.07 ? 410  ARG A O   1 
ATOM   3162 C  CB  . ARG A 1 410  ? 16.984 62.683  5.567   1.00 15.03 ? 410  ARG A CB  1 
ATOM   3163 C  CG  . ARG A 1 410  ? 17.466 64.128  5.521   1.00 15.93 ? 410  ARG A CG  1 
ATOM   3164 C  CD  . ARG A 1 410  ? 17.378 64.726  6.918   1.00 18.06 ? 410  ARG A CD  1 
ATOM   3165 N  NE  . ARG A 1 410  ? 18.013 66.047  7.063   1.00 20.21 ? 410  ARG A NE  1 
ATOM   3166 C  CZ  . ARG A 1 410  ? 17.454 67.216  6.726   1.00 21.75 ? 410  ARG A CZ  1 
ATOM   3167 N  NH1 . ARG A 1 410  ? 16.221 67.263  6.209   1.00 21.64 ? 410  ARG A NH1 1 
ATOM   3168 N  NH2 . ARG A 1 410  ? 18.130 68.345  6.914   1.00 18.91 ? 410  ARG A NH2 1 
ATOM   3169 N  N   . SER A 1 411  ? 15.031 62.114  3.162   1.00 15.50 ? 411  SER A N   1 
ATOM   3170 C  CA  . SER A 1 411  ? 14.051 62.560  2.165   1.00 15.27 ? 411  SER A CA  1 
ATOM   3171 C  C   . SER A 1 411  ? 14.603 62.707  0.761   1.00 13.64 ? 411  SER A C   1 
ATOM   3172 O  O   . SER A 1 411  ? 15.052 61.714  0.171   1.00 13.97 ? 411  SER A O   1 
ATOM   3173 C  CB  . SER A 1 411  ? 13.346 63.868  2.604   1.00 17.48 ? 411  SER A CB  1 
ATOM   3174 O  OG  . SER A 1 411  ? 14.263 64.899  2.891   1.00 22.47 ? 411  SER A OG  1 
ATOM   3175 N  N   . ASP A 1 412  ? 14.562 63.921  0.209   1.00 12.12 ? 412  ASP A N   1 
ATOM   3176 C  CA  . ASP A 1 412  ? 15.058 64.159  -1.159  1.00 12.26 ? 412  ASP A CA  1 
ATOM   3177 C  C   . ASP A 1 412  ? 16.400 64.916  -1.123  1.00 11.65 ? 412  ASP A C   1 
ATOM   3178 O  O   . ASP A 1 412  ? 16.814 65.479  -2.123  1.00 11.80 ? 412  ASP A O   1 
ATOM   3179 C  CB  . ASP A 1 412  ? 14.048 65.015  -1.943  1.00 12.46 ? 412  ASP A CB  1 
ATOM   3180 C  CG  . ASP A 1 412  ? 13.897 66.444  -1.347  1.00 13.80 ? 412  ASP A CG  1 
ATOM   3181 O  OD1 . ASP A 1 412  ? 14.397 66.690  -0.207  1.00 11.05 ? 412  ASP A OD1 1 
ATOM   3182 O  OD2 . ASP A 1 412  ? 13.286 67.309  -2.026  1.00 12.34 ? 412  ASP A OD2 1 
ATOM   3183 N  N   . ASN A 1 413  ? 17.059 64.936  0.032   1.00 11.09 ? 413  ASN A N   1 
ATOM   3184 C  CA  . ASN A 1 413  ? 18.333 65.654  0.178   1.00 10.97 ? 413  ASN A CA  1 
ATOM   3185 C  C   . ASN A 1 413  ? 19.495 64.814  -0.400  1.00 11.29 ? 413  ASN A C   1 
ATOM   3186 O  O   . ASN A 1 413  ? 20.208 64.121  0.343   1.00 10.32 ? 413  ASN A O   1 
ATOM   3187 C  CB  . ASN A 1 413  ? 18.600 65.948  1.654   1.00 9.94  ? 413  ASN A CB  1 
ATOM   3188 C  CG  . ASN A 1 413  ? 17.704 67.033  2.228   1.00 11.81 ? 413  ASN A CG  1 
ATOM   3189 O  OD1 . ASN A 1 413  ? 17.992 67.552  3.311   1.00 13.86 ? 413  ASN A OD1 1 
ATOM   3190 N  ND2 . ASN A 1 413  ? 16.610 67.377  1.529   1.00 9.72  ? 413  ASN A ND2 1 
ATOM   3191 N  N   . TYR A 1 414  ? 19.653 64.867  -1.718  1.00 10.30 ? 414  TYR A N   1 
ATOM   3192 C  CA  . TYR A 1 414  ? 20.703 64.130  -2.429  1.00 10.59 ? 414  TYR A CA  1 
ATOM   3193 C  C   . TYR A 1 414  ? 21.965 65.005  -2.504  1.00 11.02 ? 414  TYR A C   1 
ATOM   3194 O  O   . TYR A 1 414  ? 21.914 66.186  -2.894  1.00 11.29 ? 414  TYR A O   1 
ATOM   3195 C  CB  . TYR A 1 414  ? 20.249 63.735  -3.845  1.00 9.56  ? 414  TYR A CB  1 
ATOM   3196 C  CG  . TYR A 1 414  ? 19.261 62.568  -3.882  1.00 10.20 ? 414  TYR A CG  1 
ATOM   3197 C  CD1 . TYR A 1 414  ? 17.891 62.764  -3.644  1.00 10.78 ? 414  TYR A CD1 1 
ATOM   3198 C  CD2 . TYR A 1 414  ? 19.707 61.261  -4.130  1.00 10.59 ? 414  TYR A CD2 1 
ATOM   3199 C  CE1 . TYR A 1 414  ? 17.000 61.682  -3.649  1.00 10.84 ? 414  TYR A CE1 1 
ATOM   3200 C  CE2 . TYR A 1 414  ? 18.830 60.181  -4.143  1.00 9.16  ? 414  TYR A CE2 1 
ATOM   3201 C  CZ  . TYR A 1 414  ? 17.479 60.398  -3.898  1.00 11.08 ? 414  TYR A CZ  1 
ATOM   3202 O  OH  . TYR A 1 414  ? 16.624 59.319  -3.896  1.00 9.18  ? 414  TYR A OH  1 
ATOM   3203 N  N   . TRP A 1 415  ? 23.091 64.391  -2.152  1.00 9.47  ? 415  TRP A N   1 
ATOM   3204 C  CA  . TRP A 1 415  ? 24.371 65.090  -2.093  1.00 10.25 ? 415  TRP A CA  1 
ATOM   3205 C  C   . TRP A 1 415  ? 25.112 65.112  -3.427  1.00 10.79 ? 415  TRP A C   1 
ATOM   3206 O  O   . TRP A 1 415  ? 26.226 64.627  -3.505  1.00 11.60 ? 415  TRP A O   1 
ATOM   3207 C  CB  . TRP A 1 415  ? 25.273 64.450  -1.027  1.00 9.54  ? 415  TRP A CB  1 
ATOM   3208 C  CG  . TRP A 1 415  ? 24.731 64.516  0.404   1.00 9.13  ? 415  TRP A CG  1 
ATOM   3209 C  CD1 . TRP A 1 415  ? 23.445 64.307  0.802   1.00 8.64  ? 415  TRP A CD1 1 
ATOM   3210 C  CD2 . TRP A 1 415  ? 25.496 64.738  1.607   1.00 9.81  ? 415  TRP A CD2 1 
ATOM   3211 N  NE1 . TRP A 1 415  ? 23.355 64.374  2.170   1.00 10.85 ? 415  TRP A NE1 1 
ATOM   3212 C  CE2 . TRP A 1 415  ? 24.601 64.642  2.692   1.00 8.83  ? 415  TRP A CE2 1 
ATOM   3213 C  CE3 . TRP A 1 415  ? 26.858 65.011  1.868   1.00 8.28  ? 415  TRP A CE3 1 
ATOM   3214 C  CZ2 . TRP A 1 415  ? 25.014 64.807  4.030   1.00 9.77  ? 415  TRP A CZ2 1 
ATOM   3215 C  CZ3 . TRP A 1 415  ? 27.269 65.175  3.178   1.00 7.94  ? 415  TRP A CZ3 1 
ATOM   3216 C  CH2 . TRP A 1 415  ? 26.352 65.071  4.258   1.00 8.48  ? 415  TRP A CH2 1 
ATOM   3217 N  N   . SER A 1 416  ? 24.499 65.693  -4.455  1.00 9.66  ? 416  SER A N   1 
ATOM   3218 C  CA  . SER A 1 416  ? 25.164 65.781  -5.743  1.00 9.57  ? 416  SER A CA  1 
ATOM   3219 C  C   . SER A 1 416  ? 25.747 67.194  -6.023  1.00 9.53  ? 416  SER A C   1 
ATOM   3220 O  O   . SER A 1 416  ? 26.388 67.427  -7.067  1.00 9.40  ? 416  SER A O   1 
ATOM   3221 C  CB  . SER A 1 416  ? 24.204 65.353  -6.852  1.00 9.27  ? 416  SER A CB  1 
ATOM   3222 O  OG  . SER A 1 416  ? 22.938 65.961  -6.731  1.00 11.13 ? 416  SER A OG  1 
ATOM   3223 N  N   . GLY A 1 417  ? 25.522 68.139  -5.108  1.00 9.99  ? 417  GLY A N   1 
ATOM   3224 C  CA  . GLY A 1 417  ? 26.084 69.475  -5.294  1.00 9.87  ? 417  GLY A CA  1 
ATOM   3225 C  C   . GLY A 1 417  ? 27.616 69.490  -5.210  1.00 9.61  ? 417  GLY A C   1 
ATOM   3226 O  O   . GLY A 1 417  ? 28.303 70.182  -5.978  1.00 8.20  ? 417  GLY A O   1 
ATOM   3227 N  N   . TYR A 1 418  ? 28.166 68.701  -4.289  1.00 9.97  ? 418  TYR A N   1 
ATOM   3228 C  CA  . TYR A 1 418  ? 29.604 68.667  -4.095  1.00 9.14  ? 418  TYR A CA  1 
ATOM   3229 C  C   . TYR A 1 418  ? 30.354 68.047  -5.299  1.00 8.52  ? 418  TYR A C   1 
ATOM   3230 O  O   . TYR A 1 418  ? 31.573 68.058  -5.333  1.00 7.78  ? 418  TYR A O   1 
ATOM   3231 C  CB  . TYR A 1 418  ? 29.957 67.944  -2.786  1.00 9.85  ? 418  TYR A CB  1 
ATOM   3232 C  CG  . TYR A 1 418  ? 30.126 66.424  -2.884  1.00 10.79 ? 418  TYR A CG  1 
ATOM   3233 C  CD1 . TYR A 1 418  ? 31.396 65.848  -3.034  1.00 10.56 ? 418  TYR A CD1 1 
ATOM   3234 C  CD2 . TYR A 1 418  ? 29.032 65.566  -2.756  1.00 11.99 ? 418  TYR A CD2 1 
ATOM   3235 C  CE1 . TYR A 1 418  ? 31.559 64.450  -3.049  1.00 9.37  ? 418  TYR A CE1 1 
ATOM   3236 C  CE2 . TYR A 1 418  ? 29.188 64.146  -2.771  1.00 10.46 ? 418  TYR A CE2 1 
ATOM   3237 C  CZ  . TYR A 1 418  ? 30.454 63.614  -2.918  1.00 9.13  ? 418  TYR A CZ  1 
ATOM   3238 O  OH  . TYR A 1 418  ? 30.608 62.237  -2.904  1.00 10.55 ? 418  TYR A OH  1 
ATOM   3239 N  N   . TYR A 1 419  ? 29.626 67.507  -6.278  1.00 8.61  ? 419  TYR A N   1 
ATOM   3240 C  CA  . TYR A 1 419  ? 30.294 66.981  -7.471  1.00 7.99  ? 419  TYR A CA  1 
ATOM   3241 C  C   . TYR A 1 419  ? 30.804 68.201  -8.273  1.00 8.49  ? 419  TYR A C   1 
ATOM   3242 O  O   . TYR A 1 419  ? 31.619 68.057  -9.198  1.00 9.20  ? 419  TYR A O   1 
ATOM   3243 C  CB  . TYR A 1 419  ? 29.321 66.199  -8.373  1.00 8.75  ? 419  TYR A CB  1 
ATOM   3244 C  CG  . TYR A 1 419  ? 28.652 65.021  -7.718  1.00 10.10 ? 419  TYR A CG  1 
ATOM   3245 C  CD1 . TYR A 1 419  ? 27.465 64.510  -8.239  1.00 8.21  ? 419  TYR A CD1 1 
ATOM   3246 C  CD2 . TYR A 1 419  ? 29.243 64.362  -6.627  1.00 8.13  ? 419  TYR A CD2 1 
ATOM   3247 C  CE1 . TYR A 1 419  ? 26.889 63.370  -7.714  1.00 10.55 ? 419  TYR A CE1 1 
ATOM   3248 C  CE2 . TYR A 1 419  ? 28.678 63.224  -6.088  1.00 10.54 ? 419  TYR A CE2 1 
ATOM   3249 C  CZ  . TYR A 1 419  ? 27.504 62.725  -6.643  1.00 11.21 ? 419  TYR A CZ  1 
ATOM   3250 O  OH  . TYR A 1 419  ? 26.967 61.552  -6.187  1.00 11.21 ? 419  TYR A OH  1 
ATOM   3251 N  N   . THR A 1 420  ? 30.334 69.393  -7.911  1.00 7.11  ? 420  THR A N   1 
ATOM   3252 C  CA  . THR A 1 420  ? 30.718 70.638  -8.614  1.00 6.98  ? 420  THR A CA  1 
ATOM   3253 C  C   . THR A 1 420  ? 31.288 71.776  -7.754  1.00 8.13  ? 420  THR A C   1 
ATOM   3254 O  O   . THR A 1 420  ? 32.110 72.557  -8.247  1.00 9.20  ? 420  THR A O   1 
ATOM   3255 C  CB  . THR A 1 420  ? 29.490 71.190  -9.438  1.00 8.60  ? 420  THR A CB  1 
ATOM   3256 O  OG1 . THR A 1 420  ? 28.971 70.143  -10.276 1.00 7.90  ? 420  THR A OG1 1 
ATOM   3257 C  CG2 . THR A 1 420  ? 29.895 72.354  -10.346 1.00 7.80  ? 420  THR A CG2 1 
ATOM   3258 N  N   . SER A 1 421  ? 30.899 71.849  -6.476  1.00 8.73  ? 421  SER A N   1 
ATOM   3259 C  CA  . SER A 1 421  ? 31.335 72.915  -5.573  1.00 8.59  ? 421  SER A CA  1 
ATOM   3260 C  C   . SER A 1 421  ? 32.811 73.245  -5.646  1.00 8.74  ? 421  SER A C   1 
ATOM   3261 O  O   . SER A 1 421  ? 33.651 72.340  -5.644  1.00 8.30  ? 421  SER A O   1 
ATOM   3262 C  CB  . SER A 1 421  ? 30.944 72.587  -4.121  1.00 8.49  ? 421  SER A CB  1 
ATOM   3263 O  OG  . SER A 1 421  ? 29.545 72.399  -4.021  1.00 8.02  ? 421  SER A OG  1 
ATOM   3264 N  N   . ARG A 1 422  ? 33.119 74.547  -5.695  1.00 7.98  ? 422  ARG A N   1 
ATOM   3265 C  CA  . ARG A 1 422  ? 34.509 75.029  -5.767  1.00 7.47  ? 422  ARG A CA  1 
ATOM   3266 C  C   . ARG A 1 422  ? 35.217 74.346  -6.943  1.00 7.37  ? 422  ARG A C   1 
ATOM   3267 O  O   . ARG A 1 422  ? 36.263 73.678  -6.790  1.00 7.95  ? 422  ARG A O   1 
ATOM   3268 C  CB  . ARG A 1 422  ? 35.229 74.744  -4.444  1.00 6.69  ? 422  ARG A CB  1 
ATOM   3269 C  CG  . ARG A 1 422  ? 35.048 75.866  -3.359  1.00 8.91  ? 422  ARG A CG  1 
ATOM   3270 C  CD  . ARG A 1 422  ? 33.584 76.105  -2.907  1.00 8.33  ? 422  ARG A CD  1 
ATOM   3271 N  NE  . ARG A 1 422  ? 33.584 77.067  -1.787  1.00 11.29 ? 422  ARG A NE  1 
ATOM   3272 C  CZ  . ARG A 1 422  ? 33.540 76.726  -0.496  1.00 12.11 ? 422  ARG A CZ  1 
ATOM   3273 N  NH1 . ARG A 1 422  ? 33.444 75.457  -0.144  1.00 11.39 ? 422  ARG A NH1 1 
ATOM   3274 N  NH2 . ARG A 1 422  ? 33.724 77.642  0.455   1.00 13.23 ? 422  ARG A NH2 1 
ATOM   3275 N  N   . PRO A 1 423  ? 34.682 74.548  -8.157  1.00 7.67  ? 423  PRO A N   1 
ATOM   3276 C  CA  . PRO A 1 423  ? 35.284 73.925  -9.339  1.00 7.91  ? 423  PRO A CA  1 
ATOM   3277 C  C   . PRO A 1 423  ? 36.703 74.379  -9.677  1.00 8.18  ? 423  PRO A C   1 
ATOM   3278 O  O   . PRO A 1 423  ? 37.451 73.656  -10.370 1.00 7.96  ? 423  PRO A O   1 
ATOM   3279 C  CB  . PRO A 1 423  ? 34.248 74.220  -10.451 1.00 9.29  ? 423  PRO A CB  1 
ATOM   3280 C  CG  . PRO A 1 423  ? 33.752 75.581  -10.091 1.00 8.61  ? 423  PRO A CG  1 
ATOM   3281 C  CD  . PRO A 1 423  ? 33.610 75.494  -8.534  1.00 7.34  ? 423  PRO A CD  1 
ATOM   3282 N  N   . TYR A 1 424  ? 37.093 75.569  -9.237  1.00 7.34  ? 424  TYR A N   1 
ATOM   3283 C  CA  . TYR A 1 424  ? 38.460 76.030  -9.516  1.00 8.22  ? 424  TYR A CA  1 
ATOM   3284 C  C   . TYR A 1 424  ? 39.474 75.040  -8.947  1.00 7.78  ? 424  TYR A C   1 
ATOM   3285 O  O   . TYR A 1 424  ? 40.424 74.626  -9.635  1.00 8.38  ? 424  TYR A O   1 
ATOM   3286 C  CB  . TYR A 1 424  ? 38.708 77.385  -8.849  1.00 9.09  ? 424  TYR A CB  1 
ATOM   3287 C  CG  . TYR A 1 424  ? 40.084 77.923  -9.128  1.00 10.66 ? 424  TYR A CG  1 
ATOM   3288 C  CD1 . TYR A 1 424  ? 40.329 78.686  -10.277 1.00 9.23  ? 424  TYR A CD1 1 
ATOM   3289 C  CD2 . TYR A 1 424  ? 41.138 77.699  -8.235  1.00 10.24 ? 424  TYR A CD2 1 
ATOM   3290 C  CE1 . TYR A 1 424  ? 41.561 79.213  -10.525 1.00 12.23 ? 424  TYR A CE1 1 
ATOM   3291 C  CE2 . TYR A 1 424  ? 42.403 78.226  -8.482  1.00 11.48 ? 424  TYR A CE2 1 
ATOM   3292 C  CZ  . TYR A 1 424  ? 42.613 78.989  -9.628  1.00 12.86 ? 424  TYR A CZ  1 
ATOM   3293 O  OH  . TYR A 1 424  ? 43.857 79.555  -9.888  1.00 12.73 ? 424  TYR A OH  1 
ATOM   3294 N  N   . HIS A 1 425  ? 39.260 74.643  -7.685  1.00 7.94  ? 425  HIS A N   1 
ATOM   3295 C  CA  . HIS A 1 425  ? 40.183 73.730  -6.997  1.00 7.63  ? 425  HIS A CA  1 
ATOM   3296 C  C   . HIS A 1 425  ? 40.029 72.285  -7.480  1.00 8.12  ? 425  HIS A C   1 
ATOM   3297 O  O   . HIS A 1 425  ? 40.950 71.482  -7.350  1.00 7.95  ? 425  HIS A O   1 
ATOM   3298 C  CB  . HIS A 1 425  ? 39.978 73.845  -5.481  1.00 8.68  ? 425  HIS A CB  1 
ATOM   3299 C  CG  . HIS A 1 425  ? 40.013 75.265  -4.999  1.00 10.37 ? 425  HIS A CG  1 
ATOM   3300 N  ND1 . HIS A 1 425  ? 38.892 76.068  -4.994  1.00 12.40 ? 425  HIS A ND1 1 
ATOM   3301 C  CD2 . HIS A 1 425  ? 41.059 76.078  -4.707  1.00 8.82  ? 425  HIS A CD2 1 
ATOM   3302 C  CE1 . HIS A 1 425  ? 39.247 77.315  -4.729  1.00 11.42 ? 425  HIS A CE1 1 
ATOM   3303 N  NE2 . HIS A 1 425  ? 40.555 77.347  -4.555  1.00 12.46 ? 425  HIS A NE2 1 
ATOM   3304 N  N   . LYS A 1 426  ? 38.858 71.953  -8.010  1.00 7.55  ? 426  LYS A N   1 
ATOM   3305 C  CA  . LYS A 1 426  ? 38.642 70.621  -8.550  1.00 7.94  ? 426  LYS A CA  1 
ATOM   3306 C  C   . LYS A 1 426  ? 39.508 70.536  -9.829  1.00 8.85  ? 426  LYS A C   1 
ATOM   3307 O  O   . LYS A 1 426  ? 40.092 69.500  -10.131 1.00 9.33  ? 426  LYS A O   1 
ATOM   3308 C  CB  . LYS A 1 426  ? 37.149 70.410  -8.907  1.00 9.62  ? 426  LYS A CB  1 
ATOM   3309 C  CG  . LYS A 1 426  ? 36.226 70.109  -7.716  1.00 8.20  ? 426  LYS A CG  1 
ATOM   3310 C  CD  . LYS A 1 426  ? 34.747 69.976  -8.161  1.00 10.10 ? 426  LYS A CD  1 
ATOM   3311 C  CE  . LYS A 1 426  ? 33.902 69.156  -7.142  1.00 9.43  ? 426  LYS A CE  1 
ATOM   3312 N  NZ  . LYS A 1 426  ? 34.006 69.675  -5.726  1.00 9.57  ? 426  LYS A NZ  1 
ATOM   3313 N  N   . ARG A 1 427  ? 39.598 71.636  -10.576 1.00 7.77  ? 427  ARG A N   1 
ATOM   3314 C  CA  . ARG A 1 427  ? 40.421 71.649  -11.806 1.00 7.20  ? 427  ARG A CA  1 
ATOM   3315 C  C   . ARG A 1 427  ? 41.890 71.660  -11.363 1.00 7.05  ? 427  ARG A C   1 
ATOM   3316 O  O   . ARG A 1 427  ? 42.721 70.939  -11.897 1.00 7.30  ? 427  ARG A O   1 
ATOM   3317 C  CB  . ARG A 1 427  ? 40.052 72.892  -12.659 1.00 8.04  ? 427  ARG A CB  1 
ATOM   3318 C  CG  . ARG A 1 427  ? 40.995 73.213  -13.855 1.00 9.40  ? 427  ARG A CG  1 
ATOM   3319 C  CD  . ARG A 1 427  ? 41.299 71.995  -14.785 1.00 10.32 ? 427  ARG A CD  1 
ATOM   3320 N  NE  . ARG A 1 427  ? 42.280 72.406  -15.788 1.00 11.53 ? 427  ARG A NE  1 
ATOM   3321 C  CZ  . ARG A 1 427  ? 43.051 71.583  -16.487 1.00 12.01 ? 427  ARG A CZ  1 
ATOM   3322 N  NH1 . ARG A 1 427  ? 42.960 70.273  -16.310 1.00 11.20 ? 427  ARG A NH1 1 
ATOM   3323 N  NH2 . ARG A 1 427  ? 43.957 72.088  -17.325 1.00 11.09 ? 427  ARG A NH2 1 
ATOM   3324 N  N   . MET A 1 428  ? 42.193 72.457  -10.346 1.00 7.36  ? 428  MET A N   1 
ATOM   3325 C  CA  . MET A 1 428  ? 43.551 72.522  -9.842  1.00 8.35  ? 428  MET A CA  1 
ATOM   3326 C  C   . MET A 1 428  ? 44.066 71.135  -9.410  1.00 7.92  ? 428  MET A C   1 
ATOM   3327 O  O   . MET A 1 428  ? 45.252 70.812  -9.586  1.00 6.01  ? 428  MET A O   1 
ATOM   3328 C  CB  . MET A 1 428  ? 43.610 73.504  -8.667  1.00 10.10 ? 428  MET A CB  1 
ATOM   3329 C  CG  . MET A 1 428  ? 45.047 73.790  -8.198  1.00 12.20 ? 428  MET A CG  1 
ATOM   3330 S  SD  . MET A 1 428  ? 45.037 75.152  -6.997  1.00 11.94 ? 428  MET A SD  1 
ATOM   3331 C  CE  . MET A 1 428  ? 46.801 75.680  -7.042  1.00 10.68 ? 428  MET A CE  1 
ATOM   3332 N  N   . ASP A 1 429  ? 43.164 70.318  -8.852  1.00 8.20  ? 429  ASP A N   1 
ATOM   3333 C  CA  . ASP A 1 429  ? 43.501 68.959  -8.431  1.00 8.07  ? 429  ASP A CA  1 
ATOM   3334 C  C   . ASP A 1 429  ? 44.093 68.123  -9.563  1.00 7.61  ? 429  ASP A C   1 
ATOM   3335 O  O   . ASP A 1 429  ? 45.103 67.450  -9.381  1.00 7.29  ? 429  ASP A O   1 
ATOM   3336 C  CB  . ASP A 1 429  ? 42.275 68.235  -7.884  1.00 7.29  ? 429  ASP A CB  1 
ATOM   3337 C  CG  . ASP A 1 429  ? 42.564 66.757  -7.599  1.00 10.73 ? 429  ASP A CG  1 
ATOM   3338 O  OD1 . ASP A 1 429  ? 42.295 65.919  -8.509  1.00 8.92  ? 429  ASP A OD1 1 
ATOM   3339 O  OD2 . ASP A 1 429  ? 43.076 66.455  -6.482  1.00 7.43  ? 429  ASP A OD2 1 
ATOM   3340 N  N   . ARG A 1 430  ? 43.479 68.201  -10.745 1.00 7.34  ? 430  ARG A N   1 
ATOM   3341 C  CA  . ARG A 1 430  ? 43.939 67.444  -11.893 1.00 7.61  ? 430  ARG A CA  1 
ATOM   3342 C  C   . ARG A 1 430  ? 45.243 67.971  -12.444 1.00 8.50  ? 430  ARG A C   1 
ATOM   3343 O  O   . ARG A 1 430  ? 46.079 67.214  -12.976 1.00 8.76  ? 430  ARG A O   1 
ATOM   3344 C  CB  . ARG A 1 430  ? 42.857 67.477  -12.988 1.00 8.38  ? 430  ARG A CB  1 
ATOM   3345 C  CG  . ARG A 1 430  ? 41.554 66.813  -12.570 1.00 10.38 ? 430  ARG A CG  1 
ATOM   3346 C  CD  . ARG A 1 430  ? 41.762 65.344  -12.158 1.00 8.87  ? 430  ARG A CD  1 
ATOM   3347 N  NE  . ARG A 1 430  ? 40.515 64.610  -12.175 1.00 7.86  ? 430  ARG A NE  1 
ATOM   3348 C  CZ  . ARG A 1 430  ? 39.826 64.301  -11.083 1.00 9.42  ? 430  ARG A CZ  1 
ATOM   3349 N  NH1 . ARG A 1 430  ? 40.267 64.656  -9.871  1.00 7.32  ? 430  ARG A NH1 1 
ATOM   3350 N  NH2 . ARG A 1 430  ? 38.662 63.654  -11.201 1.00 9.32  ? 430  ARG A NH2 1 
ATOM   3351 N  N   . VAL A 1 431  ? 45.425 69.283  -12.342 1.00 7.49  ? 431  VAL A N   1 
ATOM   3352 C  CA  . VAL A 1 431  ? 46.660 69.866  -12.821 1.00 7.27  ? 431  VAL A CA  1 
ATOM   3353 C  C   . VAL A 1 431  ? 47.814 69.382  -11.921 1.00 7.12  ? 431  VAL A C   1 
ATOM   3354 O  O   . VAL A 1 431  ? 48.872 68.935  -12.417 1.00 8.50  ? 431  VAL A O   1 
ATOM   3355 C  CB  . VAL A 1 431  ? 46.573 71.407  -12.813 1.00 8.08  ? 431  VAL A CB  1 
ATOM   3356 C  CG1 . VAL A 1 431  ? 47.973 72.034  -13.096 1.00 7.80  ? 431  VAL A CG1 1 
ATOM   3357 C  CG2 . VAL A 1 431  ? 45.538 71.879  -13.888 1.00 5.97  ? 431  VAL A CG2 1 
ATOM   3358 N  N   . LEU A 1 432  ? 47.625 69.476  -10.606 1.00 6.74  ? 432  LEU A N   1 
ATOM   3359 C  CA  . LEU A 1 432  ? 48.674 69.047  -9.688  1.00 7.34  ? 432  LEU A CA  1 
ATOM   3360 C  C   . LEU A 1 432  ? 48.906 67.535  -9.802  1.00 7.08  ? 432  LEU A C   1 
ATOM   3361 O  O   . LEU A 1 432  ? 50.034 67.074  -9.710  1.00 7.45  ? 432  LEU A O   1 
ATOM   3362 C  CB  . LEU A 1 432  ? 48.339 69.414  -8.246  1.00 6.73  ? 432  LEU A CB  1 
ATOM   3363 C  CG  . LEU A 1 432  ? 49.374 69.113  -7.152  1.00 6.94  ? 432  LEU A CG  1 
ATOM   3364 C  CD1 . LEU A 1 432  ? 50.782 69.610  -7.514  1.00 4.42  ? 432  LEU A CD1 1 
ATOM   3365 C  CD2 . LEU A 1 432  ? 48.890 69.807  -5.849  1.00 5.50  ? 432  LEU A CD2 1 
ATOM   3366 N  N   . MET A 1 433  ? 47.828 66.779  -9.977  1.00 7.58  ? 433  MET A N   1 
ATOM   3367 C  CA  . MET A 1 433  ? 47.942 65.329  -10.162 1.00 7.19  ? 433  MET A CA  1 
ATOM   3368 C  C   . MET A 1 433  ? 49.012 65.028  -11.226 1.00 5.99  ? 433  MET A C   1 
ATOM   3369 O  O   . MET A 1 433  ? 49.937 64.215  -11.015 1.00 5.68  ? 433  MET A O   1 
ATOM   3370 C  CB  . MET A 1 433  ? 46.603 64.732  -10.641 1.00 6.19  ? 433  MET A CB  1 
ATOM   3371 C  CG  . MET A 1 433  ? 46.738 63.248  -10.999 1.00 8.40  ? 433  MET A CG  1 
ATOM   3372 S  SD  . MET A 1 433  ? 45.211 62.575  -11.683 1.00 9.18  ? 433  MET A SD  1 
ATOM   3373 C  CE  . MET A 1 433  ? 45.254 63.172  -13.436 1.00 8.14  ? 433  MET A CE  1 
ATOM   3374 N  N   . HIS A 1 434  ? 48.913 65.734  -12.353 1.00 6.12  ? 434  HIS A N   1 
ATOM   3375 C  CA  . HIS A 1 434  ? 49.843 65.526  -13.460 1.00 6.52  ? 434  HIS A CA  1 
ATOM   3376 C  C   . HIS A 1 434  ? 51.261 66.043  -13.176 1.00 7.84  ? 434  HIS A C   1 
ATOM   3377 O  O   . HIS A 1 434  ? 52.249 65.386  -13.527 1.00 6.31  ? 434  HIS A O   1 
ATOM   3378 C  CB  . HIS A 1 434  ? 49.293 66.172  -14.748 1.00 6.34  ? 434  HIS A CB  1 
ATOM   3379 C  CG  . HIS A 1 434  ? 50.299 66.215  -15.848 1.00 7.25  ? 434  HIS A CG  1 
ATOM   3380 N  ND1 . HIS A 1 434  ? 50.767 65.068  -16.466 1.00 8.39  ? 434  HIS A ND1 1 
ATOM   3381 C  CD2 . HIS A 1 434  ? 51.043 67.239  -16.339 1.00 6.75  ? 434  HIS A CD2 1 
ATOM   3382 C  CE1 . HIS A 1 434  ? 51.765 65.390  -17.275 1.00 6.38  ? 434  HIS A CE1 1 
ATOM   3383 N  NE2 . HIS A 1 434  ? 51.951 66.698  -17.216 1.00 7.51  ? 434  HIS A NE2 1 
ATOM   3384 N  N   . TYR A 1 435  ? 51.360 67.216  -12.534 1.00 7.69  ? 435  TYR A N   1 
ATOM   3385 C  CA  . TYR A 1 435  ? 52.669 67.792  -12.221 1.00 8.86  ? 435  TYR A CA  1 
ATOM   3386 C  C   . TYR A 1 435  ? 53.402 66.866  -11.267 1.00 7.91  ? 435  TYR A C   1 
ATOM   3387 O  O   . TYR A 1 435  ? 54.607 66.665  -11.403 1.00 7.96  ? 435  TYR A O   1 
ATOM   3388 C  CB  . TYR A 1 435  ? 52.543 69.167  -11.555 1.00 10.36 ? 435  TYR A CB  1 
ATOM   3389 C  CG  . TYR A 1 435  ? 52.381 70.320  -12.510 1.00 14.51 ? 435  TYR A CG  1 
ATOM   3390 C  CD1 . TYR A 1 435  ? 51.388 70.317  -13.497 1.00 16.27 ? 435  TYR A CD1 1 
ATOM   3391 C  CD2 . TYR A 1 435  ? 53.198 71.459  -12.393 1.00 19.79 ? 435  TYR A CD2 1 
ATOM   3392 C  CE1 . TYR A 1 435  ? 51.196 71.398  -14.344 1.00 16.79 ? 435  TYR A CE1 1 
ATOM   3393 C  CE2 . TYR A 1 435  ? 53.017 72.561  -13.244 1.00 20.56 ? 435  TYR A CE2 1 
ATOM   3394 C  CZ  . TYR A 1 435  ? 52.013 72.514  -14.214 1.00 21.83 ? 435  TYR A CZ  1 
ATOM   3395 O  OH  . TYR A 1 435  ? 51.864 73.592  -15.057 1.00 24.35 ? 435  TYR A OH  1 
ATOM   3396 N  N   . VAL A 1 436  ? 52.672 66.305  -10.303 1.00 6.49  ? 436  VAL A N   1 
ATOM   3397 C  CA  . VAL A 1 436  ? 53.315 65.395  -9.355  1.00 7.40  ? 436  VAL A CA  1 
ATOM   3398 C  C   . VAL A 1 436  ? 53.856 64.194  -10.120 1.00 7.88  ? 436  VAL A C   1 
ATOM   3399 O  O   . VAL A 1 436  ? 55.026 63.806  -9.978  1.00 8.82  ? 436  VAL A O   1 
ATOM   3400 C  CB  . VAL A 1 436  ? 52.327 64.940  -8.223  1.00 6.00  ? 436  VAL A CB  1 
ATOM   3401 C  CG1 . VAL A 1 436  ? 52.881 63.698  -7.508  1.00 7.43  ? 436  VAL A CG1 1 
ATOM   3402 C  CG2 . VAL A 1 436  ? 52.148 66.090  -7.190  1.00 7.05  ? 436  VAL A CG2 1 
ATOM   3403 N  N   . ARG A 1 437  ? 53.017 63.599  -10.961 1.00 7.41  ? 437  ARG A N   1 
ATOM   3404 C  CA  . ARG A 1 437  ? 53.499 62.447  -11.713 1.00 7.49  ? 437  ARG A CA  1 
ATOM   3405 C  C   . ARG A 1 437  ? 54.705 62.819  -12.596 1.00 7.22  ? 437  ARG A C   1 
ATOM   3406 O  O   . ARG A 1 437  ? 55.704 62.069  -12.652 1.00 8.22  ? 437  ARG A O   1 
ATOM   3407 C  CB  . ARG A 1 437  ? 52.363 61.856  -12.580 1.00 6.67  ? 437  ARG A CB  1 
ATOM   3408 C  CG  . ARG A 1 437  ? 52.870 60.988  -13.721 1.00 8.13  ? 437  ARG A CG  1 
ATOM   3409 C  CD  . ARG A 1 437  ? 51.762 60.377  -14.602 1.00 6.10  ? 437  ARG A CD  1 
ATOM   3410 N  NE  . ARG A 1 437  ? 52.306 59.734  -15.794 1.00 5.55  ? 437  ARG A NE  1 
ATOM   3411 C  CZ  . ARG A 1 437  ? 51.585 58.950  -16.593 1.00 6.76  ? 437  ARG A CZ  1 
ATOM   3412 N  NH1 . ARG A 1 437  ? 50.301 58.730  -16.307 1.00 5.07  ? 437  ARG A NH1 1 
ATOM   3413 N  NH2 . ARG A 1 437  ? 52.131 58.392  -17.677 1.00 7.67  ? 437  ARG A NH2 1 
ATOM   3414 N  N   . ALA A 1 438  ? 54.639 63.965  -13.281 1.00 6.51  ? 438  ALA A N   1 
ATOM   3415 C  CA  . ALA A 1 438  ? 55.734 64.349  -14.172 1.00 6.80  ? 438  ALA A CA  1 
ATOM   3416 C  C   . ALA A 1 438  ? 57.045 64.648  -13.406 1.00 6.87  ? 438  ALA A C   1 
ATOM   3417 O  O   . ALA A 1 438  ? 58.132 64.308  -13.873 1.00 6.53  ? 438  ALA A O   1 
ATOM   3418 C  CB  . ALA A 1 438  ? 55.316 65.574  -15.078 1.00 6.34  ? 438  ALA A CB  1 
ATOM   3419 N  N   . ALA A 1 439  ? 56.928 65.271  -12.235 1.00 5.92  ? 439  ALA A N   1 
ATOM   3420 C  CA  . ALA A 1 439  ? 58.082 65.577  -11.418 1.00 5.77  ? 439  ALA A CA  1 
ATOM   3421 C  C   . ALA A 1 439  ? 58.723 64.285  -10.887 1.00 6.83  ? 439  ALA A C   1 
ATOM   3422 O  O   . ALA A 1 439  ? 59.943 64.121  -10.944 1.00 6.50  ? 439  ALA A O   1 
ATOM   3423 C  CB  . ALA A 1 439  ? 57.674 66.510  -10.244 1.00 4.63  ? 439  ALA A CB  1 
ATOM   3424 N  N   . GLU A 1 440  ? 57.911 63.381  -10.361 1.00 5.73  ? 440  GLU A N   1 
ATOM   3425 C  CA  . GLU A 1 440  ? 58.457 62.133  -9.855  1.00 6.93  ? 440  GLU A CA  1 
ATOM   3426 C  C   . GLU A 1 440  ? 59.112 61.312  -10.973 1.00 6.71  ? 440  GLU A C   1 
ATOM   3427 O  O   . GLU A 1 440  ? 60.153 60.682  -10.784 1.00 8.71  ? 440  GLU A O   1 
ATOM   3428 C  CB  . GLU A 1 440  ? 57.343 61.318  -9.168  1.00 7.38  ? 440  GLU A CB  1 
ATOM   3429 C  CG  . GLU A 1 440  ? 56.885 61.936  -7.866  1.00 7.06  ? 440  GLU A CG  1 
ATOM   3430 C  CD  . GLU A 1 440  ? 56.153 60.928  -6.978  1.00 10.56 ? 440  GLU A CD  1 
ATOM   3431 O  OE1 . GLU A 1 440  ? 55.030 60.531  -7.324  1.00 9.64  ? 440  GLU A OE1 1 
ATOM   3432 O  OE2 . GLU A 1 440  ? 56.727 60.504  -5.948  1.00 13.11 ? 440  GLU A OE2 1 
ATOM   3433 N  N   . MET A 1 441  ? 58.516 61.334  -12.153 1.00 8.56  ? 441  MET A N   1 
ATOM   3434 C  CA  . MET A 1 441  ? 59.061 60.575  -13.278 1.00 7.01  ? 441  MET A CA  1 
ATOM   3435 C  C   . MET A 1 441  ? 60.369 61.156  -13.832 1.00 7.19  ? 441  MET A C   1 
ATOM   3436 O  O   . MET A 1 441  ? 61.375 60.439  -13.974 1.00 6.92  ? 441  MET A O   1 
ATOM   3437 C  CB  . MET A 1 441  ? 58.024 60.469  -14.404 1.00 6.65  ? 441  MET A CB  1 
ATOM   3438 C  CG  . MET A 1 441  ? 58.524 59.678  -15.616 1.00 6.95  ? 441  MET A CG  1 
ATOM   3439 S  SD  . MET A 1 441  ? 57.241 59.393  -16.875 1.00 8.28  ? 441  MET A SD  1 
ATOM   3440 C  CE  . MET A 1 441  ? 56.167 58.197  -16.045 1.00 5.96  ? 441  MET A CE  1 
ATOM   3441 N  N   . LEU A 1 442  ? 60.369 62.454  -14.117 1.00 6.97  ? 442  LEU A N   1 
ATOM   3442 C  CA  . LEU A 1 442  ? 61.554 63.123  -14.663 1.00 7.71  ? 442  LEU A CA  1 
ATOM   3443 C  C   . LEU A 1 442  ? 62.768 63.020  -13.751 1.00 9.73  ? 442  LEU A C   1 
ATOM   3444 O  O   . LEU A 1 442  ? 63.885 62.811  -14.238 1.00 9.64  ? 442  LEU A O   1 
ATOM   3445 C  CB  . LEU A 1 442  ? 61.246 64.606  -14.967 1.00 8.31  ? 442  LEU A CB  1 
ATOM   3446 C  CG  . LEU A 1 442  ? 60.577 64.839  -16.342 1.00 9.56  ? 442  LEU A CG  1 
ATOM   3447 C  CD1 . LEU A 1 442  ? 60.024 66.269  -16.419 1.00 10.48 ? 442  LEU A CD1 1 
ATOM   3448 C  CD2 . LEU A 1 442  ? 61.596 64.605  -17.478 1.00 8.59  ? 442  LEU A CD2 1 
ATOM   3449 N  N   . SER A 1 443  ? 62.561 63.121  -12.436 1.00 8.29  ? 443  SER A N   1 
ATOM   3450 C  CA  . SER A 1 443  ? 63.698 63.052  -11.515 1.00 9.29  ? 443  SER A CA  1 
ATOM   3451 C  C   . SER A 1 443  ? 64.080 61.609  -11.122 1.00 9.74  ? 443  SER A C   1 
ATOM   3452 O  O   . SER A 1 443  ? 65.168 61.367  -10.548 1.00 9.90  ? 443  SER A O   1 
ATOM   3453 C  CB  . SER A 1 443  ? 63.406 63.883  -10.267 1.00 9.41  ? 443  SER A CB  1 
ATOM   3454 O  OG  . SER A 1 443  ? 62.319 63.342  -9.527  1.00 9.50  ? 443  SER A OG  1 
ATOM   3455 N  N   . ALA A 1 444  ? 63.204 60.655  -11.449 1.00 9.16  ? 444  ALA A N   1 
ATOM   3456 C  CA  . ALA A 1 444  ? 63.457 59.247  -11.118 1.00 9.24  ? 444  ALA A CA  1 
ATOM   3457 C  C   . ALA A 1 444  ? 64.609 58.699  -11.933 1.00 10.59 ? 444  ALA A C   1 
ATOM   3458 O  O   . ALA A 1 444  ? 65.296 57.768  -11.494 1.00 11.12 ? 444  ALA A O   1 
ATOM   3459 C  CB  . ALA A 1 444  ? 62.240 58.406  -11.395 1.00 8.56  ? 444  ALA A CB  1 
ATOM   3460 N  N   . TRP A 1 445  ? 64.831 59.263  -13.116 1.00 11.48 ? 445  TRP A N   1 
ATOM   3461 C  CA  . TRP A 1 445  ? 65.881 58.755  -13.980 1.00 11.90 ? 445  TRP A CA  1 
ATOM   3462 C  C   . TRP A 1 445  ? 67.270 58.790  -13.362 1.00 13.37 ? 445  TRP A C   1 
ATOM   3463 O  O   . TRP A 1 445  ? 68.102 57.949  -13.675 1.00 12.41 ? 445  TRP A O   1 
ATOM   3464 C  CB  . TRP A 1 445  ? 65.885 59.507  -15.315 1.00 11.55 ? 445  TRP A CB  1 
ATOM   3465 C  CG  . TRP A 1 445  ? 64.622 59.303  -16.068 1.00 9.96  ? 445  TRP A CG  1 
ATOM   3466 C  CD1 . TRP A 1 445  ? 63.623 60.212  -16.242 1.00 10.60 ? 445  TRP A CD1 1 
ATOM   3467 C  CD2 . TRP A 1 445  ? 64.194 58.095  -16.729 1.00 9.51  ? 445  TRP A CD2 1 
ATOM   3468 N  NE1 . TRP A 1 445  ? 62.597 59.652  -16.964 1.00 9.36  ? 445  TRP A NE1 1 
ATOM   3469 C  CE2 . TRP A 1 445  ? 62.921 58.352  -17.276 1.00 10.14 ? 445  TRP A CE2 1 
ATOM   3470 C  CE3 . TRP A 1 445  ? 64.774 56.817  -16.914 1.00 10.16 ? 445  TRP A CE3 1 
ATOM   3471 C  CZ2 . TRP A 1 445  ? 62.202 57.386  -17.998 1.00 10.22 ? 445  TRP A CZ2 1 
ATOM   3472 C  CZ3 . TRP A 1 445  ? 64.061 55.855  -17.633 1.00 10.31 ? 445  TRP A CZ3 1 
ATOM   3473 C  CH2 . TRP A 1 445  ? 62.781 56.148  -18.167 1.00 9.96  ? 445  TRP A CH2 1 
ATOM   3474 N  N   . HIS A 1 446  ? 67.511 59.746  -12.479 1.00 13.94 ? 446  HIS A N   1 
ATOM   3475 C  CA  . HIS A 1 446  ? 68.815 59.878  -11.853 1.00 15.33 ? 446  HIS A CA  1 
ATOM   3476 C  C   . HIS A 1 446  ? 68.668 59.766  -10.359 1.00 16.84 ? 446  HIS A C   1 
ATOM   3477 O  O   . HIS A 1 446  ? 67.577 59.935  -9.817  1.00 16.52 ? 446  HIS A O   1 
ATOM   3478 C  CB  . HIS A 1 446  ? 69.403 61.272  -12.088 1.00 16.72 ? 446  HIS A CB  1 
ATOM   3479 C  CG  . HIS A 1 446  ? 69.870 61.525  -13.485 1.00 18.95 ? 446  HIS A CG  1 
ATOM   3480 N  ND1 . HIS A 1 446  ? 69.146 62.272  -14.383 1.00 18.80 ? 446  HIS A ND1 1 
ATOM   3481 C  CD2 . HIS A 1 446  ? 71.015 61.173  -14.122 1.00 20.23 ? 446  HIS A CD2 1 
ATOM   3482 C  CE1 . HIS A 1 446  ? 69.821 62.375  -15.517 1.00 20.62 ? 446  HIS A CE1 1 
ATOM   3483 N  NE2 . HIS A 1 446  ? 70.958 61.717  -15.383 1.00 20.78 ? 446  HIS A NE2 1 
ATOM   3484 N  N   . SER A 1 447  ? 69.808 59.550  -9.712  1.00 16.67 ? 447  SER A N   1 
ATOM   3485 C  CA  . SER A 1 447  ? 69.921 59.527  -8.262  1.00 16.20 ? 447  SER A CA  1 
ATOM   3486 C  C   . SER A 1 447  ? 70.422 60.963  -7.976  1.00 16.53 ? 447  SER A C   1 
ATOM   3487 O  O   . SER A 1 447  ? 71.301 61.464  -8.695  1.00 16.48 ? 447  SER A O   1 
ATOM   3488 C  CB  . SER A 1 447  ? 70.962 58.488  -7.849  1.00 17.19 ? 447  SER A CB  1 
ATOM   3489 O  OG  . SER A 1 447  ? 70.784 58.135  -6.506  1.00 18.70 ? 447  SER A OG  1 
ATOM   3490 N  N   . TRP A 1 448  ? 69.877 61.634  -6.961  1.00 15.59 ? 448  TRP A N   1 
ATOM   3491 C  CA  . TRP A 1 448  ? 70.273 63.007  -6.711  1.00 16.59 ? 448  TRP A CA  1 
ATOM   3492 C  C   . TRP A 1 448  ? 70.953 63.278  -5.391  1.00 17.77 ? 448  TRP A C   1 
ATOM   3493 O  O   . TRP A 1 448  ? 70.591 62.715  -4.364  1.00 17.13 ? 448  TRP A O   1 
ATOM   3494 C  CB  . TRP A 1 448  ? 69.063 63.961  -6.800  1.00 14.73 ? 448  TRP A CB  1 
ATOM   3495 C  CG  . TRP A 1 448  ? 68.384 63.974  -8.136  1.00 13.09 ? 448  TRP A CG  1 
ATOM   3496 C  CD1 . TRP A 1 448  ? 67.563 63.029  -8.643  1.00 12.84 ? 448  TRP A CD1 1 
ATOM   3497 C  CD2 . TRP A 1 448  ? 68.524 64.977  -9.146  1.00 13.59 ? 448  TRP A CD2 1 
ATOM   3498 N  NE1 . TRP A 1 448  ? 67.174 63.372  -9.915  1.00 12.92 ? 448  TRP A NE1 1 
ATOM   3499 C  CE2 . TRP A 1 448  ? 67.745 64.571  -10.245 1.00 12.89 ? 448  TRP A CE2 1 
ATOM   3500 C  CE3 . TRP A 1 448  ? 69.239 66.185  -9.225  1.00 13.85 ? 448  TRP A CE3 1 
ATOM   3501 C  CZ2 . TRP A 1 448  ? 67.648 65.326  -11.415 1.00 13.16 ? 448  TRP A CZ2 1 
ATOM   3502 C  CZ3 . TRP A 1 448  ? 69.146 66.936  -10.387 1.00 13.35 ? 448  TRP A CZ3 1 
ATOM   3503 C  CH2 . TRP A 1 448  ? 68.351 66.501  -11.467 1.00 13.66 ? 448  TRP A CH2 1 
ATOM   3504 N  N   . ASP A 1 449  ? 71.949 64.158  -5.442  1.00 19.55 ? 449  ASP A N   1 
ATOM   3505 C  CA  . ASP A 1 449  ? 72.651 64.559  -4.235  1.00 20.85 ? 449  ASP A CA  1 
ATOM   3506 C  C   . ASP A 1 449  ? 71.618 65.223  -3.313  1.00 20.34 ? 449  ASP A C   1 
ATOM   3507 O  O   . ASP A 1 449  ? 70.765 65.975  -3.774  1.00 19.19 ? 449  ASP A O   1 
ATOM   3508 C  CB  . ASP A 1 449  ? 73.742 65.574  -4.575  1.00 23.90 ? 449  ASP A CB  1 
ATOM   3509 C  CG  . ASP A 1 449  ? 74.581 65.932  -3.373  1.00 27.44 ? 449  ASP A CG  1 
ATOM   3510 O  OD1 . ASP A 1 449  ? 74.357 66.993  -2.744  1.00 27.96 ? 449  ASP A OD1 1 
ATOM   3511 O  OD2 . ASP A 1 449  ? 75.463 65.108  -3.038  1.00 31.86 ? 449  ASP A OD2 1 
ATOM   3512 N  N   . GLY A 1 450  ? 71.718 64.967  -2.012  1.00 19.85 ? 450  GLY A N   1 
ATOM   3513 C  CA  . GLY A 1 450  ? 70.781 65.554  -1.070  1.00 20.54 ? 450  GLY A CA  1 
ATOM   3514 C  C   . GLY A 1 450  ? 70.697 67.056  -1.165  1.00 20.73 ? 450  GLY A C   1 
ATOM   3515 O  O   . GLY A 1 450  ? 69.672 67.651  -0.833  1.00 21.49 ? 450  GLY A O   1 
ATOM   3516 N  N   . MET A 1 451  ? 71.768 67.685  -1.618  1.00 20.46 ? 451  MET A N   1 
ATOM   3517 C  CA  . MET A 1 451  ? 71.773 69.133  -1.736  1.00 21.71 ? 451  MET A CA  1 
ATOM   3518 C  C   . MET A 1 451  ? 70.812 69.610  -2.820  1.00 19.89 ? 451  MET A C   1 
ATOM   3519 O  O   . MET A 1 451  ? 70.499 70.796  -2.898  1.00 18.77 ? 451  MET A O   1 
ATOM   3520 C  CB  . MET A 1 451  ? 73.186 69.643  -2.066  1.00 26.05 ? 451  MET A CB  1 
ATOM   3521 C  CG  . MET A 1 451  ? 74.207 69.508  -0.933  1.00 32.08 ? 451  MET A CG  1 
ATOM   3522 S  SD  . MET A 1 451  ? 73.794 70.544  0.551   1.00 41.73 ? 451  MET A SD  1 
ATOM   3523 C  CE  . MET A 1 451  ? 73.073 69.243  1.736   1.00 37.70 ? 451  MET A CE  1 
ATOM   3524 N  N   . ALA A 1 452  ? 70.382 68.700  -3.689  1.00 18.21 ? 452  ALA A N   1 
ATOM   3525 C  CA  . ALA A 1 452  ? 69.460 69.085  -4.757  1.00 17.72 ? 452  ALA A CA  1 
ATOM   3526 C  C   . ALA A 1 452  ? 68.054 69.320  -4.205  1.00 16.62 ? 452  ALA A C   1 
ATOM   3527 O  O   . ALA A 1 452  ? 67.216 69.947  -4.858  1.00 16.49 ? 452  ALA A O   1 
ATOM   3528 C  CB  . ALA A 1 452  ? 69.432 68.002  -5.859  1.00 16.87 ? 452  ALA A CB  1 
ATOM   3529 N  N   . ARG A 1 453  ? 67.807 68.803  -3.005  1.00 15.49 ? 453  ARG A N   1 
ATOM   3530 C  CA  . ARG A 1 453  ? 66.503 68.947  -2.345  1.00 14.89 ? 453  ARG A CA  1 
ATOM   3531 C  C   . ARG A 1 453  ? 65.364 68.402  -3.208  1.00 13.87 ? 453  ARG A C   1 
ATOM   3532 O  O   . ARG A 1 453  ? 64.263 68.947  -3.216  1.00 14.71 ? 453  ARG A O   1 
ATOM   3533 C  CB  . ARG A 1 453  ? 66.257 70.421  -2.017  1.00 15.25 ? 453  ARG A CB  1 
ATOM   3534 C  CG  . ARG A 1 453  ? 67.262 71.015  -1.021  1.00 16.66 ? 453  ARG A CG  1 
ATOM   3535 C  CD  . ARG A 1 453  ? 67.036 72.518  -0.856  1.00 18.75 ? 453  ARG A CD  1 
ATOM   3536 N  NE  . ARG A 1 453  ? 65.860 72.805  -0.030  1.00 21.45 ? 453  ARG A NE  1 
ATOM   3537 C  CZ  . ARG A 1 453  ? 65.369 74.025  0.193   1.00 23.96 ? 453  ARG A CZ  1 
ATOM   3538 N  NH1 . ARG A 1 453  ? 65.955 75.108  -0.352  1.00 23.55 ? 453  ARG A NH1 1 
ATOM   3539 N  NH2 . ARG A 1 453  ? 64.287 74.165  0.950   1.00 22.84 ? 453  ARG A NH2 1 
ATOM   3540 N  N   . ILE A 1 454  ? 65.640 67.325  -3.934  1.00 12.51 ? 454  ILE A N   1 
ATOM   3541 C  CA  . ILE A 1 454  ? 64.647 66.722  -4.807  1.00 12.30 ? 454  ILE A CA  1 
ATOM   3542 C  C   . ILE A 1 454  ? 63.625 65.951  -3.982  1.00 13.02 ? 454  ILE A C   1 
ATOM   3543 O  O   . ILE A 1 454  ? 62.425 66.136  -4.158  1.00 12.70 ? 454  ILE A O   1 
ATOM   3544 C  CB  . ILE A 1 454  ? 65.291 65.764  -5.799  1.00 12.22 ? 454  ILE A CB  1 
ATOM   3545 C  CG1 . ILE A 1 454  ? 66.294 66.535  -6.702  1.00 11.13 ? 454  ILE A CG1 1 
ATOM   3546 C  CG2 . ILE A 1 454  ? 64.189 65.046  -6.614  1.00 11.05 ? 454  ILE A CG2 1 
ATOM   3547 C  CD1 . ILE A 1 454  ? 65.675 67.635  -7.612  1.00 11.29 ? 454  ILE A CD1 1 
ATOM   3548 N  N   . GLU A 1 455  ? 64.116 65.096  -3.088  1.00 11.58 ? 455  GLU A N   1 
ATOM   3549 C  CA  . GLU A 1 455  ? 63.257 64.299  -2.229  1.00 12.42 ? 455  GLU A CA  1 
ATOM   3550 C  C   . GLU A 1 455  ? 62.379 65.198  -1.384  1.00 12.26 ? 455  GLU A C   1 
ATOM   3551 O  O   . GLU A 1 455  ? 61.188 64.895  -1.155  1.00 10.13 ? 455  GLU A O   1 
ATOM   3552 C  CB  . GLU A 1 455  ? 64.076 63.395  -1.281  1.00 12.38 ? 455  GLU A CB  1 
ATOM   3553 C  CG  . GLU A 1 455  ? 64.696 62.129  -1.928  1.00 13.82 ? 455  GLU A CG  1 
ATOM   3554 C  CD  . GLU A 1 455  ? 66.010 62.386  -2.688  1.00 16.17 ? 455  GLU A CD  1 
ATOM   3555 O  OE1 . GLU A 1 455  ? 66.449 63.562  -2.768  1.00 16.76 ? 455  GLU A OE1 1 
ATOM   3556 O  OE2 . GLU A 1 455  ? 66.581 61.403  -3.223  1.00 13.21 ? 455  GLU A OE2 1 
ATOM   3557 N  N   . GLU A 1 456  ? 62.974 66.292  -0.908  1.00 11.70 ? 456  GLU A N   1 
ATOM   3558 C  CA  . GLU A 1 456  ? 62.267 67.246  -0.063  1.00 12.28 ? 456  GLU A CA  1 
ATOM   3559 C  C   . GLU A 1 456  ? 61.112 67.903  -0.816  1.00 12.17 ? 456  GLU A C   1 
ATOM   3560 O  O   . GLU A 1 456  ? 59.977 67.953  -0.309  1.00 11.37 ? 456  GLU A O   1 
ATOM   3561 C  CB  . GLU A 1 456  ? 63.238 68.328  0.447   1.00 15.31 ? 456  GLU A CB  1 
ATOM   3562 C  CG  . GLU A 1 456  ? 62.612 69.384  1.358   1.00 19.39 ? 456  GLU A CG  1 
ATOM   3563 C  CD  . GLU A 1 456  ? 63.498 70.624  1.538   1.00 22.04 ? 456  GLU A CD  1 
ATOM   3564 O  OE1 . GLU A 1 456  ? 64.735 70.516  1.398   1.00 24.38 ? 456  GLU A OE1 1 
ATOM   3565 O  OE2 . GLU A 1 456  ? 62.958 71.709  1.824   1.00 24.32 ? 456  GLU A OE2 1 
ATOM   3566 N  N   . ARG A 1 457  ? 61.389 68.416  -2.017  1.00 10.47 ? 457  ARG A N   1 
ATOM   3567 C  CA  . ARG A 1 457  ? 60.335 69.084  -2.773  1.00 10.18 ? 457  ARG A CA  1 
ATOM   3568 C  C   . ARG A 1 457  ? 59.247 68.103  -3.200  1.00 9.37  ? 457  ARG A C   1 
ATOM   3569 O  O   . ARG A 1 457  ? 58.078 68.450  -3.163  1.00 8.40  ? 457  ARG A O   1 
ATOM   3570 C  CB  . ARG A 1 457  ? 60.906 69.808  -4.005  1.00 11.84 ? 457  ARG A CB  1 
ATOM   3571 C  CG  . ARG A 1 457  ? 61.186 71.327  -3.787  1.00 14.18 ? 457  ARG A CG  1 
ATOM   3572 C  CD  . ARG A 1 457  ? 62.133 71.587  -2.610  1.00 18.03 ? 457  ARG A CD  1 
ATOM   3573 N  NE  . ARG A 1 457  ? 62.412 73.014  -2.375  1.00 19.18 ? 457  ARG A NE  1 
ATOM   3574 C  CZ  . ARG A 1 457  ? 63.325 73.745  -3.034  1.00 22.43 ? 457  ARG A CZ  1 
ATOM   3575 N  NH1 . ARG A 1 457  ? 64.091 73.212  -4.002  1.00 20.60 ? 457  ARG A NH1 1 
ATOM   3576 N  NH2 . ARG A 1 457  ? 63.489 75.031  -2.703  1.00 21.79 ? 457  ARG A NH2 1 
ATOM   3577 N  N   . LEU A 1 458  ? 59.635 66.885  -3.577  1.00 7.71  ? 458  LEU A N   1 
ATOM   3578 C  CA  . LEU A 1 458  ? 58.642 65.891  -3.997  1.00 8.29  ? 458  LEU A CA  1 
ATOM   3579 C  C   . LEU A 1 458  ? 57.749 65.458  -2.825  1.00 9.04  ? 458  LEU A C   1 
ATOM   3580 O  O   . LEU A 1 458  ? 56.533 65.276  -2.984  1.00 9.10  ? 458  LEU A O   1 
ATOM   3581 C  CB  . LEU A 1 458  ? 59.322 64.658  -4.593  1.00 7.12  ? 458  LEU A CB  1 
ATOM   3582 C  CG  . LEU A 1 458  ? 59.983 64.932  -5.958  1.00 7.60  ? 458  LEU A CG  1 
ATOM   3583 C  CD1 . LEU A 1 458  ? 60.712 63.660  -6.478  1.00 6.93  ? 458  LEU A CD1 1 
ATOM   3584 C  CD2 . LEU A 1 458  ? 58.877 65.367  -6.962  1.00 5.60  ? 458  LEU A CD2 1 
ATOM   3585 N  N   . GLU A 1 459  ? 58.339 65.273  -1.655  1.00 8.49  ? 459  GLU A N   1 
ATOM   3586 C  CA  . GLU A 1 459  ? 57.546 64.877  -0.509  1.00 9.28  ? 459  GLU A CA  1 
ATOM   3587 C  C   . GLU A 1 459  ? 56.513 65.963  -0.179  1.00 9.82  ? 459  GLU A C   1 
ATOM   3588 O  O   . GLU A 1 459  ? 55.344 65.674  0.115   1.00 8.48  ? 459  GLU A O   1 
ATOM   3589 C  CB  . GLU A 1 459  ? 58.435 64.645  0.711   1.00 11.44 ? 459  GLU A CB  1 
ATOM   3590 C  CG  . GLU A 1 459  ? 57.633 64.277  1.973   1.00 15.47 ? 459  GLU A CG  1 
ATOM   3591 C  CD  . GLU A 1 459  ? 58.505 63.648  3.061   1.00 17.30 ? 459  GLU A CD  1 
ATOM   3592 O  OE1 . GLU A 1 459  ? 59.167 64.410  3.764   1.00 17.29 ? 459  GLU A OE1 1 
ATOM   3593 O  OE2 . GLU A 1 459  ? 58.536 62.395  3.193   1.00 19.39 ? 459  GLU A OE2 1 
ATOM   3594 N  N   . GLN A 1 460  ? 56.934 67.226  -0.216  1.00 10.31 ? 460  GLN A N   1 
ATOM   3595 C  CA  . GLN A 1 460  ? 55.984 68.297  0.076   1.00 11.29 ? 460  GLN A CA  1 
ATOM   3596 C  C   . GLN A 1 460  ? 54.858 68.297  -0.984  1.00 11.19 ? 460  GLN A C   1 
ATOM   3597 O  O   . GLN A 1 460  ? 53.685 68.454  -0.651  1.00 9.22  ? 460  GLN A O   1 
ATOM   3598 C  CB  . GLN A 1 460  ? 56.703 69.638  0.061   1.00 14.90 ? 460  GLN A CB  1 
ATOM   3599 C  CG  . GLN A 1 460  ? 55.781 70.843  0.015   1.00 17.77 ? 460  GLN A CG  1 
ATOM   3600 C  CD  . GLN A 1 460  ? 56.553 72.106  -0.256  1.00 19.35 ? 460  GLN A CD  1 
ATOM   3601 O  OE1 . GLN A 1 460  ? 57.535 72.092  -0.994  1.00 23.62 ? 460  GLN A OE1 1 
ATOM   3602 N  NE2 . GLN A 1 460  ? 56.119 73.200  0.325   1.00 21.45 ? 460  GLN A NE2 1 
ATOM   3603 N  N   . ALA A 1 461  ? 55.207 68.103  -2.261  1.00 10.22 ? 461  ALA A N   1 
ATOM   3604 C  CA  . ALA A 1 461  ? 54.147 68.135  -3.272  1.00 9.08  ? 461  ALA A CA  1 
ATOM   3605 C  C   . ALA A 1 461  ? 53.176 66.962  -3.113  1.00 8.94  ? 461  ALA A C   1 
ATOM   3606 O  O   . ALA A 1 461  ? 51.964 67.157  -3.234  1.00 7.97  ? 461  ALA A O   1 
ATOM   3607 C  CB  . ALA A 1 461  ? 54.732 68.139  -4.683  1.00 8.97  ? 461  ALA A CB  1 
ATOM   3608 N  N   . ARG A 1 462  ? 53.703 65.754  -2.850  1.00 7.45  ? 462  ARG A N   1 
ATOM   3609 C  CA  . ARG A 1 462  ? 52.827 64.583  -2.676  1.00 9.05  ? 462  ARG A CA  1 
ATOM   3610 C  C   . ARG A 1 462  ? 51.880 64.793  -1.484  1.00 10.70 ? 462  ARG A C   1 
ATOM   3611 O  O   . ARG A 1 462  ? 50.698 64.371  -1.508  1.00 9.26  ? 462  ARG A O   1 
ATOM   3612 C  CB  . ARG A 1 462  ? 53.645 63.282  -2.415  1.00 8.43  ? 462  ARG A CB  1 
ATOM   3613 C  CG  . ARG A 1 462  ? 54.420 62.714  -3.632  1.00 6.37  ? 462  ARG A CG  1 
ATOM   3614 C  CD  . ARG A 1 462  ? 54.846 61.256  -3.364  1.00 6.11  ? 462  ARG A CD  1 
ATOM   3615 N  NE  . ARG A 1 462  ? 55.758 61.211  -2.227  1.00 8.68  ? 462  ARG A NE  1 
ATOM   3616 C  CZ  . ARG A 1 462  ? 57.076 61.413  -2.309  1.00 10.44 ? 462  ARG A CZ  1 
ATOM   3617 N  NH1 . ARG A 1 462  ? 57.669 61.659  -3.489  1.00 7.97  ? 462  ARG A NH1 1 
ATOM   3618 N  NH2 . ARG A 1 462  ? 57.811 61.407  -1.199  1.00 9.35  ? 462  ARG A NH2 1 
ATOM   3619 N  N   . ARG A 1 463  ? 52.421 65.384  -0.409  1.00 9.80  ? 463  ARG A N   1 
ATOM   3620 C  CA  . ARG A 1 463  ? 51.619 65.625  0.791   1.00 10.01 ? 463  ARG A CA  1 
ATOM   3621 C  C   . ARG A 1 463  ? 50.520 66.685  0.661   1.00 9.41  ? 463  ARG A C   1 
ATOM   3622 O  O   . ARG A 1 463  ? 49.438 66.495  1.219   1.00 8.19  ? 463  ARG A O   1 
ATOM   3623 C  CB  . ARG A 1 463  ? 52.522 65.924  2.006   1.00 10.31 ? 463  ARG A CB  1 
ATOM   3624 C  CG  . ARG A 1 463  ? 53.228 64.630  2.456   1.00 11.65 ? 463  ARG A CG  1 
ATOM   3625 C  CD  . ARG A 1 463  ? 54.301 64.793  3.531   1.00 11.26 ? 463  ARG A CD  1 
ATOM   3626 N  NE  . ARG A 1 463  ? 54.747 63.455  3.942   1.00 13.42 ? 463  ARG A NE  1 
ATOM   3627 C  CZ  . ARG A 1 463  ? 55.491 63.207  5.021   1.00 15.52 ? 463  ARG A CZ  1 
ATOM   3628 N  NH1 . ARG A 1 463  ? 55.878 64.221  5.786   1.00 13.88 ? 463  ARG A NH1 1 
ATOM   3629 N  NH2 . ARG A 1 463  ? 55.809 61.947  5.351   1.00 15.09 ? 463  ARG A NH2 1 
ATOM   3630 N  N   . GLU A 1 464  ? 50.788 67.785  -0.043  1.00 8.74  ? 464  GLU A N   1 
ATOM   3631 C  CA  . GLU A 1 464  ? 49.754 68.796  -0.209  1.00 9.83  ? 464  GLU A CA  1 
ATOM   3632 C  C   . GLU A 1 464  ? 48.678 68.249  -1.154  1.00 8.89  ? 464  GLU A C   1 
ATOM   3633 O  O   . GLU A 1 464  ? 47.513 68.478  -0.915  1.00 9.95  ? 464  GLU A O   1 
ATOM   3634 C  CB  . GLU A 1 464  ? 50.320 70.109  -0.758  1.00 10.50 ? 464  GLU A CB  1 
ATOM   3635 C  CG  . GLU A 1 464  ? 51.513 70.657  0.032   1.00 13.35 ? 464  GLU A CG  1 
ATOM   3636 C  CD  . GLU A 1 464  ? 51.173 71.054  1.463   1.00 14.18 ? 464  GLU A CD  1 
ATOM   3637 O  OE1 . GLU A 1 464  ? 50.124 70.657  2.001   1.00 14.03 ? 464  GLU A OE1 1 
ATOM   3638 O  OE2 . GLU A 1 464  ? 51.987 71.761  2.070   1.00 16.85 ? 464  GLU A OE2 1 
ATOM   3639 N  N   . LEU A 1 465  ? 49.054 67.547  -2.225  1.00 7.74  ? 465  LEU A N   1 
ATOM   3640 C  CA  . LEU A 1 465  ? 48.031 66.955  -3.113  1.00 7.25  ? 465  LEU A CA  1 
ATOM   3641 C  C   . LEU A 1 465  ? 47.250 65.868  -2.331  1.00 7.07  ? 465  LEU A C   1 
ATOM   3642 O  O   . LEU A 1 465  ? 46.031 65.762  -2.448  1.00 7.95  ? 465  LEU A O   1 
ATOM   3643 C  CB  . LEU A 1 465  ? 48.674 66.314  -4.354  1.00 6.99  ? 465  LEU A CB  1 
ATOM   3644 C  CG  . LEU A 1 465  ? 47.695 65.612  -5.317  1.00 6.14  ? 465  LEU A CG  1 
ATOM   3645 C  CD1 . LEU A 1 465  ? 46.597 66.593  -5.754  1.00 5.51  ? 465  LEU A CD1 1 
ATOM   3646 C  CD2 . LEU A 1 465  ? 48.468 65.080  -6.564  1.00 5.04  ? 465  LEU A CD2 1 
ATOM   3647 N  N   . SER A 1 466  ? 47.955 65.063  -1.526  1.00 6.63  ? 466  SER A N   1 
ATOM   3648 C  CA  . SER A 1 466  ? 47.300 64.016  -0.740  1.00 5.57  ? 466  SER A CA  1 
ATOM   3649 C  C   . SER A 1 466  ? 46.309 64.643  0.236   1.00 7.00  ? 466  SER A C   1 
ATOM   3650 O  O   . SER A 1 466  ? 45.164 64.167  0.396   1.00 5.43  ? 466  SER A O   1 
ATOM   3651 C  CB  . SER A 1 466  ? 48.328 63.212  0.039   1.00 4.71  ? 466  SER A CB  1 
ATOM   3652 O  OG  . SER A 1 466  ? 49.077 62.393  -0.844  1.00 6.20  ? 466  SER A OG  1 
ATOM   3653 N  N   . LEU A 1 467  ? 46.737 65.726  0.883   1.00 6.50  ? 467  LEU A N   1 
ATOM   3654 C  CA  . LEU A 1 467  ? 45.854 66.379  1.827   1.00 8.12  ? 467  LEU A CA  1 
ATOM   3655 C  C   . LEU A 1 467  ? 44.542 66.826  1.154   1.00 8.50  ? 467  LEU A C   1 
ATOM   3656 O  O   . LEU A 1 467  ? 43.451 66.673  1.719   1.00 6.88  ? 467  LEU A O   1 
ATOM   3657 C  CB  . LEU A 1 467  ? 46.552 67.592  2.448   1.00 8.34  ? 467  LEU A CB  1 
ATOM   3658 C  CG  . LEU A 1 467  ? 45.733 68.319  3.503   1.00 12.26 ? 467  LEU A CG  1 
ATOM   3659 C  CD1 . LEU A 1 467  ? 45.720 67.453  4.815   1.00 12.07 ? 467  LEU A CD1 1 
ATOM   3660 C  CD2 . LEU A 1 467  ? 46.348 69.725  3.762   1.00 10.52 ? 467  LEU A CD2 1 
ATOM   3661 N  N   . PHE A 1 468  ? 44.651 67.381  -0.046  1.00 8.18  ? 468  PHE A N   1 
ATOM   3662 C  CA  . PHE A 1 468  ? 43.470 67.870  -0.763  1.00 9.57  ? 468  PHE A CA  1 
ATOM   3663 C  C   . PHE A 1 468  ? 42.490 66.755  -1.141  1.00 9.51  ? 468  PHE A C   1 
ATOM   3664 O  O   . PHE A 1 468  ? 41.354 67.038  -1.521  1.00 10.21 ? 468  PHE A O   1 
ATOM   3665 C  CB  . PHE A 1 468  ? 43.886 68.647  -2.033  1.00 9.85  ? 468  PHE A CB  1 
ATOM   3666 C  CG  . PHE A 1 468  ? 42.759 69.448  -2.644  1.00 10.97 ? 468  PHE A CG  1 
ATOM   3667 C  CD1 . PHE A 1 468  ? 42.044 70.369  -1.863  1.00 10.58 ? 468  PHE A CD1 1 
ATOM   3668 C  CD2 . PHE A 1 468  ? 42.366 69.250  -3.959  1.00 9.05  ? 468  PHE A CD2 1 
ATOM   3669 C  CE1 . PHE A 1 468  ? 40.926 71.089  -2.403  1.00 10.24 ? 468  PHE A CE1 1 
ATOM   3670 C  CE2 . PHE A 1 468  ? 41.270 69.951  -4.500  1.00 9.75  ? 468  PHE A CE2 1 
ATOM   3671 C  CZ  . PHE A 1 468  ? 40.546 70.879  -3.708  1.00 9.05  ? 468  PHE A CZ  1 
ATOM   3672 N  N   . GLN A 1 469  ? 42.917 65.492  -1.061  1.00 8.39  ? 469  GLN A N   1 
ATOM   3673 C  CA  . GLN A 1 469  ? 42.007 64.394  -1.392  1.00 8.38  ? 469  GLN A CA  1 
ATOM   3674 C  C   . GLN A 1 469  ? 40.963 64.189  -0.289  1.00 8.58  ? 469  GLN A C   1 
ATOM   3675 O  O   . GLN A 1 469  ? 40.006 63.428  -0.458  1.00 9.24  ? 469  GLN A O   1 
ATOM   3676 C  CB  . GLN A 1 469  ? 42.795 63.089  -1.582  1.00 8.62  ? 469  GLN A CB  1 
ATOM   3677 C  CG  . GLN A 1 469  ? 43.864 63.170  -2.716  1.00 6.91  ? 469  GLN A CG  1 
ATOM   3678 C  CD  . GLN A 1 469  ? 43.296 63.752  -4.000  1.00 5.04  ? 469  GLN A CD  1 
ATOM   3679 O  OE1 . GLN A 1 469  ? 42.334 63.217  -4.585  1.00 5.74  ? 469  GLN A OE1 1 
ATOM   3680 N  NE2 . GLN A 1 469  ? 43.867 64.852  -4.432  1.00 7.02  ? 469  GLN A NE2 1 
ATOM   3681 N  N   . HIS A 1 470  ? 41.182 64.856  0.844   1.00 7.38  ? 470  HIS A N   1 
ATOM   3682 C  CA  . HIS A 1 470  ? 40.292 64.783  1.980   1.00 7.20  ? 470  HIS A CA  1 
ATOM   3683 C  C   . HIS A 1 470  ? 38.850 65.019  1.523   1.00 6.39  ? 470  HIS A C   1 
ATOM   3684 O  O   . HIS A 1 470  ? 38.615 65.741  0.551   1.00 5.75  ? 470  HIS A O   1 
ATOM   3685 C  CB  . HIS A 1 470  ? 40.724 65.818  3.049   1.00 6.21  ? 470  HIS A CB  1 
ATOM   3686 C  CG  . HIS A 1 470  ? 39.717 66.036  4.126   1.00 8.61  ? 470  HIS A CG  1 
ATOM   3687 N  ND1 . HIS A 1 470  ? 39.121 64.997  4.816   1.00 8.23  ? 470  HIS A ND1 1 
ATOM   3688 C  CD2 . HIS A 1 470  ? 39.211 67.178  4.655   1.00 8.15  ? 470  HIS A CD2 1 
ATOM   3689 C  CE1 . HIS A 1 470  ? 38.291 65.495  5.716   1.00 8.94  ? 470  HIS A CE1 1 
ATOM   3690 N  NE2 . HIS A 1 470  ? 38.324 66.814  5.639   1.00 8.57  ? 470  HIS A NE2 1 
ATOM   3691 N  N   . HIS A 1 471  ? 37.896 64.410  2.227   1.00 6.27  ? 471  HIS A N   1 
ATOM   3692 C  CA  . HIS A 1 471  ? 36.492 64.575  1.860   1.00 7.64  ? 471  HIS A CA  1 
ATOM   3693 C  C   . HIS A 1 471  ? 35.861 65.980  2.117   1.00 9.39  ? 471  HIS A C   1 
ATOM   3694 O  O   . HIS A 1 471  ? 34.639 66.137  1.987   1.00 8.95  ? 471  HIS A O   1 
ATOM   3695 C  CB  . HIS A 1 471  ? 35.639 63.451  2.472   1.00 8.52  ? 471  HIS A CB  1 
ATOM   3696 C  CG  . HIS A 1 471  ? 35.771 63.320  3.956   1.00 7.85  ? 471  HIS A CG  1 
ATOM   3697 N  ND1 . HIS A 1 471  ? 36.771 62.584  4.559   1.00 8.73  ? 471  HIS A ND1 1 
ATOM   3698 C  CD2 . HIS A 1 471  ? 35.055 63.883  4.962   1.00 8.30  ? 471  HIS A CD2 1 
ATOM   3699 C  CE1 . HIS A 1 471  ? 36.673 62.710  5.873   1.00 8.84  ? 471  HIS A CE1 1 
ATOM   3700 N  NE2 . HIS A 1 471  ? 35.643 63.493  6.141   1.00 8.25  ? 471  HIS A NE2 1 
ATOM   3701 N  N   . ASP A 1 472  ? 36.682 66.975  2.515   1.00 9.29  ? 472  ASP A N   1 
ATOM   3702 C  CA  . ASP A 1 472  ? 36.211 68.374  2.576   1.00 8.55  ? 472  ASP A CA  1 
ATOM   3703 C  C   . ASP A 1 472  ? 37.187 69.217  1.727   1.00 9.51  ? 472  ASP A C   1 
ATOM   3704 O  O   . ASP A 1 472  ? 37.117 70.457  1.705   1.00 10.52 ? 472  ASP A O   1 
ATOM   3705 C  CB  . ASP A 1 472  ? 36.174 68.936  3.987   1.00 9.99  ? 472  ASP A CB  1 
ATOM   3706 C  CG  . ASP A 1 472  ? 35.129 68.252  4.857   1.00 9.61  ? 472  ASP A CG  1 
ATOM   3707 O  OD1 . ASP A 1 472  ? 33.933 68.286  4.489   1.00 10.78 ? 472  ASP A OD1 1 
ATOM   3708 O  OD2 . ASP A 1 472  ? 35.518 67.688  5.889   1.00 9.25  ? 472  ASP A OD2 1 
ATOM   3709 N  N   . GLY A 1 473  ? 38.106 68.527  1.056   1.00 8.46  ? 473  GLY A N   1 
ATOM   3710 C  CA  . GLY A 1 473  ? 39.091 69.184  0.209   1.00 8.53  ? 473  GLY A CA  1 
ATOM   3711 C  C   . GLY A 1 473  ? 38.552 69.348  -1.197  1.00 8.86  ? 473  GLY A C   1 
ATOM   3712 O  O   . GLY A 1 473  ? 37.852 70.326  -1.508  1.00 8.08  ? 473  GLY A O   1 
ATOM   3713 N  N   . ILE A 1 474  ? 38.860 68.375  -2.055  1.00 7.90  ? 474  ILE A N   1 
ATOM   3714 C  CA  . ILE A 1 474  ? 38.426 68.400  -3.439  1.00 7.69  ? 474  ILE A CA  1 
ATOM   3715 C  C   . ILE A 1 474  ? 36.877 68.482  -3.575  1.00 8.55  ? 474  ILE A C   1 
ATOM   3716 O  O   . ILE A 1 474  ? 36.356 68.929  -4.593  1.00 8.33  ? 474  ILE A O   1 
ATOM   3717 C  CB  . ILE A 1 474  ? 38.998 67.155  -4.190  1.00 8.57  ? 474  ILE A CB  1 
ATOM   3718 C  CG1 . ILE A 1 474  ? 38.717 67.268  -5.686  1.00 8.04  ? 474  ILE A CG1 1 
ATOM   3719 C  CG2 . ILE A 1 474  ? 38.413 65.856  -3.584  1.00 8.68  ? 474  ILE A CG2 1 
ATOM   3720 C  CD1 . ILE A 1 474  ? 39.297 66.136  -6.477  1.00 10.23 ? 474  ILE A CD1 1 
ATOM   3721 N  N   . THR A 1 475  ? 36.156 68.081  -2.527  1.00 9.05  ? 475  THR A N   1 
ATOM   3722 C  CA  . THR A 1 475  ? 34.687 68.112  -2.519  1.00 8.94  ? 475  THR A CA  1 
ATOM   3723 C  C   . THR A 1 475  ? 34.136 69.553  -2.549  1.00 9.82  ? 475  THR A C   1 
ATOM   3724 O  O   . THR A 1 475  ? 32.973 69.770  -2.923  1.00 11.65 ? 475  THR A O   1 
ATOM   3725 C  CB  . THR A 1 475  ? 34.141 67.484  -1.238  1.00 9.52  ? 475  THR A CB  1 
ATOM   3726 O  OG1 . THR A 1 475  ? 34.692 68.216  -0.130  1.00 10.10 ? 475  THR A OG1 1 
ATOM   3727 C  CG2 . THR A 1 475  ? 34.526 65.958  -1.137  1.00 6.32  ? 475  THR A CG2 1 
ATOM   3728 N  N   . GLY A 1 476  ? 34.955 70.524  -2.179  1.00 9.91  ? 476  GLY A N   1 
ATOM   3729 C  CA  . GLY A 1 476  ? 34.472 71.902  -2.156  1.00 10.07 ? 476  GLY A CA  1 
ATOM   3730 C  C   . GLY A 1 476  ? 33.501 72.117  -0.984  1.00 10.07 ? 476  GLY A C   1 
ATOM   3731 O  O   . GLY A 1 476  ? 32.626 72.957  -1.075  1.00 10.70 ? 476  GLY A O   1 
ATOM   3732 N  N   . THR A 1 477  ? 33.646 71.375  0.116   1.00 9.54  ? 477  THR A N   1 
ATOM   3733 C  CA  . THR A 1 477  ? 32.736 71.513  1.259   1.00 9.39  ? 477  THR A CA  1 
ATOM   3734 C  C   . THR A 1 477  ? 33.376 72.128  2.525   1.00 10.77 ? 477  THR A C   1 
ATOM   3735 O  O   . THR A 1 477  ? 32.876 71.916  3.648   1.00 10.75 ? 477  THR A O   1 
ATOM   3736 C  CB  . THR A 1 477  ? 32.095 70.134  1.649   1.00 9.11  ? 477  THR A CB  1 
ATOM   3737 O  OG1 . THR A 1 477  ? 33.134 69.185  1.915   1.00 10.19 ? 477  THR A OG1 1 
ATOM   3738 C  CG2 . THR A 1 477  ? 31.211 69.574  0.514   1.00 8.58  ? 477  THR A CG2 1 
ATOM   3739 N  N   . ALA A 1 478  ? 34.471 72.872  2.352   1.00 10.44 ? 478  ALA A N   1 
ATOM   3740 C  CA  . ALA A 1 478  ? 35.139 73.503  3.492   1.00 11.76 ? 478  ALA A CA  1 
ATOM   3741 C  C   . ALA A 1 478  ? 34.836 75.005  3.560   1.00 11.94 ? 478  ALA A C   1 
ATOM   3742 O  O   . ALA A 1 478  ? 34.322 75.608  2.607   1.00 10.58 ? 478  ALA A O   1 
ATOM   3743 C  CB  . ALA A 1 478  ? 36.640 73.286  3.401   1.00 9.30  ? 478  ALA A CB  1 
ATOM   3744 N  N   . LYS A 1 479  ? 35.139 75.620  4.695   1.00 13.32 ? 479  LYS A N   1 
ATOM   3745 C  CA  . LYS A 1 479  ? 34.883 77.052  4.806   1.00 13.06 ? 479  LYS A CA  1 
ATOM   3746 C  C   . LYS A 1 479  ? 35.844 77.803  3.900   1.00 12.10 ? 479  LYS A C   1 
ATOM   3747 O  O   . LYS A 1 479  ? 36.906 77.303  3.544   1.00 9.51  ? 479  LYS A O   1 
ATOM   3748 C  CB  . LYS A 1 479  ? 35.038 77.539  6.268   1.00 15.35 ? 479  LYS A CB  1 
ATOM   3749 C  CG  . LYS A 1 479  ? 33.848 77.081  7.165   1.00 17.18 ? 479  LYS A CG  1 
ATOM   3750 C  CD  . LYS A 1 479  ? 33.684 77.924  8.433   1.00 21.08 ? 479  LYS A CD  1 
ATOM   3751 C  CE  . LYS A 1 479  ? 32.614 79.004  8.259   1.00 22.32 ? 479  LYS A CE  1 
ATOM   3752 N  NZ  . LYS A 1 479  ? 31.268 78.467  8.651   1.00 21.78 ? 479  LYS A NZ  1 
ATOM   3753 N  N   . THR A 1 480  ? 35.468 79.028  3.563   1.00 12.59 ? 480  THR A N   1 
ATOM   3754 C  CA  . THR A 1 480  ? 36.247 79.886  2.689   1.00 12.45 ? 480  THR A CA  1 
ATOM   3755 C  C   . THR A 1 480  ? 37.725 79.995  3.003   1.00 13.58 ? 480  THR A C   1 
ATOM   3756 O  O   . THR A 1 480  ? 38.575 79.787  2.119   1.00 13.58 ? 480  THR A O   1 
ATOM   3757 C  CB  . THR A 1 480  ? 35.635 81.307  2.704   1.00 14.30 ? 480  THR A CB  1 
ATOM   3758 O  OG1 . THR A 1 480  ? 34.274 81.209  2.289   1.00 15.53 ? 480  THR A OG1 1 
ATOM   3759 C  CG2 . THR A 1 480  ? 36.404 82.288  1.733   1.00 12.71 ? 480  THR A CG2 1 
ATOM   3760 N  N   . HIS A 1 481  ? 38.065 80.317  4.248   1.00 12.16 ? 481  HIS A N   1 
ATOM   3761 C  CA  . HIS A 1 481  ? 39.482 80.459  4.549   1.00 11.84 ? 481  HIS A CA  1 
ATOM   3762 C  C   . HIS A 1 481  ? 40.225 79.111  4.495   1.00 12.10 ? 481  HIS A C   1 
ATOM   3763 O  O   . HIS A 1 481  ? 41.448 79.085  4.329   1.00 11.28 ? 481  HIS A O   1 
ATOM   3764 C  CB  . HIS A 1 481  ? 39.696 81.181  5.908   1.00 12.27 ? 481  HIS A CB  1 
ATOM   3765 C  CG  . HIS A 1 481  ? 39.625 80.285  7.108   1.00 12.90 ? 481  HIS A CG  1 
ATOM   3766 N  ND1 . HIS A 1 481  ? 38.441 79.762  7.586   1.00 14.15 ? 481  HIS A ND1 1 
ATOM   3767 C  CD2 . HIS A 1 481  ? 40.603 79.786  7.899   1.00 14.05 ? 481  HIS A CD2 1 
ATOM   3768 C  CE1 . HIS A 1 481  ? 38.697 78.974  8.615   1.00 14.76 ? 481  HIS A CE1 1 
ATOM   3769 N  NE2 . HIS A 1 481  ? 40.003 78.972  8.825   1.00 13.82 ? 481  HIS A NE2 1 
ATOM   3770 N  N   . VAL A 1 482  ? 39.490 78.002  4.621   1.00 10.50 ? 482  VAL A N   1 
ATOM   3771 C  CA  . VAL A 1 482  ? 40.117 76.666  4.579   1.00 9.69  ? 482  VAL A CA  1 
ATOM   3772 C  C   . VAL A 1 482  ? 40.433 76.335  3.103   1.00 9.17  ? 482  VAL A C   1 
ATOM   3773 O  O   . VAL A 1 482  ? 41.497 75.823  2.795   1.00 10.67 ? 482  VAL A O   1 
ATOM   3774 C  CB  . VAL A 1 482  ? 39.185 75.598  5.242   1.00 8.33  ? 482  VAL A CB  1 
ATOM   3775 C  CG1 . VAL A 1 482  ? 39.798 74.185  5.132   1.00 6.16  ? 482  VAL A CG1 1 
ATOM   3776 C  CG2 . VAL A 1 482  ? 38.992 75.958  6.764   1.00 7.82  ? 482  VAL A CG2 1 
ATOM   3777 N  N   . VAL A 1 483  ? 39.504 76.644  2.209   1.00 9.52  ? 483  VAL A N   1 
ATOM   3778 C  CA  . VAL A 1 483  ? 39.682 76.456  0.773   1.00 9.84  ? 483  VAL A CA  1 
ATOM   3779 C  C   . VAL A 1 483  ? 40.923 77.271  0.366   1.00 10.85 ? 483  VAL A C   1 
ATOM   3780 O  O   . VAL A 1 483  ? 41.766 76.816  -0.419  1.00 11.06 ? 483  VAL A O   1 
ATOM   3781 C  CB  . VAL A 1 483  ? 38.417 76.992  0.026   1.00 12.29 ? 483  VAL A CB  1 
ATOM   3782 C  CG1 . VAL A 1 483  ? 38.639 77.077  -1.491  1.00 12.89 ? 483  VAL A CG1 1 
ATOM   3783 C  CG2 . VAL A 1 483  ? 37.193 76.067  0.371   1.00 13.96 ? 483  VAL A CG2 1 
ATOM   3784 N  N   . VAL A 1 484  ? 41.062 78.473  0.923   1.00 11.23 ? 484  VAL A N   1 
ATOM   3785 C  CA  . VAL A 1 484  ? 42.217 79.295  0.572   1.00 12.25 ? 484  VAL A CA  1 
ATOM   3786 C  C   . VAL A 1 484  ? 43.491 78.588  0.998   1.00 11.21 ? 484  VAL A C   1 
ATOM   3787 O  O   . VAL A 1 484  ? 44.500 78.555  0.270   1.00 11.59 ? 484  VAL A O   1 
ATOM   3788 C  CB  . VAL A 1 484  ? 42.141 80.671  1.250   1.00 12.20 ? 484  VAL A CB  1 
ATOM   3789 C  CG1 . VAL A 1 484  ? 43.515 81.384  1.121   1.00 10.94 ? 484  VAL A CG1 1 
ATOM   3790 C  CG2 . VAL A 1 484  ? 41.014 81.484  0.604   1.00 12.80 ? 484  VAL A CG2 1 
ATOM   3791 N  N   . ASP A 1 485  ? 43.440 77.981  2.175   1.00 12.35 ? 485  ASP A N   1 
ATOM   3792 C  CA  . ASP A 1 485  ? 44.614 77.259  2.691   1.00 10.71 ? 485  ASP A CA  1 
ATOM   3793 C  C   . ASP A 1 485  ? 44.979 76.082  1.770   1.00 10.64 ? 485  ASP A C   1 
ATOM   3794 O  O   . ASP A 1 485  ? 46.159 75.831  1.501   1.00 11.86 ? 485  ASP A O   1 
ATOM   3795 C  CB  . ASP A 1 485  ? 44.329 76.719  4.082   1.00 10.44 ? 485  ASP A CB  1 
ATOM   3796 C  CG  . ASP A 1 485  ? 45.553 76.095  4.716   1.00 11.52 ? 485  ASP A CG  1 
ATOM   3797 O  OD1 . ASP A 1 485  ? 45.515 74.944  5.155   1.00 11.40 ? 485  ASP A OD1 1 
ATOM   3798 O  OD2 . ASP A 1 485  ? 46.576 76.776  4.770   1.00 12.35 ? 485  ASP A OD2 1 
ATOM   3799 N  N   . TYR A 1 486  ? 43.988 75.320  1.323   1.00 10.73 ? 486  TYR A N   1 
ATOM   3800 C  CA  . TYR A 1 486  ? 44.285 74.197  0.407   1.00 9.21  ? 486  TYR A CA  1 
ATOM   3801 C  C   . TYR A 1 486  ? 44.901 74.727  -0.899  1.00 9.60  ? 486  TYR A C   1 
ATOM   3802 O  O   . TYR A 1 486  ? 45.789 74.099  -1.485  1.00 9.19  ? 486  TYR A O   1 
ATOM   3803 C  CB  . TYR A 1 486  ? 43.016 73.455  0.049   1.00 9.00  ? 486  TYR A CB  1 
ATOM   3804 C  CG  . TYR A 1 486  ? 42.411 72.658  1.186   1.00 10.74 ? 486  TYR A CG  1 
ATOM   3805 C  CD1 . TYR A 1 486  ? 41.028 72.634  1.370   1.00 9.99  ? 486  TYR A CD1 1 
ATOM   3806 C  CD2 . TYR A 1 486  ? 43.209 71.832  2.006   1.00 11.52 ? 486  TYR A CD2 1 
ATOM   3807 C  CE1 . TYR A 1 486  ? 40.426 71.791  2.335   1.00 11.30 ? 486  TYR A CE1 1 
ATOM   3808 C  CE2 . TYR A 1 486  ? 42.615 70.986  2.985   1.00 11.07 ? 486  TYR A CE2 1 
ATOM   3809 C  CZ  . TYR A 1 486  ? 41.219 70.979  3.126   1.00 10.61 ? 486  TYR A CZ  1 
ATOM   3810 O  OH  . TYR A 1 486  ? 40.601 70.144  4.005   1.00 11.65 ? 486  TYR A OH  1 
ATOM   3811 N  N   . GLU A 1 487  ? 44.402 75.871  -1.362  1.00 9.60  ? 487  GLU A N   1 
ATOM   3812 C  CA  . GLU A 1 487  ? 44.898 76.462  -2.604  1.00 11.67 ? 487  GLU A CA  1 
ATOM   3813 C  C   . GLU A 1 487  ? 46.367 76.877  -2.464  1.00 13.27 ? 487  GLU A C   1 
ATOM   3814 O  O   . GLU A 1 487  ? 47.181 76.614  -3.338  1.00 12.33 ? 487  GLU A O   1 
ATOM   3815 C  CB  . GLU A 1 487  ? 44.084 77.704  -2.986  1.00 12.47 ? 487  GLU A CB  1 
ATOM   3816 C  CG  . GLU A 1 487  ? 44.455 78.204  -4.370  1.00 15.72 ? 487  GLU A CG  1 
ATOM   3817 C  CD  . GLU A 1 487  ? 43.638 79.398  -4.856  1.00 18.49 ? 487  GLU A CD  1 
ATOM   3818 O  OE1 . GLU A 1 487  ? 42.463 79.525  -4.451  1.00 19.01 ? 487  GLU A OE1 1 
ATOM   3819 O  OE2 . GLU A 1 487  ? 44.176 80.188  -5.676  1.00 20.04 ? 487  GLU A OE2 1 
ATOM   3820 N  N   . GLN A 1 488  ? 46.696 77.550  -1.363  1.00 14.46 ? 488  GLN A N   1 
ATOM   3821 C  CA  . GLN A 1 488  ? 48.063 77.998  -1.155  1.00 15.63 ? 488  GLN A CA  1 
ATOM   3822 C  C   . GLN A 1 488  ? 48.985 76.796  -1.046  1.00 14.04 ? 488  GLN A C   1 
ATOM   3823 O  O   . GLN A 1 488  ? 50.088 76.821  -1.571  1.00 14.09 ? 488  GLN A O   1 
ATOM   3824 C  CB  . GLN A 1 488  ? 48.141 78.846  0.120   1.00 18.74 ? 488  GLN A CB  1 
ATOM   3825 C  CG  . GLN A 1 488  ? 47.121 79.976  0.078   1.00 25.52 ? 488  GLN A CG  1 
ATOM   3826 C  CD  . GLN A 1 488  ? 47.282 80.962  1.215   1.00 29.45 ? 488  GLN A CD  1 
ATOM   3827 O  OE1 . GLN A 1 488  ? 47.445 80.581  2.387   1.00 32.72 ? 488  GLN A OE1 1 
ATOM   3828 N  NE2 . GLN A 1 488  ? 47.234 82.253  0.875   1.00 32.45 ? 488  GLN A NE2 1 
ATOM   3829 N  N   . ARG A 1 489  ? 48.539 75.754  -0.351  1.00 11.94 ? 489  ARG A N   1 
ATOM   3830 C  CA  . ARG A 1 489  ? 49.344 74.540  -0.220  1.00 10.69 ? 489  ARG A CA  1 
ATOM   3831 C  C   . ARG A 1 489  ? 49.572 73.941  -1.614  1.00 11.29 ? 489  ARG A C   1 
ATOM   3832 O  O   . ARG A 1 489  ? 50.707 73.640  -1.992  1.00 9.70  ? 489  ARG A O   1 
ATOM   3833 C  CB  . ARG A 1 489  ? 48.643 73.506  0.670   1.00 11.46 ? 489  ARG A CB  1 
ATOM   3834 C  CG  . ARG A 1 489  ? 48.612 73.870  2.158   1.00 9.94  ? 489  ARG A CG  1 
ATOM   3835 C  CD  . ARG A 1 489  ? 47.748 72.839  2.919   1.00 12.75 ? 489  ARG A CD  1 
ATOM   3836 N  NE  . ARG A 1 489  ? 47.774 73.031  4.366   1.00 11.50 ? 489  ARG A NE  1 
ATOM   3837 C  CZ  . ARG A 1 489  ? 48.667 72.470  5.187   1.00 13.97 ? 489  ARG A CZ  1 
ATOM   3838 N  NH1 . ARG A 1 489  ? 49.603 71.662  4.697   1.00 9.50  ? 489  ARG A NH1 1 
ATOM   3839 N  NH2 . ARG A 1 489  ? 48.661 72.771  6.493   1.00 11.83 ? 489  ARG A NH2 1 
ATOM   3840 N  N   . MET A 1 490  ? 48.507 73.814  -2.404  1.00 10.85 ? 490  MET A N   1 
ATOM   3841 C  CA  . MET A 1 490  ? 48.686 73.254  -3.745  1.00 10.47 ? 490  MET A CA  1 
ATOM   3842 C  C   . MET A 1 490  ? 49.570 74.153  -4.585  1.00 10.14 ? 490  MET A C   1 
ATOM   3843 O  O   . MET A 1 490  ? 50.367 73.665  -5.359  1.00 9.72  ? 490  MET A O   1 
ATOM   3844 C  CB  . MET A 1 490  ? 47.335 72.991  -4.428  1.00 8.42  ? 490  MET A CB  1 
ATOM   3845 C  CG  . MET A 1 490  ? 46.564 71.846  -3.758  1.00 9.17  ? 490  MET A CG  1 
ATOM   3846 S  SD  . MET A 1 490  ? 45.239 71.204  -4.841  1.00 13.60 ? 490  MET A SD  1 
ATOM   3847 C  CE  . MET A 1 490  ? 43.900 72.425  -4.523  1.00 15.16 ? 490  MET A CE  1 
ATOM   3848 N  N   . GLN A 1 491  ? 49.454 75.463  -4.415  1.00 11.89 ? 491  GLN A N   1 
ATOM   3849 C  CA  . GLN A 1 491  ? 50.302 76.383  -5.173  1.00 14.15 ? 491  GLN A CA  1 
ATOM   3850 C  C   . GLN A 1 491  ? 51.794 76.129  -4.869  1.00 13.81 ? 491  GLN A C   1 
ATOM   3851 O  O   . GLN A 1 491  ? 52.644 76.101  -5.766  1.00 12.48 ? 491  GLN A O   1 
ATOM   3852 C  CB  . GLN A 1 491  ? 49.936 77.815  -4.830  1.00 18.48 ? 491  GLN A CB  1 
ATOM   3853 C  CG  . GLN A 1 491  ? 50.584 78.833  -5.715  1.00 23.63 ? 491  GLN A CG  1 
ATOM   3854 C  CD  . GLN A 1 491  ? 50.058 78.769  -7.143  1.00 27.66 ? 491  GLN A CD  1 
ATOM   3855 O  OE1 . GLN A 1 491  ? 50.686 78.180  -8.042  1.00 30.34 ? 491  GLN A OE1 1 
ATOM   3856 N  NE2 . GLN A 1 491  ? 48.887 79.371  -7.358  1.00 30.42 ? 491  GLN A NE2 1 
ATOM   3857 N  N   . GLU A 1 492  ? 52.114 75.928  -3.597  1.00 14.12 ? 492  GLU A N   1 
ATOM   3858 C  CA  . GLU A 1 492  ? 53.486 75.647  -3.235  1.00 15.59 ? 492  GLU A CA  1 
ATOM   3859 C  C   . GLU A 1 492  ? 53.865 74.291  -3.836  1.00 12.93 ? 492  GLU A C   1 
ATOM   3860 O  O   . GLU A 1 492  ? 54.997 74.112  -4.287  1.00 11.91 ? 492  GLU A O   1 
ATOM   3861 C  CB  . GLU A 1 492  ? 53.658 75.646  -1.723  1.00 18.54 ? 492  GLU A CB  1 
ATOM   3862 C  CG  . GLU A 1 492  ? 53.545 77.048  -1.097  1.00 23.98 ? 492  GLU A CG  1 
ATOM   3863 C  CD  . GLU A 1 492  ? 54.498 78.073  -1.755  1.00 27.94 ? 492  GLU A CD  1 
ATOM   3864 O  OE1 . GLU A 1 492  ? 54.019 79.177  -2.116  1.00 31.12 ? 492  GLU A OE1 1 
ATOM   3865 O  OE2 . GLU A 1 492  ? 55.716 77.791  -1.913  1.00 30.32 ? 492  GLU A OE2 1 
ATOM   3866 N  N   . ALA A 1 493  ? 52.911 73.354  -3.869  1.00 10.61 ? 493  ALA A N   1 
ATOM   3867 C  CA  . ALA A 1 493  ? 53.182 72.029  -4.452  1.00 9.32  ? 493  ALA A CA  1 
ATOM   3868 C  C   . ALA A 1 493  ? 53.490 72.168  -5.961  1.00 9.38  ? 493  ALA A C   1 
ATOM   3869 O  O   . ALA A 1 493  ? 54.393 71.506  -6.487  1.00 9.46  ? 493  ALA A O   1 
ATOM   3870 C  CB  . ALA A 1 493  ? 51.987 71.102  -4.245  1.00 7.55  ? 493  ALA A CB  1 
ATOM   3871 N  N   . LEU A 1 494  ? 52.743 73.009  -6.665  1.00 8.50  ? 494  LEU A N   1 
ATOM   3872 C  CA  . LEU A 1 494  ? 53.014 73.195  -8.097  1.00 9.93  ? 494  LEU A CA  1 
ATOM   3873 C  C   . LEU A 1 494  ? 54.438 73.761  -8.301  1.00 9.88  ? 494  LEU A C   1 
ATOM   3874 O  O   . LEU A 1 494  ? 55.175 73.285  -9.150  1.00 9.85  ? 494  LEU A O   1 
ATOM   3875 C  CB  . LEU A 1 494  ? 51.957 74.118  -8.722  1.00 10.52 ? 494  LEU A CB  1 
ATOM   3876 C  CG  . LEU A 1 494  ? 50.575 73.453  -8.844  1.00 10.17 ? 494  LEU A CG  1 
ATOM   3877 C  CD1 . LEU A 1 494  ? 49.487 74.490  -9.237  1.00 11.24 ? 494  LEU A CD1 1 
ATOM   3878 C  CD2 . LEU A 1 494  ? 50.685 72.372  -9.892  1.00 9.99  ? 494  LEU A CD2 1 
ATOM   3879 N  N   . LYS A 1 495  ? 54.816 74.775  -7.531  1.00 10.38 ? 495  LYS A N   1 
ATOM   3880 C  CA  . LYS A 1 495  ? 56.164 75.350  -7.629  1.00 12.19 ? 495  LYS A CA  1 
ATOM   3881 C  C   . LYS A 1 495  ? 57.255 74.307  -7.325  1.00 12.45 ? 495  LYS A C   1 
ATOM   3882 O  O   . LYS A 1 495  ? 58.307 74.279  -7.985  1.00 10.63 ? 495  LYS A O   1 
ATOM   3883 C  CB  . LYS A 1 495  ? 56.311 76.531  -6.661  1.00 15.34 ? 495  LYS A CB  1 
ATOM   3884 C  CG  . LYS A 1 495  ? 55.466 77.727  -7.078  1.00 19.97 ? 495  LYS A CG  1 
ATOM   3885 C  CD  . LYS A 1 495  ? 55.971 79.035  -6.477  1.00 24.68 ? 495  LYS A CD  1 
ATOM   3886 C  CE  . LYS A 1 495  ? 55.809 79.082  -4.979  1.00 28.34 ? 495  LYS A CE  1 
ATOM   3887 N  NZ  . LYS A 1 495  ? 54.378 79.181  -4.529  1.00 32.79 ? 495  LYS A NZ  1 
ATOM   3888 N  N   . ALA A 1 496  ? 57.002 73.448  -6.333  1.00 10.54 ? 496  ALA A N   1 
ATOM   3889 C  CA  . ALA A 1 496  ? 57.963 72.403  -5.992  1.00 10.22 ? 496  ALA A CA  1 
ATOM   3890 C  C   . ALA A 1 496  ? 58.136 71.475  -7.224  1.00 10.13 ? 496  ALA A C   1 
ATOM   3891 O  O   . ALA A 1 496  ? 59.266 71.153  -7.619  1.00 9.22  ? 496  ALA A O   1 
ATOM   3892 C  CB  . ALA A 1 496  ? 57.471 71.606  -4.767  1.00 9.80  ? 496  ALA A CB  1 
ATOM   3893 N  N   . CYS A 1 497  ? 57.021 71.054  -7.830  1.00 9.99  ? 497  CYS A N   1 
ATOM   3894 C  CA  . CYS A 1 497  ? 57.069 70.184  -9.023  1.00 9.32  ? 497  CYS A CA  1 
ATOM   3895 C  C   . CYS A 1 497  ? 57.858 70.850  -10.153 1.00 8.56  ? 497  CYS A C   1 
ATOM   3896 O  O   . CYS A 1 497  ? 58.731 70.242  -10.766 1.00 8.81  ? 497  CYS A O   1 
ATOM   3897 C  CB  . CYS A 1 497  ? 55.642 69.852  -9.510  1.00 9.00  ? 497  CYS A CB  1 
ATOM   3898 S  SG  . CYS A 1 497  ? 54.738 68.687  -8.372  1.00 9.19  ? 497  CYS A SG  1 
ATOM   3899 N  N   . GLN A 1 498  ? 57.571 72.115  -10.398 1.00 9.39  ? 498  GLN A N   1 
ATOM   3900 C  CA  . GLN A 1 498  ? 58.269 72.861  -11.451 1.00 10.94 ? 498  GLN A CA  1 
ATOM   3901 C  C   . GLN A 1 498  ? 59.785 72.837  -11.208 1.00 10.27 ? 498  GLN A C   1 
ATOM   3902 O  O   . GLN A 1 498  ? 60.556 72.519  -12.102 1.00 9.22  ? 498  GLN A O   1 
ATOM   3903 C  CB  . GLN A 1 498  ? 57.798 74.314  -11.479 1.00 13.14 ? 498  GLN A CB  1 
ATOM   3904 C  CG  . GLN A 1 498  ? 58.493 75.110  -12.558 1.00 17.84 ? 498  GLN A CG  1 
ATOM   3905 C  CD  . GLN A 1 498  ? 57.996 76.552  -12.695 1.00 21.07 ? 498  GLN A CD  1 
ATOM   3906 O  OE1 . GLN A 1 498  ? 57.891 77.076  -13.813 1.00 19.97 ? 498  GLN A OE1 1 
ATOM   3907 N  NE2 . GLN A 1 498  ? 57.711 77.207  -11.556 1.00 22.70 ? 498  GLN A NE2 1 
ATOM   3908 N  N   . MET A 1 499  ? 60.202 73.176  -9.993  1.00 9.76  ? 499  MET A N   1 
ATOM   3909 C  CA  . MET A 1 499  ? 61.626 73.187  -9.667  1.00 10.23 ? 499  MET A CA  1 
ATOM   3910 C  C   . MET A 1 499  ? 62.274 71.830  -9.976  1.00 9.36  ? 499  MET A C   1 
ATOM   3911 O  O   . MET A 1 499  ? 63.334 71.773  -10.590 1.00 8.87  ? 499  MET A O   1 
ATOM   3912 C  CB  . MET A 1 499  ? 61.819 73.535  -8.189  1.00 9.92  ? 499  MET A CB  1 
ATOM   3913 C  CG  . MET A 1 499  ? 63.223 73.347  -7.668  1.00 14.56 ? 499  MET A CG  1 
ATOM   3914 S  SD  . MET A 1 499  ? 64.517 74.386  -8.507  1.00 17.70 ? 499  MET A SD  1 
ATOM   3915 C  CE  . MET A 1 499  ? 64.199 75.930  -7.843  1.00 12.52 ? 499  MET A CE  1 
ATOM   3916 N  N   . VAL A 1 500  ? 61.652 70.743  -9.513  1.00 9.29  ? 500  VAL A N   1 
ATOM   3917 C  CA  . VAL A 1 500  ? 62.194 69.403  -9.744  1.00 8.48  ? 500  VAL A CA  1 
ATOM   3918 C  C   . VAL A 1 500  ? 62.208 69.054  -11.224 1.00 8.69  ? 500  VAL A C   1 
ATOM   3919 O  O   . VAL A 1 500  ? 63.192 68.531  -11.762 1.00 8.61  ? 500  VAL A O   1 
ATOM   3920 C  CB  . VAL A 1 500  ? 61.371 68.329  -8.946  1.00 7.89  ? 500  VAL A CB  1 
ATOM   3921 C  CG1 . VAL A 1 500  ? 61.805 66.934  -9.347  1.00 6.50  ? 500  VAL A CG1 1 
ATOM   3922 C  CG2 . VAL A 1 500  ? 61.618 68.509  -7.425  1.00 6.22  ? 500  VAL A CG2 1 
ATOM   3923 N  N   . MET A 1 501  ? 61.104 69.342  -11.897 1.00 8.46  ? 501  MET A N   1 
ATOM   3924 C  CA  . MET A 1 501  ? 61.002 69.041  -13.318 1.00 9.31  ? 501  MET A CA  1 
ATOM   3925 C  C   . MET A 1 501  ? 62.075 69.780  -14.127 1.00 9.57  ? 501  MET A C   1 
ATOM   3926 O  O   . MET A 1 501  ? 62.779 69.162  -14.931 1.00 10.76 ? 501  MET A O   1 
ATOM   3927 C  CB  . MET A 1 501  ? 59.623 69.423  -13.843 1.00 8.48  ? 501  MET A CB  1 
ATOM   3928 C  CG  . MET A 1 501  ? 58.500 68.525  -13.357 1.00 10.18 ? 501  MET A CG  1 
ATOM   3929 S  SD  . MET A 1 501  ? 56.864 69.214  -13.633 1.00 15.39 ? 501  MET A SD  1 
ATOM   3930 C  CE  . MET A 1 501  ? 56.716 68.972  -15.364 1.00 13.67 ? 501  MET A CE  1 
ATOM   3931 N  N   . GLN A 1 502  ? 62.219 71.086  -13.914 1.00 8.96  ? 502  GLN A N   1 
ATOM   3932 C  CA  . GLN A 1 502  ? 63.202 71.837  -14.697 1.00 10.17 ? 502  GLN A CA  1 
ATOM   3933 C  C   . GLN A 1 502  ? 64.661 71.427  -14.384 1.00 10.06 ? 502  GLN A C   1 
ATOM   3934 O  O   . GLN A 1 502  ? 65.491 71.360  -15.292 1.00 9.66  ? 502  GLN A O   1 
ATOM   3935 C  CB  . GLN A 1 502  ? 62.969 73.354  -14.557 1.00 10.11 ? 502  GLN A CB  1 
ATOM   3936 C  CG  . GLN A 1 502  ? 63.179 73.960  -13.158 1.00 10.98 ? 502  GLN A CG  1 
ATOM   3937 C  CD  . GLN A 1 502  ? 64.608 74.483  -12.974 1.00 13.94 ? 502  GLN A CD  1 
ATOM   3938 O  OE1 . GLN A 1 502  ? 65.341 74.648  -13.968 1.00 12.17 ? 502  GLN A OE1 1 
ATOM   3939 N  NE2 . GLN A 1 502  ? 65.005 74.756  -11.709 1.00 12.26 ? 502  GLN A NE2 1 
ATOM   3940 N  N   . GLN A 1 503  ? 64.969 71.119  -13.127 1.00 9.09  ? 503  GLN A N   1 
ATOM   3941 C  CA  . GLN A 1 503  ? 66.327 70.651  -12.796 1.00 9.85  ? 503  GLN A CA  1 
ATOM   3942 C  C   . GLN A 1 503  ? 66.540 69.320  -13.525 1.00 9.82  ? 503  GLN A C   1 
ATOM   3943 O  O   . GLN A 1 503  ? 67.628 69.043  -14.052 1.00 9.04  ? 503  GLN A O   1 
ATOM   3944 C  CB  . GLN A 1 503  ? 66.484 70.411  -11.285 1.00 10.55 ? 503  GLN A CB  1 
ATOM   3945 C  CG  . GLN A 1 503  ? 66.650 71.687  -10.447 1.00 13.30 ? 503  GLN A CG  1 
ATOM   3946 C  CD  . GLN A 1 503  ? 68.007 72.356  -10.671 1.00 15.21 ? 503  GLN A CD  1 
ATOM   3947 O  OE1 . GLN A 1 503  ? 68.989 71.682  -11.034 1.00 15.32 ? 503  GLN A OE1 1 
ATOM   3948 N  NE2 . GLN A 1 503  ? 68.074 73.684  -10.450 1.00 15.95 ? 503  GLN A NE2 1 
ATOM   3949 N  N   . SER A 1 504  ? 65.499 68.486  -13.548 1.00 8.31  ? 504  SER A N   1 
ATOM   3950 C  CA  . SER A 1 504  ? 65.588 67.191  -14.215 1.00 9.36  ? 504  SER A CA  1 
ATOM   3951 C  C   . SER A 1 504  ? 65.821 67.338  -15.716 1.00 9.73  ? 504  SER A C   1 
ATOM   3952 O  O   . SER A 1 504  ? 66.662 66.650  -16.297 1.00 10.58 ? 504  SER A O   1 
ATOM   3953 C  CB  . SER A 1 504  ? 64.308 66.387  -13.966 1.00 9.76  ? 504  SER A CB  1 
ATOM   3954 O  OG  . SER A 1 504  ? 64.209 66.007  -12.589 1.00 10.88 ? 504  SER A OG  1 
ATOM   3955 N  N   . VAL A 1 505  ? 65.077 68.234  -16.354 1.00 9.66  ? 505  VAL A N   1 
ATOM   3956 C  CA  . VAL A 1 505  ? 65.249 68.435  -17.794 1.00 10.03 ? 505  VAL A CA  1 
ATOM   3957 C  C   . VAL A 1 505  ? 66.676 68.927  -18.079 1.00 10.94 ? 505  VAL A C   1 
ATOM   3958 O  O   . VAL A 1 505  ? 67.357 68.477  -19.007 1.00 11.37 ? 505  VAL A O   1 
ATOM   3959 C  CB  . VAL A 1 505  ? 64.233 69.469  -18.332 1.00 10.36 ? 505  VAL A CB  1 
ATOM   3960 C  CG1 . VAL A 1 505  ? 64.564 69.860  -19.797 1.00 8.91  ? 505  VAL A CG1 1 
ATOM   3961 C  CG2 . VAL A 1 505  ? 62.816 68.868  -18.272 1.00 10.58 ? 505  VAL A CG2 1 
ATOM   3962 N  N   . TYR A 1 506  ? 67.133 69.860  -17.277 1.00 11.00 ? 506  TYR A N   1 
ATOM   3963 C  CA  . TYR A 1 506  ? 68.472 70.383  -17.501 1.00 12.90 ? 506  TYR A CA  1 
ATOM   3964 C  C   . TYR A 1 506  ? 69.526 69.258  -17.481 1.00 13.66 ? 506  TYR A C   1 
ATOM   3965 O  O   . TYR A 1 506  ? 70.394 69.171  -18.363 1.00 12.84 ? 506  TYR A O   1 
ATOM   3966 C  CB  . TYR A 1 506  ? 68.797 71.459  -16.453 1.00 12.71 ? 506  TYR A CB  1 
ATOM   3967 C  CG  . TYR A 1 506  ? 70.115 72.108  -16.735 1.00 15.36 ? 506  TYR A CG  1 
ATOM   3968 C  CD1 . TYR A 1 506  ? 70.349 72.719  -17.976 1.00 17.55 ? 506  TYR A CD1 1 
ATOM   3969 C  CD2 . TYR A 1 506  ? 71.148 72.086  -15.796 1.00 16.08 ? 506  TYR A CD2 1 
ATOM   3970 C  CE1 . TYR A 1 506  ? 71.595 73.302  -18.276 1.00 19.78 ? 506  TYR A CE1 1 
ATOM   3971 C  CE2 . TYR A 1 506  ? 72.384 72.654  -16.092 1.00 19.03 ? 506  TYR A CE2 1 
ATOM   3972 C  CZ  . TYR A 1 506  ? 72.594 73.260  -17.331 1.00 20.28 ? 506  TYR A CZ  1 
ATOM   3973 O  OH  . TYR A 1 506  ? 73.817 73.840  -17.632 1.00 26.73 ? 506  TYR A OH  1 
ATOM   3974 N  N   . ARG A 1 507  ? 69.436 68.386  -16.492 1.00 11.88 ? 507  ARG A N   1 
ATOM   3975 C  CA  . ARG A 1 507  ? 70.382 67.284  -16.381 1.00 11.60 ? 507  ARG A CA  1 
ATOM   3976 C  C   . ARG A 1 507  ? 70.246 66.233  -17.493 1.00 11.87 ? 507  ARG A C   1 
ATOM   3977 O  O   . ARG A 1 507  ? 71.237 65.715  -18.006 1.00 10.25 ? 507  ARG A O   1 
ATOM   3978 C  CB  . ARG A 1 507  ? 70.224 66.614  -15.018 1.00 12.13 ? 507  ARG A CB  1 
ATOM   3979 C  CG  . ARG A 1 507  ? 71.318 65.569  -14.715 1.00 13.30 ? 507  ARG A CG  1 
ATOM   3980 C  CD  . ARG A 1 507  ? 71.153 65.105  -13.282 1.00 13.97 ? 507  ARG A CD  1 
ATOM   3981 N  NE  . ARG A 1 507  ? 72.188 64.161  -12.868 1.00 16.10 ? 507  ARG A NE  1 
ATOM   3982 C  CZ  . ARG A 1 507  ? 72.243 63.596  -11.660 1.00 17.21 ? 507  ARG A CZ  1 
ATOM   3983 N  NH1 . ARG A 1 507  ? 71.324 63.876  -10.734 1.00 15.00 ? 507  ARG A NH1 1 
ATOM   3984 N  NH2 . ARG A 1 507  ? 73.211 62.734  -11.383 1.00 16.63 ? 507  ARG A NH2 1 
ATOM   3985 N  N   . LEU A 1 508  ? 69.013 65.942  -17.868 1.00 10.35 ? 508  LEU A N   1 
ATOM   3986 C  CA  . LEU A 1 508  ? 68.751 64.960  -18.880 1.00 10.75 ? 508  LEU A CA  1 
ATOM   3987 C  C   . LEU A 1 508  ? 69.179 65.396  -20.262 1.00 11.56 ? 508  LEU A C   1 
ATOM   3988 O  O   . LEU A 1 508  ? 69.531 64.567  -21.090 1.00 11.58 ? 508  LEU A O   1 
ATOM   3989 C  CB  . LEU A 1 508  ? 67.260 64.611  -18.895 1.00 10.00 ? 508  LEU A CB  1 
ATOM   3990 C  CG  . LEU A 1 508  ? 66.778 63.725  -17.713 1.00 11.55 ? 508  LEU A CG  1 
ATOM   3991 C  CD1 . LEU A 1 508  ? 65.243 63.778  -17.589 1.00 9.45  ? 508  LEU A CD1 1 
ATOM   3992 C  CD2 . LEU A 1 508  ? 67.260 62.280  -17.928 1.00 11.06 ? 508  LEU A CD2 1 
ATOM   3993 N  N   . LEU A 1 509  ? 69.147 66.690  -20.536 1.00 12.23 ? 509  LEU A N   1 
ATOM   3994 C  CA  . LEU A 1 509  ? 69.475 67.134  -21.883 1.00 11.71 ? 509  LEU A CA  1 
ATOM   3995 C  C   . LEU A 1 509  ? 70.769 67.942  -22.021 1.00 12.70 ? 509  LEU A C   1 
ATOM   3996 O  O   . LEU A 1 509  ? 70.925 68.705  -22.997 1.00 13.17 ? 509  LEU A O   1 
ATOM   3997 C  CB  . LEU A 1 509  ? 68.286 67.938  -22.441 1.00 10.82 ? 509  LEU A CB  1 
ATOM   3998 C  CG  . LEU A 1 509  ? 66.999 67.138  -22.659 1.00 11.01 ? 509  LEU A CG  1 
ATOM   3999 C  CD1 . LEU A 1 509  ? 65.876 68.053  -23.152 1.00 8.31  ? 509  LEU A CD1 1 
ATOM   4000 C  CD2 . LEU A 1 509  ? 67.245 66.010  -23.667 1.00 10.49 ? 509  LEU A CD2 1 
ATOM   4001 N  N   . THR A 1 510  ? 71.692 67.800  -21.057 1.00 12.01 ? 510  THR A N   1 
ATOM   4002 C  CA  . THR A 1 510  ? 72.952 68.546  -21.130 1.00 12.00 ? 510  THR A CA  1 
ATOM   4003 C  C   . THR A 1 510  ? 74.125 67.564  -21.122 1.00 12.97 ? 510  THR A C   1 
ATOM   4004 O  O   . THR A 1 510  ? 74.155 66.632  -20.302 1.00 11.11 ? 510  THR A O   1 
ATOM   4005 C  CB  . THR A 1 510  ? 73.092 69.514  -19.932 1.00 12.16 ? 510  THR A CB  1 
ATOM   4006 O  OG1 . THR A 1 510  ? 71.993 70.440  -19.936 1.00 11.43 ? 510  THR A OG1 1 
ATOM   4007 C  CG2 . THR A 1 510  ? 74.391 70.295  -20.007 1.00 12.75 ? 510  THR A CG2 1 
ATOM   4008 N  N   . LYS A 1 511  ? 75.070 67.762  -22.043 1.00 14.61 ? 511  LYS A N   1 
ATOM   4009 C  CA  . LYS A 1 511  ? 76.276 66.908  -22.140 1.00 15.77 ? 511  LYS A CA  1 
ATOM   4010 C  C   . LYS A 1 511  ? 76.769 66.744  -20.730 1.00 15.37 ? 511  LYS A C   1 
ATOM   4011 O  O   . LYS A 1 511  ? 76.993 67.722  -20.035 1.00 17.07 ? 511  LYS A O   1 
ATOM   4012 C  CB  . LYS A 1 511  ? 77.366 67.563  -23.029 1.00 17.19 ? 511  LYS A CB  1 
ATOM   4013 C  CG  . LYS A 1 511  ? 78.516 66.608  -23.263 1.00 20.45 ? 511  LYS A CG  1 
ATOM   4014 C  CD  . LYS A 1 511  ? 79.665 67.127  -24.099 1.00 22.73 ? 511  LYS A CD  1 
ATOM   4015 C  CE  . LYS A 1 511  ? 80.797 66.068  -24.009 1.00 24.97 ? 511  LYS A CE  1 
ATOM   4016 N  NZ  . LYS A 1 511  ? 81.981 66.240  -24.908 1.00 28.46 ? 511  LYS A NZ  1 
ATOM   4017 N  N   . PRO A 1 512  ? 76.937 65.495  -20.270 1.00 16.71 ? 512  PRO A N   1 
ATOM   4018 C  CA  . PRO A 1 512  ? 77.393 65.240  -18.898 1.00 16.72 ? 512  PRO A CA  1 
ATOM   4019 C  C   . PRO A 1 512  ? 78.614 66.019  -18.389 1.00 17.15 ? 512  PRO A C   1 
ATOM   4020 O  O   . PRO A 1 512  ? 78.598 66.551  -17.267 1.00 17.40 ? 512  PRO A O   1 
ATOM   4021 C  CB  . PRO A 1 512  ? 77.602 63.724  -18.882 1.00 17.28 ? 512  PRO A CB  1 
ATOM   4022 C  CG  . PRO A 1 512  ? 76.548 63.234  -19.889 1.00 18.35 ? 512  PRO A CG  1 
ATOM   4023 C  CD  . PRO A 1 512  ? 76.688 64.235  -21.003 1.00 17.52 ? 512  PRO A CD  1 
ATOM   4024 N  N   . SER A 1 513  ? 79.660 66.105  -19.209 1.00 16.64 ? 513  SER A N   1 
ATOM   4025 C  CA  . SER A 1 513  ? 80.872 66.795  -18.788 1.00 16.38 ? 513  SER A CA  1 
ATOM   4026 C  C   . SER A 1 513  ? 80.765 68.303  -18.778 1.00 16.86 ? 513  SER A C   1 
ATOM   4027 O  O   . SER A 1 513  ? 81.708 68.986  -18.417 1.00 16.22 ? 513  SER A O   1 
ATOM   4028 C  CB  . SER A 1 513  ? 82.058 66.366  -19.665 1.00 15.99 ? 513  SER A CB  1 
ATOM   4029 O  OG  . SER A 1 513  ? 81.821 66.626  -21.034 1.00 16.61 ? 513  SER A OG  1 
ATOM   4030 N  N   . ILE A 1 514  ? 79.615 68.818  -19.177 1.00 17.17 ? 514  ILE A N   1 
ATOM   4031 C  CA  . ILE A 1 514  ? 79.367 70.252  -19.220 1.00 18.40 ? 514  ILE A CA  1 
ATOM   4032 C  C   . ILE A 1 514  ? 78.359 70.606  -18.109 1.00 18.77 ? 514  ILE A C   1 
ATOM   4033 O  O   . ILE A 1 514  ? 78.380 71.701  -17.552 1.00 18.80 ? 514  ILE A O   1 
ATOM   4034 C  CB  . ILE A 1 514  ? 78.806 70.646  -20.631 1.00 18.90 ? 514  ILE A CB  1 
ATOM   4035 C  CG1 . ILE A 1 514  ? 79.909 70.493  -21.675 1.00 19.34 ? 514  ILE A CG1 1 
ATOM   4036 C  CG2 . ILE A 1 514  ? 78.323 72.082  -20.650 1.00 20.98 ? 514  ILE A CG2 1 
ATOM   4037 C  CD1 . ILE A 1 514  ? 79.460 70.722  -23.112 1.00 20.07 ? 514  ILE A CD1 1 
ATOM   4038 N  N   . TYR A 1 515  ? 77.472 69.666  -17.794 1.00 18.95 ? 515  TYR A N   1 
ATOM   4039 C  CA  . TYR A 1 515  ? 76.455 69.856  -16.760 1.00 17.70 ? 515  TYR A CA  1 
ATOM   4040 C  C   . TYR A 1 515  ? 77.037 70.385  -15.429 1.00 18.04 ? 515  TYR A C   1 
ATOM   4041 O  O   . TYR A 1 515  ? 77.818 69.705  -14.758 1.00 17.94 ? 515  TYR A O   1 
ATOM   4042 C  CB  . TYR A 1 515  ? 75.753 68.519  -16.558 1.00 16.92 ? 515  TYR A CB  1 
ATOM   4043 C  CG  . TYR A 1 515  ? 74.751 68.507  -15.462 1.00 16.39 ? 515  TYR A CG  1 
ATOM   4044 C  CD1 . TYR A 1 515  ? 73.601 69.293  -15.526 1.00 15.86 ? 515  TYR A CD1 1 
ATOM   4045 C  CD2 . TYR A 1 515  ? 74.924 67.676  -14.360 1.00 15.68 ? 515  TYR A CD2 1 
ATOM   4046 C  CE1 . TYR A 1 515  ? 72.639 69.243  -14.505 1.00 15.88 ? 515  TYR A CE1 1 
ATOM   4047 C  CE2 . TYR A 1 515  ? 73.966 67.613  -13.338 1.00 15.70 ? 515  TYR A CE2 1 
ATOM   4048 C  CZ  . TYR A 1 515  ? 72.822 68.402  -13.419 1.00 16.55 ? 515  TYR A CZ  1 
ATOM   4049 O  OH  . TYR A 1 515  ? 71.870 68.342  -12.402 1.00 16.32 ? 515  TYR A OH  1 
ATOM   4050 N  N   . SER A 1 516  ? 76.646 71.595  -15.037 1.00 17.32 ? 516  SER A N   1 
ATOM   4051 C  CA  . SER A 1 516  ? 77.168 72.233  -13.810 1.00 17.13 ? 516  SER A CA  1 
ATOM   4052 C  C   . SER A 1 516  ? 75.988 72.873  -13.110 1.00 17.26 ? 516  SER A C   1 
ATOM   4053 O  O   . SER A 1 516  ? 75.775 74.093  -13.203 1.00 17.03 ? 516  SER A O   1 
ATOM   4054 C  CB  . SER A 1 516  ? 78.186 73.316  -14.200 1.00 16.91 ? 516  SER A CB  1 
ATOM   4055 O  OG  . SER A 1 516  ? 78.811 73.858  -13.046 1.00 18.28 ? 516  SER A OG  1 
ATOM   4056 N  N   . PRO A 1 517  ? 75.217 72.072  -12.366 1.00 17.54 ? 517  PRO A N   1 
ATOM   4057 C  CA  . PRO A 1 517  ? 74.042 72.607  -11.697 1.00 17.38 ? 517  PRO A CA  1 
ATOM   4058 C  C   . PRO A 1 517  ? 74.114 73.461  -10.444 1.00 18.14 ? 517  PRO A C   1 
ATOM   4059 O  O   . PRO A 1 517  ? 74.937 73.245  -9.562  1.00 18.88 ? 517  PRO A O   1 
ATOM   4060 C  CB  . PRO A 1 517  ? 73.201 71.350  -11.472 1.00 18.05 ? 517  PRO A CB  1 
ATOM   4061 C  CG  . PRO A 1 517  ? 74.247 70.355  -11.072 1.00 17.70 ? 517  PRO A CG  1 
ATOM   4062 C  CD  . PRO A 1 517  ? 75.330 70.621  -12.145 1.00 17.60 ? 517  PRO A CD  1 
ATOM   4063 N  N   . ASP A 1 518  ? 73.238 74.457  -10.422 1.00 19.01 ? 518  ASP A N   1 
ATOM   4064 C  CA  . ASP A 1 518  ? 73.010 75.324  -9.270  1.00 18.93 ? 518  ASP A CA  1 
ATOM   4065 C  C   . ASP A 1 518  ? 71.586 74.861  -8.915  1.00 18.65 ? 518  ASP A C   1 
ATOM   4066 O  O   . ASP A 1 518  ? 70.606 75.186  -9.609  1.00 18.75 ? 518  ASP A O   1 
ATOM   4067 C  CB  . ASP A 1 518  ? 72.979 76.802  -9.647  1.00 20.11 ? 518  ASP A CB  1 
ATOM   4068 C  CG  . ASP A 1 518  ? 72.571 77.670  -8.479  1.00 21.83 ? 518  ASP A CG  1 
ATOM   4069 O  OD1 . ASP A 1 518  ? 71.934 77.137  -7.543  1.00 22.53 ? 518  ASP A OD1 1 
ATOM   4070 O  OD2 . ASP A 1 518  ? 72.865 78.878  -8.492  1.00 24.19 ? 518  ASP A OD2 1 
ATOM   4071 N  N   . PHE A 1 519  ? 71.479 74.083  -7.851  1.00 17.90 ? 519  PHE A N   1 
ATOM   4072 C  CA  . PHE A 1 519  ? 70.202 73.524  -7.459  1.00 17.88 ? 519  PHE A CA  1 
ATOM   4073 C  C   . PHE A 1 519  ? 69.131 74.526  -7.082  1.00 18.28 ? 519  PHE A C   1 
ATOM   4074 O  O   . PHE A 1 519  ? 67.977 74.154  -6.908  1.00 18.28 ? 519  PHE A O   1 
ATOM   4075 C  CB  . PHE A 1 519  ? 70.417 72.492  -6.338  1.00 17.49 ? 519  PHE A CB  1 
ATOM   4076 C  CG  . PHE A 1 519  ? 71.261 71.311  -6.768  1.00 17.26 ? 519  PHE A CG  1 
ATOM   4077 C  CD1 . PHE A 1 519  ? 70.982 70.645  -7.958  1.00 17.26 ? 519  PHE A CD1 1 
ATOM   4078 C  CD2 . PHE A 1 519  ? 72.350 70.899  -6.009  1.00 18.19 ? 519  PHE A CD2 1 
ATOM   4079 C  CE1 . PHE A 1 519  ? 71.766 69.605  -8.390  1.00 17.33 ? 519  PHE A CE1 1 
ATOM   4080 C  CE2 . PHE A 1 519  ? 73.152 69.856  -6.422  1.00 17.13 ? 519  PHE A CE2 1 
ATOM   4081 C  CZ  . PHE A 1 519  ? 72.867 69.202  -7.617  1.00 19.37 ? 519  PHE A CZ  1 
ATOM   4082 N  N   . SER A 1 520  ? 69.480 75.802  -6.994  1.00 18.52 ? 520  SER A N   1 
ATOM   4083 C  CA  . SER A 1 520  ? 68.474 76.803  -6.642  1.00 19.41 ? 520  SER A CA  1 
ATOM   4084 C  C   . SER A 1 520  ? 68.139 77.650  -7.870  1.00 19.22 ? 520  SER A C   1 
ATOM   4085 O  O   . SER A 1 520  ? 67.288 78.534  -7.810  1.00 18.88 ? 520  SER A O   1 
ATOM   4086 C  CB  . SER A 1 520  ? 69.011 77.740  -5.555  1.00 19.03 ? 520  SER A CB  1 
ATOM   4087 O  OG  . SER A 1 520  ? 70.037 78.562  -6.108  1.00 19.65 ? 520  SER A OG  1 
ATOM   4088 N  N   . PHE A 1 521  ? 68.806 77.376  -8.983  1.00 19.49 ? 521  PHE A N   1 
ATOM   4089 C  CA  . PHE A 1 521  ? 68.608 78.161  -10.203 1.00 19.23 ? 521  PHE A CA  1 
ATOM   4090 C  C   . PHE A 1 521  ? 67.480 77.634  -11.095 1.00 19.22 ? 521  PHE A C   1 
ATOM   4091 O  O   . PHE A 1 521  ? 67.174 76.448  -11.075 1.00 19.40 ? 521  PHE A O   1 
ATOM   4092 C  CB  . PHE A 1 521  ? 69.934 78.209  -10.989 1.00 20.25 ? 521  PHE A CB  1 
ATOM   4093 C  CG  . PHE A 1 521  ? 69.933 79.197  -12.123 1.00 22.21 ? 521  PHE A CG  1 
ATOM   4094 C  CD1 . PHE A 1 521  ? 69.978 80.569  -11.868 1.00 23.29 ? 521  PHE A CD1 1 
ATOM   4095 C  CD2 . PHE A 1 521  ? 69.789 78.759  -13.444 1.00 22.39 ? 521  PHE A CD2 1 
ATOM   4096 C  CE1 . PHE A 1 521  ? 69.869 81.495  -12.910 1.00 24.08 ? 521  PHE A CE1 1 
ATOM   4097 C  CE2 . PHE A 1 521  ? 69.679 79.671  -14.498 1.00 23.71 ? 521  PHE A CE2 1 
ATOM   4098 C  CZ  . PHE A 1 521  ? 69.716 81.044  -14.233 1.00 24.32 ? 521  PHE A CZ  1 
ATOM   4099 N  N   . SER A 1 522  ? 66.851 78.525  -11.864 1.00 18.76 ? 522  SER A N   1 
ATOM   4100 C  CA  . SER A 1 522  ? 65.778 78.114  -12.764 1.00 19.01 ? 522  SER A CA  1 
ATOM   4101 C  C   . SER A 1 522  ? 66.285 78.070  -14.198 1.00 16.92 ? 522  SER A C   1 
ATOM   4102 O  O   . SER A 1 522  ? 66.315 79.095  -14.871 1.00 17.17 ? 522  SER A O   1 
ATOM   4103 C  CB  . SER A 1 522  ? 64.577 79.081  -12.688 1.00 20.10 ? 522  SER A CB  1 
ATOM   4104 O  OG  . SER A 1 522  ? 63.811 78.846  -11.524 1.00 26.11 ? 522  SER A OG  1 
ATOM   4105 N  N   . TYR A 1 523  ? 66.676 76.894  -14.660 1.00 15.32 ? 523  TYR A N   1 
ATOM   4106 C  CA  . TYR A 1 523  ? 67.153 76.729  -16.031 1.00 14.19 ? 523  TYR A CA  1 
ATOM   4107 C  C   . TYR A 1 523  ? 66.021 76.827  -17.042 1.00 14.30 ? 523  TYR A C   1 
ATOM   4108 O  O   . TYR A 1 523  ? 66.227 77.231  -18.186 1.00 14.16 ? 523  TYR A O   1 
ATOM   4109 C  CB  . TYR A 1 523  ? 67.857 75.370  -16.182 1.00 13.64 ? 523  TYR A CB  1 
ATOM   4110 C  CG  . TYR A 1 523  ? 69.141 75.331  -15.373 1.00 14.97 ? 523  TYR A CG  1 
ATOM   4111 C  CD1 . TYR A 1 523  ? 69.174 74.761  -14.102 1.00 13.89 ? 523  TYR A CD1 1 
ATOM   4112 C  CD2 . TYR A 1 523  ? 70.311 75.951  -15.863 1.00 15.08 ? 523  TYR A CD2 1 
ATOM   4113 C  CE1 . TYR A 1 523  ? 70.335 74.818  -13.334 1.00 14.92 ? 523  TYR A CE1 1 
ATOM   4114 C  CE2 . TYR A 1 523  ? 71.473 76.009  -15.109 1.00 14.68 ? 523  TYR A CE2 1 
ATOM   4115 C  CZ  . TYR A 1 523  ? 71.485 75.454  -13.854 1.00 14.58 ? 523  TYR A CZ  1 
ATOM   4116 O  OH  . TYR A 1 523  ? 72.624 75.561  -13.089 1.00 16.65 ? 523  TYR A OH  1 
ATOM   4117 N  N   . PHE A 1 524  ? 64.829 76.409  -16.627 1.00 13.34 ? 524  PHE A N   1 
ATOM   4118 C  CA  . PHE A 1 524  ? 63.654 76.478  -17.496 1.00 12.75 ? 524  PHE A CA  1 
ATOM   4119 C  C   . PHE A 1 524  ? 62.464 76.961  -16.694 1.00 13.79 ? 524  PHE A C   1 
ATOM   4120 O  O   . PHE A 1 524  ? 62.422 76.784  -15.472 1.00 13.39 ? 524  PHE A O   1 
ATOM   4121 C  CB  . PHE A 1 524  ? 63.253 75.101  -18.035 1.00 12.26 ? 524  PHE A CB  1 
ATOM   4122 C  CG  . PHE A 1 524  ? 64.283 74.454  -18.901 1.00 12.61 ? 524  PHE A CG  1 
ATOM   4123 C  CD1 . PHE A 1 524  ? 65.331 73.729  -18.336 1.00 12.07 ? 524  PHE A CD1 1 
ATOM   4124 C  CD2 . PHE A 1 524  ? 64.209 74.562  -20.290 1.00 11.08 ? 524  PHE A CD2 1 
ATOM   4125 C  CE1 . PHE A 1 524  ? 66.300 73.113  -19.168 1.00 12.42 ? 524  PHE A CE1 1 
ATOM   4126 C  CE2 . PHE A 1 524  ? 65.155 73.961  -21.114 1.00 11.74 ? 524  PHE A CE2 1 
ATOM   4127 C  CZ  . PHE A 1 524  ? 66.205 73.232  -20.553 1.00 12.70 ? 524  PHE A CZ  1 
ATOM   4128 N  N   . THR A 1 525  ? 61.502 77.571  -17.369 1.00 14.00 ? 525  THR A N   1 
ATOM   4129 C  CA  . THR A 1 525  ? 60.274 77.924  -16.697 1.00 16.42 ? 525  THR A CA  1 
ATOM   4130 C  C   . THR A 1 525  ? 59.221 77.113  -17.445 1.00 16.11 ? 525  THR A C   1 
ATOM   4131 O  O   . THR A 1 525  ? 59.281 76.958  -18.669 1.00 15.28 ? 525  THR A O   1 
ATOM   4132 C  CB  . THR A 1 525  ? 59.944 79.399  -16.814 1.00 17.11 ? 525  THR A CB  1 
ATOM   4133 O  OG1 . THR A 1 525  ? 59.637 79.685  -18.169 1.00 21.56 ? 525  THR A OG1 1 
ATOM   4134 C  CG2 . THR A 1 525  ? 61.129 80.242  -16.378 1.00 18.93 ? 525  THR A CG2 1 
ATOM   4135 N  N   . LEU A 1 526  ? 58.265 76.577  -16.704 1.00 15.82 ? 526  LEU A N   1 
ATOM   4136 C  CA  . LEU A 1 526  ? 57.215 75.763  -17.295 1.00 16.66 ? 526  LEU A CA  1 
ATOM   4137 C  C   . LEU A 1 526  ? 56.195 76.695  -17.998 1.00 16.27 ? 526  LEU A C   1 
ATOM   4138 O  O   . LEU A 1 526  ? 55.929 77.797  -17.517 1.00 15.58 ? 526  LEU A O   1 
ATOM   4139 C  CB  . LEU A 1 526  ? 56.550 74.971  -16.162 1.00 18.79 ? 526  LEU A CB  1 
ATOM   4140 C  CG  . LEU A 1 526  ? 56.255 73.468  -16.185 1.00 24.12 ? 526  LEU A CG  1 
ATOM   4141 C  CD1 . LEU A 1 526  ? 57.160 72.725  -17.104 1.00 22.91 ? 526  LEU A CD1 1 
ATOM   4142 C  CD2 . LEU A 1 526  ? 56.402 72.938  -14.773 1.00 24.78 ? 526  LEU A CD2 1 
ATOM   4143 N  N   . ASP A 1 527  ? 55.664 76.283  -19.145 1.00 13.85 ? 527  ASP A N   1 
ATOM   4144 C  CA  . ASP A 1 527  ? 54.658 77.100  -19.824 1.00 15.17 ? 527  ASP A CA  1 
ATOM   4145 C  C   . ASP A 1 527  ? 53.434 76.208  -19.907 1.00 15.04 ? 527  ASP A C   1 
ATOM   4146 O  O   . ASP A 1 527  ? 53.490 75.149  -20.519 1.00 16.07 ? 527  ASP A O   1 
ATOM   4147 C  CB  . ASP A 1 527  ? 55.126 77.508  -21.225 1.00 15.22 ? 527  ASP A CB  1 
ATOM   4148 C  CG  . ASP A 1 527  ? 54.087 78.363  -21.970 1.00 17.48 ? 527  ASP A CG  1 
ATOM   4149 O  OD1 . ASP A 1 527  ? 53.790 79.481  -21.504 1.00 15.37 ? 527  ASP A OD1 1 
ATOM   4150 O  OD2 . ASP A 1 527  ? 53.564 77.906  -23.020 1.00 15.85 ? 527  ASP A OD2 1 
ATOM   4151 N  N   . ASP A 1 528  ? 52.349 76.613  -19.251 1.00 14.23 ? 528  ASP A N   1 
ATOM   4152 C  CA  . ASP A 1 528  ? 51.111 75.828  -19.231 1.00 12.47 ? 528  ASP A CA  1 
ATOM   4153 C  C   . ASP A 1 528  ? 50.016 76.686  -19.834 1.00 12.51 ? 528  ASP A C   1 
ATOM   4154 O  O   . ASP A 1 528  ? 49.654 77.718  -19.273 1.00 11.20 ? 528  ASP A O   1 
ATOM   4155 C  CB  . ASP A 1 528  ? 50.750 75.438  -17.784 1.00 12.60 ? 528  ASP A CB  1 
ATOM   4156 C  CG  . ASP A 1 528  ? 49.665 74.353  -17.710 1.00 12.97 ? 528  ASP A CG  1 
ATOM   4157 O  OD1 . ASP A 1 528  ? 48.646 74.434  -18.421 1.00 11.19 ? 528  ASP A OD1 1 
ATOM   4158 O  OD2 . ASP A 1 528  ? 49.836 73.406  -16.928 1.00 12.17 ? 528  ASP A OD2 1 
ATOM   4159 N  N   . SER A 1 529  ? 49.487 76.250  -20.975 1.00 11.73 ? 529  SER A N   1 
ATOM   4160 C  CA  . SER A 1 529  ? 48.439 77.006  -21.682 1.00 13.98 ? 529  SER A CA  1 
ATOM   4161 C  C   . SER A 1 529  ? 47.077 76.929  -21.032 1.00 14.36 ? 529  SER A C   1 
ATOM   4162 O  O   . SER A 1 529  ? 46.221 77.752  -21.323 1.00 13.99 ? 529  SER A O   1 
ATOM   4163 C  CB  . SER A 1 529  ? 48.230 76.481  -23.109 1.00 13.49 ? 529  SER A CB  1 
ATOM   4164 O  OG  . SER A 1 529  ? 49.432 76.492  -23.831 1.00 16.92 ? 529  SER A OG  1 
ATOM   4165 N  N   . ARG A 1 530  ? 46.858 75.922  -20.184 1.00 13.67 ? 530  ARG A N   1 
ATOM   4166 C  CA  . ARG A 1 530  ? 45.526 75.766  -19.630 1.00 14.39 ? 530  ARG A CA  1 
ATOM   4167 C  C   . ARG A 1 530  ? 45.362 75.951  -18.132 1.00 15.75 ? 530  ARG A C   1 
ATOM   4168 O  O   . ARG A 1 530  ? 44.263 75.761  -17.601 1.00 16.70 ? 530  ARG A O   1 
ATOM   4169 C  CB  . ARG A 1 530  ? 44.972 74.420  -20.100 1.00 12.08 ? 530  ARG A CB  1 
ATOM   4170 C  CG  . ARG A 1 530  ? 44.933 74.363  -21.617 1.00 13.03 ? 530  ARG A CG  1 
ATOM   4171 C  CD  . ARG A 1 530  ? 44.263 73.099  -22.179 1.00 14.04 ? 530  ARG A CD  1 
ATOM   4172 N  NE  . ARG A 1 530  ? 45.023 71.897  -21.826 1.00 12.31 ? 530  ARG A NE  1 
ATOM   4173 C  CZ  . ARG A 1 530  ? 44.853 70.718  -22.410 1.00 14.52 ? 530  ARG A CZ  1 
ATOM   4174 N  NH1 . ARG A 1 530  ? 43.949 70.585  -23.390 1.00 13.13 ? 530  ARG A NH1 1 
ATOM   4175 N  NH2 . ARG A 1 530  ? 45.544 69.657  -21.988 1.00 11.79 ? 530  ARG A NH2 1 
ATOM   4176 N  N   . TRP A 1 531  ? 46.435 76.323  -17.442 1.00 14.25 ? 531  TRP A N   1 
ATOM   4177 C  CA  . TRP A 1 531  ? 46.308 76.573  -16.006 1.00 14.94 ? 531  TRP A CA  1 
ATOM   4178 C  C   . TRP A 1 531  ? 47.300 77.635  -15.556 1.00 14.97 ? 531  TRP A C   1 
ATOM   4179 O  O   . TRP A 1 531  ? 48.493 77.489  -15.782 1.00 16.05 ? 531  TRP A O   1 
ATOM   4180 C  CB  . TRP A 1 531  ? 46.529 75.303  -15.178 1.00 13.48 ? 531  TRP A CB  1 
ATOM   4181 C  CG  . TRP A 1 531  ? 46.407 75.612  -13.726 1.00 15.33 ? 531  TRP A CG  1 
ATOM   4182 C  CD1 . TRP A 1 531  ? 47.414 76.013  -12.870 1.00 16.31 ? 531  TRP A CD1 1 
ATOM   4183 C  CD2 . TRP A 1 531  ? 45.190 75.690  -12.971 1.00 16.02 ? 531  TRP A CD2 1 
ATOM   4184 N  NE1 . TRP A 1 531  ? 46.885 76.336  -11.634 1.00 16.22 ? 531  TRP A NE1 1 
ATOM   4185 C  CE2 . TRP A 1 531  ? 45.526 76.150  -11.673 1.00 17.40 ? 531  TRP A CE2 1 
ATOM   4186 C  CE3 . TRP A 1 531  ? 43.856 75.422  -13.266 1.00 18.11 ? 531  TRP A CE3 1 
ATOM   4187 C  CZ2 . TRP A 1 531  ? 44.567 76.341  -10.679 1.00 19.15 ? 531  TRP A CZ2 1 
ATOM   4188 C  CZ3 . TRP A 1 531  ? 42.884 75.616  -12.265 1.00 18.62 ? 531  TRP A CZ3 1 
ATOM   4189 C  CH2 . TRP A 1 531  ? 43.250 76.069  -10.996 1.00 20.44 ? 531  TRP A CH2 1 
ATOM   4190 N  N   . PRO A 1 532  ? 46.819 78.694  -14.878 1.00 15.64 ? 532  PRO A N   1 
ATOM   4191 C  CA  . PRO A 1 532  ? 45.412 78.928  -14.514 1.00 16.11 ? 532  PRO A CA  1 
ATOM   4192 C  C   . PRO A 1 532  ? 44.476 79.121  -15.707 1.00 16.97 ? 532  PRO A C   1 
ATOM   4193 O  O   . PRO A 1 532  ? 43.242 78.985  -15.579 1.00 16.44 ? 532  PRO A O   1 
ATOM   4194 C  CB  . PRO A 1 532  ? 45.484 80.172  -13.610 1.00 17.13 ? 532  PRO A CB  1 
ATOM   4195 C  CG  . PRO A 1 532  ? 46.849 80.003  -12.937 1.00 16.83 ? 532  PRO A CG  1 
ATOM   4196 C  CD  . PRO A 1 532  ? 47.702 79.647  -14.180 1.00 15.92 ? 532  PRO A CD  1 
ATOM   4197 N  N   . GLY A 1 533  ? 45.081 79.390  -16.861 1.00 17.24 ? 533  GLY A N   1 
ATOM   4198 C  CA  . GLY A 1 533  ? 44.344 79.559  -18.090 1.00 20.38 ? 533  GLY A CA  1 
ATOM   4199 C  C   . GLY A 1 533  ? 44.192 81.007  -18.468 1.00 23.77 ? 533  GLY A C   1 
ATOM   4200 O  O   . GLY A 1 533  ? 44.210 81.901  -17.606 1.00 23.04 ? 533  GLY A O   1 
ATOM   4201 N  N   . SER A 1 534  ? 44.052 81.237  -19.770 1.00 27.55 ? 534  SER A N   1 
ATOM   4202 C  CA  . SER A 1 534  ? 43.885 82.588  -20.328 1.00 30.99 ? 534  SER A CA  1 
ATOM   4203 C  C   . SER A 1 534  ? 42.594 83.199  -19.769 1.00 31.65 ? 534  SER A C   1 
ATOM   4204 O  O   . SER A 1 534  ? 41.525 82.582  -19.843 1.00 32.14 ? 534  SER A O   1 
ATOM   4205 C  CB  . SER A 1 534  ? 43.832 82.501  -21.872 1.00 32.51 ? 534  SER A CB  1 
ATOM   4206 O  OG  . SER A 1 534  ? 43.441 83.732  -22.460 1.00 36.46 ? 534  SER A OG  1 
ATOM   4207 N  N   . GLY A 1 535  ? 42.697 84.397  -19.199 1.00 32.92 ? 535  GLY A N   1 
ATOM   4208 C  CA  . GLY A 1 535  ? 41.526 85.039  -18.620 1.00 34.58 ? 535  GLY A CA  1 
ATOM   4209 C  C   . GLY A 1 535  ? 41.356 84.709  -17.138 1.00 35.68 ? 535  GLY A C   1 
ATOM   4210 O  O   . GLY A 1 535  ? 40.492 85.275  -16.452 1.00 35.86 ? 535  GLY A O   1 
ATOM   4211 N  N   . VAL A 1 536  ? 42.166 83.780  -16.630 1.00 36.02 ? 536  VAL A N   1 
ATOM   4212 C  CA  . VAL A 1 536  ? 42.084 83.413  -15.219 1.00 36.81 ? 536  VAL A CA  1 
ATOM   4213 C  C   . VAL A 1 536  ? 43.258 84.103  -14.521 1.00 38.28 ? 536  VAL A C   1 
ATOM   4214 O  O   . VAL A 1 536  ? 43.110 84.670  -13.439 1.00 37.43 ? 536  VAL A O   1 
ATOM   4215 C  CB  . VAL A 1 536  ? 42.165 81.861  -15.021 1.00 36.60 ? 536  VAL A CB  1 
ATOM   4216 C  CG1 . VAL A 1 536  ? 41.822 81.484  -13.591 1.00 35.48 ? 536  VAL A CG1 1 
ATOM   4217 C  CG2 . VAL A 1 536  ? 41.215 81.168  -15.971 1.00 35.83 ? 536  VAL A CG2 1 
ATOM   4218 N  N   . GLU A 1 537  ? 44.415 84.076  -15.179 1.00 39.84 ? 537  GLU A N   1 
ATOM   4219 C  CA  . GLU A 1 537  ? 45.622 84.689  -14.650 1.00 41.85 ? 537  GLU A CA  1 
ATOM   4220 C  C   . GLU A 1 537  ? 46.652 84.873  -15.769 1.00 42.16 ? 537  GLU A C   1 
ATOM   4221 O  O   . GLU A 1 537  ? 46.936 83.934  -16.525 1.00 42.39 ? 537  GLU A O   1 
ATOM   4222 C  CB  . GLU A 1 537  ? 46.172 83.807  -13.524 1.00 43.44 ? 537  GLU A CB  1 
ATOM   4223 C  CG  . GLU A 1 537  ? 47.595 84.110  -13.084 1.00 46.64 ? 537  GLU A CG  1 
ATOM   4224 C  CD  . GLU A 1 537  ? 47.987 83.358  -11.799 1.00 49.06 ? 537  GLU A CD  1 
ATOM   4225 O  OE1 . GLU A 1 537  ? 49.158 82.888  -11.712 1.00 50.01 ? 537  GLU A OE1 1 
ATOM   4226 O  OE2 . GLU A 1 537  ? 47.126 83.244  -10.879 1.00 49.61 ? 537  GLU A OE2 1 
ATOM   4227 N  N   . ASP A 1 538  ? 47.198 86.083  -15.907 1.00 42.38 ? 538  ASP A N   1 
ATOM   4228 C  CA  . ASP A 1 538  ? 48.206 86.301  -16.955 1.00 42.18 ? 538  ASP A CA  1 
ATOM   4229 C  C   . ASP A 1 538  ? 49.521 85.849  -16.327 1.00 40.46 ? 538  ASP A C   1 
ATOM   4230 O  O   . ASP A 1 538  ? 50.282 86.660  -15.798 1.00 40.63 ? 538  ASP A O   1 
ATOM   4231 C  CB  . ASP A 1 538  ? 48.275 87.783  -17.365 1.00 44.18 ? 538  ASP A CB  1 
ATOM   4232 C  CG  . ASP A 1 538  ? 48.869 87.975  -18.773 1.00 46.20 ? 538  ASP A CG  1 
ATOM   4233 O  OD1 . ASP A 1 538  ? 49.881 87.302  -19.077 1.00 48.04 ? 538  ASP A OD1 1 
ATOM   4234 O  OD2 . ASP A 1 538  ? 48.336 88.795  -19.568 1.00 46.65 ? 538  ASP A OD2 1 
ATOM   4235 N  N   . SER A 1 539  ? 49.787 84.547  -16.385 1.00 38.36 ? 539  SER A N   1 
ATOM   4236 C  CA  . SER A 1 539  ? 50.991 84.002  -15.747 1.00 35.87 ? 539  SER A CA  1 
ATOM   4237 C  C   . SER A 1 539  ? 52.056 83.476  -16.690 1.00 33.82 ? 539  SER A C   1 
ATOM   4238 O  O   . SER A 1 539  ? 53.177 83.180  -16.251 1.00 34.13 ? 539  SER A O   1 
ATOM   4239 C  CB  . SER A 1 539  ? 50.609 82.862  -14.793 1.00 35.22 ? 539  SER A CB  1 
ATOM   4240 O  OG  . SER A 1 539  ? 50.219 81.702  -15.526 1.00 35.67 ? 539  SER A OG  1 
ATOM   4241 N  N   . ARG A 1 540  ? 51.706 83.334  -17.965 1.00 31.30 ? 540  ARG A N   1 
ATOM   4242 C  CA  . ARG A 1 540  ? 52.640 82.805  -18.952 1.00 28.28 ? 540  ARG A CA  1 
ATOM   4243 C  C   . ARG A 1 540  ? 53.676 83.824  -19.362 1.00 27.42 ? 540  ARG A C   1 
ATOM   4244 O  O   . ARG A 1 540  ? 53.394 85.019  -19.488 1.00 26.49 ? 540  ARG A O   1 
ATOM   4245 C  CB  . ARG A 1 540  ? 51.882 82.320  -20.172 1.00 27.36 ? 540  ARG A CB  1 
ATOM   4246 C  CG  . ARG A 1 540  ? 50.909 81.199  -19.841 1.00 24.05 ? 540  ARG A CG  1 
ATOM   4247 C  CD  . ARG A 1 540  ? 50.164 80.774  -21.087 1.00 22.35 ? 540  ARG A CD  1 
ATOM   4248 N  NE  . ARG A 1 540  ? 51.059 80.163  -22.057 1.00 18.38 ? 540  ARG A NE  1 
ATOM   4249 C  CZ  . ARG A 1 540  ? 50.683 79.827  -23.285 1.00 19.10 ? 540  ARG A CZ  1 
ATOM   4250 N  NH1 . ARG A 1 540  ? 49.435 80.058  -23.679 1.00 15.94 ? 540  ARG A NH1 1 
ATOM   4251 N  NH2 . ARG A 1 540  ? 51.549 79.252  -24.114 1.00 18.77 ? 540  ARG A NH2 1 
ATOM   4252 N  N   . THR A 1 541  ? 54.891 83.352  -19.559 1.00 26.32 ? 541  THR A N   1 
ATOM   4253 C  CA  . THR A 1 541  ? 55.932 84.264  -19.945 1.00 26.28 ? 541  THR A CA  1 
ATOM   4254 C  C   . THR A 1 541  ? 56.006 84.313  -21.467 1.00 24.49 ? 541  THR A C   1 
ATOM   4255 O  O   . THR A 1 541  ? 55.789 83.324  -22.153 1.00 24.72 ? 541  THR A O   1 
ATOM   4256 C  CB  . THR A 1 541  ? 57.295 83.828  -19.384 1.00 28.58 ? 541  THR A CB  1 
ATOM   4257 O  OG1 . THR A 1 541  ? 57.887 82.888  -20.280 1.00 31.14 ? 541  THR A OG1 1 
ATOM   4258 C  CG2 . THR A 1 541  ? 57.136 83.168  -17.992 1.00 28.10 ? 541  THR A CG2 1 
ATOM   4259 N  N   . THR A 1 542  ? 56.285 85.492  -21.990 1.00 22.08 ? 542  THR A N   1 
ATOM   4260 C  CA  . THR A 1 542  ? 56.423 85.661  -23.411 1.00 19.10 ? 542  THR A CA  1 
ATOM   4261 C  C   . THR A 1 542  ? 57.873 85.419  -23.751 1.00 17.52 ? 542  THR A C   1 
ATOM   4262 O  O   . THR A 1 542  ? 58.752 85.912  -23.054 1.00 18.85 ? 542  THR A O   1 
ATOM   4263 C  CB  . THR A 1 542  ? 56.064 87.087  -23.808 1.00 18.77 ? 542  THR A CB  1 
ATOM   4264 O  OG1 . THR A 1 542  ? 54.676 87.295  -23.556 1.00 19.36 ? 542  THR A OG1 1 
ATOM   4265 C  CG2 . THR A 1 542  ? 56.357 87.328  -25.276 1.00 17.31 ? 542  THR A CG2 1 
ATOM   4266 N  N   . ILE A 1 543  ? 58.128 84.625  -24.785 1.00 15.49 ? 543  ILE A N   1 
ATOM   4267 C  CA  . ILE A 1 543  ? 59.500 84.401  -25.237 1.00 14.21 ? 543  ILE A CA  1 
ATOM   4268 C  C   . ILE A 1 543  ? 59.835 85.693  -26.015 1.00 14.64 ? 543  ILE A C   1 
ATOM   4269 O  O   . ILE A 1 543  ? 59.236 85.967  -27.063 1.00 13.70 ? 543  ILE A O   1 
ATOM   4270 C  CB  . ILE A 1 543  ? 59.589 83.197  -26.160 1.00 13.31 ? 543  ILE A CB  1 
ATOM   4271 C  CG1 . ILE A 1 543  ? 59.242 81.931  -25.345 1.00 12.40 ? 543  ILE A CG1 1 
ATOM   4272 C  CG2 . ILE A 1 543  ? 61.009 83.138  -26.819 1.00 10.85 ? 543  ILE A CG2 1 
ATOM   4273 C  CD1 . ILE A 1 543  ? 59.180 80.657  -26.146 1.00 11.04 ? 543  ILE A CD1 1 
ATOM   4274 N  N   . ILE A 1 544  ? 60.768 86.475  -25.475 1.00 14.11 ? 544  ILE A N   1 
ATOM   4275 C  CA  . ILE A 1 544  ? 61.145 87.759  -26.043 1.00 14.77 ? 544  ILE A CA  1 
ATOM   4276 C  C   . ILE A 1 544  ? 62.356 87.629  -26.931 1.00 15.52 ? 544  ILE A C   1 
ATOM   4277 O  O   . ILE A 1 544  ? 63.465 87.352  -26.470 1.00 13.75 ? 544  ILE A O   1 
ATOM   4278 C  CB  . ILE A 1 544  ? 61.380 88.782  -24.914 1.00 15.61 ? 544  ILE A CB  1 
ATOM   4279 C  CG1 . ILE A 1 544  ? 60.043 88.959  -24.170 1.00 16.55 ? 544  ILE A CG1 1 
ATOM   4280 C  CG2 . ILE A 1 544  ? 61.876 90.143  -25.479 1.00 14.92 ? 544  ILE A CG2 1 
ATOM   4281 C  CD1 . ILE A 1 544  ? 60.053 90.043  -23.122 1.00 19.35 ? 544  ILE A CD1 1 
ATOM   4282 N  N   . LEU A 1 545  ? 62.109 87.806  -28.224 1.00 14.75 ? 545  LEU A N   1 
ATOM   4283 C  CA  . LEU A 1 545  ? 63.139 87.697  -29.246 1.00 16.36 ? 545  LEU A CA  1 
ATOM   4284 C  C   . LEU A 1 545  ? 63.267 89.037  -29.970 1.00 17.80 ? 545  LEU A C   1 
ATOM   4285 O  O   . LEU A 1 545  ? 62.337 89.820  -29.983 1.00 18.07 ? 545  LEU A O   1 
ATOM   4286 C  CB  . LEU A 1 545  ? 62.760 86.584  -30.257 1.00 14.55 ? 545  LEU A CB  1 
ATOM   4287 C  CG  . LEU A 1 545  ? 62.536 85.154  -29.714 1.00 15.21 ? 545  LEU A CG  1 
ATOM   4288 C  CD1 . LEU A 1 545  ? 62.089 84.226  -30.848 1.00 11.44 ? 545  LEU A CD1 1 
ATOM   4289 C  CD2 . LEU A 1 545  ? 63.833 84.625  -29.077 1.00 13.02 ? 545  LEU A CD2 1 
ATOM   4290 N  N   . GLY A 1 546  ? 64.415 89.295  -30.579 1.00 18.22 ? 546  GLY A N   1 
ATOM   4291 C  CA  . GLY A 1 546  ? 64.574 90.552  -31.275 1.00 19.57 ? 546  GLY A CA  1 
ATOM   4292 C  C   . GLY A 1 546  ? 65.993 90.662  -31.781 1.00 20.05 ? 546  GLY A C   1 
ATOM   4293 O  O   . GLY A 1 546  ? 66.920 90.226  -31.121 1.00 18.77 ? 546  GLY A O   1 
ATOM   4294 N  N   . GLU A 1 547  ? 66.167 91.272  -32.942 1.00 22.40 ? 547  GLU A N   1 
ATOM   4295 C  CA  . GLU A 1 547  ? 67.507 91.430  -33.525 1.00 24.23 ? 547  GLU A CA  1 
ATOM   4296 C  C   . GLU A 1 547  ? 68.482 92.095  -32.545 1.00 23.30 ? 547  GLU A C   1 
ATOM   4297 O  O   . GLU A 1 547  ? 69.668 91.759  -32.499 1.00 23.36 ? 547  GLU A O   1 
ATOM   4298 C  CB  . GLU A 1 547  ? 67.427 92.268  -34.801 1.00 27.91 ? 547  GLU A CB  1 
ATOM   4299 C  CG  . GLU A 1 547  ? 68.745 92.304  -35.581 1.00 34.48 ? 547  GLU A CG  1 
ATOM   4300 C  CD  . GLU A 1 547  ? 68.736 93.323  -36.726 1.00 38.08 ? 547  GLU A CD  1 
ATOM   4301 O  OE1 . GLU A 1 547  ? 67.709 93.397  -37.456 1.00 39.41 ? 547  GLU A OE1 1 
ATOM   4302 O  OE2 . GLU A 1 547  ? 69.764 94.037  -36.899 1.00 39.97 ? 547  GLU A OE2 1 
ATOM   4303 N  N   . ASP A 1 548  ? 67.974 93.023  -31.743 1.00 21.85 ? 548  ASP A N   1 
ATOM   4304 C  CA  . ASP A 1 548  ? 68.814 93.734  -30.779 1.00 21.30 ? 548  ASP A CA  1 
ATOM   4305 C  C   . ASP A 1 548  ? 68.770 93.175  -29.363 1.00 20.80 ? 548  ASP A C   1 
ATOM   4306 O  O   . ASP A 1 548  ? 69.176 93.866  -28.419 1.00 21.58 ? 548  ASP A O   1 
ATOM   4307 C  CB  . ASP A 1 548  ? 68.421 95.211  -30.734 1.00 22.43 ? 548  ASP A CB  1 
ATOM   4308 C  CG  . ASP A 1 548  ? 68.658 95.901  -32.042 1.00 23.31 ? 548  ASP A CG  1 
ATOM   4309 O  OD1 . ASP A 1 548  ? 69.813 95.954  -32.479 1.00 25.62 ? 548  ASP A OD1 1 
ATOM   4310 O  OD2 . ASP A 1 548  ? 67.694 96.381  -32.644 1.00 25.02 ? 548  ASP A OD2 1 
ATOM   4311 N  N   . ILE A 1 549  ? 68.281 91.951  -29.192 1.00 18.42 ? 549  ILE A N   1 
ATOM   4312 C  CA  . ILE A 1 549  ? 68.240 91.381  -27.853 1.00 18.74 ? 549  ILE A CA  1 
ATOM   4313 C  C   . ILE A 1 549  ? 68.532 89.867  -27.803 1.00 18.09 ? 549  ILE A C   1 
ATOM   4314 O  O   . ILE A 1 549  ? 69.374 89.416  -27.018 1.00 16.49 ? 549  ILE A O   1 
ATOM   4315 C  CB  . ILE A 1 549  ? 66.871 91.686  -27.146 1.00 19.69 ? 549  ILE A CB  1 
ATOM   4316 C  CG1 . ILE A 1 549  ? 66.738 90.861  -25.861 1.00 22.92 ? 549  ILE A CG1 1 
ATOM   4317 C  CG2 . ILE A 1 549  ? 65.705 91.333  -28.027 1.00 19.95 ? 549  ILE A CG2 1 
ATOM   4318 C  CD1 . ILE A 1 549  ? 66.783 91.667  -24.571 1.00 25.04 ? 549  ILE A CD1 1 
ATOM   4319 N  N   . LEU A 1 550  ? 67.858 89.092  -28.646 1.00 15.84 ? 550  LEU A N   1 
ATOM   4320 C  CA  . LEU A 1 550  ? 68.024 87.641  -28.641 1.00 16.53 ? 550  LEU A CA  1 
ATOM   4321 C  C   . LEU A 1 550  ? 67.401 87.069  -29.901 1.00 15.91 ? 550  LEU A C   1 
ATOM   4322 O  O   . LEU A 1 550  ? 66.207 87.228  -30.152 1.00 17.52 ? 550  LEU A O   1 
ATOM   4323 C  CB  . LEU A 1 550  ? 67.320 87.053  -27.407 1.00 16.97 ? 550  LEU A CB  1 
ATOM   4324 C  CG  . LEU A 1 550  ? 67.421 85.546  -27.207 1.00 16.09 ? 550  LEU A CG  1 
ATOM   4325 C  CD1 . LEU A 1 550  ? 68.880 85.222  -26.909 1.00 16.07 ? 550  LEU A CD1 1 
ATOM   4326 C  CD2 . LEU A 1 550  ? 66.510 85.110  -26.067 1.00 14.75 ? 550  LEU A CD2 1 
ATOM   4327 N  N   . PRO A 1 551  ? 68.202 86.388  -30.721 1.00 16.46 ? 551  PRO A N   1 
ATOM   4328 C  CA  . PRO A 1 551  ? 67.616 85.841  -31.938 1.00 15.77 ? 551  PRO A CA  1 
ATOM   4329 C  C   . PRO A 1 551  ? 66.810 84.537  -31.850 1.00 15.73 ? 551  PRO A C   1 
ATOM   4330 O  O   . PRO A 1 551  ? 65.939 84.299  -32.703 1.00 15.96 ? 551  PRO A O   1 
ATOM   4331 C  CB  . PRO A 1 551  ? 68.818 85.723  -32.879 1.00 16.65 ? 551  PRO A CB  1 
ATOM   4332 C  CG  . PRO A 1 551  ? 69.959 85.508  -31.978 1.00 18.18 ? 551  PRO A CG  1 
ATOM   4333 C  CD  . PRO A 1 551  ? 69.678 86.301  -30.720 1.00 16.88 ? 551  PRO A CD  1 
ATOM   4334 N  N   . SER A 1 552  ? 67.063 83.705  -30.840 1.00 13.06 ? 552  SER A N   1 
ATOM   4335 C  CA  . SER A 1 552  ? 66.359 82.428  -30.783 1.00 12.73 ? 552  SER A CA  1 
ATOM   4336 C  C   . SER A 1 552  ? 66.248 81.927  -29.369 1.00 12.18 ? 552  SER A C   1 
ATOM   4337 O  O   . SER A 1 552  ? 66.929 82.409  -28.481 1.00 10.97 ? 552  SER A O   1 
ATOM   4338 C  CB  . SER A 1 552  ? 67.102 81.371  -31.596 1.00 12.29 ? 552  SER A CB  1 
ATOM   4339 O  OG  . SER A 1 552  ? 68.355 81.085  -30.988 1.00 13.75 ? 552  SER A OG  1 
ATOM   4340 N  N   . LYS A 1 553  ? 65.417 80.908  -29.189 1.00 12.79 ? 553  LYS A N   1 
ATOM   4341 C  CA  . LYS A 1 553  ? 65.165 80.350  -27.864 1.00 12.09 ? 553  LYS A CA  1 
ATOM   4342 C  C   . LYS A 1 553  ? 64.881 78.837  -27.933 1.00 12.42 ? 553  LYS A C   1 
ATOM   4343 O  O   . LYS A 1 553  ? 64.128 78.375  -28.788 1.00 10.86 ? 553  LYS A O   1 
ATOM   4344 C  CB  . LYS A 1 553  ? 63.957 81.082  -27.255 1.00 12.64 ? 553  LYS A CB  1 
ATOM   4345 C  CG  . LYS A 1 553  ? 63.407 80.434  -25.962 1.00 12.41 ? 553  LYS A CG  1 
ATOM   4346 C  CD  . LYS A 1 553  ? 64.415 80.540  -24.810 1.00 11.23 ? 553  LYS A CD  1 
ATOM   4347 C  CE  . LYS A 1 553  ? 64.671 82.020  -24.423 1.00 11.09 ? 553  LYS A CE  1 
ATOM   4348 N  NZ  . LYS A 1 553  ? 65.809 82.155  -23.468 1.00 8.44  ? 553  LYS A NZ  1 
ATOM   4349 N  N   . HIS A 1 554  ? 65.497 78.068  -27.042 1.00 12.62 ? 554  HIS A N   1 
ATOM   4350 C  CA  . HIS A 1 554  ? 65.248 76.619  -27.008 1.00 13.35 ? 554  HIS A CA  1 
ATOM   4351 C  C   . HIS A 1 554  ? 64.055 76.358  -26.111 1.00 12.54 ? 554  HIS A C   1 
ATOM   4352 O  O   . HIS A 1 554  ? 63.937 76.998  -25.078 1.00 12.52 ? 554  HIS A O   1 
ATOM   4353 C  CB  . HIS A 1 554  ? 66.423 75.876  -26.379 1.00 15.12 ? 554  HIS A CB  1 
ATOM   4354 C  CG  . HIS A 1 554  ? 67.588 75.656  -27.297 1.00 18.25 ? 554  HIS A CG  1 
ATOM   4355 N  ND1 . HIS A 1 554  ? 68.198 76.679  -27.987 1.00 20.68 ? 554  HIS A ND1 1 
ATOM   4356 C  CD2 . HIS A 1 554  ? 68.273 74.529  -27.609 1.00 19.84 ? 554  HIS A CD2 1 
ATOM   4357 C  CE1 . HIS A 1 554  ? 69.211 76.193  -28.687 1.00 21.61 ? 554  HIS A CE1 1 
ATOM   4358 N  NE2 . HIS A 1 554  ? 69.279 74.889  -28.473 1.00 21.19 ? 554  HIS A NE2 1 
ATOM   4359 N  N   . VAL A 1 555  ? 63.191 75.418  -26.496 1.00 10.95 ? 555  VAL A N   1 
ATOM   4360 C  CA  . VAL A 1 555  ? 62.034 75.015  -25.686 1.00 10.45 ? 555  VAL A CA  1 
ATOM   4361 C  C   . VAL A 1 555  ? 62.093 73.497  -25.661 1.00 11.03 ? 555  VAL A C   1 
ATOM   4362 O  O   . VAL A 1 555  ? 62.652 72.895  -26.578 1.00 11.75 ? 555  VAL A O   1 
ATOM   4363 C  CB  . VAL A 1 555  ? 60.689 75.447  -26.277 1.00 9.23  ? 555  VAL A CB  1 
ATOM   4364 C  CG1 . VAL A 1 555  ? 60.549 76.985  -26.202 1.00 9.10  ? 555  VAL A CG1 1 
ATOM   4365 C  CG2 . VAL A 1 555  ? 60.578 74.985  -27.679 1.00 8.44  ? 555  VAL A CG2 1 
ATOM   4366 N  N   . VAL A 1 556  ? 61.557 72.876  -24.613 1.00 9.24  ? 556  VAL A N   1 
ATOM   4367 C  CA  . VAL A 1 556  ? 61.610 71.424  -24.505 1.00 9.09  ? 556  VAL A CA  1 
ATOM   4368 C  C   . VAL A 1 556  ? 60.230 70.898  -24.066 1.00 9.23  ? 556  VAL A C   1 
ATOM   4369 O  O   . VAL A 1 556  ? 59.594 71.486  -23.204 1.00 8.11  ? 556  VAL A O   1 
ATOM   4370 C  CB  . VAL A 1 556  ? 62.677 70.986  -23.441 1.00 10.14 ? 556  VAL A CB  1 
ATOM   4371 C  CG1 . VAL A 1 556  ? 62.564 69.490  -23.151 1.00 8.66  ? 556  VAL A CG1 1 
ATOM   4372 C  CG2 . VAL A 1 556  ? 64.115 71.342  -23.922 1.00 7.45  ? 556  VAL A CG2 1 
ATOM   4373 N  N   . MET A 1 557  ? 59.782 69.813  -24.691 1.00 8.25  ? 557  MET A N   1 
ATOM   4374 C  CA  . MET A 1 557  ? 58.512 69.180  -24.330 1.00 8.88  ? 557  MET A CA  1 
ATOM   4375 C  C   . MET A 1 557  ? 58.789 67.844  -23.655 1.00 8.46  ? 557  MET A C   1 
ATOM   4376 O  O   . MET A 1 557  ? 59.692 67.110  -24.072 1.00 8.85  ? 557  MET A O   1 
ATOM   4377 C  CB  . MET A 1 557  ? 57.652 68.937  -25.579 1.00 8.93  ? 557  MET A CB  1 
ATOM   4378 C  CG  . MET A 1 557  ? 56.604 70.052  -25.918 1.00 6.97  ? 557  MET A CG  1 
ATOM   4379 S  SD  . MET A 1 557  ? 57.337 71.665  -26.050 1.00 9.35  ? 557  MET A SD  1 
ATOM   4380 C  CE  . MET A 1 557  ? 58.386 71.410  -27.554 1.00 7.41  ? 557  MET A CE  1 
ATOM   4381 N  N   . HIS A 1 558  ? 58.014 67.508  -22.627 1.00 8.35  ? 558  HIS A N   1 
ATOM   4382 C  CA  . HIS A 1 558  ? 58.162 66.208  -21.960 1.00 7.41  ? 558  HIS A CA  1 
ATOM   4383 C  C   . HIS A 1 558  ? 56.848 65.440  -22.191 1.00 8.23  ? 558  HIS A C   1 
ATOM   4384 O  O   . HIS A 1 558  ? 55.753 66.038  -22.176 1.00 7.95  ? 558  HIS A O   1 
ATOM   4385 C  CB  . HIS A 1 558  ? 58.362 66.402  -20.467 1.00 6.78  ? 558  HIS A CB  1 
ATOM   4386 C  CG  . HIS A 1 558  ? 58.215 65.137  -19.659 1.00 9.24  ? 558  HIS A CG  1 
ATOM   4387 N  ND1 . HIS A 1 558  ? 57.273 64.991  -18.660 1.00 8.09  ? 558  HIS A ND1 1 
ATOM   4388 C  CD2 . HIS A 1 558  ? 58.926 63.981  -19.677 1.00 8.80  ? 558  HIS A CD2 1 
ATOM   4389 C  CE1 . HIS A 1 558  ? 57.422 63.807  -18.093 1.00 9.38  ? 558  HIS A CE1 1 
ATOM   4390 N  NE2 . HIS A 1 558  ? 58.422 63.176  -18.690 1.00 10.01 ? 558  HIS A NE2 1 
ATOM   4391 N  N   . ASN A 1 559  ? 56.957 64.129  -22.414 1.00 6.87  ? 559  ASN A N   1 
ATOM   4392 C  CA  . ASN A 1 559  ? 55.798 63.276  -22.620 1.00 6.81  ? 559  ASN A CA  1 
ATOM   4393 C  C   . ASN A 1 559  ? 55.828 62.184  -21.538 1.00 7.01  ? 559  ASN A C   1 
ATOM   4394 O  O   . ASN A 1 559  ? 56.595 61.234  -21.648 1.00 6.92  ? 559  ASN A O   1 
ATOM   4395 C  CB  . ASN A 1 559  ? 55.858 62.656  -24.032 1.00 6.75  ? 559  ASN A CB  1 
ATOM   4396 C  CG  . ASN A 1 559  ? 54.852 61.502  -24.234 1.00 7.88  ? 559  ASN A CG  1 
ATOM   4397 O  OD1 . ASN A 1 559  ? 53.752 61.513  -23.685 1.00 9.02  ? 559  ASN A OD1 1 
ATOM   4398 N  ND2 . ASN A 1 559  ? 55.224 60.526  -25.059 1.00 6.16  ? 559  ASN A ND2 1 
ATOM   4399 N  N   . THR A 1 560  ? 54.982 62.308  -20.510 1.00 5.89  ? 560  THR A N   1 
ATOM   4400 C  CA  . THR A 1 560  ? 54.980 61.333  -19.420 1.00 7.83  ? 560  THR A CA  1 
ATOM   4401 C  C   . THR A 1 560  ? 54.375 59.963  -19.785 1.00 8.52  ? 560  THR A C   1 
ATOM   4402 O  O   . THR A 1 560  ? 54.561 58.966  -19.062 1.00 7.88  ? 560  THR A O   1 
ATOM   4403 C  CB  . THR A 1 560  ? 54.234 61.920  -18.202 1.00 7.43  ? 560  THR A CB  1 
ATOM   4404 O  OG1 . THR A 1 560  ? 54.579 61.178  -17.023 1.00 8.23  ? 560  THR A OG1 1 
ATOM   4405 C  CG2 . THR A 1 560  ? 52.711 61.891  -18.450 1.00 7.49  ? 560  THR A CG2 1 
ATOM   4406 N  N   . LEU A 1 561  ? 53.656 59.920  -20.907 1.00 7.67  ? 561  LEU A N   1 
ATOM   4407 C  CA  . LEU A 1 561  ? 53.009 58.676  -21.380 1.00 7.24  ? 561  LEU A CA  1 
ATOM   4408 C  C   . LEU A 1 561  ? 54.025 57.731  -22.024 1.00 7.12  ? 561  LEU A C   1 
ATOM   4409 O  O   . LEU A 1 561  ? 54.965 58.168  -22.713 1.00 7.40  ? 561  LEU A O   1 
ATOM   4410 C  CB  . LEU A 1 561  ? 51.889 59.002  -22.393 1.00 7.79  ? 561  LEU A CB  1 
ATOM   4411 C  CG  . LEU A 1 561  ? 50.756 59.902  -21.852 1.00 8.18  ? 561  LEU A CG  1 
ATOM   4412 C  CD1 . LEU A 1 561  ? 49.649 60.041  -22.907 1.00 6.85  ? 561  LEU A CD1 1 
ATOM   4413 C  CD2 . LEU A 1 561  ? 50.179 59.282  -20.535 1.00 8.39  ? 561  LEU A CD2 1 
ATOM   4414 N  N   . PRO A 1 562  ? 53.844 56.421  -21.828 1.00 7.47  ? 562  PRO A N   1 
ATOM   4415 C  CA  . PRO A 1 562  ? 54.814 55.486  -22.421 1.00 8.52  ? 562  PRO A CA  1 
ATOM   4416 C  C   . PRO A 1 562  ? 54.654 55.093  -23.879 1.00 10.35 ? 562  PRO A C   1 
ATOM   4417 O  O   . PRO A 1 562  ? 54.749 53.912  -24.229 1.00 11.53 ? 562  PRO A O   1 
ATOM   4418 C  CB  . PRO A 1 562  ? 54.752 54.286  -21.483 1.00 7.49  ? 562  PRO A CB  1 
ATOM   4419 C  CG  . PRO A 1 562  ? 53.286 54.274  -21.096 1.00 6.45  ? 562  PRO A CG  1 
ATOM   4420 C  CD  . PRO A 1 562  ? 52.932 55.734  -20.894 1.00 5.27  ? 562  PRO A CD  1 
ATOM   4421 N  N   . HIS A 1 563  ? 54.383 56.071  -24.734 1.00 10.69 ? 563  HIS A N   1 
ATOM   4422 C  CA  . HIS A 1 563  ? 54.319 55.820  -26.169 1.00 10.68 ? 563  HIS A CA  1 
ATOM   4423 C  C   . HIS A 1 563  ? 54.649 57.116  -26.875 1.00 11.80 ? 563  HIS A C   1 
ATOM   4424 O  O   . HIS A 1 563  ? 54.479 58.194  -26.302 1.00 12.74 ? 563  HIS A O   1 
ATOM   4425 C  CB  . HIS A 1 563  ? 52.949 55.269  -26.630 1.00 10.99 ? 563  HIS A CB  1 
ATOM   4426 C  CG  . HIS A 1 563  ? 51.771 56.115  -26.249 1.00 10.84 ? 563  HIS A CG  1 
ATOM   4427 N  ND1 . HIS A 1 563  ? 50.969 55.829  -25.158 1.00 9.56  ? 563  HIS A ND1 1 
ATOM   4428 C  CD2 . HIS A 1 563  ? 51.233 57.210  -26.839 1.00 10.71 ? 563  HIS A CD2 1 
ATOM   4429 C  CE1 . HIS A 1 563  ? 49.988 56.713  -25.097 1.00 9.56  ? 563  HIS A CE1 1 
ATOM   4430 N  NE2 . HIS A 1 563  ? 50.129 57.563  -26.105 1.00 11.52 ? 563  HIS A NE2 1 
ATOM   4431 N  N   . TRP A 1 564  ? 55.188 57.005  -28.089 1.00 11.91 ? 564  TRP A N   1 
ATOM   4432 C  CA  . TRP A 1 564  ? 55.508 58.175  -28.888 1.00 11.81 ? 564  TRP A CA  1 
ATOM   4433 C  C   . TRP A 1 564  ? 54.249 59.016  -28.963 1.00 12.01 ? 564  TRP A C   1 
ATOM   4434 O  O   . TRP A 1 564  ? 53.148 58.471  -29.083 1.00 12.02 ? 564  TRP A O   1 
ATOM   4435 C  CB  . TRP A 1 564  ? 55.921 57.750  -30.291 1.00 11.93 ? 564  TRP A CB  1 
ATOM   4436 C  CG  . TRP A 1 564  ? 57.342 57.341  -30.369 1.00 10.12 ? 564  TRP A CG  1 
ATOM   4437 C  CD1 . TRP A 1 564  ? 57.854 56.070  -30.240 1.00 11.99 ? 564  TRP A CD1 1 
ATOM   4438 C  CD2 . TRP A 1 564  ? 58.462 58.221  -30.528 1.00 11.04 ? 564  TRP A CD2 1 
ATOM   4439 N  NE1 . TRP A 1 564  ? 59.235 56.115  -30.307 1.00 13.38 ? 564  TRP A NE1 1 
ATOM   4440 C  CE2 . TRP A 1 564  ? 59.634 57.424  -30.482 1.00 10.71 ? 564  TRP A CE2 1 
ATOM   4441 C  CE3 . TRP A 1 564  ? 58.588 59.613  -30.705 1.00 11.48 ? 564  TRP A CE3 1 
ATOM   4442 C  CZ2 . TRP A 1 564  ? 60.916 57.966  -30.606 1.00 9.53  ? 564  TRP A CZ2 1 
ATOM   4443 C  CZ3 . TRP A 1 564  ? 59.885 60.161  -30.835 1.00 10.53 ? 564  TRP A CZ3 1 
ATOM   4444 C  CH2 . TRP A 1 564  ? 61.021 59.336  -30.785 1.00 11.00 ? 564  TRP A CH2 1 
ATOM   4445 N  N   . ARG A 1 565  ? 54.374 60.329  -28.845 1.00 11.35 ? 565  ARG A N   1 
ATOM   4446 C  CA  . ARG A 1 565  ? 53.161 61.135  -28.907 1.00 11.50 ? 565  ARG A CA  1 
ATOM   4447 C  C   . ARG A 1 565  ? 53.354 62.427  -29.659 1.00 11.36 ? 565  ARG A C   1 
ATOM   4448 O  O   . ARG A 1 565  ? 54.390 63.093  -29.519 1.00 12.36 ? 565  ARG A O   1 
ATOM   4449 C  CB  . ARG A 1 565  ? 52.635 61.458  -27.491 1.00 10.84 ? 565  ARG A CB  1 
ATOM   4450 C  CG  . ARG A 1 565  ? 51.442 62.402  -27.499 1.00 11.50 ? 565  ARG A CG  1 
ATOM   4451 C  CD  . ARG A 1 565  ? 50.553 62.277  -26.248 1.00 12.23 ? 565  ARG A CD  1 
ATOM   4452 N  NE  . ARG A 1 565  ? 51.287 62.591  -25.036 1.00 13.21 ? 565  ARG A NE  1 
ATOM   4453 C  CZ  . ARG A 1 565  ? 50.749 63.090  -23.932 1.00 13.62 ? 565  ARG A CZ  1 
ATOM   4454 N  NH1 . ARG A 1 565  ? 49.444 63.348  -23.881 1.00 13.52 ? 565  ARG A NH1 1 
ATOM   4455 N  NH2 . ARG A 1 565  ? 51.533 63.312  -22.871 1.00 11.82 ? 565  ARG A NH2 1 
ATOM   4456 N  N   . GLU A 1 566  ? 52.376 62.776  -30.487 1.00 11.32 ? 566  GLU A N   1 
ATOM   4457 C  CA  . GLU A 1 566  ? 52.435 64.058  -31.180 1.00 12.81 ? 566  GLU A CA  1 
ATOM   4458 C  C   . GLU A 1 566  ? 51.298 64.885  -30.588 1.00 13.67 ? 566  GLU A C   1 
ATOM   4459 O  O   . GLU A 1 566  ? 50.215 64.343  -30.294 1.00 12.76 ? 566  GLU A O   1 
ATOM   4460 C  CB  . GLU A 1 566  ? 52.216 63.924  -32.700 1.00 14.14 ? 566  GLU A CB  1 
ATOM   4461 C  CG  . GLU A 1 566  ? 53.358 63.251  -33.436 1.00 14.74 ? 566  GLU A CG  1 
ATOM   4462 C  CD  . GLU A 1 566  ? 53.132 63.250  -34.941 1.00 17.29 ? 566  GLU A CD  1 
ATOM   4463 O  OE1 . GLU A 1 566  ? 51.996 62.980  -35.391 1.00 16.97 ? 566  GLU A OE1 1 
ATOM   4464 O  OE2 . GLU A 1 566  ? 54.097 63.524  -35.673 1.00 19.03 ? 566  GLU A OE2 1 
ATOM   4465 N  N   . GLN A 1 567  ? 51.544 66.178  -30.393 1.00 12.59 ? 567  GLN A N   1 
ATOM   4466 C  CA  . GLN A 1 567  ? 50.524 67.082  -29.872 1.00 12.09 ? 567  GLN A CA  1 
ATOM   4467 C  C   . GLN A 1 567  ? 50.916 68.511  -30.245 1.00 11.89 ? 567  GLN A C   1 
ATOM   4468 O  O   . GLN A 1 567  ? 52.114 68.860  -30.246 1.00 10.10 ? 567  GLN A O   1 
ATOM   4469 C  CB  . GLN A 1 567  ? 50.437 66.959  -28.329 1.00 14.75 ? 567  GLN A CB  1 
ATOM   4470 C  CG  . GLN A 1 567  ? 49.342 67.837  -27.669 1.00 15.54 ? 567  GLN A CG  1 
ATOM   4471 C  CD  . GLN A 1 567  ? 49.683 68.244  -26.215 1.00 17.91 ? 567  GLN A CD  1 
ATOM   4472 O  OE1 . GLN A 1 567  ? 49.713 67.412  -25.307 1.00 16.29 ? 567  GLN A OE1 1 
ATOM   4473 N  NE2 . GLN A 1 567  ? 49.953 69.542  -26.008 1.00 18.53 ? 567  GLN A NE2 1 
ATOM   4474 N  N   . LEU A 1 568  ? 49.936 69.338  -30.590 1.00 10.71 ? 568  LEU A N   1 
ATOM   4475 C  CA  . LEU A 1 568  ? 50.263 70.730  -30.887 1.00 10.64 ? 568  LEU A CA  1 
ATOM   4476 C  C   . LEU A 1 568  ? 50.605 71.407  -29.563 1.00 10.48 ? 568  LEU A C   1 
ATOM   4477 O  O   . LEU A 1 568  ? 49.993 71.126  -28.537 1.00 10.24 ? 568  LEU A O   1 
ATOM   4478 C  CB  . LEU A 1 568  ? 49.068 71.459  -31.553 1.00 12.13 ? 568  LEU A CB  1 
ATOM   4479 C  CG  . LEU A 1 568  ? 48.634 71.006  -32.975 1.00 13.85 ? 568  LEU A CG  1 
ATOM   4480 C  CD1 . LEU A 1 568  ? 47.621 71.993  -33.564 1.00 13.11 ? 568  LEU A CD1 1 
ATOM   4481 C  CD2 . LEU A 1 568  ? 49.867 70.986  -33.884 1.00 12.97 ? 568  LEU A CD2 1 
ATOM   4482 N  N   . VAL A 1 569  ? 51.612 72.268  -29.575 1.00 10.75 ? 569  VAL A N   1 
ATOM   4483 C  CA  . VAL A 1 569  ? 51.991 73.021  -28.393 1.00 10.96 ? 569  VAL A CA  1 
ATOM   4484 C  C   . VAL A 1 569  ? 52.054 74.492  -28.806 1.00 10.81 ? 569  VAL A C   1 
ATOM   4485 O  O   . VAL A 1 569  ? 52.310 74.801  -29.957 1.00 11.36 ? 569  VAL A O   1 
ATOM   4486 C  CB  . VAL A 1 569  ? 53.367 72.569  -27.836 1.00 10.21 ? 569  VAL A CB  1 
ATOM   4487 C  CG1 . VAL A 1 569  ? 53.238 71.147  -27.265 1.00 10.41 ? 569  VAL A CG1 1 
ATOM   4488 C  CG2 . VAL A 1 569  ? 54.455 72.628  -28.937 1.00 11.39 ? 569  VAL A CG2 1 
ATOM   4489 N  N   . ASP A 1 570  ? 51.760 75.399  -27.888 1.00 12.50 ? 570  ASP A N   1 
ATOM   4490 C  CA  . ASP A 1 570  ? 51.831 76.811  -28.238 1.00 13.38 ? 570  ASP A CA  1 
ATOM   4491 C  C   . ASP A 1 570  ? 52.658 77.582  -27.225 1.00 11.89 ? 570  ASP A C   1 
ATOM   4492 O  O   . ASP A 1 570  ? 52.815 77.163  -26.060 1.00 11.71 ? 570  ASP A O   1 
ATOM   4493 C  CB  . ASP A 1 570  ? 50.413 77.397  -28.406 1.00 16.63 ? 570  ASP A CB  1 
ATOM   4494 C  CG  . ASP A 1 570  ? 49.628 77.495  -27.088 1.00 20.19 ? 570  ASP A CG  1 
ATOM   4495 O  OD1 . ASP A 1 570  ? 49.560 76.517  -26.354 1.00 25.75 ? 570  ASP A OD1 1 
ATOM   4496 O  OD2 . ASP A 1 570  ? 49.067 78.557  -26.787 1.00 24.23 ? 570  ASP A OD2 1 
ATOM   4497 N  N   . PHE A 1 571  ? 53.247 78.678  -27.679 1.00 9.83  ? 571  PHE A N   1 
ATOM   4498 C  CA  . PHE A 1 571  ? 54.039 79.526  -26.806 1.00 11.43 ? 571  PHE A CA  1 
ATOM   4499 C  C   . PHE A 1 571  ? 53.744 80.966  -27.203 1.00 11.82 ? 571  PHE A C   1 
ATOM   4500 O  O   . PHE A 1 571  ? 53.392 81.226  -28.358 1.00 11.57 ? 571  PHE A O   1 
ATOM   4501 C  CB  . PHE A 1 571  ? 55.554 79.323  -27.030 1.00 10.38 ? 571  PHE A CB  1 
ATOM   4502 C  CG  . PHE A 1 571  ? 56.051 77.971  -26.651 1.00 9.56  ? 571  PHE A CG  1 
ATOM   4503 C  CD1 . PHE A 1 571  ? 55.957 76.902  -27.536 1.00 9.12  ? 571  PHE A CD1 1 
ATOM   4504 C  CD2 . PHE A 1 571  ? 56.565 77.751  -25.387 1.00 9.19  ? 571  PHE A CD2 1 
ATOM   4505 C  CE1 . PHE A 1 571  ? 56.371 75.609  -27.147 1.00 8.30  ? 571  PHE A CE1 1 
ATOM   4506 C  CE2 . PHE A 1 571  ? 56.978 76.466  -24.997 1.00 9.80  ? 571  PHE A CE2 1 
ATOM   4507 C  CZ  . PHE A 1 571  ? 56.873 75.405  -25.891 1.00 7.74  ? 571  PHE A CZ  1 
ATOM   4508 N  N   . TYR A 1 572  ? 53.909 81.886  -26.265 1.00 12.07 ? 572  TYR A N   1 
ATOM   4509 C  CA  . TYR A 1 572  ? 53.755 83.299  -26.581 1.00 13.37 ? 572  TYR A CA  1 
ATOM   4510 C  C   . TYR A 1 572  ? 55.127 83.785  -27.025 1.00 13.24 ? 572  TYR A C   1 
ATOM   4511 O  O   . TYR A 1 572  ? 56.137 83.442  -26.394 1.00 13.03 ? 572  TYR A O   1 
ATOM   4512 C  CB  . TYR A 1 572  ? 53.340 84.114  -25.351 1.00 14.63 ? 572  TYR A CB  1 
ATOM   4513 C  CG  . TYR A 1 572  ? 51.907 83.951  -24.904 1.00 16.53 ? 572  TYR A CG  1 
ATOM   4514 C  CD1 . TYR A 1 572  ? 50.989 83.263  -25.677 1.00 16.72 ? 572  TYR A CD1 1 
ATOM   4515 C  CD2 . TYR A 1 572  ? 51.469 84.510  -23.696 1.00 19.70 ? 572  TYR A CD2 1 
ATOM   4516 C  CE1 . TYR A 1 572  ? 49.672 83.124  -25.292 1.00 17.72 ? 572  TYR A CE1 1 
ATOM   4517 C  CE2 . TYR A 1 572  ? 50.134 84.377  -23.282 1.00 20.94 ? 572  TYR A CE2 1 
ATOM   4518 C  CZ  . TYR A 1 572  ? 49.239 83.681  -24.101 1.00 19.47 ? 572  TYR A CZ  1 
ATOM   4519 O  OH  . TYR A 1 572  ? 47.914 83.563  -23.746 1.00 19.80 ? 572  TYR A OH  1 
ATOM   4520 N  N   . VAL A 1 573  ? 55.165 84.577  -28.100 1.00 13.10 ? 573  VAL A N   1 
ATOM   4521 C  CA  . VAL A 1 573  ? 56.415 85.155  -28.616 1.00 12.17 ? 573  VAL A CA  1 
ATOM   4522 C  C   . VAL A 1 573  ? 56.185 86.662  -28.868 1.00 13.19 ? 573  VAL A C   1 
ATOM   4523 O  O   . VAL A 1 573  ? 55.053 87.089  -29.098 1.00 12.77 ? 573  VAL A O   1 
ATOM   4524 C  CB  . VAL A 1 573  ? 56.904 84.482  -29.942 1.00 13.07 ? 573  VAL A CB  1 
ATOM   4525 C  CG1 . VAL A 1 573  ? 57.435 83.079  -29.666 1.00 12.45 ? 573  VAL A CG1 1 
ATOM   4526 C  CG2 . VAL A 1 573  ? 55.791 84.439  -30.966 1.00 12.10 ? 573  VAL A CG2 1 
ATOM   4527 N  N   . SER A 1 574  ? 57.254 87.459  -28.829 1.00 13.51 ? 574  SER A N   1 
ATOM   4528 C  CA  . SER A 1 574  ? 57.134 88.909  -28.989 1.00 13.87 ? 574  SER A CA  1 
ATOM   4529 C  C   . SER A 1 574  ? 57.096 89.402  -30.439 1.00 15.50 ? 574  SER A C   1 
ATOM   4530 O  O   . SER A 1 574  ? 57.121 90.606  -30.699 1.00 15.34 ? 574  SER A O   1 
ATOM   4531 C  CB  . SER A 1 574  ? 58.273 89.599  -28.217 1.00 13.30 ? 574  SER A CB  1 
ATOM   4532 O  OG  . SER A 1 574  ? 59.526 89.237  -28.758 1.00 14.12 ? 574  SER A OG  1 
ATOM   4533 N  N   . SER A 1 575  ? 57.022 88.470  -31.383 1.00 15.51 ? 575  SER A N   1 
ATOM   4534 C  CA  . SER A 1 575  ? 56.977 88.821  -32.794 1.00 16.35 ? 575  SER A CA  1 
ATOM   4535 C  C   . SER A 1 575  ? 56.295 87.709  -33.538 1.00 16.59 ? 575  SER A C   1 
ATOM   4536 O  O   . SER A 1 575  ? 56.439 86.529  -33.187 1.00 17.54 ? 575  SER A O   1 
ATOM   4537 C  CB  . SER A 1 575  ? 58.392 88.977  -33.369 1.00 16.25 ? 575  SER A CB  1 
ATOM   4538 O  OG  . SER A 1 575  ? 58.409 88.796  -34.785 1.00 15.75 ? 575  SER A OG  1 
ATOM   4539 N  N   . PRO A 1 576  ? 55.546 88.058  -34.582 1.00 17.23 ? 576  PRO A N   1 
ATOM   4540 C  CA  . PRO A 1 576  ? 54.849 87.035  -35.378 1.00 16.12 ? 576  PRO A CA  1 
ATOM   4541 C  C   . PRO A 1 576  ? 55.805 86.371  -36.375 1.00 16.20 ? 576  PRO A C   1 
ATOM   4542 O  O   . PRO A 1 576  ? 55.482 85.347  -36.971 1.00 16.78 ? 576  PRO A O   1 
ATOM   4543 C  CB  . PRO A 1 576  ? 53.759 87.843  -36.089 1.00 17.73 ? 576  PRO A CB  1 
ATOM   4544 C  CG  . PRO A 1 576  ? 54.514 89.183  -36.385 1.00 18.49 ? 576  PRO A CG  1 
ATOM   4545 C  CD  . PRO A 1 576  ? 55.239 89.431  -35.049 1.00 16.83 ? 576  PRO A CD  1 
ATOM   4546 N  N   . PHE A 1 577  ? 56.989 86.943  -36.567 1.00 16.05 ? 577  PHE A N   1 
ATOM   4547 C  CA  . PHE A 1 577  ? 57.928 86.383  -37.544 1.00 16.80 ? 577  PHE A CA  1 
ATOM   4548 C  C   . PHE A 1 577  ? 58.891 85.414  -36.859 1.00 16.15 ? 577  PHE A C   1 
ATOM   4549 O  O   . PHE A 1 577  ? 60.070 85.725  -36.632 1.00 14.32 ? 577  PHE A O   1 
ATOM   4550 C  CB  . PHE A 1 577  ? 58.686 87.515  -38.226 1.00 17.43 ? 577  PHE A CB  1 
ATOM   4551 C  CG  . PHE A 1 577  ? 57.786 88.521  -38.883 1.00 19.03 ? 577  PHE A CG  1 
ATOM   4552 C  CD1 . PHE A 1 577  ? 57.963 89.893  -38.650 1.00 20.70 ? 577  PHE A CD1 1 
ATOM   4553 C  CD2 . PHE A 1 577  ? 56.775 88.107  -39.744 1.00 19.10 ? 577  PHE A CD2 1 
ATOM   4554 C  CE1 . PHE A 1 577  ? 57.133 90.836  -39.278 1.00 21.38 ? 577  PHE A CE1 1 
ATOM   4555 C  CE2 . PHE A 1 577  ? 55.943 89.024  -40.379 1.00 20.64 ? 577  PHE A CE2 1 
ATOM   4556 C  CZ  . PHE A 1 577  ? 56.120 90.399  -40.149 1.00 21.74 ? 577  PHE A CZ  1 
ATOM   4557 N  N   . VAL A 1 578  ? 58.374 84.219  -36.581 1.00 14.43 ? 578  VAL A N   1 
ATOM   4558 C  CA  . VAL A 1 578  ? 59.131 83.207  -35.850 1.00 14.44 ? 578  VAL A CA  1 
ATOM   4559 C  C   . VAL A 1 578  ? 58.993 81.879  -36.532 1.00 13.92 ? 578  VAL A C   1 
ATOM   4560 O  O   . VAL A 1 578  ? 57.913 81.520  -36.991 1.00 14.03 ? 578  VAL A O   1 
ATOM   4561 C  CB  . VAL A 1 578  ? 58.597 83.090  -34.374 1.00 13.31 ? 578  VAL A CB  1 
ATOM   4562 C  CG1 . VAL A 1 578  ? 59.309 81.949  -33.591 1.00 13.64 ? 578  VAL A CG1 1 
ATOM   4563 C  CG2 . VAL A 1 578  ? 58.811 84.410  -33.656 1.00 13.40 ? 578  VAL A CG2 1 
ATOM   4564 N  N   . SER A 1 579  ? 60.092 81.156  -36.629 1.00 13.77 ? 579  SER A N   1 
ATOM   4565 C  CA  . SER A 1 579  ? 60.022 79.851  -37.238 1.00 15.83 ? 579  SER A CA  1 
ATOM   4566 C  C   . SER A 1 579  ? 60.549 78.828  -36.236 1.00 14.78 ? 579  SER A C   1 
ATOM   4567 O  O   . SER A 1 579  ? 61.292 79.145  -35.312 1.00 17.15 ? 579  SER A O   1 
ATOM   4568 C  CB  . SER A 1 579  ? 60.794 79.827  -38.568 1.00 16.92 ? 579  SER A CB  1 
ATOM   4569 O  OG  . SER A 1 579  ? 62.059 80.423  -38.395 1.00 20.36 ? 579  SER A OG  1 
ATOM   4570 N  N   . VAL A 1 580  ? 60.173 77.592  -36.444 1.00 13.80 ? 580  VAL A N   1 
ATOM   4571 C  CA  . VAL A 1 580  ? 60.534 76.533  -35.549 1.00 12.81 ? 580  VAL A CA  1 
ATOM   4572 C  C   . VAL A 1 580  ? 61.358 75.481  -36.284 1.00 13.66 ? 580  VAL A C   1 
ATOM   4573 O  O   . VAL A 1 580  ? 61.124 75.201  -37.449 1.00 13.59 ? 580  VAL A O   1 
ATOM   4574 C  CB  . VAL A 1 580  ? 59.234 75.866  -35.009 1.00 13.44 ? 580  VAL A CB  1 
ATOM   4575 C  CG1 . VAL A 1 580  ? 59.566 74.744  -34.023 1.00 11.32 ? 580  VAL A CG1 1 
ATOM   4576 C  CG2 . VAL A 1 580  ? 58.336 76.922  -34.380 1.00 11.05 ? 580  VAL A CG2 1 
ATOM   4577 N  N   . THR A 1 581  ? 62.320 74.913  -35.585 1.00 13.64 ? 581  THR A N   1 
ATOM   4578 C  CA  . THR A 1 581  ? 63.154 73.848  -36.110 1.00 15.34 ? 581  THR A CA  1 
ATOM   4579 C  C   . THR A 1 581  ? 63.390 72.874  -34.954 1.00 15.61 ? 581  THR A C   1 
ATOM   4580 O  O   . THR A 1 581  ? 63.228 73.254  -33.785 1.00 14.31 ? 581  THR A O   1 
ATOM   4581 C  CB  . THR A 1 581  ? 64.547 74.359  -36.542 1.00 16.16 ? 581  THR A CB  1 
ATOM   4582 O  OG1 . THR A 1 581  ? 65.065 75.218  -35.525 1.00 16.35 ? 581  THR A OG1 1 
ATOM   4583 C  CG2 . THR A 1 581  ? 64.483 75.111  -37.891 1.00 16.05 ? 581  THR A CG2 1 
ATOM   4584 N  N   . ASP A 1 582  ? 63.768 71.636  -35.277 1.00 16.00 ? 582  ASP A N   1 
ATOM   4585 C  CA  . ASP A 1 582  ? 64.113 70.668  -34.245 1.00 17.86 ? 582  ASP A CA  1 
ATOM   4586 C  C   . ASP A 1 582  ? 65.620 70.779  -34.015 1.00 19.31 ? 582  ASP A C   1 
ATOM   4587 O  O   . ASP A 1 582  ? 66.253 71.647  -34.604 1.00 18.44 ? 582  ASP A O   1 
ATOM   4588 C  CB  . ASP A 1 582  ? 63.697 69.243  -34.625 1.00 18.02 ? 582  ASP A CB  1 
ATOM   4589 C  CG  . ASP A 1 582  ? 64.370 68.705  -35.888 1.00 17.40 ? 582  ASP A CG  1 
ATOM   4590 O  OD1 . ASP A 1 582  ? 63.818 67.697  -36.399 1.00 18.09 ? 582  ASP A OD1 1 
ATOM   4591 O  OD2 . ASP A 1 582  ? 65.418 69.233  -36.353 1.00 14.94 ? 582  ASP A OD2 1 
ATOM   4592 N  N   . LEU A 1 583  ? 66.234 69.935  -33.187 1.00 22.48 ? 583  LEU A N   1 
ATOM   4593 C  CA  . LEU A 1 583  ? 67.671 70.182  -32.989 1.00 24.37 ? 583  LEU A CA  1 
ATOM   4594 C  C   . LEU A 1 583  ? 68.584 69.717  -34.120 1.00 24.29 ? 583  LEU A C   1 
ATOM   4595 O  O   . LEU A 1 583  ? 69.777 70.036  -34.106 1.00 25.40 ? 583  LEU A O   1 
ATOM   4596 C  CB  . LEU A 1 583  ? 68.183 69.655  -31.624 1.00 26.66 ? 583  LEU A CB  1 
ATOM   4597 C  CG  . LEU A 1 583  ? 69.105 70.679  -30.932 1.00 26.41 ? 583  LEU A CG  1 
ATOM   4598 C  CD1 . LEU A 1 583  ? 68.340 71.974  -30.681 1.00 26.66 ? 583  LEU A CD1 1 
ATOM   4599 C  CD2 . LEU A 1 583  ? 69.624 70.150  -29.631 1.00 28.91 ? 583  LEU A CD2 1 
ATOM   4600 N  N   . ALA A 1 584  ? 68.036 68.991  -35.101 1.00 23.50 ? 584  ALA A N   1 
ATOM   4601 C  CA  . ALA A 1 584  ? 68.821 68.581  -36.275 1.00 21.78 ? 584  ALA A CA  1 
ATOM   4602 C  C   . ALA A 1 584  ? 68.650 69.717  -37.286 1.00 21.40 ? 584  ALA A C   1 
ATOM   4603 O  O   . ALA A 1 584  ? 69.100 69.657  -38.444 1.00 20.22 ? 584  ALA A O   1 
ATOM   4604 C  CB  . ALA A 1 584  ? 68.278 67.292  -36.860 1.00 21.64 ? 584  ALA A CB  1 
ATOM   4605 N  N   . ASN A 1 585  ? 67.954 70.750  -36.839 1.00 21.20 ? 585  ASN A N   1 
ATOM   4606 C  CA  . ASN A 1 585  ? 67.693 71.918  -37.652 1.00 21.54 ? 585  ASN A CA  1 
ATOM   4607 C  C   . ASN A 1 585  ? 66.703 71.712  -38.794 1.00 21.15 ? 585  ASN A C   1 
ATOM   4608 O  O   . ASN A 1 585  ? 66.720 72.463  -39.760 1.00 20.80 ? 585  ASN A O   1 
ATOM   4609 C  CB  . ASN A 1 585  ? 68.998 72.471  -38.206 1.00 25.66 ? 585  ASN A CB  1 
ATOM   4610 C  CG  . ASN A 1 585  ? 69.253 73.867  -37.743 1.00 28.81 ? 585  ASN A CG  1 
ATOM   4611 O  OD1 . ASN A 1 585  ? 68.472 74.772  -38.028 1.00 29.59 ? 585  ASN A OD1 1 
ATOM   4612 N  ND2 . ASN A 1 585  ? 70.336 74.056  -37.001 1.00 32.14 ? 585  ASN A ND2 1 
ATOM   4613 N  N   . ASN A 1 586  ? 65.863 70.690  -38.703 1.00 18.79 ? 586  ASN A N   1 
ATOM   4614 C  CA  . ASN A 1 586  ? 64.859 70.478  -39.713 1.00 19.55 ? 586  ASN A CA  1 
ATOM   4615 C  C   . ASN A 1 586  ? 63.720 71.458  -39.398 1.00 19.54 ? 586  ASN A C   1 
ATOM   4616 O  O   . ASN A 1 586  ? 63.357 71.657  -38.224 1.00 17.62 ? 586  ASN A O   1 
ATOM   4617 C  CB  . ASN A 1 586  ? 64.280 69.074  -39.638 1.00 20.49 ? 586  ASN A CB  1 
ATOM   4618 C  CG  . ASN A 1 586  ? 65.329 67.991  -39.770 1.00 22.72 ? 586  ASN A CG  1 
ATOM   4619 O  OD1 . ASN A 1 586  ? 66.232 68.079  -40.605 1.00 22.27 ? 586  ASN A OD1 1 
ATOM   4620 N  ND2 . ASN A 1 586  ? 65.210 66.949  -38.940 1.00 24.02 ? 586  ASN A ND2 1 
ATOM   4621 N  N   . PRO A 1 587  ? 63.150 72.091  -40.435 1.00 18.85 ? 587  PRO A N   1 
ATOM   4622 C  CA  . PRO A 1 587  ? 62.053 73.020  -40.161 1.00 17.69 ? 587  PRO A CA  1 
ATOM   4623 C  C   . PRO A 1 587  ? 60.808 72.298  -39.698 1.00 17.21 ? 587  PRO A C   1 
ATOM   4624 O  O   . PRO A 1 587  ? 60.574 71.139  -40.061 1.00 17.23 ? 587  PRO A O   1 
ATOM   4625 C  CB  . PRO A 1 587  ? 61.849 73.749  -41.493 1.00 19.78 ? 587  PRO A CB  1 
ATOM   4626 C  CG  . PRO A 1 587  ? 62.505 72.867  -42.526 1.00 20.61 ? 587  PRO A CG  1 
ATOM   4627 C  CD  . PRO A 1 587  ? 63.697 72.293  -41.794 1.00 20.89 ? 587  PRO A CD  1 
ATOM   4628 N  N   . VAL A 1 588  ? 60.026 72.964  -38.859 1.00 15.52 ? 588  VAL A N   1 
ATOM   4629 C  CA  . VAL A 1 588  ? 58.782 72.391  -38.361 1.00 15.30 ? 588  VAL A CA  1 
ATOM   4630 C  C   . VAL A 1 588  ? 57.662 73.363  -38.765 1.00 14.83 ? 588  VAL A C   1 
ATOM   4631 O  O   . VAL A 1 588  ? 57.761 74.563  -38.500 1.00 13.53 ? 588  VAL A O   1 
ATOM   4632 C  CB  . VAL A 1 588  ? 58.809 72.243  -36.816 1.00 15.86 ? 588  VAL A CB  1 
ATOM   4633 C  CG1 . VAL A 1 588  ? 57.486 71.732  -36.334 1.00 15.36 ? 588  VAL A CG1 1 
ATOM   4634 C  CG2 . VAL A 1 588  ? 59.924 71.267  -36.397 1.00 15.02 ? 588  VAL A CG2 1 
ATOM   4635 N  N   . GLU A 1 589  ? 56.625 72.856  -39.430 1.00 14.98 ? 589  GLU A N   1 
ATOM   4636 C  CA  . GLU A 1 589  ? 55.505 73.691  -39.852 1.00 15.90 ? 589  GLU A CA  1 
ATOM   4637 C  C   . GLU A 1 589  ? 54.861 74.334  -38.605 1.00 15.27 ? 589  GLU A C   1 
ATOM   4638 O  O   . GLU A 1 589  ? 54.531 73.631  -37.644 1.00 13.03 ? 589  GLU A O   1 
ATOM   4639 C  CB  . GLU A 1 589  ? 54.458 72.858  -40.590 1.00 17.76 ? 589  GLU A CB  1 
ATOM   4640 C  CG  . GLU A 1 589  ? 53.645 73.666  -41.592 1.00 25.60 ? 589  GLU A CG  1 
ATOM   4641 C  CD  . GLU A 1 589  ? 52.294 73.033  -41.918 1.00 29.49 ? 589  GLU A CD  1 
ATOM   4642 O  OE1 . GLU A 1 589  ? 52.229 71.778  -41.971 1.00 33.87 ? 589  GLU A OE1 1 
ATOM   4643 O  OE2 . GLU A 1 589  ? 51.298 73.783  -42.118 1.00 31.46 ? 589  GLU A OE2 1 
ATOM   4644 N  N   . ALA A 1 590  ? 54.671 75.648  -38.628 1.00 12.69 ? 590  ALA A N   1 
ATOM   4645 C  CA  . ALA A 1 590  ? 54.113 76.335  -37.472 1.00 13.35 ? 590  ALA A CA  1 
ATOM   4646 C  C   . ALA A 1 590  ? 53.026 77.278  -37.921 1.00 13.92 ? 590  ALA A C   1 
ATOM   4647 O  O   . ALA A 1 590  ? 52.964 77.649  -39.107 1.00 12.66 ? 590  ALA A O   1 
ATOM   4648 C  CB  . ALA A 1 590  ? 55.217 77.124  -36.757 1.00 13.54 ? 590  ALA A CB  1 
ATOM   4649 N  N   . GLN A 1 591  ? 52.158 77.648  -36.984 1.00 14.01 ? 591  GLN A N   1 
ATOM   4650 C  CA  . GLN A 1 591  ? 51.077 78.602  -37.251 1.00 13.95 ? 591  GLN A CA  1 
ATOM   4651 C  C   . GLN A 1 591  ? 51.136 79.688  -36.179 1.00 14.35 ? 591  GLN A C   1 
ATOM   4652 O  O   . GLN A 1 591  ? 51.347 79.392  -34.986 1.00 15.15 ? 591  GLN A O   1 
ATOM   4653 C  CB  . GLN A 1 591  ? 49.700 77.919  -37.190 1.00 14.12 ? 591  GLN A CB  1 
ATOM   4654 C  CG  . GLN A 1 591  ? 48.504 78.888  -37.247 1.00 13.73 ? 591  GLN A CG  1 
ATOM   4655 C  CD  . GLN A 1 591  ? 47.157 78.172  -37.021 1.00 13.77 ? 591  GLN A CD  1 
ATOM   4656 O  OE1 . GLN A 1 591  ? 46.922 77.080  -37.550 1.00 14.77 ? 591  GLN A OE1 1 
ATOM   4657 N  NE2 . GLN A 1 591  ? 46.276 78.790  -36.252 1.00 11.17 ? 591  GLN A NE2 1 
ATOM   4658 N  N   . VAL A 1 592  ? 50.953 80.936  -36.586 1.00 12.80 ? 592  VAL A N   1 
ATOM   4659 C  CA  . VAL A 1 592  ? 50.930 82.030  -35.628 1.00 12.69 ? 592  VAL A CA  1 
ATOM   4660 C  C   . VAL A 1 592  ? 49.511 82.578  -35.599 1.00 11.82 ? 592  VAL A C   1 
ATOM   4661 O  O   . VAL A 1 592  ? 48.867 82.701  -36.628 1.00 13.17 ? 592  VAL A O   1 
ATOM   4662 C  CB  . VAL A 1 592  ? 51.983 83.146  -35.978 1.00 12.95 ? 592  VAL A CB  1 
ATOM   4663 C  CG1 . VAL A 1 592  ? 51.733 84.430  -35.140 1.00 11.28 ? 592  VAL A CG1 1 
ATOM   4664 C  CG2 . VAL A 1 592  ? 53.371 82.628  -35.638 1.00 11.95 ? 592  VAL A CG2 1 
ATOM   4665 N  N   . SER A 1 593  ? 49.026 82.866  -34.405 1.00 12.92 ? 593  SER A N   1 
ATOM   4666 C  CA  . SER A 1 593  ? 47.687 83.403  -34.166 1.00 13.96 ? 593  SER A CA  1 
ATOM   4667 C  C   . SER A 1 593  ? 47.839 84.541  -33.175 1.00 14.60 ? 593  SER A C   1 
ATOM   4668 O  O   . SER A 1 593  ? 48.853 84.633  -32.465 1.00 15.82 ? 593  SER A O   1 
ATOM   4669 C  CB  . SER A 1 593  ? 46.763 82.323  -33.535 1.00 13.91 ? 593  SER A CB  1 
ATOM   4670 O  OG  . SER A 1 593  ? 46.569 81.186  -34.389 1.00 15.56 ? 593  SER A OG  1 
ATOM   4671 N  N   . PRO A 1 594  ? 46.840 85.434  -33.100 1.00 15.55 ? 594  PRO A N   1 
ATOM   4672 C  CA  . PRO A 1 594  ? 46.936 86.545  -32.141 1.00 14.68 ? 594  PRO A CA  1 
ATOM   4673 C  C   . PRO A 1 594  ? 46.692 86.027  -30.721 1.00 15.65 ? 594  PRO A C   1 
ATOM   4674 O  O   . PRO A 1 594  ? 46.311 84.857  -30.536 1.00 15.10 ? 594  PRO A O   1 
ATOM   4675 C  CB  . PRO A 1 594  ? 45.812 87.495  -32.566 1.00 13.57 ? 594  PRO A CB  1 
ATOM   4676 C  CG  . PRO A 1 594  ? 45.452 87.070  -33.988 1.00 13.90 ? 594  PRO A CG  1 
ATOM   4677 C  CD  . PRO A 1 594  ? 45.651 85.565  -33.964 1.00 15.01 ? 594  PRO A CD  1 
ATOM   4678 N  N   . VAL A 1 595  ? 46.936 86.888  -29.728 1.00 13.86 ? 595  VAL A N   1 
ATOM   4679 C  CA  . VAL A 1 595  ? 46.654 86.554  -28.336 1.00 14.23 ? 595  VAL A CA  1 
ATOM   4680 C  C   . VAL A 1 595  ? 45.370 87.367  -28.096 1.00 13.83 ? 595  VAL A C   1 
ATOM   4681 O  O   . VAL A 1 595  ? 45.384 88.605  -28.126 1.00 13.97 ? 595  VAL A O   1 
ATOM   4682 C  CB  . VAL A 1 595  ? 47.734 87.063  -27.350 1.00 13.17 ? 595  VAL A CB  1 
ATOM   4683 C  CG1 . VAL A 1 595  ? 47.263 86.814  -25.872 1.00 12.83 ? 595  VAL A CG1 1 
ATOM   4684 C  CG2 . VAL A 1 595  ? 49.022 86.338  -27.585 1.00 15.93 ? 595  VAL A CG2 1 
ATOM   4685 N  N   . TRP A 1 596  ? 44.268 86.658  -27.881 1.00 14.74 ? 596  TRP A N   1 
ATOM   4686 C  CA  . TRP A 1 596  ? 42.963 87.270  -27.678 1.00 15.82 ? 596  TRP A CA  1 
ATOM   4687 C  C   . TRP A 1 596  ? 42.550 87.168  -26.212 1.00 16.62 ? 596  TRP A C   1 
ATOM   4688 O  O   . TRP A 1 596  ? 42.645 86.087  -25.632 1.00 15.32 ? 596  TRP A O   1 
ATOM   4689 C  CB  . TRP A 1 596  ? 41.875 86.549  -28.513 1.00 14.43 ? 596  TRP A CB  1 
ATOM   4690 C  CG  . TRP A 1 596  ? 41.986 86.713  -30.016 1.00 13.88 ? 596  TRP A CG  1 
ATOM   4691 C  CD1 . TRP A 1 596  ? 42.400 85.769  -30.933 1.00 13.54 ? 596  TRP A CD1 1 
ATOM   4692 C  CD2 . TRP A 1 596  ? 41.705 87.899  -30.761 1.00 13.38 ? 596  TRP A CD2 1 
ATOM   4693 N  NE1 . TRP A 1 596  ? 42.390 86.310  -32.206 1.00 14.27 ? 596  TRP A NE1 1 
ATOM   4694 C  CE2 . TRP A 1 596  ? 41.973 87.613  -32.128 1.00 12.86 ? 596  TRP A CE2 1 
ATOM   4695 C  CE3 . TRP A 1 596  ? 41.251 89.187  -30.406 1.00 12.84 ? 596  TRP A CE3 1 
ATOM   4696 C  CZ2 . TRP A 1 596  ? 41.801 88.565  -33.138 1.00 14.26 ? 596  TRP A CZ2 1 
ATOM   4697 C  CZ3 . TRP A 1 596  ? 41.080 90.134  -31.413 1.00 13.40 ? 596  TRP A CZ3 1 
ATOM   4698 C  CH2 . TRP A 1 596  ? 41.354 89.816  -32.762 1.00 13.89 ? 596  TRP A CH2 1 
ATOM   4699 N  N   . SER A 1 597  ? 42.120 88.284  -25.622 1.00 16.65 ? 597  SER A N   1 
ATOM   4700 C  CA  . SER A 1 597  ? 41.614 88.250  -24.250 1.00 18.43 ? 597  SER A CA  1 
ATOM   4701 C  C   . SER A 1 597  ? 40.214 88.859  -24.231 1.00 18.25 ? 597  SER A C   1 
ATOM   4702 O  O   . SER A 1 597  ? 39.959 89.873  -24.880 1.00 18.54 ? 597  SER A O   1 
ATOM   4703 C  CB  . SER A 1 597  ? 42.541 88.979  -23.276 1.00 19.66 ? 597  SER A CB  1 
ATOM   4704 O  OG  . SER A 1 597  ? 43.021 90.170  -23.821 1.00 24.04 ? 597  SER A OG  1 
ATOM   4705 N  N   . TRP A 1 598  ? 39.306 88.232  -23.499 1.00 17.37 ? 598  TRP A N   1 
ATOM   4706 C  CA  . TRP A 1 598  ? 37.931 88.702  -23.443 1.00 18.45 ? 598  TRP A CA  1 
ATOM   4707 C  C   . TRP A 1 598  ? 37.667 89.636  -22.286 1.00 20.50 ? 598  TRP A C   1 
ATOM   4708 O  O   . TRP A 1 598  ? 38.074 89.379  -21.165 1.00 20.82 ? 598  TRP A O   1 
ATOM   4709 C  CB  . TRP A 1 598  ? 36.969 87.509  -23.404 1.00 16.49 ? 598  TRP A CB  1 
ATOM   4710 C  CG  . TRP A 1 598  ? 36.959 86.743  -24.708 1.00 14.25 ? 598  TRP A CG  1 
ATOM   4711 C  CD1 . TRP A 1 598  ? 37.898 85.856  -25.151 1.00 14.32 ? 598  TRP A CD1 1 
ATOM   4712 C  CD2 . TRP A 1 598  ? 35.953 86.799  -25.712 1.00 13.47 ? 598  TRP A CD2 1 
ATOM   4713 N  NE1 . TRP A 1 598  ? 37.527 85.341  -26.383 1.00 12.41 ? 598  TRP A NE1 1 
ATOM   4714 C  CE2 . TRP A 1 598  ? 36.335 85.904  -26.745 1.00 12.77 ? 598  TRP A CE2 1 
ATOM   4715 C  CE3 . TRP A 1 598  ? 34.756 87.519  -25.845 1.00 13.37 ? 598  TRP A CE3 1 
ATOM   4716 C  CZ2 . TRP A 1 598  ? 35.570 85.710  -27.879 1.00 12.54 ? 598  TRP A CZ2 1 
ATOM   4717 C  CZ3 . TRP A 1 598  ? 33.995 87.324  -26.981 1.00 13.35 ? 598  TRP A CZ3 1 
ATOM   4718 C  CH2 . TRP A 1 598  ? 34.407 86.424  -27.986 1.00 11.24 ? 598  TRP A CH2 1 
ATOM   4719 N  N   . HIS A 1 599  ? 36.980 90.730  -22.559 1.00 23.12 ? 599  HIS A N   1 
ATOM   4720 C  CA  . HIS A 1 599  ? 36.726 91.704  -21.511 1.00 26.82 ? 599  HIS A CA  1 
ATOM   4721 C  C   . HIS A 1 599  ? 35.263 92.008  -21.336 1.00 27.76 ? 599  HIS A C   1 
ATOM   4722 O  O   . HIS A 1 599  ? 34.551 92.138  -22.324 1.00 27.13 ? 599  HIS A O   1 
ATOM   4723 C  CB  . HIS A 1 599  ? 37.462 93.011  -21.852 1.00 29.84 ? 599  HIS A CB  1 
ATOM   4724 C  CG  . HIS A 1 599  ? 38.950 92.847  -21.937 1.00 32.98 ? 599  HIS A CG  1 
ATOM   4725 N  ND1 . HIS A 1 599  ? 39.692 92.297  -20.913 1.00 34.42 ? 599  HIS A ND1 1 
ATOM   4726 C  CD2 . HIS A 1 599  ? 39.819 93.056  -22.957 1.00 34.65 ? 599  HIS A CD2 1 
ATOM   4727 C  CE1 . HIS A 1 599  ? 40.948 92.161  -21.301 1.00 34.88 ? 599  HIS A CE1 1 
ATOM   4728 N  NE2 . HIS A 1 599  ? 41.053 92.613  -22.538 1.00 35.73 ? 599  HIS A NE2 1 
ATOM   4729 N  N   . HIS A 1 600  ? 34.788 92.086  -20.098 1.00 29.69 ? 600  HIS A N   1 
ATOM   4730 C  CA  . HIS A 1 600  ? 33.393 92.486  -19.946 1.00 32.01 ? 600  HIS A CA  1 
ATOM   4731 C  C   . HIS A 1 600  ? 33.484 93.994  -19.923 1.00 30.48 ? 600  HIS A C   1 
ATOM   4732 O  O   . HIS A 1 600  ? 33.901 94.575  -18.932 1.00 30.74 ? 600  HIS A O   1 
ATOM   4733 C  CB  . HIS A 1 600  ? 32.726 92.044  -18.649 1.00 35.84 ? 600  HIS A CB  1 
ATOM   4734 C  CG  . HIS A 1 600  ? 31.357 92.646  -18.484 1.00 40.90 ? 600  HIS A CG  1 
ATOM   4735 N  ND1 . HIS A 1 600  ? 30.250 92.170  -19.159 1.00 43.15 ? 600  HIS A ND1 1 
ATOM   4736 C  CD2 . HIS A 1 600  ? 30.950 93.782  -17.860 1.00 42.82 ? 600  HIS A CD2 1 
ATOM   4737 C  CE1 . HIS A 1 600  ? 29.226 92.987  -18.967 1.00 43.92 ? 600  HIS A CE1 1 
ATOM   4738 N  NE2 . HIS A 1 600  ? 29.625 93.975  -18.183 1.00 44.27 ? 600  HIS A NE2 1 
ATOM   4739 N  N   . ASP A 1 601  ? 33.116 94.618  -21.028 1.00 30.01 ? 601  ASP A N   1 
ATOM   4740 C  CA  . ASP A 1 601  ? 33.174 96.061  -21.159 1.00 30.39 ? 601  ASP A CA  1 
ATOM   4741 C  C   . ASP A 1 601  ? 32.041 96.707  -20.332 1.00 30.37 ? 601  ASP A C   1 
ATOM   4742 O  O   . ASP A 1 601  ? 30.894 96.699  -20.755 1.00 29.50 ? 601  ASP A O   1 
ATOM   4743 C  CB  . ASP A 1 601  ? 33.015 96.395  -22.632 1.00 31.58 ? 601  ASP A CB  1 
ATOM   4744 C  CG  . ASP A 1 601  ? 33.443 97.802  -22.972 1.00 32.45 ? 601  ASP A CG  1 
ATOM   4745 O  OD1 . ASP A 1 601  ? 33.045 98.766  -22.279 1.00 32.60 ? 601  ASP A OD1 1 
ATOM   4746 O  OD2 . ASP A 1 601  ? 34.172 97.939  -23.972 1.00 33.62 ? 601  ASP A OD2 1 
ATOM   4747 N  N   . THR A 1 602  ? 32.364 97.262  -19.165 1.00 31.04 ? 602  THR A N   1 
ATOM   4748 C  CA  . THR A 1 602  ? 31.342 97.889  -18.321 1.00 32.61 ? 602  THR A CA  1 
ATOM   4749 C  C   . THR A 1 602  ? 30.739 99.133  -18.938 1.00 32.37 ? 602  THR A C   1 
ATOM   4750 O  O   . THR A 1 602  ? 29.680 99.585  -18.497 1.00 33.89 ? 602  THR A O   1 
ATOM   4751 C  CB  . THR A 1 602  ? 31.866 98.280  -16.939 1.00 34.27 ? 602  THR A CB  1 
ATOM   4752 O  OG1 . THR A 1 602  ? 33.030 99.122  -17.081 1.00 35.79 ? 602  THR A OG1 1 
ATOM   4753 C  CG2 . THR A 1 602  ? 32.166 97.027  -16.120 1.00 34.69 ? 602  THR A CG2 1 
ATOM   4754 N  N   . LEU A 1 603  ? 31.396 99.675  -19.957 1.00 31.10 ? 603  LEU A N   1 
ATOM   4755 C  CA  . LEU A 1 603  ? 30.884 100.847 -20.641 1.00 30.07 ? 603  LEU A CA  1 
ATOM   4756 C  C   . LEU A 1 603  ? 29.864 100.480 -21.735 1.00 29.05 ? 603  LEU A C   1 
ATOM   4757 O  O   . LEU A 1 603  ? 28.716 100.918 -21.670 1.00 28.48 ? 603  LEU A O   1 
ATOM   4758 C  CB  . LEU A 1 603  ? 32.036 101.661 -21.238 1.00 32.05 ? 603  LEU A CB  1 
ATOM   4759 C  CG  . LEU A 1 603  ? 32.952 102.366 -20.217 1.00 33.49 ? 603  LEU A CG  1 
ATOM   4760 C  CD1 . LEU A 1 603  ? 32.132 103.353 -19.380 1.00 33.56 ? 603  LEU A CD1 1 
ATOM   4761 C  CD2 . LEU A 1 603  ? 33.604 101.322 -19.299 1.00 34.85 ? 603  LEU A CD2 1 
ATOM   4762 N  N   . THR A 1 604  ? 30.270 99.684  -22.728 1.00 26.54 ? 604  THR A N   1 
ATOM   4763 C  CA  . THR A 1 604  ? 29.353 99.279  -23.802 1.00 24.17 ? 604  THR A CA  1 
ATOM   4764 C  C   . THR A 1 604  ? 28.440 98.148  -23.347 1.00 22.02 ? 604  THR A C   1 
ATOM   4765 O  O   . THR A 1 604  ? 27.523 97.766  -24.069 1.00 21.61 ? 604  THR A O   1 
ATOM   4766 C  CB  . THR A 1 604  ? 30.108 98.751  -25.032 1.00 24.91 ? 604  THR A CB  1 
ATOM   4767 O  OG1 . THR A 1 604  ? 30.928 97.630  -24.630 1.00 25.42 ? 604  THR A OG1 1 
ATOM   4768 C  CG2 . THR A 1 604  ? 30.989 99.869  -25.656 1.00 24.24 ? 604  THR A CG2 1 
ATOM   4769 N  N   . LYS A 1 605  ? 28.700 97.607  -22.164 1.00 21.16 ? 605  LYS A N   1 
ATOM   4770 C  CA  . LYS A 1 605  ? 27.915 96.493  -21.631 1.00 20.76 ? 605  LYS A CA  1 
ATOM   4771 C  C   . LYS A 1 605  ? 27.911 95.304  -22.586 1.00 20.88 ? 605  LYS A C   1 
ATOM   4772 O  O   . LYS A 1 605  ? 26.857 94.753  -22.853 1.00 20.89 ? 605  LYS A O   1 
ATOM   4773 C  CB  . LYS A 1 605  ? 26.443 96.901  -21.377 1.00 21.33 ? 605  LYS A CB  1 
ATOM   4774 C  CG  . LYS A 1 605  ? 26.275 97.994  -20.342 1.00 21.61 ? 605  LYS A CG  1 
ATOM   4775 C  CD  . LYS A 1 605  ? 26.743 97.528  -18.941 1.00 24.58 ? 605  LYS A CD  1 
ATOM   4776 C  CE  . LYS A 1 605  ? 26.709 98.721  -17.965 1.00 24.15 ? 605  LYS A CE  1 
ATOM   4777 N  NZ  . LYS A 1 605  ? 27.208 98.435  -16.588 1.00 27.67 ? 605  LYS A NZ  1 
ATOM   4778 N  N   . THR A 1 606  ? 29.075 94.937  -23.123 1.00 20.91 ? 606  THR A N   1 
ATOM   4779 C  CA  . THR A 1 606  ? 29.209 93.787  -24.019 1.00 19.63 ? 606  THR A CA  1 
ATOM   4780 C  C   . THR A 1 606  ? 30.452 93.008  -23.579 1.00 19.51 ? 606  THR A C   1 
ATOM   4781 O  O   . THR A 1 606  ? 31.253 93.509  -22.789 1.00 20.00 ? 606  THR A O   1 
ATOM   4782 C  CB  . THR A 1 606  ? 29.393 94.217  -25.486 1.00 20.75 ? 606  THR A CB  1 
ATOM   4783 O  OG1 . THR A 1 606  ? 30.564 95.052  -25.598 1.00 21.10 ? 606  THR A OG1 1 
ATOM   4784 C  CG2 . THR A 1 606  ? 28.149 94.956  -25.976 1.00 18.98 ? 606  THR A CG2 1 
ATOM   4785 N  N   . ILE A 1 607  ? 30.588 91.773  -24.053 1.00 18.41 ? 607  ILE A N   1 
ATOM   4786 C  CA  . ILE A 1 607  ? 31.751 90.949  -23.729 1.00 17.04 ? 607  ILE A CA  1 
ATOM   4787 C  C   . ILE A 1 607  ? 32.380 90.729  -25.104 1.00 17.25 ? 607  ILE A C   1 
ATOM   4788 O  O   . ILE A 1 607  ? 31.797 90.059  -25.956 1.00 15.39 ? 607  ILE A O   1 
ATOM   4789 C  CB  . ILE A 1 607  ? 31.325 89.624  -23.100 1.00 17.68 ? 607  ILE A CB  1 
ATOM   4790 C  CG1 . ILE A 1 607  ? 30.458 89.899  -21.868 1.00 18.07 ? 607  ILE A CG1 1 
ATOM   4791 C  CG2 . ILE A 1 607  ? 32.580 88.834  -22.686 1.00 17.42 ? 607  ILE A CG2 1 
ATOM   4792 C  CD1 . ILE A 1 607  ? 29.593 88.754  -21.424 1.00 17.87 ? 607  ILE A CD1 1 
ATOM   4793 N  N   . HIS A 1 608  ? 33.558 91.310  -25.327 1.00 17.54 ? 608  HIS A N   1 
ATOM   4794 C  CA  . HIS A 1 608  ? 34.210 91.233  -26.636 1.00 18.15 ? 608  HIS A CA  1 
ATOM   4795 C  C   . HIS A 1 608  ? 35.702 91.030  -26.479 1.00 17.50 ? 608  HIS A C   1 
ATOM   4796 O  O   . HIS A 1 608  ? 36.281 91.361  -25.431 1.00 18.72 ? 608  HIS A O   1 
ATOM   4797 C  CB  . HIS A 1 608  ? 33.925 92.504  -27.411 1.00 20.84 ? 608  HIS A CB  1 
ATOM   4798 C  CG  . HIS A 1 608  ? 34.359 93.730  -26.690 1.00 23.96 ? 608  HIS A CG  1 
ATOM   4799 N  ND1 . HIS A 1 608  ? 35.445 94.481  -27.086 1.00 27.14 ? 608  HIS A ND1 1 
ATOM   4800 C  CD2 . HIS A 1 608  ? 33.894 94.309  -25.559 1.00 24.89 ? 608  HIS A CD2 1 
ATOM   4801 C  CE1 . HIS A 1 608  ? 35.629 95.474  -26.231 1.00 25.98 ? 608  HIS A CE1 1 
ATOM   4802 N  NE2 . HIS A 1 608  ? 34.702 95.391  -25.293 1.00 27.27 ? 608  HIS A NE2 1 
ATOM   4803 N  N   . PRO A 1 609  ? 36.365 90.503  -27.522 1.00 16.42 ? 609  PRO A N   1 
ATOM   4804 C  CA  . PRO A 1 609  ? 37.805 90.263  -27.402 1.00 16.70 ? 609  PRO A CA  1 
ATOM   4805 C  C   . PRO A 1 609  ? 38.720 91.381  -27.860 1.00 17.21 ? 609  PRO A C   1 
ATOM   4806 O  O   . PRO A 1 609  ? 38.382 92.125  -28.768 1.00 17.72 ? 609  PRO A O   1 
ATOM   4807 C  CB  . PRO A 1 609  ? 37.991 88.999  -28.229 1.00 16.66 ? 609  PRO A CB  1 
ATOM   4808 C  CG  . PRO A 1 609  ? 37.097 89.306  -29.427 1.00 16.65 ? 609  PRO A CG  1 
ATOM   4809 C  CD  . PRO A 1 609  ? 35.852 89.988  -28.803 1.00 17.10 ? 609  PRO A CD  1 
ATOM   4810 N  N   . GLN A 1 610  ? 39.887 91.473  -27.236 1.00 17.70 ? 610  GLN A N   1 
ATOM   4811 C  CA  . GLN A 1 610  ? 40.877 92.487  -27.584 1.00 20.15 ? 610  GLN A CA  1 
ATOM   4812 C  C   . GLN A 1 610  ? 42.109 91.712  -27.951 1.00 18.39 ? 610  GLN A C   1 
ATOM   4813 O  O   . GLN A 1 610  ? 42.432 90.729  -27.288 1.00 17.99 ? 610  GLN A O   1 
ATOM   4814 C  CB  . GLN A 1 610  ? 41.183 93.379  -26.378 1.00 23.86 ? 610  GLN A CB  1 
ATOM   4815 C  CG  . GLN A 1 610  ? 39.967 94.092  -25.834 1.00 31.23 ? 610  GLN A CG  1 
ATOM   4816 C  CD  . GLN A 1 610  ? 39.425 95.143  -26.792 1.00 35.12 ? 610  GLN A CD  1 
ATOM   4817 O  OE1 . GLN A 1 610  ? 38.925 94.826  -27.890 1.00 38.26 ? 610  GLN A OE1 1 
ATOM   4818 N  NE2 . GLN A 1 610  ? 39.524 96.411  -26.387 1.00 37.78 ? 610  GLN A NE2 1 
ATOM   4819 N  N   . GLY A 1 611  ? 42.786 92.138  -29.007 1.00 17.69 ? 611  GLY A N   1 
ATOM   4820 C  CA  . GLY A 1 611  ? 43.990 91.441  -29.424 1.00 16.55 ? 611  GLY A CA  1 
ATOM   4821 C  C   . GLY A 1 611  ? 45.250 92.161  -28.967 1.00 17.45 ? 611  GLY A C   1 
ATOM   4822 O  O   . GLY A 1 611  ? 45.276 93.396  -28.900 1.00 16.29 ? 611  GLY A O   1 
ATOM   4823 N  N   . SER A 1 612  ? 46.290 91.405  -28.629 1.00 17.94 ? 612  SER A N   1 
ATOM   4824 C  CA  . SER A 1 612  ? 47.560 92.006  -28.203 1.00 18.39 ? 612  SER A CA  1 
ATOM   4825 C  C   . SER A 1 612  ? 48.258 92.543  -29.448 1.00 19.18 ? 612  SER A C   1 
ATOM   4826 O  O   . SER A 1 612  ? 48.151 91.946  -30.521 1.00 18.37 ? 612  SER A O   1 
ATOM   4827 C  CB  . SER A 1 612  ? 48.470 90.947  -27.564 1.00 18.21 ? 612  SER A CB  1 
ATOM   4828 O  OG  . SER A 1 612  ? 49.789 91.456  -27.404 1.00 17.29 ? 612  SER A OG  1 
ATOM   4829 N  N   . THR A 1 613  ? 48.936 93.687  -29.328 1.00 20.60 ? 613  THR A N   1 
ATOM   4830 C  CA  . THR A 1 613  ? 49.679 94.227  -30.459 1.00 22.01 ? 613  THR A CA  1 
ATOM   4831 C  C   . THR A 1 613  ? 51.178 93.950  -30.241 1.00 23.78 ? 613  THR A C   1 
ATOM   4832 O  O   . THR A 1 613  ? 52.015 94.294  -31.094 1.00 23.73 ? 613  THR A O   1 
ATOM   4833 C  CB  . THR A 1 613  ? 49.488 95.747  -30.601 1.00 22.63 ? 613  THR A CB  1 
ATOM   4834 O  OG1 . THR A 1 613  ? 49.927 96.373  -29.394 1.00 22.88 ? 613  THR A OG1 1 
ATOM   4835 C  CG2 . THR A 1 613  ? 48.006 96.098  -30.834 1.00 21.79 ? 613  THR A CG2 1 
ATOM   4836 N  N   . THR A 1 614  ? 51.512 93.296  -29.119 1.00 24.63 ? 614  THR A N   1 
ATOM   4837 C  CA  . THR A 1 614  ? 52.912 92.981  -28.809 1.00 24.44 ? 614  THR A CA  1 
ATOM   4838 C  C   . THR A 1 614  ? 53.266 91.501  -28.532 1.00 24.25 ? 614  THR A C   1 
ATOM   4839 O  O   . THR A 1 614  ? 54.449 91.164  -28.431 1.00 24.37 ? 614  THR A O   1 
ATOM   4840 C  CB  . THR A 1 614  ? 53.349 93.778  -27.620 1.00 24.52 ? 614  THR A CB  1 
ATOM   4841 O  OG1 . THR A 1 614  ? 52.441 93.517  -26.546 1.00 25.91 ? 614  THR A OG1 1 
ATOM   4842 C  CG2 . THR A 1 614  ? 53.339 95.286  -27.960 1.00 26.58 ? 614  THR A CG2 1 
ATOM   4843 N  N   . LYS A 1 615  ? 52.271 90.636  -28.358 1.00 22.23 ? 615  LYS A N   1 
ATOM   4844 C  CA  . LYS A 1 615  ? 52.552 89.224  -28.124 1.00 21.76 ? 615  LYS A CA  1 
ATOM   4845 C  C   . LYS A 1 615  ? 51.686 88.463  -29.094 1.00 20.50 ? 615  LYS A C   1 
ATOM   4846 O  O   . LYS A 1 615  ? 50.580 88.914  -29.453 1.00 19.33 ? 615  LYS A O   1 
ATOM   4847 C  CB  . LYS A 1 615  ? 52.158 88.748  -26.722 1.00 23.30 ? 615  LYS A CB  1 
ATOM   4848 C  CG  . LYS A 1 615  ? 52.161 89.781  -25.638 1.00 27.74 ? 615  LYS A CG  1 
ATOM   4849 C  CD  . LYS A 1 615  ? 52.026 89.127  -24.237 1.00 28.10 ? 615  LYS A CD  1 
ATOM   4850 C  CE  . LYS A 1 615  ? 50.883 88.100  -24.157 1.00 29.48 ? 615  LYS A CE  1 
ATOM   4851 N  NZ  . LYS A 1 615  ? 50.643 87.684  -22.740 1.00 29.15 ? 615  LYS A NZ  1 
ATOM   4852 N  N   . TYR A 1 616  ? 52.176 87.290  -29.472 1.00 18.10 ? 616  TYR A N   1 
ATOM   4853 C  CA  . TYR A 1 616  ? 51.487 86.416  -30.410 1.00 17.48 ? 616  TYR A CA  1 
ATOM   4854 C  C   . TYR A 1 616  ? 51.657 84.981  -29.984 1.00 15.63 ? 616  TYR A C   1 
ATOM   4855 O  O   . TYR A 1 616  ? 52.566 84.675  -29.222 1.00 14.69 ? 616  TYR A O   1 
ATOM   4856 C  CB  . TYR A 1 616  ? 52.059 86.598  -31.823 1.00 16.69 ? 616  TYR A CB  1 
ATOM   4857 C  CG  . TYR A 1 616  ? 52.077 88.054  -32.248 1.00 19.00 ? 616  TYR A CG  1 
ATOM   4858 C  CD1 . TYR A 1 616  ? 53.154 88.882  -31.897 1.00 18.47 ? 616  TYR A CD1 1 
ATOM   4859 C  CD2 . TYR A 1 616  ? 50.960 88.636  -32.889 1.00 18.38 ? 616  TYR A CD2 1 
ATOM   4860 C  CE1 . TYR A 1 616  ? 53.127 90.228  -32.153 1.00 20.06 ? 616  TYR A CE1 1 
ATOM   4861 C  CE2 . TYR A 1 616  ? 50.921 89.992  -33.151 1.00 18.79 ? 616  TYR A CE2 1 
ATOM   4862 C  CZ  . TYR A 1 616  ? 52.005 90.782  -32.775 1.00 20.28 ? 616  TYR A CZ  1 
ATOM   4863 O  OH  . TYR A 1 616  ? 51.973 92.134  -32.955 1.00 23.25 ? 616  TYR A OH  1 
ATOM   4864 N  N   . ARG A 1 617  ? 50.784 84.105  -30.486 1.00 15.86 ? 617  ARG A N   1 
ATOM   4865 C  CA  . ARG A 1 617  ? 50.843 82.675  -30.183 1.00 15.21 ? 617  ARG A CA  1 
ATOM   4866 C  C   . ARG A 1 617  ? 51.483 81.909  -31.323 1.00 14.50 ? 617  ARG A C   1 
ATOM   4867 O  O   . ARG A 1 617  ? 51.078 82.072  -32.479 1.00 15.26 ? 617  ARG A O   1 
ATOM   4868 C  CB  . ARG A 1 617  ? 49.455 82.098  -29.988 1.00 16.37 ? 617  ARG A CB  1 
ATOM   4869 C  CG  . ARG A 1 617  ? 48.806 82.361  -28.656 1.00 18.91 ? 617  ARG A CG  1 
ATOM   4870 C  CD  . ARG A 1 617  ? 47.394 81.727  -28.586 1.00 19.97 ? 617  ARG A CD  1 
ATOM   4871 N  NE  . ARG A 1 617  ? 47.389 80.262  -28.545 1.00 19.48 ? 617  ARG A NE  1 
ATOM   4872 C  CZ  . ARG A 1 617  ? 46.784 79.475  -29.437 1.00 21.01 ? 617  ARG A CZ  1 
ATOM   4873 N  NH1 . ARG A 1 617  ? 46.129 79.992  -30.470 1.00 22.60 ? 617  ARG A NH1 1 
ATOM   4874 N  NH2 . ARG A 1 617  ? 46.791 78.160  -29.283 1.00 18.83 ? 617  ARG A NH2 1 
ATOM   4875 N  N   . ILE A 1 618  ? 52.494 81.096  -31.043 1.00 12.99 ? 618  ILE A N   1 
ATOM   4876 C  CA  . ILE A 1 618  ? 53.057 80.298  -32.131 1.00 12.31 ? 618  ILE A CA  1 
ATOM   4877 C  C   . ILE A 1 618  ? 52.702 78.872  -31.774 1.00 11.17 ? 618  ILE A C   1 
ATOM   4878 O  O   . ILE A 1 618  ? 52.858 78.465  -30.630 1.00 11.21 ? 618  ILE A O   1 
ATOM   4879 C  CB  . ILE A 1 618  ? 54.589 80.481  -32.345 1.00 12.07 ? 618  ILE A CB  1 
ATOM   4880 C  CG1 . ILE A 1 618  ? 55.008 79.601  -33.532 1.00 14.21 ? 618  ILE A CG1 1 
ATOM   4881 C  CG2 . ILE A 1 618  ? 55.383 80.155  -31.105 1.00 12.63 ? 618  ILE A CG2 1 
ATOM   4882 C  CD1 . ILE A 1 618  ? 56.325 79.970  -34.189 1.00 13.88 ? 618  ILE A CD1 1 
ATOM   4883 N  N   . ILE A 1 619  ? 52.200 78.135  -32.757 1.00 10.00 ? 619  ILE A N   1 
ATOM   4884 C  CA  . ILE A 1 619  ? 51.727 76.763  -32.578 1.00 11.08 ? 619  ILE A CA  1 
ATOM   4885 C  C   . ILE A 1 619  ? 52.417 75.793  -33.538 1.00 11.45 ? 619  ILE A C   1 
ATOM   4886 O  O   . ILE A 1 619  ? 52.496 76.062  -34.735 1.00 11.79 ? 619  ILE A O   1 
ATOM   4887 C  CB  . ILE A 1 619  ? 50.207 76.706  -32.898 1.00 12.50 ? 619  ILE A CB  1 
ATOM   4888 C  CG1 . ILE A 1 619  ? 49.483 77.813  -32.114 1.00 15.71 ? 619  ILE A CG1 1 
ATOM   4889 C  CG2 . ILE A 1 619  ? 49.655 75.333  -32.636 1.00 12.25 ? 619  ILE A CG2 1 
ATOM   4890 C  CD1 . ILE A 1 619  ? 48.163 78.335  -32.816 1.00 16.86 ? 619  ILE A CD1 1 
ATOM   4891 N  N   . PHE A 1 620  ? 52.871 74.657  -33.031 1.00 9.87  ? 620  PHE A N   1 
ATOM   4892 C  CA  . PHE A 1 620  ? 53.500 73.668  -33.884 1.00 10.17 ? 620  PHE A CA  1 
ATOM   4893 C  C   . PHE A 1 620  ? 53.341 72.306  -33.249 1.00 10.80 ? 620  PHE A C   1 
ATOM   4894 O  O   . PHE A 1 620  ? 53.088 72.208  -32.056 1.00 11.66 ? 620  PHE A O   1 
ATOM   4895 C  CB  . PHE A 1 620  ? 54.986 73.972  -34.108 1.00 7.68  ? 620  PHE A CB  1 
ATOM   4896 C  CG  . PHE A 1 620  ? 55.834 73.866  -32.869 1.00 8.51  ? 620  PHE A CG  1 
ATOM   4897 C  CD1 . PHE A 1 620  ? 56.466 72.670  -32.544 1.00 9.00  ? 620  PHE A CD1 1 
ATOM   4898 C  CD2 . PHE A 1 620  ? 56.052 74.972  -32.059 1.00 6.91  ? 620  PHE A CD2 1 
ATOM   4899 C  CE1 . PHE A 1 620  ? 57.313 72.560  -31.430 1.00 7.82  ? 620  PHE A CE1 1 
ATOM   4900 C  CE2 . PHE A 1 620  ? 56.908 74.887  -30.931 1.00 9.32  ? 620  PHE A CE2 1 
ATOM   4901 C  CZ  . PHE A 1 620  ? 57.541 73.662  -30.621 1.00 7.20  ? 620  PHE A CZ  1 
ATOM   4902 N  N   . LYS A 1 621  ? 53.474 71.272  -34.070 1.00 11.13 ? 621  LYS A N   1 
ATOM   4903 C  CA  . LYS A 1 621  ? 53.352 69.892  -33.634 1.00 12.14 ? 621  LYS A CA  1 
ATOM   4904 C  C   . LYS A 1 621  ? 54.643 69.360  -33.017 1.00 11.55 ? 621  LYS A C   1 
ATOM   4905 O  O   . LYS A 1 621  ? 55.677 69.271  -33.698 1.00 10.95 ? 621  LYS A O   1 
ATOM   4906 C  CB  . LYS A 1 621  ? 52.944 69.024  -34.842 1.00 12.66 ? 621  LYS A CB  1 
ATOM   4907 C  CG  . LYS A 1 621  ? 52.643 67.564  -34.524 1.00 13.77 ? 621  LYS A CG  1 
ATOM   4908 C  CD  . LYS A 1 621  ? 51.832 66.893  -35.652 1.00 16.38 ? 621  LYS A CD  1 
ATOM   4909 C  CE  . LYS A 1 621  ? 52.553 66.958  -36.988 1.00 21.20 ? 621  LYS A CE  1 
ATOM   4910 N  NZ  . LYS A 1 621  ? 51.828 66.210  -38.093 1.00 23.26 ? 621  LYS A NZ  1 
ATOM   4911 N  N   . ALA A 1 622  ? 54.610 69.024  -31.725 1.00 10.69 ? 622  ALA A N   1 
ATOM   4912 C  CA  . ALA A 1 622  ? 55.801 68.449  -31.095 1.00 11.67 ? 622  ALA A CA  1 
ATOM   4913 C  C   . ALA A 1 622  ? 55.697 66.925  -31.185 1.00 11.51 ? 622  ALA A C   1 
ATOM   4914 O  O   . ALA A 1 622  ? 54.605 66.362  -31.075 1.00 13.13 ? 622  ALA A O   1 
ATOM   4915 C  CB  . ALA A 1 622  ? 55.895 68.845  -29.623 1.00 9.75  ? 622  ALA A CB  1 
ATOM   4916 N  N   . ARG A 1 623  ? 56.829 66.256  -31.345 1.00 12.61 ? 623  ARG A N   1 
ATOM   4917 C  CA  . ARG A 1 623  ? 56.840 64.796  -31.414 1.00 12.34 ? 623  ARG A CA  1 
ATOM   4918 C  C   . ARG A 1 623  ? 57.816 64.361  -30.319 1.00 10.97 ? 623  ARG A C   1 
ATOM   4919 O  O   . ARG A 1 623  ? 58.980 64.705  -30.345 1.00 10.99 ? 623  ARG A O   1 
ATOM   4920 C  CB  . ARG A 1 623  ? 57.274 64.305  -32.796 1.00 14.54 ? 623  ARG A CB  1 
ATOM   4921 C  CG  . ARG A 1 623  ? 57.309 62.775  -32.862 1.00 15.54 ? 623  ARG A CG  1 
ATOM   4922 C  CD  . ARG A 1 623  ? 57.256 62.212  -34.320 1.00 19.11 ? 623  ARG A CD  1 
ATOM   4923 N  NE  . ARG A 1 623  ? 57.479 60.762  -34.327 1.00 18.41 ? 623  ARG A NE  1 
ATOM   4924 C  CZ  . ARG A 1 623  ? 58.683 60.199  -34.219 1.00 20.72 ? 623  ARG A CZ  1 
ATOM   4925 N  NH1 . ARG A 1 623  ? 59.773 60.958  -34.120 1.00 20.97 ? 623  ARG A NH1 1 
ATOM   4926 N  NH2 . ARG A 1 623  ? 58.799 58.881  -34.134 1.00 22.24 ? 623  ARG A NH2 1 
ATOM   4927 N  N   . VAL A 1 624  ? 57.318 63.617  -29.336 1.00 10.19 ? 624  VAL A N   1 
ATOM   4928 C  CA  . VAL A 1 624  ? 58.154 63.270  -28.192 1.00 10.72 ? 624  VAL A CA  1 
ATOM   4929 C  C   . VAL A 1 624  ? 58.208 61.788  -27.887 1.00 8.91  ? 624  VAL A C   1 
ATOM   4930 O  O   . VAL A 1 624  ? 57.186 61.130  -27.914 1.00 8.17  ? 624  VAL A O   1 
ATOM   4931 C  CB  . VAL A 1 624  ? 57.626 64.018  -26.936 1.00 11.52 ? 624  VAL A CB  1 
ATOM   4932 C  CG1 . VAL A 1 624  ? 58.656 63.942  -25.785 1.00 10.16 ? 624  VAL A CG1 1 
ATOM   4933 C  CG2 . VAL A 1 624  ? 57.310 65.504  -27.328 1.00 11.64 ? 624  VAL A CG2 1 
ATOM   4934 N  N   . PRO A 1 625  ? 59.406 61.266  -27.558 1.00 8.57  ? 625  PRO A N   1 
ATOM   4935 C  CA  . PRO A 1 625  ? 59.563 59.845  -27.244 1.00 8.11  ? 625  PRO A CA  1 
ATOM   4936 C  C   . PRO A 1 625  ? 58.722 59.397  -26.029 1.00 9.61  ? 625  PRO A C   1 
ATOM   4937 O  O   . PRO A 1 625  ? 58.247 60.202  -25.245 1.00 7.55  ? 625  PRO A O   1 
ATOM   4938 C  CB  . PRO A 1 625  ? 61.066 59.712  -26.947 1.00 8.50  ? 625  PRO A CB  1 
ATOM   4939 C  CG  . PRO A 1 625  ? 61.701 60.925  -27.686 1.00 8.29  ? 625  PRO A CG  1 
ATOM   4940 C  CD  . PRO A 1 625  ? 60.679 61.989  -27.340 1.00 8.40  ? 625  PRO A CD  1 
ATOM   4941 N  N   . PRO A 1 626  ? 58.512 58.082  -25.894 1.00 10.18 ? 626  PRO A N   1 
ATOM   4942 C  CA  . PRO A 1 626  ? 57.751 57.564  -24.763 1.00 9.38  ? 626  PRO A CA  1 
ATOM   4943 C  C   . PRO A 1 626  ? 58.512 58.040  -23.515 1.00 10.21 ? 626  PRO A C   1 
ATOM   4944 O  O   . PRO A 1 626  ? 59.736 57.916  -23.480 1.00 9.03  ? 626  PRO A O   1 
ATOM   4945 C  CB  . PRO A 1 626  ? 57.906 56.052  -24.902 1.00 9.15  ? 626  PRO A CB  1 
ATOM   4946 C  CG  . PRO A 1 626  ? 58.212 55.826  -26.352 1.00 10.01 ? 626  PRO A CG  1 
ATOM   4947 C  CD  . PRO A 1 626  ? 59.068 56.993  -26.728 1.00 8.85  ? 626  PRO A CD  1 
ATOM   4948 N  N   . MET A 1 627  ? 57.807 58.568  -22.507 1.00 9.50  ? 627  MET A N   1 
ATOM   4949 C  CA  . MET A 1 627  ? 58.449 58.991  -21.246 1.00 9.23  ? 627  MET A CA  1 
ATOM   4950 C  C   . MET A 1 627  ? 59.746 59.738  -21.527 1.00 9.56  ? 627  MET A C   1 
ATOM   4951 O  O   . MET A 1 627  ? 60.754 59.530  -20.837 1.00 6.94  ? 627  MET A O   1 
ATOM   4952 C  CB  . MET A 1 627  ? 58.746 57.738  -20.400 1.00 9.62  ? 627  MET A CB  1 
ATOM   4953 C  CG  . MET A 1 627  ? 57.463 56.984  -19.980 1.00 10.83 ? 627  MET A CG  1 
ATOM   4954 S  SD  . MET A 1 627  ? 57.762 55.345  -19.250 1.00 12.46 ? 627  MET A SD  1 
ATOM   4955 C  CE  . MET A 1 627  ? 58.603 55.744  -17.708 1.00 13.60 ? 627  MET A CE  1 
ATOM   4956 N  N   . GLY A 1 628  ? 59.695 60.649  -22.506 1.00 10.52 ? 628  GLY A N   1 
ATOM   4957 C  CA  . GLY A 1 628  ? 60.906 61.335  -22.934 1.00 9.21  ? 628  GLY A CA  1 
ATOM   4958 C  C   . GLY A 1 628  ? 60.797 62.834  -23.155 1.00 10.25 ? 628  GLY A C   1 
ATOM   4959 O  O   . GLY A 1 628  ? 59.827 63.486  -22.758 1.00 8.37  ? 628  GLY A O   1 
ATOM   4960 N  N   . LEU A 1 629  ? 61.803 63.364  -23.837 1.00 8.87  ? 629  LEU A N   1 
ATOM   4961 C  CA  . LEU A 1 629  ? 61.912 64.798  -24.080 1.00 9.21  ? 629  LEU A CA  1 
ATOM   4962 C  C   . LEU A 1 629  ? 62.320 65.070  -25.536 1.00 9.13  ? 629  LEU A C   1 
ATOM   4963 O  O   . LEU A 1 629  ? 63.018 64.253  -26.161 1.00 7.94  ? 629  LEU A O   1 
ATOM   4964 C  CB  . LEU A 1 629  ? 62.992 65.357  -23.153 1.00 7.84  ? 629  LEU A CB  1 
ATOM   4965 C  CG  . LEU A 1 629  ? 62.732 65.216  -21.648 1.00 11.17 ? 629  LEU A CG  1 
ATOM   4966 C  CD1 . LEU A 1 629  ? 64.046 65.474  -20.876 1.00 8.98  ? 629  LEU A CD1 1 
ATOM   4967 C  CD2 . LEU A 1 629  ? 61.684 66.261  -21.216 1.00 10.36 ? 629  LEU A CD2 1 
ATOM   4968 N  N   . ALA A 1 630  ? 61.913 66.223  -26.051 1.00 9.51  ? 630  ALA A N   1 
ATOM   4969 C  CA  . ALA A 1 630  ? 62.246 66.596  -27.415 1.00 9.86  ? 630  ALA A CA  1 
ATOM   4970 C  C   . ALA A 1 630  ? 62.466 68.090  -27.371 1.00 11.00 ? 630  ALA A C   1 
ATOM   4971 O  O   . ALA A 1 630  ? 61.663 68.821  -26.795 1.00 11.55 ? 630  ALA A O   1 
ATOM   4972 C  CB  . ALA A 1 630  ? 61.128 66.241  -28.360 1.00 9.16  ? 630  ALA A CB  1 
ATOM   4973 N  N   . THR A 1 631  ? 63.597 68.520  -27.931 1.00 11.93 ? 631  THR A N   1 
ATOM   4974 C  CA  . THR A 1 631  ? 64.004 69.934  -27.934 1.00 11.14 ? 631  THR A CA  1 
ATOM   4975 C  C   . THR A 1 631  ? 63.734 70.600  -29.276 1.00 11.99 ? 631  THR A C   1 
ATOM   4976 O  O   . THR A 1 631  ? 63.961 69.976  -30.320 1.00 12.25 ? 631  THR A O   1 
ATOM   4977 C  CB  . THR A 1 631  ? 65.528 70.037  -27.629 1.00 11.41 ? 631  THR A CB  1 
ATOM   4978 O  OG1 . THR A 1 631  ? 65.796 69.322  -26.421 1.00 9.77  ? 631  THR A OG1 1 
ATOM   4979 C  CG2 . THR A 1 631  ? 65.979 71.513  -27.439 1.00 11.08 ? 631  THR A CG2 1 
ATOM   4980 N  N   . TYR A 1 632  ? 63.230 71.843  -29.243 1.00 11.13 ? 632  TYR A N   1 
ATOM   4981 C  CA  . TYR A 1 632  ? 62.979 72.631  -30.460 1.00 10.31 ? 632  TYR A CA  1 
ATOM   4982 C  C   . TYR A 1 632  ? 63.577 74.032  -30.261 1.00 10.83 ? 632  TYR A C   1 
ATOM   4983 O  O   . TYR A 1 632  ? 63.906 74.412  -29.133 1.00 7.76  ? 632  TYR A O   1 
ATOM   4984 C  CB  . TYR A 1 632  ? 61.471 72.759  -30.784 1.00 12.11 ? 632  TYR A CB  1 
ATOM   4985 C  CG  . TYR A 1 632  ? 60.794 71.442  -31.140 1.00 11.86 ? 632  TYR A CG  1 
ATOM   4986 C  CD1 . TYR A 1 632  ? 60.411 70.544  -30.139 1.00 12.17 ? 632  TYR A CD1 1 
ATOM   4987 C  CD2 . TYR A 1 632  ? 60.590 71.071  -32.472 1.00 12.00 ? 632  TYR A CD2 1 
ATOM   4988 C  CE1 . TYR A 1 632  ? 59.844 69.293  -30.454 1.00 11.18 ? 632  TYR A CE1 1 
ATOM   4989 C  CE2 . TYR A 1 632  ? 60.003 69.799  -32.805 1.00 10.67 ? 632  TYR A CE2 1 
ATOM   4990 C  CZ  . TYR A 1 632  ? 59.647 68.936  -31.784 1.00 11.88 ? 632  TYR A CZ  1 
ATOM   4991 O  OH  . TYR A 1 632  ? 59.089 67.701  -32.077 1.00 12.40 ? 632  TYR A OH  1 
ATOM   4992 N  N   . VAL A 1 633  ? 63.692 74.785  -31.357 1.00 10.55 ? 633  VAL A N   1 
ATOM   4993 C  CA  . VAL A 1 633  ? 64.254 76.137  -31.351 1.00 11.70 ? 633  VAL A CA  1 
ATOM   4994 C  C   . VAL A 1 633  ? 63.320 77.091  -32.111 1.00 12.11 ? 633  VAL A C   1 
ATOM   4995 O  O   . VAL A 1 633  ? 62.870 76.770  -33.207 1.00 13.35 ? 633  VAL A O   1 
ATOM   4996 C  CB  . VAL A 1 633  ? 65.648 76.168  -32.045 1.00 10.99 ? 633  VAL A CB  1 
ATOM   4997 C  CG1 . VAL A 1 633  ? 66.238 77.629  -32.058 1.00 11.23 ? 633  VAL A CG1 1 
ATOM   4998 C  CG2 . VAL A 1 633  ? 66.588 75.193  -31.319 1.00 11.26 ? 633  VAL A CG2 1 
ATOM   4999 N  N   . LEU A 1 634  ? 63.017 78.232  -31.504 1.00 12.40 ? 634  LEU A N   1 
ATOM   5000 C  CA  . LEU A 1 634  ? 62.173 79.251  -32.120 1.00 13.57 ? 634  LEU A CA  1 
ATOM   5001 C  C   . LEU A 1 634  ? 63.140 80.372  -32.482 1.00 14.51 ? 634  LEU A C   1 
ATOM   5002 O  O   . LEU A 1 634  ? 63.900 80.842  -31.627 1.00 13.51 ? 634  LEU A O   1 
ATOM   5003 C  CB  . LEU A 1 634  ? 61.144 79.771  -31.135 1.00 15.37 ? 634  LEU A CB  1 
ATOM   5004 C  CG  . LEU A 1 634  ? 60.311 78.741  -30.364 1.00 17.60 ? 634  LEU A CG  1 
ATOM   5005 C  CD1 . LEU A 1 634  ? 59.145 79.479  -29.722 1.00 17.65 ? 634  LEU A CD1 1 
ATOM   5006 C  CD2 . LEU A 1 634  ? 59.813 77.643  -31.256 1.00 15.44 ? 634  LEU A CD2 1 
ATOM   5007 N  N   . THR A 1 635  ? 63.122 80.772  -33.747 1.00 14.52 ? 635  THR A N   1 
ATOM   5008 C  CA  . THR A 1 635  ? 64.040 81.784  -34.224 1.00 14.28 ? 635  THR A CA  1 
ATOM   5009 C  C   . THR A 1 635  ? 63.264 82.945  -34.844 1.00 15.29 ? 635  THR A C   1 
ATOM   5010 O  O   . THR A 1 635  ? 62.312 82.734  -35.596 1.00 14.31 ? 635  THR A O   1 
ATOM   5011 C  CB  . THR A 1 635  ? 64.976 81.170  -35.309 1.00 13.92 ? 635  THR A CB  1 
ATOM   5012 O  OG1 . THR A 1 635  ? 65.641 80.017  -34.767 1.00 13.59 ? 635  THR A OG1 1 
ATOM   5013 C  CG2 . THR A 1 635  ? 66.009 82.201  -35.793 1.00 10.46 ? 635  THR A CG2 1 
ATOM   5014 N  N   . ILE A 1 636  ? 63.668 84.176  -34.537 1.00 17.17 ? 636  ILE A N   1 
ATOM   5015 C  CA  . ILE A 1 636  ? 62.972 85.329  -35.103 1.00 17.80 ? 636  ILE A CA  1 
ATOM   5016 C  C   . ILE A 1 636  ? 63.532 85.628  -36.495 1.00 19.17 ? 636  ILE A C   1 
ATOM   5017 O  O   . ILE A 1 636  ? 64.682 85.321  -36.793 1.00 18.31 ? 636  ILE A O   1 
ATOM   5018 C  CB  . ILE A 1 636  ? 63.092 86.592  -34.179 1.00 18.19 ? 636  ILE A CB  1 
ATOM   5019 C  CG1 . ILE A 1 636  ? 62.178 87.717  -34.693 1.00 18.89 ? 636  ILE A CG1 1 
ATOM   5020 C  CG2 . ILE A 1 636  ? 64.528 87.076  -34.134 1.00 17.78 ? 636  ILE A CG2 1 
ATOM   5021 C  CD1 . ILE A 1 636  ? 62.257 89.011  -33.875 1.00 18.87 ? 636  ILE A CD1 1 
ATOM   5022 N  N   . SER A 1 637  ? 62.693 86.202  -37.351 1.00 20.62 ? 637  SER A N   1 
ATOM   5023 C  CA  . SER A 1 637  ? 63.081 86.538  -38.698 1.00 23.77 ? 637  SER A CA  1 
ATOM   5024 C  C   . SER A 1 637  ? 62.616 87.976  -38.915 1.00 25.20 ? 637  SER A C   1 
ATOM   5025 O  O   . SER A 1 637  ? 61.784 88.471  -38.175 1.00 24.64 ? 637  SER A O   1 
ATOM   5026 C  CB  . SER A 1 637  ? 62.396 85.569  -39.666 1.00 24.91 ? 637  SER A CB  1 
ATOM   5027 O  OG  . SER A 1 637  ? 62.761 85.842  -40.986 1.00 29.36 ? 637  SER A OG  1 
ATOM   5028 N  N   . ASP A 1 638  ? 63.155 88.671  -39.908 1.00 27.89 ? 638  ASP A N   1 
ATOM   5029 C  CA  . ASP A 1 638  ? 62.718 90.050  -40.089 1.00 30.74 ? 638  ASP A CA  1 
ATOM   5030 C  C   . ASP A 1 638  ? 61.392 90.101  -40.854 1.00 31.54 ? 638  ASP A C   1 
ATOM   5031 O  O   . ASP A 1 638  ? 60.746 91.144  -40.894 1.00 32.56 ? 638  ASP A O   1 
ATOM   5032 C  CB  . ASP A 1 638  ? 63.793 90.877  -40.804 1.00 33.65 ? 638  ASP A CB  1 
ATOM   5033 C  CG  . ASP A 1 638  ? 63.735 90.717  -42.299 1.00 37.51 ? 638  ASP A CG  1 
ATOM   5034 O  OD1 . ASP A 1 638  ? 63.944 89.577  -42.793 1.00 39.92 ? 638  ASP A OD1 1 
ATOM   5035 O  OD2 . ASP A 1 638  ? 63.460 91.733  -42.988 1.00 40.39 ? 638  ASP A OD2 1 
ATOM   5036 N  N   . SER A 1 639  ? 60.975 88.968  -41.430 1.00 31.35 ? 639  SER A N   1 
ATOM   5037 C  CA  . SER A 1 639  ? 59.721 88.908  -42.183 1.00 31.14 ? 639  SER A CA  1 
ATOM   5038 C  C   . SER A 1 639  ? 59.144 87.500  -42.180 1.00 30.06 ? 639  SER A C   1 
ATOM   5039 O  O   . SER A 1 639  ? 59.798 86.561  -41.739 1.00 29.62 ? 639  SER A O   1 
ATOM   5040 C  CB  . SER A 1 639  ? 59.954 89.322  -43.631 1.00 32.43 ? 639  SER A CB  1 
ATOM   5041 O  OG  . SER A 1 639  ? 60.659 88.303  -44.317 1.00 34.27 ? 639  SER A OG  1 
ATOM   5042 N  N   . LYS A 1 640  ? 57.929 87.358  -42.700 1.00 29.53 ? 640  LYS A N   1 
ATOM   5043 C  CA  . LYS A 1 640  ? 57.257 86.064  -42.743 1.00 29.10 ? 640  LYS A CA  1 
ATOM   5044 C  C   . LYS A 1 640  ? 58.168 84.899  -43.135 1.00 27.58 ? 640  LYS A C   1 
ATOM   5045 O  O   . LYS A 1 640  ? 58.661 84.833  -44.258 1.00 27.95 ? 640  LYS A O   1 
ATOM   5046 C  CB  . LYS A 1 640  ? 56.052 86.107  -43.688 1.00 30.25 ? 640  LYS A CB  1 
ATOM   5047 C  CG  . LYS A 1 640  ? 54.987 87.124  -43.292 1.00 33.18 ? 640  LYS A CG  1 
ATOM   5048 C  CD  . LYS A 1 640  ? 53.540 86.652  -43.592 1.00 34.92 ? 640  LYS A CD  1 
ATOM   5049 C  CE  . LYS A 1 640  ? 53.226 86.593  -45.064 1.00 35.47 ? 640  LYS A CE  1 
ATOM   5050 N  NZ  . LYS A 1 640  ? 53.332 87.934  -45.705 1.00 36.75 ? 640  LYS A NZ  1 
ATOM   5051 N  N   . PRO A 1 641  ? 58.415 83.964  -42.200 1.00 26.27 ? 641  PRO A N   1 
ATOM   5052 C  CA  . PRO A 1 641  ? 59.273 82.829  -42.534 1.00 24.61 ? 641  PRO A CA  1 
ATOM   5053 C  C   . PRO A 1 641  ? 58.535 81.804  -43.391 1.00 23.69 ? 641  PRO A C   1 
ATOM   5054 O  O   . PRO A 1 641  ? 57.318 81.697  -43.359 1.00 22.63 ? 641  PRO A O   1 
ATOM   5055 C  CB  . PRO A 1 641  ? 59.684 82.284  -41.161 1.00 25.88 ? 641  PRO A CB  1 
ATOM   5056 C  CG  . PRO A 1 641  ? 58.560 82.621  -40.303 1.00 26.08 ? 641  PRO A CG  1 
ATOM   5057 C  CD  . PRO A 1 641  ? 58.133 84.003  -40.755 1.00 25.67 ? 641  PRO A CD  1 
ATOM   5058 N  N   . GLU A 1 642  ? 59.294 81.043  -44.153 1.00 23.09 ? 642  GLU A N   1 
ATOM   5059 C  CA  . GLU A 1 642  ? 58.749 80.046  -45.050 1.00 23.23 ? 642  GLU A CA  1 
ATOM   5060 C  C   . GLU A 1 642  ? 57.849 78.959  -44.456 1.00 21.94 ? 642  GLU A C   1 
ATOM   5061 O  O   . GLU A 1 642  ? 56.876 78.531  -45.094 1.00 20.83 ? 642  GLU A O   1 
ATOM   5062 C  CB  . GLU A 1 642  ? 59.921 79.397  -45.808 1.00 25.52 ? 642  GLU A CB  1 
ATOM   5063 C  CG  . GLU A 1 642  ? 59.554 78.231  -46.701 1.00 30.35 ? 642  GLU A CG  1 
ATOM   5064 C  CD  . GLU A 1 642  ? 60.774 77.626  -47.424 1.00 33.83 ? 642  GLU A CD  1 
ATOM   5065 O  OE1 . GLU A 1 642  ? 60.651 76.468  -47.909 1.00 36.58 ? 642  GLU A OE1 1 
ATOM   5066 O  OE2 . GLU A 1 642  ? 61.843 78.297  -47.507 1.00 34.31 ? 642  GLU A OE2 1 
ATOM   5067 N  N   . HIS A 1 643  ? 58.148 78.500  -43.245 1.00 19.10 ? 643  HIS A N   1 
ATOM   5068 C  CA  . HIS A 1 643  ? 57.354 77.400  -42.665 1.00 17.86 ? 643  HIS A CA  1 
ATOM   5069 C  C   . HIS A 1 643  ? 56.349 77.798  -41.600 1.00 16.52 ? 643  HIS A C   1 
ATOM   5070 O  O   . HIS A 1 643  ? 55.871 76.953  -40.841 1.00 14.85 ? 643  HIS A O   1 
ATOM   5071 C  CB  . HIS A 1 643  ? 58.317 76.342  -42.108 1.00 18.11 ? 643  HIS A CB  1 
ATOM   5072 C  CG  . HIS A 1 643  ? 59.165 75.724  -43.171 1.00 19.77 ? 643  HIS A CG  1 
ATOM   5073 N  ND1 . HIS A 1 643  ? 58.692 74.736  -44.007 1.00 21.63 ? 643  HIS A ND1 1 
ATOM   5074 C  CD2 . HIS A 1 643  ? 60.393 76.057  -43.639 1.00 19.75 ? 643  HIS A CD2 1 
ATOM   5075 C  CE1 . HIS A 1 643  ? 59.588 74.491  -44.951 1.00 20.42 ? 643  HIS A CE1 1 
ATOM   5076 N  NE2 . HIS A 1 643  ? 60.628 75.282  -44.749 1.00 21.72 ? 643  HIS A NE2 1 
ATOM   5077 N  N   . THR A 1 644  ? 56.050 79.086  -41.543 1.00 15.66 ? 644  THR A N   1 
ATOM   5078 C  CA  . THR A 1 644  ? 55.093 79.599  -40.582 1.00 16.01 ? 644  THR A CA  1 
ATOM   5079 C  C   . THR A 1 644  ? 53.940 80.231  -41.365 1.00 16.31 ? 644  THR A C   1 
ATOM   5080 O  O   . THR A 1 644  ? 54.188 80.981  -42.314 1.00 14.72 ? 644  THR A O   1 
ATOM   5081 C  CB  . THR A 1 644  ? 55.746 80.659  -39.688 1.00 17.01 ? 644  THR A CB  1 
ATOM   5082 O  OG1 . THR A 1 644  ? 56.821 80.044  -38.959 1.00 17.11 ? 644  THR A OG1 1 
ATOM   5083 C  CG2 . THR A 1 644  ? 54.710 81.265  -38.674 1.00 17.14 ? 644  THR A CG2 1 
ATOM   5084 N  N   . SER A 1 645  ? 52.704 79.872  -41.010 1.00 14.61 ? 645  SER A N   1 
ATOM   5085 C  CA  . SER A 1 645  ? 51.521 80.441  -41.641 1.00 15.38 ? 645  SER A CA  1 
ATOM   5086 C  C   . SER A 1 645  ? 50.827 81.289  -40.567 1.00 15.06 ? 645  SER A C   1 
ATOM   5087 O  O   . SER A 1 645  ? 51.162 81.223  -39.371 1.00 14.02 ? 645  SER A O   1 
ATOM   5088 C  CB  . SER A 1 645  ? 50.583 79.351  -42.188 1.00 16.36 ? 645  SER A CB  1 
ATOM   5089 O  OG  . SER A 1 645  ? 50.041 78.554  -41.146 1.00 15.37 ? 645  SER A OG  1 
ATOM   5090 N  N   . TYR A 1 646  ? 49.889 82.118  -41.010 1.00 14.18 ? 646  TYR A N   1 
ATOM   5091 C  CA  . TYR A 1 646  ? 49.169 83.021  -40.128 1.00 13.89 ? 646  TYR A CA  1 
ATOM   5092 C  C   . TYR A 1 646  ? 47.674 82.799  -40.253 1.00 13.61 ? 646  TYR A C   1 
ATOM   5093 O  O   . TYR A 1 646  ? 47.146 82.706  -41.359 1.00 13.47 ? 646  TYR A O   1 
ATOM   5094 C  CB  . TYR A 1 646  ? 49.527 84.489  -40.453 1.00 13.87 ? 646  TYR A CB  1 
ATOM   5095 C  CG  . TYR A 1 646  ? 50.993 84.763  -40.241 1.00 14.12 ? 646  TYR A CG  1 
ATOM   5096 C  CD1 . TYR A 1 646  ? 51.921 84.462  -41.243 1.00 14.73 ? 646  TYR A CD1 1 
ATOM   5097 C  CD2 . TYR A 1 646  ? 51.472 85.135  -38.995 1.00 13.09 ? 646  TYR A CD2 1 
ATOM   5098 C  CE1 . TYR A 1 646  ? 53.274 84.511  -40.997 1.00 14.80 ? 646  TYR A CE1 1 
ATOM   5099 C  CE2 . TYR A 1 646  ? 52.824 85.181  -38.734 1.00 13.00 ? 646  TYR A CE2 1 
ATOM   5100 C  CZ  . TYR A 1 646  ? 53.718 84.860  -39.742 1.00 14.59 ? 646  TYR A CZ  1 
ATOM   5101 O  OH  . TYR A 1 646  ? 55.061 84.843  -39.496 1.00 16.15 ? 646  TYR A OH  1 
ATOM   5102 N  N   . ALA A 1 647  ? 46.998 82.701  -39.112 1.00 12.53 ? 647  ALA A N   1 
ATOM   5103 C  CA  . ALA A 1 647  ? 45.568 82.477  -39.114 1.00 11.97 ? 647  ALA A CA  1 
ATOM   5104 C  C   . ALA A 1 647  ? 44.750 83.721  -39.491 1.00 12.15 ? 647  ALA A C   1 
ATOM   5105 O  O   . ALA A 1 647  ? 45.159 84.863  -39.266 1.00 11.48 ? 647  ALA A O   1 
ATOM   5106 C  CB  . ALA A 1 647  ? 45.129 81.966  -37.741 1.00 13.58 ? 647  ALA A CB  1 
ATOM   5107 N  N   . SER A 1 648  ? 43.601 83.506  -40.105 1.00 12.47 ? 648  SER A N   1 
ATOM   5108 C  CA  . SER A 1 648  ? 42.730 84.642  -40.424 1.00 12.57 ? 648  SER A CA  1 
ATOM   5109 C  C   . SER A 1 648  ? 41.871 84.784  -39.171 1.00 12.46 ? 648  SER A C   1 
ATOM   5110 O  O   . SER A 1 648  ? 41.747 83.814  -38.385 1.00 12.98 ? 648  SER A O   1 
ATOM   5111 C  CB  . SER A 1 648  ? 41.840 84.296  -41.616 1.00 13.33 ? 648  SER A CB  1 
ATOM   5112 O  OG  . SER A 1 648  ? 41.060 83.170  -41.262 1.00 16.78 ? 648  SER A OG  1 
ATOM   5113 N  N   . ASN A 1 649  ? 41.299 85.966  -38.947 1.00 11.53 ? 649  ASN A N   1 
ATOM   5114 C  CA  . ASN A 1 649  ? 40.434 86.179  -37.784 1.00 12.26 ? 649  ASN A CA  1 
ATOM   5115 C  C   . ASN A 1 649  ? 39.207 86.919  -38.232 1.00 13.25 ? 649  ASN A C   1 
ATOM   5116 O  O   . ASN A 1 649  ? 39.307 87.928  -38.962 1.00 12.43 ? 649  ASN A O   1 
ATOM   5117 C  CB  . ASN A 1 649  ? 41.130 86.999  -36.697 1.00 11.47 ? 649  ASN A CB  1 
ATOM   5118 C  CG  . ASN A 1 649  ? 42.319 86.276  -36.094 1.00 13.15 ? 649  ASN A CG  1 
ATOM   5119 O  OD1 . ASN A 1 649  ? 42.185 85.507  -35.121 1.00 12.26 ? 649  ASN A OD1 1 
ATOM   5120 N  ND2 . ASN A 1 649  ? 43.488 86.485  -36.690 1.00 11.23 ? 649  ASN A ND2 1 
ATOM   5121 N  N   . LEU A 1 650  ? 38.057 86.461  -37.749 1.00 12.73 ? 650  LEU A N   1 
ATOM   5122 C  CA  . LEU A 1 650  ? 36.772 87.072  -38.112 1.00 13.98 ? 650  LEU A CA  1 
ATOM   5123 C  C   . LEU A 1 650  ? 35.955 87.340  -36.876 1.00 14.36 ? 650  LEU A C   1 
ATOM   5124 O  O   . LEU A 1 650  ? 35.586 86.403  -36.154 1.00 13.85 ? 650  LEU A O   1 
ATOM   5125 C  CB  . LEU A 1 650  ? 35.971 86.132  -39.013 1.00 12.81 ? 650  LEU A CB  1 
ATOM   5126 C  CG  . LEU A 1 650  ? 34.542 86.516  -39.401 1.00 13.81 ? 650  LEU A CG  1 
ATOM   5127 C  CD1 . LEU A 1 650  ? 34.530 87.823  -40.267 1.00 13.26 ? 650  LEU A CD1 1 
ATOM   5128 C  CD2 . LEU A 1 650  ? 33.956 85.333  -40.210 1.00 12.95 ? 650  LEU A CD2 1 
ATOM   5129 N  N   . LEU A 1 651  ? 35.644 88.611  -36.654 1.00 14.85 ? 651  LEU A N   1 
ATOM   5130 C  CA  . LEU A 1 651  ? 34.857 89.021  -35.503 1.00 15.41 ? 651  LEU A CA  1 
ATOM   5131 C  C   . LEU A 1 651  ? 33.412 89.309  -35.943 1.00 16.34 ? 651  LEU A C   1 
ATOM   5132 O  O   . LEU A 1 651  ? 33.141 90.227  -36.735 1.00 17.28 ? 651  LEU A O   1 
ATOM   5133 C  CB  . LEU A 1 651  ? 35.529 90.232  -34.865 1.00 17.98 ? 651  LEU A CB  1 
ATOM   5134 C  CG  . LEU A 1 651  ? 35.216 90.716  -33.438 1.00 20.41 ? 651  LEU A CG  1 
ATOM   5135 C  CD1 . LEU A 1 651  ? 34.066 91.693  -33.430 1.00 22.64 ? 651  LEU A CD1 1 
ATOM   5136 C  CD2 . LEU A 1 651  ? 34.915 89.510  -32.565 1.00 20.40 ? 651  LEU A CD2 1 
ATOM   5137 N  N   . LEU A 1 652  ? 32.480 88.505  -35.441 1.00 15.39 ? 652  LEU A N   1 
ATOM   5138 C  CA  . LEU A 1 652  ? 31.083 88.637  -35.804 1.00 15.41 ? 652  LEU A CA  1 
ATOM   5139 C  C   . LEU A 1 652  ? 30.244 89.285  -34.712 1.00 17.49 ? 652  LEU A C   1 
ATOM   5140 O  O   . LEU A 1 652  ? 30.055 88.747  -33.612 1.00 15.34 ? 652  LEU A O   1 
ATOM   5141 C  CB  . LEU A 1 652  ? 30.511 87.266  -36.170 1.00 15.18 ? 652  LEU A CB  1 
ATOM   5142 C  CG  . LEU A 1 652  ? 31.249 86.520  -37.295 1.00 13.81 ? 652  LEU A CG  1 
ATOM   5143 C  CD1 . LEU A 1 652  ? 30.688 85.106  -37.392 1.00 15.18 ? 652  LEU A CD1 1 
ATOM   5144 C  CD2 . LEU A 1 652  ? 31.082 87.242  -38.649 1.00 13.21 ? 652  LEU A CD2 1 
ATOM   5145 N  N   . ARG A 1 653  ? 29.761 90.473  -35.039 1.00 18.16 ? 653  ARG A N   1 
ATOM   5146 C  CA  . ARG A 1 653  ? 28.939 91.247  -34.145 1.00 21.33 ? 653  ARG A CA  1 
ATOM   5147 C  C   . ARG A 1 653  ? 28.419 92.454  -34.919 1.00 22.92 ? 653  ARG A C   1 
ATOM   5148 O  O   . ARG A 1 653  ? 28.977 92.839  -35.957 1.00 22.20 ? 653  ARG A O   1 
ATOM   5149 C  CB  . ARG A 1 653  ? 29.757 91.713  -32.965 1.00 21.44 ? 653  ARG A CB  1 
ATOM   5150 C  CG  . ARG A 1 653  ? 30.861 92.641  -33.329 1.00 23.95 ? 653  ARG A CG  1 
ATOM   5151 C  CD  . ARG A 1 653  ? 30.689 93.872  -32.492 1.00 27.24 ? 653  ARG A CD  1 
ATOM   5152 N  NE  . ARG A 1 653  ? 31.502 93.853  -31.290 1.00 28.37 ? 653  ARG A NE  1 
ATOM   5153 C  CZ  . ARG A 1 653  ? 31.176 94.459  -30.152 1.00 29.73 ? 653  ARG A CZ  1 
ATOM   5154 N  NH1 . ARG A 1 653  ? 30.038 95.120  -30.041 1.00 31.41 ? 653  ARG A NH1 1 
ATOM   5155 N  NH2 . ARG A 1 653  ? 32.014 94.445  -29.134 1.00 31.38 ? 653  ARG A NH2 1 
ATOM   5156 N  N   . LYS A 1 654  ? 27.344 93.030  -34.414 1.00 25.11 ? 654  LYS A N   1 
ATOM   5157 C  CA  . LYS A 1 654  ? 26.758 94.215  -35.022 1.00 27.51 ? 654  LYS A CA  1 
ATOM   5158 C  C   . LYS A 1 654  ? 27.593 95.361  -34.445 1.00 27.70 ? 654  LYS A C   1 
ATOM   5159 O  O   . LYS A 1 654  ? 28.202 95.204  -33.401 1.00 28.22 ? 654  LYS A O   1 
ATOM   5160 C  CB  . LYS A 1 654  ? 25.301 94.339  -34.570 1.00 28.51 ? 654  LYS A CB  1 
ATOM   5161 C  CG  . LYS A 1 654  ? 24.447 93.155  -34.995 1.00 31.06 ? 654  LYS A CG  1 
ATOM   5162 C  CD  . LYS A 1 654  ? 23.430 93.546  -36.061 1.00 33.14 ? 654  LYS A CD  1 
ATOM   5163 C  CE  . LYS A 1 654  ? 24.082 94.219  -37.265 1.00 34.74 ? 654  LYS A CE  1 
ATOM   5164 N  NZ  . LYS A 1 654  ? 23.050 94.636  -38.302 1.00 37.16 ? 654  LYS A NZ  1 
ATOM   5165 N  N   . ASN A 1 655  ? 27.665 96.489  -35.121 1.00 28.27 ? 655  ASN A N   1 
ATOM   5166 C  CA  . ASN A 1 655  ? 28.417 97.589  -34.540 1.00 29.26 ? 655  ASN A CA  1 
ATOM   5167 C  C   . ASN A 1 655  ? 29.854 97.219  -34.158 1.00 28.73 ? 655  ASN A C   1 
ATOM   5168 O  O   . ASN A 1 655  ? 30.242 97.315  -32.995 1.00 28.31 ? 655  ASN A O   1 
ATOM   5169 C  CB  . ASN A 1 655  ? 27.694 98.081  -33.285 1.00 31.63 ? 655  ASN A CB  1 
ATOM   5170 C  CG  . ASN A 1 655  ? 28.220 99.416  -32.811 1.00 35.22 ? 655  ASN A CG  1 
ATOM   5171 O  OD1 . ASN A 1 655  ? 28.473 100.319 -33.630 1.00 36.63 ? 655  ASN A OD1 1 
ATOM   5172 N  ND2 . ASN A 1 655  ? 28.374 99.569  -31.492 1.00 35.25 ? 655  ASN A ND2 1 
ATOM   5173 N  N   . PRO A 1 656  ? 30.669 96.791  -35.128 1.00 27.66 ? 656  PRO A N   1 
ATOM   5174 C  CA  . PRO A 1 656  ? 32.032 96.449  -34.724 1.00 27.16 ? 656  PRO A CA  1 
ATOM   5175 C  C   . PRO A 1 656  ? 32.926 97.673  -34.733 1.00 26.21 ? 656  PRO A C   1 
ATOM   5176 O  O   . PRO A 1 656  ? 32.574 98.691  -35.314 1.00 26.46 ? 656  PRO A O   1 
ATOM   5177 C  CB  . PRO A 1 656  ? 32.461 95.468  -35.808 1.00 27.29 ? 656  PRO A CB  1 
ATOM   5178 C  CG  . PRO A 1 656  ? 31.818 96.087  -37.026 1.00 26.72 ? 656  PRO A CG  1 
ATOM   5179 C  CD  . PRO A 1 656  ? 30.415 96.358  -36.514 1.00 27.50 ? 656  PRO A CD  1 
ATOM   5180 N  N   . THR A 1 657  ? 34.078 97.550  -34.081 1.00 25.33 ? 657  THR A N   1 
ATOM   5181 C  CA  . THR A 1 657  ? 35.094 98.593  -34.058 1.00 24.09 ? 657  THR A CA  1 
ATOM   5182 C  C   . THR A 1 657  ? 36.409 97.904  -34.437 1.00 23.81 ? 657  THR A C   1 
ATOM   5183 O  O   . THR A 1 657  ? 36.534 96.685  -34.304 1.00 24.11 ? 657  THR A O   1 
ATOM   5184 C  CB  . THR A 1 657  ? 35.220 99.236  -32.668 1.00 24.46 ? 657  THR A CB  1 
ATOM   5185 O  OG1 . THR A 1 657  ? 35.283 98.216  -31.666 1.00 25.35 ? 657  THR A OG1 1 
ATOM   5186 C  CG2 . THR A 1 657  ? 34.018 100.133 -32.395 1.00 23.43 ? 657  THR A CG2 1 
ATOM   5187 N  N   . SER A 1 658  ? 37.374 98.676  -34.911 1.00 22.00 ? 658  SER A N   1 
ATOM   5188 C  CA  . SER A 1 658  ? 38.666 98.150  -35.329 1.00 22.28 ? 658  SER A CA  1 
ATOM   5189 C  C   . SER A 1 658  ? 39.386 97.327  -34.241 1.00 22.35 ? 658  SER A C   1 
ATOM   5190 O  O   . SER A 1 658  ? 39.180 97.538  -33.034 1.00 20.41 ? 658  SER A O   1 
ATOM   5191 C  CB  . SER A 1 658  ? 39.559 99.310  -35.782 1.00 22.68 ? 658  SER A CB  1 
ATOM   5192 O  OG  . SER A 1 658  ? 39.787 100.190 -34.693 1.00 25.40 ? 658  SER A OG  1 
ATOM   5193 N  N   . LEU A 1 659  ? 40.221 96.389  -34.695 1.00 22.05 ? 659  LEU A N   1 
ATOM   5194 C  CA  . LEU A 1 659  ? 40.999 95.505  -33.825 1.00 22.58 ? 659  LEU A CA  1 
ATOM   5195 C  C   . LEU A 1 659  ? 42.373 95.381  -34.453 1.00 22.88 ? 659  LEU A C   1 
ATOM   5196 O  O   . LEU A 1 659  ? 42.638 94.476  -35.248 1.00 23.58 ? 659  LEU A O   1 
ATOM   5197 C  CB  . LEU A 1 659  ? 40.351 94.120  -33.721 1.00 22.77 ? 659  LEU A CB  1 
ATOM   5198 C  CG  . LEU A 1 659  ? 39.072 94.014  -32.880 1.00 23.73 ? 659  LEU A CG  1 
ATOM   5199 C  CD1 . LEU A 1 659  ? 38.410 92.657  -33.102 1.00 25.13 ? 659  LEU A CD1 1 
ATOM   5200 C  CD2 . LEU A 1 659  ? 39.391 94.202  -31.429 1.00 23.16 ? 659  LEU A CD2 1 
ATOM   5201 N  N   . PRO A 1 660  ? 43.255 96.336  -34.154 1.00 23.26 ? 660  PRO A N   1 
ATOM   5202 C  CA  . PRO A 1 660  ? 44.615 96.318  -34.703 1.00 23.00 ? 660  PRO A CA  1 
ATOM   5203 C  C   . PRO A 1 660  ? 45.452 95.211  -34.029 1.00 22.04 ? 660  PRO A C   1 
ATOM   5204 O  O   . PRO A 1 660  ? 45.219 94.865  -32.883 1.00 21.52 ? 660  PRO A O   1 
ATOM   5205 C  CB  . PRO A 1 660  ? 45.124 97.730  -34.394 1.00 23.04 ? 660  PRO A CB  1 
ATOM   5206 C  CG  . PRO A 1 660  ? 44.425 98.057  -33.109 1.00 22.90 ? 660  PRO A CG  1 
ATOM   5207 C  CD  . PRO A 1 660  ? 43.006 97.572  -33.390 1.00 23.40 ? 660  PRO A CD  1 
ATOM   5208 N  N   . LEU A 1 661  ? 46.430 94.664  -34.737 1.00 22.76 ? 661  LEU A N   1 
ATOM   5209 C  CA  . LEU A 1 661  ? 47.225 93.579  -34.151 1.00 21.35 ? 661  LEU A CA  1 
ATOM   5210 C  C   . LEU A 1 661  ? 48.748 93.766  -34.307 1.00 21.04 ? 661  LEU A C   1 
ATOM   5211 O  O   . LEU A 1 661  ? 49.486 92.811  -34.549 1.00 20.79 ? 661  LEU A O   1 
ATOM   5212 C  CB  . LEU A 1 661  ? 46.776 92.257  -34.789 1.00 20.71 ? 661  LEU A CB  1 
ATOM   5213 C  CG  . LEU A 1 661  ? 45.318 91.836  -34.563 1.00 19.70 ? 661  LEU A CG  1 
ATOM   5214 C  CD1 . LEU A 1 661  ? 45.021 90.526  -35.311 1.00 18.40 ? 661  LEU A CD1 1 
ATOM   5215 C  CD2 . LEU A 1 661  ? 45.097 91.657  -33.082 1.00 19.61 ? 661  LEU A CD2 1 
ATOM   5216 N  N   . GLY A 1 662  ? 49.213 95.003  -34.175 1.00 21.18 ? 662  GLY A N   1 
ATOM   5217 C  CA  . GLY A 1 662  ? 50.633 95.263  -34.308 1.00 20.91 ? 662  GLY A CA  1 
ATOM   5218 C  C   . GLY A 1 662  ? 51.208 94.680  -35.578 1.00 21.31 ? 662  GLY A C   1 
ATOM   5219 O  O   . GLY A 1 662  ? 50.666 94.895  -36.663 1.00 20.68 ? 662  GLY A O   1 
ATOM   5220 N  N   . GLN A 1 663  ? 52.280 93.904  -35.463 1.00 22.17 ? 663  GLN A N   1 
ATOM   5221 C  CA  . GLN A 1 663  ? 52.883 93.355  -36.663 1.00 23.52 ? 663  GLN A CA  1 
ATOM   5222 C  C   . GLN A 1 663  ? 52.161 92.183  -37.292 1.00 22.68 ? 663  GLN A C   1 
ATOM   5223 O  O   . GLN A 1 663  ? 52.536 91.757  -38.375 1.00 23.03 ? 663  GLN A O   1 
ATOM   5224 C  CB  . GLN A 1 663  ? 54.316 92.917  -36.419 1.00 26.35 ? 663  GLN A CB  1 
ATOM   5225 C  CG  . GLN A 1 663  ? 55.213 93.905  -35.701 1.00 29.24 ? 663  GLN A CG  1 
ATOM   5226 C  CD  . GLN A 1 663  ? 56.472 93.177  -35.219 1.00 30.27 ? 663  GLN A CD  1 
ATOM   5227 O  OE1 . GLN A 1 663  ? 57.370 92.894  -36.026 1.00 29.37 ? 663  GLN A OE1 1 
ATOM   5228 N  NE2 . GLN A 1 663  ? 56.513 92.822  -33.914 1.00 29.99 ? 663  GLN A NE2 1 
ATOM   5229 N  N   . TYR A 1 664  ? 51.140 91.654  -36.638 1.00 22.36 ? 664  TYR A N   1 
ATOM   5230 C  CA  . TYR A 1 664  ? 50.427 90.528  -37.221 1.00 21.89 ? 664  TYR A CA  1 
ATOM   5231 C  C   . TYR A 1 664  ? 50.133 90.838  -38.691 1.00 22.48 ? 664  TYR A C   1 
ATOM   5232 O  O   . TYR A 1 664  ? 49.520 91.843  -39.002 1.00 21.97 ? 664  TYR A O   1 
ATOM   5233 C  CB  . TYR A 1 664  ? 49.140 90.290  -36.450 1.00 20.52 ? 664  TYR A CB  1 
ATOM   5234 C  CG  . TYR A 1 664  ? 48.557 88.937  -36.719 1.00 18.52 ? 664  TYR A CG  1 
ATOM   5235 C  CD1 . TYR A 1 664  ? 49.111 87.803  -36.130 1.00 16.87 ? 664  TYR A CD1 1 
ATOM   5236 C  CD2 . TYR A 1 664  ? 47.421 88.788  -37.528 1.00 17.27 ? 664  TYR A CD2 1 
ATOM   5237 C  CE1 . TYR A 1 664  ? 48.542 86.552  -36.319 1.00 15.86 ? 664  TYR A CE1 1 
ATOM   5238 C  CE2 . TYR A 1 664  ? 46.844 87.535  -37.738 1.00 15.58 ? 664  TYR A CE2 1 
ATOM   5239 C  CZ  . TYR A 1 664  ? 47.413 86.419  -37.118 1.00 15.49 ? 664  TYR A CZ  1 
ATOM   5240 O  OH  . TYR A 1 664  ? 46.863 85.178  -37.264 1.00 13.22 ? 664  TYR A OH  1 
ATOM   5241 N  N   . PRO A 1 665  ? 50.568 89.967  -39.612 1.00 23.94 ? 665  PRO A N   1 
ATOM   5242 C  CA  . PRO A 1 665  ? 50.381 90.141  -41.064 1.00 25.31 ? 665  PRO A CA  1 
ATOM   5243 C  C   . PRO A 1 665  ? 48.984 90.044  -41.694 1.00 25.90 ? 665  PRO A C   1 
ATOM   5244 O  O   . PRO A 1 665  ? 48.808 90.377  -42.865 1.00 27.23 ? 665  PRO A O   1 
ATOM   5245 C  CB  . PRO A 1 665  ? 51.327 89.096  -41.653 1.00 25.16 ? 665  PRO A CB  1 
ATOM   5246 C  CG  . PRO A 1 665  ? 51.199 87.988  -40.675 1.00 26.51 ? 665  PRO A CG  1 
ATOM   5247 C  CD  . PRO A 1 665  ? 51.233 88.682  -39.323 1.00 24.18 ? 665  PRO A CD  1 
ATOM   5248 N  N   . GLU A 1 666  ? 47.991 89.599  -40.937 1.00 25.82 ? 666  GLU A N   1 
ATOM   5249 C  CA  . GLU A 1 666  ? 46.660 89.445  -41.498 1.00 25.20 ? 666  GLU A CA  1 
ATOM   5250 C  C   . GLU A 1 666  ? 45.676 90.336  -40.758 1.00 23.09 ? 666  GLU A C   1 
ATOM   5251 O  O   . GLU A 1 666  ? 45.560 90.250  -39.540 1.00 21.68 ? 666  GLU A O   1 
ATOM   5252 C  CB  . GLU A 1 666  ? 46.242 87.980  -41.380 1.00 28.09 ? 666  GLU A CB  1 
ATOM   5253 C  CG  . GLU A 1 666  ? 44.838 87.714  -41.845 1.00 32.61 ? 666  GLU A CG  1 
ATOM   5254 C  CD  . GLU A 1 666  ? 44.791 87.206  -43.276 1.00 35.88 ? 666  GLU A CD  1 
ATOM   5255 O  OE1 . GLU A 1 666  ? 45.824 87.360  -44.009 1.00 35.05 ? 666  GLU A OE1 1 
ATOM   5256 O  OE2 . GLU A 1 666  ? 43.708 86.663  -43.641 1.00 37.25 ? 666  GLU A OE2 1 
ATOM   5257 N  N   . ASP A 1 667  ? 44.972 91.185  -41.507 1.00 21.04 ? 667  ASP A N   1 
ATOM   5258 C  CA  . ASP A 1 667  ? 43.993 92.116  -40.926 1.00 21.17 ? 667  ASP A CA  1 
ATOM   5259 C  C   . ASP A 1 667  ? 42.734 91.383  -40.477 1.00 17.88 ? 667  ASP A C   1 
ATOM   5260 O  O   . ASP A 1 667  ? 42.219 90.548  -41.201 1.00 16.81 ? 667  ASP A O   1 
ATOM   5261 C  CB  . ASP A 1 667  ? 43.569 93.184  -41.961 1.00 23.10 ? 667  ASP A CB  1 
ATOM   5262 C  CG  . ASP A 1 667  ? 44.721 94.060  -42.395 1.00 27.55 ? 667  ASP A CG  1 
ATOM   5263 O  OD1 . ASP A 1 667  ? 45.376 94.659  -41.506 1.00 29.63 ? 667  ASP A OD1 1 
ATOM   5264 O  OD2 . ASP A 1 667  ? 44.972 94.139  -43.618 1.00 29.46 ? 667  ASP A OD2 1 
ATOM   5265 N  N   . VAL A 1 668  ? 42.241 91.715  -39.304 1.00 15.99 ? 668  VAL A N   1 
ATOM   5266 C  CA  . VAL A 1 668  ? 41.025 91.113  -38.806 1.00 14.73 ? 668  VAL A CA  1 
ATOM   5267 C  C   . VAL A 1 668  ? 39.868 91.539  -39.713 1.00 15.67 ? 668  VAL A C   1 
ATOM   5268 O  O   . VAL A 1 668  ? 39.823 92.697  -40.155 1.00 14.26 ? 668  VAL A O   1 
ATOM   5269 C  CB  . VAL A 1 668  ? 40.732 91.598  -37.380 1.00 15.60 ? 668  VAL A CB  1 
ATOM   5270 C  CG1 . VAL A 1 668  ? 39.372 91.050  -36.906 1.00 14.63 ? 668  VAL A CG1 1 
ATOM   5271 C  CG2 . VAL A 1 668  ? 41.883 91.160  -36.434 1.00 14.18 ? 668  VAL A CG2 1 
ATOM   5272 N  N   . LYS A 1 669  ? 38.954 90.602  -39.981 1.00 14.17 ? 669  LYS A N   1 
ATOM   5273 C  CA  . LYS A 1 669  ? 37.774 90.830  -40.806 1.00 15.27 ? 669  LYS A CA  1 
ATOM   5274 C  C   . LYS A 1 669  ? 36.546 90.918  -39.882 1.00 14.58 ? 669  LYS A C   1 
ATOM   5275 O  O   . LYS A 1 669  ? 36.559 90.349  -38.786 1.00 13.98 ? 669  LYS A O   1 
ATOM   5276 C  CB  . LYS A 1 669  ? 37.613 89.675  -41.784 1.00 18.36 ? 669  LYS A CB  1 
ATOM   5277 C  CG  . LYS A 1 669  ? 38.064 89.975  -43.226 1.00 24.63 ? 669  LYS A CG  1 
ATOM   5278 C  CD  . LYS A 1 669  ? 39.514 90.500  -43.288 1.00 28.94 ? 669  LYS A CD  1 
ATOM   5279 C  CE  . LYS A 1 669  ? 39.919 90.967  -44.701 1.00 30.40 ? 669  LYS A CE  1 
ATOM   5280 N  NZ  . LYS A 1 669  ? 39.476 89.970  -45.754 1.00 30.89 ? 669  LYS A NZ  1 
ATOM   5281 N  N   . PHE A 1 670  ? 35.497 91.620  -40.312 1.00 13.04 ? 670  PHE A N   1 
ATOM   5282 C  CA  . PHE A 1 670  ? 34.273 91.763  -39.506 1.00 13.93 ? 670  PHE A CA  1 
ATOM   5283 C  C   . PHE A 1 670  ? 33.002 91.344  -40.255 1.00 14.13 ? 670  PHE A C   1 
ATOM   5284 O  O   . PHE A 1 670  ? 33.010 91.211  -41.478 1.00 13.34 ? 670  PHE A O   1 
ATOM   5285 C  CB  . PHE A 1 670  ? 34.107 93.224  -39.024 1.00 13.45 ? 670  PHE A CB  1 
ATOM   5286 C  CG  . PHE A 1 670  ? 35.258 93.724  -38.220 1.00 13.78 ? 670  PHE A CG  1 
ATOM   5287 C  CD1 . PHE A 1 670  ? 36.394 94.231  -38.847 1.00 13.02 ? 670  PHE A CD1 1 
ATOM   5288 C  CD2 . PHE A 1 670  ? 35.242 93.633  -36.839 1.00 14.30 ? 670  PHE A CD2 1 
ATOM   5289 C  CE1 . PHE A 1 670  ? 37.495 94.635  -38.102 1.00 14.05 ? 670  PHE A CE1 1 
ATOM   5290 C  CE2 . PHE A 1 670  ? 36.336 94.028  -36.090 1.00 14.82 ? 670  PHE A CE2 1 
ATOM   5291 C  CZ  . PHE A 1 670  ? 37.469 94.533  -36.721 1.00 14.06 ? 670  PHE A CZ  1 
ATOM   5292 N  N   . GLY A 1 671  ? 31.906 91.154  -39.518 1.00 14.75 ? 671  GLY A N   1 
ATOM   5293 C  CA  . GLY A 1 671  ? 30.645 90.776  -40.152 1.00 14.14 ? 671  GLY A CA  1 
ATOM   5294 C  C   . GLY A 1 671  ? 29.520 90.661  -39.146 1.00 14.46 ? 671  GLY A C   1 
ATOM   5295 O  O   . GLY A 1 671  ? 29.761 90.643  -37.948 1.00 11.97 ? 671  GLY A O   1 
ATOM   5296 N  N   . ASP A 1 672  ? 28.275 90.631  -39.622 1.00 15.05 ? 672  ASP A N   1 
ATOM   5297 C  CA  . ASP A 1 672  ? 27.145 90.448  -38.718 1.00 16.45 ? 672  ASP A CA  1 
ATOM   5298 C  C   . ASP A 1 672  ? 27.119 88.959  -38.318 1.00 16.15 ? 672  ASP A C   1 
ATOM   5299 O  O   . ASP A 1 672  ? 27.607 88.121  -39.050 1.00 14.53 ? 672  ASP A O   1 
ATOM   5300 C  CB  . ASP A 1 672  ? 25.824 90.746  -39.422 1.00 18.47 ? 672  ASP A CB  1 
ATOM   5301 C  CG  . ASP A 1 672  ? 25.620 92.221  -39.670 1.00 20.81 ? 672  ASP A CG  1 
ATOM   5302 O  OD1 . ASP A 1 672  ? 26.247 93.042  -38.974 1.00 22.81 ? 672  ASP A OD1 1 
ATOM   5303 O  OD2 . ASP A 1 672  ? 24.805 92.556  -40.538 1.00 23.90 ? 672  ASP A OD2 1 
ATOM   5304 N  N   . PRO A 1 673  ? 26.554 88.636  -37.151 1.00 16.66 ? 673  PRO A N   1 
ATOM   5305 C  CA  . PRO A 1 673  ? 26.478 87.240  -36.700 1.00 16.82 ? 673  PRO A CA  1 
ATOM   5306 C  C   . PRO A 1 673  ? 25.873 86.398  -37.811 1.00 17.34 ? 673  PRO A C   1 
ATOM   5307 O  O   . PRO A 1 673  ? 24.974 86.839  -38.505 1.00 17.39 ? 673  PRO A O   1 
ATOM   5308 C  CB  . PRO A 1 673  ? 25.549 87.319  -35.505 1.00 16.73 ? 673  PRO A CB  1 
ATOM   5309 C  CG  . PRO A 1 673  ? 25.836 88.640  -34.926 1.00 17.83 ? 673  PRO A CG  1 
ATOM   5310 C  CD  . PRO A 1 673  ? 25.977 89.546  -36.144 1.00 17.08 ? 673  PRO A CD  1 
ATOM   5311 N  N   . ARG A 1 674  ? 26.379 85.189  -37.982 1.00 18.36 ? 674  ARG A N   1 
ATOM   5312 C  CA  . ARG A 1 674  ? 25.877 84.275  -38.994 1.00 18.79 ? 674  ARG A CA  1 
ATOM   5313 C  C   . ARG A 1 674  ? 26.388 82.863  -38.698 1.00 19.15 ? 674  ARG A C   1 
ATOM   5314 O  O   . ARG A 1 674  ? 27.393 82.690  -37.995 1.00 18.42 ? 674  ARG A O   1 
ATOM   5315 C  CB  . ARG A 1 674  ? 26.354 84.708  -40.385 1.00 18.85 ? 674  ARG A CB  1 
ATOM   5316 C  CG  . ARG A 1 674  ? 27.850 84.626  -40.586 1.00 20.65 ? 674  ARG A CG  1 
ATOM   5317 C  CD  . ARG A 1 674  ? 28.180 84.755  -42.049 1.00 23.20 ? 674  ARG A CD  1 
ATOM   5318 N  NE  . ARG A 1 674  ? 29.532 84.321  -42.338 1.00 25.74 ? 674  ARG A NE  1 
ATOM   5319 C  CZ  . ARG A 1 674  ? 30.585 85.119  -42.483 1.00 28.22 ? 674  ARG A CZ  1 
ATOM   5320 N  NH1 . ARG A 1 674  ? 30.467 86.453  -42.368 1.00 29.52 ? 674  ARG A NH1 1 
ATOM   5321 N  NH2 . ARG A 1 674  ? 31.770 84.569  -42.758 1.00 29.02 ? 674  ARG A NH2 1 
ATOM   5322 N  N   . GLU A 1 675  ? 25.712 81.850  -39.226 1.00 17.99 ? 675  GLU A N   1 
ATOM   5323 C  CA  . GLU A 1 675  ? 26.177 80.499  -38.999 1.00 18.61 ? 675  GLU A CA  1 
ATOM   5324 C  C   . GLU A 1 675  ? 27.508 80.299  -39.718 1.00 17.78 ? 675  GLU A C   1 
ATOM   5325 O  O   . GLU A 1 675  ? 27.791 80.949  -40.725 1.00 17.38 ? 675  GLU A O   1 
ATOM   5326 C  CB  . GLU A 1 675  ? 25.146 79.472  -39.490 1.00 20.96 ? 675  GLU A CB  1 
ATOM   5327 C  CG  . GLU A 1 675  ? 23.801 79.595  -38.809 1.00 23.40 ? 675  GLU A CG  1 
ATOM   5328 C  CD  . GLU A 1 675  ? 23.005 78.308  -38.839 1.00 26.82 ? 675  GLU A CD  1 
ATOM   5329 O  OE1 . GLU A 1 675  ? 23.159 77.549  -39.827 1.00 25.64 ? 675  GLU A OE1 1 
ATOM   5330 O  OE2 . GLU A 1 675  ? 22.219 78.074  -37.868 1.00 28.98 ? 675  GLU A OE2 1 
ATOM   5331 N  N   . ILE A 1 676  ? 28.347 79.419  -39.180 1.00 17.26 ? 676  ILE A N   1 
ATOM   5332 C  CA  . ILE A 1 676  ? 29.640 79.155  -39.789 1.00 17.33 ? 676  ILE A CA  1 
ATOM   5333 C  C   . ILE A 1 676  ? 29.989 77.686  -39.684 1.00 16.18 ? 676  ILE A C   1 
ATOM   5334 O  O   . ILE A 1 676  ? 29.458 76.975  -38.809 1.00 13.94 ? 676  ILE A O   1 
ATOM   5335 C  CB  . ILE A 1 676  ? 30.771 79.933  -39.118 1.00 19.80 ? 676  ILE A CB  1 
ATOM   5336 C  CG1 . ILE A 1 676  ? 30.816 79.609  -37.644 1.00 21.69 ? 676  ILE A CG1 1 
ATOM   5337 C  CG2 . ILE A 1 676  ? 30.596 81.457  -39.314 1.00 22.53 ? 676  ILE A CG2 1 
ATOM   5338 C  CD1 . ILE A 1 676  ? 32.184 79.821  -37.088 1.00 25.29 ? 676  ILE A CD1 1 
ATOM   5339 N  N   . SER A 1 677  ? 30.866 77.246  -40.583 1.00 15.19 ? 677  SER A N   1 
ATOM   5340 C  CA  . SER A 1 677  ? 31.352 75.873  -40.608 1.00 18.06 ? 677  SER A CA  1 
ATOM   5341 C  C   . SER A 1 677  ? 32.851 75.923  -40.716 1.00 17.41 ? 677  SER A C   1 
ATOM   5342 O  O   . SER A 1 677  ? 33.399 76.807  -41.366 1.00 18.12 ? 677  SER A O   1 
ATOM   5343 C  CB  . SER A 1 677  ? 30.820 75.093  -41.818 1.00 19.94 ? 677  SER A CB  1 
ATOM   5344 O  OG  . SER A 1 677  ? 29.407 75.144  -41.821 1.00 26.19 ? 677  SER A OG  1 
ATOM   5345 N  N   . LEU A 1 678  ? 33.511 74.967  -40.085 1.00 16.03 ? 678  LEU A N   1 
ATOM   5346 C  CA  . LEU A 1 678  ? 34.958 74.904  -40.129 1.00 17.53 ? 678  LEU A CA  1 
ATOM   5347 C  C   . LEU A 1 678  ? 35.415 73.464  -40.228 1.00 17.03 ? 678  LEU A C   1 
ATOM   5348 O  O   . LEU A 1 678  ? 34.760 72.540  -39.736 1.00 15.64 ? 678  LEU A O   1 
ATOM   5349 C  CB  . LEU A 1 678  ? 35.581 75.500  -38.856 1.00 18.27 ? 678  LEU A CB  1 
ATOM   5350 C  CG  . LEU A 1 678  ? 35.492 76.994  -38.499 1.00 19.52 ? 678  LEU A CG  1 
ATOM   5351 C  CD1 . LEU A 1 678  ? 36.036 77.196  -37.064 1.00 20.91 ? 678  LEU A CD1 1 
ATOM   5352 C  CD2 . LEU A 1 678  ? 36.317 77.819  -39.466 1.00 21.68 ? 678  LEU A CD2 1 
ATOM   5353 N  N   . ARG A 1 679  ? 36.557 73.289  -40.858 1.00 17.16 ? 679  ARG A N   1 
ATOM   5354 C  CA  . ARG A 1 679  ? 37.147 71.980  -40.957 1.00 18.89 ? 679  ARG A CA  1 
ATOM   5355 C  C   . ARG A 1 679  ? 38.675 72.111  -40.891 1.00 18.77 ? 679  ARG A C   1 
ATOM   5356 O  O   . ARG A 1 679  ? 39.269 72.853  -41.680 1.00 19.79 ? 679  ARG A O   1 
ATOM   5357 C  CB  . ARG A 1 679  ? 36.737 71.298  -42.266 1.00 20.05 ? 679  ARG A CB  1 
ATOM   5358 C  CG  . ARG A 1 679  ? 37.373 69.925  -42.405 1.00 23.27 ? 679  ARG A CG  1 
ATOM   5359 C  CD  . ARG A 1 679  ? 37.087 69.206  -43.726 1.00 25.88 ? 679  ARG A CD  1 
ATOM   5360 N  NE  . ARG A 1 679  ? 37.466 67.809  -43.520 1.00 29.20 ? 679  ARG A NE  1 
ATOM   5361 C  CZ  . ARG A 1 679  ? 37.566 66.871  -44.458 1.00 31.14 ? 679  ARG A CZ  1 
ATOM   5362 N  NH1 . ARG A 1 679  ? 37.314 67.149  -45.740 1.00 32.45 ? 679  ARG A NH1 1 
ATOM   5363 N  NH2 . ARG A 1 679  ? 37.936 65.642  -44.101 1.00 32.71 ? 679  ARG A NH2 1 
ATOM   5364 N  N   . VAL A 1 680  ? 39.318 71.415  -39.951 1.00 17.53 ? 680  VAL A N   1 
ATOM   5365 C  CA  . VAL A 1 680  ? 40.777 71.458  -39.894 1.00 17.31 ? 680  VAL A CA  1 
ATOM   5366 C  C   . VAL A 1 680  ? 41.304 70.094  -40.356 1.00 19.42 ? 680  VAL A C   1 
ATOM   5367 O  O   . VAL A 1 680  ? 40.740 69.032  -39.995 1.00 18.30 ? 680  VAL A O   1 
ATOM   5368 C  CB  . VAL A 1 680  ? 41.295 71.760  -38.472 1.00 16.93 ? 680  VAL A CB  1 
ATOM   5369 C  CG1 . VAL A 1 680  ? 42.800 71.596  -38.420 1.00 15.19 ? 680  VAL A CG1 1 
ATOM   5370 C  CG2 . VAL A 1 680  ? 40.925 73.199  -38.063 1.00 15.17 ? 680  VAL A CG2 1 
ATOM   5371 N  N   . GLY A 1 681  ? 42.381 70.123  -41.143 1.00 20.59 ? 681  GLY A N   1 
ATOM   5372 C  CA  . GLY A 1 681  ? 42.972 68.894  -41.653 1.00 23.11 ? 681  GLY A CA  1 
ATOM   5373 C  C   . GLY A 1 681  ? 41.923 68.053  -42.362 1.00 24.80 ? 681  GLY A C   1 
ATOM   5374 O  O   . GLY A 1 681  ? 41.110 68.583  -43.116 1.00 23.18 ? 681  GLY A O   1 
ATOM   5375 N  N   . ASN A 1 682  ? 41.943 66.741  -42.136 1.00 26.98 ? 682  ASN A N   1 
ATOM   5376 C  CA  . ASN A 1 682  ? 40.935 65.851  -42.730 1.00 29.28 ? 682  ASN A CA  1 
ATOM   5377 C  C   . ASN A 1 682  ? 39.931 65.540  -41.639 1.00 29.35 ? 682  ASN A C   1 
ATOM   5378 O  O   . ASN A 1 682  ? 39.078 64.669  -41.803 1.00 31.56 ? 682  ASN A O   1 
ATOM   5379 C  CB  . ASN A 1 682  ? 41.534 64.527  -43.159 1.00 30.87 ? 682  ASN A CB  1 
ATOM   5380 C  CG  . ASN A 1 682  ? 42.654 64.697  -44.103 1.00 34.17 ? 682  ASN A CG  1 
ATOM   5381 O  OD1 . ASN A 1 682  ? 42.534 65.410  -45.116 1.00 35.81 ? 682  ASN A OD1 1 
ATOM   5382 N  ND2 . ASN A 1 682  ? 43.777 64.049  -43.796 1.00 35.26 ? 682  ASN A ND2 1 
ATOM   5383 N  N   . GLY A 1 683  ? 40.044 66.253  -40.526 1.00 27.35 ? 683  GLY A N   1 
ATOM   5384 C  CA  . GLY A 1 683  ? 39.170 65.997  -39.402 1.00 24.88 ? 683  GLY A CA  1 
ATOM   5385 C  C   . GLY A 1 683  ? 37.708 66.200  -39.699 1.00 22.36 ? 683  GLY A C   1 
ATOM   5386 O  O   . GLY A 1 683  ? 37.298 66.321  -40.864 1.00 21.87 ? 683  GLY A O   1 
ATOM   5387 N  N   . PRO A 1 684  ? 36.889 66.238  -38.643 1.00 19.97 ? 684  PRO A N   1 
ATOM   5388 C  CA  . PRO A 1 684  ? 35.455 66.437  -38.845 1.00 19.26 ? 684  PRO A CA  1 
ATOM   5389 C  C   . PRO A 1 684  ? 35.171 67.881  -39.258 1.00 18.38 ? 684  PRO A C   1 
ATOM   5390 O  O   . PRO A 1 684  ? 36.031 68.752  -39.141 1.00 17.59 ? 684  PRO A O   1 
ATOM   5391 C  CB  . PRO A 1 684  ? 34.874 66.123  -37.475 1.00 18.91 ? 684  PRO A CB  1 
ATOM   5392 C  CG  . PRO A 1 684  ? 35.955 66.656  -36.528 1.00 18.78 ? 684  PRO A CG  1 
ATOM   5393 C  CD  . PRO A 1 684  ? 37.214 66.119  -37.209 1.00 20.19 ? 684  PRO A CD  1 
ATOM   5394 N  N   . THR A 1 685  ? 33.965 68.119  -39.765 1.00 18.07 ? 685  THR A N   1 
ATOM   5395 C  CA  . THR A 1 685  ? 33.563 69.466  -40.137 1.00 16.67 ? 685  THR A CA  1 
ATOM   5396 C  C   . THR A 1 685  ? 32.505 69.805  -39.104 1.00 16.48 ? 685  THR A C   1 
ATOM   5397 O  O   . THR A 1 685  ? 31.586 69.013  -38.854 1.00 15.86 ? 685  THR A O   1 
ATOM   5398 C  CB  . THR A 1 685  ? 32.952 69.514  -41.554 1.00 17.22 ? 685  THR A CB  1 
ATOM   5399 O  OG1 . THR A 1 685  ? 33.956 69.162  -42.507 1.00 16.59 ? 685  THR A OG1 1 
ATOM   5400 C  CG2 . THR A 1 685  ? 32.412 70.899  -41.852 1.00 16.22 ? 685  THR A CG2 1 
ATOM   5401 N  N   . LEU A 1 686  ? 32.641 70.978  -38.498 1.00 14.74 ? 686  LEU A N   1 
ATOM   5402 C  CA  . LEU A 1 686  ? 31.723 71.380  -37.468 1.00 14.74 ? 686  LEU A CA  1 
ATOM   5403 C  C   . LEU A 1 686  ? 30.960 72.624  -37.886 1.00 13.76 ? 686  LEU A C   1 
ATOM   5404 O  O   . LEU A 1 686  ? 31.543 73.551  -38.452 1.00 13.40 ? 686  LEU A O   1 
ATOM   5405 C  CB  . LEU A 1 686  ? 32.484 71.689  -36.174 1.00 15.05 ? 686  LEU A CB  1 
ATOM   5406 C  CG  . LEU A 1 686  ? 33.504 70.729  -35.565 1.00 18.48 ? 686  LEU A CG  1 
ATOM   5407 C  CD1 . LEU A 1 686  ? 33.739 71.186  -34.113 1.00 18.54 ? 686  LEU A CD1 1 
ATOM   5408 C  CD2 . LEU A 1 686  ? 33.067 69.311  -35.603 1.00 17.35 ? 686  LEU A CD2 1 
ATOM   5409 N  N   . ALA A 1 687  ? 29.671 72.642  -37.569 1.00 12.74 ? 687  ALA A N   1 
ATOM   5410 C  CA  . ALA A 1 687  ? 28.820 73.771  -37.885 1.00 14.21 ? 687  ALA A CA  1 
ATOM   5411 C  C   . ALA A 1 687  ? 28.381 74.430  -36.592 1.00 14.79 ? 687  ALA A C   1 
ATOM   5412 O  O   . ALA A 1 687  ? 28.026 73.751  -35.615 1.00 15.79 ? 687  ALA A O   1 
ATOM   5413 C  CB  . ALA A 1 687  ? 27.572 73.314  -38.704 1.00 14.79 ? 687  ALA A CB  1 
ATOM   5414 N  N   . PHE A 1 688  ? 28.394 75.759  -36.597 1.00 14.03 ? 688  PHE A N   1 
ATOM   5415 C  CA  . PHE A 1 688  ? 28.012 76.543  -35.448 1.00 12.58 ? 688  PHE A CA  1 
ATOM   5416 C  C   . PHE A 1 688  ? 26.847 77.468  -35.780 1.00 12.87 ? 688  PHE A C   1 
ATOM   5417 O  O   . PHE A 1 688  ? 26.684 77.907  -36.915 1.00 13.88 ? 688  PHE A O   1 
ATOM   5418 C  CB  . PHE A 1 688  ? 29.190 77.413  -34.980 1.00 12.98 ? 688  PHE A CB  1 
ATOM   5419 C  CG  . PHE A 1 688  ? 30.425 76.641  -34.656 1.00 11.39 ? 688  PHE A CG  1 
ATOM   5420 C  CD1 . PHE A 1 688  ? 31.238 76.144  -35.676 1.00 11.52 ? 688  PHE A CD1 1 
ATOM   5421 C  CD2 . PHE A 1 688  ? 30.757 76.383  -33.338 1.00 11.02 ? 688  PHE A CD2 1 
ATOM   5422 C  CE1 . PHE A 1 688  ? 32.367 75.397  -35.394 1.00 11.95 ? 688  PHE A CE1 1 
ATOM   5423 C  CE2 . PHE A 1 688  ? 31.893 75.634  -33.030 1.00 11.76 ? 688  PHE A CE2 1 
ATOM   5424 C  CZ  . PHE A 1 688  ? 32.707 75.135  -34.058 1.00 9.96  ? 688  PHE A CZ  1 
ATOM   5425 N  N   . SER A 1 689  ? 26.062 77.782  -34.765 1.00 13.22 ? 689  SER A N   1 
ATOM   5426 C  CA  . SER A 1 689  ? 24.934 78.680  -34.913 1.00 14.88 ? 689  SER A CA  1 
ATOM   5427 C  C   . SER A 1 689  ? 25.506 80.100  -34.891 1.00 14.83 ? 689  SER A C   1 
ATOM   5428 O  O   . SER A 1 689  ? 26.688 80.307  -34.594 1.00 13.21 ? 689  SER A O   1 
ATOM   5429 C  CB  . SER A 1 689  ? 23.970 78.518  -33.751 1.00 13.26 ? 689  SER A CB  1 
ATOM   5430 O  OG  . SER A 1 689  ? 24.565 79.027  -32.587 1.00 16.24 ? 689  SER A OG  1 
ATOM   5431 N  N   . GLU A 1 690  ? 24.655 81.069  -35.194 1.00 15.69 ? 690  GLU A N   1 
ATOM   5432 C  CA  . GLU A 1 690  ? 25.106 82.437  -35.225 1.00 17.73 ? 690  GLU A CA  1 
ATOM   5433 C  C   . GLU A 1 690  ? 25.475 82.944  -33.832 1.00 17.89 ? 690  GLU A C   1 
ATOM   5434 O  O   . GLU A 1 690  ? 25.974 84.063  -33.696 1.00 17.24 ? 690  GLU A O   1 
ATOM   5435 C  CB  . GLU A 1 690  ? 24.053 83.319  -35.904 1.00 20.00 ? 690  GLU A CB  1 
ATOM   5436 C  CG  . GLU A 1 690  ? 22.872 83.680  -35.083 1.00 23.41 ? 690  GLU A CG  1 
ATOM   5437 C  CD  . GLU A 1 690  ? 21.978 84.681  -35.834 1.00 27.04 ? 690  GLU A CD  1 
ATOM   5438 O  OE1 . GLU A 1 690  ? 21.388 84.291  -36.862 1.00 28.10 ? 690  GLU A OE1 1 
ATOM   5439 O  OE2 . GLU A 1 690  ? 21.882 85.861  -35.405 1.00 28.80 ? 690  GLU A OE2 1 
ATOM   5440 N  N   . GLN A 1 691  ? 25.214 82.133  -32.800 1.00 17.14 ? 691  GLN A N   1 
ATOM   5441 C  CA  . GLN A 1 691  ? 25.628 82.504  -31.444 1.00 16.93 ? 691  GLN A CA  1 
ATOM   5442 C  C   . GLN A 1 691  ? 26.946 81.825  -31.062 1.00 15.42 ? 691  GLN A C   1 
ATOM   5443 O  O   . GLN A 1 691  ? 27.343 81.835  -29.904 1.00 15.57 ? 691  GLN A O   1 
ATOM   5444 C  CB  . GLN A 1 691  ? 24.591 82.127  -30.412 1.00 20.53 ? 691  GLN A CB  1 
ATOM   5445 C  CG  . GLN A 1 691  ? 23.456 83.078  -30.384 1.00 25.76 ? 691  GLN A CG  1 
ATOM   5446 C  CD  . GLN A 1 691  ? 22.193 82.327  -30.474 1.00 29.86 ? 691  GLN A CD  1 
ATOM   5447 O  OE1 . GLN A 1 691  ? 21.579 81.984  -29.449 1.00 32.00 ? 691  GLN A OE1 1 
ATOM   5448 N  NE2 . GLN A 1 691  ? 21.794 82.008  -31.700 1.00 32.67 ? 691  GLN A NE2 1 
ATOM   5449 N  N   . GLY A 1 692  ? 27.614 81.226  -32.032 1.00 13.02 ? 692  GLY A N   1 
ATOM   5450 C  CA  . GLY A 1 692  ? 28.900 80.615  -31.754 1.00 14.70 ? 692  GLY A CA  1 
ATOM   5451 C  C   . GLY A 1 692  ? 28.858 79.275  -31.050 1.00 14.97 ? 692  GLY A C   1 
ATOM   5452 O  O   . GLY A 1 692  ? 29.885 78.818  -30.543 1.00 16.58 ? 692  GLY A O   1 
ATOM   5453 N  N   . LEU A 1 693  ? 27.692 78.635  -31.037 1.00 14.91 ? 693  LEU A N   1 
ATOM   5454 C  CA  . LEU A 1 693  ? 27.571 77.322  -30.386 1.00 14.74 ? 693  LEU A CA  1 
ATOM   5455 C  C   . LEU A 1 693  ? 27.481 76.183  -31.375 1.00 14.99 ? 693  LEU A C   1 
ATOM   5456 O  O   . LEU A 1 693  ? 26.830 76.297  -32.427 1.00 12.92 ? 693  LEU A O   1 
ATOM   5457 C  CB  . LEU A 1 693  ? 26.346 77.314  -29.478 1.00 15.42 ? 693  LEU A CB  1 
ATOM   5458 C  CG  . LEU A 1 693  ? 26.515 78.275  -28.294 1.00 15.96 ? 693  LEU A CG  1 
ATOM   5459 C  CD1 . LEU A 1 693  ? 25.139 78.787  -27.853 1.00 18.38 ? 693  LEU A CD1 1 
ATOM   5460 C  CD2 . LEU A 1 693  ? 27.230 77.584  -27.159 1.00 14.43 ? 693  LEU A CD2 1 
ATOM   5461 N  N   . LEU A 1 694  ? 28.123 75.069  -31.045 1.00 14.24 ? 694  LEU A N   1 
ATOM   5462 C  CA  . LEU A 1 694  ? 28.102 73.928  -31.942 1.00 13.65 ? 694  LEU A CA  1 
ATOM   5463 C  C   . LEU A 1 694  ? 26.655 73.567  -32.280 1.00 14.60 ? 694  LEU A C   1 
ATOM   5464 O  O   . LEU A 1 694  ? 25.769 73.629  -31.428 1.00 12.83 ? 694  LEU A O   1 
ATOM   5465 C  CB  . LEU A 1 694  ? 28.793 72.722  -31.292 1.00 14.70 ? 694  LEU A CB  1 
ATOM   5466 C  CG  . LEU A 1 694  ? 28.930 71.448  -32.142 1.00 14.01 ? 694  LEU A CG  1 
ATOM   5467 C  CD1 . LEU A 1 694  ? 29.833 71.708  -33.336 1.00 14.19 ? 694  LEU A CD1 1 
ATOM   5468 C  CD2 . LEU A 1 694  ? 29.518 70.311  -31.277 1.00 13.40 ? 694  LEU A CD2 1 
ATOM   5469 N  N   . LYS A 1 695  ? 26.465 73.162  -33.529 1.00 15.63 ? 695  LYS A N   1 
ATOM   5470 C  CA  . LYS A 1 695  ? 25.170 72.788  -34.084 1.00 17.60 ? 695  LYS A CA  1 
ATOM   5471 C  C   . LYS A 1 695  ? 25.237 71.371  -34.675 1.00 16.14 ? 695  LYS A C   1 
ATOM   5472 O  O   . LYS A 1 695  ? 24.300 70.599  -34.577 1.00 16.63 ? 695  LYS A O   1 
ATOM   5473 C  CB  . LYS A 1 695  ? 24.843 73.801  -35.193 1.00 20.55 ? 695  LYS A CB  1 
ATOM   5474 C  CG  . LYS A 1 695  ? 23.551 73.654  -35.855 1.00 26.10 ? 695  LYS A CG  1 
ATOM   5475 C  CD  . LYS A 1 695  ? 23.314 74.820  -36.846 1.00 28.65 ? 695  LYS A CD  1 
ATOM   5476 C  CE  . LYS A 1 695  ? 21.970 74.621  -37.566 1.00 31.17 ? 695  LYS A CE  1 
ATOM   5477 N  NZ  . LYS A 1 695  ? 21.631 75.668  -38.593 1.00 32.10 ? 695  LYS A NZ  1 
ATOM   5478 N  N   . SER A 1 696  ? 26.339 71.029  -35.314 1.00 16.46 ? 696  SER A N   1 
ATOM   5479 C  CA  . SER A 1 696  ? 26.429 69.705  -35.913 1.00 16.20 ? 696  SER A CA  1 
ATOM   5480 C  C   . SER A 1 696  ? 27.857 69.293  -36.170 1.00 16.60 ? 696  SER A C   1 
ATOM   5481 O  O   . SER A 1 696  ? 28.750 70.128  -36.284 1.00 16.98 ? 696  SER A O   1 
ATOM   5482 C  CB  . SER A 1 696  ? 25.655 69.682  -37.239 1.00 16.52 ? 696  SER A CB  1 
ATOM   5483 O  OG  . SER A 1 696  ? 26.305 70.455  -38.235 1.00 16.45 ? 696  SER A OG  1 
ATOM   5484 N  N   . ILE A 1 697  ? 28.061 67.989  -36.296 1.00 16.53 ? 697  ILE A N   1 
ATOM   5485 C  CA  . ILE A 1 697  ? 29.379 67.435  -36.562 1.00 16.57 ? 697  ILE A CA  1 
ATOM   5486 C  C   . ILE A 1 697  ? 29.267 66.486  -37.748 1.00 18.46 ? 697  ILE A C   1 
ATOM   5487 O  O   . ILE A 1 697  ? 28.372 65.604  -37.783 1.00 18.15 ? 697  ILE A O   1 
ATOM   5488 C  CB  . ILE A 1 697  ? 29.914 66.615  -35.370 1.00 15.47 ? 697  ILE A CB  1 
ATOM   5489 C  CG1 . ILE A 1 697  ? 30.015 67.499  -34.119 1.00 15.22 ? 697  ILE A CG1 1 
ATOM   5490 C  CG2 . ILE A 1 697  ? 31.266 66.007  -35.719 1.00 15.06 ? 697  ILE A CG2 1 
ATOM   5491 C  CD1 . ILE A 1 697  ? 30.491 66.759  -32.824 1.00 13.69 ? 697  ILE A CD1 1 
ATOM   5492 N  N   . GLN A 1 698  ? 30.143 66.677  -38.727 1.00 18.86 ? 698  GLN A N   1 
ATOM   5493 C  CA  . GLN A 1 698  ? 30.166 65.806  -39.885 1.00 20.43 ? 698  GLN A CA  1 
ATOM   5494 C  C   . GLN A 1 698  ? 31.505 65.100  -39.852 1.00 20.41 ? 698  GLN A C   1 
ATOM   5495 O  O   . GLN A 1 698  ? 32.551 65.717  -40.076 1.00 20.43 ? 698  GLN A O   1 
ATOM   5496 C  CB  . GLN A 1 698  ? 30.033 66.602  -41.189 1.00 21.43 ? 698  GLN A CB  1 
ATOM   5497 C  CG  . GLN A 1 698  ? 29.923 65.681  -42.399 1.00 23.21 ? 698  GLN A CG  1 
ATOM   5498 C  CD  . GLN A 1 698  ? 30.173 66.423  -43.708 1.00 25.72 ? 698  GLN A CD  1 
ATOM   5499 O  OE1 . GLN A 1 698  ? 31.065 67.262  -43.786 1.00 25.84 ? 698  GLN A OE1 1 
ATOM   5500 N  NE2 . GLN A 1 698  ? 29.399 66.102  -44.738 1.00 25.64 ? 698  GLN A NE2 1 
ATOM   5501 N  N   . LEU A 1 699  ? 31.483 63.803  -39.588 1.00 21.02 ? 699  LEU A N   1 
ATOM   5502 C  CA  . LEU A 1 699  ? 32.718 63.047  -39.467 1.00 23.14 ? 699  LEU A CA  1 
ATOM   5503 C  C   . LEU A 1 699  ? 33.586 62.985  -40.712 1.00 24.83 ? 699  LEU A C   1 
ATOM   5504 O  O   . LEU A 1 699  ? 34.801 63.167  -40.632 1.00 24.92 ? 699  LEU A O   1 
ATOM   5505 C  CB  . LEU A 1 699  ? 32.416 61.620  -38.980 1.00 23.08 ? 699  LEU A CB  1 
ATOM   5506 C  CG  . LEU A 1 699  ? 31.743 61.519  -37.600 1.00 23.32 ? 699  LEU A CG  1 
ATOM   5507 C  CD1 . LEU A 1 699  ? 31.608 60.068  -37.199 1.00 23.29 ? 699  LEU A CD1 1 
ATOM   5508 C  CD2 . LEU A 1 699  ? 32.565 62.249  -36.567 1.00 22.49 ? 699  LEU A CD2 1 
ATOM   5509 N  N   . THR A 1 700  ? 32.970 62.741  -41.860 1.00 26.53 ? 700  THR A N   1 
ATOM   5510 C  CA  . THR A 1 700  ? 33.722 62.617  -43.104 1.00 29.83 ? 700  THR A CA  1 
ATOM   5511 C  C   . THR A 1 700  ? 33.078 63.420  -44.218 1.00 31.84 ? 700  THR A C   1 
ATOM   5512 O  O   . THR A 1 700  ? 31.948 63.859  -44.092 1.00 32.05 ? 700  THR A O   1 
ATOM   5513 C  CB  . THR A 1 700  ? 33.799 61.132  -43.565 1.00 28.95 ? 700  THR A CB  1 
ATOM   5514 O  OG1 . THR A 1 700  ? 32.468 60.608  -43.728 1.00 29.14 ? 700  THR A OG1 1 
ATOM   5515 C  CG2 . THR A 1 700  ? 34.529 60.291  -42.540 1.00 29.08 ? 700  THR A CG2 1 
ATOM   5516 N  N   . GLN A 1 701  ? 33.820 63.594  -45.309 1.00 35.98 ? 701  GLN A N   1 
ATOM   5517 C  CA  . GLN A 1 701  ? 33.356 64.324  -46.491 1.00 39.26 ? 701  GLN A CA  1 
ATOM   5518 C  C   . GLN A 1 701  ? 31.910 64.034  -46.849 1.00 40.41 ? 701  GLN A C   1 
ATOM   5519 O  O   . GLN A 1 701  ? 31.101 64.957  -47.006 1.00 40.90 ? 701  GLN A O   1 
ATOM   5520 C  CB  . GLN A 1 701  ? 34.231 63.972  -47.704 1.00 41.31 ? 701  GLN A CB  1 
ATOM   5521 C  CG  . GLN A 1 701  ? 35.521 64.763  -47.798 1.00 43.97 ? 701  GLN A CG  1 
ATOM   5522 C  CD  . GLN A 1 701  ? 35.256 66.233  -48.087 1.00 46.15 ? 701  GLN A CD  1 
ATOM   5523 O  OE1 . GLN A 1 701  ? 36.185 67.040  -48.207 1.00 46.37 ? 701  GLN A OE1 1 
ATOM   5524 N  NE2 . GLN A 1 701  ? 33.973 66.589  -48.201 1.00 47.36 ? 701  GLN A NE2 1 
ATOM   5525 N  N   . ASP A 1 702  ? 31.596 62.747  -46.965 1.00 41.94 ? 702  ASP A N   1 
ATOM   5526 C  CA  . ASP A 1 702  ? 30.260 62.281  -47.343 1.00 44.02 ? 702  ASP A CA  1 
ATOM   5527 C  C   . ASP A 1 702  ? 29.181 62.218  -46.246 1.00 43.38 ? 702  ASP A C   1 
ATOM   5528 O  O   . ASP A 1 702  ? 28.040 62.671  -46.455 1.00 43.58 ? 702  ASP A O   1 
ATOM   5529 C  CB  . ASP A 1 702  ? 30.382 60.896  -47.995 1.00 47.20 ? 702  ASP A CB  1 
ATOM   5530 C  CG  . ASP A 1 702  ? 30.907 59.823  -47.025 1.00 50.50 ? 702  ASP A CG  1 
ATOM   5531 O  OD1 . ASP A 1 702  ? 32.073 59.945  -46.548 1.00 52.03 ? 702  ASP A OD1 1 
ATOM   5532 O  OD2 . ASP A 1 702  ? 30.147 58.857  -46.744 1.00 52.06 ? 702  ASP A OD2 1 
ATOM   5533 N  N   . SER A 1 703  ? 29.557 61.655  -45.093 1.00 42.02 ? 703  SER A N   1 
ATOM   5534 C  CA  . SER A 1 703  ? 28.659 61.475  -43.951 1.00 39.76 ? 703  SER A CA  1 
ATOM   5535 C  C   . SER A 1 703  ? 27.734 62.649  -43.669 1.00 38.70 ? 703  SER A C   1 
ATOM   5536 O  O   . SER A 1 703  ? 27.972 63.761  -44.115 1.00 38.48 ? 703  SER A O   1 
ATOM   5537 C  CB  . SER A 1 703  ? 29.473 61.153  -42.685 1.00 40.33 ? 703  SER A CB  1 
ATOM   5538 O  OG  . SER A 1 703  ? 30.330 62.226  -42.308 1.00 38.25 ? 703  SER A OG  1 
ATOM   5539 N  N   . PRO A 1 704  ? 26.643 62.400  -42.931 1.00 36.76 ? 704  PRO A N   1 
ATOM   5540 C  CA  . PRO A 1 704  ? 25.715 63.484  -42.614 1.00 35.56 ? 704  PRO A CA  1 
ATOM   5541 C  C   . PRO A 1 704  ? 26.231 64.416  -41.521 1.00 33.65 ? 704  PRO A C   1 
ATOM   5542 O  O   . PRO A 1 704  ? 27.199 64.103  -40.819 1.00 31.63 ? 704  PRO A O   1 
ATOM   5543 C  CB  . PRO A 1 704  ? 24.453 62.744  -42.170 1.00 36.06 ? 704  PRO A CB  1 
ATOM   5544 C  CG  . PRO A 1 704  ? 24.985 61.487  -41.573 1.00 36.70 ? 704  PRO A CG  1 
ATOM   5545 C  CD  . PRO A 1 704  ? 26.090 61.092  -42.529 1.00 36.41 ? 704  PRO A CD  1 
ATOM   5546 N  N   . HIS A 1 705  ? 25.574 65.570  -41.420 1.00 31.63 ? 705  HIS A N   1 
ATOM   5547 C  CA  . HIS A 1 705  ? 25.868 66.567  -40.405 1.00 28.84 ? 705  HIS A CA  1 
ATOM   5548 C  C   . HIS A 1 705  ? 25.029 66.123  -39.220 1.00 26.19 ? 705  HIS A C   1 
ATOM   5549 O  O   . HIS A 1 705  ? 23.848 66.422  -39.135 1.00 25.50 ? 705  HIS A O   1 
ATOM   5550 C  CB  . HIS A 1 705  ? 25.435 67.957  -40.887 1.00 31.13 ? 705  HIS A CB  1 
ATOM   5551 C  CG  . HIS A 1 705  ? 26.280 68.480  -42.004 1.00 33.15 ? 705  HIS A CG  1 
ATOM   5552 N  ND1 . HIS A 1 705  ? 27.518 69.045  -41.790 1.00 33.02 ? 705  HIS A ND1 1 
ATOM   5553 C  CD2 . HIS A 1 705  ? 26.139 68.385  -43.349 1.00 34.19 ? 705  HIS A CD2 1 
ATOM   5554 C  CE1 . HIS A 1 705  ? 28.108 69.264  -42.951 1.00 34.66 ? 705  HIS A CE1 1 
ATOM   5555 N  NE2 . HIS A 1 705  ? 27.293 68.871  -43.915 1.00 35.29 ? 705  HIS A NE2 1 
ATOM   5556 N  N   . VAL A 1 706  ? 25.653 65.391  -38.304 1.00 23.61 ? 706  VAL A N   1 
ATOM   5557 C  CA  . VAL A 1 706  ? 24.958 64.883  -37.127 1.00 20.79 ? 706  VAL A CA  1 
ATOM   5558 C  C   . VAL A 1 706  ? 24.621 65.978  -36.126 1.00 20.57 ? 706  VAL A C   1 
ATOM   5559 O  O   . VAL A 1 706  ? 25.517 66.617  -35.600 1.00 20.89 ? 706  VAL A O   1 
ATOM   5560 C  CB  . VAL A 1 706  ? 25.835 63.859  -36.405 1.00 20.23 ? 706  VAL A CB  1 
ATOM   5561 C  CG1 . VAL A 1 706  ? 25.098 63.298  -35.204 1.00 19.23 ? 706  VAL A CG1 1 
ATOM   5562 C  CG2 . VAL A 1 706  ? 26.283 62.790  -37.377 1.00 18.95 ? 706  VAL A CG2 1 
ATOM   5563 N  N   . PRO A 1 707  ? 23.328 66.186  -35.828 1.00 19.87 ? 707  PRO A N   1 
ATOM   5564 C  CA  . PRO A 1 707  ? 22.885 67.209  -34.871 1.00 19.56 ? 707  PRO A CA  1 
ATOM   5565 C  C   . PRO A 1 707  ? 23.526 67.065  -33.473 1.00 19.16 ? 707  PRO A C   1 
ATOM   5566 O  O   . PRO A 1 707  ? 23.207 66.120  -32.749 1.00 18.01 ? 707  PRO A O   1 
ATOM   5567 C  CB  . PRO A 1 707  ? 21.375 66.970  -34.775 1.00 20.36 ? 707  PRO A CB  1 
ATOM   5568 C  CG  . PRO A 1 707  ? 21.024 66.318  -36.075 1.00 20.24 ? 707  PRO A CG  1 
ATOM   5569 C  CD  . PRO A 1 707  ? 22.182 65.405  -36.341 1.00 19.91 ? 707  PRO A CD  1 
ATOM   5570 N  N   . VAL A 1 708  ? 24.395 68.010  -33.093 1.00 17.77 ? 708  VAL A N   1 
ATOM   5571 C  CA  . VAL A 1 708  ? 25.040 68.003  -31.768 1.00 15.07 ? 708  VAL A CA  1 
ATOM   5572 C  C   . VAL A 1 708  ? 25.016 69.478  -31.364 1.00 16.20 ? 708  VAL A C   1 
ATOM   5573 O  O   . VAL A 1 708  ? 25.742 70.298  -31.912 1.00 13.97 ? 708  VAL A O   1 
ATOM   5574 C  CB  . VAL A 1 708  ? 26.493 67.474  -31.843 1.00 13.86 ? 708  VAL A CB  1 
ATOM   5575 C  CG1 . VAL A 1 708  ? 27.146 67.497  -30.436 1.00 13.43 ? 708  VAL A CG1 1 
ATOM   5576 C  CG2 . VAL A 1 708  ? 26.506 66.048  -32.415 1.00 11.89 ? 708  VAL A CG2 1 
ATOM   5577 N  N   . HIS A 1 709  ? 24.168 69.823  -30.414 1.00 16.37 ? 709  HIS A N   1 
ATOM   5578 C  CA  . HIS A 1 709  ? 24.036 71.228  -30.051 1.00 17.55 ? 709  HIS A CA  1 
ATOM   5579 C  C   . HIS A 1 709  ? 24.468 71.508  -28.610 1.00 16.07 ? 709  HIS A C   1 
ATOM   5580 O  O   . HIS A 1 709  ? 24.044 70.798  -27.698 1.00 15.81 ? 709  HIS A O   1 
ATOM   5581 C  CB  . HIS A 1 709  ? 22.562 71.691  -30.166 1.00 20.05 ? 709  HIS A CB  1 
ATOM   5582 C  CG  . HIS A 1 709  ? 22.010 71.766  -31.564 1.00 24.56 ? 709  HIS A CG  1 
ATOM   5583 N  ND1 . HIS A 1 709  ? 21.850 70.660  -32.376 1.00 27.74 ? 709  HIS A ND1 1 
ATOM   5584 C  CD2 . HIS A 1 709  ? 21.474 72.810  -32.252 1.00 26.72 ? 709  HIS A CD2 1 
ATOM   5585 C  CE1 . HIS A 1 709  ? 21.240 71.014  -33.495 1.00 26.42 ? 709  HIS A CE1 1 
ATOM   5586 N  NE2 . HIS A 1 709  ? 21.000 72.315  -33.444 1.00 28.20 ? 709  HIS A NE2 1 
ATOM   5587 N  N   . PHE A 1 710  ? 25.280 72.543  -28.413 1.00 13.52 ? 710  PHE A N   1 
ATOM   5588 C  CA  . PHE A 1 710  ? 25.685 72.946  -27.072 1.00 12.67 ? 710  PHE A CA  1 
ATOM   5589 C  C   . PHE A 1 710  ? 24.677 74.023  -26.655 1.00 12.51 ? 710  PHE A C   1 
ATOM   5590 O  O   . PHE A 1 710  ? 24.269 74.865  -27.482 1.00 11.61 ? 710  PHE A O   1 
ATOM   5591 C  CB  . PHE A 1 710  ? 27.096 73.553  -27.062 1.00 12.59 ? 710  PHE A CB  1 
ATOM   5592 C  CG  . PHE A 1 710  ? 28.201 72.569  -26.682 1.00 13.82 ? 710  PHE A CG  1 
ATOM   5593 C  CD1 . PHE A 1 710  ? 29.272 72.347  -27.530 1.00 14.63 ? 710  PHE A CD1 1 
ATOM   5594 C  CD2 . PHE A 1 710  ? 28.180 71.915  -25.463 1.00 12.83 ? 710  PHE A CD2 1 
ATOM   5595 C  CE1 . PHE A 1 710  ? 30.323 71.483  -27.170 1.00 14.05 ? 710  PHE A CE1 1 
ATOM   5596 C  CE2 . PHE A 1 710  ? 29.207 71.059  -25.093 1.00 13.34 ? 710  PHE A CE2 1 
ATOM   5597 C  CZ  . PHE A 1 710  ? 30.287 70.843  -25.951 1.00 12.91 ? 710  PHE A CZ  1 
ATOM   5598 N  N   . LYS A 1 711  ? 24.273 73.996  -25.391 1.00 10.26 ? 711  LYS A N   1 
ATOM   5599 C  CA  . LYS A 1 711  ? 23.328 74.984  -24.872 1.00 13.07 ? 711  LYS A CA  1 
ATOM   5600 C  C   . LYS A 1 711  ? 23.719 75.205  -23.425 1.00 12.53 ? 711  LYS A C   1 
ATOM   5601 O  O   . LYS A 1 711  ? 24.193 74.268  -22.778 1.00 12.85 ? 711  LYS A O   1 
ATOM   5602 C  CB  . LYS A 1 711  ? 21.903 74.435  -24.890 1.00 14.90 ? 711  LYS A CB  1 
ATOM   5603 C  CG  . LYS A 1 711  ? 20.857 75.434  -24.395 1.00 20.17 ? 711  LYS A CG  1 
ATOM   5604 C  CD  . LYS A 1 711  ? 19.434 74.841  -24.514 1.00 22.60 ? 711  LYS A CD  1 
ATOM   5605 C  CE  . LYS A 1 711  ? 19.039 74.606  -25.971 1.00 23.40 ? 711  LYS A CE  1 
ATOM   5606 N  NZ  . LYS A 1 711  ? 17.787 73.752  -26.043 1.00 25.51 ? 711  LYS A NZ  1 
ATOM   5607 N  N   . PHE A 1 712  ? 23.519 76.419  -22.920 1.00 9.98  ? 712  PHE A N   1 
ATOM   5608 C  CA  . PHE A 1 712  ? 23.833 76.723  -21.541 1.00 10.34 ? 712  PHE A CA  1 
ATOM   5609 C  C   . PHE A 1 712  ? 22.554 77.073  -20.828 1.00 10.51 ? 712  PHE A C   1 
ATOM   5610 O  O   . PHE A 1 712  ? 21.716 77.835  -21.350 1.00 9.28  ? 712  PHE A O   1 
ATOM   5611 C  CB  . PHE A 1 712  ? 24.835 77.890  -21.442 1.00 10.95 ? 712  PHE A CB  1 
ATOM   5612 C  CG  . PHE A 1 712  ? 26.246 77.482  -21.749 1.00 10.51 ? 712  PHE A CG  1 
ATOM   5613 C  CD1 . PHE A 1 712  ? 26.733 77.533  -23.049 1.00 9.65  ? 712  PHE A CD1 1 
ATOM   5614 C  CD2 . PHE A 1 712  ? 27.072 76.991  -20.733 1.00 10.46 ? 712  PHE A CD2 1 
ATOM   5615 C  CE1 . PHE A 1 712  ? 28.017 77.099  -23.333 1.00 10.94 ? 712  PHE A CE1 1 
ATOM   5616 C  CE2 . PHE A 1 712  ? 28.346 76.562  -21.007 1.00 9.86  ? 712  PHE A CE2 1 
ATOM   5617 C  CZ  . PHE A 1 712  ? 28.823 76.611  -22.307 1.00 9.77  ? 712  PHE A CZ  1 
ATOM   5618 N  N   . LEU A 1 713  ? 22.380 76.494  -19.647 1.00 10.73 ? 713  LEU A N   1 
ATOM   5619 C  CA  . LEU A 1 713  ? 21.178 76.743  -18.866 1.00 12.13 ? 713  LEU A CA  1 
ATOM   5620 C  C   . LEU A 1 713  ? 21.493 77.050  -17.410 1.00 13.06 ? 713  LEU A C   1 
ATOM   5621 O  O   . LEU A 1 713  ? 22.663 77.009  -16.988 1.00 13.82 ? 713  LEU A O   1 
ATOM   5622 C  CB  . LEU A 1 713  ? 20.221 75.541  -18.975 1.00 11.08 ? 713  LEU A CB  1 
ATOM   5623 C  CG  . LEU A 1 713  ? 19.841 75.132  -20.403 1.00 11.50 ? 713  LEU A CG  1 
ATOM   5624 C  CD1 . LEU A 1 713  ? 20.817 74.064  -20.891 1.00 13.15 ? 713  LEU A CD1 1 
ATOM   5625 C  CD2 . LEU A 1 713  ? 18.389 74.559  -20.436 1.00 12.30 ? 713  LEU A CD2 1 
ATOM   5626 N  N   . LYS A 1 714  ? 20.468 77.403  -16.642 1.00 13.05 ? 714  LYS A N   1 
ATOM   5627 C  CA  . LYS A 1 714  ? 20.662 77.684  -15.239 1.00 15.98 ? 714  LYS A CA  1 
ATOM   5628 C  C   . LYS A 1 714  ? 19.579 77.067  -14.357 1.00 16.14 ? 714  LYS A C   1 
ATOM   5629 O  O   . LYS A 1 714  ? 18.388 77.070  -14.703 1.00 16.36 ? 714  LYS A O   1 
ATOM   5630 C  CB  . LYS A 1 714  ? 20.751 79.209  -14.971 1.00 19.05 ? 714  LYS A CB  1 
ATOM   5631 C  CG  . LYS A 1 714  ? 19.681 80.052  -15.661 1.00 24.20 ? 714  LYS A CG  1 
ATOM   5632 C  CD  . LYS A 1 714  ? 19.695 81.560  -15.256 1.00 28.52 ? 714  LYS A CD  1 
ATOM   5633 C  CE  . LYS A 1 714  ? 21.042 82.273  -15.502 1.00 31.48 ? 714  LYS A CE  1 
ATOM   5634 N  NZ  . LYS A 1 714  ? 20.996 83.763  -15.248 1.00 33.14 ? 714  LYS A NZ  1 
ATOM   5635 N  N   . TYR A 1 715  ? 20.030 76.506  -13.227 1.00 14.61 ? 715  TYR A N   1 
ATOM   5636 C  CA  . TYR A 1 715  ? 19.160 75.931  -12.227 1.00 14.46 ? 715  TYR A CA  1 
ATOM   5637 C  C   . TYR A 1 715  ? 19.100 76.971  -11.137 1.00 14.80 ? 715  TYR A C   1 
ATOM   5638 O  O   . TYR A 1 715  ? 20.066 77.714  -10.928 1.00 15.02 ? 715  TYR A O   1 
ATOM   5639 C  CB  . TYR A 1 715  ? 19.760 74.657  -11.610 1.00 14.41 ? 715  TYR A CB  1 
ATOM   5640 C  CG  . TYR A 1 715  ? 19.674 73.446  -12.500 1.00 13.16 ? 715  TYR A CG  1 
ATOM   5641 C  CD1 . TYR A 1 715  ? 20.786 72.998  -13.230 1.00 13.14 ? 715  TYR A CD1 1 
ATOM   5642 C  CD2 . TYR A 1 715  ? 18.470 72.731  -12.605 1.00 12.60 ? 715  TYR A CD2 1 
ATOM   5643 C  CE1 . TYR A 1 715  ? 20.700 71.839  -14.058 1.00 11.75 ? 715  TYR A CE1 1 
ATOM   5644 C  CE2 . TYR A 1 715  ? 18.375 71.603  -13.417 1.00 12.41 ? 715  TYR A CE2 1 
ATOM   5645 C  CZ  . TYR A 1 715  ? 19.483 71.160  -14.135 1.00 12.57 ? 715  TYR A CZ  1 
ATOM   5646 O  OH  . TYR A 1 715  ? 19.354 70.040  -14.917 1.00 10.04 ? 715  TYR A OH  1 
ATOM   5647 N  N   . GLY A 1 716  ? 17.978 77.016  -10.438 1.00 15.50 ? 716  GLY A N   1 
ATOM   5648 C  CA  . GLY A 1 716  ? 17.809 77.949  -9.334  1.00 14.39 ? 716  GLY A CA  1 
ATOM   5649 C  C   . GLY A 1 716  ? 17.790 77.207  -8.004  1.00 16.63 ? 716  GLY A C   1 
ATOM   5650 O  O   . GLY A 1 716  ? 18.230 76.045  -7.881  1.00 15.79 ? 716  GLY A O   1 
ATOM   5651 N  N   . VAL A 1 717  ? 17.272 77.887  -6.991  1.00 16.89 ? 717  VAL A N   1 
ATOM   5652 C  CA  . VAL A 1 717  ? 17.164 77.341  -5.646  1.00 18.05 ? 717  VAL A CA  1 
ATOM   5653 C  C   . VAL A 1 717  ? 15.701 77.499  -5.210  1.00 19.55 ? 717  VAL A C   1 
ATOM   5654 O  O   . VAL A 1 717  ? 15.020 78.426  -5.646  1.00 19.04 ? 717  VAL A O   1 
ATOM   5655 C  CB  . VAL A 1 717  ? 18.075 78.112  -4.702  1.00 18.40 ? 717  VAL A CB  1 
ATOM   5656 C  CG1 . VAL A 1 717  ? 17.813 77.701  -3.276  1.00 20.41 ? 717  VAL A CG1 1 
ATOM   5657 C  CG2 . VAL A 1 717  ? 19.557 77.865  -5.099  1.00 18.48 ? 717  VAL A CG2 1 
ATOM   5658 N  N   . ARG A 1 718  ? 15.217 76.600  -4.362  1.00 20.04 ? 718  ARG A N   1 
ATOM   5659 C  CA  . ARG A 1 718  ? 13.823 76.668  -3.910  1.00 21.70 ? 718  ARG A CA  1 
ATOM   5660 C  C   . ARG A 1 718  ? 13.557 77.841  -2.968  1.00 23.58 ? 718  ARG A C   1 
ATOM   5661 O  O   . ARG A 1 718  ? 14.343 78.082  -2.066  1.00 23.06 ? 718  ARG A O   1 
ATOM   5662 C  CB  . ARG A 1 718  ? 13.449 75.362  -3.203  1.00 20.09 ? 718  ARG A CB  1 
ATOM   5663 C  CG  . ARG A 1 718  ? 13.539 74.184  -4.118  1.00 18.63 ? 718  ARG A CG  1 
ATOM   5664 C  CD  . ARG A 1 718  ? 13.456 72.828  -3.422  1.00 16.62 ? 718  ARG A CD  1 
ATOM   5665 N  NE  . ARG A 1 718  ? 13.716 71.795  -4.425  1.00 15.49 ? 718  ARG A NE  1 
ATOM   5666 C  CZ  . ARG A 1 718  ? 13.735 70.485  -4.194  1.00 15.04 ? 718  ARG A CZ  1 
ATOM   5667 N  NH1 . ARG A 1 718  ? 13.484 70.006  -2.982  1.00 16.18 ? 718  ARG A NH1 1 
ATOM   5668 N  NH2 . ARG A 1 718  ? 14.064 69.660  -5.171  1.00 15.56 ? 718  ARG A NH2 1 
ATOM   5669 N  N   . SER A 1 719  ? 12.434 78.540  -3.153  1.00 25.88 ? 719  SER A N   1 
ATOM   5670 C  CA  . SER A 1 719  ? 12.094 79.668  -2.275  1.00 30.04 ? 719  SER A CA  1 
ATOM   5671 C  C   . SER A 1 719  ? 11.501 79.205  -0.935  1.00 31.74 ? 719  SER A C   1 
ATOM   5672 O  O   . SER A 1 719  ? 11.481 79.946  0.033   1.00 32.95 ? 719  SER A O   1 
ATOM   5673 C  CB  . SER A 1 719  ? 11.126 80.623  -2.980  1.00 30.50 ? 719  SER A CB  1 
ATOM   5674 O  OG  . SER A 1 719  ? 10.008 79.910  -3.449  1.00 33.00 ? 719  SER A OG  1 
ATOM   5675 N  N   . HIS A 1 720  ? 11.016 77.975  -0.881  1.00 33.53 ? 720  HIS A N   1 
ATOM   5676 C  CA  . HIS A 1 720  ? 10.503 77.446  0.371   1.00 35.40 ? 720  HIS A CA  1 
ATOM   5677 C  C   . HIS A 1 720  ? 11.025 76.006  0.467   1.00 34.40 ? 720  HIS A C   1 
ATOM   5678 O  O   . HIS A 1 720  ? 11.235 75.337  -0.548  1.00 34.21 ? 720  HIS A O   1 
ATOM   5679 C  CB  . HIS A 1 720  ? 8.970  77.495  0.391   1.00 38.74 ? 720  HIS A CB  1 
ATOM   5680 C  CG  . HIS A 1 720  ? 8.319  76.525  -0.545  1.00 42.74 ? 720  HIS A CG  1 
ATOM   5681 N  ND1 . HIS A 1 720  ? 8.118  75.196  -0.219  1.00 44.16 ? 720  HIS A ND1 1 
ATOM   5682 C  CD2 . HIS A 1 720  ? 7.843  76.683  -1.805  1.00 44.26 ? 720  HIS A CD2 1 
ATOM   5683 C  CE1 . HIS A 1 720  ? 7.549  74.577  -1.241  1.00 45.66 ? 720  HIS A CE1 1 
ATOM   5684 N  NE2 . HIS A 1 720  ? 7.372  75.456  -2.217  1.00 46.49 ? 720  HIS A NE2 1 
ATOM   5685 N  N   . GLY A 1 721  ? 11.266 75.530  1.680   1.00 32.55 ? 721  GLY A N   1 
ATOM   5686 C  CA  . GLY A 1 721  ? 11.779 74.178  1.802   1.00 29.83 ? 721  GLY A CA  1 
ATOM   5687 C  C   . GLY A 1 721  ? 13.294 74.182  1.904   1.00 27.14 ? 721  GLY A C   1 
ATOM   5688 O  O   . GLY A 1 721  ? 13.889 75.222  2.187   1.00 26.01 ? 721  GLY A O   1 
ATOM   5689 N  N   . ASP A 1 722  ? 13.913 73.030  1.646   1.00 24.74 ? 722  ASP A N   1 
ATOM   5690 C  CA  . ASP A 1 722  ? 15.363 72.886  1.759   1.00 22.47 ? 722  ASP A CA  1 
ATOM   5691 C  C   . ASP A 1 722  ? 16.111 73.607  0.650   1.00 21.52 ? 722  ASP A C   1 
ATOM   5692 O  O   . ASP A 1 722  ? 15.707 73.561  -0.517  1.00 21.62 ? 722  ASP A O   1 
ATOM   5693 C  CB  . ASP A 1 722  ? 15.743 71.401  1.787   1.00 20.59 ? 722  ASP A CB  1 
ATOM   5694 C  CG  . ASP A 1 722  ? 15.162 70.672  3.006   1.00 22.24 ? 722  ASP A CG  1 
ATOM   5695 O  OD1 . ASP A 1 722  ? 15.007 69.429  2.952   1.00 19.91 ? 722  ASP A OD1 1 
ATOM   5696 O  OD2 . ASP A 1 722  ? 14.879 71.339  4.026   1.00 19.92 ? 722  ASP A OD2 1 
ATOM   5697 N  N   . ARG A 1 723  ? 17.192 74.282  1.044   1.00 20.62 ? 723  ARG A N   1 
ATOM   5698 C  CA  . ARG A 1 723  ? 18.049 75.025  0.124   1.00 20.72 ? 723  ARG A CA  1 
ATOM   5699 C  C   . ARG A 1 723  ? 19.322 74.297  -0.308  1.00 18.64 ? 723  ARG A C   1 
ATOM   5700 O  O   . ARG A 1 723  ? 19.968 73.602  0.477   1.00 17.58 ? 723  ARG A O   1 
ATOM   5701 C  CB  . ARG A 1 723  ? 18.483 76.358  0.736   1.00 23.79 ? 723  ARG A CB  1 
ATOM   5702 C  CG  . ARG A 1 723  ? 17.551 77.527  0.433   1.00 31.11 ? 723  ARG A CG  1 
ATOM   5703 C  CD  . ARG A 1 723  ? 16.187 77.328  1.053   1.00 35.57 ? 723  ARG A CD  1 
ATOM   5704 N  NE  . ARG A 1 723  ? 15.369 78.548  1.079   1.00 40.14 ? 723  ARG A NE  1 
ATOM   5705 C  CZ  . ARG A 1 723  ? 15.769 79.711  1.600   1.00 42.50 ? 723  ARG A CZ  1 
ATOM   5706 N  NH1 . ARG A 1 723  ? 16.987 79.835  2.127   1.00 43.39 ? 723  ARG A NH1 1 
ATOM   5707 N  NH2 . ARG A 1 723  ? 14.930 80.740  1.652   1.00 43.36 ? 723  ARG A NH2 1 
ATOM   5708 N  N   . SER A 1 724  ? 19.671 74.465  -1.575  1.00 16.23 ? 724  SER A N   1 
ATOM   5709 C  CA  . SER A 1 724  ? 20.895 73.894  -2.100  1.00 15.42 ? 724  SER A CA  1 
ATOM   5710 C  C   . SER A 1 724  ? 22.062 74.587  -1.378  1.00 15.35 ? 724  SER A C   1 
ATOM   5711 O  O   . SER A 1 724  ? 21.972 75.800  -1.056  1.00 14.68 ? 724  SER A O   1 
ATOM   5712 C  CB  . SER A 1 724  ? 21.007 74.191  -3.594  1.00 12.68 ? 724  SER A CB  1 
ATOM   5713 O  OG  . SER A 1 724  ? 19.957 73.579  -4.330  1.00 15.50 ? 724  SER A OG  1 
ATOM   5714 N  N   . GLY A 1 725  ? 23.147 73.842  -1.154  1.00 14.10 ? 725  GLY A N   1 
ATOM   5715 C  CA  . GLY A 1 725  ? 24.344 74.392  -0.519  1.00 12.57 ? 725  GLY A CA  1 
ATOM   5716 C  C   . GLY A 1 725  ? 25.582 73.706  -1.091  1.00 13.32 ? 725  GLY A C   1 
ATOM   5717 O  O   . GLY A 1 725  ? 25.522 73.139  -2.208  1.00 13.39 ? 725  GLY A O   1 
ATOM   5718 N  N   . ALA A 1 726  ? 26.700 73.732  -0.355  1.00 10.32 ? 726  ALA A N   1 
ATOM   5719 C  CA  . ALA A 1 726  ? 27.946 73.103  -0.825  1.00 9.83  ? 726  ALA A CA  1 
ATOM   5720 C  C   . ALA A 1 726  ? 27.768 71.593  -1.059  1.00 9.41  ? 726  ALA A C   1 
ATOM   5721 O  O   . ALA A 1 726  ? 28.401 71.019  -1.944  1.00 10.34 ? 726  ALA A O   1 
ATOM   5722 C  CB  . ALA A 1 726  ? 29.078 73.330  0.199   1.00 9.46  ? 726  ALA A CB  1 
ATOM   5723 N  N   . TYR A 1 727  ? 26.928 70.953  -0.245  1.00 9.00  ? 727  TYR A N   1 
ATOM   5724 C  CA  . TYR A 1 727  ? 26.698 69.508  -0.369  1.00 9.62  ? 727  TYR A CA  1 
ATOM   5725 C  C   . TYR A 1 727  ? 25.501 69.153  -1.244  1.00 9.38  ? 727  TYR A C   1 
ATOM   5726 O  O   . TYR A 1 727  ? 25.597 68.333  -2.164  1.00 8.93  ? 727  TYR A O   1 
ATOM   5727 C  CB  . TYR A 1 727  ? 26.418 68.881  0.997   1.00 8.54  ? 727  TYR A CB  1 
ATOM   5728 C  CG  . TYR A 1 727  ? 27.447 69.144  2.055   1.00 9.78  ? 727  TYR A CG  1 
ATOM   5729 C  CD1 . TYR A 1 727  ? 27.412 70.311  2.818   1.00 9.81  ? 727  TYR A CD1 1 
ATOM   5730 C  CD2 . TYR A 1 727  ? 28.461 68.201  2.316   1.00 7.38  ? 727  TYR A CD2 1 
ATOM   5731 C  CE1 . TYR A 1 727  ? 28.374 70.547  3.835   1.00 10.81 ? 727  TYR A CE1 1 
ATOM   5732 C  CE2 . TYR A 1 727  ? 29.412 68.416  3.327   1.00 7.90  ? 727  TYR A CE2 1 
ATOM   5733 C  CZ  . TYR A 1 727  ? 29.365 69.588  4.083   1.00 8.25  ? 727  TYR A CZ  1 
ATOM   5734 O  OH  . TYR A 1 727  ? 30.263 69.777  5.117   1.00 8.08  ? 727  TYR A OH  1 
ATOM   5735 N  N   . LEU A 1 728  ? 24.362 69.775  -0.934  1.00 9.08  ? 728  LEU A N   1 
ATOM   5736 C  CA  . LEU A 1 728  ? 23.105 69.451  -1.611  1.00 10.71 ? 728  LEU A CA  1 
ATOM   5737 C  C   . LEU A 1 728  ? 22.749 70.174  -2.919  1.00 11.03 ? 728  LEU A C   1 
ATOM   5738 O  O   . LEU A 1 728  ? 22.956 71.380  -3.068  1.00 11.10 ? 728  LEU A O   1 
ATOM   5739 C  CB  . LEU A 1 728  ? 21.923 69.657  -0.618  1.00 10.68 ? 728  LEU A CB  1 
ATOM   5740 C  CG  . LEU A 1 728  ? 22.036 69.070  0.802   1.00 9.77  ? 728  LEU A CG  1 
ATOM   5741 C  CD1 . LEU A 1 728  ? 20.717 69.216  1.581   1.00 10.57 ? 728  LEU A CD1 1 
ATOM   5742 C  CD2 . LEU A 1 728  ? 22.399 67.617  0.692   1.00 12.28 ? 728  LEU A CD2 1 
ATOM   5743 N  N   . PHE A 1 729  ? 22.203 69.420  -3.868  1.00 12.53 ? 729  PHE A N   1 
ATOM   5744 C  CA  . PHE A 1 729  ? 21.705 70.014  -5.111  1.00 12.57 ? 729  PHE A CA  1 
ATOM   5745 C  C   . PHE A 1 729  ? 20.151 69.836  -4.986  1.00 13.50 ? 729  PHE A C   1 
ATOM   5746 O  O   . PHE A 1 729  ? 19.644 68.721  -5.113  1.00 11.45 ? 729  PHE A O   1 
ATOM   5747 C  CB  . PHE A 1 729  ? 22.225 69.241  -6.313  1.00 12.16 ? 729  PHE A CB  1 
ATOM   5748 C  CG  . PHE A 1 729  ? 21.679 69.715  -7.642  1.00 13.18 ? 729  PHE A CG  1 
ATOM   5749 C  CD1 . PHE A 1 729  ? 21.563 68.822  -8.705  1.00 12.17 ? 729  PHE A CD1 1 
ATOM   5750 C  CD2 . PHE A 1 729  ? 21.345 71.058  -7.852  1.00 13.45 ? 729  PHE A CD2 1 
ATOM   5751 C  CE1 . PHE A 1 729  ? 21.118 69.258  -9.963  1.00 12.00 ? 729  PHE A CE1 1 
ATOM   5752 C  CE2 . PHE A 1 729  ? 20.906 71.503  -9.096  1.00 12.03 ? 729  PHE A CE2 1 
ATOM   5753 C  CZ  . PHE A 1 729  ? 20.786 70.610  -10.155 1.00 11.54 ? 729  PHE A CZ  1 
ATOM   5754 N  N   . LEU A 1 730  ? 19.429 70.937  -4.742  1.00 14.21 ? 730  LEU A N   1 
ATOM   5755 C  CA  . LEU A 1 730  ? 17.969 70.961  -4.580  1.00 14.23 ? 730  LEU A CA  1 
ATOM   5756 C  C   . LEU A 1 730  ? 17.387 71.975  -5.560  1.00 15.16 ? 730  LEU A C   1 
ATOM   5757 O  O   . LEU A 1 730  ? 16.918 73.057  -5.162  1.00 14.88 ? 730  LEU A O   1 
ATOM   5758 C  CB  . LEU A 1 730  ? 17.618 71.369  -3.144  1.00 12.95 ? 730  LEU A CB  1 
ATOM   5759 C  CG  . LEU A 1 730  ? 17.995 70.266  -2.135  1.00 10.56 ? 730  LEU A CG  1 
ATOM   5760 C  CD1 . LEU A 1 730  ? 17.984 70.804  -0.735  1.00 13.33 ? 730  LEU A CD1 1 
ATOM   5761 C  CD2 . LEU A 1 730  ? 17.019 69.101  -2.266  1.00 10.00 ? 730  LEU A CD2 1 
ATOM   5762 N  N   . PRO A 1 731  ? 17.399 71.635  -6.856  1.00 14.61 ? 731  PRO A N   1 
ATOM   5763 C  CA  . PRO A 1 731  ? 16.883 72.544  -7.881  1.00 15.90 ? 731  PRO A CA  1 
ATOM   5764 C  C   . PRO A 1 731  ? 15.412 72.899  -7.774  1.00 16.85 ? 731  PRO A C   1 
ATOM   5765 O  O   . PRO A 1 731  ? 14.599 72.105  -7.312  1.00 17.66 ? 731  PRO A O   1 
ATOM   5766 C  CB  . PRO A 1 731  ? 17.203 71.813  -9.189  1.00 14.65 ? 731  PRO A CB  1 
ATOM   5767 C  CG  . PRO A 1 731  ? 17.106 70.350  -8.772  1.00 14.51 ? 731  PRO A CG  1 
ATOM   5768 C  CD  . PRO A 1 731  ? 17.748 70.321  -7.423  1.00 13.38 ? 731  PRO A CD  1 
ATOM   5769 N  N   . ASN A 1 732  ? 15.068 74.113  -8.186  1.00 18.47 ? 732  ASN A N   1 
ATOM   5770 C  CA  . ASN A 1 732  ? 13.671 74.503  -8.189  1.00 18.43 ? 732  ASN A CA  1 
ATOM   5771 C  C   . ASN A 1 732  ? 13.161 74.191  -9.591  1.00 17.81 ? 732  ASN A C   1 
ATOM   5772 O  O   . ASN A 1 732  ? 12.722 75.074  -10.316 1.00 18.51 ? 732  ASN A O   1 
ATOM   5773 C  CB  . ASN A 1 732  ? 13.519 75.988  -7.860  1.00 20.22 ? 732  ASN A CB  1 
ATOM   5774 C  CG  . ASN A 1 732  ? 14.143 76.892  -8.903  1.00 22.23 ? 732  ASN A CG  1 
ATOM   5775 O  OD1 . ASN A 1 732  ? 15.114 76.524  -9.575  1.00 22.29 ? 732  ASN A OD1 1 
ATOM   5776 N  ND2 . ASN A 1 732  ? 13.597 78.109  -9.030  1.00 23.79 ? 732  ASN A ND2 1 
ATOM   5777 N  N   . GLY A 1 733  ? 13.261 72.919  -9.971  1.00 16.77 ? 733  GLY A N   1 
ATOM   5778 C  CA  . GLY A 1 733  ? 12.784 72.457  -11.261 1.00 16.91 ? 733  GLY A CA  1 
ATOM   5779 C  C   . GLY A 1 733  ? 13.882 72.339  -12.314 1.00 17.58 ? 733  GLY A C   1 
ATOM   5780 O  O   . GLY A 1 733  ? 15.041 72.653  -12.040 1.00 15.67 ? 733  GLY A O   1 
ATOM   5781 N  N   . PRO A 1 734  ? 13.533 71.884  -13.534 1.00 17.45 ? 734  PRO A N   1 
ATOM   5782 C  CA  . PRO A 1 734  ? 14.447 71.715  -14.666 1.00 16.75 ? 734  PRO A CA  1 
ATOM   5783 C  C   . PRO A 1 734  ? 15.078 73.068  -14.974 1.00 16.35 ? 734  PRO A C   1 
ATOM   5784 O  O   . PRO A 1 734  ? 14.487 74.111  -14.706 1.00 15.68 ? 734  PRO A O   1 
ATOM   5785 C  CB  . PRO A 1 734  ? 13.523 71.271  -15.792 1.00 16.53 ? 734  PRO A CB  1 
ATOM   5786 C  CG  . PRO A 1 734  ? 12.440 70.550  -15.067 1.00 18.15 ? 734  PRO A CG  1 
ATOM   5787 C  CD  . PRO A 1 734  ? 12.177 71.419  -13.883 1.00 17.22 ? 734  PRO A CD  1 
ATOM   5788 N  N   . ALA A 1 735  ? 16.245 73.046  -15.602 1.00 16.66 ? 735  ALA A N   1 
ATOM   5789 C  CA  . ALA A 1 735  ? 16.960 74.273  -15.911 1.00 16.74 ? 735  ALA A CA  1 
ATOM   5790 C  C   . ALA A 1 735  ? 16.272 75.120  -16.988 1.00 18.05 ? 735  ALA A C   1 
ATOM   5791 O  O   . ALA A 1 735  ? 15.568 74.584  -17.834 1.00 18.69 ? 735  ALA A O   1 
ATOM   5792 C  CB  . ALA A 1 735  ? 18.389 73.936  -16.339 1.00 15.15 ? 735  ALA A CB  1 
ATOM   5793 N  N   . SER A 1 736  ? 16.510 76.435  -16.950 1.00 18.01 ? 736  SER A N   1 
ATOM   5794 C  CA  . SER A 1 736  ? 15.951 77.382  -17.911 1.00 17.86 ? 736  SER A CA  1 
ATOM   5795 C  C   . SER A 1 736  ? 17.101 77.881  -18.769 1.00 18.25 ? 736  SER A C   1 
ATOM   5796 O  O   . SER A 1 736  ? 18.211 78.093  -18.278 1.00 15.68 ? 736  SER A O   1 
ATOM   5797 C  CB  . SER A 1 736  ? 15.340 78.560  -17.174 1.00 18.67 ? 736  SER A CB  1 
ATOM   5798 O  OG  . SER A 1 736  ? 14.462 78.075  -16.171 1.00 22.48 ? 736  SER A OG  1 
ATOM   5799 N  N   . PRO A 1 737  ? 16.851 78.111  -20.057 1.00 19.25 ? 737  PRO A N   1 
ATOM   5800 C  CA  . PRO A 1 737  ? 17.970 78.584  -20.886 1.00 20.49 ? 737  PRO A CA  1 
ATOM   5801 C  C   . PRO A 1 737  ? 18.559 79.926  -20.426 1.00 21.24 ? 737  PRO A C   1 
ATOM   5802 O  O   . PRO A 1 737  ? 17.850 80.788  -19.902 1.00 21.81 ? 737  PRO A O   1 
ATOM   5803 C  CB  . PRO A 1 737  ? 17.354 78.684  -22.296 1.00 21.34 ? 737  PRO A CB  1 
ATOM   5804 C  CG  . PRO A 1 737  ? 16.101 77.774  -22.222 1.00 21.60 ? 737  PRO A CG  1 
ATOM   5805 C  CD  . PRO A 1 737  ? 15.594 78.065  -20.820 1.00 20.19 ? 737  PRO A CD  1 
ATOM   5806 N  N   . VAL A 1 738  ? 19.868 80.082  -20.584 1.00 22.39 ? 738  VAL A N   1 
ATOM   5807 C  CA  . VAL A 1 738  ? 20.521 81.342  -20.249 1.00 22.60 ? 738  VAL A CA  1 
ATOM   5808 C  C   . VAL A 1 738  ? 20.159 82.257  -21.450 1.00 23.56 ? 738  VAL A C   1 
ATOM   5809 O  O   . VAL A 1 738  ? 20.265 81.829  -22.603 1.00 22.14 ? 738  VAL A O   1 
ATOM   5810 C  CB  . VAL A 1 738  ? 22.073 81.160  -20.176 1.00 23.45 ? 738  VAL A CB  1 
ATOM   5811 C  CG1 . VAL A 1 738  ? 22.767 82.534  -20.168 1.00 23.45 ? 738  VAL A CG1 1 
ATOM   5812 C  CG2 . VAL A 1 738  ? 22.454 80.359  -18.918 1.00 23.07 ? 738  VAL A CG2 1 
ATOM   5813 N  N   . GLU A 1 739  ? 19.690 83.473  -21.192 1.00 24.37 ? 739  GLU A N   1 
ATOM   5814 C  CA  . GLU A 1 739  ? 19.346 84.387  -22.290 1.00 25.13 ? 739  GLU A CA  1 
ATOM   5815 C  C   . GLU A 1 739  ? 20.672 84.904  -22.811 1.00 24.21 ? 739  GLU A C   1 
ATOM   5816 O  O   . GLU A 1 739  ? 21.438 85.530  -22.076 1.00 23.33 ? 739  GLU A O   1 
ATOM   5817 C  CB  . GLU A 1 739  ? 18.496 85.553  -21.793 1.00 27.97 ? 739  GLU A CB  1 
ATOM   5818 C  CG  . GLU A 1 739  ? 17.051 85.190  -21.526 1.00 33.36 ? 739  GLU A CG  1 
ATOM   5819 C  CD  . GLU A 1 739  ? 16.220 86.398  -21.061 1.00 36.59 ? 739  GLU A CD  1 
ATOM   5820 O  OE1 . GLU A 1 739  ? 15.015 86.211  -20.780 1.00 39.27 ? 739  GLU A OE1 1 
ATOM   5821 O  OE2 . GLU A 1 739  ? 16.766 87.525  -20.976 1.00 37.49 ? 739  GLU A OE2 1 
ATOM   5822 N  N   . LEU A 1 740  ? 20.928 84.643  -24.082 1.00 23.85 ? 740  LEU A N   1 
ATOM   5823 C  CA  . LEU A 1 740  ? 22.199 84.996  -24.691 1.00 23.60 ? 740  LEU A CA  1 
ATOM   5824 C  C   . LEU A 1 740  ? 22.344 86.368  -25.319 1.00 24.09 ? 740  LEU A C   1 
ATOM   5825 O  O   . LEU A 1 740  ? 23.468 86.769  -25.617 1.00 24.72 ? 740  LEU A O   1 
ATOM   5826 C  CB  . LEU A 1 740  ? 22.550 83.932  -25.729 1.00 22.65 ? 740  LEU A CB  1 
ATOM   5827 C  CG  . LEU A 1 740  ? 22.518 82.474  -25.231 1.00 22.28 ? 740  LEU A CG  1 
ATOM   5828 C  CD1 . LEU A 1 740  ? 22.932 81.567  -26.351 1.00 21.23 ? 740  LEU A CD1 1 
ATOM   5829 C  CD2 . LEU A 1 740  ? 23.455 82.297  -24.019 1.00 22.17 ? 740  LEU A CD2 1 
ATOM   5830 N  N   . GLY A 1 741  ? 21.239 87.087  -25.529 1.00 23.65 ? 741  GLY A N   1 
ATOM   5831 C  CA  . GLY A 1 741  ? 21.343 88.389  -26.172 1.00 24.61 ? 741  GLY A CA  1 
ATOM   5832 C  C   . GLY A 1 741  ? 21.921 88.161  -27.560 1.00 24.57 ? 741  GLY A C   1 
ATOM   5833 O  O   . GLY A 1 741  ? 21.630 87.142  -28.174 1.00 25.79 ? 741  GLY A O   1 
ATOM   5834 N  N   . GLN A 1 742  ? 22.731 89.078  -28.082 1.00 25.74 ? 742  GLN A N   1 
ATOM   5835 C  CA  . GLN A 1 742  ? 23.341 88.857  -29.407 1.00 25.78 ? 742  GLN A CA  1 
ATOM   5836 C  C   . GLN A 1 742  ? 24.845 88.827  -29.102 1.00 23.74 ? 742  GLN A C   1 
ATOM   5837 O  O   . GLN A 1 742  ? 25.532 89.818  -29.234 1.00 24.65 ? 742  GLN A O   1 
ATOM   5838 C  CB  . GLN A 1 742  ? 22.984 90.007  -30.369 1.00 28.87 ? 742  GLN A CB  1 
ATOM   5839 C  CG  . GLN A 1 742  ? 23.138 89.648  -31.863 1.00 32.77 ? 742  GLN A CG  1 
ATOM   5840 C  CD  . GLN A 1 742  ? 22.440 90.635  -32.829 1.00 36.25 ? 742  GLN A CD  1 
ATOM   5841 O  OE1 . GLN A 1 742  ? 21.580 91.458  -32.427 1.00 37.47 ? 742  GLN A OE1 1 
ATOM   5842 N  NE2 . GLN A 1 742  ? 22.797 90.542  -34.111 1.00 36.20 ? 742  GLN A NE2 1 
ATOM   5843 N  N   . PRO A 1 743  ? 25.367 87.668  -28.687 1.00 21.82 ? 743  PRO A N   1 
ATOM   5844 C  CA  . PRO A 1 743  ? 26.793 87.561  -28.344 1.00 19.38 ? 743  PRO A CA  1 
ATOM   5845 C  C   . PRO A 1 743  ? 27.839 87.780  -29.425 1.00 17.72 ? 743  PRO A C   1 
ATOM   5846 O  O   . PRO A 1 743  ? 27.607 87.510  -30.601 1.00 15.37 ? 743  PRO A O   1 
ATOM   5847 C  CB  . PRO A 1 743  ? 26.889 86.173  -27.727 1.00 18.90 ? 743  PRO A CB  1 
ATOM   5848 C  CG  . PRO A 1 743  ? 25.884 85.381  -28.569 1.00 20.92 ? 743  PRO A CG  1 
ATOM   5849 C  CD  . PRO A 1 743  ? 24.701 86.352  -28.625 1.00 20.26 ? 743  PRO A CD  1 
ATOM   5850 N  N   . VAL A 1 744  ? 29.010 88.259  -29.000 1.00 14.94 ? 744  VAL A N   1 
ATOM   5851 C  CA  . VAL A 1 744  ? 30.108 88.481  -29.930 1.00 14.30 ? 744  VAL A CA  1 
ATOM   5852 C  C   . VAL A 1 744  ? 30.832 87.155  -30.180 1.00 13.55 ? 744  VAL A C   1 
ATOM   5853 O  O   . VAL A 1 744  ? 31.227 86.465  -29.245 1.00 14.07 ? 744  VAL A O   1 
ATOM   5854 C  CB  . VAL A 1 744  ? 31.105 89.503  -29.374 1.00 14.88 ? 744  VAL A CB  1 
ATOM   5855 C  CG1 . VAL A 1 744  ? 32.324 89.577  -30.297 1.00 12.15 ? 744  VAL A CG1 1 
ATOM   5856 C  CG2 . VAL A 1 744  ? 30.413 90.869  -29.213 1.00 15.43 ? 744  VAL A CG2 1 
ATOM   5857 N  N   . VAL A 1 745  ? 31.009 86.812  -31.448 1.00 12.75 ? 745  VAL A N   1 
ATOM   5858 C  CA  . VAL A 1 745  ? 31.658 85.574  -31.825 1.00 12.12 ? 745  VAL A CA  1 
ATOM   5859 C  C   . VAL A 1 745  ? 32.949 85.827  -32.579 1.00 12.42 ? 745  VAL A C   1 
ATOM   5860 O  O   . VAL A 1 745  ? 32.985 86.586  -33.555 1.00 12.85 ? 745  VAL A O   1 
ATOM   5861 C  CB  . VAL A 1 745  ? 30.711 84.718  -32.712 1.00 11.48 ? 745  VAL A CB  1 
ATOM   5862 C  CG1 . VAL A 1 745  ? 31.415 83.441  -33.163 1.00 12.07 ? 745  VAL A CG1 1 
ATOM   5863 C  CG2 . VAL A 1 745  ? 29.438 84.381  -31.933 1.00 13.24 ? 745  VAL A CG2 1 
ATOM   5864 N  N   . LEU A 1 746  ? 34.021 85.197  -32.118 1.00 11.49 ? 746  LEU A N   1 
ATOM   5865 C  CA  . LEU A 1 746  ? 35.321 85.335  -32.764 1.00 10.95 ? 746  LEU A CA  1 
ATOM   5866 C  C   . LEU A 1 746  ? 35.734 84.030  -33.452 1.00 12.11 ? 746  LEU A C   1 
ATOM   5867 O  O   . LEU A 1 746  ? 35.831 82.970  -32.804 1.00 11.35 ? 746  LEU A O   1 
ATOM   5868 C  CB  . LEU A 1 746  ? 36.375 85.700  -31.721 1.00 11.39 ? 746  LEU A CB  1 
ATOM   5869 C  CG  . LEU A 1 746  ? 37.829 85.612  -32.191 1.00 12.39 ? 746  LEU A CG  1 
ATOM   5870 C  CD1 . LEU A 1 746  ? 38.078 86.691  -33.237 1.00 12.00 ? 746  LEU A CD1 1 
ATOM   5871 C  CD2 . LEU A 1 746  ? 38.779 85.794  -30.989 1.00 12.75 ? 746  LEU A CD2 1 
ATOM   5872 N  N   . VAL A 1 747  ? 36.027 84.101  -34.739 1.00 11.63 ? 747  VAL A N   1 
ATOM   5873 C  CA  . VAL A 1 747  ? 36.408 82.908  -35.464 1.00 12.23 ? 747  VAL A CA  1 
ATOM   5874 C  C   . VAL A 1 747  ? 37.856 83.024  -35.924 1.00 13.85 ? 747  VAL A C   1 
ATOM   5875 O  O   . VAL A 1 747  ? 38.224 83.977  -36.617 1.00 14.92 ? 747  VAL A O   1 
ATOM   5876 C  CB  . VAL A 1 747  ? 35.468 82.722  -36.698 1.00 13.23 ? 747  VAL A CB  1 
ATOM   5877 C  CG1 . VAL A 1 747  ? 35.852 81.482  -37.495 1.00 13.64 ? 747  VAL A CG1 1 
ATOM   5878 C  CG2 . VAL A 1 747  ? 34.011 82.656  -36.246 1.00 11.20 ? 747  VAL A CG2 1 
ATOM   5879 N  N   . THR A 1 748  ? 38.697 82.078  -35.534 1.00 13.59 ? 748  THR A N   1 
ATOM   5880 C  CA  . THR A 1 748  ? 40.087 82.108  -35.978 1.00 14.41 ? 748  THR A CA  1 
ATOM   5881 C  C   . THR A 1 748  ? 40.258 80.872  -36.826 1.00 14.99 ? 748  THR A C   1 
ATOM   5882 O  O   . THR A 1 748  ? 39.915 79.782  -36.390 1.00 15.86 ? 748  THR A O   1 
ATOM   5883 C  CB  . THR A 1 748  ? 41.062 82.095  -34.774 1.00 14.70 ? 748  THR A CB  1 
ATOM   5884 O  OG1 . THR A 1 748  ? 40.863 83.304  -34.024 1.00 15.20 ? 748  THR A OG1 1 
ATOM   5885 C  CG2 . THR A 1 748  ? 42.526 82.008  -35.249 1.00 14.70 ? 748  THR A CG2 1 
ATOM   5886 N  N   . LYS A 1 749  ? 40.764 81.030  -38.041 1.00 15.43 ? 749  LYS A N   1 
ATOM   5887 C  CA  . LYS A 1 749  ? 40.931 79.884  -38.911 1.00 16.34 ? 749  LYS A CA  1 
ATOM   5888 C  C   . LYS A 1 749  ? 42.379 79.738  -39.317 1.00 15.39 ? 749  LYS A C   1 
ATOM   5889 O  O   . LYS A 1 749  ? 42.971 80.636  -39.942 1.00 15.05 ? 749  LYS A O   1 
ATOM   5890 C  CB  . LYS A 1 749  ? 40.036 80.012  -40.151 1.00 17.70 ? 749  LYS A CB  1 
ATOM   5891 C  CG  . LYS A 1 749  ? 40.300 78.963  -41.208 1.00 21.23 ? 749  LYS A CG  1 
ATOM   5892 C  CD  . LYS A 1 749  ? 39.231 79.018  -42.312 1.00 24.30 ? 749  LYS A CD  1 
ATOM   5893 C  CE  . LYS A 1 749  ? 39.685 78.231  -43.525 1.00 25.72 ? 749  LYS A CE  1 
ATOM   5894 N  NZ  . LYS A 1 749  ? 38.688 78.345  -44.631 1.00 30.38 ? 749  LYS A NZ  1 
ATOM   5895 N  N   . GLY A 1 750  ? 42.941 78.588  -38.973 1.00 13.99 ? 750  GLY A N   1 
ATOM   5896 C  CA  . GLY A 1 750  ? 44.340 78.352  -39.272 1.00 13.87 ? 750  GLY A CA  1 
ATOM   5897 C  C   . GLY A 1 750  ? 44.507 76.998  -39.889 1.00 14.84 ? 750  GLY A C   1 
ATOM   5898 O  O   . GLY A 1 750  ? 43.576 76.174  -39.901 1.00 14.29 ? 750  GLY A O   1 
ATOM   5899 N  N   . LYS A 1 751  ? 45.692 76.759  -40.418 1.00 15.69 ? 751  LYS A N   1 
ATOM   5900 C  CA  . LYS A 1 751  ? 45.972 75.486  -41.030 1.00 16.72 ? 751  LYS A CA  1 
ATOM   5901 C  C   . LYS A 1 751  ? 46.181 74.386  -39.983 1.00 15.93 ? 751  LYS A C   1 
ATOM   5902 O  O   . LYS A 1 751  ? 45.868 73.224  -40.221 1.00 15.27 ? 751  LYS A O   1 
ATOM   5903 C  CB  . LYS A 1 751  ? 47.213 75.614  -41.908 1.00 20.45 ? 751  LYS A CB  1 
ATOM   5904 C  CG  . LYS A 1 751  ? 47.559 74.333  -42.614 1.00 25.65 ? 751  LYS A CG  1 
ATOM   5905 C  CD  . LYS A 1 751  ? 48.517 74.574  -43.793 1.00 30.44 ? 751  LYS A CD  1 
ATOM   5906 C  CE  . LYS A 1 751  ? 49.086 73.243  -44.271 1.00 32.98 ? 751  LYS A CE  1 
ATOM   5907 N  NZ  . LYS A 1 751  ? 47.987 72.229  -44.459 1.00 35.48 ? 751  LYS A NZ  1 
ATOM   5908 N  N   . LEU A 1 752  ? 46.714 74.743  -38.825 1.00 14.25 ? 752  LEU A N   1 
ATOM   5909 C  CA  . LEU A 1 752  ? 46.947 73.739  -37.784 1.00 14.79 ? 752  LEU A CA  1 
ATOM   5910 C  C   . LEU A 1 752  ? 45.865 73.762  -36.713 1.00 14.90 ? 752  LEU A C   1 
ATOM   5911 O  O   . LEU A 1 752  ? 45.535 72.730  -36.129 1.00 15.39 ? 752  LEU A O   1 
ATOM   5912 C  CB  . LEU A 1 752  ? 48.306 73.977  -37.120 1.00 14.53 ? 752  LEU A CB  1 
ATOM   5913 C  CG  . LEU A 1 752  ? 49.517 73.983  -38.067 1.00 15.87 ? 752  LEU A CG  1 
ATOM   5914 C  CD1 . LEU A 1 752  ? 50.793 74.085  -37.248 1.00 16.43 ? 752  LEU A CD1 1 
ATOM   5915 C  CD2 . LEU A 1 752  ? 49.524 72.727  -38.905 1.00 16.78 ? 752  LEU A CD2 1 
ATOM   5916 N  N   . GLU A 1 753  ? 45.301 74.946  -36.482 1.00 13.57 ? 753  GLU A N   1 
ATOM   5917 C  CA  . GLU A 1 753  ? 44.297 75.125  -35.455 1.00 13.01 ? 753  GLU A CA  1 
ATOM   5918 C  C   . GLU A 1 753  ? 43.293 76.241  -35.781 1.00 13.02 ? 753  GLU A C   1 
ATOM   5919 O  O   . GLU A 1 753  ? 43.668 77.365  -36.130 1.00 12.66 ? 753  GLU A O   1 
ATOM   5920 C  CB  . GLU A 1 753  ? 44.995 75.463  -34.124 1.00 11.94 ? 753  GLU A CB  1 
ATOM   5921 C  CG  . GLU A 1 753  ? 44.061 75.637  -32.949 1.00 15.38 ? 753  GLU A CG  1 
ATOM   5922 C  CD  . GLU A 1 753  ? 44.777 76.092  -31.658 1.00 17.98 ? 753  GLU A CD  1 
ATOM   5923 O  OE1 . GLU A 1 753  ? 45.033 77.304  -31.486 1.00 19.78 ? 753  GLU A OE1 1 
ATOM   5924 O  OE2 . GLU A 1 753  ? 45.075 75.221  -30.817 1.00 19.55 ? 753  GLU A OE2 1 
ATOM   5925 N  N   . SER A 1 754  ? 42.018 75.922  -35.643 1.00 12.40 ? 754  SER A N   1 
ATOM   5926 C  CA  . SER A 1 754  ? 40.973 76.907  -35.843 1.00 11.89 ? 754  SER A CA  1 
ATOM   5927 C  C   . SER A 1 754  ? 40.145 76.864  -34.565 1.00 12.34 ? 754  SER A C   1 
ATOM   5928 O  O   . SER A 1 754  ? 40.246 75.907  -33.782 1.00 12.61 ? 754  SER A O   1 
ATOM   5929 C  CB  . SER A 1 754  ? 40.119 76.519  -37.034 1.00 11.52 ? 754  SER A CB  1 
ATOM   5930 O  OG  . SER A 1 754  ? 40.920 76.486  -38.206 1.00 13.08 ? 754  SER A OG  1 
ATOM   5931 N  N   . SER A 1 755  ? 39.335 77.884  -34.334 1.00 11.42 ? 755  SER A N   1 
ATOM   5932 C  CA  . SER A 1 755  ? 38.489 77.872  -33.166 1.00 11.44 ? 755  SER A CA  1 
ATOM   5933 C  C   . SER A 1 755  ? 37.348 78.876  -33.312 1.00 11.08 ? 755  SER A C   1 
ATOM   5934 O  O   . SER A 1 755  ? 37.387 79.786  -34.166 1.00 11.31 ? 755  SER A O   1 
ATOM   5935 C  CB  . SER A 1 755  ? 39.313 78.197  -31.908 1.00 13.54 ? 755  SER A CB  1 
ATOM   5936 O  OG  . SER A 1 755  ? 39.636 79.551  -31.867 1.00 13.40 ? 755  SER A OG  1 
ATOM   5937 N  N   . VAL A 1 756  ? 36.312 78.679  -32.517 1.00 9.77  ? 756  VAL A N   1 
ATOM   5938 C  CA  . VAL A 1 756  ? 35.185 79.601  -32.489 1.00 10.93 ? 756  VAL A CA  1 
ATOM   5939 C  C   . VAL A 1 756  ? 34.984 79.887  -31.006 1.00 11.88 ? 756  VAL A C   1 
ATOM   5940 O  O   . VAL A 1 756  ? 34.783 78.951  -30.209 1.00 11.68 ? 756  VAL A O   1 
ATOM   5941 C  CB  . VAL A 1 756  ? 33.892 78.974  -33.035 1.00 10.78 ? 756  VAL A CB  1 
ATOM   5942 C  CG1 . VAL A 1 756  ? 32.694 79.939  -32.808 1.00 8.71  ? 756  VAL A CG1 1 
ATOM   5943 C  CG2 . VAL A 1 756  ? 34.070 78.611  -34.502 1.00 9.40  ? 756  VAL A CG2 1 
ATOM   5944 N  N   . SER A 1 757  ? 35.034 81.167  -30.654 1.00 11.46 ? 757  SER A N   1 
ATOM   5945 C  CA  . SER A 1 757  ? 34.869 81.605  -29.268 1.00 11.81 ? 757  SER A CA  1 
ATOM   5946 C  C   . SER A 1 757  ? 33.734 82.599  -29.156 1.00 11.38 ? 757  SER A C   1 
ATOM   5947 O  O   . SER A 1 757  ? 33.581 83.446  -30.023 1.00 11.05 ? 757  SER A O   1 
ATOM   5948 C  CB  . SER A 1 757  ? 36.156 82.279  -28.770 1.00 11.92 ? 757  SER A CB  1 
ATOM   5949 O  OG  . SER A 1 757  ? 37.272 81.416  -28.993 1.00 16.34 ? 757  SER A OG  1 
ATOM   5950 N  N   . VAL A 1 758  ? 32.944 82.510  -28.098 1.00 11.87 ? 758  VAL A N   1 
ATOM   5951 C  CA  . VAL A 1 758  ? 31.849 83.463  -27.924 1.00 11.65 ? 758  VAL A CA  1 
ATOM   5952 C  C   . VAL A 1 758  ? 31.729 83.870  -26.457 1.00 13.00 ? 758  VAL A C   1 
ATOM   5953 O  O   . VAL A 1 758  ? 31.925 83.038  -25.544 1.00 11.72 ? 758  VAL A O   1 
ATOM   5954 C  CB  . VAL A 1 758  ? 30.525 82.872  -28.454 1.00 12.10 ? 758  VAL A CB  1 
ATOM   5955 C  CG1 . VAL A 1 758  ? 30.245 81.498  -27.819 1.00 10.09 ? 758  VAL A CG1 1 
ATOM   5956 C  CG2 . VAL A 1 758  ? 29.385 83.850  -28.211 1.00 10.88 ? 758  VAL A CG2 1 
ATOM   5957 N  N   . GLY A 1 759  ? 31.476 85.163  -26.248 1.00 12.58 ? 759  GLY A N   1 
ATOM   5958 C  CA  . GLY A 1 759  ? 31.328 85.736  -24.927 1.00 12.46 ? 759  GLY A CA  1 
ATOM   5959 C  C   . GLY A 1 759  ? 29.865 85.700  -24.508 1.00 14.09 ? 759  GLY A C   1 
ATOM   5960 O  O   . GLY A 1 759  ? 29.041 86.549  -24.893 1.00 13.40 ? 759  GLY A O   1 
ATOM   5961 N  N   . LEU A 1 760  ? 29.534 84.688  -23.729 1.00 13.74 ? 760  LEU A N   1 
ATOM   5962 C  CA  . LEU A 1 760  ? 28.184 84.500  -23.228 1.00 14.93 ? 760  LEU A CA  1 
ATOM   5963 C  C   . LEU A 1 760  ? 28.139 84.984  -21.803 1.00 14.65 ? 760  LEU A C   1 
ATOM   5964 O  O   . LEU A 1 760  ? 29.183 85.187  -21.178 1.00 16.30 ? 760  LEU A O   1 
ATOM   5965 C  CB  . LEU A 1 760  ? 27.821 83.004  -23.260 1.00 15.27 ? 760  LEU A CB  1 
ATOM   5966 C  CG  . LEU A 1 760  ? 27.985 82.282  -24.591 1.00 15.70 ? 760  LEU A CG  1 
ATOM   5967 C  CD1 . LEU A 1 760  ? 27.752 80.784  -24.437 1.00 15.70 ? 760  LEU A CD1 1 
ATOM   5968 C  CD2 . LEU A 1 760  ? 26.981 82.872  -25.567 1.00 16.68 ? 760  LEU A CD2 1 
ATOM   5969 N  N   . PRO A 1 761  ? 26.933 85.186  -21.252 1.00 16.31 ? 761  PRO A N   1 
ATOM   5970 C  CA  . PRO A 1 761  ? 26.846 85.645  -19.853 1.00 17.54 ? 761  PRO A CA  1 
ATOM   5971 C  C   . PRO A 1 761  ? 27.415 84.541  -18.968 1.00 17.82 ? 761  PRO A C   1 
ATOM   5972 O  O   . PRO A 1 761  ? 26.946 83.389  -19.014 1.00 17.17 ? 761  PRO A O   1 
ATOM   5973 C  CB  . PRO A 1 761  ? 25.333 85.832  -19.632 1.00 18.65 ? 761  PRO A CB  1 
ATOM   5974 C  CG  . PRO A 1 761  ? 24.852 86.198  -21.015 1.00 18.49 ? 761  PRO A CG  1 
ATOM   5975 C  CD  . PRO A 1 761  ? 25.614 85.224  -21.903 1.00 16.59 ? 761  PRO A CD  1 
ATOM   5976 N  N   . SER A 1 762  ? 28.437 84.897  -18.206 1.00 17.07 ? 762  SER A N   1 
ATOM   5977 C  CA  . SER A 1 762  ? 29.110 83.987  -17.282 1.00 17.42 ? 762  SER A CA  1 
ATOM   5978 C  C   . SER A 1 762  ? 30.093 83.007  -17.897 1.00 16.61 ? 762  SER A C   1 
ATOM   5979 O  O   . SER A 1 762  ? 30.799 82.309  -17.156 1.00 16.76 ? 762  SER A O   1 
ATOM   5980 C  CB  . SER A 1 762  ? 28.097 83.168  -16.488 1.00 17.59 ? 762  SER A CB  1 
ATOM   5981 O  OG  . SER A 1 762  ? 27.376 83.968  -15.587 1.00 19.54 ? 762  SER A OG  1 
ATOM   5982 N  N   . VAL A 1 763  ? 30.137 82.935  -19.224 1.00 15.17 ? 763  VAL A N   1 
ATOM   5983 C  CA  . VAL A 1 763  ? 31.022 81.970  -19.875 1.00 14.22 ? 763  VAL A CA  1 
ATOM   5984 C  C   . VAL A 1 763  ? 31.599 82.380  -21.231 1.00 13.50 ? 763  VAL A C   1 
ATOM   5985 O  O   . VAL A 1 763  ? 30.846 82.763  -22.124 1.00 14.07 ? 763  VAL A O   1 
ATOM   5986 C  CB  . VAL A 1 763  ? 30.281 80.625  -20.164 1.00 14.16 ? 763  VAL A CB  1 
ATOM   5987 C  CG1 . VAL A 1 763  ? 31.269 79.607  -20.750 1.00 13.30 ? 763  VAL A CG1 1 
ATOM   5988 C  CG2 . VAL A 1 763  ? 29.600 80.097  -18.909 1.00 13.08 ? 763  VAL A CG2 1 
ATOM   5989 N  N   . VAL A 1 764  ? 32.921 82.316  -21.388 1.00 11.99 ? 764  VAL A N   1 
ATOM   5990 C  CA  . VAL A 1 764  ? 33.503 82.551  -22.693 1.00 11.93 ? 764  VAL A CA  1 
ATOM   5991 C  C   . VAL A 1 764  ? 33.676 81.088  -23.100 1.00 12.37 ? 764  VAL A C   1 
ATOM   5992 O  O   . VAL A 1 764  ? 34.489 80.366  -22.514 1.00 12.08 ? 764  VAL A O   1 
ATOM   5993 C  CB  . VAL A 1 764  ? 34.882 83.244  -22.674 1.00 13.07 ? 764  VAL A CB  1 
ATOM   5994 C  CG1 . VAL A 1 764  ? 35.443 83.252  -24.098 1.00 12.11 ? 764  VAL A CG1 1 
ATOM   5995 C  CG2 . VAL A 1 764  ? 34.735 84.701  -22.139 1.00 10.55 ? 764  VAL A CG2 1 
ATOM   5996 N  N   . HIS A 1 765  ? 32.876 80.672  -24.084 1.00 11.90 ? 765  HIS A N   1 
ATOM   5997 C  CA  . HIS A 1 765  ? 32.805 79.294  -24.581 1.00 12.13 ? 765  HIS A CA  1 
ATOM   5998 C  C   . HIS A 1 765  ? 33.668 79.188  -25.816 1.00 13.31 ? 765  HIS A C   1 
ATOM   5999 O  O   . HIS A 1 765  ? 33.524 80.005  -26.729 1.00 13.21 ? 765  HIS A O   1 
ATOM   6000 C  CB  . HIS A 1 765  ? 31.330 78.990  -24.905 1.00 10.65 ? 765  HIS A CB  1 
ATOM   6001 C  CG  . HIS A 1 765  ? 31.099 77.654  -25.527 1.00 9.72  ? 765  HIS A CG  1 
ATOM   6002 N  ND1 . HIS A 1 765  ? 31.376 76.469  -24.878 1.00 7.85  ? 765  HIS A ND1 1 
ATOM   6003 C  CD2 . HIS A 1 765  ? 30.600 77.315  -26.742 1.00 8.45  ? 765  HIS A CD2 1 
ATOM   6004 C  CE1 . HIS A 1 765  ? 31.062 75.454  -25.666 1.00 8.03  ? 765  HIS A CE1 1 
ATOM   6005 N  NE2 . HIS A 1 765  ? 30.585 75.940  -26.802 1.00 10.79 ? 765  HIS A NE2 1 
ATOM   6006 N  N   . GLN A 1 766  ? 34.547 78.191  -25.874 1.00 12.63 ? 766  GLN A N   1 
ATOM   6007 C  CA  . GLN A 1 766  ? 35.451 78.101  -27.017 1.00 13.75 ? 766  GLN A CA  1 
ATOM   6008 C  C   . GLN A 1 766  ? 35.543 76.709  -27.559 1.00 12.20 ? 766  GLN A C   1 
ATOM   6009 O  O   . GLN A 1 766  ? 35.766 75.788  -26.786 1.00 11.62 ? 766  GLN A O   1 
ATOM   6010 C  CB  . GLN A 1 766  ? 36.882 78.536  -26.623 1.00 15.36 ? 766  GLN A CB  1 
ATOM   6011 C  CG  . GLN A 1 766  ? 36.940 79.827  -25.745 1.00 19.70 ? 766  GLN A CG  1 
ATOM   6012 C  CD  . GLN A 1 766  ? 38.014 79.766  -24.611 1.00 24.85 ? 766  GLN A CD  1 
ATOM   6013 O  OE1 . GLN A 1 766  ? 39.221 79.550  -24.889 1.00 25.37 ? 766  GLN A OE1 1 
ATOM   6014 N  NE2 . GLN A 1 766  ? 37.569 79.946  -23.331 1.00 20.80 ? 766  GLN A NE2 1 
ATOM   6015 N  N   . THR A 1 767  ? 35.385 76.561  -28.881 1.00 10.96 ? 767  THR A N   1 
ATOM   6016 C  CA  . THR A 1 767  ? 35.509 75.269  -29.531 1.00 11.01 ? 767  THR A CA  1 
ATOM   6017 C  C   . THR A 1 767  ? 36.768 75.312  -30.392 1.00 11.95 ? 767  THR A C   1 
ATOM   6018 O  O   . THR A 1 767  ? 36.877 76.107  -31.337 1.00 9.96  ? 767  THR A O   1 
ATOM   6019 C  CB  . THR A 1 767  ? 34.280 74.933  -30.392 1.00 12.06 ? 767  THR A CB  1 
ATOM   6020 O  OG1 . THR A 1 767  ? 33.116 74.970  -29.556 1.00 12.70 ? 767  THR A OG1 1 
ATOM   6021 C  CG2 . THR A 1 767  ? 34.421 73.527  -31.013 1.00 11.65 ? 767  THR A CG2 1 
ATOM   6022 N  N   . ILE A 1 768  ? 37.730 74.452  -30.053 1.00 9.98  ? 768  ILE A N   1 
ATOM   6023 C  CA  . ILE A 1 768  ? 39.001 74.436  -30.763 1.00 11.67 ? 768  ILE A CA  1 
ATOM   6024 C  C   . ILE A 1 768  ? 39.176 73.192  -31.584 1.00 11.21 ? 768  ILE A C   1 
ATOM   6025 O  O   . ILE A 1 768  ? 38.927 72.073  -31.107 1.00 11.46 ? 768  ILE A O   1 
ATOM   6026 C  CB  . ILE A 1 768  ? 40.168 74.558  -29.760 1.00 12.96 ? 768  ILE A CB  1 
ATOM   6027 C  CG1 . ILE A 1 768  ? 39.950 75.787  -28.867 1.00 14.46 ? 768  ILE A CG1 1 
ATOM   6028 C  CG2 . ILE A 1 768  ? 41.467 74.708  -30.495 1.00 15.46 ? 768  ILE A CG2 1 
ATOM   6029 C  CD1 . ILE A 1 768  ? 40.778 75.764  -27.594 1.00 16.37 ? 768  ILE A CD1 1 
ATOM   6030 N  N   . MET A 1 769  ? 39.643 73.381  -32.806 1.00 11.25 ? 769  MET A N   1 
ATOM   6031 C  CA  . MET A 1 769  ? 39.850 72.280  -33.736 1.00 13.35 ? 769  MET A CA  1 
ATOM   6032 C  C   . MET A 1 769  ? 41.288 72.154  -34.221 1.00 13.14 ? 769  MET A C   1 
ATOM   6033 O  O   . MET A 1 769  ? 41.878 73.125  -34.714 1.00 13.71 ? 769  MET A O   1 
ATOM   6034 C  CB  . MET A 1 769  ? 38.940 72.474  -34.948 1.00 13.60 ? 769  MET A CB  1 
ATOM   6035 C  CG  . MET A 1 769  ? 37.464 72.417  -34.594 1.00 17.26 ? 769  MET A CG  1 
ATOM   6036 S  SD  . MET A 1 769  ? 36.422 73.123  -35.902 1.00 19.49 ? 769  MET A SD  1 
ATOM   6037 C  CE  . MET A 1 769  ? 36.521 74.767  -35.439 1.00 22.56 ? 769  MET A CE  1 
ATOM   6038 N  N   . ARG A 1 770  ? 41.829 70.947  -34.122 1.00 12.76 ? 770  ARG A N   1 
ATOM   6039 C  CA  . ARG A 1 770  ? 43.193 70.699  -34.552 1.00 14.31 ? 770  ARG A CA  1 
ATOM   6040 C  C   . ARG A 1 770  ? 43.281 69.488  -35.472 1.00 14.45 ? 770  ARG A C   1 
ATOM   6041 O  O   . ARG A 1 770  ? 44.366 68.980  -35.737 1.00 14.60 ? 770  ARG A O   1 
ATOM   6042 C  CB  . ARG A 1 770  ? 44.077 70.478  -33.336 1.00 14.68 ? 770  ARG A CB  1 
ATOM   6043 C  CG  . ARG A 1 770  ? 44.076 71.647  -32.336 1.00 18.48 ? 770  ARG A CG  1 
ATOM   6044 C  CD  . ARG A 1 770  ? 45.112 71.424  -31.275 1.00 20.43 ? 770  ARG A CD  1 
ATOM   6045 N  NE  . ARG A 1 770  ? 45.151 72.467  -30.260 1.00 25.02 ? 770  ARG A NE  1 
ATOM   6046 C  CZ  . ARG A 1 770  ? 44.379 72.504  -29.178 1.00 27.12 ? 770  ARG A CZ  1 
ATOM   6047 N  NH1 . ARG A 1 770  ? 43.478 71.555  -28.953 1.00 28.88 ? 770  ARG A NH1 1 
ATOM   6048 N  NH2 . ARG A 1 770  ? 44.535 73.476  -28.287 1.00 30.58 ? 770  ARG A NH2 1 
ATOM   6049 N  N   . GLY A 1 771  ? 42.141 69.014  -35.944 1.00 15.15 ? 771  GLY A N   1 
ATOM   6050 C  CA  . GLY A 1 771  ? 42.190 67.870  -36.827 1.00 18.33 ? 771  GLY A CA  1 
ATOM   6051 C  C   . GLY A 1 771  ? 41.454 66.644  -36.349 1.00 19.13 ? 771  GLY A C   1 
ATOM   6052 O  O   . GLY A 1 771  ? 41.206 65.734  -37.157 1.00 21.43 ? 771  GLY A O   1 
ATOM   6053 N  N   . GLY A 1 772  ? 41.134 66.588  -35.054 1.00 18.33 ? 772  GLY A N   1 
ATOM   6054 C  CA  . GLY A 1 772  ? 40.403 65.446  -34.536 1.00 17.28 ? 772  GLY A CA  1 
ATOM   6055 C  C   . GLY A 1 772  ? 39.222 65.929  -33.705 1.00 15.92 ? 772  GLY A C   1 
ATOM   6056 O  O   . GLY A 1 772  ? 38.642 66.995  -33.966 1.00 15.63 ? 772  GLY A O   1 
ATOM   6057 N  N   . ALA A 1 773  ? 38.864 65.156  -32.704 1.00 14.27 ? 773  ALA A N   1 
ATOM   6058 C  CA  . ALA A 1 773  ? 37.767 65.549  -31.844 1.00 13.08 ? 773  ALA A CA  1 
ATOM   6059 C  C   . ALA A 1 773  ? 38.132 66.949  -31.343 1.00 12.89 ? 773  ALA A C   1 
ATOM   6060 O  O   . ALA A 1 773  ? 39.269 67.214  -30.949 1.00 13.16 ? 773  ALA A O   1 
ATOM   6061 C  CB  . ALA A 1 773  ? 37.643 64.599  -30.675 1.00 12.55 ? 773  ALA A CB  1 
ATOM   6062 N  N   . PRO A 1 774  ? 37.170 67.855  -31.354 1.00 11.68 ? 774  PRO A N   1 
ATOM   6063 C  CA  . PRO A 1 774  ? 37.470 69.214  -30.891 1.00 11.67 ? 774  PRO A CA  1 
ATOM   6064 C  C   . PRO A 1 774  ? 37.697 69.265  -29.365 1.00 12.21 ? 774  PRO A C   1 
ATOM   6065 O  O   . PRO A 1 774  ? 37.286 68.357  -28.621 1.00 11.84 ? 774  PRO A O   1 
ATOM   6066 C  CB  . PRO A 1 774  ? 36.218 69.993  -31.294 1.00 12.63 ? 774  PRO A CB  1 
ATOM   6067 C  CG  . PRO A 1 774  ? 35.115 68.966  -31.207 1.00 13.10 ? 774  PRO A CG  1 
ATOM   6068 C  CD  . PRO A 1 774  ? 35.781 67.733  -31.842 1.00 11.35 ? 774  PRO A CD  1 
ATOM   6069 N  N   . GLU A 1 775  ? 38.362 70.325  -28.926 1.00 11.94 ? 775  GLU A N   1 
ATOM   6070 C  CA  . GLU A 1 775  ? 38.586 70.575  -27.519 1.00 12.22 ? 775  GLU A CA  1 
ATOM   6071 C  C   . GLU A 1 775  ? 37.628 71.706  -27.176 1.00 12.31 ? 775  GLU A C   1 
ATOM   6072 O  O   . GLU A 1 775  ? 37.419 72.632  -27.960 1.00 11.50 ? 775  GLU A O   1 
ATOM   6073 C  CB  . GLU A 1 775  ? 40.025 71.015  -27.235 1.00 13.41 ? 775  GLU A CB  1 
ATOM   6074 C  CG  . GLU A 1 775  ? 40.253 71.510  -25.768 1.00 17.44 ? 775  GLU A CG  1 
ATOM   6075 C  CD  . GLU A 1 775  ? 41.668 72.052  -25.496 1.00 18.96 ? 775  GLU A CD  1 
ATOM   6076 O  OE1 . GLU A 1 775  ? 42.550 71.855  -26.331 1.00 23.15 ? 775  GLU A OE1 1 
ATOM   6077 O  OE2 . GLU A 1 775  ? 41.903 72.666  -24.432 1.00 20.14 ? 775  GLU A OE2 1 
ATOM   6078 N  N   . ILE A 1 776  ? 37.016 71.629  -26.012 1.00 11.63 ? 776  ILE A N   1 
ATOM   6079 C  CA  . ILE A 1 776  ? 36.097 72.688  -25.613 1.00 11.49 ? 776  ILE A CA  1 
ATOM   6080 C  C   . ILE A 1 776  ? 36.707 73.326  -24.370 1.00 11.15 ? 776  ILE A C   1 
ATOM   6081 O  O   . ILE A 1 776  ? 37.181 72.612  -23.481 1.00 11.02 ? 776  ILE A O   1 
ATOM   6082 C  CB  . ILE A 1 776  ? 34.732 72.128  -25.203 1.00 11.62 ? 776  ILE A CB  1 
ATOM   6083 C  CG1 . ILE A 1 776  ? 34.180 71.195  -26.295 1.00 13.03 ? 776  ILE A CG1 1 
ATOM   6084 C  CG2 . ILE A 1 776  ? 33.785 73.289  -24.827 1.00 11.27 ? 776  ILE A CG2 1 
ATOM   6085 C  CD1 . ILE A 1 776  ? 33.933 71.880  -27.646 1.00 12.86 ? 776  ILE A CD1 1 
ATOM   6086 N  N   . ARG A 1 777  ? 36.725 74.653  -24.308 1.00 10.40 ? 777  ARG A N   1 
ATOM   6087 C  CA  . ARG A 1 777  ? 37.209 75.338  -23.100 1.00 9.57  ? 777  ARG A CA  1 
ATOM   6088 C  C   . ARG A 1 777  ? 36.147 76.348  -22.672 1.00 10.91 ? 777  ARG A C   1 
ATOM   6089 O  O   . ARG A 1 777  ? 35.597 77.115  -23.509 1.00 9.85  ? 777  ARG A O   1 
ATOM   6090 C  CB  . ARG A 1 777  ? 38.545 76.072  -23.361 1.00 11.97 ? 777  ARG A CB  1 
ATOM   6091 C  CG  . ARG A 1 777  ? 39.700 75.177  -23.810 1.00 11.49 ? 777  ARG A CG  1 
ATOM   6092 C  CD  . ARG A 1 777  ? 41.035 75.947  -23.803 1.00 14.43 ? 777  ARG A CD  1 
ATOM   6093 N  NE  . ARG A 1 777  ? 42.104 75.128  -24.374 1.00 14.15 ? 777  ARG A NE  1 
ATOM   6094 C  CZ  . ARG A 1 777  ? 43.248 75.599  -24.871 1.00 16.92 ? 777  ARG A CZ  1 
ATOM   6095 N  NH1 . ARG A 1 777  ? 43.503 76.912  -24.864 1.00 16.15 ? 777  ARG A NH1 1 
ATOM   6096 N  NH2 . ARG A 1 777  ? 44.117 74.760  -25.437 1.00 15.84 ? 777  ARG A NH2 1 
ATOM   6097 N  N   . ASN A 1 778  ? 35.814 76.333  -21.387 1.00 8.85  ? 778  ASN A N   1 
ATOM   6098 C  CA  . ASN A 1 778  ? 34.868 77.292  -20.862 1.00 8.99  ? 778  ASN A CA  1 
ATOM   6099 C  C   . ASN A 1 778  ? 35.540 78.151  -19.794 1.00 9.38  ? 778  ASN A C   1 
ATOM   6100 O  O   . ASN A 1 778  ? 35.973 77.619  -18.745 1.00 8.21  ? 778  ASN A O   1 
ATOM   6101 C  CB  . ASN A 1 778  ? 33.668 76.617  -20.165 1.00 9.18  ? 778  ASN A CB  1 
ATOM   6102 C  CG  . ASN A 1 778  ? 32.707 75.955  -21.134 1.00 10.43 ? 778  ASN A CG  1 
ATOM   6103 O  OD1 . ASN A 1 778  ? 32.633 76.318  -22.328 1.00 8.53  ? 778  ASN A OD1 1 
ATOM   6104 N  ND2 . ASN A 1 778  ? 31.937 74.994  -20.616 1.00 9.55  ? 778  ASN A ND2 1 
ATOM   6105 N  N   . LEU A 1 779  ? 35.611 79.457  -20.027 1.00 8.79  ? 779  LEU A N   1 
ATOM   6106 C  CA  . LEU A 1 779  ? 36.147 80.348  -19.001 1.00 9.84  ? 779  LEU A CA  1 
ATOM   6107 C  C   . LEU A 1 779  ? 34.893 80.755  -18.208 1.00 9.16  ? 779  LEU A C   1 
ATOM   6108 O  O   . LEU A 1 779  ? 34.119 81.625  -18.621 1.00 9.42  ? 779  LEU A O   1 
ATOM   6109 C  CB  . LEU A 1 779  ? 36.837 81.559  -19.638 1.00 10.28 ? 779  LEU A CB  1 
ATOM   6110 C  CG  . LEU A 1 779  ? 37.357 82.642  -18.672 1.00 13.42 ? 779  LEU A CG  1 
ATOM   6111 C  CD1 . LEU A 1 779  ? 38.328 82.038  -17.644 1.00 14.59 ? 779  LEU A CD1 1 
ATOM   6112 C  CD2 . LEU A 1 779  ? 38.071 83.748  -19.484 1.00 14.78 ? 779  LEU A CD2 1 
ATOM   6113 N  N   . VAL A 1 780  ? 34.689 80.100  -17.073 1.00 9.91  ? 780  VAL A N   1 
ATOM   6114 C  CA  . VAL A 1 780  ? 33.512 80.325  -16.250 1.00 9.63  ? 780  VAL A CA  1 
ATOM   6115 C  C   . VAL A 1 780  ? 33.665 81.337  -15.107 1.00 11.13 ? 780  VAL A C   1 
ATOM   6116 O  O   . VAL A 1 780  ? 34.470 81.154  -14.206 1.00 11.25 ? 780  VAL A O   1 
ATOM   6117 C  CB  . VAL A 1 780  ? 32.982 78.963  -15.659 1.00 9.15  ? 780  VAL A CB  1 
ATOM   6118 C  CG1 . VAL A 1 780  ? 31.679 79.187  -14.887 1.00 7.14  ? 780  VAL A CG1 1 
ATOM   6119 C  CG2 . VAL A 1 780  ? 32.773 77.949  -16.791 1.00 6.73  ? 780  VAL A CG2 1 
ATOM   6120 N  N   . ASP A 1 781  ? 32.876 82.410  -15.178 1.00 10.42 ? 781  ASP A N   1 
ATOM   6121 C  CA  . ASP A 1 781  ? 32.860 83.445  -14.143 1.00 11.95 ? 781  ASP A CA  1 
ATOM   6122 C  C   . ASP A 1 781  ? 31.400 83.705  -13.803 1.00 11.39 ? 781  ASP A C   1 
ATOM   6123 O  O   . ASP A 1 781  ? 30.737 84.532  -14.437 1.00 10.67 ? 781  ASP A O   1 
ATOM   6124 C  CB  . ASP A 1 781  ? 33.500 84.735  -14.655 1.00 12.58 ? 781  ASP A CB  1 
ATOM   6125 C  CG  . ASP A 1 781  ? 33.620 85.811  -13.567 1.00 13.83 ? 781  ASP A CG  1 
ATOM   6126 O  OD1 . ASP A 1 781  ? 34.056 86.924  -13.904 1.00 16.08 ? 781  ASP A OD1 1 
ATOM   6127 O  OD2 . ASP A 1 781  ? 33.293 85.558  -12.396 1.00 14.07 ? 781  ASP A OD2 1 
ATOM   6128 N  N   . ILE A 1 782  ? 30.907 82.973  -12.822 1.00 11.43 ? 782  ILE A N   1 
ATOM   6129 C  CA  . ILE A 1 782  ? 29.521 83.081  -12.373 1.00 14.07 ? 782  ILE A CA  1 
ATOM   6130 C  C   . ILE A 1 782  ? 29.290 84.423  -11.631 1.00 17.26 ? 782  ILE A C   1 
ATOM   6131 O  O   . ILE A 1 782  ? 28.188 84.711  -11.162 1.00 18.07 ? 782  ILE A O   1 
ATOM   6132 C  CB  . ILE A 1 782  ? 29.209 81.885  -11.449 1.00 14.46 ? 782  ILE A CB  1 
ATOM   6133 C  CG1 . ILE A 1 782  ? 27.707 81.677  -11.294 1.00 15.12 ? 782  ILE A CG1 1 
ATOM   6134 C  CG2 . ILE A 1 782  ? 29.878 82.106  -10.098 1.00 14.43 ? 782  ILE A CG2 1 
ATOM   6135 C  CD1 . ILE A 1 782  ? 27.385 80.275  -10.696 1.00 11.21 ? 782  ILE A CD1 1 
ATOM   6136 N  N   . GLY A 1 783  ? 30.349 85.218  -11.515 1.00 18.93 ? 783  GLY A N   1 
ATOM   6137 C  CA  . GLY A 1 783  ? 30.247 86.545  -10.922 1.00 21.69 ? 783  GLY A CA  1 
ATOM   6138 C  C   . GLY A 1 783  ? 29.390 86.646  -9.689  1.00 22.71 ? 783  GLY A C   1 
ATOM   6139 O  O   . GLY A 1 783  ? 29.617 85.925  -8.715  1.00 22.93 ? 783  GLY A O   1 
ATOM   6140 N  N   . SER A 1 784  ? 28.394 87.518  -9.714  1.00 24.23 ? 784  SER A N   1 
ATOM   6141 C  CA  . SER A 1 784  ? 27.548 87.638  -8.529  1.00 27.20 ? 784  SER A CA  1 
ATOM   6142 C  C   . SER A 1 784  ? 26.114 87.103  -8.707  1.00 27.89 ? 784  SER A C   1 
ATOM   6143 O  O   . SER A 1 784  ? 25.194 87.496  -7.969  1.00 28.37 ? 784  SER A O   1 
ATOM   6144 C  CB  . SER A 1 784  ? 27.521 89.090  -8.037  1.00 28.23 ? 784  SER A CB  1 
ATOM   6145 O  OG  . SER A 1 784  ? 26.711 89.885  -8.890  1.00 30.79 ? 784  SER A OG  1 
ATOM   6146 N  N   . LEU A 1 785  ? 25.920 86.190  -9.660  1.00 26.81 ? 785  LEU A N   1 
ATOM   6147 C  CA  . LEU A 1 785  ? 24.596 85.620  -9.871  1.00 26.29 ? 785  LEU A CA  1 
ATOM   6148 C  C   . LEU A 1 785  ? 24.299 84.673  -8.721  1.00 26.09 ? 785  LEU A C   1 
ATOM   6149 O  O   . LEU A 1 785  ? 24.551 83.469  -8.816  1.00 27.09 ? 785  LEU A O   1 
ATOM   6150 C  CB  . LEU A 1 785  ? 24.549 84.836  -11.186 1.00 25.26 ? 785  LEU A CB  1 
ATOM   6151 C  CG  . LEU A 1 785  ? 24.854 85.580  -12.494 1.00 25.45 ? 785  LEU A CG  1 
ATOM   6152 C  CD1 . LEU A 1 785  ? 24.960 84.574  -13.608 1.00 23.27 ? 785  LEU A CD1 1 
ATOM   6153 C  CD2 . LEU A 1 785  ? 23.776 86.625  -12.798 1.00 24.80 ? 785  LEU A CD2 1 
ATOM   6154 N  N   . ASP A 1 786  ? 23.745 85.191  -7.638  1.00 25.02 ? 786  ASP A N   1 
ATOM   6155 C  CA  . ASP A 1 786  ? 23.436 84.331  -6.498  1.00 23.83 ? 786  ASP A CA  1 
ATOM   6156 C  C   . ASP A 1 786  ? 22.382 83.256  -6.769  1.00 21.51 ? 786  ASP A C   1 
ATOM   6157 O  O   . ASP A 1 786  ? 21.516 83.397  -7.643  1.00 19.45 ? 786  ASP A O   1 
ATOM   6158 C  CB  . ASP A 1 786  ? 23.008 85.169  -5.298  1.00 25.95 ? 786  ASP A CB  1 
ATOM   6159 C  CG  . ASP A 1 786  ? 24.188 85.812  -4.585  1.00 28.48 ? 786  ASP A CG  1 
ATOM   6160 O  OD1 . ASP A 1 786  ? 25.331 85.819  -5.124  1.00 29.49 ? 786  ASP A OD1 1 
ATOM   6161 O  OD2 . ASP A 1 786  ? 23.955 86.310  -3.467  1.00 30.09 ? 786  ASP A OD2 1 
ATOM   6162 N  N   . ASN A 1 787  ? 22.499 82.167  -6.018  1.00 18.98 ? 787  ASN A N   1 
ATOM   6163 C  CA  . ASN A 1 787  ? 21.582 81.042  -6.133  1.00 18.71 ? 787  ASN A CA  1 
ATOM   6164 C  C   . ASN A 1 787  ? 21.360 80.628  -7.564  1.00 16.74 ? 787  ASN A C   1 
ATOM   6165 O  O   . ASN A 1 787  ? 20.232 80.480  -8.016  1.00 15.57 ? 787  ASN A O   1 
ATOM   6166 C  CB  . ASN A 1 787  ? 20.251 81.390  -5.468  1.00 18.45 ? 787  ASN A CB  1 
ATOM   6167 C  CG  . ASN A 1 787  ? 20.415 81.605  -3.983  1.00 21.65 ? 787  ASN A CG  1 
ATOM   6168 O  OD1 . ASN A 1 787  ? 21.032 80.782  -3.293  1.00 21.92 ? 787  ASN A OD1 1 
ATOM   6169 N  ND2 . ASN A 1 787  ? 19.888 82.713  -3.480  1.00 22.06 ? 787  ASN A ND2 1 
ATOM   6170 N  N   . THR A 1 788  ? 22.459 80.432  -8.265  1.00 14.71 ? 788  THR A N   1 
ATOM   6171 C  CA  . THR A 1 788  ? 22.413 80.024  -9.652  1.00 14.26 ? 788  THR A CA  1 
ATOM   6172 C  C   . THR A 1 788  ? 23.421 78.884  -9.875  1.00 13.11 ? 788  THR A C   1 
ATOM   6173 O  O   . THR A 1 788  ? 24.491 78.898  -9.281  1.00 11.00 ? 788  THR A O   1 
ATOM   6174 C  CB  . THR A 1 788  ? 22.822 81.209  -10.561 1.00 15.09 ? 788  THR A CB  1 
ATOM   6175 O  OG1 . THR A 1 788  ? 21.918 82.309  -10.337 1.00 16.52 ? 788  THR A OG1 1 
ATOM   6176 C  CG2 . THR A 1 788  ? 22.788 80.789  -12.038 1.00 14.77 ? 788  THR A CG2 1 
ATOM   6177 N  N   . GLU A 1 789  ? 23.078 77.918  -10.725 1.00 11.75 ? 789  GLU A N   1 
ATOM   6178 C  CA  . GLU A 1 789  ? 24.004 76.833  -11.060 1.00 12.16 ? 789  GLU A CA  1 
ATOM   6179 C  C   . GLU A 1 789  ? 23.982 76.834  -12.583 1.00 12.28 ? 789  GLU A C   1 
ATOM   6180 O  O   . GLU A 1 789  ? 22.914 76.729  -13.178 1.00 13.73 ? 789  GLU A O   1 
ATOM   6181 C  CB  . GLU A 1 789  ? 23.544 75.460  -10.476 1.00 11.88 ? 789  GLU A CB  1 
ATOM   6182 C  CG  . GLU A 1 789  ? 23.328 75.494  -8.957  1.00 10.61 ? 789  GLU A CG  1 
ATOM   6183 C  CD  . GLU A 1 789  ? 23.504 74.135  -8.239  1.00 11.68 ? 789  GLU A CD  1 
ATOM   6184 O  OE1 . GLU A 1 789  ? 24.300 73.271  -8.718  1.00 11.68 ? 789  GLU A OE1 1 
ATOM   6185 O  OE2 . GLU A 1 789  ? 22.856 73.934  -7.183  1.00 11.46 ? 789  GLU A OE2 1 
ATOM   6186 N  N   . ILE A 1 790  ? 25.146 77.015  -13.202 1.00 11.19 ? 790  ILE A N   1 
ATOM   6187 C  CA  . ILE A 1 790  ? 25.271 77.037  -14.654 1.00 11.91 ? 790  ILE A CA  1 
ATOM   6188 C  C   . ILE A 1 790  ? 25.626 75.645  -15.171 1.00 12.60 ? 790  ILE A C   1 
ATOM   6189 O  O   . ILE A 1 790  ? 26.590 75.036  -14.709 1.00 12.95 ? 790  ILE A O   1 
ATOM   6190 C  CB  . ILE A 1 790  ? 26.358 78.042  -15.090 1.00 13.86 ? 790  ILE A CB  1 
ATOM   6191 C  CG1 . ILE A 1 790  ? 25.956 79.443  -14.581 1.00 15.15 ? 790  ILE A CG1 1 
ATOM   6192 C  CG2 . ILE A 1 790  ? 26.524 78.034  -16.633 1.00 13.46 ? 790  ILE A CG2 1 
ATOM   6193 C  CD1 . ILE A 1 790  ? 27.078 80.475  -14.613 1.00 20.12 ? 790  ILE A CD1 1 
ATOM   6194 N  N   . VAL A 1 791  ? 24.839 75.160  -16.126 1.00 10.88 ? 791  VAL A N   1 
ATOM   6195 C  CA  . VAL A 1 791  ? 25.036 73.847  -16.694 1.00 11.07 ? 791  VAL A CA  1 
ATOM   6196 C  C   . VAL A 1 791  ? 25.269 73.962  -18.183 1.00 10.50 ? 791  VAL A C   1 
ATOM   6197 O  O   . VAL A 1 791  ? 24.741 74.865  -18.842 1.00 10.46 ? 791  VAL A O   1 
ATOM   6198 C  CB  . VAL A 1 791  ? 23.790 72.947  -16.447 1.00 11.55 ? 791  VAL A CB  1 
ATOM   6199 C  CG1 . VAL A 1 791  ? 22.592 73.493  -17.190 1.00 11.55 ? 791  VAL A CG1 1 
ATOM   6200 C  CG2 . VAL A 1 791  ? 24.083 71.507  -16.877 1.00 11.24 ? 791  VAL A CG2 1 
ATOM   6201 N  N   . MET A 1 792  ? 26.098 73.065  -18.697 1.00 11.01 ? 792  MET A N   1 
ATOM   6202 C  CA  . MET A 1 792  ? 26.386 73.023  -20.118 1.00 10.66 ? 792  MET A CA  1 
ATOM   6203 C  C   . MET A 1 792  ? 25.743 71.725  -20.585 1.00 10.82 ? 792  MET A C   1 
ATOM   6204 O  O   . MET A 1 792  ? 26.034 70.666  -20.041 1.00 10.70 ? 792  MET A O   1 
ATOM   6205 C  CB  . MET A 1 792  ? 27.899 72.988  -20.387 1.00 11.13 ? 792  MET A CB  1 
ATOM   6206 C  CG  . MET A 1 792  ? 28.210 72.873  -21.890 1.00 8.34  ? 792  MET A CG  1 
ATOM   6207 S  SD  . MET A 1 792  ? 30.009 72.899  -22.249 1.00 12.03 ? 792  MET A SD  1 
ATOM   6208 C  CE  . MET A 1 792  ? 30.552 71.236  -21.528 1.00 9.67  ? 792  MET A CE  1 
ATOM   6209 N  N   . ARG A 1 793  ? 24.878 71.816  -21.588 1.00 10.58 ? 793  ARG A N   1 
ATOM   6210 C  CA  . ARG A 1 793  ? 24.173 70.657  -22.104 1.00 11.43 ? 793  ARG A CA  1 
ATOM   6211 C  C   . ARG A 1 793  ? 24.427 70.409  -23.584 1.00 11.90 ? 793  ARG A C   1 
ATOM   6212 O  O   . ARG A 1 793  ? 24.654 71.338  -24.357 1.00 11.71 ? 793  ARG A O   1 
ATOM   6213 C  CB  . ARG A 1 793  ? 22.647 70.830  -21.873 1.00 11.49 ? 793  ARG A CB  1 
ATOM   6214 C  CG  . ARG A 1 793  ? 21.750 69.657  -22.374 1.00 11.18 ? 793  ARG A CG  1 
ATOM   6215 C  CD  . ARG A 1 793  ? 20.239 69.919  -22.041 1.00 12.29 ? 793  ARG A CD  1 
ATOM   6216 N  NE  . ARG A 1 793  ? 19.988 69.964  -20.603 1.00 11.71 ? 793  ARG A NE  1 
ATOM   6217 C  CZ  . ARG A 1 793  ? 18.923 70.521  -20.016 1.00 13.14 ? 793  ARG A CZ  1 
ATOM   6218 N  NH1 . ARG A 1 793  ? 17.961 71.109  -20.733 1.00 12.76 ? 793  ARG A NH1 1 
ATOM   6219 N  NH2 . ARG A 1 793  ? 18.828 70.513  -18.694 1.00 12.45 ? 793  ARG A NH2 1 
ATOM   6220 N  N   . LEU A 1 794  ? 24.393 69.132  -23.954 1.00 11.76 ? 794  LEU A N   1 
ATOM   6221 C  CA  . LEU A 1 794  ? 24.520 68.689  -25.338 1.00 11.92 ? 794  LEU A CA  1 
ATOM   6222 C  C   . LEU A 1 794  ? 23.184 68.015  -25.697 1.00 13.50 ? 794  LEU A C   1 
ATOM   6223 O  O   . LEU A 1 794  ? 22.698 67.152  -24.950 1.00 12.25 ? 794  LEU A O   1 
ATOM   6224 C  CB  . LEU A 1 794  ? 25.680 67.685  -25.495 1.00 12.27 ? 794  LEU A CB  1 
ATOM   6225 C  CG  . LEU A 1 794  ? 27.096 68.299  -25.500 1.00 12.11 ? 794  LEU A CG  1 
ATOM   6226 C  CD1 . LEU A 1 794  ? 28.166 67.312  -25.008 1.00 12.70 ? 794  LEU A CD1 1 
ATOM   6227 C  CD2 . LEU A 1 794  ? 27.409 68.736  -26.906 1.00 13.36 ? 794  LEU A CD2 1 
ATOM   6228 N  N   . GLU A 1 795  ? 22.578 68.444  -26.812 1.00 12.55 ? 795  GLU A N   1 
ATOM   6229 C  CA  . GLU A 1 795  ? 21.332 67.868  -27.306 1.00 13.32 ? 795  GLU A CA  1 
ATOM   6230 C  C   . GLU A 1 795  ? 21.659 67.158  -28.627 1.00 13.41 ? 795  GLU A C   1 
ATOM   6231 O  O   . GLU A 1 795  ? 22.277 67.740  -29.530 1.00 11.09 ? 795  GLU A O   1 
ATOM   6232 C  CB  . GLU A 1 795  ? 20.283 68.971  -27.525 1.00 14.78 ? 795  GLU A CB  1 
ATOM   6233 C  CG  . GLU A 1 795  ? 20.083 69.812  -26.276 1.00 16.73 ? 795  GLU A CG  1 
ATOM   6234 C  CD  . GLU A 1 795  ? 19.150 71.006  -26.453 1.00 21.23 ? 795  GLU A CD  1 
ATOM   6235 O  OE1 . GLU A 1 795  ? 19.196 71.682  -27.509 1.00 22.42 ? 795  GLU A OE1 1 
ATOM   6236 O  OE2 . GLU A 1 795  ? 18.380 71.290  -25.521 1.00 21.18 ? 795  GLU A OE2 1 
ATOM   6237 N  N   . THR A 1 796  ? 21.324 65.874  -28.700 1.00 12.14 ? 796  THR A N   1 
ATOM   6238 C  CA  . THR A 1 796  ? 21.554 65.104  -29.901 1.00 13.31 ? 796  THR A CA  1 
ATOM   6239 C  C   . THR A 1 796  ? 20.268 64.319  -30.143 1.00 14.62 ? 796  THR A C   1 
ATOM   6240 O  O   . THR A 1 796  ? 19.307 64.388  -29.349 1.00 15.38 ? 796  THR A O   1 
ATOM   6241 C  CB  . THR A 1 796  ? 22.696 64.043  -29.748 1.00 14.66 ? 796  THR A CB  1 
ATOM   6242 O  OG1 . THR A 1 796  ? 22.222 62.978  -28.904 1.00 13.80 ? 796  THR A OG1 1 
ATOM   6243 C  CG2 . THR A 1 796  ? 23.969 64.667  -29.158 1.00 14.19 ? 796  THR A CG2 1 
ATOM   6244 N  N   . HIS A 1 797  ? 20.269 63.565  -31.226 1.00 15.38 ? 797  HIS A N   1 
ATOM   6245 C  CA  . HIS A 1 797  ? 19.136 62.730  -31.574 1.00 17.32 ? 797  HIS A CA  1 
ATOM   6246 C  C   . HIS A 1 797  ? 19.480 61.253  -31.323 1.00 17.49 ? 797  HIS A C   1 
ATOM   6247 O  O   . HIS A 1 797  ? 18.736 60.352  -31.707 1.00 19.20 ? 797  HIS A O   1 
ATOM   6248 C  CB  . HIS A 1 797  ? 18.721 63.034  -33.024 1.00 18.74 ? 797  HIS A CB  1 
ATOM   6249 C  CG  . HIS A 1 797  ? 18.141 64.413  -33.182 1.00 18.92 ? 797  HIS A CG  1 
ATOM   6250 N  ND1 . HIS A 1 797  ? 17.960 65.017  -34.403 1.00 18.57 ? 797  HIS A ND1 1 
ATOM   6251 C  CD2 . HIS A 1 797  ? 17.740 65.322  -32.254 1.00 20.52 ? 797  HIS A CD2 1 
ATOM   6252 C  CE1 . HIS A 1 797  ? 17.479 66.236  -34.230 1.00 18.41 ? 797  HIS A CE1 1 
ATOM   6253 N  NE2 . HIS A 1 797  ? 17.331 66.449  -32.934 1.00 20.66 ? 797  HIS A NE2 1 
ATOM   6254 N  N   . ILE A 1 798  ? 20.595 61.019  -30.623 1.00 16.67 ? 798  ILE A N   1 
ATOM   6255 C  CA  . ILE A 1 798  ? 21.024 59.663  -30.262 1.00 15.56 ? 798  ILE A CA  1 
ATOM   6256 C  C   . ILE A 1 798  ? 19.902 59.061  -29.426 1.00 15.47 ? 798  ILE A C   1 
ATOM   6257 O  O   . ILE A 1 798  ? 19.379 59.691  -28.507 1.00 13.65 ? 798  ILE A O   1 
ATOM   6258 C  CB  . ILE A 1 798  ? 22.343 59.678  -29.425 1.00 16.36 ? 798  ILE A CB  1 
ATOM   6259 C  CG1 . ILE A 1 798  ? 23.495 60.203  -30.295 1.00 15.22 ? 798  ILE A CG1 1 
ATOM   6260 C  CG2 . ILE A 1 798  ? 22.653 58.256  -28.886 1.00 13.93 ? 798  ILE A CG2 1 
ATOM   6261 C  CD1 . ILE A 1 798  ? 24.838 60.391  -29.542 1.00 14.28 ? 798  ILE A CD1 1 
ATOM   6262 N  N   . ASP A 1 799  ? 19.531 57.831  -29.757 1.00 15.84 ? 799  ASP A N   1 
ATOM   6263 C  CA  . ASP A 1 799  ? 18.443 57.156  -29.076 1.00 15.68 ? 799  ASP A CA  1 
ATOM   6264 C  C   . ASP A 1 799  ? 18.953 56.359  -27.870 1.00 15.65 ? 799  ASP A C   1 
ATOM   6265 O  O   . ASP A 1 799  ? 18.940 55.124  -27.881 1.00 13.85 ? 799  ASP A O   1 
ATOM   6266 C  CB  . ASP A 1 799  ? 17.752 56.221  -30.070 1.00 17.88 ? 799  ASP A CB  1 
ATOM   6267 C  CG  . ASP A 1 799  ? 16.458 55.644  -29.525 1.00 18.68 ? 799  ASP A CG  1 
ATOM   6268 O  OD1 . ASP A 1 799  ? 15.973 54.666  -30.113 1.00 21.20 ? 799  ASP A OD1 1 
ATOM   6269 O  OD2 . ASP A 1 799  ? 15.929 56.156  -28.515 1.00 21.15 ? 799  ASP A OD2 1 
ATOM   6270 N  N   . SER A 1 800  ? 19.399 57.078  -26.839 1.00 15.67 ? 800  SER A N   1 
ATOM   6271 C  CA  . SER A 1 800  ? 19.952 56.472  -25.616 1.00 14.33 ? 800  SER A CA  1 
ATOM   6272 C  C   . SER A 1 800  ? 18.878 56.097  -24.586 1.00 14.56 ? 800  SER A C   1 
ATOM   6273 O  O   . SER A 1 800  ? 19.135 55.326  -23.661 1.00 14.20 ? 800  SER A O   1 
ATOM   6274 C  CB  . SER A 1 800  ? 20.944 57.449  -24.972 1.00 14.19 ? 800  SER A CB  1 
ATOM   6275 O  OG  . SER A 1 800  ? 20.328 58.708  -24.766 1.00 12.50 ? 800  SER A OG  1 
ATOM   6276 N  N   . GLY A 1 801  ? 17.676 56.647  -24.734 1.00 14.23 ? 801  GLY A N   1 
ATOM   6277 C  CA  . GLY A 1 801  ? 16.602 56.306  -23.814 1.00 13.11 ? 801  GLY A CA  1 
ATOM   6278 C  C   . GLY A 1 801  ? 16.912 56.800  -22.427 1.00 12.74 ? 801  GLY A C   1 
ATOM   6279 O  O   . GLY A 1 801  ? 17.095 57.996  -22.249 1.00 13.66 ? 801  GLY A O   1 
ATOM   6280 N  N   . ASP A 1 802  ? 16.979 55.898  -21.449 1.00 11.70 ? 802  ASP A N   1 
ATOM   6281 C  CA  . ASP A 1 802  ? 17.268 56.277  -20.065 1.00 11.67 ? 802  ASP A CA  1 
ATOM   6282 C  C   . ASP A 1 802  ? 18.666 55.804  -19.604 1.00 12.36 ? 802  ASP A C   1 
ATOM   6283 O  O   . ASP A 1 802  ? 18.975 55.806  -18.406 1.00 12.81 ? 802  ASP A O   1 
ATOM   6284 C  CB  . ASP A 1 802  ? 16.198 55.690  -19.130 1.00 12.28 ? 802  ASP A CB  1 
ATOM   6285 C  CG  . ASP A 1 802  ? 16.069 54.172  -19.243 1.00 13.89 ? 802  ASP A CG  1 
ATOM   6286 O  OD1 . ASP A 1 802  ? 15.201 53.606  -18.529 1.00 16.13 ? 802  ASP A OD1 1 
ATOM   6287 O  OD2 . ASP A 1 802  ? 16.810 53.534  -20.031 1.00 14.03 ? 802  ASP A OD2 1 
ATOM   6288 N  N   . ILE A 1 803  ? 19.505 55.416  -20.555 1.00 11.66 ? 803  ILE A N   1 
ATOM   6289 C  CA  . ILE A 1 803  ? 20.844 54.934  -20.237 1.00 10.85 ? 803  ILE A CA  1 
ATOM   6290 C  C   . ILE A 1 803  ? 21.952 55.934  -20.567 1.00 11.24 ? 803  ILE A C   1 
ATOM   6291 O  O   . ILE A 1 803  ? 21.921 56.597  -21.608 1.00 10.06 ? 803  ILE A O   1 
ATOM   6292 C  CB  . ILE A 1 803  ? 21.179 53.640  -21.059 1.00 11.03 ? 803  ILE A CB  1 
ATOM   6293 C  CG1 . ILE A 1 803  ? 20.195 52.505  -20.726 1.00 12.00 ? 803  ILE A CG1 1 
ATOM   6294 C  CG2 . ILE A 1 803  ? 22.627 53.228  -20.814 1.00 9.96  ? 803  ILE A CG2 1 
ATOM   6295 C  CD1 . ILE A 1 803  ? 20.099 52.145  -19.210 1.00 11.38 ? 803  ILE A CD1 1 
ATOM   6296 N  N   . PHE A 1 804  ? 22.932 56.038  -19.677 1.00 9.68  ? 804  PHE A N   1 
ATOM   6297 C  CA  . PHE A 1 804  ? 24.120 56.846  -19.949 1.00 10.14 ? 804  PHE A CA  1 
ATOM   6298 C  C   . PHE A 1 804  ? 25.265 56.232  -19.119 1.00 11.16 ? 804  PHE A C   1 
ATOM   6299 O  O   . PHE A 1 804  ? 25.021 55.372  -18.248 1.00 12.01 ? 804  PHE A O   1 
ATOM   6300 C  CB  . PHE A 1 804  ? 23.906 58.360  -19.651 1.00 7.66  ? 804  PHE A CB  1 
ATOM   6301 C  CG  . PHE A 1 804  ? 23.528 58.698  -18.213 1.00 8.67  ? 804  PHE A CG  1 
ATOM   6302 C  CD1 . PHE A 1 804  ? 24.461 59.333  -17.357 1.00 8.33  ? 804  PHE A CD1 1 
ATOM   6303 C  CD2 . PHE A 1 804  ? 22.250 58.429  -17.724 1.00 7.99  ? 804  PHE A CD2 1 
ATOM   6304 C  CE1 . PHE A 1 804  ? 24.116 59.683  -16.064 1.00 6.88  ? 804  PHE A CE1 1 
ATOM   6305 C  CE2 . PHE A 1 804  ? 21.889 58.774  -16.402 1.00 7.29  ? 804  PHE A CE2 1 
ATOM   6306 C  CZ  . PHE A 1 804  ? 22.818 59.398  -15.577 1.00 8.02  ? 804  PHE A CZ  1 
ATOM   6307 N  N   . TYR A 1 805  ? 26.493 56.653  -19.399 1.00 10.50 ? 805  TYR A N   1 
ATOM   6308 C  CA  . TYR A 1 805  ? 27.656 56.133  -18.689 1.00 10.09 ? 805  TYR A CA  1 
ATOM   6309 C  C   . TYR A 1 805  ? 28.478 57.273  -18.118 1.00 9.58  ? 805  TYR A C   1 
ATOM   6310 O  O   . TYR A 1 805  ? 28.594 58.320  -18.742 1.00 8.41  ? 805  TYR A O   1 
ATOM   6311 C  CB  . TYR A 1 805  ? 28.533 55.318  -19.630 1.00 8.86  ? 805  TYR A CB  1 
ATOM   6312 C  CG  . TYR A 1 805  ? 27.846 54.082  -20.179 1.00 9.94  ? 805  TYR A CG  1 
ATOM   6313 C  CD1 . TYR A 1 805  ? 26.835 54.189  -21.164 1.00 8.98  ? 805  TYR A CD1 1 
ATOM   6314 C  CD2 . TYR A 1 805  ? 28.173 52.807  -19.701 1.00 8.81  ? 805  TYR A CD2 1 
ATOM   6315 C  CE1 . TYR A 1 805  ? 26.181 53.058  -21.656 1.00 9.48  ? 805  TYR A CE1 1 
ATOM   6316 C  CE2 . TYR A 1 805  ? 27.510 51.642  -20.200 1.00 9.65  ? 805  TYR A CE2 1 
ATOM   6317 C  CZ  . TYR A 1 805  ? 26.522 51.791  -21.183 1.00 8.69  ? 805  TYR A CZ  1 
ATOM   6318 O  OH  . TYR A 1 805  ? 25.906 50.683  -21.748 1.00 8.57  ? 805  TYR A OH  1 
ATOM   6319 N  N   . THR A 1 806  ? 29.021 57.066  -16.918 1.00 8.59  ? 806  THR A N   1 
ATOM   6320 C  CA  . THR A 1 806  ? 29.885 58.054  -16.274 1.00 8.41  ? 806  THR A CA  1 
ATOM   6321 C  C   . THR A 1 806  ? 31.064 57.259  -15.668 1.00 8.19  ? 806  THR A C   1 
ATOM   6322 O  O   . THR A 1 806  ? 30.924 56.077  -15.400 1.00 9.12  ? 806  THR A O   1 
ATOM   6323 C  CB  . THR A 1 806  ? 29.156 58.817  -15.157 1.00 8.67  ? 806  THR A CB  1 
ATOM   6324 O  OG1 . THR A 1 806  ? 28.758 57.897  -14.123 1.00 10.34 ? 806  THR A OG1 1 
ATOM   6325 C  CG2 . THR A 1 806  ? 27.918 59.544  -15.715 1.00 6.19  ? 806  THR A CG2 1 
ATOM   6326 N  N   . ASP A 1 807  ? 32.213 57.894  -15.446 1.00 7.56  ? 807  ASP A N   1 
ATOM   6327 C  CA  . ASP A 1 807  ? 33.331 57.149  -14.899 1.00 7.72  ? 807  ASP A CA  1 
ATOM   6328 C  C   . ASP A 1 807  ? 33.416 57.223  -13.375 1.00 8.67  ? 807  ASP A C   1 
ATOM   6329 O  O   . ASP A 1 807  ? 32.779 58.084  -12.731 1.00 8.55  ? 807  ASP A O   1 
ATOM   6330 C  CB  . ASP A 1 807  ? 34.674 57.617  -15.508 1.00 6.71  ? 807  ASP A CB  1 
ATOM   6331 C  CG  . ASP A 1 807  ? 35.113 58.956  -15.006 1.00 9.32  ? 807  ASP A CG  1 
ATOM   6332 O  OD1 . ASP A 1 807  ? 36.273 59.056  -14.574 1.00 10.03 ? 807  ASP A OD1 1 
ATOM   6333 O  OD2 . ASP A 1 807  ? 34.315 59.912  -15.040 1.00 10.93 ? 807  ASP A OD2 1 
ATOM   6334 N  N   . LEU A 1 808  ? 34.174 56.285  -12.807 1.00 7.42  ? 808  LEU A N   1 
ATOM   6335 C  CA  . LEU A 1 808  ? 34.402 56.272  -11.372 1.00 8.15  ? 808  LEU A CA  1 
ATOM   6336 C  C   . LEU A 1 808  ? 35.908 56.478  -11.180 1.00 7.88  ? 808  LEU A C   1 
ATOM   6337 O  O   . LEU A 1 808  ? 36.718 55.620  -11.548 1.00 8.58  ? 808  LEU A O   1 
ATOM   6338 C  CB  . LEU A 1 808  ? 33.932 54.949  -10.721 1.00 7.25  ? 808  LEU A CB  1 
ATOM   6339 C  CG  . LEU A 1 808  ? 32.408 54.738  -10.572 1.00 8.26  ? 808  LEU A CG  1 
ATOM   6340 C  CD1 . LEU A 1 808  ? 32.140 53.245  -10.294 1.00 7.30  ? 808  LEU A CD1 1 
ATOM   6341 C  CD2 . LEU A 1 808  ? 31.856 55.563  -9.383  1.00 7.55  ? 808  LEU A CD2 1 
ATOM   6342 N  N   . ASN A 1 809  ? 36.252 57.656  -10.654 1.00 7.26  ? 809  ASN A N   1 
ATOM   6343 C  CA  . ASN A 1 809  ? 37.619 58.028  -10.343 1.00 6.87  ? 809  ASN A CA  1 
ATOM   6344 C  C   . ASN A 1 809  ? 38.576 57.886  -11.501 1.00 6.44  ? 809  ASN A C   1 
ATOM   6345 O  O   . ASN A 1 809  ? 39.721 57.546  -11.271 1.00 5.27  ? 809  ASN A O   1 
ATOM   6346 C  CB  . ASN A 1 809  ? 38.134 57.172  -9.182  1.00 5.31  ? 809  ASN A CB  1 
ATOM   6347 C  CG  . ASN A 1 809  ? 37.119 57.067  -8.051  1.00 6.96  ? 809  ASN A CG  1 
ATOM   6348 O  OD1 . ASN A 1 809  ? 36.274 56.146  -8.014  1.00 6.22  ? 809  ASN A OD1 1 
ATOM   6349 N  ND2 . ASN A 1 809  ? 37.156 58.038  -7.150  1.00 4.50  ? 809  ASN A ND2 1 
ATOM   6350 N  N   . GLY A 1 810  ? 38.129 58.155  -12.726 1.00 7.22  ? 810  GLY A N   1 
ATOM   6351 C  CA  . GLY A 1 810  ? 39.028 58.037  -13.868 1.00 7.97  ? 810  GLY A CA  1 
ATOM   6352 C  C   . GLY A 1 810  ? 39.561 56.615  -14.084 1.00 10.20 ? 810  GLY A C   1 
ATOM   6353 O  O   . GLY A 1 810  ? 40.551 56.390  -14.820 1.00 11.09 ? 810  GLY A O   1 
ATOM   6354 N  N   . LEU A 1 811  ? 38.909 55.647  -13.458 1.00 8.44  ? 811  LEU A N   1 
ATOM   6355 C  CA  . LEU A 1 811  ? 39.355 54.261  -13.546 1.00 10.46 ? 811  LEU A CA  1 
ATOM   6356 C  C   . LEU A 1 811  ? 38.472 53.333  -14.385 1.00 10.56 ? 811  LEU A C   1 
ATOM   6357 O  O   . LEU A 1 811  ? 38.972 52.439  -15.077 1.00 11.52 ? 811  LEU A O   1 
ATOM   6358 C  CB  . LEU A 1 811  ? 39.481 53.670  -12.132 1.00 10.27 ? 811  LEU A CB  1 
ATOM   6359 C  CG  . LEU A 1 811  ? 39.806 52.171  -12.035 1.00 13.23 ? 811  LEU A CG  1 
ATOM   6360 C  CD1 . LEU A 1 811  ? 41.245 51.938  -12.532 1.00 13.08 ? 811  LEU A CD1 1 
ATOM   6361 C  CD2 . LEU A 1 811  ? 39.638 51.683  -10.569 1.00 13.49 ? 811  LEU A CD2 1 
ATOM   6362 N  N   . GLN A 1 812  ? 37.164 53.554  -14.347 1.00 8.88  ? 812  GLN A N   1 
ATOM   6363 C  CA  . GLN A 1 812  ? 36.249 52.672  -15.057 1.00 8.88  ? 812  GLN A CA  1 
ATOM   6364 C  C   . GLN A 1 812  ? 34.992 53.432  -15.384 1.00 8.90  ? 812  GLN A C   1 
ATOM   6365 O  O   . GLN A 1 812  ? 34.716 54.444  -14.749 1.00 8.82  ? 812  GLN A O   1 
ATOM   6366 C  CB  . GLN A 1 812  ? 35.849 51.526  -14.136 1.00 10.07 ? 812  GLN A CB  1 
ATOM   6367 C  CG  . GLN A 1 812  ? 35.318 52.025  -12.761 1.00 10.70 ? 812  GLN A CG  1 
ATOM   6368 C  CD  . GLN A 1 812  ? 35.011 50.872  -11.790 1.00 13.68 ? 812  GLN A CD  1 
ATOM   6369 O  OE1 . GLN A 1 812  ? 33.994 50.197  -11.913 1.00 12.88 ? 812  GLN A OE1 1 
ATOM   6370 N  NE2 . GLN A 1 812  ? 35.906 50.652  -10.826 1.00 14.30 ? 812  GLN A NE2 1 
ATOM   6371 N  N   . PHE A 1 813  ? 34.232 52.925  -16.353 1.00 7.13  ? 813  PHE A N   1 
ATOM   6372 C  CA  . PHE A 1 813  ? 32.968 53.539  -16.714 1.00 9.11  ? 813  PHE A CA  1 
ATOM   6373 C  C   . PHE A 1 813  ? 31.850 52.615  -16.281 1.00 9.99  ? 813  PHE A C   1 
ATOM   6374 O  O   . PHE A 1 813  ? 31.876 51.394  -16.535 1.00 10.53 ? 813  PHE A O   1 
ATOM   6375 C  CB  . PHE A 1 813  ? 32.902 53.811  -18.222 1.00 9.31  ? 813  PHE A CB  1 
ATOM   6376 C  CG  . PHE A 1 813  ? 33.627 55.060  -18.616 1.00 8.58  ? 813  PHE A CG  1 
ATOM   6377 C  CD1 . PHE A 1 813  ? 35.029 55.078  -18.674 1.00 7.63  ? 813  PHE A CD1 1 
ATOM   6378 C  CD2 . PHE A 1 813  ? 32.919 56.240  -18.838 1.00 10.43 ? 813  PHE A CD2 1 
ATOM   6379 C  CE1 . PHE A 1 813  ? 35.717 56.250  -18.946 1.00 7.03  ? 813  PHE A CE1 1 
ATOM   6380 C  CE2 . PHE A 1 813  ? 33.602 57.416  -19.108 1.00 10.40 ? 813  PHE A CE2 1 
ATOM   6381 C  CZ  . PHE A 1 813  ? 35.026 57.400  -19.160 1.00 8.11  ? 813  PHE A CZ  1 
ATOM   6382 N  N   . ILE A 1 814  ? 30.890 53.199  -15.589 1.00 9.18  ? 814  ILE A N   1 
ATOM   6383 C  CA  . ILE A 1 814  ? 29.782 52.443  -15.068 1.00 7.72  ? 814  ILE A CA  1 
ATOM   6384 C  C   . ILE A 1 814  ? 28.473 52.878  -15.729 1.00 8.78  ? 814  ILE A C   1 
ATOM   6385 O  O   . ILE A 1 814  ? 28.237 54.058  -15.989 1.00 6.60  ? 814  ILE A O   1 
ATOM   6386 C  CB  . ILE A 1 814  ? 29.739 52.612  -13.506 1.00 8.28  ? 814  ILE A CB  1 
ATOM   6387 C  CG1 . ILE A 1 814  ? 28.715 51.635  -12.889 1.00 7.62  ? 814  ILE A CG1 1 
ATOM   6388 C  CG2 . ILE A 1 814  ? 29.390 54.087  -13.128 1.00 5.33  ? 814  ILE A CG2 1 
ATOM   6389 C  CD1 . ILE A 1 814  ? 28.853 51.430  -11.328 1.00 6.58  ? 814  ILE A CD1 1 
ATOM   6390 N  N   . LYS A 1 815  ? 27.632 51.900  -16.024 1.00 9.20  ? 815  LYS A N   1 
ATOM   6391 C  CA  . LYS A 1 815  ? 26.345 52.161  -16.653 1.00 9.86  ? 815  LYS A CA  1 
ATOM   6392 C  C   . LYS A 1 815  ? 25.385 52.774  -15.662 1.00 9.60  ? 815  LYS A C   1 
ATOM   6393 O  O   . LYS A 1 815  ? 25.201 52.250  -14.550 1.00 11.10 ? 815  LYS A O   1 
ATOM   6394 C  CB  . LYS A 1 815  ? 25.754 50.844  -17.183 1.00 9.76  ? 815  LYS A CB  1 
ATOM   6395 C  CG  . LYS A 1 815  ? 24.403 50.958  -17.925 1.00 12.80 ? 815  LYS A CG  1 
ATOM   6396 C  CD  . LYS A 1 815  ? 24.039 49.553  -18.469 1.00 16.89 ? 815  LYS A CD  1 
ATOM   6397 C  CE  . LYS A 1 815  ? 22.811 49.575  -19.336 1.00 20.92 ? 815  LYS A CE  1 
ATOM   6398 N  NZ  . LYS A 1 815  ? 22.579 48.198  -19.914 1.00 23.59 ? 815  LYS A NZ  1 
ATOM   6399 N  N   . ARG A 1 816  ? 24.768 53.877  -16.067 1.00 9.00  ? 816  ARG A N   1 
ATOM   6400 C  CA  . ARG A 1 816  ? 23.797 54.583  -15.234 1.00 8.63  ? 816  ARG A CA  1 
ATOM   6401 C  C   . ARG A 1 816  ? 22.431 54.466  -15.894 1.00 8.95  ? 816  ARG A C   1 
ATOM   6402 O  O   . ARG A 1 816  ? 22.351 54.351  -17.121 1.00 7.59  ? 816  ARG A O   1 
ATOM   6403 C  CB  . ARG A 1 816  ? 24.132 56.081  -15.178 1.00 10.17 ? 816  ARG A CB  1 
ATOM   6404 C  CG  . ARG A 1 816  ? 25.524 56.393  -14.694 1.00 9.00  ? 816  ARG A CG  1 
ATOM   6405 C  CD  . ARG A 1 816  ? 25.670 55.852  -13.285 1.00 8.78  ? 816  ARG A CD  1 
ATOM   6406 N  NE  . ARG A 1 816  ? 26.844 56.391  -12.618 1.00 8.72  ? 816  ARG A NE  1 
ATOM   6407 C  CZ  . ARG A 1 816  ? 27.240 55.992  -11.412 1.00 10.34 ? 816  ARG A CZ  1 
ATOM   6408 N  NH1 . ARG A 1 816  ? 26.542 55.058  -10.793 1.00 6.81  ? 816  ARG A NH1 1 
ATOM   6409 N  NH2 . ARG A 1 816  ? 28.330 56.511  -10.839 1.00 9.28  ? 816  ARG A NH2 1 
ATOM   6410 N  N   . ARG A 1 817  ? 21.366 54.486  -15.095 1.00 7.99  ? 817  ARG A N   1 
ATOM   6411 C  CA  . ARG A 1 817  ? 20.014 54.457  -15.656 1.00 10.29 ? 817  ARG A CA  1 
ATOM   6412 C  C   . ARG A 1 817  ? 19.214 55.589  -14.985 1.00 9.94  ? 817  ARG A C   1 
ATOM   6413 O  O   . ARG A 1 817  ? 19.043 55.611  -13.764 1.00 11.60 ? 817  ARG A O   1 
ATOM   6414 C  CB  . ARG A 1 817  ? 19.299 53.091  -15.450 1.00 11.00 ? 817  ARG A CB  1 
ATOM   6415 C  CG  . ARG A 1 817  ? 17.813 53.116  -15.957 1.00 12.42 ? 817  ARG A CG  1 
ATOM   6416 C  CD  . ARG A 1 817  ? 17.015 51.815  -15.679 1.00 12.83 ? 817  ARG A CD  1 
ATOM   6417 N  NE  . ARG A 1 817  ? 17.498 50.757  -16.552 1.00 14.53 ? 817  ARG A NE  1 
ATOM   6418 C  CZ  . ARG A 1 817  ? 18.269 49.756  -16.158 1.00 15.30 ? 817  ARG A CZ  1 
ATOM   6419 N  NH1 . ARG A 1 817  ? 18.622 49.662  -14.883 1.00 14.99 ? 817  ARG A NH1 1 
ATOM   6420 N  NH2 . ARG A 1 817  ? 18.731 48.890  -17.053 1.00 15.62 ? 817  ARG A NH2 1 
ATOM   6421 N  N   . ARG A 1 818  ? 18.786 56.556  -15.790 1.00 10.04 ? 818  ARG A N   1 
ATOM   6422 C  CA  . ARG A 1 818  ? 18.010 57.700  -15.298 1.00 11.27 ? 818  ARG A CA  1 
ATOM   6423 C  C   . ARG A 1 818  ? 16.715 57.117  -14.731 1.00 11.50 ? 818  ARG A C   1 
ATOM   6424 O  O   . ARG A 1 818  ? 16.057 56.334  -15.411 1.00 12.70 ? 818  ARG A O   1 
ATOM   6425 C  CB  . ARG A 1 818  ? 17.667 58.644  -16.468 1.00 12.02 ? 818  ARG A CB  1 
ATOM   6426 C  CG  . ARG A 1 818  ? 16.948 59.937  -16.042 1.00 14.07 ? 818  ARG A CG  1 
ATOM   6427 C  CD  . ARG A 1 818  ? 16.307 60.662  -17.247 1.00 14.49 ? 818  ARG A CD  1 
ATOM   6428 N  NE  . ARG A 1 818  ? 15.018 60.029  -17.571 1.00 16.69 ? 818  ARG A NE  1 
ATOM   6429 C  CZ  . ARG A 1 818  ? 14.720 59.421  -18.720 1.00 17.02 ? 818  ARG A CZ  1 
ATOM   6430 N  NH1 . ARG A 1 818  ? 15.611 59.348  -19.719 1.00 14.46 ? 818  ARG A NH1 1 
ATOM   6431 N  NH2 . ARG A 1 818  ? 13.518 58.842  -18.848 1.00 15.89 ? 818  ARG A NH2 1 
ATOM   6432 N  N   . LEU A 1 819  ? 16.353 57.478  -13.511 1.00 10.66 ? 819  LEU A N   1 
ATOM   6433 C  CA  . LEU A 1 819  ? 15.147 56.920  -12.903 1.00 12.15 ? 819  LEU A CA  1 
ATOM   6434 C  C   . LEU A 1 819  ? 14.170 58.043  -12.621 1.00 13.05 ? 819  LEU A C   1 
ATOM   6435 O  O   . LEU A 1 819  ? 14.435 58.904  -11.768 1.00 12.59 ? 819  LEU A O   1 
ATOM   6436 C  CB  . LEU A 1 819  ? 15.492 56.200  -11.595 1.00 11.27 ? 819  LEU A CB  1 
ATOM   6437 C  CG  . LEU A 1 819  ? 16.364 54.943  -11.760 1.00 10.78 ? 819  LEU A CG  1 
ATOM   6438 C  CD1 . LEU A 1 819  ? 16.845 54.473  -10.405 1.00 10.44 ? 819  LEU A CD1 1 
ATOM   6439 C  CD2 . LEU A 1 819  ? 15.555 53.818  -12.486 1.00 11.08 ? 819  LEU A CD2 1 
ATOM   6440 N  N   . ASP A 1 820  ? 13.048 58.044  -13.340 1.00 12.87 ? 820  ASP A N   1 
ATOM   6441 C  CA  . ASP A 1 820  ? 12.084 59.108  -13.131 1.00 14.38 ? 820  ASP A CA  1 
ATOM   6442 C  C   . ASP A 1 820  ? 11.367 58.963  -11.798 1.00 14.00 ? 820  ASP A C   1 
ATOM   6443 O  O   . ASP A 1 820  ? 10.737 59.915  -11.316 1.00 13.29 ? 820  ASP A O   1 
ATOM   6444 C  CB  . ASP A 1 820  ? 11.119 59.203  -14.325 1.00 15.78 ? 820  ASP A CB  1 
ATOM   6445 C  CG  . ASP A 1 820  ? 11.851 59.566  -15.641 1.00 19.42 ? 820  ASP A CG  1 
ATOM   6446 O  OD1 . ASP A 1 820  ? 12.912 60.260  -15.609 1.00 21.09 ? 820  ASP A OD1 1 
ATOM   6447 O  OD2 . ASP A 1 820  ? 11.368 59.160  -16.714 1.00 18.60 ? 820  ASP A OD2 1 
ATOM   6448 N  N   . LYS A 1 821  ? 11.487 57.796  -11.163 1.00 13.18 ? 821  LYS A N   1 
ATOM   6449 C  CA  . LYS A 1 821  ? 10.848 57.660  -9.838  1.00 14.56 ? 821  LYS A CA  1 
ATOM   6450 C  C   . LYS A 1 821  ? 11.690 58.428  -8.807  1.00 14.33 ? 821  LYS A C   1 
ATOM   6451 O  O   . LYS A 1 821  ? 11.286 58.579  -7.664  1.00 15.75 ? 821  LYS A O   1 
ATOM   6452 C  CB  . LYS A 1 821  ? 10.708 56.189  -9.395  1.00 14.42 ? 821  LYS A CB  1 
ATOM   6453 C  CG  . LYS A 1 821  ? 12.031 55.471  -9.212  1.00 14.98 ? 821  LYS A CG  1 
ATOM   6454 C  CD  . LYS A 1 821  ? 11.851 53.965  -9.065  1.00 15.14 ? 821  LYS A CD  1 
ATOM   6455 C  CE  . LYS A 1 821  ? 13.194 53.279  -9.022  1.00 15.92 ? 821  LYS A CE  1 
ATOM   6456 N  NZ  . LYS A 1 821  ? 13.071 51.807  -9.085  1.00 13.32 ? 821  LYS A NZ  1 
ATOM   6457 N  N   . LEU A 1 822  ? 12.855 58.929  -9.212  1.00 13.80 ? 822  LEU A N   1 
ATOM   6458 C  CA  . LEU A 1 822  ? 13.688 59.704  -8.285  1.00 12.37 ? 822  LEU A CA  1 
ATOM   6459 C  C   . LEU A 1 822  ? 13.743 61.156  -8.746  1.00 12.93 ? 822  LEU A C   1 
ATOM   6460 O  O   . LEU A 1 822  ? 13.623 61.432  -9.938  1.00 12.10 ? 822  LEU A O   1 
ATOM   6461 C  CB  . LEU A 1 822  ? 15.122 59.162  -8.258  1.00 12.36 ? 822  LEU A CB  1 
ATOM   6462 C  CG  . LEU A 1 822  ? 15.293 57.700  -7.793  1.00 12.90 ? 822  LEU A CG  1 
ATOM   6463 C  CD1 . LEU A 1 822  ? 16.759 57.379  -7.688  1.00 10.70 ? 822  LEU A CD1 1 
ATOM   6464 C  CD2 . LEU A 1 822  ? 14.629 57.522  -6.411  1.00 11.72 ? 822  LEU A CD2 1 
ATOM   6465 N  N   . PRO A 1 823  ? 13.937 62.093  -7.811  1.00 12.53 ? 823  PRO A N   1 
ATOM   6466 C  CA  . PRO A 1 823  ? 14.017 63.510  -8.167  1.00 12.49 ? 823  PRO A CA  1 
ATOM   6467 C  C   . PRO A 1 823  ? 15.251 63.813  -9.030  1.00 14.48 ? 823  PRO A C   1 
ATOM   6468 O  O   . PRO A 1 823  ? 16.252 63.069  -9.032  1.00 13.27 ? 823  PRO A O   1 
ATOM   6469 C  CB  . PRO A 1 823  ? 14.042 64.211  -6.817  1.00 12.75 ? 823  PRO A CB  1 
ATOM   6470 C  CG  . PRO A 1 823  ? 14.695 63.230  -5.909  1.00 13.51 ? 823  PRO A CG  1 
ATOM   6471 C  CD  . PRO A 1 823  ? 14.029 61.904  -6.353  1.00 12.62 ? 823  PRO A CD  1 
ATOM   6472 N  N   . LEU A 1 824  ? 15.172 64.924  -9.761  1.00 13.09 ? 824  LEU A N   1 
ATOM   6473 C  CA  . LEU A 1 824  ? 16.238 65.333  -10.668 1.00 13.02 ? 824  LEU A CA  1 
ATOM   6474 C  C   . LEU A 1 824  ? 17.671 65.206  -10.093 1.00 13.09 ? 824  LEU A C   1 
ATOM   6475 O  O   . LEU A 1 824  ? 18.578 64.627  -10.723 1.00 10.81 ? 824  LEU A O   1 
ATOM   6476 C  CB  . LEU A 1 824  ? 15.983 66.792  -11.074 1.00 12.71 ? 824  LEU A CB  1 
ATOM   6477 C  CG  . LEU A 1 824  ? 16.756 67.345  -12.281 1.00 14.04 ? 824  LEU A CG  1 
ATOM   6478 C  CD1 . LEU A 1 824  ? 15.912 68.533  -12.861 1.00 12.68 ? 824  LEU A CD1 1 
ATOM   6479 C  CD2 . LEU A 1 824  ? 18.210 67.788  -11.912 1.00 10.90 ? 824  LEU A CD2 1 
ATOM   6480 N  N   . GLN A 1 825  ? 17.851 65.737  -8.885  1.00 11.96 ? 825  GLN A N   1 
ATOM   6481 C  CA  . GLN A 1 825  ? 19.162 65.770  -8.268  1.00 11.28 ? 825  GLN A CA  1 
ATOM   6482 C  C   . GLN A 1 825  ? 19.739 64.403  -7.988  1.00 11.92 ? 825  GLN A C   1 
ATOM   6483 O  O   . GLN A 1 825  ? 20.969 64.258  -7.850  1.00 11.66 ? 825  GLN A O   1 
ATOM   6484 C  CB  . GLN A 1 825  ? 19.129 66.623  -6.992  1.00 11.00 ? 825  GLN A CB  1 
ATOM   6485 C  CG  . GLN A 1 825  ? 18.214 66.115  -5.853  1.00 11.41 ? 825  GLN A CG  1 
ATOM   6486 C  CD  . GLN A 1 825  ? 16.776 66.611  -5.932  1.00 12.61 ? 825  GLN A CD  1 
ATOM   6487 O  OE1 . GLN A 1 825  ? 16.318 67.071  -6.980  1.00 13.20 ? 825  GLN A OE1 1 
ATOM   6488 N  NE2 . GLN A 1 825  ? 16.048 66.498  -4.815  1.00 12.36 ? 825  GLN A NE2 1 
ATOM   6489 N  N   . ALA A 1 826  ? 18.861 63.406  -7.905  1.00 10.20 ? 826  ALA A N   1 
ATOM   6490 C  CA  . ALA A 1 826  ? 19.295 62.033  -7.652  1.00 10.15 ? 826  ALA A CA  1 
ATOM   6491 C  C   . ALA A 1 826  ? 19.848 61.431  -8.945  1.00 10.83 ? 826  ALA A C   1 
ATOM   6492 O  O   . ALA A 1 826  ? 20.613 60.474  -8.914  1.00 10.23 ? 826  ALA A O   1 
ATOM   6493 C  CB  . ALA A 1 826  ? 18.121 61.206  -7.146  1.00 10.22 ? 826  ALA A CB  1 
ATOM   6494 N  N   . ASN A 1 827  ? 19.449 61.971  -10.099 1.00 10.85 ? 827  ASN A N   1 
ATOM   6495 C  CA  . ASN A 1 827  ? 19.978 61.426  -11.345 1.00 11.05 ? 827  ASN A CA  1 
ATOM   6496 C  C   . ASN A 1 827  ? 21.291 62.091  -11.728 1.00 10.42 ? 827  ASN A C   1 
ATOM   6497 O  O   . ASN A 1 827  ? 21.820 61.865  -12.821 1.00 11.22 ? 827  ASN A O   1 
ATOM   6498 C  CB  . ASN A 1 827  ? 18.920 61.512  -12.450 1.00 11.33 ? 827  ASN A CB  1 
ATOM   6499 C  CG  . ASN A 1 827  ? 17.769 60.557  -12.181 1.00 12.91 ? 827  ASN A CG  1 
ATOM   6500 O  OD1 . ASN A 1 827  ? 17.943 59.361  -12.290 1.00 11.54 ? 827  ASN A OD1 1 
ATOM   6501 N  ND2 . ASN A 1 827  ? 16.618 61.082  -11.772 1.00 12.18 ? 827  ASN A ND2 1 
ATOM   6502 N  N   . TYR A 1 828  ? 21.800 62.943  -10.832 1.00 10.64 ? 828  TYR A N   1 
ATOM   6503 C  CA  . TYR A 1 828  ? 23.112 63.569  -11.051 1.00 10.35 ? 828  TYR A CA  1 
ATOM   6504 C  C   . TYR A 1 828  ? 24.161 62.622  -10.447 1.00 10.79 ? 828  TYR A C   1 
ATOM   6505 O  O   . TYR A 1 828  ? 23.932 62.034  -9.371  1.00 10.37 ? 828  TYR A O   1 
ATOM   6506 C  CB  . TYR A 1 828  ? 23.224 64.947  -10.381 1.00 8.74  ? 828  TYR A CB  1 
ATOM   6507 C  CG  . TYR A 1 828  ? 23.242 66.095  -11.382 1.00 8.55  ? 828  TYR A CG  1 
ATOM   6508 C  CD1 . TYR A 1 828  ? 22.147 66.348  -12.226 1.00 7.07  ? 828  TYR A CD1 1 
ATOM   6509 C  CD2 . TYR A 1 828  ? 24.373 66.905  -11.519 1.00 8.95  ? 828  TYR A CD2 1 
ATOM   6510 C  CE1 . TYR A 1 828  ? 22.195 67.364  -13.181 1.00 7.63  ? 828  TYR A CE1 1 
ATOM   6511 C  CE2 . TYR A 1 828  ? 24.417 67.933  -12.470 1.00 9.25  ? 828  TYR A CE2 1 
ATOM   6512 C  CZ  . TYR A 1 828  ? 23.340 68.153  -13.296 1.00 7.95  ? 828  TYR A CZ  1 
ATOM   6513 O  OH  . TYR A 1 828  ? 23.438 69.122  -14.280 1.00 9.46  ? 828  TYR A OH  1 
ATOM   6514 N  N   . TYR A 1 829  ? 25.271 62.455  -11.172 1.00 9.63  ? 829  TYR A N   1 
ATOM   6515 C  CA  . TYR A 1 829  ? 26.384 61.593  -10.765 1.00 10.16 ? 829  TYR A CA  1 
ATOM   6516 C  C   . TYR A 1 829  ? 27.720 62.326  -10.917 1.00 10.50 ? 829  TYR A C   1 
ATOM   6517 O  O   . TYR A 1 829  ? 27.809 63.347  -11.606 1.00 8.65  ? 829  TYR A O   1 
ATOM   6518 C  CB  . TYR A 1 829  ? 26.444 60.326  -11.632 1.00 9.04  ? 829  TYR A CB  1 
ATOM   6519 C  CG  . TYR A 1 829  ? 25.289 59.403  -11.396 1.00 9.09  ? 829  TYR A CG  1 
ATOM   6520 C  CD1 . TYR A 1 829  ? 24.114 59.489  -12.172 1.00 10.13 ? 829  TYR A CD1 1 
ATOM   6521 C  CD2 . TYR A 1 829  ? 25.334 58.486  -10.358 1.00 8.53  ? 829  TYR A CD2 1 
ATOM   6522 C  CE1 . TYR A 1 829  ? 22.992 58.656  -11.891 1.00 9.31  ? 829  TYR A CE1 1 
ATOM   6523 C  CE2 . TYR A 1 829  ? 24.245 57.662  -10.058 1.00 9.37  ? 829  TYR A CE2 1 
ATOM   6524 C  CZ  . TYR A 1 829  ? 23.068 57.748  -10.824 1.00 10.52 ? 829  TYR A CZ  1 
ATOM   6525 O  OH  . TYR A 1 829  ? 22.000 56.955  -10.473 1.00 9.05  ? 829  TYR A OH  1 
ATOM   6526 N  N   . PRO A 1 830  ? 28.770 61.819  -10.250 1.00 10.49 ? 830  PRO A N   1 
ATOM   6527 C  CA  . PRO A 1 830  ? 30.058 62.498  -10.395 1.00 9.59  ? 830  PRO A CA  1 
ATOM   6528 C  C   . PRO A 1 830  ? 30.517 62.237  -11.829 1.00 9.57  ? 830  PRO A C   1 
ATOM   6529 O  O   . PRO A 1 830  ? 30.270 61.138  -12.376 1.00 6.75  ? 830  PRO A O   1 
ATOM   6530 C  CB  . PRO A 1 830  ? 30.992 61.750  -9.437  1.00 11.97 ? 830  PRO A CB  1 
ATOM   6531 C  CG  . PRO A 1 830  ? 30.072 60.991  -8.478  1.00 12.86 ? 830  PRO A CG  1 
ATOM   6532 C  CD  . PRO A 1 830  ? 28.800 60.711  -9.269  1.00 10.29 ? 830  PRO A CD  1 
ATOM   6533 N  N   . ILE A 1 831  ? 31.160 63.223  -12.441 1.00 6.97  ? 831  ILE A N   1 
ATOM   6534 C  CA  . ILE A 1 831  ? 31.748 63.030  -13.785 1.00 7.68  ? 831  ILE A CA  1 
ATOM   6535 C  C   . ILE A 1 831  ? 33.230 63.352  -13.513 1.00 8.08  ? 831  ILE A C   1 
ATOM   6536 O  O   . ILE A 1 831  ? 33.721 64.417  -13.870 1.00 7.01  ? 831  ILE A O   1 
ATOM   6537 C  CB  . ILE A 1 831  ? 31.219 64.029  -14.849 1.00 6.42  ? 831  ILE A CB  1 
ATOM   6538 C  CG1 . ILE A 1 831  ? 29.673 64.088  -14.845 1.00 7.11  ? 831  ILE A CG1 1 
ATOM   6539 C  CG2 . ILE A 1 831  ? 31.784 63.640  -16.222 1.00 6.01  ? 831  ILE A CG2 1 
ATOM   6540 C  CD1 . ILE A 1 831  ? 28.943 62.730  -15.048 1.00 6.86  ? 831  ILE A CD1 1 
ATOM   6541 N  N   . PRO A 1 832  ? 33.965 62.406  -12.899 1.00 9.17  ? 832  PRO A N   1 
ATOM   6542 C  CA  . PRO A 1 832  ? 35.373 62.713  -12.604 1.00 7.88  ? 832  PRO A CA  1 
ATOM   6543 C  C   . PRO A 1 832  ? 36.280 62.882  -13.788 1.00 8.56  ? 832  PRO A C   1 
ATOM   6544 O  O   . PRO A 1 832  ? 37.272 63.602  -13.692 1.00 6.26  ? 832  PRO A O   1 
ATOM   6545 C  CB  . PRO A 1 832  ? 35.808 61.596  -11.634 1.00 8.92  ? 832  PRO A CB  1 
ATOM   6546 C  CG  . PRO A 1 832  ? 34.832 60.472  -11.891 1.00 10.93 ? 832  PRO A CG  1 
ATOM   6547 C  CD  . PRO A 1 832  ? 33.516 61.192  -12.194 1.00 8.26  ? 832  PRO A CD  1 
ATOM   6548 N  N   . SER A 1 833  ? 35.955 62.245  -14.910 1.00 8.21  ? 833  SER A N   1 
ATOM   6549 C  CA  . SER A 1 833  ? 36.791 62.427  -16.091 1.00 8.85  ? 833  SER A CA  1 
ATOM   6550 C  C   . SER A 1 833  ? 36.049 62.199  -17.422 1.00 8.51  ? 833  SER A C   1 
ATOM   6551 O  O   . SER A 1 833  ? 36.584 62.506  -18.476 1.00 7.04  ? 833  SER A O   1 
ATOM   6552 C  CB  . SER A 1 833  ? 38.017 61.505  -16.031 1.00 10.30 ? 833  SER A CB  1 
ATOM   6553 O  OG  . SER A 1 833  ? 37.710 60.167  -16.358 1.00 11.23 ? 833  SER A OG  1 
ATOM   6554 N  N   . GLY A 1 834  ? 34.832 61.652  -17.368 1.00 7.74  ? 834  GLY A N   1 
ATOM   6555 C  CA  . GLY A 1 834  ? 34.107 61.432  -18.619 1.00 7.09  ? 834  GLY A CA  1 
ATOM   6556 C  C   . GLY A 1 834  ? 32.719 60.833  -18.516 1.00 7.70  ? 834  GLY A C   1 
ATOM   6557 O  O   . GLY A 1 834  ? 32.323 60.189  -17.524 1.00 6.52  ? 834  GLY A O   1 
ATOM   6558 N  N   . MET A 1 835  ? 31.954 61.058  -19.572 1.00 9.11  ? 835  MET A N   1 
ATOM   6559 C  CA  . MET A 1 835  ? 30.594 60.545  -19.637 1.00 9.35  ? 835  MET A CA  1 
ATOM   6560 C  C   . MET A 1 835  ? 30.214 60.322  -21.121 1.00 10.27 ? 835  MET A C   1 
ATOM   6561 O  O   . MET A 1 835  ? 30.784 60.947  -22.029 1.00 9.26  ? 835  MET A O   1 
ATOM   6562 C  CB  . MET A 1 835  ? 29.632 61.556  -18.997 1.00 8.13  ? 835  MET A CB  1 
ATOM   6563 C  CG  . MET A 1 835  ? 29.423 62.863  -19.814 1.00 8.24  ? 835  MET A CG  1 
ATOM   6564 S  SD  . MET A 1 835  ? 28.649 64.168  -18.859 1.00 11.21 ? 835  MET A SD  1 
ATOM   6565 C  CE  . MET A 1 835  ? 27.070 63.461  -18.542 1.00 6.22  ? 835  MET A CE  1 
ATOM   6566 N  N   . PHE A 1 836  ? 29.278 59.410  -21.370 1.00 9.64  ? 836  PHE A N   1 
ATOM   6567 C  CA  . PHE A 1 836  ? 28.841 59.216  -22.749 1.00 9.35  ? 836  PHE A CA  1 
ATOM   6568 C  C   . PHE A 1 836  ? 27.445 58.611  -22.842 1.00 10.11 ? 836  PHE A C   1 
ATOM   6569 O  O   . PHE A 1 836  ? 26.911 58.075  -21.860 1.00 7.75  ? 836  PHE A O   1 
ATOM   6570 C  CB  . PHE A 1 836  ? 29.881 58.400  -23.556 1.00 8.42  ? 836  PHE A CB  1 
ATOM   6571 C  CG  . PHE A 1 836  ? 30.010 56.918  -23.170 1.00 10.87 ? 836  PHE A CG  1 
ATOM   6572 C  CD1 . PHE A 1 836  ? 29.117 55.955  -23.677 1.00 10.91 ? 836  PHE A CD1 1 
ATOM   6573 C  CD2 . PHE A 1 836  ? 31.071 56.479  -22.386 1.00 9.47  ? 836  PHE A CD2 1 
ATOM   6574 C  CE1 . PHE A 1 836  ? 29.291 54.582  -23.410 1.00 10.14 ? 836  PHE A CE1 1 
ATOM   6575 C  CE2 . PHE A 1 836  ? 31.256 55.095  -22.107 1.00 10.47 ? 836  PHE A CE2 1 
ATOM   6576 C  CZ  . PHE A 1 836  ? 30.370 54.156  -22.618 1.00 11.92 ? 836  PHE A CZ  1 
ATOM   6577 N  N   . ILE A 1 837  ? 26.844 58.766  -24.022 1.00 9.30  ? 837  ILE A N   1 
ATOM   6578 C  CA  . ILE A 1 837  ? 25.550 58.183  -24.321 1.00 9.67  ? 837  ILE A CA  1 
ATOM   6579 C  C   . ILE A 1 837  ? 25.721 57.520  -25.673 1.00 10.15 ? 837  ILE A C   1 
ATOM   6580 O  O   . ILE A 1 837  ? 26.606 57.907  -26.475 1.00 8.51  ? 837  ILE A O   1 
ATOM   6581 C  CB  . ILE A 1 837  ? 24.426 59.222  -24.447 1.00 9.37  ? 837  ILE A CB  1 
ATOM   6582 C  CG1 . ILE A 1 837  ? 24.868 60.391  -25.313 1.00 10.13 ? 837  ILE A CG1 1 
ATOM   6583 C  CG2 . ILE A 1 837  ? 23.955 59.639  -23.074 1.00 9.83  ? 837  ILE A CG2 1 
ATOM   6584 C  CD1 . ILE A 1 837  ? 23.645 61.296  -25.742 1.00 8.26  ? 837  ILE A CD1 1 
ATOM   6585 N  N   . GLU A 1 838  ? 24.892 56.527  -25.938 1.00 10.49 ? 838  GLU A N   1 
ATOM   6586 C  CA  . GLU A 1 838  ? 24.972 55.851  -27.225 1.00 12.01 ? 838  GLU A CA  1 
ATOM   6587 C  C   . GLU A 1 838  ? 23.705 55.072  -27.585 1.00 12.23 ? 838  GLU A C   1 
ATOM   6588 O  O   . GLU A 1 838  ? 22.823 54.822  -26.740 1.00 11.05 ? 838  GLU A O   1 
ATOM   6589 C  CB  . GLU A 1 838  ? 26.142 54.856  -27.209 1.00 11.71 ? 838  GLU A CB  1 
ATOM   6590 C  CG  . GLU A 1 838  ? 25.881 53.661  -26.239 1.00 13.67 ? 838  GLU A CG  1 
ATOM   6591 C  CD  . GLU A 1 838  ? 27.024 52.624  -26.197 1.00 15.77 ? 838  GLU A CD  1 
ATOM   6592 O  OE1 . GLU A 1 838  ? 26.865 51.610  -25.488 1.00 17.87 ? 838  GLU A OE1 1 
ATOM   6593 O  OE2 . GLU A 1 838  ? 28.060 52.796  -26.866 1.00 16.28 ? 838  GLU A OE2 1 
ATOM   6594 N  N   . ASP A 1 839  ? 23.596 54.718  -28.862 1.00 13.18 ? 839  ASP A N   1 
ATOM   6595 C  CA  . ASP A 1 839  ? 22.519 53.840  -29.280 1.00 13.77 ? 839  ASP A CA  1 
ATOM   6596 C  C   . ASP A 1 839  ? 23.224 52.750  -30.063 1.00 14.86 ? 839  ASP A C   1 
ATOM   6597 O  O   . ASP A 1 839  ? 24.438 52.569  -29.921 1.00 13.03 ? 839  ASP A O   1 
ATOM   6598 C  CB  . ASP A 1 839  ? 21.417 54.526  -30.095 1.00 13.76 ? 839  ASP A CB  1 
ATOM   6599 C  CG  . ASP A 1 839  ? 21.933 55.286  -31.289 1.00 13.70 ? 839  ASP A CG  1 
ATOM   6600 O  OD1 . ASP A 1 839  ? 23.001 54.945  -31.845 1.00 12.30 ? 839  ASP A OD1 1 
ATOM   6601 O  OD2 . ASP A 1 839  ? 21.223 56.235  -31.667 1.00 14.99 ? 839  ASP A OD2 1 
ATOM   6602 N  N   . ALA A 1 840  ? 22.491 52.034  -30.909 1.00 15.27 ? 840  ALA A N   1 
ATOM   6603 C  CA  . ALA A 1 840  ? 23.105 50.951  -31.644 1.00 15.26 ? 840  ALA A CA  1 
ATOM   6604 C  C   . ALA A 1 840  ? 24.207 51.409  -32.593 1.00 15.33 ? 840  ALA A C   1 
ATOM   6605 O  O   . ALA A 1 840  ? 25.174 50.681  -32.822 1.00 14.37 ? 840  ALA A O   1 
ATOM   6606 C  CB  . ALA A 1 840  ? 22.030 50.184  -32.426 1.00 14.56 ? 840  ALA A CB  1 
ATOM   6607 N  N   . ASN A 1 841  ? 24.081 52.627  -33.114 1.00 14.45 ? 841  ASN A N   1 
ATOM   6608 C  CA  . ASN A 1 841  ? 25.032 53.119  -34.102 1.00 14.65 ? 841  ASN A CA  1 
ATOM   6609 C  C   . ASN A 1 841  ? 25.976 54.260  -33.764 1.00 14.11 ? 841  ASN A C   1 
ATOM   6610 O  O   . ASN A 1 841  ? 27.059 54.375  -34.346 1.00 13.31 ? 841  ASN A O   1 
ATOM   6611 C  CB  . ASN A 1 841  ? 24.244 53.546  -35.353 1.00 15.68 ? 841  ASN A CB  1 
ATOM   6612 C  CG  . ASN A 1 841  ? 23.493 52.386  -35.969 1.00 17.64 ? 841  ASN A CG  1 
ATOM   6613 O  OD1 . ASN A 1 841  ? 24.071 51.331  -36.190 1.00 18.30 ? 841  ASN A OD1 1 
ATOM   6614 N  ND2 . ASN A 1 841  ? 22.212 52.569  -36.230 1.00 16.23 ? 841  ASN A ND2 1 
ATOM   6615 N  N   . THR A 1 842  ? 25.541 55.114  -32.866 1.00 13.45 ? 842  THR A N   1 
ATOM   6616 C  CA  . THR A 1 842  ? 26.307 56.305  -32.555 1.00 13.77 ? 842  THR A CA  1 
ATOM   6617 C  C   . THR A 1 842  ? 26.540 56.525  -31.075 1.00 12.82 ? 842  THR A C   1 
ATOM   6618 O  O   . THR A 1 842  ? 25.704 56.169  -30.232 1.00 12.67 ? 842  THR A O   1 
ATOM   6619 C  CB  . THR A 1 842  ? 25.574 57.546  -33.133 1.00 14.01 ? 842  THR A CB  1 
ATOM   6620 O  OG1 . THR A 1 842  ? 25.153 57.264  -34.471 1.00 13.50 ? 842  THR A OG1 1 
ATOM   6621 C  CG2 . THR A 1 842  ? 26.475 58.770  -33.136 1.00 14.97 ? 842  THR A CG2 1 
ATOM   6622 N  N   . ARG A 1 843  ? 27.705 57.090  -30.776 1.00 11.70 ? 843  ARG A N   1 
ATOM   6623 C  CA  . ARG A 1 843  ? 28.061 57.430  -29.407 1.00 11.59 ? 843  ARG A CA  1 
ATOM   6624 C  C   . ARG A 1 843  ? 28.621 58.853  -29.361 1.00 11.32 ? 843  ARG A C   1 
ATOM   6625 O  O   . ARG A 1 843  ? 29.315 59.294  -30.281 1.00 10.17 ? 843  ARG A O   1 
ATOM   6626 C  CB  . ARG A 1 843  ? 29.154 56.493  -28.865 1.00 11.17 ? 843  ARG A CB  1 
ATOM   6627 C  CG  . ARG A 1 843  ? 29.615 56.861  -27.430 1.00 10.00 ? 843  ARG A CG  1 
ATOM   6628 C  CD  . ARG A 1 843  ? 30.771 55.970  -26.927 1.00 6.69  ? 843  ARG A CD  1 
ATOM   6629 N  NE  . ARG A 1 843  ? 30.372 54.581  -26.618 1.00 8.86  ? 843  ARG A NE  1 
ATOM   6630 C  CZ  . ARG A 1 843  ? 31.210 53.686  -26.079 1.00 10.05 ? 843  ARG A CZ  1 
ATOM   6631 N  NH1 . ARG A 1 843  ? 32.465 54.045  -25.807 1.00 8.91  ? 843  ARG A NH1 1 
ATOM   6632 N  NH2 . ARG A 1 843  ? 30.814 52.448  -25.783 1.00 9.17  ? 843  ARG A NH2 1 
ATOM   6633 N  N   . LEU A 1 844  ? 28.314 59.561  -28.280 1.00 11.83 ? 844  LEU A N   1 
ATOM   6634 C  CA  . LEU A 1 844  ? 28.880 60.891  -28.073 1.00 10.68 ? 844  LEU A CA  1 
ATOM   6635 C  C   . LEU A 1 844  ? 29.538 60.801  -26.699 1.00 10.80 ? 844  LEU A C   1 
ATOM   6636 O  O   . LEU A 1 844  ? 28.851 60.491  -25.701 1.00 9.84  ? 844  LEU A O   1 
ATOM   6637 C  CB  . LEU A 1 844  ? 27.810 61.983  -28.037 1.00 9.75  ? 844  LEU A CB  1 
ATOM   6638 C  CG  . LEU A 1 844  ? 28.427 63.391  -27.903 1.00 10.44 ? 844  LEU A CG  1 
ATOM   6639 C  CD1 . LEU A 1 844  ? 29.284 63.745  -29.116 1.00 9.12  ? 844  LEU A CD1 1 
ATOM   6640 C  CD2 . LEU A 1 844  ? 27.329 64.402  -27.794 1.00 10.69 ? 844  LEU A CD2 1 
ATOM   6641 N  N   . THR A 1 845  ? 30.849 61.055  -26.645 1.00 10.05 ? 845  THR A N   1 
ATOM   6642 C  CA  . THR A 1 845  ? 31.579 61.001  -25.363 1.00 9.69  ? 845  THR A CA  1 
ATOM   6643 C  C   . THR A 1 845  ? 32.144 62.389  -25.012 1.00 9.66  ? 845  THR A C   1 
ATOM   6644 O  O   . THR A 1 845  ? 32.805 63.016  -25.839 1.00 10.36 ? 845  THR A O   1 
ATOM   6645 C  CB  . THR A 1 845  ? 32.800 60.023  -25.427 1.00 10.76 ? 845  THR A CB  1 
ATOM   6646 O  OG1 . THR A 1 845  ? 32.367 58.714  -25.847 1.00 10.32 ? 845  THR A OG1 1 
ATOM   6647 C  CG2 . THR A 1 845  ? 33.472 59.902  -24.035 1.00 8.19  ? 845  THR A CG2 1 
ATOM   6648 N  N   . LEU A 1 846  ? 31.884 62.868  -23.796 1.00 9.24  ? 846  LEU A N   1 
ATOM   6649 C  CA  . LEU A 1 846  ? 32.441 64.136  -23.362 1.00 8.35  ? 846  LEU A CA  1 
ATOM   6650 C  C   . LEU A 1 846  ? 33.522 63.834  -22.294 1.00 6.99  ? 846  LEU A C   1 
ATOM   6651 O  O   . LEU A 1 846  ? 33.223 63.258  -21.237 1.00 5.05  ? 846  LEU A O   1 
ATOM   6652 C  CB  . LEU A 1 846  ? 31.338 65.019  -22.766 1.00 8.73  ? 846  LEU A CB  1 
ATOM   6653 C  CG  . LEU A 1 846  ? 31.858 66.349  -22.176 1.00 11.92 ? 846  LEU A CG  1 
ATOM   6654 C  CD1 . LEU A 1 846  ? 32.393 67.232  -23.317 1.00 10.71 ? 846  LEU A CD1 1 
ATOM   6655 C  CD2 . LEU A 1 846  ? 30.707 67.109  -21.431 1.00 10.34 ? 846  LEU A CD2 1 
ATOM   6656 N  N   . LEU A 1 847  ? 34.776 64.184  -22.584 1.00 7.30  ? 847  LEU A N   1 
ATOM   6657 C  CA  . LEU A 1 847  ? 35.884 63.936  -21.636 1.00 8.91  ? 847  LEU A CA  1 
ATOM   6658 C  C   . LEU A 1 847  ? 36.182 65.257  -20.892 1.00 8.68  ? 847  LEU A C   1 
ATOM   6659 O  O   . LEU A 1 847  ? 36.088 66.322  -21.497 1.00 8.66  ? 847  LEU A O   1 
ATOM   6660 C  CB  . LEU A 1 847  ? 37.148 63.458  -22.363 1.00 6.63  ? 847  LEU A CB  1 
ATOM   6661 C  CG  . LEU A 1 847  ? 37.170 62.045  -22.981 1.00 8.51  ? 847  LEU A CG  1 
ATOM   6662 C  CD1 . LEU A 1 847  ? 36.456 60.986  -22.077 1.00 6.13  ? 847  LEU A CD1 1 
ATOM   6663 C  CD2 . LEU A 1 847  ? 36.472 62.136  -24.328 1.00 5.94  ? 847  LEU A CD2 1 
ATOM   6664 N  N   . THR A 1 848  ? 36.533 65.177  -19.603 1.00 8.91  ? 848  THR A N   1 
ATOM   6665 C  CA  . THR A 1 848  ? 36.780 66.379  -18.794 1.00 10.14 ? 848  THR A CA  1 
ATOM   6666 C  C   . THR A 1 848  ? 38.178 66.465  -18.202 1.00 11.68 ? 848  THR A C   1 
ATOM   6667 O  O   . THR A 1 848  ? 38.827 65.434  -17.943 1.00 11.09 ? 848  THR A O   1 
ATOM   6668 C  CB  . THR A 1 848  ? 35.824 66.439  -17.618 1.00 11.58 ? 848  THR A CB  1 
ATOM   6669 O  OG1 . THR A 1 848  ? 36.271 65.528  -16.591 1.00 14.31 ? 848  THR A OG1 1 
ATOM   6670 C  CG2 . THR A 1 848  ? 34.426 66.023  -18.053 1.00 11.56 ? 848  THR A CG2 1 
ATOM   6671 N  N   . GLY A 1 849  ? 38.652 67.702  -18.014 1.00 11.06 ? 849  GLY A N   1 
ATOM   6672 C  CA  . GLY A 1 849  ? 39.960 67.900  -17.417 1.00 9.79  ? 849  GLY A CA  1 
ATOM   6673 C  C   . GLY A 1 849  ? 39.754 68.255  -15.945 1.00 10.32 ? 849  GLY A C   1 
ATOM   6674 O  O   . GLY A 1 849  ? 40.669 68.715  -15.261 1.00 9.39  ? 849  GLY A O   1 
ATOM   6675 N  N   . GLN A 1 850  ? 38.543 68.031  -15.444 1.00 9.41  ? 850  GLN A N   1 
ATOM   6676 C  CA  . GLN A 1 850  ? 38.228 68.331  -14.048 1.00 8.72  ? 850  GLN A CA  1 
ATOM   6677 C  C   . GLN A 1 850  ? 36.953 67.591  -13.628 1.00 9.38  ? 850  GLN A C   1 
ATOM   6678 O  O   . GLN A 1 850  ? 36.071 67.347  -14.454 1.00 9.95  ? 850  GLN A O   1 
ATOM   6679 C  CB  . GLN A 1 850  ? 38.019 69.869  -13.856 1.00 9.26  ? 850  GLN A CB  1 
ATOM   6680 C  CG  . GLN A 1 850  ? 36.870 70.475  -14.702 1.00 7.00  ? 850  GLN A CG  1 
ATOM   6681 C  CD  . GLN A 1 850  ? 37.228 70.582  -16.175 1.00 9.08  ? 850  GLN A CD  1 
ATOM   6682 O  OE1 . GLN A 1 850  ? 38.347 70.982  -16.532 1.00 8.60  ? 850  GLN A OE1 1 
ATOM   6683 N  NE2 . GLN A 1 850  ? 36.278 70.238  -17.048 1.00 7.33  ? 850  GLN A NE2 1 
ATOM   6684 N  N   . PRO A 1 851  ? 36.838 67.240  -12.333 1.00 8.74  ? 851  PRO A N   1 
ATOM   6685 C  CA  . PRO A 1 851  ? 35.622 66.531  -11.891 1.00 8.86  ? 851  PRO A CA  1 
ATOM   6686 C  C   . PRO A 1 851  ? 34.518 67.547  -11.709 1.00 9.54  ? 851  PRO A C   1 
ATOM   6687 O  O   . PRO A 1 851  ? 34.750 68.605  -11.124 1.00 7.82  ? 851  PRO A O   1 
ATOM   6688 C  CB  . PRO A 1 851  ? 36.031 65.884  -10.554 1.00 7.23  ? 851  PRO A CB  1 
ATOM   6689 C  CG  . PRO A 1 851  ? 37.073 66.894  -9.977  1.00 7.32  ? 851  PRO A CG  1 
ATOM   6690 C  CD  . PRO A 1 851  ? 37.857 67.335  -11.261 1.00 7.18  ? 851  PRO A CD  1 
ATOM   6691 N  N   . LEU A 1 852  ? 33.333 67.223  -12.229 1.00 9.77  ? 852  LEU A N   1 
ATOM   6692 C  CA  . LEU A 1 852  ? 32.154 68.087  -12.141 1.00 10.16 ? 852  LEU A CA  1 
ATOM   6693 C  C   . LEU A 1 852  ? 30.928 67.158  -12.024 1.00 10.10 ? 852  LEU A C   1 
ATOM   6694 O  O   . LEU A 1 852  ? 31.064 65.929  -12.159 1.00 11.45 ? 852  LEU A O   1 
ATOM   6695 C  CB  . LEU A 1 852  ? 32.030 68.945  -13.414 1.00 10.68 ? 852  LEU A CB  1 
ATOM   6696 C  CG  . LEU A 1 852  ? 33.124 70.005  -13.613 1.00 10.21 ? 852  LEU A CG  1 
ATOM   6697 C  CD1 . LEU A 1 852  ? 33.034 70.635  -15.005 1.00 10.13 ? 852  LEU A CD1 1 
ATOM   6698 C  CD2 . LEU A 1 852  ? 32.948 71.065  -12.579 1.00 10.18 ? 852  LEU A CD2 1 
ATOM   6699 N  N   . GLY A 1 853  ? 29.746 67.717  -11.793 1.00 7.74  ? 853  GLY A N   1 
ATOM   6700 C  CA  . GLY A 1 853  ? 28.579 66.863  -11.663 1.00 8.85  ? 853  GLY A CA  1 
ATOM   6701 C  C   . GLY A 1 853  ? 27.811 66.837  -12.980 1.00 8.68  ? 853  GLY A C   1 
ATOM   6702 O  O   . GLY A 1 853  ? 27.812 67.823  -13.712 1.00 7.12  ? 853  GLY A O   1 
ATOM   6703 N  N   . GLY A 1 854  ? 27.153 65.731  -13.305 1.00 8.64  ? 854  GLY A N   1 
ATOM   6704 C  CA  . GLY A 1 854  ? 26.425 65.735  -14.570 1.00 9.13  ? 854  GLY A CA  1 
ATOM   6705 C  C   . GLY A 1 854  ? 25.364 64.674  -14.691 1.00 9.47  ? 854  GLY A C   1 
ATOM   6706 O  O   . GLY A 1 854  ? 25.145 63.908  -13.764 1.00 10.01 ? 854  GLY A O   1 
ATOM   6707 N  N   . SER A 1 855  ? 24.714 64.607  -15.850 1.00 10.92 ? 855  SER A N   1 
ATOM   6708 C  CA  . SER A 1 855  ? 23.657 63.629  -16.033 1.00 11.88 ? 855  SER A CA  1 
ATOM   6709 C  C   . SER A 1 855  ? 23.228 63.591  -17.480 1.00 12.09 ? 855  SER A C   1 
ATOM   6710 O  O   . SER A 1 855  ? 23.810 64.270  -18.332 1.00 9.92  ? 855  SER A O   1 
ATOM   6711 C  CB  . SER A 1 855  ? 22.421 64.032  -15.186 1.00 13.09 ? 855  SER A CB  1 
ATOM   6712 O  OG  . SER A 1 855  ? 21.436 62.999  -15.152 1.00 11.23 ? 855  SER A OG  1 
ATOM   6713 N  N   . SER A 1 856  ? 22.178 62.799  -17.720 1.00 12.71 ? 856  SER A N   1 
ATOM   6714 C  CA  . SER A 1 856  ? 21.514 62.682  -19.017 1.00 12.21 ? 856  SER A CA  1 
ATOM   6715 C  C   . SER A 1 856  ? 20.048 62.638  -18.578 1.00 13.06 ? 856  SER A C   1 
ATOM   6716 O  O   . SER A 1 856  ? 19.527 61.555  -18.247 1.00 11.66 ? 856  SER A O   1 
ATOM   6717 C  CB  . SER A 1 856  ? 21.842 61.371  -19.713 1.00 12.12 ? 856  SER A CB  1 
ATOM   6718 O  OG  . SER A 1 856  ? 21.089 61.284  -20.898 1.00 11.45 ? 856  SER A OG  1 
ATOM   6719 N  N   . LEU A 1 857  ? 19.397 63.803  -18.567 1.00 13.03 ? 857  LEU A N   1 
ATOM   6720 C  CA  . LEU A 1 857  ? 18.009 63.910  -18.088 1.00 11.85 ? 857  LEU A CA  1 
ATOM   6721 C  C   . LEU A 1 857  ? 16.948 63.576  -19.133 1.00 11.89 ? 857  LEU A C   1 
ATOM   6722 O  O   . LEU A 1 857  ? 15.764 63.508  -18.818 1.00 14.11 ? 857  LEU A O   1 
ATOM   6723 C  CB  . LEU A 1 857  ? 17.774 65.313  -17.509 1.00 11.32 ? 857  LEU A CB  1 
ATOM   6724 C  CG  . LEU A 1 857  ? 18.662 65.663  -16.307 1.00 10.01 ? 857  LEU A CG  1 
ATOM   6725 C  CD1 . LEU A 1 857  ? 18.442 67.122  -15.879 1.00 10.94 ? 857  LEU A CD1 1 
ATOM   6726 C  CD2 . LEU A 1 857  ? 18.342 64.740  -15.140 1.00 11.54 ? 857  LEU A CD2 1 
ATOM   6727 N  N   . ALA A 1 858  ? 17.377 63.371  -20.363 1.00 11.98 ? 858  ALA A N   1 
ATOM   6728 C  CA  . ALA A 1 858  ? 16.487 62.995  -21.442 1.00 12.80 ? 858  ALA A CA  1 
ATOM   6729 C  C   . ALA A 1 858  ? 17.312 62.254  -22.493 1.00 12.94 ? 858  ALA A C   1 
ATOM   6730 O  O   . ALA A 1 858  ? 18.509 62.505  -22.647 1.00 10.61 ? 858  ALA A O   1 
ATOM   6731 C  CB  . ALA A 1 858  ? 15.820 64.247  -22.072 1.00 14.09 ? 858  ALA A CB  1 
ATOM   6732 N  N   . SER A 1 859  ? 16.656 61.338  -23.200 1.00 12.28 ? 859  SER A N   1 
ATOM   6733 C  CA  . SER A 1 859  ? 17.271 60.560  -24.245 1.00 11.79 ? 859  SER A CA  1 
ATOM   6734 C  C   . SER A 1 859  ? 17.983 61.521  -25.199 1.00 11.60 ? 859  SER A C   1 
ATOM   6735 O  O   . SER A 1 859  ? 17.432 62.567  -25.544 1.00 12.02 ? 859  SER A O   1 
ATOM   6736 C  CB  . SER A 1 859  ? 16.183 59.761  -25.012 1.00 11.99 ? 859  SER A CB  1 
ATOM   6737 O  OG  . SER A 1 859  ? 16.741 59.051  -26.108 1.00 11.86 ? 859  SER A OG  1 
ATOM   6738 N  N   . GLY A 1 860  ? 19.206 61.161  -25.579 1.00 9.33  ? 860  GLY A N   1 
ATOM   6739 C  CA  . GLY A 1 860  ? 20.015 61.948  -26.493 1.00 8.94  ? 860  GLY A CA  1 
ATOM   6740 C  C   . GLY A 1 860  ? 20.755 63.129  -25.876 1.00 10.78 ? 860  GLY A C   1 
ATOM   6741 O  O   . GLY A 1 860  ? 21.490 63.850  -26.583 1.00 10.81 ? 860  GLY A O   1 
ATOM   6742 N  N   . GLU A 1 861  ? 20.582 63.325  -24.575 1.00 9.32  ? 861  GLU A N   1 
ATOM   6743 C  CA  . GLU A 1 861  ? 21.217 64.445  -23.875 1.00 11.17 ? 861  GLU A CA  1 
ATOM   6744 C  C   . GLU A 1 861  ? 22.389 64.105  -22.954 1.00 10.65 ? 861  GLU A C   1 
ATOM   6745 O  O   . GLU A 1 861  ? 22.473 63.002  -22.394 1.00 10.14 ? 861  GLU A O   1 
ATOM   6746 C  CB  . GLU A 1 861  ? 20.190 65.179  -23.001 1.00 12.72 ? 861  GLU A CB  1 
ATOM   6747 C  CG  . GLU A 1 861  ? 19.257 66.090  -23.739 1.00 14.47 ? 861  GLU A CG  1 
ATOM   6748 C  CD  . GLU A 1 861  ? 18.291 66.776  -22.811 1.00 16.12 ? 861  GLU A CD  1 
ATOM   6749 O  OE1 . GLU A 1 861  ? 18.493 66.757  -21.554 1.00 15.31 ? 861  GLU A OE1 1 
ATOM   6750 O  OE2 . GLU A 1 861  ? 17.321 67.346  -23.348 1.00 15.16 ? 861  GLU A OE2 1 
ATOM   6751 N  N   . LEU A 1 862  ? 23.257 65.095  -22.768 1.00 10.11 ? 862  LEU A N   1 
ATOM   6752 C  CA  . LEU A 1 862  ? 24.384 64.983  -21.837 1.00 10.76 ? 862  LEU A CA  1 
ATOM   6753 C  C   . LEU A 1 862  ? 24.468 66.358  -21.196 1.00 10.92 ? 862  LEU A C   1 
ATOM   6754 O  O   . LEU A 1 862  ? 24.259 67.364  -21.875 1.00 10.19 ? 862  LEU A O   1 
ATOM   6755 C  CB  . LEU A 1 862  ? 25.731 64.705  -22.556 1.00 10.67 ? 862  LEU A CB  1 
ATOM   6756 C  CG  . LEU A 1 862  ? 26.109 63.345  -23.158 1.00 8.95  ? 862  LEU A CG  1 
ATOM   6757 C  CD1 . LEU A 1 862  ? 27.492 63.389  -23.838 1.00 6.92  ? 862  LEU A CD1 1 
ATOM   6758 C  CD2 . LEU A 1 862  ? 26.133 62.338  -22.019 1.00 10.61 ? 862  LEU A CD2 1 
ATOM   6759 N  N   . GLU A 1 863  ? 24.740 66.431  -19.899 1.00 10.50 ? 863  GLU A N   1 
ATOM   6760 C  CA  . GLU A 1 863  ? 24.906 67.755  -19.291 1.00 9.53  ? 863  GLU A CA  1 
ATOM   6761 C  C   . GLU A 1 863  ? 25.852 67.668  -18.106 1.00 10.25 ? 863  GLU A C   1 
ATOM   6762 O  O   . GLU A 1 863  ? 25.919 66.644  -17.393 1.00 7.66  ? 863  GLU A O   1 
ATOM   6763 C  CB  . GLU A 1 863  ? 23.579 68.367  -18.856 1.00 11.05 ? 863  GLU A CB  1 
ATOM   6764 C  CG  . GLU A 1 863  ? 22.999 67.862  -17.546 1.00 10.40 ? 863  GLU A CG  1 
ATOM   6765 C  CD  . GLU A 1 863  ? 21.699 68.576  -17.244 1.00 12.61 ? 863  GLU A CD  1 
ATOM   6766 O  OE1 . GLU A 1 863  ? 21.552 69.123  -16.123 1.00 13.63 ? 863  GLU A OE1 1 
ATOM   6767 O  OE2 . GLU A 1 863  ? 20.820 68.606  -18.159 1.00 13.74 ? 863  GLU A OE2 1 
ATOM   6768 N  N   . ILE A 1 864  ? 26.578 68.752  -17.906 1.00 9.75  ? 864  ILE A N   1 
ATOM   6769 C  CA  . ILE A 1 864  ? 27.567 68.796  -16.850 1.00 10.30 ? 864  ILE A CA  1 
ATOM   6770 C  C   . ILE A 1 864  ? 27.607 70.210  -16.292 1.00 9.48  ? 864  ILE A C   1 
ATOM   6771 O  O   . ILE A 1 864  ? 27.703 71.177  -17.051 1.00 9.62  ? 864  ILE A O   1 
ATOM   6772 C  CB  . ILE A 1 864  ? 28.926 68.343  -17.443 1.00 11.56 ? 864  ILE A CB  1 
ATOM   6773 C  CG1 . ILE A 1 864  ? 30.017 68.343  -16.373 1.00 11.96 ? 864  ILE A CG1 1 
ATOM   6774 C  CG2 . ILE A 1 864  ? 29.300 69.215  -18.662 1.00 11.62 ? 864  ILE A CG2 1 
ATOM   6775 C  CD1 . ILE A 1 864  ? 31.218 67.464  -16.819 1.00 12.32 ? 864  ILE A CD1 1 
ATOM   6776 N  N   . MET A 1 865  ? 27.501 70.312  -14.973 1.00 8.88  ? 865  MET A N   1 
ATOM   6777 C  CA  . MET A 1 865  ? 27.496 71.594  -14.276 1.00 9.63  ? 865  MET A CA  1 
ATOM   6778 C  C   . MET A 1 865  ? 28.860 72.299  -14.316 1.00 10.20 ? 865  MET A C   1 
ATOM   6779 O  O   . MET A 1 865  ? 29.891 71.675  -14.097 1.00 9.14  ? 865  MET A O   1 
ATOM   6780 C  CB  . MET A 1 865  ? 27.101 71.379  -12.817 1.00 9.27  ? 865  MET A CB  1 
ATOM   6781 C  CG  . MET A 1 865  ? 26.551 72.647  -12.161 1.00 9.11  ? 865  MET A CG  1 
ATOM   6782 S  SD  . MET A 1 865  ? 24.906 73.013  -12.927 1.00 11.34 ? 865  MET A SD  1 
ATOM   6783 C  CE  . MET A 1 865  ? 23.883 71.779  -12.008 1.00 9.19  ? 865  MET A CE  1 
ATOM   6784 N  N   . GLN A 1 866  ? 28.854 73.606  -14.566 1.00 9.79  ? 866  GLN A N   1 
ATOM   6785 C  CA  . GLN A 1 866  ? 30.095 74.373  -14.649 1.00 8.78  ? 866  GLN A CA  1 
ATOM   6786 C  C   . GLN A 1 866  ? 30.497 75.038  -13.317 1.00 8.75  ? 866  GLN A C   1 
ATOM   6787 O  O   . GLN A 1 866  ? 31.672 75.009  -12.935 1.00 8.80  ? 866  GLN A O   1 
ATOM   6788 C  CB  . GLN A 1 866  ? 29.959 75.423  -15.765 1.00 8.84  ? 866  GLN A CB  1 
ATOM   6789 C  CG  . GLN A 1 866  ? 29.625 74.780  -17.127 1.00 9.16  ? 866  GLN A CG  1 
ATOM   6790 C  CD  . GLN A 1 866  ? 30.675 73.753  -17.547 1.00 12.11 ? 866  GLN A CD  1 
ATOM   6791 O  OE1 . GLN A 1 866  ? 31.814 74.114  -17.849 1.00 11.37 ? 866  GLN A OE1 1 
ATOM   6792 N  NE2 . GLN A 1 866  ? 30.301 72.472  -17.553 1.00 11.48 ? 866  GLN A NE2 1 
ATOM   6793 N  N   . ASP A 1 867  ? 29.546 75.667  -12.640 1.00 8.35  ? 867  ASP A N   1 
ATOM   6794 C  CA  . ASP A 1 867  ? 29.813 76.302  -11.357 1.00 10.29 ? 867  ASP A CA  1 
ATOM   6795 C  C   . ASP A 1 867  ? 28.457 76.557  -10.697 1.00 11.76 ? 867  ASP A C   1 
ATOM   6796 O  O   . ASP A 1 867  ? 27.408 76.488  -11.371 1.00 12.04 ? 867  ASP A O   1 
ATOM   6797 C  CB  . ASP A 1 867  ? 30.599 77.637  -11.519 1.00 10.61 ? 867  ASP A CB  1 
ATOM   6798 C  CG  . ASP A 1 867  ? 31.311 78.059  -10.232 1.00 11.15 ? 867  ASP A CG  1 
ATOM   6799 O  OD1 . ASP A 1 867  ? 31.075 77.410  -9.191  1.00 9.17  ? 867  ASP A OD1 1 
ATOM   6800 O  OD2 . ASP A 1 867  ? 32.096 79.029  -10.252 1.00 11.25 ? 867  ASP A OD2 1 
ATOM   6801 N  N   . ARG A 1 868  ? 28.484 76.791  -9.380  1.00 11.69 ? 868  ARG A N   1 
ATOM   6802 C  CA  . ARG A 1 868  ? 27.279 77.043  -8.596  1.00 12.65 ? 868  ARG A CA  1 
ATOM   6803 C  C   . ARG A 1 868  ? 27.598 78.077  -7.503  1.00 12.62 ? 868  ARG A C   1 
ATOM   6804 O  O   . ARG A 1 868  ? 28.652 78.035  -6.883  1.00 11.58 ? 868  ARG A O   1 
ATOM   6805 C  CB  . ARG A 1 868  ? 26.769 75.743  -7.952  1.00 11.38 ? 868  ARG A CB  1 
ATOM   6806 C  CG  . ARG A 1 868  ? 27.813 74.972  -7.139  1.00 12.14 ? 868  ARG A CG  1 
ATOM   6807 C  CD  . ARG A 1 868  ? 27.516 73.441  -7.215  1.00 10.96 ? 868  ARG A CD  1 
ATOM   6808 N  NE  . ARG A 1 868  ? 26.148 73.140  -6.814  1.00 8.88  ? 868  ARG A NE  1 
ATOM   6809 C  CZ  . ARG A 1 868  ? 25.787 72.865  -5.565  1.00 10.57 ? 868  ARG A CZ  1 
ATOM   6810 N  NH1 . ARG A 1 868  ? 26.698 72.828  -4.579  1.00 11.41 ? 868  ARG A NH1 1 
ATOM   6811 N  NH2 . ARG A 1 868  ? 24.513 72.653  -5.281  1.00 8.62  ? 868  ARG A NH2 1 
ATOM   6812 N  N   . ARG A 1 869  ? 26.681 79.004  -7.279  1.00 11.58 ? 869  ARG A N   1 
ATOM   6813 C  CA  . ARG A 1 869  ? 26.886 80.050  -6.277  1.00 12.12 ? 869  ARG A CA  1 
ATOM   6814 C  C   . ARG A 1 869  ? 25.619 80.032  -5.463  1.00 12.81 ? 869  ARG A C   1 
ATOM   6815 O  O   . ARG A 1 869  ? 24.542 80.305  -5.970  1.00 12.25 ? 869  ARG A O   1 
ATOM   6816 C  CB  . ARG A 1 869  ? 27.091 81.397  -6.965  1.00 11.99 ? 869  ARG A CB  1 
ATOM   6817 C  CG  . ARG A 1 869  ? 27.253 82.579  -6.013  1.00 12.83 ? 869  ARG A CG  1 
ATOM   6818 C  CD  . ARG A 1 869  ? 27.710 83.815  -6.784  1.00 14.50 ? 869  ARG A CD  1 
ATOM   6819 N  NE  . ARG A 1 869  ? 27.833 84.998  -5.928  1.00 16.10 ? 869  ARG A NE  1 
ATOM   6820 C  CZ  . ARG A 1 869  ? 28.962 85.416  -5.360  1.00 16.94 ? 869  ARG A CZ  1 
ATOM   6821 N  NH1 . ARG A 1 869  ? 30.093 84.753  -5.555  1.00 16.49 ? 869  ARG A NH1 1 
ATOM   6822 N  NH2 . ARG A 1 869  ? 28.960 86.511  -4.581  1.00 16.30 ? 869  ARG A NH2 1 
ATOM   6823 N  N   . LEU A 1 870  ? 25.752 79.685  -4.194  1.00 13.85 ? 870  LEU A N   1 
ATOM   6824 C  CA  . LEU A 1 870  ? 24.589 79.553  -3.337  1.00 15.37 ? 870  LEU A CA  1 
ATOM   6825 C  C   . LEU A 1 870  ? 24.691 80.402  -2.066  1.00 15.79 ? 870  LEU A C   1 
ATOM   6826 O  O   . LEU A 1 870  ? 25.683 80.346  -1.307  1.00 14.77 ? 870  LEU A O   1 
ATOM   6827 C  CB  . LEU A 1 870  ? 24.416 78.074  -2.998  1.00 15.50 ? 870  LEU A CB  1 
ATOM   6828 C  CG  . LEU A 1 870  ? 24.482 77.275  -4.313  1.00 17.94 ? 870  LEU A CG  1 
ATOM   6829 C  CD1 . LEU A 1 870  ? 25.103 75.971  -4.035  1.00 18.88 ? 870  LEU A CD1 1 
ATOM   6830 C  CD2 . LEU A 1 870  ? 23.099 77.105  -4.965  1.00 18.07 ? 870  LEU A CD2 1 
ATOM   6831 N  N   . ALA A 1 871  ? 23.636 81.173  -1.834  1.00 16.54 ? 871  ALA A N   1 
ATOM   6832 C  CA  . ALA A 1 871  ? 23.602 82.077  -0.702  1.00 18.10 ? 871  ALA A CA  1 
ATOM   6833 C  C   . ALA A 1 871  ? 23.354 81.388  0.630   1.00 19.21 ? 871  ALA A C   1 
ATOM   6834 O  O   . ALA A 1 871  ? 23.754 81.913  1.657   1.00 20.24 ? 871  ALA A O   1 
ATOM   6835 C  CB  . ALA A 1 871  ? 22.518 83.161  -0.935  1.00 19.23 ? 871  ALA A CB  1 
ATOM   6836 N  N   . SER A 1 872  ? 22.703 80.220  0.625   1.00 18.78 ? 872  SER A N   1 
ATOM   6837 C  CA  . SER A 1 872  ? 22.381 79.551  1.897   1.00 18.65 ? 872  SER A CA  1 
ATOM   6838 C  C   . SER A 1 872  ? 23.208 78.354  2.298   1.00 17.17 ? 872  SER A C   1 
ATOM   6839 O  O   . SER A 1 872  ? 23.808 77.693  1.474   1.00 15.65 ? 872  SER A O   1 
ATOM   6840 C  CB  . SER A 1 872  ? 20.918 79.089  1.901   1.00 20.94 ? 872  SER A CB  1 
ATOM   6841 O  OG  . SER A 1 872  ? 20.037 80.157  1.586   1.00 23.65 ? 872  SER A OG  1 
ATOM   6842 N  N   . ASP A 1 873  ? 23.214 78.089  3.597   1.00 16.63 ? 873  ASP A N   1 
ATOM   6843 C  CA  . ASP A 1 873  ? 23.894 76.921  4.149   1.00 16.15 ? 873  ASP A CA  1 
ATOM   6844 C  C   . ASP A 1 873  ? 22.888 75.775  3.979   1.00 14.87 ? 873  ASP A C   1 
ATOM   6845 O  O   . ASP A 1 873  ? 21.685 76.017  4.027   1.00 14.37 ? 873  ASP A O   1 
ATOM   6846 C  CB  . ASP A 1 873  ? 24.156 77.114  5.624   1.00 15.20 ? 873  ASP A CB  1 
ATOM   6847 C  CG  . ASP A 1 873  ? 24.663 75.862  6.274   1.00 16.29 ? 873  ASP A CG  1 
ATOM   6848 O  OD1 . ASP A 1 873  ? 23.975 75.358  7.168   1.00 15.17 ? 873  ASP A OD1 1 
ATOM   6849 O  OD2 . ASP A 1 873  ? 25.751 75.365  5.880   1.00 16.00 ? 873  ASP A OD2 1 
ATOM   6850 N  N   . ASP A 1 874  ? 23.358 74.545  3.792   1.00 14.89 ? 874  ASP A N   1 
ATOM   6851 C  CA  . ASP A 1 874  ? 22.446 73.415  3.612   1.00 14.54 ? 874  ASP A CA  1 
ATOM   6852 C  C   . ASP A 1 874  ? 22.385 72.469  4.826   1.00 15.81 ? 874  ASP A C   1 
ATOM   6853 O  O   . ASP A 1 874  ? 22.139 71.274  4.699   1.00 15.44 ? 874  ASP A O   1 
ATOM   6854 C  CB  . ASP A 1 874  ? 22.772 72.648  2.322   1.00 14.03 ? 874  ASP A CB  1 
ATOM   6855 C  CG  . ASP A 1 874  ? 24.286 72.349  2.155   1.00 15.84 ? 874  ASP A CG  1 
ATOM   6856 O  OD1 . ASP A 1 874  ? 25.108 72.643  3.084   1.00 14.86 ? 874  ASP A OD1 1 
ATOM   6857 O  OD2 . ASP A 1 874  ? 24.639 71.807  1.076   1.00 14.34 ? 874  ASP A OD2 1 
ATOM   6858 N  N   . GLU A 1 875  ? 22.643 73.027  6.000   1.00 16.04 ? 875  GLU A N   1 
ATOM   6859 C  CA  . GLU A 1 875  ? 22.512 72.299  7.258   1.00 17.14 ? 875  GLU A CA  1 
ATOM   6860 C  C   . GLU A 1 875  ? 23.271 71.004  7.466   1.00 16.72 ? 875  GLU A C   1 
ATOM   6861 O  O   . GLU A 1 875  ? 22.750 70.086  8.113   1.00 14.98 ? 875  GLU A O   1 
ATOM   6862 C  CB  . GLU A 1 875  ? 21.019 72.032  7.520   1.00 20.19 ? 875  GLU A CB  1 
ATOM   6863 C  CG  . GLU A 1 875  ? 20.104 73.250  7.260   1.00 25.56 ? 875  GLU A CG  1 
ATOM   6864 C  CD  . GLU A 1 875  ? 18.670 73.020  7.728   1.00 28.90 ? 875  GLU A CD  1 
ATOM   6865 O  OE1 . GLU A 1 875  ? 18.400 73.207  8.932   1.00 31.65 ? 875  GLU A OE1 1 
ATOM   6866 O  OE2 . GLU A 1 875  ? 17.819 72.626  6.904   1.00 31.87 ? 875  GLU A OE2 1 
ATOM   6867 N  N   . ARG A 1 876  ? 24.496 70.913  6.949   1.00 15.16 ? 876  ARG A N   1 
ATOM   6868 C  CA  . ARG A 1 876  ? 25.278 69.710  7.172   1.00 12.73 ? 876  ARG A CA  1 
ATOM   6869 C  C   . ARG A 1 876  ? 26.509 70.095  7.997   1.00 13.13 ? 876  ARG A C   1 
ATOM   6870 O  O   . ARG A 1 876  ? 27.470 69.328  8.120   1.00 11.46 ? 876  ARG A O   1 
ATOM   6871 C  CB  . ARG A 1 876  ? 25.670 69.058  5.825   1.00 14.12 ? 876  ARG A CB  1 
ATOM   6872 C  CG  . ARG A 1 876  ? 24.475 68.436  5.029   1.00 9.31  ? 876  ARG A CG  1 
ATOM   6873 C  CD  . ARG A 1 876  ? 23.661 67.468  5.884   1.00 10.26 ? 876  ARG A CD  1 
ATOM   6874 N  NE  . ARG A 1 876  ? 22.545 66.797  5.202   1.00 10.11 ? 876  ARG A NE  1 
ATOM   6875 C  CZ  . ARG A 1 876  ? 21.350 67.354  4.949   1.00 11.85 ? 876  ARG A CZ  1 
ATOM   6876 N  NH1 . ARG A 1 876  ? 21.112 68.616  5.303   1.00 7.10  ? 876  ARG A NH1 1 
ATOM   6877 N  NH2 . ARG A 1 876  ? 20.370 66.616  4.412   1.00 10.56 ? 876  ARG A NH2 1 
ATOM   6878 N  N   . GLY A 1 877  ? 26.477 71.305  8.555   1.00 13.12 ? 877  GLY A N   1 
ATOM   6879 C  CA  . GLY A 1 877  ? 27.569 71.770  9.410   1.00 12.90 ? 877  GLY A CA  1 
ATOM   6880 C  C   . GLY A 1 877  ? 28.564 72.801  8.865   1.00 14.01 ? 877  GLY A C   1 
ATOM   6881 O  O   . GLY A 1 877  ? 29.334 73.395  9.655   1.00 14.47 ? 877  GLY A O   1 
ATOM   6882 N  N   . LEU A 1 878  ? 28.548 73.063  7.555   1.00 13.29 ? 878  LEU A N   1 
ATOM   6883 C  CA  . LEU A 1 878  ? 29.515 74.002  6.997   1.00 13.28 ? 878  LEU A CA  1 
ATOM   6884 C  C   . LEU A 1 878  ? 29.287 75.423  7.509   1.00 15.07 ? 878  LEU A C   1 
ATOM   6885 O  O   . LEU A 1 878  ? 30.249 76.182  7.714   1.00 14.61 ? 878  LEU A O   1 
ATOM   6886 C  CB  . LEU A 1 878  ? 29.491 73.930  5.460   1.00 13.22 ? 878  LEU A CB  1 
ATOM   6887 C  CG  . LEU A 1 878  ? 30.341 74.947  4.689   1.00 13.62 ? 878  LEU A CG  1 
ATOM   6888 C  CD1 . LEU A 1 878  ? 31.827 74.828  5.150   1.00 12.98 ? 878  LEU A CD1 1 
ATOM   6889 C  CD2 . LEU A 1 878  ? 30.210 74.676  3.191   1.00 11.07 ? 878  LEU A CD2 1 
ATOM   6890 N  N   . GLY A 1 879  ? 28.024 75.776  7.745   1.00 14.39 ? 879  GLY A N   1 
ATOM   6891 C  CA  . GLY A 1 879  ? 27.715 77.094  8.284   1.00 16.09 ? 879  GLY A CA  1 
ATOM   6892 C  C   . GLY A 1 879  ? 27.866 78.264  7.329   1.00 16.89 ? 879  GLY A C   1 
ATOM   6893 O  O   . GLY A 1 879  ? 28.020 79.412  7.756   1.00 16.56 ? 879  GLY A O   1 
ATOM   6894 N  N   . GLN A 1 880  ? 27.846 77.989  6.028   1.00 15.61 ? 880  GLN A N   1 
ATOM   6895 C  CA  . GLN A 1 880  ? 27.944 79.065  5.057   1.00 15.86 ? 880  GLN A CA  1 
ATOM   6896 C  C   . GLN A 1 880  ? 27.492 78.542  3.695   1.00 16.08 ? 880  GLN A C   1 
ATOM   6897 O  O   . GLN A 1 880  ? 27.372 77.319  3.495   1.00 15.70 ? 880  GLN A O   1 
ATOM   6898 C  CB  . GLN A 1 880  ? 29.399 79.595  4.965   1.00 16.31 ? 880  GLN A CB  1 
ATOM   6899 C  CG  . GLN A 1 880  ? 30.406 78.587  4.308   1.00 14.60 ? 880  GLN A CG  1 
ATOM   6900 C  CD  . GLN A 1 880  ? 31.741 79.232  3.899   1.00 13.46 ? 880  GLN A CD  1 
ATOM   6901 O  OE1 . GLN A 1 880  ? 32.589 79.504  4.740   1.00 12.66 ? 880  GLN A OE1 1 
ATOM   6902 N  NE2 . GLN A 1 880  ? 31.918 79.485  2.599   1.00 14.90 ? 880  GLN A NE2 1 
ATOM   6903 N  N   . GLY A 1 881  ? 27.212 79.466  2.780   1.00 15.67 ? 881  GLY A N   1 
ATOM   6904 C  CA  . GLY A 1 881  ? 26.834 79.069  1.440   1.00 15.36 ? 881  GLY A CA  1 
ATOM   6905 C  C   . GLY A 1 881  ? 28.123 79.000  0.616   1.00 16.36 ? 881  GLY A C   1 
ATOM   6906 O  O   . GLY A 1 881  ? 29.229 78.841  1.163   1.00 16.61 ? 881  GLY A O   1 
ATOM   6907 N  N   . VAL A 1 882  ? 27.984 79.105  -0.700  1.00 14.30 ? 882  VAL A N   1 
ATOM   6908 C  CA  . VAL A 1 882  ? 29.130 79.097  -1.587  1.00 14.29 ? 882  VAL A CA  1 
ATOM   6909 C  C   . VAL A 1 882  ? 29.105 80.411  -2.345  1.00 13.72 ? 882  VAL A C   1 
ATOM   6910 O  O   . VAL A 1 882  ? 28.394 80.546  -3.344  1.00 12.57 ? 882  VAL A O   1 
ATOM   6911 C  CB  . VAL A 1 882  ? 29.044 77.920  -2.562  1.00 13.52 ? 882  VAL A CB  1 
ATOM   6912 C  CG1 . VAL A 1 882  ? 30.181 77.994  -3.582  1.00 13.05 ? 882  VAL A CG1 1 
ATOM   6913 C  CG2 . VAL A 1 882  ? 29.086 76.622  -1.749  1.00 13.99 ? 882  VAL A CG2 1 
ATOM   6914 N  N   . LEU A 1 883  ? 29.870 81.379  -1.854  1.00 15.02 ? 883  LEU A N   1 
ATOM   6915 C  CA  . LEU A 1 883  ? 29.905 82.690  -2.483  1.00 16.24 ? 883  LEU A CA  1 
ATOM   6916 C  C   . LEU A 1 883  ? 31.323 83.147  -2.776  1.00 16.26 ? 883  LEU A C   1 
ATOM   6917 O  O   . LEU A 1 883  ? 31.561 84.342  -2.973  1.00 18.46 ? 883  LEU A O   1 
ATOM   6918 C  CB  . LEU A 1 883  ? 29.220 83.710  -1.574  1.00 17.49 ? 883  LEU A CB  1 
ATOM   6919 C  CG  . LEU A 1 883  ? 27.747 83.441  -1.244  1.00 18.13 ? 883  LEU A CG  1 
ATOM   6920 C  CD1 . LEU A 1 883  ? 27.250 84.477  -0.211  1.00 17.16 ? 883  LEU A CD1 1 
ATOM   6921 C  CD2 . LEU A 1 883  ? 26.924 83.538  -2.525  1.00 17.71 ? 883  LEU A CD2 1 
ATOM   6922 N  N   . ASP A 1 884  ? 32.263 82.207  -2.798  1.00 14.40 ? 884  ASP A N   1 
ATOM   6923 C  CA  . ASP A 1 884  ? 33.665 82.521  -3.074  1.00 14.06 ? 884  ASP A CA  1 
ATOM   6924 C  C   . ASP A 1 884  ? 34.133 82.085  -4.471  1.00 13.68 ? 884  ASP A C   1 
ATOM   6925 O  O   . ASP A 1 884  ? 35.308 81.798  -4.683  1.00 13.27 ? 884  ASP A O   1 
ATOM   6926 C  CB  . ASP A 1 884  ? 34.565 81.896  -2.018  1.00 14.25 ? 884  ASP A CB  1 
ATOM   6927 C  CG  . ASP A 1 884  ? 34.332 80.397  -1.844  1.00 16.73 ? 884  ASP A CG  1 
ATOM   6928 O  OD1 . ASP A 1 884  ? 34.997 79.828  -0.944  1.00 17.96 ? 884  ASP A OD1 1 
ATOM   6929 O  OD2 . ASP A 1 884  ? 33.499 79.793  -2.575  1.00 17.08 ? 884  ASP A OD2 1 
ATOM   6930 N  N   . ASN A 1 885  ? 33.201 82.054  -5.415  1.00 12.92 ? 885  ASN A N   1 
ATOM   6931 C  CA  . ASN A 1 885  ? 33.498 81.665  -6.777  1.00 12.83 ? 885  ASN A CA  1 
ATOM   6932 C  C   . ASN A 1 885  ? 34.556 82.535  -7.391  1.00 13.94 ? 885  ASN A C   1 
ATOM   6933 O  O   . ASN A 1 885  ? 34.680 83.713  -7.044  1.00 14.02 ? 885  ASN A O   1 
ATOM   6934 C  CB  . ASN A 1 885  ? 32.253 81.781  -7.657  1.00 12.68 ? 885  ASN A CB  1 
ATOM   6935 C  CG  . ASN A 1 885  ? 31.019 81.179  -7.004  1.00 13.31 ? 885  ASN A CG  1 
ATOM   6936 O  OD1 . ASN A 1 885  ? 30.431 81.767  -6.077  1.00 12.69 ? 885  ASN A OD1 1 
ATOM   6937 N  ND2 . ASN A 1 885  ? 30.638 80.002  -7.461  1.00 11.35 ? 885  ASN A ND2 1 
ATOM   6938 N  N   . LYS A 1 886  ? 35.312 81.948  -8.313  1.00 12.69 ? 886  LYS A N   1 
ATOM   6939 C  CA  . LYS A 1 886  ? 36.299 82.690  -9.034  1.00 14.36 ? 886  LYS A CA  1 
ATOM   6940 C  C   . LYS A 1 886  ? 36.416 82.099  -10.441 1.00 14.46 ? 886  LYS A C   1 
ATOM   6941 O  O   . LYS A 1 886  ? 36.065 80.929  -10.701 1.00 14.52 ? 886  LYS A O   1 
ATOM   6942 C  CB  . LYS A 1 886  ? 37.641 82.670  -8.290  1.00 16.61 ? 886  LYS A CB  1 
ATOM   6943 C  CG  . LYS A 1 886  ? 38.142 81.285  -8.010  1.00 18.84 ? 886  LYS A CG  1 
ATOM   6944 C  CD  . LYS A 1 886  ? 39.232 81.279  -6.939  1.00 22.86 ? 886  LYS A CD  1 
ATOM   6945 C  CE  . LYS A 1 886  ? 40.485 81.967  -7.403  1.00 20.16 ? 886  LYS A CE  1 
ATOM   6946 N  NZ  . LYS A 1 886  ? 41.671 81.517  -6.597  1.00 22.07 ? 886  LYS A NZ  1 
ATOM   6947 N  N   . PRO A 1 887  ? 36.899 82.908  -11.385 1.00 12.97 ? 887  PRO A N   1 
ATOM   6948 C  CA  . PRO A 1 887  ? 37.051 82.450  -12.761 1.00 12.09 ? 887  PRO A CA  1 
ATOM   6949 C  C   . PRO A 1 887  ? 37.803 81.119  -12.876 1.00 11.13 ? 887  PRO A C   1 
ATOM   6950 O  O   . PRO A 1 887  ? 38.858 80.944  -12.290 1.00 10.79 ? 887  PRO A O   1 
ATOM   6951 C  CB  . PRO A 1 887  ? 37.852 83.582  -13.405 1.00 13.48 ? 887  PRO A CB  1 
ATOM   6952 C  CG  . PRO A 1 887  ? 37.391 84.803  -12.651 1.00 12.82 ? 887  PRO A CG  1 
ATOM   6953 C  CD  . PRO A 1 887  ? 37.366 84.303  -11.226 1.00 14.02 ? 887  PRO A CD  1 
ATOM   6954 N  N   . VAL A 1 888  ? 37.249 80.179  -13.620 1.00 9.92  ? 888  VAL A N   1 
ATOM   6955 C  CA  . VAL A 1 888  ? 37.932 78.927  -13.819 1.00 10.24 ? 888  VAL A CA  1 
ATOM   6956 C  C   . VAL A 1 888  ? 37.798 78.569  -15.294 1.00 10.95 ? 888  VAL A C   1 
ATOM   6957 O  O   . VAL A 1 888  ? 36.782 78.910  -15.948 1.00 11.21 ? 888  VAL A O   1 
ATOM   6958 C  CB  . VAL A 1 888  ? 37.342 77.779  -12.918 1.00 11.39 ? 888  VAL A CB  1 
ATOM   6959 C  CG1 . VAL A 1 888  ? 35.797 77.694  -13.087 1.00 10.47 ? 888  VAL A CG1 1 
ATOM   6960 C  CG2 . VAL A 1 888  ? 38.017 76.424  -13.291 1.00 8.90  ? 888  VAL A CG2 1 
ATOM   6961 N  N   . LEU A 1 889  ? 38.824 77.900  -15.798 1.00 10.07 ? 889  LEU A N   1 
ATOM   6962 C  CA  . LEU A 1 889  ? 38.881 77.450  -17.182 1.00 9.94  ? 889  LEU A CA  1 
ATOM   6963 C  C   . LEU A 1 889  ? 38.682 75.952  -17.208 1.00 9.62  ? 889  LEU A C   1 
ATOM   6964 O  O   . LEU A 1 889  ? 39.599 75.190  -16.870 1.00 8.11  ? 889  LEU A O   1 
ATOM   6965 C  CB  . LEU A 1 889  ? 40.242 77.760  -17.827 1.00 9.67  ? 889  LEU A CB  1 
ATOM   6966 C  CG  . LEU A 1 889  ? 40.263 77.386  -19.336 1.00 10.10 ? 889  LEU A CG  1 
ATOM   6967 C  CD1 . LEU A 1 889  ? 39.493 78.440  -20.173 1.00 10.25 ? 889  LEU A CD1 1 
ATOM   6968 C  CD2 . LEU A 1 889  ? 41.712 77.249  -19.830 1.00 10.85 ? 889  LEU A CD2 1 
ATOM   6969 N  N   . HIS A 1 890  ? 37.471 75.525  -17.562 1.00 9.31  ? 890  HIS A N   1 
ATOM   6970 C  CA  . HIS A 1 890  ? 37.172 74.103  -17.664 1.00 9.29  ? 890  HIS A CA  1 
ATOM   6971 C  C   . HIS A 1 890  ? 37.540 73.653  -19.068 1.00 9.74  ? 890  HIS A C   1 
ATOM   6972 O  O   . HIS A 1 890  ? 37.281 74.363  -20.023 1.00 10.97 ? 890  HIS A O   1 
ATOM   6973 C  CB  . HIS A 1 890  ? 35.679 73.862  -17.461 1.00 9.45  ? 890  HIS A CB  1 
ATOM   6974 C  CG  . HIS A 1 890  ? 35.218 74.081  -16.059 1.00 9.04  ? 890  HIS A CG  1 
ATOM   6975 N  ND1 . HIS A 1 890  ? 35.969 73.705  -14.967 1.00 7.43  ? 890  HIS A ND1 1 
ATOM   6976 C  CD2 . HIS A 1 890  ? 34.047 74.544  -15.571 1.00 7.29  ? 890  HIS A CD2 1 
ATOM   6977 C  CE1 . HIS A 1 890  ? 35.272 73.915  -13.866 1.00 8.94  ? 890  HIS A CE1 1 
ATOM   6978 N  NE2 . HIS A 1 890  ? 34.102 74.424  -14.206 1.00 9.20  ? 890  HIS A NE2 1 
ATOM   6979 N  N   . ILE A 1 891  ? 38.131 72.473  -19.203 1.00 9.86  ? 891  ILE A N   1 
ATOM   6980 C  CA  . ILE A 1 891  ? 38.498 71.970  -20.518 1.00 8.70  ? 891  ILE A CA  1 
ATOM   6981 C  C   . ILE A 1 891  ? 37.870 70.598  -20.760 1.00 9.06  ? 891  ILE A C   1 
ATOM   6982 O  O   . ILE A 1 891  ? 37.628 69.842  -19.818 1.00 8.69  ? 891  ILE A O   1 
ATOM   6983 C  CB  . ILE A 1 891  ? 40.029 71.898  -20.677 1.00 7.64  ? 891  ILE A CB  1 
ATOM   6984 C  CG1 . ILE A 1 891  ? 40.618 70.914  -19.664 1.00 8.76  ? 891  ILE A CG1 1 
ATOM   6985 C  CG2 . ILE A 1 891  ? 40.624 73.299  -20.445 1.00 7.39  ? 891  ILE A CG2 1 
ATOM   6986 C  CD1 . ILE A 1 891  ? 42.170 70.725  -19.804 1.00 11.18 ? 891  ILE A CD1 1 
ATOM   6987 N  N   . TYR A 1 892  ? 37.613 70.293  -22.031 1.00 7.86  ? 892  TYR A N   1 
ATOM   6988 C  CA  . TYR A 1 892  ? 36.990 69.034  -22.421 1.00 9.18  ? 892  TYR A CA  1 
ATOM   6989 C  C   . TYR A 1 892  ? 37.417 68.639  -23.814 1.00 9.32  ? 892  TYR A C   1 
ATOM   6990 O  O   . TYR A 1 892  ? 38.031 69.418  -24.531 1.00 9.14  ? 892  TYR A O   1 
ATOM   6991 C  CB  . TYR A 1 892  ? 35.450 69.164  -22.508 1.00 7.68  ? 892  TYR A CB  1 
ATOM   6992 C  CG  . TYR A 1 892  ? 34.794 69.830  -21.347 1.00 8.33  ? 892  TYR A CG  1 
ATOM   6993 C  CD1 . TYR A 1 892  ? 34.798 71.235  -21.216 1.00 7.45  ? 892  TYR A CD1 1 
ATOM   6994 C  CD2 . TYR A 1 892  ? 34.162 69.066  -20.354 1.00 7.60  ? 892  TYR A CD2 1 
ATOM   6995 C  CE1 . TYR A 1 892  ? 34.183 71.857  -20.120 1.00 8.26  ? 892  TYR A CE1 1 
ATOM   6996 C  CE2 . TYR A 1 892  ? 33.552 69.679  -19.254 1.00 7.56  ? 892  TYR A CE2 1 
ATOM   6997 C  CZ  . TYR A 1 892  ? 33.564 71.068  -19.139 1.00 8.44  ? 892  TYR A CZ  1 
ATOM   6998 O  OH  . TYR A 1 892  ? 32.978 71.648  -18.031 1.00 9.84  ? 892  TYR A OH  1 
ATOM   6999 N  N   . ARG A 1 893  ? 37.083 67.402  -24.178 1.00 10.26 ? 893  ARG A N   1 
ATOM   7000 C  CA  . ARG A 1 893  ? 37.289 66.926  -25.551 1.00 10.44 ? 893  ARG A CA  1 
ATOM   7001 C  C   . ARG A 1 893  ? 35.897 66.334  -25.868 1.00 10.83 ? 893  ARG A C   1 
ATOM   7002 O  O   . ARG A 1 893  ? 35.299 65.680  -25.013 1.00 10.40 ? 893  ARG A O   1 
ATOM   7003 C  CB  . ARG A 1 893  ? 38.360 65.844  -25.671 1.00 9.93  ? 893  ARG A CB  1 
ATOM   7004 C  CG  . ARG A 1 893  ? 39.829 66.336  -25.547 1.00 10.83 ? 893  ARG A CG  1 
ATOM   7005 C  CD  . ARG A 1 893  ? 40.196 67.414  -26.599 1.00 10.47 ? 893  ARG A CD  1 
ATOM   7006 N  NE  . ARG A 1 893  ? 40.211 66.898  -27.970 1.00 12.00 ? 893  ARG A NE  1 
ATOM   7007 C  CZ  . ARG A 1 893  ? 41.101 66.024  -28.452 1.00 12.72 ? 893  ARG A CZ  1 
ATOM   7008 N  NH1 . ARG A 1 893  ? 42.069 65.529  -27.681 1.00 13.32 ? 893  ARG A NH1 1 
ATOM   7009 N  NH2 . ARG A 1 893  ? 41.053 65.674  -29.723 1.00 12.56 ? 893  ARG A NH2 1 
ATOM   7010 N  N   . LEU A 1 894  ? 35.380 66.594  -27.064 1.00 10.43 ? 894  LEU A N   1 
ATOM   7011 C  CA  . LEU A 1 894  ? 34.046 66.095  -27.435 1.00 11.57 ? 894  LEU A CA  1 
ATOM   7012 C  C   . LEU A 1 894  ? 34.228 65.112  -28.610 1.00 10.56 ? 894  LEU A C   1 
ATOM   7013 O  O   . LEU A 1 894  ? 34.632 65.497  -29.707 1.00 9.90  ? 894  LEU A O   1 
ATOM   7014 C  CB  . LEU A 1 894  ? 33.123 67.274  -27.816 1.00 11.07 ? 894  LEU A CB  1 
ATOM   7015 C  CG  . LEU A 1 894  ? 31.655 66.872  -28.152 1.00 12.75 ? 894  LEU A CG  1 
ATOM   7016 C  CD1 . LEU A 1 894  ? 30.926 66.407  -26.892 1.00 12.46 ? 894  LEU A CD1 1 
ATOM   7017 C  CD2 . LEU A 1 894  ? 30.892 68.067  -28.769 1.00 11.97 ? 894  LEU A CD2 1 
ATOM   7018 N  N   . VAL A 1 895  ? 33.929 63.839  -28.356 1.00 11.27 ? 895  VAL A N   1 
ATOM   7019 C  CA  . VAL A 1 895  ? 34.109 62.792  -29.349 1.00 11.99 ? 895  VAL A CA  1 
ATOM   7020 C  C   . VAL A 1 895  ? 32.811 62.187  -29.881 1.00 11.10 ? 895  VAL A C   1 
ATOM   7021 O  O   . VAL A 1 895  ? 32.133 61.484  -29.166 1.00 10.82 ? 895  VAL A O   1 
ATOM   7022 C  CB  . VAL A 1 895  ? 34.913 61.603  -28.760 1.00 12.12 ? 895  VAL A CB  1 
ATOM   7023 C  CG1 . VAL A 1 895  ? 35.238 60.622  -29.872 1.00 12.69 ? 895  VAL A CG1 1 
ATOM   7024 C  CG2 . VAL A 1 895  ? 36.168 62.098  -28.039 1.00 14.25 ? 895  VAL A CG2 1 
ATOM   7025 N  N   . LEU A 1 896  ? 32.485 62.452  -31.139 1.00 12.05 ? 896  LEU A N   1 
ATOM   7026 C  CA  . LEU A 1 896  ? 31.291 61.866  -31.746 1.00 10.99 ? 896  LEU A CA  1 
ATOM   7027 C  C   . LEU A 1 896  ? 31.869 60.719  -32.581 1.00 10.94 ? 896  LEU A C   1 
ATOM   7028 O  O   . LEU A 1 896  ? 32.793 60.950  -33.363 1.00 10.03 ? 896  LEU A O   1 
ATOM   7029 C  CB  . LEU A 1 896  ? 30.585 62.855  -32.686 1.00 9.73  ? 896  LEU A CB  1 
ATOM   7030 C  CG  . LEU A 1 896  ? 29.440 62.222  -33.523 1.00 11.23 ? 896  LEU A CG  1 
ATOM   7031 C  CD1 . LEU A 1 896  ? 28.191 61.987  -32.645 1.00 11.75 ? 896  LEU A CD1 1 
ATOM   7032 C  CD2 . LEU A 1 896  ? 29.072 63.144  -34.693 1.00 13.91 ? 896  LEU A CD2 1 
ATOM   7033 N  N   . GLU A 1 897  ? 31.347 59.503  -32.420 1.00 10.40 ? 897  GLU A N   1 
ATOM   7034 C  CA  . GLU A 1 897  ? 31.872 58.365  -33.190 1.00 12.99 ? 897  GLU A CA  1 
ATOM   7035 C  C   . GLU A 1 897  ? 30.785 57.354  -33.553 1.00 13.28 ? 897  GLU A C   1 
ATOM   7036 O  O   . GLU A 1 897  ? 29.773 57.266  -32.877 1.00 14.23 ? 897  GLU A O   1 
ATOM   7037 C  CB  . GLU A 1 897  ? 32.916 57.564  -32.384 1.00 12.46 ? 897  GLU A CB  1 
ATOM   7038 C  CG  . GLU A 1 897  ? 33.760 58.310  -31.413 1.00 15.32 ? 897  GLU A CG  1 
ATOM   7039 C  CD  . GLU A 1 897  ? 34.424 57.372  -30.373 1.00 11.99 ? 897  GLU A CD  1 
ATOM   7040 O  OE1 . GLU A 1 897  ? 33.827 57.092  -29.297 1.00 13.19 ? 897  GLU A OE1 1 
ATOM   7041 O  OE2 . GLU A 1 897  ? 35.551 56.943  -30.657 1.00 12.08 ? 897  GLU A OE2 1 
ATOM   7042 N  N   . LYS A 1 898  ? 31.023 56.569  -34.599 1.00 14.64 ? 898  LYS A N   1 
ATOM   7043 C  CA  . LYS A 1 898  ? 30.098 55.504  -34.991 1.00 16.65 ? 898  LYS A CA  1 
ATOM   7044 C  C   . LYS A 1 898  ? 30.587 54.269  -34.196 1.00 17.39 ? 898  LYS A C   1 
ATOM   7045 O  O   . LYS A 1 898  ? 31.792 53.982  -34.169 1.00 18.43 ? 898  LYS A O   1 
ATOM   7046 C  CB  . LYS A 1 898  ? 30.187 55.231  -36.502 1.00 17.75 ? 898  LYS A CB  1 
ATOM   7047 C  CG  . LYS A 1 898  ? 29.780 56.416  -37.384 1.00 21.30 ? 898  LYS A CG  1 
ATOM   7048 C  CD  . LYS A 1 898  ? 28.432 57.011  -36.918 1.00 25.90 ? 898  LYS A CD  1 
ATOM   7049 C  CE  . LYS A 1 898  ? 27.187 56.238  -37.417 1.00 27.91 ? 898  LYS A CE  1 
ATOM   7050 N  NZ  . LYS A 1 898  ? 27.281 54.765  -37.243 1.00 30.04 ? 898  LYS A NZ  1 
ATOM   7051 N  N   . VAL A 1 899  ? 29.680 53.553  -33.544 1.00 16.16 ? 899  VAL A N   1 
ATOM   7052 C  CA  . VAL A 1 899  ? 30.084 52.391  -32.748 1.00 15.61 ? 899  VAL A CA  1 
ATOM   7053 C  C   . VAL A 1 899  ? 29.374 51.109  -33.199 1.00 15.61 ? 899  VAL A C   1 
ATOM   7054 O  O   . VAL A 1 899  ? 29.430 50.082  -32.518 1.00 12.65 ? 899  VAL A O   1 
ATOM   7055 C  CB  . VAL A 1 899  ? 29.763 52.625  -31.241 1.00 14.05 ? 899  VAL A CB  1 
ATOM   7056 C  CG1 . VAL A 1 899  ? 30.713 53.698  -30.666 1.00 16.03 ? 899  VAL A CG1 1 
ATOM   7057 C  CG2 . VAL A 1 899  ? 28.305 53.098  -31.078 1.00 13.55 ? 899  VAL A CG2 1 
ATOM   7058 N  N   . ASN A 1 900  ? 28.726 51.158  -34.359 1.00 15.49 ? 900  ASN A N   1 
ATOM   7059 C  CA  . ASN A 1 900  ? 27.981 49.978  -34.811 1.00 17.00 ? 900  ASN A CA  1 
ATOM   7060 C  C   . ASN A 1 900  ? 28.863 48.749  -35.049 1.00 16.91 ? 900  ASN A C   1 
ATOM   7061 O  O   . ASN A 1 900  ? 28.380 47.625  -35.024 1.00 18.23 ? 900  ASN A O   1 
ATOM   7062 C  CB  . ASN A 1 900  ? 27.189 50.308  -36.077 1.00 18.87 ? 900  ASN A CB  1 
ATOM   7063 C  CG  . ASN A 1 900  ? 28.055 50.868  -37.143 1.00 20.34 ? 900  ASN A CG  1 
ATOM   7064 O  OD1 . ASN A 1 900  ? 28.659 51.926  -36.974 1.00 21.74 ? 900  ASN A OD1 1 
ATOM   7065 N  ND2 . ASN A 1 900  ? 28.156 50.153  -38.258 1.00 22.86 ? 900  ASN A ND2 1 
ATOM   7066 N  N   . ASN A 1 901  ? 30.155 48.952  -35.262 1.00 16.16 ? 901  ASN A N   1 
ATOM   7067 C  CA  . ASN A 1 901  ? 31.035 47.821  -35.497 1.00 16.97 ? 901  ASN A CA  1 
ATOM   7068 C  C   . ASN A 1 901  ? 31.793 47.417  -34.255 1.00 16.97 ? 901  ASN A C   1 
ATOM   7069 O  O   . ASN A 1 901  ? 32.545 46.445  -34.282 1.00 16.03 ? 901  ASN A O   1 
ATOM   7070 C  CB  . ASN A 1 901  ? 32.048 48.149  -36.594 1.00 19.02 ? 901  ASN A CB  1 
ATOM   7071 C  CG  . ASN A 1 901  ? 31.419 48.157  -37.966 1.00 22.17 ? 901  ASN A CG  1 
ATOM   7072 O  OD1 . ASN A 1 901  ? 30.548 47.332  -38.255 1.00 24.47 ? 901  ASN A OD1 1 
ATOM   7073 N  ND2 . ASN A 1 901  ? 31.864 49.081  -38.837 1.00 23.58 ? 901  ASN A ND2 1 
ATOM   7074 N  N   . CYS A 1 902  ? 31.613 48.163  -33.169 1.00 15.07 ? 902  CYS A N   1 
ATOM   7075 C  CA  . CYS A 1 902  ? 32.347 47.847  -31.961 1.00 15.32 ? 902  CYS A CA  1 
ATOM   7076 C  C   . CYS A 1 902  ? 31.822 46.634  -31.203 1.00 14.98 ? 902  CYS A C   1 
ATOM   7077 O  O   . CYS A 1 902  ? 30.617 46.426  -31.111 1.00 15.40 ? 902  CYS A O   1 
ATOM   7078 C  CB  . CYS A 1 902  ? 32.336 49.040  -31.021 1.00 15.10 ? 902  CYS A CB  1 
ATOM   7079 S  SG  . CYS A 1 902  ? 33.085 50.565  -31.667 1.00 14.32 ? 902  CYS A SG  1 
ATOM   7080 N  N   . VAL A 1 903  ? 32.732 45.835  -30.662 1.00 13.80 ? 903  VAL A N   1 
ATOM   7081 C  CA  . VAL A 1 903  ? 32.332 44.687  -29.854 1.00 14.25 ? 903  VAL A CA  1 
ATOM   7082 C  C   . VAL A 1 903  ? 32.031 45.257  -28.465 1.00 14.94 ? 903  VAL A C   1 
ATOM   7083 O  O   . VAL A 1 903  ? 32.934 45.678  -27.742 1.00 14.96 ? 903  VAL A O   1 
ATOM   7084 C  CB  . VAL A 1 903  ? 33.452 43.633  -29.789 1.00 14.34 ? 903  VAL A CB  1 
ATOM   7085 C  CG1 . VAL A 1 903  ? 33.068 42.511  -28.802 1.00 12.50 ? 903  VAL A CG1 1 
ATOM   7086 C  CG2 . VAL A 1 903  ? 33.649 43.045  -31.188 1.00 13.25 ? 903  VAL A CG2 1 
ATOM   7087 N  N   . ARG A 1 904  ? 30.758 45.312  -28.119 1.00 15.18 ? 904  ARG A N   1 
ATOM   7088 C  CA  . ARG A 1 904  ? 30.336 45.866  -26.835 1.00 16.60 ? 904  ARG A CA  1 
ATOM   7089 C  C   . ARG A 1 904  ? 29.797 44.841  -25.848 1.00 16.20 ? 904  ARG A C   1 
ATOM   7090 O  O   . ARG A 1 904  ? 29.452 43.723  -26.223 1.00 14.68 ? 904  ARG A O   1 
ATOM   7091 C  CB  . ARG A 1 904  ? 29.256 46.936  -27.059 1.00 16.68 ? 904  ARG A CB  1 
ATOM   7092 C  CG  . ARG A 1 904  ? 29.805 48.221  -27.650 1.00 18.92 ? 904  ARG A CG  1 
ATOM   7093 C  CD  . ARG A 1 904  ? 28.683 49.205  -27.956 1.00 20.71 ? 904  ARG A CD  1 
ATOM   7094 N  NE  . ARG A 1 904  ? 27.986 48.857  -29.183 1.00 21.45 ? 904  ARG A NE  1 
ATOM   7095 C  CZ  . ARG A 1 904  ? 27.021 49.603  -29.717 1.00 24.36 ? 904  ARG A CZ  1 
ATOM   7096 N  NH1 . ARG A 1 904  ? 26.647 50.726  -29.112 1.00 22.63 ? 904  ARG A NH1 1 
ATOM   7097 N  NH2 . ARG A 1 904  ? 26.443 49.239  -30.859 1.00 21.71 ? 904  ARG A NH2 1 
ATOM   7098 N  N   . PRO A 1 905  ? 29.730 45.219  -24.556 1.00 16.00 ? 905  PRO A N   1 
ATOM   7099 C  CA  . PRO A 1 905  ? 29.208 44.298  -23.542 1.00 14.61 ? 905  PRO A CA  1 
ATOM   7100 C  C   . PRO A 1 905  ? 27.732 44.075  -23.870 1.00 15.25 ? 905  PRO A C   1 
ATOM   7101 O  O   . PRO A 1 905  ? 27.112 44.911  -24.524 1.00 13.47 ? 905  PRO A O   1 
ATOM   7102 C  CB  . PRO A 1 905  ? 29.355 45.076  -22.236 1.00 14.64 ? 905  PRO A CB  1 
ATOM   7103 C  CG  . PRO A 1 905  ? 30.446 46.102  -22.529 1.00 15.03 ? 905  PRO A CG  1 
ATOM   7104 C  CD  . PRO A 1 905  ? 30.232 46.476  -23.959 1.00 15.52 ? 905  PRO A CD  1 
ATOM   7105 N  N   . SER A 1 906  ? 27.173 42.958  -23.424 1.00 16.09 ? 906  SER A N   1 
ATOM   7106 C  CA  . SER A 1 906  ? 25.760 42.695  -23.663 1.00 18.17 ? 906  SER A CA  1 
ATOM   7107 C  C   . SER A 1 906  ? 24.945 43.711  -22.863 1.00 18.46 ? 906  SER A C   1 
ATOM   7108 O  O   . SER A 1 906  ? 25.472 44.432  -22.000 1.00 16.63 ? 906  SER A O   1 
ATOM   7109 C  CB  . SER A 1 906  ? 25.373 41.289  -23.196 1.00 19.22 ? 906  SER A CB  1 
ATOM   7110 O  OG  . SER A 1 906  ? 24.884 41.339  -21.852 1.00 23.97 ? 906  SER A OG  1 
ATOM   7111 N  N   . LYS A 1 907  ? 23.648 43.738  -23.122 1.00 19.52 ? 907  LYS A N   1 
ATOM   7112 C  CA  . LYS A 1 907  ? 22.759 44.668  -22.443 1.00 21.98 ? 907  LYS A CA  1 
ATOM   7113 C  C   . LYS A 1 907  ? 22.691 44.554  -20.930 1.00 20.54 ? 907  LYS A C   1 
ATOM   7114 O  O   . LYS A 1 907  ? 22.327 45.504  -20.276 1.00 22.06 ? 907  LYS A O   1 
ATOM   7115 C  CB  . LYS A 1 907  ? 21.347 44.519  -22.994 1.00 24.94 ? 907  LYS A CB  1 
ATOM   7116 C  CG  . LYS A 1 907  ? 21.253 44.781  -24.485 1.00 30.73 ? 907  LYS A CG  1 
ATOM   7117 C  CD  . LYS A 1 907  ? 19.802 44.658  -24.951 1.00 34.29 ? 907  LYS A CD  1 
ATOM   7118 C  CE  . LYS A 1 907  ? 19.657 44.967  -26.435 1.00 36.16 ? 907  LYS A CE  1 
ATOM   7119 N  NZ  . LYS A 1 907  ? 18.232 44.729  -26.825 1.00 38.53 ? 907  LYS A NZ  1 
ATOM   7120 N  N   . LEU A 1 908  ? 23.013 43.398  -20.365 1.00 20.07 ? 908  LEU A N   1 
ATOM   7121 C  CA  . LEU A 1 908  ? 22.927 43.238  -18.915 1.00 19.40 ? 908  LEU A CA  1 
ATOM   7122 C  C   . LEU A 1 908  ? 24.247 43.524  -18.188 1.00 17.45 ? 908  LEU A C   1 
ATOM   7123 O  O   . LEU A 1 908  ? 24.315 43.486  -16.968 1.00 16.47 ? 908  LEU A O   1 
ATOM   7124 C  CB  . LEU A 1 908  ? 22.445 41.818  -18.591 1.00 20.99 ? 908  LEU A CB  1 
ATOM   7125 C  CG  . LEU A 1 908  ? 21.177 41.322  -19.311 1.00 22.11 ? 908  LEU A CG  1 
ATOM   7126 C  CD1 . LEU A 1 908  ? 20.920 39.834  -18.982 1.00 23.14 ? 908  LEU A CD1 1 
ATOM   7127 C  CD2 . LEU A 1 908  ? 19.976 42.166  -18.892 1.00 23.46 ? 908  LEU A CD2 1 
ATOM   7128 N  N   . HIS A 1 909  ? 25.307 43.795  -18.940 1.00 16.45 ? 909  HIS A N   1 
ATOM   7129 C  CA  . HIS A 1 909  ? 26.610 44.074  -18.324 1.00 15.71 ? 909  HIS A CA  1 
ATOM   7130 C  C   . HIS A 1 909  ? 26.549 45.470  -17.672 1.00 15.43 ? 909  HIS A C   1 
ATOM   7131 O  O   . HIS A 1 909  ? 26.075 46.414  -18.282 1.00 16.39 ? 909  HIS A O   1 
ATOM   7132 C  CB  . HIS A 1 909  ? 27.695 44.020  -19.401 1.00 14.68 ? 909  HIS A CB  1 
ATOM   7133 C  CG  . HIS A 1 909  ? 29.074 43.795  -18.861 1.00 13.44 ? 909  HIS A CG  1 
ATOM   7134 N  ND1 . HIS A 1 909  ? 29.763 44.757  -18.146 1.00 14.02 ? 909  HIS A ND1 1 
ATOM   7135 C  CD2 . HIS A 1 909  ? 29.901 42.726  -18.951 1.00 12.13 ? 909  HIS A CD2 1 
ATOM   7136 C  CE1 . HIS A 1 909  ? 30.960 44.290  -17.830 1.00 14.10 ? 909  HIS A CE1 1 
ATOM   7137 N  NE2 . HIS A 1 909  ? 31.068 43.059  -18.310 1.00 12.70 ? 909  HIS A NE2 1 
ATOM   7138 N  N   . PRO A 1 910  ? 27.020 45.605  -16.424 1.00 14.81 ? 910  PRO A N   1 
ATOM   7139 C  CA  . PRO A 1 910  ? 26.992 46.908  -15.730 1.00 13.54 ? 910  PRO A CA  1 
ATOM   7140 C  C   . PRO A 1 910  ? 28.070 47.917  -16.138 1.00 12.75 ? 910  PRO A C   1 
ATOM   7141 O  O   . PRO A 1 910  ? 28.069 49.045  -15.644 1.00 12.13 ? 910  PRO A O   1 
ATOM   7142 C  CB  . PRO A 1 910  ? 27.148 46.540  -14.249 1.00 14.40 ? 910  PRO A CB  1 
ATOM   7143 C  CG  . PRO A 1 910  ? 27.086 45.028  -14.188 1.00 15.33 ? 910  PRO A CG  1 
ATOM   7144 C  CD  . PRO A 1 910  ? 27.558 44.555  -15.539 1.00 15.02 ? 910  PRO A CD  1 
ATOM   7145 N  N   . ALA A 1 911  ? 29.001 47.512  -17.004 1.00 11.78 ? 911  ALA A N   1 
ATOM   7146 C  CA  . ALA A 1 911  ? 30.074 48.399  -17.420 1.00 10.89 ? 911  ALA A CA  1 
ATOM   7147 C  C   . ALA A 1 911  ? 30.026 48.867  -18.862 1.00 10.64 ? 911  ALA A C   1 
ATOM   7148 O  O   . ALA A 1 911  ? 29.314 48.305  -19.705 1.00 9.65  ? 911  ALA A O   1 
ATOM   7149 C  CB  . ALA A 1 911  ? 31.421 47.718  -17.200 1.00 10.57 ? 911  ALA A CB  1 
ATOM   7150 N  N   . GLY A 1 912  ? 30.862 49.873  -19.133 1.00 10.17 ? 912  GLY A N   1 
ATOM   7151 C  CA  . GLY A 1 912  ? 31.008 50.415  -20.468 1.00 9.81  ? 912  GLY A CA  1 
ATOM   7152 C  C   . GLY A 1 912  ? 32.485 50.667  -20.678 1.00 10.11 ? 912  GLY A C   1 
ATOM   7153 O  O   . GLY A 1 912  ? 33.237 50.789  -19.684 1.00 10.04 ? 912  GLY A O   1 
ATOM   7154 N  N   . TYR A 1 913  ? 32.913 50.753  -21.936 1.00 10.54 ? 913  TYR A N   1 
ATOM   7155 C  CA  . TYR A 1 913  ? 34.326 50.997  -22.248 1.00 10.23 ? 913  TYR A CA  1 
ATOM   7156 C  C   . TYR A 1 913  ? 34.525 52.034  -23.345 1.00 10.83 ? 913  TYR A C   1 
ATOM   7157 O  O   . TYR A 1 913  ? 33.744 52.132  -24.286 1.00 9.87  ? 913  TYR A O   1 
ATOM   7158 C  CB  . TYR A 1 913  ? 35.032 49.708  -22.665 1.00 12.18 ? 913  TYR A CB  1 
ATOM   7159 C  CG  . TYR A 1 913  ? 35.021 48.670  -21.581 1.00 11.08 ? 913  TYR A CG  1 
ATOM   7160 C  CD1 . TYR A 1 913  ? 34.031 47.706  -21.537 1.00 12.38 ? 913  TYR A CD1 1 
ATOM   7161 C  CD2 . TYR A 1 913  ? 35.932 48.733  -20.528 1.00 10.67 ? 913  TYR A CD2 1 
ATOM   7162 C  CE1 . TYR A 1 913  ? 33.936 46.819  -20.452 1.00 11.62 ? 913  TYR A CE1 1 
ATOM   7163 C  CE2 . TYR A 1 913  ? 35.856 47.858  -19.447 1.00 10.50 ? 913  TYR A CE2 1 
ATOM   7164 C  CZ  . TYR A 1 913  ? 34.852 46.904  -19.413 1.00 11.22 ? 913  TYR A CZ  1 
ATOM   7165 O  OH  . TYR A 1 913  ? 34.740 46.054  -18.333 1.00 12.20 ? 913  TYR A OH  1 
ATOM   7166 N  N   . LEU A 1 914  ? 35.584 52.808  -23.213 1.00 10.58 ? 914  LEU A N   1 
ATOM   7167 C  CA  . LEU A 1 914  ? 35.914 53.821  -24.200 1.00 10.85 ? 914  LEU A CA  1 
ATOM   7168 C  C   . LEU A 1 914  ? 36.543 53.215  -25.445 1.00 10.68 ? 914  LEU A C   1 
ATOM   7169 O  O   . LEU A 1 914  ? 37.016 52.059  -25.453 1.00 10.34 ? 914  LEU A O   1 
ATOM   7170 C  CB  . LEU A 1 914  ? 36.919 54.814  -23.619 1.00 8.69  ? 914  LEU A CB  1 
ATOM   7171 C  CG  . LEU A 1 914  ? 36.481 55.660  -22.421 1.00 9.55  ? 914  LEU A CG  1 
ATOM   7172 C  CD1 . LEU A 1 914  ? 37.599 56.662  -22.108 1.00 4.33  ? 914  LEU A CD1 1 
ATOM   7173 C  CD2 . LEU A 1 914  ? 35.130 56.404  -22.708 1.00 8.94  ? 914  LEU A CD2 1 
ATOM   7174 N  N   . THR A 1 915  ? 36.554 54.026  -26.498 1.00 11.17 ? 915  THR A N   1 
ATOM   7175 C  CA  . THR A 1 915  ? 37.183 53.672  -27.747 1.00 10.56 ? 915  THR A CA  1 
ATOM   7176 C  C   . THR A 1 915  ? 38.580 54.265  -27.612 1.00 11.26 ? 915  THR A C   1 
ATOM   7177 O  O   . THR A 1 915  ? 38.864 55.081  -26.718 1.00 9.61  ? 915  THR A O   1 
ATOM   7178 C  CB  . THR A 1 915  ? 36.573 54.406  -28.932 1.00 12.32 ? 915  THR A CB  1 
ATOM   7179 O  OG1 . THR A 1 915  ? 36.546 55.821  -28.639 1.00 13.22 ? 915  THR A OG1 1 
ATOM   7180 C  CG2 . THR A 1 915  ? 35.185 53.892  -29.243 1.00 12.00 ? 915  THR A CG2 1 
ATOM   7181 N  N   . SER A 1 916  ? 39.441 53.871  -28.532 1.00 11.39 ? 916  SER A N   1 
ATOM   7182 C  CA  . SER A 1 916  ? 40.811 54.364  -28.583 1.00 11.86 ? 916  SER A CA  1 
ATOM   7183 C  C   . SER A 1 916  ? 40.823 55.896  -28.685 1.00 12.08 ? 916  SER A C   1 
ATOM   7184 O  O   . SER A 1 916  ? 41.550 56.557  -27.957 1.00 11.70 ? 916  SER A O   1 
ATOM   7185 C  CB  . SER A 1 916  ? 41.516 53.758  -29.795 1.00 12.71 ? 916  SER A CB  1 
ATOM   7186 O  OG  . SER A 1 916  ? 42.759 54.406  -30.025 1.00 17.18 ? 916  SER A OG  1 
ATOM   7187 N  N   . ALA A 1 917  ? 40.002 56.469  -29.568 1.00 11.56 ? 917  ALA A N   1 
ATOM   7188 C  CA  . ALA A 1 917  ? 39.999 57.931  -29.712 1.00 10.26 ? 917  ALA A CA  1 
ATOM   7189 C  C   . ALA A 1 917  ? 39.562 58.633  -28.436 1.00 9.80  ? 917  ALA A C   1 
ATOM   7190 O  O   . ALA A 1 917  ? 40.159 59.644  -28.053 1.00 9.57  ? 917  ALA A O   1 
ATOM   7191 C  CB  . ALA A 1 917  ? 39.084 58.368  -30.885 1.00 11.51 ? 917  ALA A CB  1 
ATOM   7192 N  N   . ALA A 1 918  ? 38.525 58.108  -27.781 1.00 8.47  ? 918  ALA A N   1 
ATOM   7193 C  CA  . ALA A 1 918  ? 38.024 58.736  -26.551 1.00 9.07  ? 918  ALA A CA  1 
ATOM   7194 C  C   . ALA A 1 918  ? 39.064 58.636  -25.443 1.00 8.97  ? 918  ALA A C   1 
ATOM   7195 O  O   . ALA A 1 918  ? 39.273 59.581  -24.678 1.00 8.65  ? 918  ALA A O   1 
ATOM   7196 C  CB  . ALA A 1 918  ? 36.704 58.109  -26.119 1.00 7.40  ? 918  ALA A CB  1 
ATOM   7197 N  N   . HIS A 1 919  ? 39.746 57.509  -25.388 1.00 7.69  ? 919  HIS A N   1 
ATOM   7198 C  CA  . HIS A 1 919  ? 40.765 57.319  -24.372 1.00 9.17  ? 919  HIS A CA  1 
ATOM   7199 C  C   . HIS A 1 919  ? 41.937 58.279  -24.599 1.00 8.84  ? 919  HIS A C   1 
ATOM   7200 O  O   . HIS A 1 919  ? 42.369 58.955  -23.676 1.00 9.13  ? 919  HIS A O   1 
ATOM   7201 C  CB  . HIS A 1 919  ? 41.241 55.870  -24.377 1.00 8.81  ? 919  HIS A CB  1 
ATOM   7202 C  CG  . HIS A 1 919  ? 42.375 55.618  -23.436 1.00 11.84 ? 919  HIS A CG  1 
ATOM   7203 N  ND1 . HIS A 1 919  ? 43.628 55.227  -23.864 1.00 12.07 ? 919  HIS A ND1 1 
ATOM   7204 C  CD2 . HIS A 1 919  ? 42.441 55.682  -22.088 1.00 10.15 ? 919  HIS A CD2 1 
ATOM   7205 C  CE1 . HIS A 1 919  ? 44.417 55.048  -22.822 1.00 10.60 ? 919  HIS A CE1 1 
ATOM   7206 N  NE2 . HIS A 1 919  ? 43.722 55.318  -21.736 1.00 12.11 ? 919  HIS A NE2 1 
ATOM   7207 N  N   . LYS A 1 920  ? 42.458 58.343  -25.817 1.00 9.04  ? 920  LYS A N   1 
ATOM   7208 C  CA  . LYS A 1 920  ? 43.545 59.270  -26.054 1.00 8.71  ? 920  LYS A CA  1 
ATOM   7209 C  C   . LYS A 1 920  ? 43.099 60.713  -25.783 1.00 8.47  ? 920  LYS A C   1 
ATOM   7210 O  O   . LYS A 1 920  ? 43.899 61.533  -25.325 1.00 7.74  ? 920  LYS A O   1 
ATOM   7211 C  CB  . LYS A 1 920  ? 44.073 59.122  -27.487 1.00 10.81 ? 920  LYS A CB  1 
ATOM   7212 C  CG  . LYS A 1 920  ? 44.932 57.852  -27.660 1.00 13.48 ? 920  LYS A CG  1 
ATOM   7213 C  CD  . LYS A 1 920  ? 45.612 57.795  -29.023 1.00 13.63 ? 920  LYS A CD  1 
ATOM   7214 C  CE  . LYS A 1 920  ? 46.566 56.624  -29.073 1.00 13.51 ? 920  LYS A CE  1 
ATOM   7215 N  NZ  . LYS A 1 920  ? 47.725 56.813  -28.175 1.00 15.09 ? 920  LYS A NZ  1 
ATOM   7216 N  N   . ALA A 1 921  ? 41.839 61.033  -26.071 1.00 8.50  ? 921  ALA A N   1 
ATOM   7217 C  CA  . ALA A 1 921  ? 41.360 62.403  -25.824 1.00 9.26  ? 921  ALA A CA  1 
ATOM   7218 C  C   . ALA A 1 921  ? 41.405 62.663  -24.311 1.00 9.81  ? 921  ALA A C   1 
ATOM   7219 O  O   . ALA A 1 921  ? 41.741 63.774  -23.872 1.00 9.93  ? 921  ALA A O   1 
ATOM   7220 C  CB  . ALA A 1 921  ? 39.932 62.591  -26.358 1.00 6.62  ? 921  ALA A CB  1 
ATOM   7221 N  N   . SER A 1 922  ? 41.054 61.662  -23.503 1.00 9.39  ? 922  SER A N   1 
ATOM   7222 C  CA  . SER A 1 922  ? 41.114 61.860  -22.044 1.00 9.31  ? 922  SER A CA  1 
ATOM   7223 C  C   . SER A 1 922  ? 42.569 62.091  -21.632 1.00 9.10  ? 922  SER A C   1 
ATOM   7224 O  O   . SER A 1 922  ? 42.873 62.954  -20.804 1.00 9.33  ? 922  SER A O   1 
ATOM   7225 C  CB  . SER A 1 922  ? 40.584 60.626  -21.282 1.00 9.94  ? 922  SER A CB  1 
ATOM   7226 O  OG  . SER A 1 922  ? 40.580 60.899  -19.880 1.00 5.80  ? 922  SER A OG  1 
ATOM   7227 N  N   . GLN A 1 923  ? 43.482 61.308  -22.201 1.00 8.78  ? 923  GLN A N   1 
ATOM   7228 C  CA  . GLN A 1 923  ? 44.889 61.476  -21.867 1.00 8.73  ? 923  GLN A CA  1 
ATOM   7229 C  C   . GLN A 1 923  ? 45.425 62.855  -22.282 1.00 8.59  ? 923  GLN A C   1 
ATOM   7230 O  O   . GLN A 1 923  ? 46.287 63.396  -21.596 1.00 8.78  ? 923  GLN A O   1 
ATOM   7231 C  CB  . GLN A 1 923  ? 45.721 60.372  -22.511 1.00 7.89  ? 923  GLN A CB  1 
ATOM   7232 C  CG  . GLN A 1 923  ? 45.442 58.973  -21.935 1.00 7.22  ? 923  GLN A CG  1 
ATOM   7233 C  CD  . GLN A 1 923  ? 46.378 57.971  -22.531 1.00 9.15  ? 923  GLN A CD  1 
ATOM   7234 O  OE1 . GLN A 1 923  ? 46.505 57.910  -23.767 1.00 8.68  ? 923  GLN A OE1 1 
ATOM   7235 N  NE2 . GLN A 1 923  ? 47.054 57.171  -21.677 1.00 6.82  ? 923  GLN A NE2 1 
ATOM   7236 N  N   . SER A 1 924  ? 44.899 63.433  -23.368 1.00 8.14  ? 924  SER A N   1 
ATOM   7237 C  CA  . SER A 1 924  ? 45.355 64.764  -23.827 1.00 9.77  ? 924  SER A CA  1 
ATOM   7238 C  C   . SER A 1 924  ? 44.948 65.837  -22.815 1.00 10.17 ? 924  SER A C   1 
ATOM   7239 O  O   . SER A 1 924  ? 45.590 66.878  -22.707 1.00 11.74 ? 924  SER A O   1 
ATOM   7240 C  CB  . SER A 1 924  ? 44.754 65.137  -25.204 1.00 10.72 ? 924  SER A CB  1 
ATOM   7241 O  OG  . SER A 1 924  ? 43.372 65.511  -25.069 1.00 10.11 ? 924  SER A OG  1 
ATOM   7242 N  N   . LEU A 1 925  ? 43.861 65.596  -22.093 1.00 9.02  ? 925  LEU A N   1 
ATOM   7243 C  CA  . LEU A 1 925  ? 43.397 66.544  -21.070 1.00 9.69  ? 925  LEU A CA  1 
ATOM   7244 C  C   . LEU A 1 925  ? 44.126 66.380  -19.722 1.00 9.26  ? 925  LEU A C   1 
ATOM   7245 O  O   . LEU A 1 925  ? 44.531 67.373  -19.078 1.00 9.17  ? 925  LEU A O   1 
ATOM   7246 C  CB  . LEU A 1 925  ? 41.873 66.350  -20.815 1.00 9.49  ? 925  LEU A CB  1 
ATOM   7247 C  CG  . LEU A 1 925  ? 40.945 66.606  -22.028 1.00 11.38 ? 925  LEU A CG  1 
ATOM   7248 C  CD1 . LEU A 1 925  ? 39.491 66.173  -21.689 1.00 9.83  ? 925  LEU A CD1 1 
ATOM   7249 C  CD2 . LEU A 1 925  ? 41.005 68.089  -22.412 1.00 9.07  ? 925  LEU A CD2 1 
ATOM   7250 N  N   . LEU A 1 926  ? 44.252 65.133  -19.274 1.00 6.75  ? 926  LEU A N   1 
ATOM   7251 C  CA  . LEU A 1 926  ? 44.847 64.870  -17.969 1.00 8.60  ? 926  LEU A CA  1 
ATOM   7252 C  C   . LEU A 1 926  ? 46.359 64.836  -17.960 1.00 8.87  ? 926  LEU A C   1 
ATOM   7253 O  O   . LEU A 1 926  ? 46.963 65.244  -16.986 1.00 9.75  ? 926  LEU A O   1 
ATOM   7254 C  CB  . LEU A 1 926  ? 44.324 63.548  -17.406 1.00 6.99  ? 926  LEU A CB  1 
ATOM   7255 C  CG  . LEU A 1 926  ? 42.821 63.534  -17.121 1.00 8.97  ? 926  LEU A CG  1 
ATOM   7256 C  CD1 . LEU A 1 926  ? 42.434 62.166  -16.554 1.00 8.33  ? 926  LEU A CD1 1 
ATOM   7257 C  CD2 . LEU A 1 926  ? 42.483 64.673  -16.133 1.00 10.03 ? 926  LEU A CD2 1 
ATOM   7258 N  N   . ASP A 1 927  ? 46.965 64.335  -19.029 1.00 6.80  ? 927  ASP A N   1 
ATOM   7259 C  CA  . ASP A 1 927  ? 48.417 64.258  -19.061 1.00 8.10  ? 927  ASP A CA  1 
ATOM   7260 C  C   . ASP A 1 927  ? 49.021 64.771  -20.369 1.00 7.24  ? 927  ASP A C   1 
ATOM   7261 O  O   . ASP A 1 927  ? 49.610 64.023  -21.143 1.00 7.14  ? 927  ASP A O   1 
ATOM   7262 C  CB  . ASP A 1 927  ? 48.854 62.815  -18.741 1.00 7.01  ? 927  ASP A CB  1 
ATOM   7263 C  CG  . ASP A 1 927  ? 48.517 62.417  -17.297 1.00 9.51  ? 927  ASP A CG  1 
ATOM   7264 O  OD1 . ASP A 1 927  ? 49.266 62.785  -16.347 1.00 8.48  ? 927  ASP A OD1 1 
ATOM   7265 O  OD2 . ASP A 1 927  ? 47.474 61.741  -17.118 1.00 7.49  ? 927  ASP A OD2 1 
ATOM   7266 N  N   . PRO A 1 928  ? 48.872 66.084  -20.619 1.00 8.55  ? 928  PRO A N   1 
ATOM   7267 C  CA  . PRO A 1 928  ? 49.386 66.751  -21.819 1.00 8.37  ? 928  PRO A CA  1 
ATOM   7268 C  C   . PRO A 1 928  ? 50.904 66.781  -21.783 1.00 8.75  ? 928  PRO A C   1 
ATOM   7269 O  O   . PRO A 1 928  ? 51.516 66.472  -20.755 1.00 8.46  ? 928  PRO A O   1 
ATOM   7270 C  CB  . PRO A 1 928  ? 48.819 68.173  -21.701 1.00 8.44  ? 928  PRO A CB  1 
ATOM   7271 C  CG  . PRO A 1 928  ? 48.916 68.412  -20.234 1.00 10.16 ? 928  PRO A CG  1 
ATOM   7272 C  CD  . PRO A 1 928  ? 48.390 67.076  -19.642 1.00 8.60  ? 928  PRO A CD  1 
ATOM   7273 N  N   . LEU A 1 929  ? 51.514 67.156  -22.909 1.00 8.94  ? 929  LEU A N   1 
ATOM   7274 C  CA  . LEU A 1 929  ? 52.968 67.309  -22.951 1.00 9.68  ? 929  LEU A CA  1 
ATOM   7275 C  C   . LEU A 1 929  ? 53.281 68.452  -21.988 1.00 9.31  ? 929  LEU A C   1 
ATOM   7276 O  O   . LEU A 1 929  ? 52.479 69.354  -21.819 1.00 9.70  ? 929  LEU A O   1 
ATOM   7277 C  CB  . LEU A 1 929  ? 53.449 67.728  -24.350 1.00 9.42  ? 929  LEU A CB  1 
ATOM   7278 C  CG  . LEU A 1 929  ? 53.179 66.743  -25.492 1.00 10.87 ? 929  LEU A CG  1 
ATOM   7279 C  CD1 . LEU A 1 929  ? 53.677 67.360  -26.809 1.00 10.10 ? 929  LEU A CD1 1 
ATOM   7280 C  CD2 . LEU A 1 929  ? 53.929 65.415  -25.216 1.00 9.79  ? 929  LEU A CD2 1 
ATOM   7281 N  N   . ASP A 1 930  ? 54.435 68.405  -21.335 1.00 10.90 ? 930  ASP A N   1 
ATOM   7282 C  CA  . ASP A 1 930  ? 54.841 69.506  -20.462 1.00 10.92 ? 930  ASP A CA  1 
ATOM   7283 C  C   . ASP A 1 930  ? 55.761 70.371  -21.324 1.00 10.79 ? 930  ASP A C   1 
ATOM   7284 O  O   . ASP A 1 930  ? 56.544 69.851  -22.152 1.00 11.51 ? 930  ASP A O   1 
ATOM   7285 C  CB  . ASP A 1 930  ? 55.590 68.962  -19.241 1.00 9.87  ? 930  ASP A CB  1 
ATOM   7286 C  CG  . ASP A 1 930  ? 54.766 67.929  -18.498 1.00 14.26 ? 930  ASP A CG  1 
ATOM   7287 O  OD1 . ASP A 1 930  ? 53.708 68.327  -17.921 1.00 10.38 ? 930  ASP A OD1 1 
ATOM   7288 O  OD2 . ASP A 1 930  ? 55.169 66.727  -18.528 1.00 11.19 ? 930  ASP A OD2 1 
ATOM   7289 N  N   . LYS A 1 931  ? 55.685 71.680  -21.141 1.00 10.71 ? 931  LYS A N   1 
ATOM   7290 C  CA  . LYS A 1 931  ? 56.493 72.580  -21.948 1.00 10.62 ? 931  LYS A CA  1 
ATOM   7291 C  C   . LYS A 1 931  ? 57.444 73.393  -21.100 1.00 10.96 ? 931  LYS A C   1 
ATOM   7292 O  O   . LYS A 1 931  ? 57.036 73.974  -20.078 1.00 9.87  ? 931  LYS A O   1 
ATOM   7293 C  CB  . LYS A 1 931  ? 55.577 73.536  -22.745 1.00 11.73 ? 931  LYS A CB  1 
ATOM   7294 C  CG  . LYS A 1 931  ? 54.525 72.852  -23.666 1.00 11.02 ? 931  LYS A CG  1 
ATOM   7295 C  CD  . LYS A 1 931  ? 53.670 73.888  -24.432 1.00 12.70 ? 931  LYS A CD  1 
ATOM   7296 C  CE  . LYS A 1 931  ? 52.936 74.792  -23.465 1.00 15.28 ? 931  LYS A CE  1 
ATOM   7297 N  NZ  . LYS A 1 931  ? 51.914 75.638  -24.071 1.00 16.36 ? 931  LYS A NZ  1 
ATOM   7298 N  N   . PHE A 1 932  ? 58.710 73.455  -21.529 1.00 10.19 ? 932  PHE A N   1 
ATOM   7299 C  CA  . PHE A 1 932  ? 59.728 74.212  -20.799 1.00 9.47  ? 932  PHE A CA  1 
ATOM   7300 C  C   . PHE A 1 932  ? 60.455 75.226  -21.690 1.00 9.46  ? 932  PHE A C   1 
ATOM   7301 O  O   . PHE A 1 932  ? 60.888 74.893  -22.777 1.00 9.05  ? 932  PHE A O   1 
ATOM   7302 C  CB  . PHE A 1 932  ? 60.805 73.297  -20.224 1.00 9.24  ? 932  PHE A CB  1 
ATOM   7303 C  CG  . PHE A 1 932  ? 60.288 72.195  -19.385 1.00 8.45  ? 932  PHE A CG  1 
ATOM   7304 C  CD1 . PHE A 1 932  ? 59.715 71.060  -19.972 1.00 9.41  ? 932  PHE A CD1 1 
ATOM   7305 C  CD2 . PHE A 1 932  ? 60.422 72.262  -18.001 1.00 9.43  ? 932  PHE A CD2 1 
ATOM   7306 C  CE1 . PHE A 1 932  ? 59.274 69.974  -19.188 1.00 9.07  ? 932  PHE A CE1 1 
ATOM   7307 C  CE2 . PHE A 1 932  ? 59.999 71.200  -17.205 1.00 10.87 ? 932  PHE A CE2 1 
ATOM   7308 C  CZ  . PHE A 1 932  ? 59.419 70.041  -17.818 1.00 11.32 ? 932  PHE A CZ  1 
ATOM   7309 N  N   . ILE A 1 933  ? 60.605 76.447  -21.204 1.00 9.57  ? 933  ILE A N   1 
ATOM   7310 C  CA  . ILE A 1 933  ? 61.297 77.503  -21.954 1.00 10.12 ? 933  ILE A CA  1 
ATOM   7311 C  C   . ILE A 1 933  ? 62.642 77.718  -21.276 1.00 11.66 ? 933  ILE A C   1 
ATOM   7312 O  O   . ILE A 1 933  ? 62.689 77.965  -20.067 1.00 11.02 ? 933  ILE A O   1 
ATOM   7313 C  CB  . ILE A 1 933  ? 60.539 78.837  -21.864 1.00 9.96  ? 933  ILE A CB  1 
ATOM   7314 C  CG1 . ILE A 1 933  ? 59.071 78.644  -22.294 1.00 9.47  ? 933  ILE A CG1 1 
ATOM   7315 C  CG2 . ILE A 1 933  ? 61.251 79.887  -22.682 1.00 7.19  ? 933  ILE A CG2 1 
ATOM   7316 C  CD1 . ILE A 1 933  ? 58.239 79.929  -22.134 1.00 8.58  ? 933  ILE A CD1 1 
ATOM   7317 N  N   . PHE A 1 934  ? 63.730 77.614  -22.041 1.00 11.29 ? 934  PHE A N   1 
ATOM   7318 C  CA  . PHE A 1 934  ? 65.047 77.818  -21.468 1.00 12.76 ? 934  PHE A CA  1 
ATOM   7319 C  C   . PHE A 1 934  ? 65.172 79.302  -21.005 1.00 13.83 ? 934  PHE A C   1 
ATOM   7320 O  O   . PHE A 1 934  ? 64.853 80.241  -21.744 1.00 13.12 ? 934  PHE A O   1 
ATOM   7321 C  CB  . PHE A 1 934  ? 66.129 77.459  -22.481 1.00 14.20 ? 934  PHE A CB  1 
ATOM   7322 C  CG  . PHE A 1 934  ? 67.495 77.475  -21.887 1.00 15.64 ? 934  PHE A CG  1 
ATOM   7323 C  CD1 . PHE A 1 934  ? 67.895 76.458  -21.024 1.00 15.38 ? 934  PHE A CD1 1 
ATOM   7324 C  CD2 . PHE A 1 934  ? 68.345 78.565  -22.112 1.00 15.55 ? 934  PHE A CD2 1 
ATOM   7325 C  CE1 . PHE A 1 934  ? 69.142 76.519  -20.372 1.00 17.76 ? 934  PHE A CE1 1 
ATOM   7326 C  CE2 . PHE A 1 934  ? 69.593 78.655  -21.486 1.00 15.87 ? 934  PHE A CE2 1 
ATOM   7327 C  CZ  . PHE A 1 934  ? 69.997 77.624  -20.605 1.00 17.35 ? 934  PHE A CZ  1 
ATOM   7328 N  N   . ALA A 1 935  ? 65.641 79.514  -19.782 1.00 15.85 ? 935  ALA A N   1 
ATOM   7329 C  CA  . ALA A 1 935  ? 65.666 80.869  -19.245 1.00 18.30 ? 935  ALA A CA  1 
ATOM   7330 C  C   . ALA A 1 935  ? 66.817 81.805  -19.617 1.00 20.03 ? 935  ALA A C   1 
ATOM   7331 O  O   . ALA A 1 935  ? 66.588 83.006  -19.754 1.00 22.67 ? 935  ALA A O   1 
ATOM   7332 C  CB  . ALA A 1 935  ? 65.535 80.813  -17.742 1.00 18.82 ? 935  ALA A CB  1 
ATOM   7333 N  N   . GLU A 1 936  ? 68.033 81.284  -19.764 1.00 18.58 ? 936  GLU A N   1 
ATOM   7334 C  CA  . GLU A 1 936  ? 69.200 82.120  -20.099 1.00 19.87 ? 936  GLU A CA  1 
ATOM   7335 C  C   . GLU A 1 936  ? 69.261 82.318  -21.628 1.00 19.15 ? 936  GLU A C   1 
ATOM   7336 O  O   . GLU A 1 936  ? 68.483 81.704  -22.376 1.00 17.52 ? 936  GLU A O   1 
ATOM   7337 C  CB  . GLU A 1 936  ? 70.494 81.429  -19.642 1.00 22.18 ? 936  GLU A CB  1 
ATOM   7338 C  CG  . GLU A 1 936  ? 70.608 81.173  -18.116 1.00 25.90 ? 936  GLU A CG  1 
ATOM   7339 C  CD  . GLU A 1 936  ? 71.674 80.095  -17.762 1.00 28.84 ? 936  GLU A CD  1 
ATOM   7340 O  OE1 . GLU A 1 936  ? 71.395 78.873  -17.938 1.00 29.65 ? 936  GLU A OE1 1 
ATOM   7341 O  OE2 . GLU A 1 936  ? 72.799 80.462  -17.318 1.00 29.87 ? 936  GLU A OE2 1 
ATOM   7342 N  N   . ASN A 1 937  ? 70.194 83.140  -22.102 1.00 18.20 ? 937  ASN A N   1 
ATOM   7343 C  CA  . ASN A 1 937  ? 70.262 83.347  -23.538 1.00 19.62 ? 937  ASN A CA  1 
ATOM   7344 C  C   . ASN A 1 937  ? 70.828 82.171  -24.273 1.00 19.35 ? 937  ASN A C   1 
ATOM   7345 O  O   . ASN A 1 937  ? 70.420 81.899  -25.412 1.00 20.25 ? 937  ASN A O   1 
ATOM   7346 C  CB  . ASN A 1 937  ? 71.073 84.585  -23.877 1.00 19.87 ? 937  ASN A CB  1 
ATOM   7347 C  CG  . ASN A 1 937  ? 70.450 85.829  -23.308 1.00 21.16 ? 937  ASN A CG  1 
ATOM   7348 O  OD1 . ASN A 1 937  ? 69.233 85.908  -23.136 1.00 21.42 ? 937  ASN A OD1 1 
ATOM   7349 N  ND2 . ASN A 1 937  ? 71.266 86.801  -23.018 1.00 22.22 ? 937  ASN A ND2 1 
ATOM   7350 N  N   . GLU A 1 938  ? 71.766 81.469  -23.651 1.00 18.95 ? 938  GLU A N   1 
ATOM   7351 C  CA  . GLU A 1 938  ? 72.357 80.331  -24.336 1.00 21.15 ? 938  GLU A CA  1 
ATOM   7352 C  C   . GLU A 1 938  ? 72.419 79.067  -23.488 1.00 20.40 ? 938  GLU A C   1 
ATOM   7353 O  O   . GLU A 1 938  ? 72.797 79.095  -22.307 1.00 19.50 ? 938  GLU A O   1 
ATOM   7354 C  CB  . GLU A 1 938  ? 73.757 80.680  -24.848 1.00 24.82 ? 938  GLU A CB  1 
ATOM   7355 C  CG  . GLU A 1 938  ? 74.485 79.462  -25.384 1.00 30.93 ? 938  GLU A CG  1 
ATOM   7356 C  CD  . GLU A 1 938  ? 75.742 79.790  -26.176 1.00 35.18 ? 938  GLU A CD  1 
ATOM   7357 O  OE1 . GLU A 1 938  ? 76.548 80.638  -25.711 1.00 37.54 ? 938  GLU A OE1 1 
ATOM   7358 O  OE2 . GLU A 1 938  ? 75.923 79.175  -27.259 1.00 38.05 ? 938  GLU A OE2 1 
ATOM   7359 N  N   . TRP A 1 939  ? 72.059 77.953  -24.112 1.00 19.40 ? 939  TRP A N   1 
ATOM   7360 C  CA  . TRP A 1 939  ? 72.059 76.668  -23.431 1.00 19.57 ? 939  TRP A CA  1 
ATOM   7361 C  C   . TRP A 1 939  ? 73.242 75.868  -23.948 1.00 20.00 ? 939  TRP A C   1 
ATOM   7362 O  O   . TRP A 1 939  ? 73.126 75.196  -24.964 1.00 21.31 ? 939  TRP A O   1 
ATOM   7363 C  CB  . TRP A 1 939  ? 70.751 75.914  -23.718 1.00 17.43 ? 939  TRP A CB  1 
ATOM   7364 C  CG  . TRP A 1 939  ? 70.666 74.542  -23.047 1.00 15.85 ? 939  TRP A CG  1 
ATOM   7365 C  CD1 . TRP A 1 939  ? 71.587 73.977  -22.201 1.00 14.90 ? 939  TRP A CD1 1 
ATOM   7366 C  CD2 . TRP A 1 939  ? 69.598 73.586  -23.175 1.00 14.25 ? 939  TRP A CD2 1 
ATOM   7367 N  NE1 . TRP A 1 939  ? 71.155 72.726  -21.793 1.00 14.03 ? 939  TRP A NE1 1 
ATOM   7368 C  CE2 . TRP A 1 939  ? 69.939 72.465  -22.377 1.00 14.08 ? 939  TRP A CE2 1 
ATOM   7369 C  CE3 . TRP A 1 939  ? 68.387 73.568  -23.886 1.00 12.40 ? 939  TRP A CE3 1 
ATOM   7370 C  CZ2 . TRP A 1 939  ? 69.108 71.337  -22.270 1.00 13.33 ? 939  TRP A CZ2 1 
ATOM   7371 C  CZ3 . TRP A 1 939  ? 67.556 72.441  -23.774 1.00 13.24 ? 939  TRP A CZ3 1 
ATOM   7372 C  CH2 . TRP A 1 939  ? 67.927 71.344  -22.970 1.00 12.41 ? 939  TRP A CH2 1 
ATOM   7373 N  N   . ILE A 1 940  ? 74.367 75.932  -23.240 1.00 20.18 ? 940  ILE A N   1 
ATOM   7374 C  CA  . ILE A 1 940  ? 75.587 75.218  -23.640 1.00 20.77 ? 940  ILE A CA  1 
ATOM   7375 C  C   . ILE A 1 940  ? 75.518 73.709  -23.349 1.00 19.99 ? 940  ILE A C   1 
ATOM   7376 O  O   . ILE A 1 940  ? 75.250 73.312  -22.230 1.00 20.71 ? 940  ILE A O   1 
ATOM   7377 C  CB  . ILE A 1 940  ? 76.807 75.817  -22.896 1.00 22.32 ? 940  ILE A CB  1 
ATOM   7378 C  CG1 . ILE A 1 940  ? 76.944 77.295  -23.260 1.00 24.09 ? 940  ILE A CG1 1 
ATOM   7379 C  CG2 . ILE A 1 940  ? 78.077 75.086  -23.284 1.00 22.82 ? 940  ILE A CG2 1 
ATOM   7380 C  CD1 . ILE A 1 940  ? 77.523 78.154  -22.168 1.00 27.36 ? 940  ILE A CD1 1 
ATOM   7381 N  N   . GLY A 1 941  ? 75.762 72.881  -24.354 1.00 19.98 ? 941  GLY A N   1 
ATOM   7382 C  CA  . GLY A 1 941  ? 75.740 71.442  -24.145 1.00 20.41 ? 941  GLY A CA  1 
ATOM   7383 C  C   . GLY A 1 941  ? 74.380 70.804  -24.410 1.00 20.44 ? 941  GLY A C   1 
ATOM   7384 O  O   . GLY A 1 941  ? 74.229 69.588  -24.259 1.00 20.07 ? 941  GLY A O   1 
ATOM   7385 N  N   . ALA A 1 942  ? 73.410 71.626  -24.819 1.00 19.58 ? 942  ALA A N   1 
ATOM   7386 C  CA  . ALA A 1 942  ? 72.049 71.176  -25.117 1.00 19.73 ? 942  ALA A CA  1 
ATOM   7387 C  C   . ALA A 1 942  ? 71.991 69.974  -26.046 1.00 19.61 ? 942  ALA A C   1 
ATOM   7388 O  O   . ALA A 1 942  ? 72.735 69.894  -27.010 1.00 20.75 ? 942  ALA A O   1 
ATOM   7389 C  CB  . ALA A 1 942  ? 71.232 72.339  -25.720 1.00 18.32 ? 942  ALA A CB  1 
ATOM   7390 N  N   . GLN A 1 943  ? 71.093 69.043  -25.759 1.00 18.97 ? 943  GLN A N   1 
ATOM   7391 C  CA  . GLN A 1 943  ? 70.913 67.856  -26.576 1.00 18.08 ? 943  GLN A CA  1 
ATOM   7392 C  C   . GLN A 1 943  ? 69.491 67.886  -27.085 1.00 17.54 ? 943  GLN A C   1 
ATOM   7393 O  O   . GLN A 1 943  ? 68.616 68.497  -26.472 1.00 17.18 ? 943  GLN A O   1 
ATOM   7394 C  CB  . GLN A 1 943  ? 71.158 66.611  -25.749 1.00 19.33 ? 943  GLN A CB  1 
ATOM   7395 C  CG  . GLN A 1 943  ? 72.556 66.581  -25.139 1.00 23.95 ? 943  GLN A CG  1 
ATOM   7396 C  CD  . GLN A 1 943  ? 72.804 65.322  -24.283 1.00 27.56 ? 943  GLN A CD  1 
ATOM   7397 O  OE1 . GLN A 1 943  ? 71.892 64.832  -23.589 1.00 29.02 ? 943  GLN A OE1 1 
ATOM   7398 N  NE2 . GLN A 1 943  ? 74.040 64.815  -24.312 1.00 26.44 ? 943  GLN A NE2 1 
ATOM   7399 N  N   . GLY A 1 944  ? 69.234 67.226  -28.201 1.00 16.26 ? 944  GLY A N   1 
ATOM   7400 C  CA  . GLY A 1 944  ? 67.900 67.295  -28.762 1.00 16.17 ? 944  GLY A CA  1 
ATOM   7401 C  C   . GLY A 1 944  ? 66.838 66.299  -28.342 1.00 16.96 ? 944  GLY A C   1 
ATOM   7402 O  O   . GLY A 1 944  ? 65.670 66.500  -28.671 1.00 17.29 ? 944  GLY A O   1 
ATOM   7403 N  N   . GLN A 1 945  ? 67.206 65.247  -27.613 1.00 15.33 ? 945  GLN A N   1 
ATOM   7404 C  CA  . GLN A 1 945  ? 66.208 64.253  -27.277 1.00 16.13 ? 945  GLN A CA  1 
ATOM   7405 C  C   . GLN A 1 945  ? 66.650 63.321  -26.162 1.00 15.33 ? 945  GLN A C   1 
ATOM   7406 O  O   . GLN A 1 945  ? 67.838 63.068  -25.972 1.00 14.93 ? 945  GLN A O   1 
ATOM   7407 C  CB  . GLN A 1 945  ? 65.906 63.411  -28.516 1.00 17.64 ? 945  GLN A CB  1 
ATOM   7408 C  CG  . GLN A 1 945  ? 64.735 62.425  -28.403 1.00 21.27 ? 945  GLN A CG  1 
ATOM   7409 C  CD  . GLN A 1 945  ? 64.588 61.552  -29.677 1.00 23.20 ? 945  GLN A CD  1 
ATOM   7410 O  OE1 . GLN A 1 945  ? 65.333 60.588  -29.879 1.00 24.22 ? 945  GLN A OE1 1 
ATOM   7411 N  NE2 . GLN A 1 945  ? 63.640 61.914  -30.537 1.00 23.11 ? 945  GLN A NE2 1 
ATOM   7412 N  N   . PHE A 1 946  ? 65.670 62.814  -25.434 1.00 13.78 ? 946  PHE A N   1 
ATOM   7413 C  CA  . PHE A 1 946  ? 65.913 61.864  -24.374 1.00 12.45 ? 946  PHE A CA  1 
ATOM   7414 C  C   . PHE A 1 946  ? 64.791 60.855  -24.457 1.00 12.68 ? 946  PHE A C   1 
ATOM   7415 O  O   . PHE A 1 946  ? 63.627 61.231  -24.590 1.00 12.19 ? 946  PHE A O   1 
ATOM   7416 C  CB  . PHE A 1 946  ? 65.876 62.538  -22.987 1.00 12.89 ? 946  PHE A CB  1 
ATOM   7417 C  CG  . PHE A 1 946  ? 65.747 61.552  -21.837 1.00 12.75 ? 946  PHE A CG  1 
ATOM   7418 C  CD1 . PHE A 1 946  ? 66.815 60.713  -21.495 1.00 14.17 ? 946  PHE A CD1 1 
ATOM   7419 C  CD2 . PHE A 1 946  ? 64.525 61.397  -21.169 1.00 13.12 ? 946  PHE A CD2 1 
ATOM   7420 C  CE1 . PHE A 1 946  ? 66.672 59.698  -20.493 1.00 14.11 ? 946  PHE A CE1 1 
ATOM   7421 C  CE2 . PHE A 1 946  ? 64.357 60.408  -20.182 1.00 14.40 ? 946  PHE A CE2 1 
ATOM   7422 C  CZ  . PHE A 1 946  ? 65.440 59.544  -19.843 1.00 14.10 ? 946  PHE A CZ  1 
ATOM   7423 N  N   . GLY A 1 947  ? 65.142 59.577  -24.384 1.00 12.51 ? 947  GLY A N   1 
ATOM   7424 C  CA  . GLY A 1 947  ? 64.131 58.539  -24.377 1.00 11.30 ? 947  GLY A CA  1 
ATOM   7425 C  C   . GLY A 1 947  ? 63.817 57.958  -25.728 1.00 12.11 ? 947  GLY A C   1 
ATOM   7426 O  O   . GLY A 1 947  ? 62.894 57.187  -25.833 1.00 11.96 ? 947  GLY A O   1 
ATOM   7427 N  N   . GLY A 1 948  ? 64.591 58.312  -26.756 1.00 12.69 ? 948  GLY A N   1 
ATOM   7428 C  CA  . GLY A 1 948  ? 64.334 57.794  -28.087 1.00 13.69 ? 948  GLY A CA  1 
ATOM   7429 C  C   . GLY A 1 948  ? 64.356 56.282  -28.127 1.00 14.58 ? 948  GLY A C   1 
ATOM   7430 O  O   . GLY A 1 948  ? 63.771 55.690  -29.009 1.00 15.21 ? 948  GLY A O   1 
ATOM   7431 N  N   . ASP A 1 949  ? 65.018 55.647  -27.165 1.00 16.58 ? 949  ASP A N   1 
ATOM   7432 C  CA  . ASP A 1 949  ? 65.084 54.179  -27.134 1.00 19.24 ? 949  ASP A CA  1 
ATOM   7433 C  C   . ASP A 1 949  ? 64.089 53.545  -26.156 1.00 19.40 ? 949  ASP A C   1 
ATOM   7434 O  O   . ASP A 1 949  ? 64.092 52.327  -25.968 1.00 18.91 ? 949  ASP A O   1 
ATOM   7435 C  CB  . ASP A 1 949  ? 66.509 53.729  -26.777 1.00 22.02 ? 949  ASP A CB  1 
ATOM   7436 C  CG  . ASP A 1 949  ? 66.971 54.267  -25.422 1.00 26.52 ? 949  ASP A CG  1 
ATOM   7437 O  OD1 . ASP A 1 949  ? 66.306 55.182  -24.830 1.00 28.31 ? 949  ASP A OD1 1 
ATOM   7438 O  OD2 . ASP A 1 949  ? 68.020 53.779  -24.948 1.00 28.91 ? 949  ASP A OD2 1 
ATOM   7439 N  N   . HIS A 1 950  ? 63.255 54.369  -25.516 1.00 17.73 ? 950  HIS A N   1 
ATOM   7440 C  CA  . HIS A 1 950  ? 62.258 53.858  -24.577 1.00 16.10 ? 950  HIS A CA  1 
ATOM   7441 C  C   . HIS A 1 950  ? 61.221 53.112  -25.394 1.00 14.87 ? 950  HIS A C   1 
ATOM   7442 O  O   . HIS A 1 950  ? 60.849 53.558  -26.457 1.00 14.93 ? 950  HIS A O   1 
ATOM   7443 C  CB  . HIS A 1 950  ? 61.565 55.010  -23.845 1.00 16.08 ? 950  HIS A CB  1 
ATOM   7444 C  CG  . HIS A 1 950  ? 62.425 55.675  -22.813 1.00 14.16 ? 950  HIS A CG  1 
ATOM   7445 N  ND1 . HIS A 1 950  ? 62.062 56.847  -22.189 1.00 13.31 ? 950  HIS A ND1 1 
ATOM   7446 C  CD2 . HIS A 1 950  ? 63.663 55.374  -22.362 1.00 14.28 ? 950  HIS A CD2 1 
ATOM   7447 C  CE1 . HIS A 1 950  ? 63.048 57.245  -21.405 1.00 13.41 ? 950  HIS A CE1 1 
ATOM   7448 N  NE2 . HIS A 1 950  ? 64.034 56.369  -21.495 1.00 15.04 ? 950  HIS A NE2 1 
ATOM   7449 N  N   . PRO A 1 951  ? 60.772 51.957  -24.918 1.00 14.74 ? 951  PRO A N   1 
ATOM   7450 C  CA  . PRO A 1 951  ? 59.764 51.159  -25.623 1.00 15.08 ? 951  PRO A CA  1 
ATOM   7451 C  C   . PRO A 1 951  ? 58.469 51.962  -25.729 1.00 14.30 ? 951  PRO A C   1 
ATOM   7452 O  O   . PRO A 1 951  ? 58.083 52.606  -24.767 1.00 13.70 ? 951  PRO A O   1 
ATOM   7453 C  CB  . PRO A 1 951  ? 59.573 49.949  -24.709 1.00 15.96 ? 951  PRO A CB  1 
ATOM   7454 C  CG  . PRO A 1 951  ? 60.888 49.835  -23.994 1.00 16.47 ? 951  PRO A CG  1 
ATOM   7455 C  CD  . PRO A 1 951  ? 61.300 51.247  -23.733 1.00 15.66 ? 951  PRO A CD  1 
ATOM   7456 N  N   . SER A 1 952  ? 57.813 51.916  -26.888 1.00 13.94 ? 952  SER A N   1 
ATOM   7457 C  CA  . SER A 1 952  ? 56.548 52.608  -27.116 1.00 13.92 ? 952  SER A CA  1 
ATOM   7458 C  C   . SER A 1 952  ? 55.481 51.545  -26.944 1.00 15.92 ? 952  SER A C   1 
ATOM   7459 O  O   . SER A 1 952  ? 55.193 50.763  -27.881 1.00 17.24 ? 952  SER A O   1 
ATOM   7460 C  CB  . SER A 1 952  ? 56.497 53.194  -28.529 1.00 14.17 ? 952  SER A CB  1 
ATOM   7461 O  OG  . SER A 1 952  ? 55.350 54.008  -28.693 1.00 13.32 ? 952  SER A OG  1 
ATOM   7462 N  N   . ALA A 1 953  ? 54.916 51.504  -25.734 1.00 15.17 ? 953  ALA A N   1 
ATOM   7463 C  CA  . ALA A 1 953  ? 53.924 50.504  -25.341 1.00 14.31 ? 953  ALA A CA  1 
ATOM   7464 C  C   . ALA A 1 953  ? 52.579 50.623  -26.012 1.00 14.23 ? 953  ALA A C   1 
ATOM   7465 O  O   . ALA A 1 953  ? 52.201 51.709  -26.469 1.00 13.11 ? 953  ALA A O   1 
ATOM   7466 C  CB  . ALA A 1 953  ? 53.725 50.564  -23.819 1.00 14.00 ? 953  ALA A CB  1 
ATOM   7467 N  N   . ARG A 1 954  ? 51.830 49.515  -25.991 1.00 13.40 ? 954  ARG A N   1 
ATOM   7468 C  CA  . ARG A 1 954  ? 50.492 49.471  -26.563 1.00 13.93 ? 954  ARG A CA  1 
ATOM   7469 C  C   . ARG A 1 954  ? 49.657 50.574  -25.921 1.00 12.31 ? 954  ARG A C   1 
ATOM   7470 O  O   . ARG A 1 954  ? 49.750 50.831  -24.705 1.00 9.93  ? 954  ARG A O   1 
ATOM   7471 C  CB  . ARG A 1 954  ? 49.819 48.121  -26.325 1.00 16.85 ? 954  ARG A CB  1 
ATOM   7472 C  CG  . ARG A 1 954  ? 48.411 48.115  -26.955 1.00 23.34 ? 954  ARG A CG  1 
ATOM   7473 C  CD  . ARG A 1 954  ? 48.050 46.782  -27.610 1.00 26.78 ? 954  ARG A CD  1 
ATOM   7474 N  NE  . ARG A 1 954  ? 47.544 45.790  -26.665 1.00 31.75 ? 954  ARG A NE  1 
ATOM   7475 C  CZ  . ARG A 1 954  ? 46.362 45.871  -26.061 1.00 34.22 ? 954  ARG A CZ  1 
ATOM   7476 N  NH1 . ARG A 1 954  ? 45.577 46.918  -26.311 1.00 37.17 ? 954  ARG A NH1 1 
ATOM   7477 N  NH2 . ARG A 1 954  ? 45.944 44.904  -25.236 1.00 33.91 ? 954  ARG A NH2 1 
ATOM   7478 N  N   . GLU A 1 955  ? 48.808 51.188  -26.740 1.00 10.97 ? 955  GLU A N   1 
ATOM   7479 C  CA  . GLU A 1 955  ? 48.020 52.352  -26.325 1.00 12.41 ? 955  GLU A CA  1 
ATOM   7480 C  C   . GLU A 1 955  ? 47.140 52.246  -25.090 1.00 10.83 ? 955  GLU A C   1 
ATOM   7481 O  O   . GLU A 1 955  ? 46.824 53.278  -24.517 1.00 9.98  ? 955  GLU A O   1 
ATOM   7482 C  CB  . GLU A 1 955  ? 47.150 52.832  -27.480 1.00 13.68 ? 955  GLU A CB  1 
ATOM   7483 C  CG  . GLU A 1 955  ? 45.984 51.892  -27.739 1.00 16.53 ? 955  GLU A CG  1 
ATOM   7484 C  CD  . GLU A 1 955  ? 45.136 52.291  -28.944 1.00 18.39 ? 955  GLU A CD  1 
ATOM   7485 O  OE1 . GLU A 1 955  ? 44.994 53.487  -29.213 1.00 20.03 ? 955  GLU A OE1 1 
ATOM   7486 O  OE2 . GLU A 1 955  ? 44.593 51.394  -29.618 1.00 22.26 ? 955  GLU A OE2 1 
ATOM   7487 N  N   . ASP A 1 956  ? 46.722 51.041  -24.695 1.00 10.42 ? 956  ASP A N   1 
ATOM   7488 C  CA  . ASP A 1 956  ? 45.855 50.915  -23.500 1.00 11.29 ? 956  ASP A CA  1 
ATOM   7489 C  C   . ASP A 1 956  ? 46.657 50.739  -22.207 1.00 11.20 ? 956  ASP A C   1 
ATOM   7490 O  O   . ASP A 1 956  ? 46.094 50.622  -21.110 1.00 12.08 ? 956  ASP A O   1 
ATOM   7491 C  CB  . ASP A 1 956  ? 44.826 49.760  -23.647 1.00 11.41 ? 956  ASP A CB  1 
ATOM   7492 C  CG  . ASP A 1 956  ? 45.479 48.394  -23.994 1.00 13.65 ? 956  ASP A CG  1 
ATOM   7493 O  OD1 . ASP A 1 956  ? 46.713 48.346  -24.152 1.00 12.68 ? 956  ASP A OD1 1 
ATOM   7494 O  OD2 . ASP A 1 956  ? 44.742 47.362  -24.120 1.00 12.74 ? 956  ASP A OD2 1 
ATOM   7495 N  N   . LEU A 1 957  ? 47.973 50.738  -22.330 1.00 10.87 ? 957  LEU A N   1 
ATOM   7496 C  CA  . LEU A 1 957  ? 48.845 50.603  -21.158 1.00 11.04 ? 957  LEU A CA  1 
ATOM   7497 C  C   . LEU A 1 957  ? 49.419 51.940  -20.752 1.00 10.74 ? 957  LEU A C   1 
ATOM   7498 O  O   . LEU A 1 957  ? 49.786 52.737  -21.610 1.00 8.73  ? 957  LEU A O   1 
ATOM   7499 C  CB  . LEU A 1 957  ? 50.005 49.673  -21.480 1.00 11.98 ? 957  LEU A CB  1 
ATOM   7500 C  CG  . LEU A 1 957  ? 50.863 49.197  -20.308 1.00 15.43 ? 957  LEU A CG  1 
ATOM   7501 C  CD1 . LEU A 1 957  ? 50.040 48.248  -19.398 1.00 14.82 ? 957  LEU A CD1 1 
ATOM   7502 C  CD2 . LEU A 1 957  ? 52.118 48.494  -20.862 1.00 15.32 ? 957  LEU A CD2 1 
ATOM   7503 N  N   . ASP A 1 958  ? 49.524 52.176  -19.444 1.00 10.33 ? 958  ASP A N   1 
ATOM   7504 C  CA  . ASP A 1 958  ? 50.134 53.415  -18.949 1.00 10.43 ? 958  ASP A CA  1 
ATOM   7505 C  C   . ASP A 1 958  ? 51.081 53.130  -17.769 1.00 10.78 ? 958  ASP A C   1 
ATOM   7506 O  O   . ASP A 1 958  ? 50.867 52.172  -17.025 1.00 11.85 ? 958  ASP A O   1 
ATOM   7507 C  CB  . ASP A 1 958  ? 49.040 54.405  -18.475 1.00 9.59  ? 958  ASP A CB  1 
ATOM   7508 C  CG  . ASP A 1 958  ? 49.576 55.831  -18.280 1.00 10.36 ? 958  ASP A CG  1 
ATOM   7509 O  OD1 . ASP A 1 958  ? 50.682 56.160  -18.774 1.00 7.51  ? 958  ASP A OD1 1 
ATOM   7510 O  OD2 . ASP A 1 958  ? 48.873 56.627  -17.624 1.00 10.69 ? 958  ASP A OD2 1 
ATOM   7511 N  N   . VAL A 1 959  ? 52.157 53.913  -17.646 1.00 10.10 ? 959  VAL A N   1 
ATOM   7512 C  CA  . VAL A 1 959  ? 53.045 53.820  -16.477 1.00 10.59 ? 959  VAL A CA  1 
ATOM   7513 C  C   . VAL A 1 959  ? 52.455 54.940  -15.598 1.00 10.01 ? 959  VAL A C   1 
ATOM   7514 O  O   . VAL A 1 959  ? 52.877 56.097  -15.669 1.00 9.76  ? 959  VAL A O   1 
ATOM   7515 C  CB  . VAL A 1 959  ? 54.540 54.133  -16.826 1.00 12.04 ? 959  VAL A CB  1 
ATOM   7516 C  CG1 . VAL A 1 959  ? 55.367 54.411  -15.534 1.00 10.53 ? 959  VAL A CG1 1 
ATOM   7517 C  CG2 . VAL A 1 959  ? 55.161 52.899  -17.561 1.00 12.26 ? 959  VAL A CG2 1 
ATOM   7518 N  N   . SER A 1 960  ? 51.435 54.601  -14.816 1.00 9.04  ? 960  SER A N   1 
ATOM   7519 C  CA  . SER A 1 960  ? 50.749 55.572  -13.963 1.00 8.05  ? 960  SER A CA  1 
ATOM   7520 C  C   . SER A 1 960  ? 51.677 56.310  -12.987 1.00 8.86  ? 960  SER A C   1 
ATOM   7521 O  O   . SER A 1 960  ? 51.495 57.516  -12.719 1.00 8.20  ? 960  SER A O   1 
ATOM   7522 C  CB  . SER A 1 960  ? 49.642 54.856  -13.175 1.00 7.82  ? 960  SER A CB  1 
ATOM   7523 O  OG  . SER A 1 960  ? 48.826 54.115  -14.082 1.00 8.15  ? 960  SER A OG  1 
ATOM   7524 N  N   . VAL A 1 961  ? 52.654 55.576  -12.462 1.00 9.08  ? 961  VAL A N   1 
ATOM   7525 C  CA  . VAL A 1 961  ? 53.627 56.117  -11.499 1.00 8.31  ? 961  VAL A CA  1 
ATOM   7526 C  C   . VAL A 1 961  ? 55.032 55.572  -11.776 1.00 9.63  ? 961  VAL A C   1 
ATOM   7527 O  O   . VAL A 1 961  ? 55.209 54.365  -12.029 1.00 8.16  ? 961  VAL A O   1 
ATOM   7528 C  CB  . VAL A 1 961  ? 53.305 55.682  -10.000 1.00 10.24 ? 961  VAL A CB  1 
ATOM   7529 C  CG1 . VAL A 1 961  ? 54.414 56.209  -9.039  1.00 9.73  ? 961  VAL A CG1 1 
ATOM   7530 C  CG2 . VAL A 1 961  ? 51.917 56.233  -9.530  1.00 7.16  ? 961  VAL A CG2 1 
ATOM   7531 N  N   . MET A 1 962  ? 56.017 56.471  -11.758 1.00 8.77  ? 962  MET A N   1 
ATOM   7532 C  CA  . MET A 1 962  ? 57.397 56.066  -11.831 1.00 9.59  ? 962  MET A CA  1 
ATOM   7533 C  C   . MET A 1 962  ? 57.997 56.838  -10.659 1.00 10.29 ? 962  MET A C   1 
ATOM   7534 O  O   . MET A 1 962  ? 57.974 58.078  -10.637 1.00 10.50 ? 962  MET A O   1 
ATOM   7535 C  CB  . MET A 1 962  ? 58.079 56.475  -13.142 1.00 10.49 ? 962  MET A CB  1 
ATOM   7536 C  CG  . MET A 1 962  ? 59.513 55.993  -13.131 1.00 11.22 ? 962  MET A CG  1 
ATOM   7537 S  SD  . MET A 1 962  ? 60.349 56.383  -14.651 1.00 11.75 ? 962  MET A SD  1 
ATOM   7538 C  CE  . MET A 1 962  ? 62.069 55.837  -14.255 1.00 14.71 ? 962  MET A CE  1 
ATOM   7539 N  N   . ARG A 1 963  ? 58.503 56.114  -9.654  1.00 10.13 ? 963  ARG A N   1 
ATOM   7540 C  CA  . ARG A 1 963  ? 59.053 56.783  -8.495  1.00 9.39  ? 963  ARG A CA  1 
ATOM   7541 C  C   . ARG A 1 963  ? 60.308 56.106  -7.954  1.00 8.57  ? 963  ARG A C   1 
ATOM   7542 O  O   . ARG A 1 963  ? 60.269 54.936  -7.606  1.00 7.52  ? 963  ARG A O   1 
ATOM   7543 C  CB  . ARG A 1 963  ? 57.968 56.852  -7.366  1.00 10.05 ? 963  ARG A CB  1 
ATOM   7544 C  CG  . ARG A 1 963  ? 58.470 57.352  -5.974  1.00 9.23  ? 963  ARG A CG  1 
ATOM   7545 C  CD  . ARG A 1 963  ? 57.365 57.312  -4.869  1.00 9.71  ? 963  ARG A CD  1 
ATOM   7546 N  NE  . ARG A 1 963  ? 56.163 58.013  -5.331  1.00 10.25 ? 963  ARG A NE  1 
ATOM   7547 C  CZ  . ARG A 1 963  ? 54.922 57.526  -5.270  1.00 8.41  ? 963  ARG A CZ  1 
ATOM   7548 N  NH1 . ARG A 1 963  ? 54.684 56.336  -4.724  1.00 7.90  ? 963  ARG A NH1 1 
ATOM   7549 N  NH2 . ARG A 1 963  ? 53.930 58.178  -5.874  1.00 6.75  ? 963  ARG A NH2 1 
ATOM   7550 N  N   . ARG A 1 964  ? 61.413 56.847  -7.871  1.00 9.22  ? 964  ARG A N   1 
ATOM   7551 C  CA  . ARG A 1 964  ? 62.634 56.280  -7.286  1.00 9.43  ? 964  ARG A CA  1 
ATOM   7552 C  C   . ARG A 1 964  ? 62.342 56.252  -5.785  1.00 9.61  ? 964  ARG A C   1 
ATOM   7553 O  O   . ARG A 1 964  ? 61.936 57.259  -5.179  1.00 10.57 ? 964  ARG A O   1 
ATOM   7554 C  CB  . ARG A 1 964  ? 63.882 57.137  -7.575  1.00 9.36  ? 964  ARG A CB  1 
ATOM   7555 C  CG  . ARG A 1 964  ? 65.174 56.553  -6.917  1.00 10.52 ? 964  ARG A CG  1 
ATOM   7556 C  CD  . ARG A 1 964  ? 66.454 57.288  -7.386  1.00 11.50 ? 964  ARG A CD  1 
ATOM   7557 N  NE  . ARG A 1 964  ? 66.664 57.164  -8.831  1.00 12.01 ? 964  ARG A NE  1 
ATOM   7558 C  CZ  . ARG A 1 964  ? 67.449 56.258  -9.410  1.00 12.76 ? 964  ARG A CZ  1 
ATOM   7559 N  NH1 . ARG A 1 964  ? 68.113 55.373  -8.670  1.00 12.39 ? 964  ARG A NH1 1 
ATOM   7560 N  NH2 . ARG A 1 964  ? 67.601 56.261  -10.734 1.00 13.01 ? 964  ARG A NH2 1 
ATOM   7561 N  N   . LEU A 1 965  ? 62.548 55.087  -5.195  1.00 9.60  ? 965  LEU A N   1 
ATOM   7562 C  CA  . LEU A 1 965  ? 62.230 54.845  -3.791  1.00 9.36  ? 965  LEU A CA  1 
ATOM   7563 C  C   . LEU A 1 965  ? 63.395 54.951  -2.798  1.00 10.82 ? 965  LEU A C   1 
ATOM   7564 O  O   . LEU A 1 965  ? 63.164 54.873  -1.579  1.00 10.02 ? 965  LEU A O   1 
ATOM   7565 C  CB  . LEU A 1 965  ? 61.621 53.440  -3.673  1.00 8.25  ? 965  LEU A CB  1 
ATOM   7566 C  CG  . LEU A 1 965  ? 60.372 53.126  -4.528  1.00 9.30  ? 965  LEU A CG  1 
ATOM   7567 C  CD1 . LEU A 1 965  ? 60.034 51.602  -4.408  1.00 6.53  ? 965  LEU A CD1 1 
ATOM   7568 C  CD2 . LEU A 1 965  ? 59.196 53.983  -4.054  1.00 8.34  ? 965  LEU A CD2 1 
ATOM   7569 N  N   . THR A 1 966  ? 64.618 55.117  -3.315  1.00 9.89  ? 966  THR A N   1 
ATOM   7570 C  CA  . THR A 1 966  ? 65.817 55.203  -2.489  1.00 12.07 ? 966  THR A CA  1 
ATOM   7571 C  C   . THR A 1 966  ? 66.576 56.504  -2.687  1.00 12.12 ? 966  THR A C   1 
ATOM   7572 O  O   . THR A 1 966  ? 66.556 57.062  -3.793  1.00 12.45 ? 966  THR A O   1 
ATOM   7573 C  CB  . THR A 1 966  ? 66.812 54.084  -2.848  1.00 10.84 ? 966  THR A CB  1 
ATOM   7574 O  OG1 . THR A 1 966  ? 67.013 54.062  -4.262  1.00 13.70 ? 966  THR A OG1 1 
ATOM   7575 C  CG2 . THR A 1 966  ? 66.316 52.731  -2.352  1.00 11.87 ? 966  THR A CG2 1 
ATOM   7576 N  N   . LYS A 1 967  ? 67.231 56.963  -1.623  1.00 11.78 ? 967  LYS A N   1 
ATOM   7577 C  CA  . LYS A 1 967  ? 68.056 58.165  -1.650  1.00 14.54 ? 967  LYS A CA  1 
ATOM   7578 C  C   . LYS A 1 967  ? 69.431 57.759  -2.193  1.00 14.73 ? 967  LYS A C   1 
ATOM   7579 O  O   . LYS A 1 967  ? 69.737 56.564  -2.271  1.00 14.39 ? 967  LYS A O   1 
ATOM   7580 C  CB  . LYS A 1 967  ? 68.165 58.781  -0.252  1.00 15.61 ? 967  LYS A CB  1 
ATOM   7581 C  CG  . LYS A 1 967  ? 66.810 59.318  0.239   1.00 19.50 ? 967  LYS A CG  1 
ATOM   7582 C  CD  . LYS A 1 967  ? 66.968 60.171  1.492   1.00 21.99 ? 967  LYS A CD  1 
ATOM   7583 C  CE  . LYS A 1 967  ? 65.784 61.078  1.688   1.00 25.20 ? 967  LYS A CE  1 
ATOM   7584 N  NZ  . LYS A 1 967  ? 66.047 62.071  2.797   1.00 28.57 ? 967  LYS A NZ  1 
ATOM   7585 N  N   . SER A 1 968  ? 70.248 58.737  -2.571  1.00 15.64 ? 968  SER A N   1 
ATOM   7586 C  CA  . SER A 1 968  ? 71.545 58.455  -3.194  1.00 17.48 ? 968  SER A CA  1 
ATOM   7587 C  C   . SER A 1 968  ? 72.526 57.613  -2.372  1.00 17.44 ? 968  SER A C   1 
ATOM   7588 O  O   . SER A 1 968  ? 73.334 56.871  -2.936  1.00 18.58 ? 968  SER A O   1 
ATOM   7589 C  CB  . SER A 1 968  ? 72.242 59.770  -3.616  1.00 17.45 ? 968  SER A CB  1 
ATOM   7590 O  OG  . SER A 1 968  ? 72.623 60.509  -2.478  1.00 21.81 ? 968  SER A OG  1 
ATOM   7591 N  N   . SER A 1 969  ? 72.445 57.704  -1.054  1.00 18.39 ? 969  SER A N   1 
ATOM   7592 C  CA  . SER A 1 969  ? 73.359 56.941  -0.210  1.00 19.82 ? 969  SER A CA  1 
ATOM   7593 C  C   . SER A 1 969  ? 73.060 55.454  -0.155  1.00 19.98 ? 969  SER A C   1 
ATOM   7594 O  O   . SER A 1 969  ? 73.827 54.712  0.443   1.00 21.15 ? 969  SER A O   1 
ATOM   7595 C  CB  . SER A 1 969  ? 73.357 57.492  1.209   1.00 20.70 ? 969  SER A CB  1 
ATOM   7596 O  OG  . SER A 1 969  ? 72.091 57.243  1.788   1.00 26.49 ? 969  SER A OG  1 
ATOM   7597 N  N   . ALA A 1 970  ? 71.963 54.996  -0.759  1.00 19.10 ? 970  ALA A N   1 
ATOM   7598 C  CA  . ALA A 1 970  ? 71.647 53.561  -0.743  1.00 17.93 ? 970  ALA A CA  1 
ATOM   7599 C  C   . ALA A 1 970  ? 72.446 52.787  -1.779  1.00 18.24 ? 970  ALA A C   1 
ATOM   7600 O  O   . ALA A 1 970  ? 72.355 53.070  -2.978  1.00 17.29 ? 970  ALA A O   1 
ATOM   7601 C  CB  . ALA A 1 970  ? 70.153 53.330  -1.005  1.00 17.36 ? 970  ALA A CB  1 
ATOM   7602 N  N   . LYS A 1 971  ? 73.187 51.781  -1.331  1.00 18.11 ? 971  LYS A N   1 
ATOM   7603 C  CA  . LYS A 1 971  ? 73.980 50.969  -2.247  1.00 20.01 ? 971  LYS A CA  1 
ATOM   7604 C  C   . LYS A 1 971  ? 73.103 50.352  -3.324  1.00 19.56 ? 971  LYS A C   1 
ATOM   7605 O  O   . LYS A 1 971  ? 73.480 50.302  -4.493  1.00 20.89 ? 971  LYS A O   1 
ATOM   7606 C  CB  . LYS A 1 971  ? 74.672 49.842  -1.489  1.00 22.07 ? 971  LYS A CB  1 
ATOM   7607 C  CG  . LYS A 1 971  ? 75.734 49.144  -2.307  1.00 24.63 ? 971  LYS A CG  1 
ATOM   7608 C  CD  . LYS A 1 971  ? 76.459 48.087  -1.466  1.00 28.14 ? 971  LYS A CD  1 
ATOM   7609 C  CE  . LYS A 1 971  ? 77.715 47.602  -2.194  1.00 31.10 ? 971  LYS A CE  1 
ATOM   7610 N  NZ  . LYS A 1 971  ? 77.507 47.499  -3.689  1.00 33.77 ? 971  LYS A NZ  1 
ATOM   7611 N  N   . THR A 1 972  ? 71.952 49.827  -2.930  1.00 18.55 ? 972  THR A N   1 
ATOM   7612 C  CA  . THR A 1 972  ? 71.071 49.236  -3.921  1.00 18.35 ? 972  THR A CA  1 
ATOM   7613 C  C   . THR A 1 972  ? 69.943 50.218  -4.205  1.00 17.20 ? 972  THR A C   1 
ATOM   7614 O  O   . THR A 1 972  ? 69.127 50.496  -3.342  1.00 17.37 ? 972  THR A O   1 
ATOM   7615 C  CB  . THR A 1 972  ? 70.468 47.881  -3.441  1.00 19.54 ? 972  THR A CB  1 
ATOM   7616 O  OG1 . THR A 1 972  ? 71.533 46.962  -3.191  1.00 20.89 ? 972  THR A OG1 1 
ATOM   7617 C  CG2 . THR A 1 972  ? 69.576 47.257  -4.527  1.00 18.75 ? 972  THR A CG2 1 
ATOM   7618 N  N   . GLN A 1 973  ? 69.949 50.796  -5.396  1.00 15.33 ? 973  GLN A N   1 
ATOM   7619 C  CA  . GLN A 1 973  ? 68.895 51.705  -5.766  1.00 15.42 ? 973  GLN A CA  1 
ATOM   7620 C  C   . GLN A 1 973  ? 67.631 50.929  -6.148  1.00 14.36 ? 973  GLN A C   1 
ATOM   7621 O  O   . GLN A 1 973  ? 67.700 49.828  -6.700  1.00 14.96 ? 973  GLN A O   1 
ATOM   7622 C  CB  . GLN A 1 973  ? 69.333 52.573  -6.934  1.00 13.62 ? 973  GLN A CB  1 
ATOM   7623 C  CG  . GLN A 1 973  ? 70.376 53.623  -6.564  1.00 14.11 ? 973  GLN A CG  1 
ATOM   7624 C  CD  . GLN A 1 973  ? 69.883 54.603  -5.536  1.00 14.68 ? 973  GLN A CD  1 
ATOM   7625 O  OE1 . GLN A 1 973  ? 68.869 55.277  -5.745  1.00 14.48 ? 973  GLN A OE1 1 
ATOM   7626 N  NE2 . GLN A 1 973  ? 70.600 54.703  -4.418  1.00 13.21 ? 973  GLN A NE2 1 
ATOM   7627 N  N   . ARG A 1 974  ? 66.481 51.523  -5.842  1.00 13.94 ? 974  ARG A N   1 
ATOM   7628 C  CA  . ARG A 1 974  ? 65.199 50.932  -6.161  1.00 13.00 ? 974  ARG A CA  1 
ATOM   7629 C  C   . ARG A 1 974  ? 64.264 51.938  -6.795  1.00 11.75 ? 974  ARG A C   1 
ATOM   7630 O  O   . ARG A 1 974  ? 64.137 53.095  -6.338  1.00 10.86 ? 974  ARG A O   1 
ATOM   7631 C  CB  . ARG A 1 974  ? 64.534 50.362  -4.916  1.00 14.29 ? 974  ARG A CB  1 
ATOM   7632 C  CG  . ARG A 1 974  ? 65.381 49.347  -4.129  1.00 15.20 ? 974  ARG A CG  1 
ATOM   7633 C  CD  . ARG A 1 974  ? 64.781 49.162  -2.716  1.00 18.02 ? 974  ARG A CD  1 
ATOM   7634 N  NE  . ARG A 1 974  ? 63.562 48.363  -2.764  1.00 21.24 ? 974  ARG A NE  1 
ATOM   7635 C  CZ  . ARG A 1 974  ? 62.422 48.678  -2.162  1.00 20.91 ? 974  ARG A CZ  1 
ATOM   7636 N  NH1 . ARG A 1 974  ? 62.322 49.789  -1.446  1.00 23.06 ? 974  ARG A NH1 1 
ATOM   7637 N  NH2 . ARG A 1 974  ? 61.377 47.882  -2.292  1.00 21.30 ? 974  ARG A NH2 1 
ATOM   7638 N  N   . VAL A 1 975  ? 63.604 51.490  -7.852  1.00 11.01 ? 975  VAL A N   1 
ATOM   7639 C  CA  . VAL A 1 975  ? 62.652 52.337  -8.560  1.00 10.52 ? 975  VAL A CA  1 
ATOM   7640 C  C   . VAL A 1 975  ? 61.316 51.620  -8.677  1.00 10.44 ? 975  VAL A C   1 
ATOM   7641 O  O   . VAL A 1 975  ? 61.243 50.458  -9.124  1.00 10.66 ? 975  VAL A O   1 
ATOM   7642 C  CB  . VAL A 1 975  ? 63.180 52.716  -9.962  1.00 11.68 ? 975  VAL A CB  1 
ATOM   7643 C  CG1 . VAL A 1 975  ? 62.145 53.650  -10.704 1.00 9.95  ? 975  VAL A CG1 1 
ATOM   7644 C  CG2 . VAL A 1 975  ? 64.492 53.477  -9.808  1.00 10.55 ? 975  VAL A CG2 1 
ATOM   7645 N  N   . GLY A 1 976  ? 60.261 52.306  -8.243  1.00 10.08 ? 976  GLY A N   1 
ATOM   7646 C  CA  . GLY A 1 976  ? 58.932 51.719  -8.286  1.00 9.57  ? 976  GLY A CA  1 
ATOM   7647 C  C   . GLY A 1 976  ? 58.097 52.230  -9.456  1.00 9.84  ? 976  GLY A C   1 
ATOM   7648 O  O   . GLY A 1 976  ? 58.174 53.418  -9.849  1.00 8.84  ? 976  GLY A O   1 
ATOM   7649 N  N   . TYR A 1 977  ? 57.318 51.312  -10.019 1.00 8.80  ? 977  TYR A N   1 
ATOM   7650 C  CA  . TYR A 1 977  ? 56.419 51.598  -11.118 1.00 10.23 ? 977  TYR A CA  1 
ATOM   7651 C  C   . TYR A 1 977  ? 55.011 51.054  -10.871 1.00 10.10 ? 977  TYR A C   1 
ATOM   7652 O  O   . TYR A 1 977  ? 54.847 49.914  -10.413 1.00 9.26  ? 977  TYR A O   1 
ATOM   7653 C  CB  . TYR A 1 977  ? 56.892 50.942  -12.435 1.00 9.90  ? 977  TYR A CB  1 
ATOM   7654 C  CG  . TYR A 1 977  ? 58.290 51.303  -12.866 1.00 12.03 ? 977  TYR A CG  1 
ATOM   7655 C  CD1 . TYR A 1 977  ? 59.394 50.623  -12.350 1.00 11.54 ? 977  TYR A CD1 1 
ATOM   7656 C  CD2 . TYR A 1 977  ? 58.507 52.321  -13.808 1.00 10.97 ? 977  TYR A CD2 1 
ATOM   7657 C  CE1 . TYR A 1 977  ? 60.701 50.950  -12.761 1.00 13.30 ? 977  TYR A CE1 1 
ATOM   7658 C  CE2 . TYR A 1 977  ? 59.785 52.653  -14.231 1.00 11.99 ? 977  TYR A CE2 1 
ATOM   7659 C  CZ  . TYR A 1 977  ? 60.889 51.972  -13.708 1.00 13.34 ? 977  TYR A CZ  1 
ATOM   7660 O  OH  . TYR A 1 977  ? 62.167 52.338  -14.104 1.00 13.37 ? 977  TYR A OH  1 
ATOM   7661 N  N   . VAL A 1 978  ? 54.006 51.861  -11.187 1.00 8.93  ? 978  VAL A N   1 
ATOM   7662 C  CA  . VAL A 1 978  ? 52.620 51.403  -11.107 1.00 9.04  ? 978  VAL A CA  1 
ATOM   7663 C  C   . VAL A 1 978  ? 52.193 51.348  -12.584 1.00 9.31  ? 978  VAL A C   1 
ATOM   7664 O  O   . VAL A 1 978  ? 52.298 52.353  -13.283 1.00 8.51  ? 978  VAL A O   1 
ATOM   7665 C  CB  . VAL A 1 978  ? 51.721 52.372  -10.324 1.00 9.54  ? 978  VAL A CB  1 
ATOM   7666 C  CG1 . VAL A 1 978  ? 50.273 51.896  -10.398 1.00 10.34 ? 978  VAL A CG1 1 
ATOM   7667 C  CG2 . VAL A 1 978  ? 52.189 52.406  -8.836  1.00 9.67  ? 978  VAL A CG2 1 
ATOM   7668 N  N   . LEU A 1 979  ? 51.780 50.165  -13.056 1.00 8.60  ? 979  LEU A N   1 
ATOM   7669 C  CA  . LEU A 1 979  ? 51.366 49.971  -14.450 1.00 11.99 ? 979  LEU A CA  1 
ATOM   7670 C  C   . LEU A 1 979  ? 49.878 49.710  -14.510 1.00 12.29 ? 979  LEU A C   1 
ATOM   7671 O  O   . LEU A 1 979  ? 49.392 48.812  -13.844 1.00 13.11 ? 979  LEU A O   1 
ATOM   7672 C  CB  . LEU A 1 979  ? 52.040 48.761  -15.085 1.00 14.06 ? 979  LEU A CB  1 
ATOM   7673 C  CG  . LEU A 1 979  ? 53.323 48.789  -15.913 1.00 19.30 ? 979  LEU A CG  1 
ATOM   7674 C  CD1 . LEU A 1 979  ? 53.365 47.461  -16.722 1.00 21.04 ? 979  LEU A CD1 1 
ATOM   7675 C  CD2 . LEU A 1 979  ? 53.306 49.935  -16.898 1.00 19.48 ? 979  LEU A CD2 1 
ATOM   7676 N  N   . HIS A 1 980  ? 49.162 50.465  -15.325 1.00 11.07 ? 980  HIS A N   1 
ATOM   7677 C  CA  . HIS A 1 980  ? 47.724 50.267  -15.426 1.00 11.32 ? 980  HIS A CA  1 
ATOM   7678 C  C   . HIS A 1 980  ? 47.345 50.023  -16.872 1.00 11.18 ? 980  HIS A C   1 
ATOM   7679 O  O   . HIS A 1 980  ? 47.829 50.748  -17.749 1.00 11.70 ? 980  HIS A O   1 
ATOM   7680 C  CB  . HIS A 1 980  ? 46.956 51.513  -14.949 1.00 11.52 ? 980  HIS A CB  1 
ATOM   7681 C  CG  . HIS A 1 980  ? 45.480 51.407  -15.184 1.00 13.65 ? 980  HIS A CG  1 
ATOM   7682 N  ND1 . HIS A 1 980  ? 44.675 50.558  -14.454 1.00 12.65 ? 980  HIS A ND1 1 
ATOM   7683 C  CD2 . HIS A 1 980  ? 44.683 51.952  -16.135 1.00 13.87 ? 980  HIS A CD2 1 
ATOM   7684 C  CE1 . HIS A 1 980  ? 43.450 50.579  -14.942 1.00 13.30 ? 980  HIS A CE1 1 
ATOM   7685 N  NE2 . HIS A 1 980  ? 43.425 51.417  -15.965 1.00 15.28 ? 980  HIS A NE2 1 
ATOM   7686 N  N   . ARG A 1 981  ? 46.529 48.999  -17.136 1.00 11.00 ? 981  ARG A N   1 
ATOM   7687 C  CA  . ARG A 1 981  ? 46.046 48.782  -18.499 1.00 11.58 ? 981  ARG A CA  1 
ATOM   7688 C  C   . ARG A 1 981  ? 44.542 48.955  -18.437 1.00 11.68 ? 981  ARG A C   1 
ATOM   7689 O  O   . ARG A 1 981  ? 43.870 48.312  -17.626 1.00 10.88 ? 981  ARG A O   1 
ATOM   7690 C  CB  . ARG A 1 981  ? 46.344 47.383  -19.063 1.00 13.60 ? 981  ARG A CB  1 
ATOM   7691 C  CG  . ARG A 1 981  ? 46.247 47.376  -20.624 1.00 16.84 ? 981  ARG A CG  1 
ATOM   7692 C  CD  . ARG A 1 981  ? 46.241 45.988  -21.251 1.00 20.36 ? 981  ARG A CD  1 
ATOM   7693 N  NE  . ARG A 1 981  ? 47.527 45.347  -21.075 1.00 24.26 ? 981  ARG A NE  1 
ATOM   7694 C  CZ  . ARG A 1 981  ? 48.510 45.346  -21.986 1.00 26.85 ? 981  ARG A CZ  1 
ATOM   7695 N  NH1 . ARG A 1 981  ? 48.371 45.958  -23.173 1.00 25.72 ? 981  ARG A NH1 1 
ATOM   7696 N  NH2 . ARG A 1 981  ? 49.653 44.717  -21.709 1.00 27.17 ? 981  ARG A NH2 1 
ATOM   7697 N  N   . THR A 1 982  ? 44.008 49.845  -19.278 1.00 11.39 ? 982  THR A N   1 
ATOM   7698 C  CA  . THR A 1 982  ? 42.571 50.079  -19.303 1.00 11.14 ? 982  THR A CA  1 
ATOM   7699 C  C   . THR A 1 982  ? 42.041 49.057  -20.315 1.00 11.06 ? 982  THR A C   1 
ATOM   7700 O  O   . THR A 1 982  ? 42.775 48.144  -20.703 1.00 10.06 ? 982  THR A O   1 
ATOM   7701 C  CB  . THR A 1 982  ? 42.272 51.521  -19.750 1.00 11.20 ? 982  THR A CB  1 
ATOM   7702 O  OG1 . THR A 1 982  ? 40.869 51.768  -19.663 1.00 13.18 ? 982  THR A OG1 1 
ATOM   7703 C  CG2 . THR A 1 982  ? 42.752 51.759  -21.208 1.00 11.19 ? 982  THR A CG2 1 
ATOM   7704 N  N   . ASN A 1 983  ? 40.777 49.165  -20.709 1.00 10.18 ? 983  ASN A N   1 
ATOM   7705 C  CA  . ASN A 1 983  ? 40.254 48.232  -21.721 1.00 11.06 ? 983  ASN A CA  1 
ATOM   7706 C  C   . ASN A 1 983  ? 39.522 49.070  -22.773 1.00 11.71 ? 983  ASN A C   1 
ATOM   7707 O  O   . ASN A 1 983  ? 38.572 49.805  -22.454 1.00 10.99 ? 983  ASN A O   1 
ATOM   7708 C  CB  . ASN A 1 983  ? 39.269 47.229  -21.139 1.00 10.29 ? 983  ASN A CB  1 
ATOM   7709 C  CG  . ASN A 1 983  ? 38.726 46.257  -22.206 1.00 11.16 ? 983  ASN A CG  1 
ATOM   7710 O  OD1 . ASN A 1 983  ? 39.437 45.371  -22.632 1.00 11.27 ? 983  ASN A OD1 1 
ATOM   7711 N  ND2 . ASN A 1 983  ? 37.481 46.441  -22.628 1.00 7.89  ? 983  ASN A ND2 1 
ATOM   7712 N  N   . LEU A 1 984  ? 39.969 48.961  -24.012 1.00 12.91 ? 984  LEU A N   1 
ATOM   7713 C  CA  . LEU A 1 984  ? 39.381 49.733  -25.093 1.00 15.12 ? 984  LEU A CA  1 
ATOM   7714 C  C   . LEU A 1 984  ? 38.581 48.838  -26.020 1.00 16.24 ? 984  LEU A C   1 
ATOM   7715 O  O   . LEU A 1 984  ? 38.940 47.684  -26.259 1.00 16.06 ? 984  LEU A O   1 
ATOM   7716 C  CB  . LEU A 1 984  ? 40.487 50.457  -25.868 1.00 14.94 ? 984  LEU A CB  1 
ATOM   7717 C  CG  . LEU A 1 984  ? 41.414 51.378  -25.027 1.00 15.35 ? 984  LEU A CG  1 
ATOM   7718 C  CD1 . LEU A 1 984  ? 42.594 51.862  -25.901 1.00 13.84 ? 984  LEU A CD1 1 
ATOM   7719 C  CD2 . LEU A 1 984  ? 40.628 52.572  -24.474 1.00 14.84 ? 984  LEU A CD2 1 
ATOM   7720 N  N   . MET A 1 985  ? 37.476 49.364  -26.533 1.00 18.15 ? 985  MET A N   1 
ATOM   7721 C  CA  . MET A 1 985  ? 36.645 48.575  -27.439 1.00 19.89 ? 985  MET A CA  1 
ATOM   7722 C  C   . MET A 1 985  ? 37.339 48.218  -28.743 1.00 20.87 ? 985  MET A C   1 
ATOM   7723 O  O   . MET A 1 985  ? 38.072 49.026  -29.308 1.00 20.83 ? 985  MET A O   1 
ATOM   7724 C  CB  . MET A 1 985  ? 35.365 49.318  -27.774 1.00 19.99 ? 985  MET A CB  1 
ATOM   7725 C  CG  . MET A 1 985  ? 34.535 49.593  -26.578 1.00 21.84 ? 985  MET A CG  1 
ATOM   7726 S  SD  . MET A 1 985  ? 32.823 49.508  -26.989 1.00 23.85 ? 985  MET A SD  1 
ATOM   7727 C  CE  . MET A 1 985  ? 32.584 51.055  -27.867 1.00 22.31 ? 985  MET A CE  1 
ATOM   7728 N  N   . GLN A 1 986  ? 37.101 46.985  -29.192 1.00 22.74 ? 986  GLN A N   1 
ATOM   7729 C  CA  . GLN A 1 986  ? 37.624 46.457  -30.460 1.00 23.44 ? 986  GLN A CA  1 
ATOM   7730 C  C   . GLN A 1 986  ? 36.590 46.953  -31.478 1.00 21.88 ? 986  GLN A C   1 
ATOM   7731 O  O   . GLN A 1 986  ? 35.424 46.528  -31.413 1.00 20.46 ? 986  GLN A O   1 
ATOM   7732 C  CB  . GLN A 1 986  ? 37.571 44.917  -30.460 1.00 27.50 ? 986  GLN A CB  1 
ATOM   7733 C  CG  . GLN A 1 986  ? 38.414 44.195  -29.430 1.00 31.87 ? 986  GLN A CG  1 
ATOM   7734 C  CD  . GLN A 1 986  ? 39.894 44.310  -29.708 1.00 35.79 ? 986  GLN A CD  1 
ATOM   7735 O  OE1 . GLN A 1 986  ? 40.543 45.277  -29.302 1.00 40.38 ? 986  GLN A OE1 1 
ATOM   7736 N  NE2 . GLN A 1 986  ? 40.444 43.323  -30.414 1.00 38.02 ? 986  GLN A NE2 1 
ATOM   7737 N  N   . CYS A 1 987  ? 36.990 47.834  -32.394 1.00 20.16 ? 987  CYS A N   1 
ATOM   7738 C  CA  . CYS A 1 987  ? 36.044 48.353  -33.370 1.00 20.40 ? 987  CYS A CA  1 
ATOM   7739 C  C   . CYS A 1 987  ? 36.489 48.156  -34.814 1.00 22.35 ? 987  CYS A C   1 
ATOM   7740 O  O   . CYS A 1 987  ? 36.023 48.865  -35.709 1.00 21.89 ? 987  CYS A O   1 
ATOM   7741 C  CB  . CYS A 1 987  ? 35.749 49.840  -33.126 1.00 19.24 ? 987  CYS A CB  1 
ATOM   7742 S  SG  . CYS A 1 987  ? 35.094 50.282  -31.473 1.00 17.41 ? 987  CYS A SG  1 
ATOM   7743 N  N   . GLY A 1 988  ? 37.378 47.183  -35.039 1.00 24.17 ? 988  GLY A N   1 
ATOM   7744 C  CA  . GLY A 1 988  ? 37.807 46.889  -36.388 1.00 28.38 ? 988  GLY A CA  1 
ATOM   7745 C  C   . GLY A 1 988  ? 39.079 47.550  -36.842 1.00 31.97 ? 988  GLY A C   1 
ATOM   7746 O  O   . GLY A 1 988  ? 39.534 47.310  -37.972 1.00 31.55 ? 988  GLY A O   1 
ATOM   7747 N  N   . THR A 1 989  ? 39.657 48.394  -35.993 1.00 35.27 ? 989  THR A N   1 
ATOM   7748 C  CA  . THR A 1 989  ? 40.915 49.043  -36.363 1.00 39.14 ? 989  THR A CA  1 
ATOM   7749 C  C   . THR A 1 989  ? 42.051 48.069  -36.069 1.00 42.16 ? 989  THR A C   1 
ATOM   7750 O  O   . THR A 1 989  ? 42.245 47.656  -34.922 1.00 42.74 ? 989  THR A O   1 
ATOM   7751 C  CB  . THR A 1 989  ? 41.135 50.319  -35.576 1.00 38.65 ? 989  THR A CB  1 
ATOM   7752 O  OG1 . THR A 1 989  ? 40.024 51.195  -35.782 1.00 39.40 ? 989  THR A OG1 1 
ATOM   7753 C  CG2 . THR A 1 989  ? 42.394 50.997  -36.037 1.00 39.59 ? 989  THR A CG2 1 
ATOM   7754 N  N   . PRO A 1 990  ? 42.813 47.676  -37.107 1.00 45.38 ? 990  PRO A N   1 
ATOM   7755 C  CA  . PRO A 1 990  ? 43.921 46.736  -36.900 1.00 47.69 ? 990  PRO A CA  1 
ATOM   7756 C  C   . PRO A 1 990  ? 44.892 47.148  -35.789 1.00 50.33 ? 990  PRO A C   1 
ATOM   7757 O  O   . PRO A 1 990  ? 45.290 46.303  -34.973 1.00 50.91 ? 990  PRO A O   1 
ATOM   7758 C  CB  . PRO A 1 990  ? 44.588 46.674  -38.275 1.00 47.45 ? 990  PRO A CB  1 
ATOM   7759 C  CG  . PRO A 1 990  ? 43.433 46.896  -39.220 1.00 46.95 ? 990  PRO A CG  1 
ATOM   7760 C  CD  . PRO A 1 990  ? 42.690 48.039  -38.532 1.00 45.70 ? 990  PRO A CD  1 
ATOM   7761 N  N   . GLU A 1 991  ? 45.259 48.434  -35.746 1.00 52.51 ? 991  GLU A N   1 
ATOM   7762 C  CA  . GLU A 1 991  ? 46.194 48.952  -34.728 1.00 55.25 ? 991  GLU A CA  1 
ATOM   7763 C  C   . GLU A 1 991  ? 47.298 47.927  -34.392 1.00 55.56 ? 991  GLU A C   1 
ATOM   7764 O  O   . GLU A 1 991  ? 47.107 47.018  -33.569 1.00 55.85 ? 991  GLU A O   1 
ATOM   7765 C  CB  . GLU A 1 991  ? 45.414 49.343  -33.466 1.00 56.94 ? 991  GLU A CB  1 
ATOM   7766 C  CG  . GLU A 1 991  ? 44.436 50.504  -33.691 1.00 59.02 ? 991  GLU A CG  1 
ATOM   7767 C  CD  . GLU A 1 991  ? 43.216 50.453  -32.775 1.00 60.30 ? 991  GLU A CD  1 
ATOM   7768 O  OE1 . GLU A 1 991  ? 42.468 49.442  -32.829 1.00 61.20 ? 991  GLU A OE1 1 
ATOM   7769 O  OE2 . GLU A 1 991  ? 43.007 51.426  -32.012 1.00 59.87 ? 991  GLU A OE2 1 
ATOM   7770 N  N   . GLU A 1 992  ? 48.458 48.091  -35.016 1.00 55.84 ? 992  GLU A N   1 
ATOM   7771 C  CA  . GLU A 1 992  ? 49.533 47.131  -34.821 1.00 56.74 ? 992  GLU A CA  1 
ATOM   7772 C  C   . GLU A 1 992  ? 50.827 47.656  -34.198 1.00 55.52 ? 992  GLU A C   1 
ATOM   7773 O  O   . GLU A 1 992  ? 50.843 48.615  -33.423 1.00 54.86 ? 992  GLU A O   1 
ATOM   7774 C  CB  . GLU A 1 992  ? 49.879 46.490  -36.175 1.00 58.61 ? 992  GLU A CB  1 
ATOM   7775 C  CG  . GLU A 1 992  ? 48.681 46.069  -37.047 1.00 60.84 ? 992  GLU A CG  1 
ATOM   7776 C  CD  . GLU A 1 992  ? 47.959 44.815  -36.540 1.00 62.07 ? 992  GLU A CD  1 
ATOM   7777 O  OE1 . GLU A 1 992  ? 48.643 43.829  -36.170 1.00 63.11 ? 992  GLU A OE1 1 
ATOM   7778 O  OE2 . GLU A 1 992  ? 46.706 44.802  -36.531 1.00 63.07 ? 992  GLU A OE2 1 
ATOM   7779 N  N   . HIS A 1 993  ? 51.906 46.979  -34.585 1.00 54.27 ? 993  HIS A N   1 
ATOM   7780 C  CA  . HIS A 1 993  ? 53.286 47.252  -34.183 1.00 52.69 ? 993  HIS A CA  1 
ATOM   7781 C  C   . HIS A 1 993  ? 53.606 48.032  -32.914 1.00 50.26 ? 993  HIS A C   1 
ATOM   7782 O  O   . HIS A 1 993  ? 53.822 49.254  -32.961 1.00 50.12 ? 993  HIS A O   1 
ATOM   7783 C  CB  . HIS A 1 993  ? 54.069 47.891  -35.356 1.00 54.42 ? 993  HIS A CB  1 
ATOM   7784 C  CG  . HIS A 1 993  ? 53.398 49.078  -35.985 1.00 56.03 ? 993  HIS A CG  1 
ATOM   7785 N  ND1 . HIS A 1 993  ? 52.335 48.963  -36.859 1.00 57.52 ? 993  HIS A ND1 1 
ATOM   7786 C  CD2 . HIS A 1 993  ? 53.666 50.404  -35.897 1.00 56.51 ? 993  HIS A CD2 1 
ATOM   7787 C  CE1 . HIS A 1 993  ? 51.980 50.166  -37.283 1.00 57.32 ? 993  HIS A CE1 1 
ATOM   7788 N  NE2 . HIS A 1 993  ? 52.773 51.058  -36.714 1.00 56.77 ? 993  HIS A NE2 1 
ATOM   7789 N  N   . THR A 1 994  ? 53.651 47.327  -31.783 1.00 46.62 ? 994  THR A N   1 
ATOM   7790 C  CA  . THR A 1 994  ? 54.025 47.973  -30.524 1.00 42.94 ? 994  THR A CA  1 
ATOM   7791 C  C   . THR A 1 994  ? 55.035 47.086  -29.788 1.00 40.55 ? 994  THR A C   1 
ATOM   7792 O  O   . THR A 1 994  ? 55.090 45.870  -29.988 1.00 40.35 ? 994  THR A O   1 
ATOM   7793 C  CB  . THR A 1 994  ? 52.799 48.283  -29.600 1.00 42.62 ? 994  THR A CB  1 
ATOM   7794 O  OG1 . THR A 1 994  ? 52.108 47.071  -29.273 1.00 41.79 ? 994  THR A OG1 1 
ATOM   7795 C  CG2 . THR A 1 994  ? 51.843 49.232  -30.290 1.00 41.56 ? 994  THR A CG2 1 
ATOM   7796 N  N   . GLN A 1 995  ? 55.846 47.712  -28.946 1.00 37.13 ? 995  GLN A N   1 
ATOM   7797 C  CA  . GLN A 1 995  ? 56.855 46.991  -28.202 1.00 33.93 ? 995  GLN A CA  1 
ATOM   7798 C  C   . GLN A 1 995  ? 56.434 46.662  -26.794 1.00 31.53 ? 995  GLN A C   1 
ATOM   7799 O  O   . GLN A 1 995  ? 55.731 47.427  -26.125 1.00 29.63 ? 995  GLN A O   1 
ATOM   7800 C  CB  . GLN A 1 995  ? 58.135 47.800  -28.095 1.00 34.79 ? 995  GLN A CB  1 
ATOM   7801 C  CG  . GLN A 1 995  ? 58.721 48.225  -29.392 1.00 35.30 ? 995  GLN A CG  1 
ATOM   7802 C  CD  . GLN A 1 995  ? 59.581 49.426  -29.184 1.00 36.59 ? 995  GLN A CD  1 
ATOM   7803 O  OE1 . GLN A 1 995  ? 59.120 50.567  -29.339 1.00 33.13 ? 995  GLN A OE1 1 
ATOM   7804 N  NE2 . GLN A 1 995  ? 60.844 49.188  -28.778 1.00 37.12 ? 995  GLN A NE2 1 
ATOM   7805 N  N   . LYS A 1 996  ? 56.912 45.514  -26.349 1.00 28.00 ? 996  LYS A N   1 
ATOM   7806 C  CA  . LYS A 1 996  ? 56.642 45.060  -25.014 1.00 27.22 ? 996  LYS A CA  1 
ATOM   7807 C  C   . LYS A 1 996  ? 57.357 46.052  -24.085 1.00 23.95 ? 996  LYS A C   1 
ATOM   7808 O  O   . LYS A 1 996  ? 58.505 46.438  -24.333 1.00 22.38 ? 996  LYS A O   1 
ATOM   7809 C  CB  . LYS A 1 996  ? 57.200 43.638  -24.838 1.00 28.46 ? 996  LYS A CB  1 
ATOM   7810 C  CG  . LYS A 1 996  ? 56.994 43.042  -23.470 1.00 30.86 ? 996  LYS A CG  1 
ATOM   7811 C  CD  . LYS A 1 996  ? 57.173 41.509  -23.521 1.00 34.24 ? 996  LYS A CD  1 
ATOM   7812 C  CE  . LYS A 1 996  ? 57.194 40.914  -22.132 1.00 35.71 ? 996  LYS A CE  1 
ATOM   7813 N  NZ  . LYS A 1 996  ? 58.369 41.479  -21.400 1.00 37.49 ? 996  LYS A NZ  1 
ATOM   7814 N  N   . LEU A 1 997  ? 56.659 46.486  -23.044 1.00 21.76 ? 997  LEU A N   1 
ATOM   7815 C  CA  . LEU A 1 997  ? 57.249 47.398  -22.080 1.00 20.02 ? 997  LEU A CA  1 
ATOM   7816 C  C   . LEU A 1 997  ? 57.655 46.628  -20.824 1.00 18.72 ? 997  LEU A C   1 
ATOM   7817 O  O   . LEU A 1 997  ? 56.820 46.074  -20.121 1.00 18.38 ? 997  LEU A O   1 
ATOM   7818 C  CB  . LEU A 1 997  ? 56.259 48.504  -21.712 1.00 20.24 ? 997  LEU A CB  1 
ATOM   7819 C  CG  . LEU A 1 997  ? 56.753 49.460  -20.623 1.00 20.88 ? 997  LEU A CG  1 
ATOM   7820 C  CD1 . LEU A 1 997  ? 57.954 50.259  -21.116 1.00 20.15 ? 997  LEU A CD1 1 
ATOM   7821 C  CD2 . LEU A 1 997  ? 55.630 50.386  -20.234 1.00 20.23 ? 997  LEU A CD2 1 
ATOM   7822 N  N   . ASP A 1 998  ? 58.946 46.588  -20.541 1.00 17.79 ? 998  ASP A N   1 
ATOM   7823 C  CA  . ASP A 1 998  ? 59.418 45.909  -19.343 1.00 17.73 ? 998  ASP A CA  1 
ATOM   7824 C  C   . ASP A 1 998  ? 59.983 47.025  -18.490 1.00 17.04 ? 998  ASP A C   1 
ATOM   7825 O  O   . ASP A 1 998  ? 61.114 47.450  -18.691 1.00 18.13 ? 998  ASP A O   1 
ATOM   7826 C  CB  . ASP A 1 998  ? 60.520 44.895  -19.685 1.00 18.12 ? 998  ASP A CB  1 
ATOM   7827 C  CG  . ASP A 1 998  ? 61.153 44.299  -18.436 1.00 18.54 ? 998  ASP A CG  1 
ATOM   7828 O  OD1 . ASP A 1 998  ? 62.227 43.660  -18.561 1.00 17.49 ? 998  ASP A OD1 1 
ATOM   7829 O  OD2 . ASP A 1 998  ? 60.566 44.484  -17.338 1.00 14.94 ? 998  ASP A OD2 1 
ATOM   7830 N  N   . VAL A 1 999  ? 59.198 47.527  -17.547 1.00 16.71 ? 999  VAL A N   1 
ATOM   7831 C  CA  . VAL A 1 999  ? 59.691 48.623  -16.709 1.00 16.39 ? 999  VAL A CA  1 
ATOM   7832 C  C   . VAL A 1 999  ? 60.920 48.262  -15.885 1.00 16.54 ? 999  VAL A C   1 
ATOM   7833 O  O   . VAL A 1 999  ? 61.689 49.153  -15.502 1.00 15.63 ? 999  VAL A O   1 
ATOM   7834 C  CB  . VAL A 1 999  ? 58.602 49.150  -15.754 1.00 14.62 ? 999  VAL A CB  1 
ATOM   7835 C  CG1 . VAL A 1 999  ? 57.459 49.670  -16.576 1.00 14.45 ? 999  VAL A CG1 1 
ATOM   7836 C  CG2 . VAL A 1 999  ? 58.144 48.049  -14.776 1.00 14.94 ? 999  VAL A CG2 1 
ATOM   7837 N  N   . CYS A 1 1000 ? 61.112 46.973  -15.610 1.00 15.43 ? 1000 CYS A N   1 
ATOM   7838 C  CA  . CYS A 1 1000 ? 62.274 46.585  -14.817 1.00 17.86 ? 1000 CYS A CA  1 
ATOM   7839 C  C   . CYS A 1 1000 ? 63.596 46.835  -15.567 1.00 17.87 ? 1000 CYS A C   1 
ATOM   7840 O  O   . CYS A 1 1000 ? 64.658 46.951  -14.947 1.00 17.86 ? 1000 CYS A O   1 
ATOM   7841 C  CB  . CYS A 1 1000 ? 62.139 45.129  -14.314 1.00 20.75 ? 1000 CYS A CB  1 
ATOM   7842 S  SG  . CYS A 1 1000 ? 61.345 45.105  -12.650 1.00 23.27 ? 1000 CYS A SG  1 
ATOM   7843 N  N   . HIS A 1 1001 ? 63.530 46.957  -16.889 1.00 17.81 ? 1001 HIS A N   1 
ATOM   7844 C  CA  . HIS A 1 1001 ? 64.742 47.273  -17.631 1.00 18.54 ? 1001 HIS A CA  1 
ATOM   7845 C  C   . HIS A 1 1001 ? 64.818 48.726  -18.140 1.00 18.66 ? 1001 HIS A C   1 
ATOM   7846 O  O   . HIS A 1 1001 ? 65.656 49.048  -18.986 1.00 20.44 ? 1001 HIS A O   1 
ATOM   7847 C  CB  . HIS A 1 1001 ? 64.943 46.298  -18.784 1.00 19.02 ? 1001 HIS A CB  1 
ATOM   7848 C  CG  . HIS A 1 1001 ? 65.453 44.965  -18.346 1.00 19.74 ? 1001 HIS A CG  1 
ATOM   7849 N  ND1 . HIS A 1 1001 ? 64.621 43.963  -17.902 1.00 19.51 ? 1001 HIS A ND1 1 
ATOM   7850 C  CD2 . HIS A 1 1001 ? 66.716 44.486  -18.225 1.00 20.26 ? 1001 HIS A CD2 1 
ATOM   7851 C  CE1 . HIS A 1 1001 ? 65.344 42.923  -17.524 1.00 19.99 ? 1001 HIS A CE1 1 
ATOM   7852 N  NE2 . HIS A 1 1001 ? 66.619 43.215  -17.707 1.00 20.49 ? 1001 HIS A NE2 1 
ATOM   7853 N  N   . LEU A 1 1002 ? 63.967 49.619  -17.636 1.00 17.82 ? 1002 LEU A N   1 
ATOM   7854 C  CA  . LEU A 1 1002 ? 64.040 51.019  -18.082 1.00 17.79 ? 1002 LEU A CA  1 
ATOM   7855 C  C   . LEU A 1 1002 ? 65.331 51.659  -17.550 1.00 19.34 ? 1002 LEU A C   1 
ATOM   7856 O  O   . LEU A 1 1002 ? 65.882 52.553  -18.180 1.00 20.51 ? 1002 LEU A O   1 
ATOM   7857 C  CB  . LEU A 1 1002 ? 62.821 51.823  -17.612 1.00 18.19 ? 1002 LEU A CB  1 
ATOM   7858 C  CG  . LEU A 1 1002 ? 61.547 51.615  -18.418 1.00 17.97 ? 1002 LEU A CG  1 
ATOM   7859 C  CD1 . LEU A 1 1002 ? 60.386 52.358  -17.777 1.00 17.55 ? 1002 LEU A CD1 1 
ATOM   7860 C  CD2 . LEU A 1 1002 ? 61.801 52.076  -19.856 1.00 17.31 ? 1002 LEU A CD2 1 
ATOM   7861 N  N   . LEU A 1 1003 ? 65.804 51.223  -16.383 1.00 19.37 ? 1003 LEU A N   1 
ATOM   7862 C  CA  . LEU A 1 1003 ? 67.057 51.737  -15.847 1.00 19.92 ? 1003 LEU A CA  1 
ATOM   7863 C  C   . LEU A 1 1003 ? 68.105 50.626  -15.998 1.00 21.09 ? 1003 LEU A C   1 
ATOM   7864 O  O   . LEU A 1 1003 ? 67.780 49.451  -15.944 1.00 19.99 ? 1003 LEU A O   1 
ATOM   7865 C  CB  . LEU A 1 1003 ? 66.923 52.124  -14.382 1.00 22.22 ? 1003 LEU A CB  1 
ATOM   7866 C  CG  . LEU A 1 1003 ? 66.470 53.569  -14.163 1.00 25.14 ? 1003 LEU A CG  1 
ATOM   7867 C  CD1 . LEU A 1 1003 ? 64.985 53.730  -14.410 1.00 25.68 ? 1003 LEU A CD1 1 
ATOM   7868 C  CD2 . LEU A 1 1003 ? 66.773 53.946  -12.750 1.00 27.87 ? 1003 LEU A CD2 1 
ATOM   7869 N  N   . PRO A 1 1004 ? 69.379 50.992  -16.191 1.00 20.51 ? 1004 PRO A N   1 
ATOM   7870 C  CA  . PRO A 1 1004 ? 70.407 49.965  -16.350 1.00 20.47 ? 1004 PRO A CA  1 
ATOM   7871 C  C   . PRO A 1 1004 ? 70.859 49.289  -15.075 1.00 20.23 ? 1004 PRO A C   1 
ATOM   7872 O  O   . PRO A 1 1004 ? 70.518 49.704  -13.957 1.00 18.28 ? 1004 PRO A O   1 
ATOM   7873 C  CB  . PRO A 1 1004 ? 71.543 50.734  -17.016 1.00 20.75 ? 1004 PRO A CB  1 
ATOM   7874 C  CG  . PRO A 1 1004 ? 71.463 52.053  -16.312 1.00 20.45 ? 1004 PRO A CG  1 
ATOM   7875 C  CD  . PRO A 1 1004 ? 69.959 52.342  -16.344 1.00 21.30 ? 1004 PRO A CD  1 
ATOM   7876 N  N   . ASN A 1 1005 ? 71.630 48.227  -15.270 1.00 19.85 ? 1005 ASN A N   1 
ATOM   7877 C  CA  . ASN A 1 1005 ? 72.200 47.464  -14.181 1.00 21.11 ? 1005 ASN A CA  1 
ATOM   7878 C  C   . ASN A 1 1005 ? 71.158 46.889  -13.247 1.00 20.67 ? 1005 ASN A C   1 
ATOM   7879 O  O   . ASN A 1 1005 ? 71.345 46.889  -12.029 1.00 21.40 ? 1005 ASN A O   1 
ATOM   7880 C  CB  . ASN A 1 1005 ? 73.156 48.340  -13.380 1.00 23.11 ? 1005 ASN A CB  1 
ATOM   7881 C  CG  . ASN A 1 1005 ? 74.155 49.070  -14.259 1.00 26.51 ? 1005 ASN A CG  1 
ATOM   7882 O  OD1 . ASN A 1 1005 ? 74.911 48.450  -15.008 1.00 26.96 ? 1005 ASN A OD1 1 
ATOM   7883 N  ND2 . ASN A 1 1005 ? 74.163 50.403  -14.171 1.00 27.98 ? 1005 ASN A ND2 1 
ATOM   7884 N  N   . VAL A 1 1006 ? 70.064 46.376  -13.796 1.00 21.01 ? 1006 VAL A N   1 
ATOM   7885 C  CA  . VAL A 1 1006 ? 69.038 45.811  -12.930 1.00 20.34 ? 1006 VAL A CA  1 
ATOM   7886 C  C   . VAL A 1 1006 ? 69.583 44.506  -12.334 1.00 20.16 ? 1006 VAL A C   1 
ATOM   7887 O  O   . VAL A 1 1006 ? 70.160 43.695  -13.039 1.00 20.90 ? 1006 VAL A O   1 
ATOM   7888 C  CB  . VAL A 1 1006 ? 67.714 45.565  -13.716 1.00 19.37 ? 1006 VAL A CB  1 
ATOM   7889 C  CG1 . VAL A 1 1006 ? 67.908 44.518  -14.758 1.00 19.02 ? 1006 VAL A CG1 1 
ATOM   7890 C  CG2 . VAL A 1 1006 ? 66.609 45.142  -12.772 1.00 18.71 ? 1006 VAL A CG2 1 
ATOM   7891 N  N   . ALA A 1 1007 ? 69.391 44.315  -11.037 1.00 20.40 ? 1007 ALA A N   1 
ATOM   7892 C  CA  . ALA A 1 1007 ? 69.859 43.124  -10.351 1.00 20.41 ? 1007 ALA A CA  1 
ATOM   7893 C  C   . ALA A 1 1007 ? 68.671 42.318  -9.834  1.00 21.38 ? 1007 ALA A C   1 
ATOM   7894 O  O   . ALA A 1 1007 ? 68.784 41.129  -9.559  1.00 20.99 ? 1007 ALA A O   1 
ATOM   7895 C  CB  . ALA A 1 1007 ? 70.764 43.525  -9.189  1.00 20.86 ? 1007 ALA A CB  1 
ATOM   7896 N  N   . ARG A 1 1008 ? 67.521 42.970  -9.700  1.00 20.90 ? 1008 ARG A N   1 
ATOM   7897 C  CA  . ARG A 1 1008 ? 66.339 42.274  -9.220  1.00 20.26 ? 1008 ARG A CA  1 
ATOM   7898 C  C   . ARG A 1 1008 ? 65.070 42.999  -9.652  1.00 20.15 ? 1008 ARG A C   1 
ATOM   7899 O  O   . ARG A 1 1008 ? 65.070 44.230  -9.826  1.00 18.70 ? 1008 ARG A O   1 
ATOM   7900 C  CB  . ARG A 1 1008 ? 66.396 42.195  -7.707  1.00 22.45 ? 1008 ARG A CB  1 
ATOM   7901 C  CG  . ARG A 1 1008 ? 65.361 41.319  -7.089  1.00 26.71 ? 1008 ARG A CG  1 
ATOM   7902 C  CD  . ARG A 1 1008 ? 65.434 41.438  -5.564  1.00 29.55 ? 1008 ARG A CD  1 
ATOM   7903 N  NE  . ARG A 1 1008 ? 64.654 40.391  -4.910  1.00 34.27 ? 1008 ARG A NE  1 
ATOM   7904 C  CZ  . ARG A 1 1008 ? 65.041 39.115  -4.784  1.00 37.13 ? 1008 ARG A CZ  1 
ATOM   7905 N  NH1 . ARG A 1 1008 ? 66.222 38.716  -5.267  1.00 37.36 ? 1008 ARG A NH1 1 
ATOM   7906 N  NH2 . ARG A 1 1008 ? 64.235 38.231  -4.187  1.00 36.67 ? 1008 ARG A NH2 1 
ATOM   7907 N  N   . CYS A 1 1009 ? 64.003 42.226  -9.841  1.00 19.12 ? 1009 CYS A N   1 
ATOM   7908 C  CA  . CYS A 1 1009 ? 62.710 42.759  -10.237 1.00 20.06 ? 1009 CYS A CA  1 
ATOM   7909 C  C   . CYS A 1 1009 ? 61.635 42.055  -9.414  1.00 19.90 ? 1009 CYS A C   1 
ATOM   7910 O  O   . CYS A 1 1009 ? 61.519 40.822  -9.454  1.00 18.79 ? 1009 CYS A O   1 
ATOM   7911 C  CB  . CYS A 1 1009 ? 62.449 42.518  -11.727 1.00 21.68 ? 1009 CYS A CB  1 
ATOM   7912 S  SG  . CYS A 1 1009 ? 60.865 43.182  -12.413 1.00 26.37 ? 1009 CYS A SG  1 
ATOM   7913 N  N   . GLU A 1 1010 ? 60.854 42.842  -8.671  1.00 17.78 ? 1010 GLU A N   1 
ATOM   7914 C  CA  . GLU A 1 1010 ? 59.781 42.300  -7.846  1.00 17.53 ? 1010 GLU A CA  1 
ATOM   7915 C  C   . GLU A 1 1010 ? 58.418 42.932  -8.091  1.00 17.62 ? 1010 GLU A C   1 
ATOM   7916 O  O   . GLU A 1 1010 ? 58.302 44.156  -8.328  1.00 16.21 ? 1010 GLU A O   1 
ATOM   7917 C  CB  . GLU A 1 1010 ? 60.149 42.474  -6.365  1.00 19.19 ? 1010 GLU A CB  1 
ATOM   7918 C  CG  . GLU A 1 1010 ? 61.383 41.658  -5.979  1.00 24.60 ? 1010 GLU A CG  1 
ATOM   7919 C  CD  . GLU A 1 1010 ? 62.138 42.197  -4.776  1.00 28.11 ? 1010 GLU A CD  1 
ATOM   7920 O  OE1 . GLU A 1 1010 ? 62.548 43.400  -4.771  1.00 29.68 ? 1010 GLU A OE1 1 
ATOM   7921 O  OE2 . GLU A 1 1010 ? 62.339 41.386  -3.835  1.00 30.21 ? 1010 GLU A OE2 1 
ATOM   7922 N  N   . ARG A 1 1011 ? 57.385 42.096  -8.057  1.00 16.56 ? 1011 ARG A N   1 
ATOM   7923 C  CA  . ARG A 1 1011 ? 56.021 42.597  -8.137  1.00 15.74 ? 1011 ARG A CA  1 
ATOM   7924 C  C   . ARG A 1 1011 ? 55.672 42.906  -6.672  1.00 14.79 ? 1011 ARG A C   1 
ATOM   7925 O  O   . ARG A 1 1011 ? 56.003 42.128  -5.772  1.00 13.38 ? 1011 ARG A O   1 
ATOM   7926 C  CB  . ARG A 1 1011 ? 55.071 41.545  -8.676  1.00 17.36 ? 1011 ARG A CB  1 
ATOM   7927 C  CG  . ARG A 1 1011 ? 53.694 42.142  -8.938  1.00 21.95 ? 1011 ARG A CG  1 
ATOM   7928 C  CD  . ARG A 1 1011 ? 52.896 41.207  -9.761  1.00 25.59 ? 1011 ARG A CD  1 
ATOM   7929 N  NE  . ARG A 1 1011 ? 52.546 40.065  -8.950  1.00 30.42 ? 1011 ARG A NE  1 
ATOM   7930 C  CZ  . ARG A 1 1011 ? 51.569 40.097  -8.051  1.00 32.63 ? 1011 ARG A CZ  1 
ATOM   7931 N  NH1 . ARG A 1 1011 ? 50.873 41.224  -7.886  1.00 35.71 ? 1011 ARG A NH1 1 
ATOM   7932 N  NH2 . ARG A 1 1011 ? 51.276 39.022  -7.330  1.00 33.82 ? 1011 ARG A NH2 1 
ATOM   7933 N  N   . THR A 1 1012 ? 55.002 44.026  -6.435  1.00 13.13 ? 1012 THR A N   1 
ATOM   7934 C  CA  . THR A 1 1012 ? 54.677 44.440  -5.073  1.00 11.89 ? 1012 THR A CA  1 
ATOM   7935 C  C   . THR A 1 1012 ? 53.229 44.969  -4.971  1.00 11.97 ? 1012 THR A C   1 
ATOM   7936 O  O   . THR A 1 1012 ? 52.514 45.131  -5.961  1.00 11.84 ? 1012 THR A O   1 
ATOM   7937 C  CB  . THR A 1 1012 ? 55.584 45.639  -4.625  1.00 12.54 ? 1012 THR A CB  1 
ATOM   7938 O  OG1 . THR A 1 1012 ? 55.245 46.793  -5.418  1.00 11.70 ? 1012 THR A OG1 1 
ATOM   7939 C  CG2 . THR A 1 1012 ? 57.086 45.354  -4.840  1.00 10.91 ? 1012 THR A CG2 1 
ATOM   7940 N  N   . THR A 1 1013 ? 52.809 45.240  -3.753  1.00 11.47 ? 1013 THR A N   1 
ATOM   7941 C  CA  . THR A 1 1013 ? 51.532 45.846  -3.544  1.00 10.31 ? 1013 THR A CA  1 
ATOM   7942 C  C   . THR A 1 1013 ? 51.643 47.244  -4.200  1.00 10.54 ? 1013 THR A C   1 
ATOM   7943 O  O   . THR A 1 1013 ? 52.753 47.786  -4.378  1.00 9.47  ? 1013 THR A O   1 
ATOM   7944 C  CB  . THR A 1 1013 ? 51.257 45.967  -2.037  1.00 10.85 ? 1013 THR A CB  1 
ATOM   7945 O  OG1 . THR A 1 1013 ? 52.471 46.361  -1.357  1.00 9.81  ? 1013 THR A OG1 1 
ATOM   7946 C  CG2 . THR A 1 1013 ? 50.756 44.621  -1.464  1.00 10.13 ? 1013 THR A CG2 1 
ATOM   7947 N  N   . LEU A 1 1014 ? 50.501 47.853  -4.535  1.00 10.38 ? 1014 LEU A N   1 
ATOM   7948 C  CA  . LEU A 1 1014 ? 50.507 49.160  -5.191  1.00 9.00  ? 1014 LEU A CA  1 
ATOM   7949 C  C   . LEU A 1 1014 ? 51.196 50.268  -4.435  1.00 9.14  ? 1014 LEU A C   1 
ATOM   7950 O  O   . LEU A 1 1014 ? 51.572 51.276  -5.034  1.00 9.82  ? 1014 LEU A O   1 
ATOM   7951 C  CB  . LEU A 1 1014 ? 49.067 49.610  -5.551  1.00 7.43  ? 1014 LEU A CB  1 
ATOM   7952 C  CG  . LEU A 1 1014 ? 48.276 48.617  -6.421  1.00 6.86  ? 1014 LEU A CG  1 
ATOM   7953 C  CD1 . LEU A 1 1014 ? 46.946 49.279  -6.868  1.00 6.01  ? 1014 LEU A CD1 1 
ATOM   7954 C  CD2 . LEU A 1 1014 ? 49.072 48.233  -7.618  1.00 8.48  ? 1014 LEU A CD2 1 
ATOM   7955 N  N   . THR A 1 1015 ? 51.393 50.085  -3.132  1.00 9.74  ? 1015 THR A N   1 
ATOM   7956 C  CA  . THR A 1 1015 ? 52.059 51.071  -2.283  1.00 8.29  ? 1015 THR A CA  1 
ATOM   7957 C  C   . THR A 1 1015 ? 53.576 50.839  -2.217  1.00 9.62  ? 1015 THR A C   1 
ATOM   7958 O  O   . THR A 1 1015 ? 54.283 51.590  -1.544  1.00 6.85  ? 1015 THR A O   1 
ATOM   7959 C  CB  . THR A 1 1015 ? 51.543 50.957  -0.817  1.00 9.70  ? 1015 THR A CB  1 
ATOM   7960 O  OG1 . THR A 1 1015 ? 51.679 49.597  -0.387  1.00 9.30  ? 1015 THR A OG1 1 
ATOM   7961 C  CG2 . THR A 1 1015 ? 50.085 51.406  -0.682  1.00 8.22  ? 1015 THR A CG2 1 
ATOM   7962 N  N   . PHE A 1 1016 ? 54.042 49.788  -2.907  1.00 9.10  ? 1016 PHE A N   1 
ATOM   7963 C  CA  . PHE A 1 1016 ? 55.442 49.325  -2.924  1.00 9.85  ? 1016 PHE A CA  1 
ATOM   7964 C  C   . PHE A 1 1016 ? 55.929 48.792  -1.574  1.00 10.48 ? 1016 PHE A C   1 
ATOM   7965 O  O   . PHE A 1 1016 ? 57.123 48.503  -1.433  1.00 10.63 ? 1016 PHE A O   1 
ATOM   7966 C  CB  . PHE A 1 1016 ? 56.416 50.437  -3.359  1.00 10.89 ? 1016 PHE A CB  1 
ATOM   7967 C  CG  . PHE A 1 1016 ? 56.053 51.092  -4.657  1.00 9.57  ? 1016 PHE A CG  1 
ATOM   7968 C  CD1 . PHE A 1 1016 ? 55.862 52.469  -4.718  1.00 8.83  ? 1016 PHE A CD1 1 
ATOM   7969 C  CD2 . PHE A 1 1016 ? 55.902 50.326  -5.816  1.00 7.03  ? 1016 PHE A CD2 1 
ATOM   7970 C  CE1 . PHE A 1 1016 ? 55.525 53.085  -5.920  1.00 8.66  ? 1016 PHE A CE1 1 
ATOM   7971 C  CE2 . PHE A 1 1016 ? 55.565 50.920  -7.034  1.00 7.55  ? 1016 PHE A CE2 1 
ATOM   7972 C  CZ  . PHE A 1 1016 ? 55.377 52.299  -7.088  1.00 10.04 ? 1016 PHE A CZ  1 
ATOM   7973 N  N   . LEU A 1 1017 ? 55.029 48.624  -0.600  1.00 11.15 ? 1017 LEU A N   1 
ATOM   7974 C  CA  . LEU A 1 1017 ? 55.443 48.201  0.748   1.00 10.68 ? 1017 LEU A CA  1 
ATOM   7975 C  C   . LEU A 1 1017 ? 55.606 46.718  0.974   1.00 12.62 ? 1017 LEU A C   1 
ATOM   7976 O  O   . LEU A 1 1017 ? 56.227 46.313  1.948   1.00 13.11 ? 1017 LEU A O   1 
ATOM   7977 C  CB  . LEU A 1 1017 ? 54.492 48.801  1.822   1.00 9.54  ? 1017 LEU A CB  1 
ATOM   7978 C  CG  . LEU A 1 1017 ? 54.415 50.353  1.774   1.00 8.32  ? 1017 LEU A CG  1 
ATOM   7979 C  CD1 . LEU A 1 1017 ? 53.377 50.900  2.744   1.00 7.78  ? 1017 LEU A CD1 1 
ATOM   7980 C  CD2 . LEU A 1 1017 ? 55.784 50.918  2.130   1.00 7.62  ? 1017 LEU A CD2 1 
ATOM   7981 N  N   . GLN A 1 1018 ? 55.080 45.885  0.096   1.00 12.84 ? 1018 GLN A N   1 
ATOM   7982 C  CA  . GLN A 1 1018 ? 55.260 44.462  0.309   1.00 15.26 ? 1018 GLN A CA  1 
ATOM   7983 C  C   . GLN A 1 1018 ? 55.609 43.735  -0.996  1.00 15.43 ? 1018 GLN A C   1 
ATOM   7984 O  O   . GLN A 1 1018 ? 54.909 43.889  -1.989  1.00 14.71 ? 1018 GLN A O   1 
ATOM   7985 C  CB  . GLN A 1 1018 ? 53.993 43.833  0.908   1.00 18.13 ? 1018 GLN A CB  1 
ATOM   7986 C  CG  . GLN A 1 1018 ? 54.184 42.331  1.169   1.00 20.73 ? 1018 GLN A CG  1 
ATOM   7987 C  CD  . GLN A 1 1018 ? 52.897 41.588  1.492   1.00 24.23 ? 1018 GLN A CD  1 
ATOM   7988 O  OE1 . GLN A 1 1018 ? 51.799 42.170  1.503   1.00 25.47 ? 1018 GLN A OE1 1 
ATOM   7989 N  NE2 . GLN A 1 1018 ? 53.023 40.276  1.739   1.00 24.54 ? 1018 GLN A NE2 1 
ATOM   7990 N  N   . ASN A 1 1019 ? 56.690 42.950  -0.983  1.00 15.41 ? 1019 ASN A N   1 
ATOM   7991 C  CA  . ASN A 1 1019 ? 57.098 42.177  -2.151  1.00 17.40 ? 1019 ASN A CA  1 
ATOM   7992 C  C   . ASN A 1 1019 ? 56.164 40.979  -2.249  1.00 18.56 ? 1019 ASN A C   1 
ATOM   7993 O  O   . ASN A 1 1019 ? 55.974 40.244  -1.284  1.00 20.42 ? 1019 ASN A O   1 
ATOM   7994 C  CB  . ASN A 1 1019 ? 58.552 41.701  -2.022  1.00 17.50 ? 1019 ASN A CB  1 
ATOM   7995 C  CG  . ASN A 1 1019 ? 59.538 42.866  -1.960  1.00 19.59 ? 1019 ASN A CG  1 
ATOM   7996 O  OD1 . ASN A 1 1019 ? 59.305 43.919  -2.573  1.00 20.69 ? 1019 ASN A OD1 1 
ATOM   7997 N  ND2 . ASN A 1 1019 ? 60.640 42.686  -1.232  1.00 20.26 ? 1019 ASN A ND2 1 
ATOM   7998 N  N   . LEU A 1 1020 ? 55.586 40.781  -3.418  1.00 19.13 ? 1020 LEU A N   1 
ATOM   7999 C  CA  . LEU A 1 1020 ? 54.642 39.706  -3.597  1.00 18.88 ? 1020 LEU A CA  1 
ATOM   8000 C  C   . LEU A 1 1020 ? 55.204 38.659  -4.529  1.00 19.52 ? 1020 LEU A C   1 
ATOM   8001 O  O   . LEU A 1 1020 ? 54.819 37.493  -4.473  1.00 18.03 ? 1020 LEU A O   1 
ATOM   8002 C  CB  . LEU A 1 1020 ? 53.332 40.247  -4.199  1.00 18.15 ? 1020 LEU A CB  1 
ATOM   8003 C  CG  . LEU A 1 1020 ? 52.526 41.341  -3.478  1.00 19.27 ? 1020 LEU A CG  1 
ATOM   8004 C  CD1 . LEU A 1 1020 ? 51.430 41.878  -4.411  1.00 18.59 ? 1020 LEU A CD1 1 
ATOM   8005 C  CD2 . LEU A 1 1020 ? 51.912 40.789  -2.219  1.00 18.12 ? 1020 LEU A CD2 1 
ATOM   8006 N  N   . GLU A 1 1021 ? 56.109 39.068  -5.402  1.00 21.20 ? 1021 GLU A N   1 
ATOM   8007 C  CA  . GLU A 1 1021 ? 56.662 38.117  -6.367  1.00 23.48 ? 1021 GLU A CA  1 
ATOM   8008 C  C   . GLU A 1 1021 ? 58.063 38.470  -6.857  1.00 23.92 ? 1021 GLU A C   1 
ATOM   8009 O  O   . GLU A 1 1021 ? 58.353 39.617  -7.208  1.00 23.19 ? 1021 GLU A O   1 
ATOM   8010 C  CB  . GLU A 1 1021 ? 55.701 38.009  -7.548  1.00 24.13 ? 1021 GLU A CB  1 
ATOM   8011 C  CG  . GLU A 1 1021 ? 56.103 36.959  -8.541  1.00 30.15 ? 1021 GLU A CG  1 
ATOM   8012 C  CD  . GLU A 1 1021 ? 55.079 36.760  -9.633  1.00 31.56 ? 1021 GLU A CD  1 
ATOM   8013 O  OE1 . GLU A 1 1021 ? 55.328 35.874  -10.482 1.00 34.19 ? 1021 GLU A OE1 1 
ATOM   8014 O  OE2 . GLU A 1 1021 ? 54.045 37.479  -9.641  1.00 31.73 ? 1021 GLU A OE2 1 
ATOM   8015 N  N   . HIS A 1 1022 ? 58.936 37.476  -6.853  1.00 25.09 ? 1022 HIS A N   1 
ATOM   8016 C  CA  . HIS A 1 1022 ? 60.314 37.636  -7.300  1.00 26.69 ? 1022 HIS A CA  1 
ATOM   8017 C  C   . HIS A 1 1022 ? 60.290 37.227  -8.770  1.00 26.68 ? 1022 HIS A C   1 
ATOM   8018 O  O   . HIS A 1 1022 ? 59.993 36.082  -9.101  1.00 26.88 ? 1022 HIS A O   1 
ATOM   8019 C  CB  . HIS A 1 1022 ? 61.219 36.727  -6.474  1.00 29.74 ? 1022 HIS A CB  1 
ATOM   8020 C  CG  . HIS A 1 1022 ? 62.634 36.720  -6.937  1.00 33.40 ? 1022 HIS A CG  1 
ATOM   8021 N  ND1 . HIS A 1 1022 ? 63.454 37.825  -6.830  1.00 35.59 ? 1022 HIS A ND1 1 
ATOM   8022 C  CD2 . HIS A 1 1022 ? 63.351 35.777  -7.595  1.00 34.63 ? 1022 HIS A CD2 1 
ATOM   8023 C  CE1 . HIS A 1 1022 ? 64.614 37.562  -7.408  1.00 36.57 ? 1022 HIS A CE1 1 
ATOM   8024 N  NE2 . HIS A 1 1022 ? 64.577 36.328  -7.881  1.00 36.17 ? 1022 HIS A NE2 1 
ATOM   8025 N  N   . LEU A 1 1023 ? 60.615 38.160  -9.657  1.00 26.38 ? 1023 LEU A N   1 
ATOM   8026 C  CA  . LEU A 1 1023 ? 60.497 37.897  -11.080 1.00 25.92 ? 1023 LEU A CA  1 
ATOM   8027 C  C   . LEU A 1 1023 ? 61.666 37.323  -11.860 1.00 27.07 ? 1023 LEU A C   1 
ATOM   8028 O  O   . LEU A 1 1023 ? 62.785 37.856  -11.860 1.00 25.11 ? 1023 LEU A O   1 
ATOM   8029 C  CB  . LEU A 1 1023 ? 60.013 39.169  -11.778 1.00 24.21 ? 1023 LEU A CB  1 
ATOM   8030 C  CG  . LEU A 1 1023 ? 58.727 39.733  -11.183 1.00 23.18 ? 1023 LEU A CG  1 
ATOM   8031 C  CD1 . LEU A 1 1023 ? 58.614 41.176  -11.528 1.00 24.22 ? 1023 LEU A CD1 1 
ATOM   8032 C  CD2 . LEU A 1 1023 ? 57.518 38.933  -11.693 1.00 24.12 ? 1023 LEU A CD2 1 
ATOM   8033 N  N   . ASP A 1 1024 ? 61.354 36.239  -12.566 1.00 29.09 ? 1024 ASP A N   1 
ATOM   8034 C  CA  . ASP A 1 1024 ? 62.314 35.534  -13.402 1.00 30.43 ? 1024 ASP A CA  1 
ATOM   8035 C  C   . ASP A 1 1024 ? 62.840 36.412  -14.513 1.00 30.02 ? 1024 ASP A C   1 
ATOM   8036 O  O   . ASP A 1 1024 ? 62.082 37.167  -15.155 1.00 30.15 ? 1024 ASP A O   1 
ATOM   8037 C  CB  . ASP A 1 1024 ? 61.659 34.316  -14.028 1.00 33.77 ? 1024 ASP A CB  1 
ATOM   8038 C  CG  . ASP A 1 1024 ? 61.389 33.234  -13.022 1.00 38.47 ? 1024 ASP A CG  1 
ATOM   8039 O  OD1 . ASP A 1 1024 ? 60.537 32.353  -13.329 1.00 40.18 ? 1024 ASP A OD1 1 
ATOM   8040 O  OD2 . ASP A 1 1024 ? 62.036 33.268  -11.929 1.00 41.23 ? 1024 ASP A OD2 1 
ATOM   8041 N  N   . GLY A 1 1025 ? 64.137 36.296  -14.750 1.00 29.14 ? 1025 GLY A N   1 
ATOM   8042 C  CA  . GLY A 1 1025 ? 64.763 37.064  -15.806 1.00 28.40 ? 1025 GLY A CA  1 
ATOM   8043 C  C   . GLY A 1 1025 ? 64.694 38.544  -15.524 1.00 28.16 ? 1025 GLY A C   1 
ATOM   8044 O  O   . GLY A 1 1025 ? 65.071 39.345  -16.364 1.00 28.87 ? 1025 GLY A O   1 
ATOM   8045 N  N   . MET A 1 1026 ? 64.240 38.896  -14.325 1.00 27.50 ? 1026 MET A N   1 
ATOM   8046 C  CA  . MET A 1 1026 ? 64.093 40.287  -13.915 1.00 27.39 ? 1026 MET A CA  1 
ATOM   8047 C  C   . MET A 1 1026 ? 63.226 41.010  -14.928 1.00 26.63 ? 1026 MET A C   1 
ATOM   8048 O  O   . MET A 1 1026 ? 63.472 42.158  -15.273 1.00 25.24 ? 1026 MET A O   1 
ATOM   8049 C  CB  . MET A 1 1026 ? 65.450 40.967  -13.815 1.00 28.91 ? 1026 MET A CB  1 
ATOM   8050 C  CG  . MET A 1 1026 ? 66.436 40.170  -12.973 1.00 32.19 ? 1026 MET A CG  1 
ATOM   8051 S  SD  . MET A 1 1026 ? 68.041 40.949  -12.839 1.00 35.02 ? 1026 MET A SD  1 
ATOM   8052 C  CE  . MET A 1 1026 ? 68.713 40.611  -14.488 1.00 34.48 ? 1026 MET A CE  1 
ATOM   8053 N  N   . VAL A 1 1027 ? 62.192 40.328  -15.390 1.00 25.50 ? 1027 VAL A N   1 
ATOM   8054 C  CA  . VAL A 1 1027 ? 61.308 40.918  -16.368 1.00 26.60 ? 1027 VAL A CA  1 
ATOM   8055 C  C   . VAL A 1 1027 ? 59.921 41.152  -15.802 1.00 27.24 ? 1027 VAL A C   1 
ATOM   8056 O  O   . VAL A 1 1027 ? 59.261 40.224  -15.347 1.00 27.56 ? 1027 VAL A O   1 
ATOM   8057 C  CB  . VAL A 1 1027 ? 61.212 40.034  -17.628 1.00 25.56 ? 1027 VAL A CB  1 
ATOM   8058 C  CG1 . VAL A 1 1027 ? 60.110 40.549  -18.549 1.00 26.57 ? 1027 VAL A CG1 1 
ATOM   8059 C  CG2 . VAL A 1 1027 ? 62.577 40.045  -18.370 1.00 24.85 ? 1027 VAL A CG2 1 
ATOM   8060 N  N   . ALA A 1 1028 ? 59.484 42.404  -15.832 1.00 27.35 ? 1028 ALA A N   1 
ATOM   8061 C  CA  . ALA A 1 1028 ? 58.160 42.756  -15.331 1.00 28.44 ? 1028 ALA A CA  1 
ATOM   8062 C  C   . ALA A 1 1028 ? 57.172 42.559  -16.455 1.00 29.05 ? 1028 ALA A C   1 
ATOM   8063 O  O   . ALA A 1 1028 ? 57.141 43.346  -17.404 1.00 31.43 ? 1028 ALA A O   1 
ATOM   8064 C  CB  . ALA A 1 1028 ? 58.123 44.207  -14.877 1.00 27.86 ? 1028 ALA A CB  1 
ATOM   8065 N  N   . PRO A 1 1029 ? 56.346 41.517  -16.371 1.00 28.63 ? 1029 PRO A N   1 
ATOM   8066 C  CA  . PRO A 1 1029 ? 55.357 41.276  -17.436 1.00 28.80 ? 1029 PRO A CA  1 
ATOM   8067 C  C   . PRO A 1 1029 ? 54.268 42.375  -17.469 1.00 28.38 ? 1029 PRO A C   1 
ATOM   8068 O  O   . PRO A 1 1029 ? 54.058 43.059  -16.473 1.00 29.29 ? 1029 PRO A O   1 
ATOM   8069 C  CB  . PRO A 1 1029 ? 54.786 39.911  -17.071 1.00 28.68 ? 1029 PRO A CB  1 
ATOM   8070 C  CG  . PRO A 1 1029 ? 54.927 39.853  -15.561 1.00 29.19 ? 1029 PRO A CG  1 
ATOM   8071 C  CD  . PRO A 1 1029 ? 56.207 40.576  -15.243 1.00 28.08 ? 1029 PRO A CD  1 
ATOM   8072 N  N   . GLU A 1 1030 ? 53.599 42.570  -18.605 1.00 27.66 ? 1030 GLU A N   1 
ATOM   8073 C  CA  . GLU A 1 1030 ? 52.551 43.588  -18.673 1.00 26.48 ? 1030 GLU A CA  1 
ATOM   8074 C  C   . GLU A 1 1030 ? 51.281 43.019  -18.036 1.00 25.51 ? 1030 GLU A C   1 
ATOM   8075 O  O   . GLU A 1 1030 ? 51.107 41.792  -17.899 1.00 26.29 ? 1030 GLU A O   1 
ATOM   8076 C  CB  . GLU A 1 1030 ? 52.284 44.039  -20.129 1.00 27.53 ? 1030 GLU A CB  1 
ATOM   8077 C  CG  . GLU A 1 1030 ? 53.546 44.568  -20.871 1.00 27.83 ? 1030 GLU A CG  1 
ATOM   8078 C  CD  . GLU A 1 1030 ? 53.245 45.085  -22.288 1.00 28.38 ? 1030 GLU A CD  1 
ATOM   8079 O  OE1 . GLU A 1 1030 ? 52.282 44.574  -22.899 1.00 28.94 ? 1030 GLU A OE1 1 
ATOM   8080 O  OE2 . GLU A 1 1030 ? 53.964 45.984  -22.793 1.00 25.16 ? 1030 GLU A OE2 1 
ATOM   8081 N  N   . VAL A 1 1031 ? 50.400 43.919  -17.629 1.00 23.25 ? 1031 VAL A N   1 
ATOM   8082 C  CA  . VAL A 1 1031 ? 49.176 43.536  -16.967 1.00 20.64 ? 1031 VAL A CA  1 
ATOM   8083 C  C   . VAL A 1 1031 ? 48.013 43.335  -17.928 1.00 18.58 ? 1031 VAL A C   1 
ATOM   8084 O  O   . VAL A 1 1031 ? 48.072 43.727  -19.087 1.00 18.72 ? 1031 VAL A O   1 
ATOM   8085 C  CB  . VAL A 1 1031 ? 48.815 44.604  -15.904 1.00 20.74 ? 1031 VAL A CB  1 
ATOM   8086 C  CG1 . VAL A 1 1031 ? 50.021 44.814  -14.987 1.00 22.35 ? 1031 VAL A CG1 1 
ATOM   8087 C  CG2 . VAL A 1 1031 ? 48.459 45.896  -16.560 1.00 19.70 ? 1031 VAL A CG2 1 
ATOM   8088 N  N   . CYS A 1 1032 ? 46.960 42.720  -17.417 1.00 16.47 ? 1032 CYS A N   1 
ATOM   8089 C  CA  . CYS A 1 1032 ? 45.747 42.429  -18.166 1.00 15.77 ? 1032 CYS A CA  1 
ATOM   8090 C  C   . CYS A 1 1032 ? 44.832 43.651  -18.226 1.00 12.80 ? 1032 CYS A C   1 
ATOM   8091 O  O   . CYS A 1 1032 ? 44.940 44.531  -17.397 1.00 13.17 ? 1032 CYS A O   1 
ATOM   8092 C  CB  . CYS A 1 1032 ? 44.976 41.301  -17.466 1.00 16.01 ? 1032 CYS A CB  1 
ATOM   8093 S  SG  . CYS A 1 1032 ? 45.780 39.661  -17.547 1.00 19.08 ? 1032 CYS A SG  1 
ATOM   8094 N  N   . PRO A 1 1033 ? 43.874 43.669  -19.182 1.00 12.48 ? 1033 PRO A N   1 
ATOM   8095 C  CA  . PRO A 1 1033 ? 42.937 44.779  -19.316 1.00 11.63 ? 1033 PRO A CA  1 
ATOM   8096 C  C   . PRO A 1 1033 ? 42.206 44.982  -17.974 1.00 10.69 ? 1033 PRO A C   1 
ATOM   8097 O  O   . PRO A 1 1033 ? 41.718 44.022  -17.368 1.00 9.05  ? 1033 PRO A O   1 
ATOM   8098 C  CB  . PRO A 1 1033 ? 41.976 44.289  -20.408 1.00 12.08 ? 1033 PRO A CB  1 
ATOM   8099 C  CG  . PRO A 1 1033 ? 42.826 43.384  -21.262 1.00 12.05 ? 1033 PRO A CG  1 
ATOM   8100 C  CD  . PRO A 1 1033 ? 43.597 42.630  -20.200 1.00 12.91 ? 1033 PRO A CD  1 
ATOM   8101 N  N   . MET A 1 1034 ? 42.136 46.239  -17.562 1.00 11.15 ? 1034 MET A N   1 
ATOM   8102 C  CA  . MET A 1 1034 ? 41.510 46.709  -16.337 1.00 12.64 ? 1034 MET A CA  1 
ATOM   8103 C  C   . MET A 1 1034 ? 42.282 46.360  -15.070 1.00 13.71 ? 1034 MET A C   1 
ATOM   8104 O  O   . MET A 1 1034 ? 41.779 46.574  -13.966 1.00 14.64 ? 1034 MET A O   1 
ATOM   8105 C  CB  . MET A 1 1034 ? 40.079 46.215  -16.197 1.00 11.84 ? 1034 MET A CB  1 
ATOM   8106 C  CG  . MET A 1 1034 ? 39.146 46.718  -17.298 1.00 13.36 ? 1034 MET A CG  1 
ATOM   8107 S  SD  . MET A 1 1034 ? 39.209 48.504  -17.387 1.00 12.10 ? 1034 MET A SD  1 
ATOM   8108 C  CE  . MET A 1 1034 ? 38.300 48.989  -15.887 1.00 13.21 ? 1034 MET A CE  1 
ATOM   8109 N  N   . GLU A 1 1035 ? 43.491 45.840  -15.221 1.00 13.16 ? 1035 GLU A N   1 
ATOM   8110 C  CA  . GLU A 1 1035 ? 44.291 45.511  -14.048 1.00 13.70 ? 1035 GLU A CA  1 
ATOM   8111 C  C   . GLU A 1 1035 ? 45.386 46.538  -13.825 1.00 12.84 ? 1035 GLU A C   1 
ATOM   8112 O  O   . GLU A 1 1035 ? 45.765 47.260  -14.747 1.00 11.69 ? 1035 GLU A O   1 
ATOM   8113 C  CB  . GLU A 1 1035 ? 44.898 44.111  -14.186 1.00 16.71 ? 1035 GLU A CB  1 
ATOM   8114 C  CG  . GLU A 1 1035 ? 43.820 43.019  -14.059 1.00 23.26 ? 1035 GLU A CG  1 
ATOM   8115 C  CD  . GLU A 1 1035 ? 43.287 42.840  -12.605 1.00 27.09 ? 1035 GLU A CD  1 
ATOM   8116 O  OE1 . GLU A 1 1035 ? 43.134 43.839  -11.864 1.00 27.70 ? 1035 GLU A OE1 1 
ATOM   8117 O  OE2 . GLU A 1 1035 ? 43.000 41.688  -12.216 1.00 30.49 ? 1035 GLU A OE2 1 
ATOM   8118 N  N   . THR A 1 1036 ? 45.890 46.579  -12.591 1.00 12.33 ? 1036 THR A N   1 
ATOM   8119 C  CA  . THR A 1 1036 ? 46.944 47.493  -12.181 1.00 11.09 ? 1036 THR A CA  1 
ATOM   8120 C  C   . THR A 1 1036 ? 47.920 46.699  -11.328 1.00 11.71 ? 1036 THR A C   1 
ATOM   8121 O  O   . THR A 1 1036 ? 47.514 45.953  -10.438 1.00 11.19 ? 1036 THR A O   1 
ATOM   8122 C  CB  . THR A 1 1036 ? 46.400 48.636  -11.310 1.00 10.30 ? 1036 THR A CB  1 
ATOM   8123 O  OG1 . THR A 1 1036 ? 45.275 49.239  -11.966 1.00 7.69  ? 1036 THR A OG1 1 
ATOM   8124 C  CG2 . THR A 1 1036 ? 47.490 49.675  -11.083 1.00 8.48  ? 1036 THR A CG2 1 
ATOM   8125 N  N   . ALA A 1 1037 ? 49.207 46.853  -11.611 1.00 11.66 ? 1037 ALA A N   1 
ATOM   8126 C  CA  . ALA A 1 1037 ? 50.240 46.139  -10.874 1.00 11.31 ? 1037 ALA A CA  1 
ATOM   8127 C  C   . ALA A 1 1037 ? 51.371 47.104  -10.567 1.00 11.62 ? 1037 ALA A C   1 
ATOM   8128 O  O   . ALA A 1 1037 ? 51.478 48.173  -11.191 1.00 12.44 ? 1037 ALA A O   1 
ATOM   8129 C  CB  . ALA A 1 1037 ? 50.764 44.954  -11.708 1.00 13.12 ? 1037 ALA A CB  1 
ATOM   8130 N  N   . ALA A 1 1038 ? 52.185 46.747  -9.576  1.00 9.53  ? 1038 ALA A N   1 
ATOM   8131 C  CA  . ALA A 1 1038 ? 53.312 47.570  -9.192  1.00 10.45 ? 1038 ALA A CA  1 
ATOM   8132 C  C   . ALA A 1 1038 ? 54.554 46.687  -9.228  1.00 11.18 ? 1038 ALA A C   1 
ATOM   8133 O  O   . ALA A 1 1038 ? 54.512 45.489  -8.888  1.00 10.87 ? 1038 ALA A O   1 
ATOM   8134 C  CB  . ALA A 1 1038 ? 53.114 48.173  -7.792  1.00 7.57  ? 1038 ALA A CB  1 
ATOM   8135 N  N   . TYR A 1 1039 ? 55.645 47.270  -9.711  1.00 11.69 ? 1039 TYR A N   1 
ATOM   8136 C  CA  . TYR A 1 1039 ? 56.903 46.558  -9.773  1.00 11.36 ? 1039 TYR A CA  1 
ATOM   8137 C  C   . TYR A 1 1039 ? 57.989 47.464  -9.222  1.00 12.38 ? 1039 TYR A C   1 
ATOM   8138 O  O   . TYR A 1 1039 ? 57.907 48.697  -9.349  1.00 11.29 ? 1039 TYR A O   1 
ATOM   8139 C  CB  . TYR A 1 1039 ? 57.245 46.183  -11.217 1.00 10.86 ? 1039 TYR A CB  1 
ATOM   8140 C  CG  . TYR A 1 1039 ? 56.204 45.321  -11.897 1.00 12.91 ? 1039 TYR A CG  1 
ATOM   8141 C  CD1 . TYR A 1 1039 ? 55.260 45.886  -12.775 1.00 14.09 ? 1039 TYR A CD1 1 
ATOM   8142 C  CD2 . TYR A 1 1039 ? 56.182 43.935  -11.701 1.00 14.22 ? 1039 TYR A CD2 1 
ATOM   8143 C  CE1 . TYR A 1 1039 ? 54.325 45.075  -13.457 1.00 16.73 ? 1039 TYR A CE1 1 
ATOM   8144 C  CE2 . TYR A 1 1039 ? 55.264 43.132  -12.359 1.00 14.95 ? 1039 TYR A CE2 1 
ATOM   8145 C  CZ  . TYR A 1 1039 ? 54.348 43.703  -13.238 1.00 16.78 ? 1039 TYR A CZ  1 
ATOM   8146 O  OH  . TYR A 1 1039 ? 53.498 42.896  -13.947 1.00 19.26 ? 1039 TYR A OH  1 
ATOM   8147 N  N   . VAL A 1 1040 ? 59.011 46.852  -8.627  1.00 12.56 ? 1040 VAL A N   1 
ATOM   8148 C  CA  . VAL A 1 1040 ? 60.144 47.588  -8.105  1.00 12.39 ? 1040 VAL A CA  1 
ATOM   8149 C  C   . VAL A 1 1040 ? 61.389 46.932  -8.687  1.00 14.98 ? 1040 VAL A C   1 
ATOM   8150 O  O   . VAL A 1 1040 ? 61.568 45.699  -8.581  1.00 14.42 ? 1040 VAL A O   1 
ATOM   8151 C  CB  . VAL A 1 1040 ? 60.223 47.540  -6.568  1.00 13.18 ? 1040 VAL A CB  1 
ATOM   8152 C  CG1 . VAL A 1 1040 ? 61.539 48.221  -6.081  1.00 11.96 ? 1040 VAL A CG1 1 
ATOM   8153 C  CG2 . VAL A 1 1040 ? 59.002 48.271  -5.963  1.00 11.48 ? 1040 VAL A CG2 1 
ATOM   8154 N  N   . SER A 1 1041 ? 62.229 47.736  -9.338  1.00 14.18 ? 1041 SER A N   1 
ATOM   8155 C  CA  . SER A 1 1041 ? 63.482 47.206  -9.877  1.00 15.50 ? 1041 SER A CA  1 
ATOM   8156 C  C   . SER A 1 1041 ? 64.609 47.694  -8.951  1.00 14.38 ? 1041 SER A C   1 
ATOM   8157 O  O   . SER A 1 1041 ? 64.576 48.820  -8.448  1.00 14.26 ? 1041 SER A O   1 
ATOM   8158 C  CB  . SER A 1 1041 ? 63.710 47.680  -11.326 1.00 15.15 ? 1041 SER A CB  1 
ATOM   8159 O  OG  . SER A 1 1041 ? 63.708 49.101  -11.453 1.00 15.53 ? 1041 SER A OG  1 
ATOM   8160 N  N   . SER A 1 1042 ? 65.580 46.826  -8.699  1.00 14.21 ? 1042 SER A N   1 
ATOM   8161 C  CA  . SER A 1 1042 ? 66.742 47.127  -7.835  1.00 14.46 ? 1042 SER A CA  1 
ATOM   8162 C  C   . SER A 1 1042 ? 67.932 47.164  -8.775  1.00 14.77 ? 1042 SER A C   1 
ATOM   8163 O  O   . SER A 1 1042 ? 68.038 46.340  -9.691  1.00 15.44 ? 1042 SER A O   1 
ATOM   8164 C  CB  . SER A 1 1042 ? 66.929 46.031  -6.778  1.00 13.94 ? 1042 SER A CB  1 
ATOM   8165 O  OG  . SER A 1 1042 ? 65.747 45.915  -5.994  1.00 15.81 ? 1042 SER A OG  1 
ATOM   8166 N  N   . HIS A 1 1043 ? 68.807 48.133  -8.563  1.00 16.04 ? 1043 HIS A N   1 
ATOM   8167 C  CA  . HIS A 1 1043 ? 69.957 48.338  -9.432  1.00 18.66 ? 1043 HIS A CA  1 
ATOM   8168 C  C   . HIS A 1 1043 ? 71.208 48.459  -8.597  1.00 20.45 ? 1043 HIS A C   1 
ATOM   8169 O  O   . HIS A 1 1043 ? 71.223 49.075  -7.527  1.00 19.81 ? 1043 HIS A O   1 
ATOM   8170 C  CB  . HIS A 1 1043 ? 69.752 49.613  -10.260 1.00 17.53 ? 1043 HIS A CB  1 
ATOM   8171 C  CG  . HIS A 1 1043 ? 68.475 49.601  -11.036 1.00 16.52 ? 1043 HIS A CG  1 
ATOM   8172 N  ND1 . HIS A 1 1043 ? 68.399 49.132  -12.332 1.00 15.97 ? 1043 HIS A ND1 1 
ATOM   8173 C  CD2 . HIS A 1 1043 ? 67.205 49.874  -10.658 1.00 15.69 ? 1043 HIS A CD2 1 
ATOM   8174 C  CE1 . HIS A 1 1043 ? 67.138 49.114  -12.717 1.00 16.26 ? 1043 HIS A CE1 1 
ATOM   8175 N  NE2 . HIS A 1 1043 ? 66.392 49.557  -11.720 1.00 16.63 ? 1043 HIS A NE2 1 
ATOM   8176 N  N   . SER A 1 1044 ? 72.267 47.863  -9.103  1.00 23.41 ? 1044 SER A N   1 
ATOM   8177 C  CA  . SER A 1 1044 ? 73.509 47.889  -8.375  1.00 27.45 ? 1044 SER A CA  1 
ATOM   8178 C  C   . SER A 1 1044 ? 74.434 48.950  -8.931  1.00 29.01 ? 1044 SER A C   1 
ATOM   8179 O  O   . SER A 1 1044 ? 75.639 48.657  -8.913  1.00 31.58 ? 1044 SER A O   1 
ATOM   8180 C  CB  . SER A 1 1044 ? 74.159 46.508  -8.483  1.00 27.48 ? 1044 SER A CB  1 
ATOM   8181 O  OG  . SER A 1 1044 ? 74.058 46.017  -9.827  1.00 28.44 ? 1044 SER A OG  1 
HETATM 8182 C  C1  . NAG B 2 .    ? 57.962 45.091  13.631  1.00 39.77 ? 2001 NAG A C1  1 
HETATM 8183 C  C2  . NAG B 2 .    ? 59.451 44.985  13.967  1.00 42.68 ? 2001 NAG A C2  1 
HETATM 8184 C  C3  . NAG B 2 .    ? 59.958 43.547  13.805  1.00 43.53 ? 2001 NAG A C3  1 
HETATM 8185 C  C4  . NAG B 2 .    ? 58.801 42.559  13.780  1.00 42.78 ? 2001 NAG A C4  1 
HETATM 8186 C  C5  . NAG B 2 .    ? 57.794 42.898  12.662  1.00 43.57 ? 2001 NAG A C5  1 
HETATM 8187 C  C6  . NAG B 2 .    ? 56.423 42.340  12.980  1.00 43.95 ? 2001 NAG A C6  1 
HETATM 8188 C  C7  . NAG B 2 .    ? 61.373 46.304  13.357  1.00 47.69 ? 2001 NAG A C7  1 
HETATM 8189 C  C8  . NAG B 2 .    ? 61.513 47.130  14.635  1.00 47.59 ? 2001 NAG A C8  1 
HETATM 8190 N  N2  . NAG B 2 .    ? 60.166 45.850  13.056  1.00 46.41 ? 2001 NAG A N2  1 
HETATM 8191 O  O3  . NAG B 2 .    ? 60.837 43.223  14.877  1.00 44.19 ? 2001 NAG A O3  1 
HETATM 8192 O  O4  . NAG B 2 .    ? 59.302 41.248  13.577  1.00 43.32 ? 2001 NAG A O4  1 
HETATM 8193 O  O5  . NAG B 2 .    ? 57.649 44.344  12.460  1.00 41.07 ? 2001 NAG A O5  1 
HETATM 8194 O  O6  . NAG B 2 .    ? 55.646 42.217  11.800  1.00 46.81 ? 2001 NAG A O6  1 
HETATM 8195 O  O7  . NAG B 2 .    ? 62.350 46.103  12.628  1.00 49.76 ? 2001 NAG A O7  1 
HETATM 8196 ZN ZN  . ZN  C 3 .    ? 34.871 64.380  7.978   1.00 13.41 ? 2004 ZN  A ZN  1 
HETATM 8197 C  C5  . GUL D 4 .    ? 30.362 66.077  6.652   1.00 10.61 ? 2003 GUL A C5  1 
HETATM 8198 C  C2  . GUL D 4 .    ? 32.477 65.776  8.807   1.00 10.32 ? 2003 GUL A C2  1 
HETATM 8199 F  F1  . GUL D 4 .    ? 29.686 65.550  5.777   1.00 10.76 ? 2003 GUL A F1  1 
HETATM 8200 O  O2  . GUL D 4 .    ? 33.498 65.424  9.560   1.00 9.02  ? 2003 GUL A O2  1 
HETATM 8201 C  C3  . GUL D 4 .    ? 32.845 66.491  7.447   1.00 10.28 ? 2003 GUL A C3  1 
HETATM 8202 O  O3  . GUL D 4 .    ? 34.124 66.129  6.993   1.00 7.71  ? 2003 GUL A O3  1 
HETATM 8203 C  C4  . GUL D 4 .    ? 31.871 66.573  6.138   1.00 9.67  ? 2003 GUL A C4  1 
HETATM 8204 O  O4  . GUL D 4 .    ? 31.641 67.595  5.377   1.00 10.57 ? 2003 GUL A O4  1 
HETATM 8205 C  C6  . GUL D 4 .    ? 29.422 67.142  7.300   1.00 11.16 ? 2003 GUL A C6  1 
HETATM 8206 O  O6  . GUL D 4 .    ? 28.553 66.911  7.997   1.00 12.73 ? 2003 GUL A O6  1 
HETATM 8207 O  O   . GUL D 4 .    ? 30.351 65.005  7.757   1.00 9.68  ? 2003 GUL A O   1 
HETATM 8208 C  C1  . GUL D 4 .    ? 31.572 64.548  8.326   1.00 11.88 ? 2003 GUL A C1  1 
HETATM 8209 C  C1  . MPD E 5 .    ? 14.689 61.022  10.167  1.00 23.06 ? 2002 MPD A C1  1 
HETATM 8210 C  C2  . MPD E 5 .    ? 16.106 61.166  10.571  1.00 23.33 ? 2002 MPD A C2  1 
HETATM 8211 O  O2  . MPD E 5 .    ? 16.876 60.155  9.860   1.00 24.86 ? 2002 MPD A O2  1 
HETATM 8212 C  CM  . MPD E 5 .    ? 16.637 62.530  10.179  1.00 23.78 ? 2002 MPD A CM  1 
HETATM 8213 C  C3  . MPD E 5 .    ? 16.226 60.890  12.093  1.00 21.03 ? 2002 MPD A C3  1 
HETATM 8214 C  C4  . MPD E 5 .    ? 17.614 60.675  12.682  1.00 21.08 ? 2002 MPD A C4  1 
HETATM 8215 O  O4  . MPD E 5 .    ? 17.550 59.746  13.762  1.00 18.45 ? 2002 MPD A O4  1 
HETATM 8216 C  C5  . MPD E 5 .    ? 18.195 62.001  13.231  1.00 19.75 ? 2002 MPD A C5  1 
HETATM 8217 O  O   . HOH F 6 .    ? 42.053 63.617  -7.277  1.00 9.34  ? 2005 HOH A O   1 
HETATM 8218 O  O   . HOH F 6 .    ? 53.644 64.955  -19.951 1.00 5.01  ? 2006 HOH A O   1 
HETATM 8219 O  O   . HOH F 6 .    ? 39.140 62.880  -19.211 1.00 6.28  ? 2007 HOH A O   1 
HETATM 8220 O  O   . HOH F 6 .    ? 52.282 54.192  -4.857  1.00 6.41  ? 2008 HOH A O   1 
HETATM 8221 O  O   . HOH F 6 .    ? 56.143 53.409  -0.722  1.00 4.89  ? 2009 HOH A O   1 
HETATM 8222 O  O   . HOH F 6 .    ? 31.305 50.013  -24.089 1.00 6.01  ? 2010 HOH A O   1 
HETATM 8223 O  O   . HOH F 6 .    ? 49.904 48.559  1.252   1.00 3.28  ? 2011 HOH A O   1 
HETATM 8224 O  O   . HOH F 6 .    ? 36.693 57.823  13.416  1.00 7.35  ? 2012 HOH A O   1 
HETATM 8225 O  O   . HOH F 6 .    ? 26.757 69.064  -9.276  1.00 10.36 ? 2013 HOH A O   1 
HETATM 8226 O  O   . HOH F 6 .    ? 39.271 64.806  -14.871 1.00 11.95 ? 2014 HOH A O   1 
HETATM 8227 O  O   . HOH F 6 .    ? 34.228 58.672  -8.736  1.00 8.59  ? 2015 HOH A O   1 
HETATM 8228 O  O   . HOH F 6 .    ? 61.062 59.802  -8.350  1.00 9.06  ? 2016 HOH A O   1 
HETATM 8229 O  O   . HOH F 6 .    ? 36.637 72.703  0.132   1.00 9.50  ? 2017 HOH A O   1 
HETATM 8230 O  O   . HOH F 6 .    ? 31.670 47.057  -8.081  1.00 7.27  ? 2018 HOH A O   1 
HETATM 8231 O  O   . HOH F 6 .    ? 30.166 55.902  17.326  1.00 8.94  ? 2019 HOH A O   1 
HETATM 8232 O  O   . HOH F 6 .    ? 26.164 49.679  -13.728 1.00 5.60  ? 2020 HOH A O   1 
HETATM 8233 O  O   . HOH F 6 .    ? 37.663 52.274  -21.108 1.00 10.55 ? 2021 HOH A O   1 
HETATM 8234 O  O   . HOH F 6 .    ? 33.020 62.816  0.104   1.00 8.32  ? 2022 HOH A O   1 
HETATM 8235 O  O   . HOH F 6 .    ? 24.716 52.994  -11.714 1.00 8.61  ? 2023 HOH A O   1 
HETATM 8236 O  O   . HOH F 6 .    ? 63.106 61.383  -7.645  1.00 5.99  ? 2024 HOH A O   1 
HETATM 8237 O  O   . HOH F 6 .    ? 41.192 59.192  13.281  1.00 9.36  ? 2025 HOH A O   1 
HETATM 8238 O  O   . HOH F 6 .    ? 47.303 55.894  -15.410 1.00 10.25 ? 2026 HOH A O   1 
HETATM 8239 O  O   . HOH F 6 .    ? 56.249 55.845  -2.180  1.00 8.27  ? 2027 HOH A O   1 
HETATM 8240 O  O   . HOH F 6 .    ? 67.347 60.787  -5.742  1.00 12.30 ? 2028 HOH A O   1 
HETATM 8241 O  O   . HOH F 6 .    ? 26.193 48.813  -10.986 1.00 10.33 ? 2029 HOH A O   1 
HETATM 8242 O  O   . HOH F 6 .    ? 65.656 60.310  -7.833  1.00 12.06 ? 2030 HOH A O   1 
HETATM 8243 O  O   . HOH F 6 .    ? 32.572 60.205  -1.885  1.00 9.63  ? 2031 HOH A O   1 
HETATM 8244 O  O   . HOH F 6 .    ? 20.039 54.783  16.181  1.00 15.91 ? 2032 HOH A O   1 
HETATM 8245 O  O   . HOH F 6 .    ? 23.673 55.562  -23.385 1.00 7.19  ? 2033 HOH A O   1 
HETATM 8246 O  O   . HOH F 6 .    ? 39.262 57.445  14.776  1.00 9.02  ? 2034 HOH A O   1 
HETATM 8247 O  O   . HOH F 6 .    ? 20.255 58.815  -21.835 1.00 10.40 ? 2035 HOH A O   1 
HETATM 8248 O  O   . HOH F 6 .    ? 27.866 61.156  19.451  1.00 7.62  ? 2036 HOH A O   1 
HETATM 8249 O  O   . HOH F 6 .    ? 33.982 56.353  -26.377 1.00 7.55  ? 2037 HOH A O   1 
HETATM 8250 O  O   . HOH F 6 .    ? 26.337 40.071  7.936   1.00 12.67 ? 2038 HOH A O   1 
HETATM 8251 O  O   . HOH F 6 .    ? 63.775 50.230  -13.987 1.00 8.03  ? 2039 HOH A O   1 
HETATM 8252 O  O   . HOH F 6 .    ? 37.477 57.094  1.721   1.00 8.41  ? 2040 HOH A O   1 
HETATM 8253 O  O   . HOH F 6 .    ? 24.098 42.024  6.791   1.00 7.04  ? 2041 HOH A O   1 
HETATM 8254 O  O   . HOH F 6 .    ? 31.825 65.492  18.768  1.00 12.93 ? 2042 HOH A O   1 
HETATM 8255 O  O   . HOH F 6 .    ? 51.491 56.632  -5.688  1.00 7.48  ? 2043 HOH A O   1 
HETATM 8256 O  O   . HOH F 6 .    ? 19.908 56.101  7.168   1.00 9.43  ? 2044 HOH A O   1 
HETATM 8257 O  O   . HOH F 6 .    ? 28.240 43.996  13.230  1.00 9.56  ? 2045 HOH A O   1 
HETATM 8258 O  O   . HOH F 6 .    ? 30.190 58.566  -11.778 1.00 5.91  ? 2046 HOH A O   1 
HETATM 8259 O  O   . HOH F 6 .    ? 64.995 59.386  -3.731  1.00 11.62 ? 2047 HOH A O   1 
HETATM 8260 O  O   . HOH F 6 .    ? 46.297 67.652  -15.713 1.00 11.24 ? 2048 HOH A O   1 
HETATM 8261 O  O   . HOH F 6 .    ? 60.755 58.380  -3.022  1.00 10.37 ? 2049 HOH A O   1 
HETATM 8262 O  O   . HOH F 6 .    ? 60.603 62.340  -1.423  1.00 13.92 ? 2050 HOH A O   1 
HETATM 8263 O  O   . HOH F 6 .    ? 53.656 59.917  -9.492  1.00 11.01 ? 2051 HOH A O   1 
HETATM 8264 O  O   . HOH F 6 .    ? 18.660 51.072  -12.410 1.00 12.43 ? 2052 HOH A O   1 
HETATM 8265 O  O   . HOH F 6 .    ? 28.885 42.825  -11.906 1.00 13.50 ? 2053 HOH A O   1 
HETATM 8266 O  O   . HOH F 6 .    ? 34.577 79.172  -9.349  1.00 8.81  ? 2054 HOH A O   1 
HETATM 8267 O  O   . HOH F 6 .    ? 21.625 58.017  -7.848  1.00 10.23 ? 2055 HOH A O   1 
HETATM 8268 O  O   . HOH F 6 .    ? 37.055 71.832  -4.643  1.00 6.67  ? 2056 HOH A O   1 
HETATM 8269 O  O   . HOH F 6 .    ? 55.719 59.428  -11.618 1.00 9.15  ? 2057 HOH A O   1 
HETATM 8270 O  O   . HOH F 6 .    ? 36.760 44.942  -5.449  1.00 10.13 ? 2058 HOH A O   1 
HETATM 8271 O  O   . HOH F 6 .    ? 51.285 53.411  -24.070 1.00 11.23 ? 2059 HOH A O   1 
HETATM 8272 O  O   . HOH F 6 .    ? 35.087 50.661  -17.638 1.00 13.62 ? 2060 HOH A O   1 
HETATM 8273 O  O   . HOH F 6 .    ? 60.613 54.877  -0.327  1.00 13.14 ? 2061 HOH A O   1 
HETATM 8274 O  O   . HOH F 6 .    ? 42.950 56.924  6.032   1.00 8.16  ? 2062 HOH A O   1 
HETATM 8275 O  O   . HOH F 6 .    ? 47.846 59.296  -25.715 1.00 9.86  ? 2063 HOH A O   1 
HETATM 8276 O  O   . HOH F 6 .    ? 37.993 73.421  -2.431  1.00 12.70 ? 2064 HOH A O   1 
HETATM 8277 O  O   . HOH F 6 .    ? 19.321 55.374  11.495  1.00 11.72 ? 2065 HOH A O   1 
HETATM 8278 O  O   . HOH F 6 .    ? 25.997 39.737  5.192   1.00 10.21 ? 2066 HOH A O   1 
HETATM 8279 O  O   . HOH F 6 .    ? 23.352 54.235  -3.625  1.00 8.27  ? 2067 HOH A O   1 
HETATM 8280 O  O   . HOH F 6 .    ? 34.236 52.497  -1.136  1.00 12.03 ? 2068 HOH A O   1 
HETATM 8281 O  O   . HOH F 6 .    ? 50.993 44.239  -8.043  1.00 8.07  ? 2069 HOH A O   1 
HETATM 8282 O  O   . HOH F 6 .    ? 37.526 59.011  10.990  1.00 12.88 ? 2070 HOH A O   1 
HETATM 8283 O  O   . HOH F 6 .    ? 16.431 49.081  24.006  1.00 14.29 ? 2071 HOH A O   1 
HETATM 8284 O  O   . HOH F 6 .    ? 19.318 53.520  8.094   1.00 11.36 ? 2072 HOH A O   1 
HETATM 8285 O  O   . HOH F 6 .    ? 11.757 51.608  14.240  1.00 12.22 ? 2073 HOH A O   1 
HETATM 8286 O  O   . HOH F 6 .    ? 16.946 56.220  10.121  1.00 8.71  ? 2074 HOH A O   1 
HETATM 8287 O  O   . HOH F 6 .    ? 67.986 65.709  -3.559  1.00 15.30 ? 2075 HOH A O   1 
HETATM 8288 O  O   . HOH F 6 .    ? 22.854 53.189  -24.426 1.00 12.29 ? 2076 HOH A O   1 
HETATM 8289 O  O   . HOH F 6 .    ? 52.099 50.745  6.287   1.00 9.26  ? 2077 HOH A O   1 
HETATM 8290 O  O   . HOH F 6 .    ? 17.643 52.944  6.182   1.00 11.43 ? 2078 HOH A O   1 
HETATM 8291 O  O   . HOH F 6 .    ? 68.871 58.292  -5.113  1.00 9.20  ? 2079 HOH A O   1 
HETATM 8292 O  O   . HOH F 6 .    ? 33.474 48.140  -10.197 1.00 7.92  ? 2080 HOH A O   1 
HETATM 8293 O  O   . HOH F 6 .    ? 26.809 41.636  -13.205 1.00 8.17  ? 2081 HOH A O   1 
HETATM 8294 O  O   . HOH F 6 .    ? 26.739 60.966  -3.340  1.00 8.73  ? 2082 HOH A O   1 
HETATM 8295 O  O   . HOH F 6 .    ? 49.455 62.281  -8.648  1.00 13.73 ? 2083 HOH A O   1 
HETATM 8296 O  O   . HOH F 6 .    ? 41.025 52.290  -17.031 1.00 10.76 ? 2084 HOH A O   1 
HETATM 8297 O  O   . HOH F 6 .    ? 31.356 76.846  -6.352  1.00 13.71 ? 2085 HOH A O   1 
HETATM 8298 O  O   . HOH F 6 .    ? 43.342 68.270  -24.992 1.00 11.65 ? 2086 HOH A O   1 
HETATM 8299 O  O   . HOH F 6 .    ? 32.762 81.088  -11.732 1.00 10.51 ? 2087 HOH A O   1 
HETATM 8300 O  O   . HOH F 6 .    ? 20.537 66.281  -19.511 1.00 9.74  ? 2088 HOH A O   1 
HETATM 8301 O  O   . HOH F 6 .    ? 40.430 62.751  6.188   1.00 7.78  ? 2089 HOH A O   1 
HETATM 8302 O  O   . HOH F 6 .    ? 42.184 47.375  -24.579 1.00 12.73 ? 2090 HOH A O   1 
HETATM 8303 O  O   . HOH F 6 .    ? 44.523 41.952  -0.508  1.00 15.95 ? 2091 HOH A O   1 
HETATM 8304 O  O   . HOH F 6 .    ? 38.622 55.267  -31.806 1.00 15.33 ? 2092 HOH A O   1 
HETATM 8305 O  O   . HOH F 6 .    ? 22.291 54.438  -12.026 1.00 10.60 ? 2093 HOH A O   1 
HETATM 8306 O  O   . HOH F 6 .    ? 48.226 89.319  -30.848 1.00 11.65 ? 2094 HOH A O   1 
HETATM 8307 O  O   . HOH F 6 .    ? 36.802 51.761  3.744   1.00 7.55  ? 2095 HOH A O   1 
HETATM 8308 O  O   . HOH F 6 .    ? 38.873 62.161  8.120   1.00 11.36 ? 2096 HOH A O   1 
HETATM 8309 O  O   . HOH F 6 .    ? 47.450 46.097  3.632   1.00 8.88  ? 2097 HOH A O   1 
HETATM 8310 O  O   . HOH F 6 .    ? 33.505 57.119  -35.995 1.00 11.34 ? 2098 HOH A O   1 
HETATM 8311 O  O   . HOH F 6 .    ? 32.358 77.648  -29.683 1.00 11.34 ? 2099 HOH A O   1 
HETATM 8312 O  O   . HOH F 6 .    ? 39.231 39.145  17.209  1.00 14.03 ? 2100 HOH A O   1 
HETATM 8313 O  O   . HOH F 6 .    ? 35.936 53.159  1.331   1.00 8.81  ? 2101 HOH A O   1 
HETATM 8314 O  O   . HOH F 6 .    ? 14.367 60.133  5.110   1.00 11.15 ? 2102 HOH A O   1 
HETATM 8315 O  O   . HOH F 6 .    ? 21.599 57.172  4.937   1.00 12.36 ? 2103 HOH A O   1 
HETATM 8316 O  O   . HOH F 6 .    ? 43.058 48.111  11.229  1.00 11.94 ? 2104 HOH A O   1 
HETATM 8317 O  O   . HOH F 6 .    ? 26.124 72.779  5.640   1.00 7.22  ? 2105 HOH A O   1 
HETATM 8318 O  O   . HOH F 6 .    ? 27.339 48.577  -21.552 1.00 16.62 ? 2106 HOH A O   1 
HETATM 8319 O  O   . HOH F 6 .    ? 33.404 78.742  -5.144  1.00 10.92 ? 2107 HOH A O   1 
HETATM 8320 O  O   . HOH F 6 .    ? 49.961 59.454  -11.619 1.00 14.18 ? 2108 HOH A O   1 
HETATM 8321 O  O   . HOH F 6 .    ? 25.635 51.288  -9.611  1.00 9.33  ? 2109 HOH A O   1 
HETATM 8322 O  O   . HOH F 6 .    ? 40.188 56.365  5.751   1.00 10.92 ? 2110 HOH A O   1 
HETATM 8323 O  O   . HOH F 6 .    ? 14.086 59.829  -3.502  1.00 10.57 ? 2111 HOH A O   1 
HETATM 8324 O  O   . HOH F 6 .    ? 19.694 53.547  -11.797 1.00 8.68  ? 2112 HOH A O   1 
HETATM 8325 O  O   . HOH F 6 .    ? 26.232 63.691  16.987  1.00 16.63 ? 2113 HOH A O   1 
HETATM 8326 O  O   . HOH F 6 .    ? 19.853 57.420  -11.962 1.00 12.48 ? 2114 HOH A O   1 
HETATM 8327 O  O   . HOH F 6 .    ? 47.211 48.520  11.521  1.00 17.21 ? 2115 HOH A O   1 
HETATM 8328 O  O   . HOH F 6 .    ? 67.787 81.623  -25.759 1.00 10.35 ? 2116 HOH A O   1 
HETATM 8329 O  O   . HOH F 6 .    ? 22.841 51.623  -8.799  1.00 14.96 ? 2117 HOH A O   1 
HETATM 8330 O  O   . HOH F 6 .    ? 46.584 70.314  -36.697 1.00 11.89 ? 2118 HOH A O   1 
HETATM 8331 O  O   . HOH F 6 .    ? 20.584 57.516  -5.286  1.00 10.03 ? 2119 HOH A O   1 
HETATM 8332 O  O   . HOH F 6 .    ? 18.094 60.671  24.463  1.00 13.80 ? 2120 HOH A O   1 
HETATM 8333 O  O   . HOH F 6 .    ? 41.188 68.466  -32.637 1.00 18.09 ? 2121 HOH A O   1 
HETATM 8334 O  O   . HOH F 6 .    ? 38.368 40.036  1.758   1.00 11.09 ? 2122 HOH A O   1 
HETATM 8335 O  O   . HOH F 6 .    ? 23.812 58.194  6.319   1.00 9.48  ? 2123 HOH A O   1 
HETATM 8336 O  O   . HOH F 6 .    ? 18.121 59.824  -20.096 1.00 16.97 ? 2124 HOH A O   1 
HETATM 8337 O  O   . HOH F 6 .    ? 41.302 77.569  -14.229 1.00 13.84 ? 2125 HOH A O   1 
HETATM 8338 O  O   . HOH F 6 .    ? 52.851 58.999  -1.745  1.00 17.06 ? 2126 HOH A O   1 
HETATM 8339 O  O   . HOH F 6 .    ? 47.902 49.535  13.700  1.00 10.68 ? 2127 HOH A O   1 
HETATM 8340 O  O   . HOH F 6 .    ? 35.184 43.654  28.708  1.00 14.48 ? 2128 HOH A O   1 
HETATM 8341 O  O   . HOH F 6 .    ? 59.532 60.553  -6.319  1.00 11.98 ? 2129 HOH A O   1 
HETATM 8342 O  O   . HOH F 6 .    ? 53.667 72.534  -19.355 1.00 10.69 ? 2130 HOH A O   1 
HETATM 8343 O  O   . HOH F 6 .    ? 39.693 53.934  -20.929 1.00 10.82 ? 2131 HOH A O   1 
HETATM 8344 O  O   . HOH F 6 .    ? 33.130 36.759  -4.405  1.00 18.25 ? 2132 HOH A O   1 
HETATM 8345 O  O   . HOH F 6 .    ? 14.424 63.996  -16.367 1.00 15.26 ? 2133 HOH A O   1 
HETATM 8346 O  O   . HOH F 6 .    ? 47.482 42.991  -2.507  1.00 18.50 ? 2134 HOH A O   1 
HETATM 8347 O  O   . HOH F 6 .    ? 46.873 55.842  -25.631 1.00 18.34 ? 2135 HOH A O   1 
HETATM 8348 O  O   . HOH F 6 .    ? 32.010 58.627  -28.537 1.00 14.44 ? 2136 HOH A O   1 
HETATM 8349 O  O   . HOH F 6 .    ? 49.185 50.170  28.205  1.00 11.81 ? 2137 HOH A O   1 
HETATM 8350 O  O   . HOH F 6 .    ? 26.391 37.510  29.418  1.00 16.66 ? 2138 HOH A O   1 
HETATM 8351 O  O   . HOH F 6 .    ? 51.895 46.645  1.247   1.00 9.65  ? 2139 HOH A O   1 
HETATM 8352 O  O   . HOH F 6 .    ? 41.666 58.751  -16.170 1.00 11.24 ? 2140 HOH A O   1 
HETATM 8353 O  O   . HOH F 6 .    ? 13.800 54.161  4.332   1.00 16.13 ? 2141 HOH A O   1 
HETATM 8354 O  O   . HOH F 6 .    ? 67.703 78.985  -25.496 1.00 8.64  ? 2142 HOH A O   1 
HETATM 8355 O  O   . HOH F 6 .    ? 42.047 75.122  -16.251 1.00 18.33 ? 2143 HOH A O   1 
HETATM 8356 O  O   . HOH F 6 .    ? 23.002 56.140  30.782  1.00 15.98 ? 2144 HOH A O   1 
HETATM 8357 O  O   . HOH F 6 .    ? 56.945 61.059  1.451   1.00 15.40 ? 2145 HOH A O   1 
HETATM 8358 O  O   . HOH F 6 .    ? 20.137 74.429  -6.857  1.00 10.82 ? 2146 HOH A O   1 
HETATM 8359 O  O   . HOH F 6 .    ? 13.448 53.674  1.760   1.00 20.46 ? 2147 HOH A O   1 
HETATM 8360 O  O   . HOH F 6 .    ? 34.145 34.462  16.116  1.00 18.74 ? 2148 HOH A O   1 
HETATM 8361 O  O   . HOH F 6 .    ? 33.962 64.536  -32.288 1.00 13.91 ? 2149 HOH A O   1 
HETATM 8362 O  O   . HOH F 6 .    ? 13.945 49.111  15.388  1.00 11.48 ? 2150 HOH A O   1 
HETATM 8363 O  O   . HOH F 6 .    ? 30.237 35.273  -12.426 1.00 20.50 ? 2151 HOH A O   1 
HETATM 8364 O  O   . HOH F 6 .    ? 18.269 54.971  14.092  1.00 12.18 ? 2152 HOH A O   1 
HETATM 8365 O  O   . HOH F 6 .    ? 15.405 60.381  15.462  1.00 18.18 ? 2153 HOH A O   1 
HETATM 8366 O  O   . HOH F 6 .    ? 16.914 74.752  -3.252  1.00 12.85 ? 2154 HOH A O   1 
HETATM 8367 O  O   . HOH F 6 .    ? 56.586 46.210  -17.494 1.00 12.49 ? 2155 HOH A O   1 
HETATM 8368 O  O   . HOH F 6 .    ? 45.687 59.891  -18.372 1.00 9.25  ? 2156 HOH A O   1 
HETATM 8369 O  O   . HOH F 6 .    ? 28.043 84.564  -35.546 1.00 12.42 ? 2157 HOH A O   1 
HETATM 8370 O  O   . HOH F 6 .    ? 73.049 65.201  -7.942  1.00 16.36 ? 2158 HOH A O   1 
HETATM 8371 O  O   . HOH F 6 .    ? 73.825 65.913  -17.783 1.00 14.89 ? 2159 HOH A O   1 
HETATM 8372 O  O   . HOH F 6 .    ? 59.283 50.048  -0.642  1.00 15.14 ? 2160 HOH A O   1 
HETATM 8373 O  O   . HOH F 6 .    ? 23.208 78.526  -24.767 1.00 20.95 ? 2161 HOH A O   1 
HETATM 8374 O  O   . HOH F 6 .    ? 14.396 54.458  -16.149 1.00 14.24 ? 2162 HOH A O   1 
HETATM 8375 O  O   . HOH F 6 .    ? 43.484 73.198  5.601   1.00 10.34 ? 2163 HOH A O   1 
HETATM 8376 O  O   . HOH F 6 .    ? 11.930 55.100  -12.462 1.00 17.12 ? 2164 HOH A O   1 
HETATM 8377 O  O   . HOH F 6 .    ? 63.608 44.622  -6.958  1.00 12.60 ? 2165 HOH A O   1 
HETATM 8378 O  O   . HOH F 6 .    ? 24.770 51.119  -24.156 1.00 13.89 ? 2166 HOH A O   1 
HETATM 8379 O  O   . HOH F 6 .    ? 35.425 45.292  -27.537 1.00 11.12 ? 2167 HOH A O   1 
HETATM 8380 O  O   . HOH F 6 .    ? 28.663 49.907  -24.565 1.00 16.62 ? 2168 HOH A O   1 
HETATM 8381 O  O   . HOH F 6 .    ? 54.871 80.982  -23.632 1.00 16.05 ? 2169 HOH A O   1 
HETATM 8382 O  O   . HOH F 6 .    ? 24.096 63.406  7.467   1.00 7.11  ? 2170 HOH A O   1 
HETATM 8383 O  O   . HOH F 6 .    ? 49.754 57.618  -7.659  1.00 11.84 ? 2171 HOH A O   1 
HETATM 8384 O  O   . HOH F 6 .    ? 46.200 70.964  -0.006  1.00 20.21 ? 2172 HOH A O   1 
HETATM 8385 O  O   . HOH F 6 .    ? 24.373 55.678  -1.944  1.00 11.62 ? 2173 HOH A O   1 
HETATM 8386 O  O   . HOH F 6 .    ? 28.668 41.292  -21.673 1.00 12.02 ? 2174 HOH A O   1 
HETATM 8387 O  O   . HOH F 6 .    ? 36.965 45.705  27.429  1.00 11.33 ? 2175 HOH A O   1 
HETATM 8388 O  O   . HOH F 6 .    ? 41.432 41.307  -17.672 1.00 13.78 ? 2176 HOH A O   1 
HETATM 8389 O  O   . HOH F 6 .    ? 40.369 62.584  -32.081 1.00 13.82 ? 2177 HOH A O   1 
HETATM 8390 O  O   . HOH F 6 .    ? 49.295 59.254  -28.804 1.00 8.76  ? 2178 HOH A O   1 
HETATM 8391 O  O   . HOH F 6 .    ? 64.315 39.449  -10.404 1.00 23.44 ? 2179 HOH A O   1 
HETATM 8392 O  O   . HOH F 6 .    ? 19.274 72.489  3.031   1.00 19.25 ? 2180 HOH A O   1 
HETATM 8393 O  O   . HOH F 6 .    ? 17.105 70.403  -16.265 1.00 12.20 ? 2181 HOH A O   1 
HETATM 8394 O  O   . HOH F 6 .    ? 9.418  52.385  16.873  1.00 20.78 ? 2182 HOH A O   1 
HETATM 8395 O  O   . HOH F 6 .    ? 53.872 71.187  -36.940 1.00 8.43  ? 2183 HOH A O   1 
HETATM 8396 O  O   . HOH F 6 .    ? 50.869 70.908  -23.552 1.00 18.03 ? 2184 HOH A O   1 
HETATM 8397 O  O   . HOH F 6 .    ? 49.420 44.192  4.329   1.00 14.24 ? 2185 HOH A O   1 
HETATM 8398 O  O   . HOH F 6 .    ? 59.569 68.035  2.340   1.00 25.46 ? 2186 HOH A O   1 
HETATM 8399 O  O   . HOH F 6 .    ? 25.376 53.885  11.065  1.00 11.54 ? 2187 HOH A O   1 
HETATM 8400 O  O   . HOH F 6 .    ? 69.055 61.434  -2.533  1.00 10.95 ? 2188 HOH A O   1 
HETATM 8401 O  O   . HOH F 6 .    ? 58.193 77.321  -38.606 1.00 12.53 ? 2189 HOH A O   1 
HETATM 8402 O  O   . HOH F 6 .    ? 44.362 46.271  9.961   1.00 11.90 ? 2190 HOH A O   1 
HETATM 8403 O  O   . HOH F 6 .    ? 46.557 57.401  -18.814 1.00 10.69 ? 2191 HOH A O   1 
HETATM 8404 O  O   . HOH F 6 .    ? 33.619 83.525  -10.434 1.00 14.63 ? 2192 HOH A O   1 
HETATM 8405 O  O   . HOH F 6 .    ? 47.007 68.439  -30.380 1.00 12.84 ? 2193 HOH A O   1 
HETATM 8406 O  O   . HOH F 6 .    ? 44.560 56.166  -15.456 1.00 14.78 ? 2194 HOH A O   1 
HETATM 8407 O  O   . HOH F 6 .    ? 13.194 66.972  -4.771  1.00 12.11 ? 2195 HOH A O   1 
HETATM 8408 O  O   . HOH F 6 .    ? 24.449 39.212  -11.483 1.00 18.69 ? 2196 HOH A O   1 
HETATM 8409 O  O   . HOH F 6 .    ? 41.550 61.194  -29.800 1.00 12.79 ? 2197 HOH A O   1 
HETATM 8410 O  O   . HOH F 6 .    ? 27.121 41.380  13.330  1.00 14.36 ? 2198 HOH A O   1 
HETATM 8411 O  O   . HOH F 6 .    ? 41.995 87.831  -40.922 1.00 11.33 ? 2199 HOH A O   1 
HETATM 8412 O  O   . HOH F 6 .    ? 69.895 69.948  -12.816 1.00 14.09 ? 2200 HOH A O   1 
HETATM 8413 O  O   . HOH F 6 .    ? 64.149 77.841  -35.324 1.00 14.19 ? 2201 HOH A O   1 
HETATM 8414 O  O   . HOH F 6 .    ? 20.676 65.396  7.797   1.00 11.16 ? 2202 HOH A O   1 
HETATM 8415 O  O   . HOH F 6 .    ? 11.326 61.469  -18.483 1.00 22.94 ? 2203 HOH A O   1 
HETATM 8416 O  O   . HOH F 6 .    ? 24.604 70.695  -8.790  1.00 10.86 ? 2204 HOH A O   1 
HETATM 8417 O  O   . HOH F 6 .    ? 25.077 39.996  14.172  1.00 16.67 ? 2205 HOH A O   1 
HETATM 8418 O  O   . HOH F 6 .    ? 22.612 63.321  -33.105 1.00 20.74 ? 2206 HOH A O   1 
HETATM 8419 O  O   . HOH F 6 .    ? 41.729 43.268  7.926   1.00 13.51 ? 2207 HOH A O   1 
HETATM 8420 O  O   . HOH F 6 .    ? 13.448 58.013  -22.074 1.00 13.32 ? 2208 HOH A O   1 
HETATM 8421 O  O   . HOH F 6 .    ? 41.456 50.447  33.318  1.00 26.36 ? 2209 HOH A O   1 
HETATM 8422 O  O   . HOH F 6 .    ? 45.925 52.971  -19.449 1.00 18.80 ? 2210 HOH A O   1 
HETATM 8423 O  O   . HOH F 6 .    ? 51.203 76.341  -41.220 1.00 24.82 ? 2211 HOH A O   1 
HETATM 8424 O  O   . HOH F 6 .    ? 25.650 86.311  -31.938 1.00 14.58 ? 2212 HOH A O   1 
HETATM 8425 O  O   . HOH F 6 .    ? 12.374 56.301  5.294   1.00 18.66 ? 2213 HOH A O   1 
HETATM 8426 O  O   . HOH F 6 .    ? 22.543 56.827  -34.233 1.00 15.69 ? 2214 HOH A O   1 
HETATM 8427 O  O   . HOH F 6 .    ? 43.558 72.605  -42.004 1.00 27.06 ? 2215 HOH A O   1 
HETATM 8428 O  O   . HOH F 6 .    ? 44.488 58.689  -16.074 1.00 17.59 ? 2216 HOH A O   1 
HETATM 8429 O  O   . HOH F 6 .    ? 31.558 81.641  0.389   1.00 18.81 ? 2217 HOH A O   1 
HETATM 8430 O  O   . HOH F 6 .    ? 52.044 56.404  -30.413 1.00 20.27 ? 2218 HOH A O   1 
HETATM 8431 O  O   . HOH F 6 .    ? 17.362 70.105  -23.438 1.00 19.41 ? 2219 HOH A O   1 
HETATM 8432 O  O   . HOH F 6 .    ? 37.594 47.059  29.700  1.00 17.22 ? 2220 HOH A O   1 
HETATM 8433 O  O   . HOH F 6 .    ? 49.710 55.079  -29.145 1.00 20.27 ? 2221 HOH A O   1 
HETATM 8434 O  O   . HOH F 6 .    ? 36.251 79.023  -5.159  1.00 19.03 ? 2222 HOH A O   1 
HETATM 8435 O  O   . HOH F 6 .    ? 62.140 62.628  25.769  1.00 16.58 ? 2223 HOH A O   1 
HETATM 8436 O  O   . HOH F 6 .    ? 11.333 53.295  6.729   1.00 19.83 ? 2224 HOH A O   1 
HETATM 8437 O  O   . HOH F 6 .    ? 13.883 60.861  -22.376 1.00 14.70 ? 2225 HOH A O   1 
HETATM 8438 O  O   . HOH F 6 .    ? 50.589 62.092  26.292  1.00 18.12 ? 2226 HOH A O   1 
HETATM 8439 O  O   . HOH F 6 .    ? 68.559 78.848  -18.248 1.00 23.14 ? 2227 HOH A O   1 
HETATM 8440 O  O   . HOH F 6 .    ? 84.236 68.263  -17.338 1.00 17.18 ? 2228 HOH A O   1 
HETATM 8441 O  O   . HOH F 6 .    ? 21.831 40.582  -8.830  1.00 38.70 ? 2229 HOH A O   1 
HETATM 8442 O  O   . HOH F 6 .    ? 52.881 69.920  18.341  1.00 20.10 ? 2230 HOH A O   1 
HETATM 8443 O  O   . HOH F 6 .    ? 42.705 53.574  35.555  1.00 23.17 ? 2231 HOH A O   1 
HETATM 8444 O  O   . HOH F 6 .    ? 70.571 52.035  -12.681 1.00 13.14 ? 2232 HOH A O   1 
HETATM 8445 O  O   . HOH F 6 .    ? 34.692 71.242  13.476  1.00 23.06 ? 2233 HOH A O   1 
HETATM 8446 O  O   . HOH F 6 .    ? 27.253 46.304  13.635  1.00 18.40 ? 2234 HOH A O   1 
HETATM 8447 O  O   . HOH F 6 .    ? 14.116 49.703  19.712  1.00 18.81 ? 2235 HOH A O   1 
HETATM 8448 O  O   . HOH F 6 .    ? 49.735 73.377  -21.811 1.00 17.75 ? 2236 HOH A O   1 
HETATM 8449 O  O   . HOH F 6 .    ? 48.772 44.401  -6.109  1.00 23.47 ? 2237 HOH A O   1 
HETATM 8450 O  O   . HOH F 6 .    ? 61.375 76.782  -39.856 1.00 14.28 ? 2238 HOH A O   1 
HETATM 8451 O  O   . HOH F 6 .    ? 22.663 78.760  -30.337 1.00 18.64 ? 2239 HOH A O   1 
HETATM 8452 O  O   . HOH F 6 .    ? 43.484 88.575  -38.668 1.00 16.46 ? 2240 HOH A O   1 
HETATM 8453 O  O   . HOH F 6 .    ? 35.757 77.606  -7.327  1.00 12.80 ? 2241 HOH A O   1 
HETATM 8454 O  O   . HOH F 6 .    ? 24.661 68.341  21.837  1.00 16.51 ? 2242 HOH A O   1 
HETATM 8455 O  O   . HOH F 6 .    ? 68.126 49.343  -1.043  1.00 27.22 ? 2243 HOH A O   1 
HETATM 8456 O  O   . HOH F 6 .    ? 54.045 47.879  15.568  1.00 19.12 ? 2244 HOH A O   1 
HETATM 8457 O  O   . HOH F 6 .    ? 54.959 50.554  16.890  1.00 24.94 ? 2245 HOH A O   1 
HETATM 8458 O  O   . HOH F 6 .    ? 39.174 48.778  -33.062 1.00 22.62 ? 2246 HOH A O   1 
HETATM 8459 O  O   . HOH F 6 .    ? 22.847 45.218  -13.586 1.00 20.26 ? 2247 HOH A O   1 
HETATM 8460 O  O   . HOH F 6 .    ? 67.047 55.273  0.924   1.00 12.93 ? 2248 HOH A O   1 
HETATM 8461 O  O   . HOH F 6 .    ? 48.050 44.009  -8.694  1.00 23.66 ? 2249 HOH A O   1 
HETATM 8462 O  O   . HOH F 6 .    ? 26.931 87.894  -23.720 1.00 20.54 ? 2250 HOH A O   1 
HETATM 8463 O  O   . HOH F 6 .    ? 18.860 48.818  37.708  1.00 15.24 ? 2251 HOH A O   1 
HETATM 8464 O  O   . HOH F 6 .    ? 83.559 67.592  -22.718 1.00 28.92 ? 2252 HOH A O   1 
HETATM 8465 O  O   . HOH F 6 .    ? 43.111 59.768  -19.133 1.00 21.15 ? 2253 HOH A O   1 
HETATM 8466 O  O   . HOH F 6 .    ? 47.393 78.893  -40.568 1.00 16.40 ? 2254 HOH A O   1 
HETATM 8467 O  O   . HOH F 6 .    ? 8.663  57.513  -6.920  1.00 25.68 ? 2255 HOH A O   1 
HETATM 8468 O  O   . HOH F 6 .    ? 54.716 90.316  -23.764 1.00 33.07 ? 2256 HOH A O   1 
HETATM 8469 O  O   . HOH F 6 .    ? 27.641 36.696  -19.601 1.00 24.16 ? 2257 HOH A O   1 
HETATM 8470 O  O   . HOH F 6 .    ? 72.279 59.036  -11.389 1.00 23.47 ? 2258 HOH A O   1 
HETATM 8471 O  O   . HOH F 6 .    ? 11.853 59.598  -4.982  1.00 19.00 ? 2259 HOH A O   1 
HETATM 8472 O  O   . HOH F 6 .    ? 23.720 46.067  -15.964 1.00 22.13 ? 2260 HOH A O   1 
HETATM 8473 O  O   . HOH F 6 .    ? 50.067 70.836  -17.736 1.00 23.16 ? 2261 HOH A O   1 
HETATM 8474 O  O   . HOH F 6 .    ? 45.082 90.106  -25.677 1.00 18.81 ? 2262 HOH A O   1 
HETATM 8475 O  O   . HOH F 6 .    ? 16.034 72.197  -19.154 1.00 12.70 ? 2263 HOH A O   1 
HETATM 8476 O  O   . HOH F 6 .    ? 19.990 52.706  -24.242 1.00 19.23 ? 2264 HOH A O   1 
HETATM 8477 O  O   . HOH F 6 .    ? 59.548 76.505  -9.016  1.00 16.11 ? 2265 HOH A O   1 
HETATM 8478 O  O   . HOH F 6 .    ? 66.825 60.050  -27.265 1.00 19.37 ? 2266 HOH A O   1 
HETATM 8479 O  O   . HOH F 6 .    ? 38.456 51.330  -29.951 1.00 20.62 ? 2267 HOH A O   1 
HETATM 8480 O  O   . HOH F 6 .    ? 40.488 82.785  -10.874 1.00 16.67 ? 2268 HOH A O   1 
HETATM 8481 O  O   . HOH F 6 .    ? 42.009 48.917  31.251  1.00 16.35 ? 2269 HOH A O   1 
HETATM 8482 O  O   . HOH F 6 .    ? 24.129 52.977  -5.955  1.00 19.60 ? 2270 HOH A O   1 
HETATM 8483 O  O   . HOH F 6 .    ? 53.258 47.105  -24.978 1.00 14.25 ? 2271 HOH A O   1 
HETATM 8484 O  O   . HOH F 6 .    ? 32.393 89.118  -43.111 1.00 22.77 ? 2272 HOH A O   1 
HETATM 8485 O  O   . HOH F 6 .    ? 35.990 36.160  -4.565  1.00 18.46 ? 2273 HOH A O   1 
HETATM 8486 O  O   . HOH F 6 .    ? 69.993 83.023  -30.059 1.00 33.47 ? 2274 HOH A O   1 
HETATM 8487 O  O   . HOH F 6 .    ? 49.610 82.503  -43.944 1.00 15.76 ? 2275 HOH A O   1 
HETATM 8488 O  O   . HOH F 6 .    ? 68.282 79.676  -34.763 1.00 24.94 ? 2276 HOH A O   1 
HETATM 8489 O  O   . HOH F 6 .    ? 28.968 47.077  37.115  1.00 19.37 ? 2277 HOH A O   1 
HETATM 8490 O  O   . HOH F 6 .    ? 18.590 70.040  4.084   1.00 9.66  ? 2278 HOH A O   1 
HETATM 8491 O  O   . HOH F 6 .    ? 14.036 68.382  -7.870  1.00 19.47 ? 2279 HOH A O   1 
HETATM 8492 O  O   . HOH F 6 .    ? 50.393 72.519  9.297   1.00 25.57 ? 2280 HOH A O   1 
HETATM 8493 O  O   . HOH F 6 .    ? 39.497 75.608  -40.298 1.00 16.85 ? 2281 HOH A O   1 
HETATM 8494 O  O   . HOH F 6 .    ? 28.639 65.127  19.667  1.00 17.42 ? 2282 HOH A O   1 
HETATM 8495 O  O   . HOH F 6 .    ? 11.727 58.611  7.762   1.00 26.79 ? 2283 HOH A O   1 
HETATM 8496 O  O   . HOH F 6 .    ? 52.525 78.868  -17.369 1.00 27.33 ? 2284 HOH A O   1 
HETATM 8497 O  O   . HOH F 6 .    ? 18.384 65.097  -27.099 1.00 39.67 ? 2285 HOH A O   1 
HETATM 8498 O  O   . HOH F 6 .    ? 44.742 79.466  -33.361 1.00 17.11 ? 2286 HOH A O   1 
HETATM 8499 O  O   . HOH F 6 .    ? 36.150 81.115  6.287   1.00 24.24 ? 2287 HOH A O   1 
HETATM 8500 O  O   . HOH F 6 .    ? 16.725 60.610  -28.321 1.00 20.16 ? 2288 HOH A O   1 
HETATM 8501 O  O   . HOH F 6 .    ? 29.669 87.503  -17.861 1.00 33.46 ? 2289 HOH A O   1 
HETATM 8502 O  O   . HOH F 6 .    ? 8.705  54.961  -6.185  1.00 25.40 ? 2290 HOH A O   1 
HETATM 8503 O  O   . HOH F 6 .    ? 46.636 61.663  -26.106 1.00 18.17 ? 2291 HOH A O   1 
HETATM 8504 O  O   . HOH F 6 .    ? 43.144 82.214  -10.216 1.00 16.99 ? 2292 HOH A O   1 
HETATM 8505 O  O   . HOH F 6 .    ? 10.313 50.806  18.683  1.00 24.28 ? 2293 HOH A O   1 
HETATM 8506 O  O   . HOH F 6 .    ? 12.886 42.602  12.595  1.00 21.72 ? 2294 HOH A O   1 
HETATM 8507 O  O   . HOH F 6 .    ? 35.812 45.215  30.830  1.00 23.17 ? 2295 HOH A O   1 
HETATM 8508 O  O   . HOH F 6 .    ? 15.750 75.210  -11.699 1.00 21.41 ? 2296 HOH A O   1 
HETATM 8509 O  O   . HOH F 6 .    ? 25.288 46.890  -20.892 1.00 23.38 ? 2297 HOH A O   1 
HETATM 8510 O  O   . HOH F 6 .    ? 56.885 64.930  24.254  1.00 20.02 ? 2298 HOH A O   1 
HETATM 8511 O  O   . HOH F 6 .    ? 38.609 94.155  -42.201 1.00 19.00 ? 2299 HOH A O   1 
HETATM 8512 O  O   . HOH F 6 .    ? 34.746 59.650  -34.970 1.00 22.23 ? 2300 HOH A O   1 
HETATM 8513 O  O   . HOH F 6 .    ? 32.893 41.059  -17.919 1.00 20.79 ? 2301 HOH A O   1 
HETATM 8514 O  O   . HOH F 6 .    ? 20.765 42.691  -7.499  1.00 16.17 ? 2302 HOH A O   1 
HETATM 8515 O  O   . HOH F 6 .    ? 19.212 76.739  4.760   1.00 28.72 ? 2303 HOH A O   1 
HETATM 8516 O  O   . HOH F 6 .    ? 43.460 80.710  4.976   1.00 22.37 ? 2304 HOH A O   1 
HETATM 8517 O  O   . HOH F 6 .    ? 32.949 85.301  -5.596  1.00 21.45 ? 2305 HOH A O   1 
HETATM 8518 O  O   . HOH F 6 .    ? 31.342 33.689  2.882   1.00 23.63 ? 2306 HOH A O   1 
HETATM 8519 O  O   . HOH F 6 .    ? 21.570 78.567  -1.419  1.00 14.98 ? 2307 HOH A O   1 
HETATM 8520 O  O   . HOH F 6 .    ? 55.261 59.140  3.950   1.00 20.68 ? 2308 HOH A O   1 
HETATM 8521 O  O   . HOH F 6 .    ? 13.404 62.473  -20.079 1.00 16.65 ? 2309 HOH A O   1 
HETATM 8522 O  O   . HOH F 6 .    ? 17.029 50.860  -19.557 1.00 25.66 ? 2310 HOH A O   1 
HETATM 8523 O  O   . HOH F 6 .    ? 14.231 62.917  -12.101 1.00 16.38 ? 2311 HOH A O   1 
HETATM 8524 O  O   . HOH F 6 .    ? 53.088 86.751  -21.406 1.00 27.02 ? 2312 HOH A O   1 
HETATM 8525 O  O   . HOH F 6 .    ? 70.953 49.558  -0.126  1.00 24.83 ? 2313 HOH A O   1 
HETATM 8526 O  O   . HOH F 6 .    ? 58.109 42.589  1.562   1.00 23.59 ? 2314 HOH A O   1 
HETATM 8527 O  O   . HOH F 6 .    ? 74.605 76.415  -14.442 1.00 24.99 ? 2315 HOH A O   1 
HETATM 8528 O  O   . HOH F 6 .    ? 24.950 83.215  -16.965 1.00 20.65 ? 2316 HOH A O   1 
HETATM 8529 O  O   . HOH F 6 .    ? 56.853 67.583  -35.449 1.00 21.63 ? 2317 HOH A O   1 
HETATM 8530 O  O   . HOH F 6 .    ? 48.824 50.527  -29.534 1.00 19.96 ? 2318 HOH A O   1 
HETATM 8531 O  O   . HOH F 6 .    ? 66.597 71.637  -6.825  1.00 19.33 ? 2319 HOH A O   1 
HETATM 8532 O  O   . HOH F 6 .    ? 28.784 93.677  -38.605 1.00 17.76 ? 2320 HOH A O   1 
HETATM 8533 O  O   . HOH F 6 .    ? 32.615 64.769  -10.138 1.00 17.72 ? 2321 HOH A O   1 
HETATM 8534 O  O   . HOH F 6 .    ? 13.345 51.048  -1.842  1.00 26.28 ? 2322 HOH A O   1 
HETATM 8535 O  O   . HOH F 6 .    ? 39.428 49.208  30.257  1.00 34.20 ? 2323 HOH A O   1 
HETATM 8536 O  O   . HOH F 6 .    ? 67.848 58.680  -24.195 1.00 16.08 ? 2324 HOH A O   1 
HETATM 8537 O  O   . HOH F 6 .    ? 20.750 58.924  -34.692 1.00 15.96 ? 2325 HOH A O   1 
HETATM 8538 O  O   . HOH F 6 .    ? 37.413 75.644  -42.558 1.00 22.42 ? 2326 HOH A O   1 
HETATM 8539 O  O   . HOH F 6 .    ? 31.892 51.241  -35.500 1.00 22.93 ? 2327 HOH A O   1 
HETATM 8540 O  O   . HOH F 6 .    ? 12.874 71.128  -0.615  1.00 20.81 ? 2328 HOH A O   1 
HETATM 8541 O  O   . HOH F 6 .    ? 36.951 41.073  -24.823 1.00 33.91 ? 2329 HOH A O   1 
HETATM 8542 O  O   . HOH F 6 .    ? 19.286 42.807  -2.486  1.00 23.14 ? 2330 HOH A O   1 
HETATM 8543 O  O   . HOH F 6 .    ? 50.005 44.103  7.285   1.00 17.93 ? 2331 HOH A O   1 
HETATM 8544 O  O   . HOH F 6 .    ? 37.344 45.477  -25.488 1.00 18.54 ? 2332 HOH A O   1 
HETATM 8545 O  O   . HOH F 6 .    ? 75.198 74.176  -19.756 1.00 21.74 ? 2333 HOH A O   1 
HETATM 8546 O  O   . HOH F 6 .    ? 50.288 61.120  -31.263 1.00 14.65 ? 2334 HOH A O   1 
HETATM 8547 O  O   . HOH F 6 .    ? 42.808 56.708  -31.642 1.00 22.38 ? 2335 HOH A O   1 
HETATM 8548 O  O   . HOH F 6 .    ? 13.313 68.801  1.022   1.00 20.68 ? 2336 HOH A O   1 
HETATM 8549 O  O   . HOH F 6 .    ? 41.124 82.749  -31.461 1.00 26.25 ? 2337 HOH A O   1 
HETATM 8550 O  O   . HOH F 6 .    ? 26.883 52.218  22.566  1.00 21.72 ? 2338 HOH A O   1 
HETATM 8551 O  O   . HOH F 6 .    ? 12.633 66.466  -9.646  1.00 21.50 ? 2339 HOH A O   1 
HETATM 8552 O  O   . HOH F 6 .    ? 42.468 39.354  -15.851 1.00 23.64 ? 2340 HOH A O   1 
HETATM 8553 O  O   . HOH F 6 .    ? 48.062 48.439  16.517  1.00 14.54 ? 2341 HOH A O   1 
HETATM 8554 O  O   . HOH F 6 .    ? 11.229 46.866  17.760  1.00 22.64 ? 2342 HOH A O   1 
HETATM 8555 O  O   . HOH F 6 .    ? 16.377 67.963  -19.774 1.00 19.59 ? 2343 HOH A O   1 
HETATM 8556 O  O   . HOH F 6 .    ? 5.229  52.799  -6.070  1.00 29.84 ? 2344 HOH A O   1 
HETATM 8557 O  O   . HOH F 6 .    ? 56.224 91.057  -26.095 1.00 21.22 ? 2345 HOH A O   1 
HETATM 8558 O  O   . HOH F 6 .    ? 39.086 83.360  -27.514 1.00 22.49 ? 2346 HOH A O   1 
HETATM 8559 O  O   . HOH F 6 .    ? 60.671 56.947  15.878  1.00 26.97 ? 2347 HOH A O   1 
HETATM 8560 O  O   . HOH F 6 .    ? 13.355 51.519  21.551  1.00 20.10 ? 2348 HOH A O   1 
HETATM 8561 O  O   . HOH F 6 .    ? 43.298 93.861  -37.850 1.00 18.90 ? 2349 HOH A O   1 
HETATM 8562 O  O   . HOH F 6 .    ? 28.019 35.463  -6.772  1.00 24.69 ? 2350 HOH A O   1 
HETATM 8563 O  O   . HOH F 6 .    ? 80.368 64.159  -21.483 1.00 23.24 ? 2351 HOH A O   1 
HETATM 8564 O  O   . HOH F 6 .    ? 51.321 45.313  9.554   1.00 33.63 ? 2352 HOH A O   1 
HETATM 8565 O  O   . HOH F 6 .    ? 20.817 46.727  -17.251 1.00 26.53 ? 2353 HOH A O   1 
HETATM 8566 O  O   . HOH F 6 .    ? 47.440 71.796  -20.450 1.00 22.76 ? 2354 HOH A O   1 
HETATM 8567 O  O   . HOH F 6 .    ? 21.567 86.160  -30.707 1.00 27.50 ? 2355 HOH A O   1 
HETATM 8568 O  O   . HOH F 6 .    ? 32.906 67.016  21.306  1.00 20.62 ? 2356 HOH A O   1 
HETATM 8569 O  O   . HOH F 6 .    ? 14.678 62.024  -14.550 1.00 20.12 ? 2357 HOH A O   1 
HETATM 8570 O  O   . HOH F 6 .    ? 50.367 73.662  -25.323 1.00 22.51 ? 2358 HOH A O   1 
HETATM 8571 O  O   . HOH F 6 .    ? 41.984 79.532  -23.857 1.00 28.31 ? 2359 HOH A O   1 
HETATM 8572 O  O   . HOH F 6 .    ? 39.944 45.302  25.612  1.00 30.28 ? 2360 HOH A O   1 
HETATM 8573 O  O   . HOH F 6 .    ? 50.731 76.634  14.388  1.00 23.00 ? 2361 HOH A O   1 
HETATM 8574 O  O   . HOH F 6 .    ? 38.526 45.080  -33.614 1.00 20.16 ? 2362 HOH A O   1 
HETATM 8575 O  O   . HOH F 6 .    ? 61.397 54.248  -29.114 1.00 21.00 ? 2363 HOH A O   1 
HETATM 8576 O  O   . HOH F 6 .    ? 53.595 46.874  23.497  1.00 29.79 ? 2364 HOH A O   1 
HETATM 8577 O  O   . HOH F 6 .    ? 57.016 43.264  -20.003 1.00 20.06 ? 2365 HOH A O   1 
HETATM 8578 O  O   . HOH F 6 .    ? 67.605 54.801  -18.415 1.00 18.68 ? 2366 HOH A O   1 
HETATM 8579 O  O   . HOH F 6 .    ? 42.233 79.908  -31.884 1.00 40.75 ? 2367 HOH A O   1 
HETATM 8580 O  O   . HOH F 6 .    ? 28.961 62.354  -39.813 1.00 22.33 ? 2368 HOH A O   1 
HETATM 8581 O  O   . HOH F 6 .    ? 27.142 61.379  10.362  1.00 35.96 ? 2369 HOH A O   1 
HETATM 8582 O  O   . HOH F 6 .    ? 45.749 45.205  23.064  1.00 24.76 ? 2370 HOH A O   1 
HETATM 8583 O  O   . HOH F 6 .    ? 34.952 51.374  35.826  1.00 31.05 ? 2371 HOH A O   1 
HETATM 8584 O  O   . HOH F 6 .    ? 57.699 62.460  7.789   1.00 32.79 ? 2372 HOH A O   1 
HETATM 8585 O  O   . HOH F 6 .    ? 25.218 33.483  13.285  1.00 29.46 ? 2373 HOH A O   1 
HETATM 8586 O  O   . HOH F 6 .    ? 27.341 59.395  8.541   1.00 13.77 ? 2374 HOH A O   1 
HETATM 8587 O  O   . HOH F 6 .    ? 42.213 94.550  -29.799 1.00 34.99 ? 2375 HOH A O   1 
HETATM 8588 O  O   . HOH F 6 .    ? 13.850 58.120  -1.426  1.00 17.93 ? 2376 HOH A O   1 
HETATM 8589 O  O   . HOH F 6 .    ? 49.365 76.450  5.168   1.00 32.03 ? 2377 HOH A O   1 
HETATM 8590 O  O   . HOH F 6 .    ? 27.589 67.671  28.163  1.00 22.58 ? 2378 HOH A O   1 
HETATM 8591 O  O   . HOH F 6 .    ? 41.846 39.471  16.348  1.00 31.31 ? 2379 HOH A O   1 
HETATM 8592 O  O   . HOH F 6 .    ? 58.778 46.371  -1.457  1.00 21.75 ? 2380 HOH A O   1 
HETATM 8593 O  O   . HOH F 6 .    ? 73.505 76.982  -18.707 1.00 29.78 ? 2381 HOH A O   1 
HETATM 8594 O  O   . HOH F 6 .    ? 19.553 39.310  17.460  1.00 13.63 ? 2382 HOH A O   1 
HETATM 8595 O  O   . HOH F 6 .    ? 39.580 58.985  -18.105 1.00 15.87 ? 2383 HOH A O   1 
HETATM 8596 O  O   . HOH F 6 .    ? 28.079 47.025  -31.417 1.00 24.28 ? 2384 HOH A O   1 
HETATM 8597 O  O   . HOH F 6 .    ? 68.549 47.024  -16.874 1.00 25.70 ? 2385 HOH A O   1 
HETATM 8598 O  O   . HOH F 6 .    ? 66.421 62.798  -13.610 1.00 21.06 ? 2386 HOH A O   1 
HETATM 8599 O  O   . HOH F 6 .    ? 26.668 75.202  1.990   1.00 19.96 ? 2387 HOH A O   1 
HETATM 8600 O  O   . HOH F 6 .    ? 40.113 39.297  9.176   1.00 23.70 ? 2388 HOH A O   1 
HETATM 8601 O  O   . HOH F 6 .    ? 20.936 47.612  38.777  1.00 30.38 ? 2389 HOH A O   1 
HETATM 8602 O  O   . HOH F 6 .    ? 42.028 74.865  -41.506 1.00 25.91 ? 2390 HOH A O   1 
HETATM 8603 O  O   . HOH F 6 .    ? 14.327 55.967  27.129  1.00 28.08 ? 2391 HOH A O   1 
HETATM 8604 O  O   . HOH F 6 .    ? 28.642 59.731  -39.333 1.00 29.52 ? 2392 HOH A O   1 
HETATM 8605 O  O   . HOH F 6 .    ? 39.119 43.186  22.671  1.00 29.19 ? 2393 HOH A O   1 
HETATM 8606 O  O   . HOH F 6 .    ? 16.445 52.795  -22.551 1.00 30.14 ? 2394 HOH A O   1 
HETATM 8607 O  O   . HOH F 6 .    ? 27.145 35.086  29.394  1.00 23.65 ? 2395 HOH A O   1 
HETATM 8608 O  O   . HOH F 6 .    ? 17.440 80.665  -7.322  1.00 24.34 ? 2396 HOH A O   1 
HETATM 8609 O  O   . HOH F 6 .    ? 48.187 41.863  3.631   1.00 23.08 ? 2397 HOH A O   1 
HETATM 8610 O  O   . HOH F 6 .    ? 73.599 51.474  -11.357 1.00 32.84 ? 2398 HOH A O   1 
HETATM 8611 O  O   . HOH F 6 .    ? 58.734 53.703  -22.381 1.00 19.11 ? 2399 HOH A O   1 
HETATM 8612 O  O   . HOH F 6 .    ? 47.543 79.631  -18.519 1.00 24.16 ? 2400 HOH A O   1 
HETATM 8613 O  O   . HOH F 6 .    ? 40.933 96.380  -37.436 1.00 26.47 ? 2401 HOH A O   1 
HETATM 8614 O  O   . HOH F 6 .    ? 61.073 63.717  15.327  1.00 19.24 ? 2402 HOH A O   1 
HETATM 8615 O  O   . HOH F 6 .    ? 59.453 37.728  -15.334 1.00 34.81 ? 2403 HOH A O   1 
HETATM 8616 O  O   . HOH F 6 .    ? 21.021 30.260  17.702  1.00 45.16 ? 2404 HOH A O   1 
HETATM 8617 O  O   . HOH F 6 .    ? 46.170 97.126  -44.073 1.00 30.36 ? 2405 HOH A O   1 
HETATM 8618 O  O   . HOH F 6 .    ? 21.432 86.298  -19.262 1.00 28.42 ? 2406 HOH A O   1 
HETATM 8619 O  O   . HOH F 6 .    ? 20.444 68.332  22.274  1.00 20.16 ? 2407 HOH A O   1 
HETATM 8620 O  O   . HOH F 6 .    ? 45.392 69.769  -17.975 1.00 26.97 ? 2408 HOH A O   1 
HETATM 8621 O  O   . HOH F 6 .    ? 16.198 70.531  6.144   1.00 35.24 ? 2409 HOH A O   1 
HETATM 8622 O  O   . HOH F 6 .    ? 51.142 52.840  -28.768 1.00 20.10 ? 2410 HOH A O   1 
HETATM 8623 O  O   . HOH F 6 .    ? 19.160 83.618  -25.683 1.00 29.32 ? 2411 HOH A O   1 
HETATM 8624 O  O   . HOH F 6 .    ? 40.016 86.141  -22.005 1.00 30.40 ? 2412 HOH A O   1 
HETATM 8625 O  O   . HOH F 6 .    ? 22.413 66.730  28.952  1.00 33.24 ? 2413 HOH A O   1 
HETATM 8626 O  O   . HOH F 6 .    ? 24.999 59.204  -36.546 1.00 37.81 ? 2414 HOH A O   1 
HETATM 8627 O  O   . HOH F 6 .    ? 58.274 34.823  -5.869  1.00 28.58 ? 2415 HOH A O   1 
HETATM 8628 O  O   . HOH F 6 .    ? 50.377 79.083  -15.846 1.00 26.37 ? 2416 HOH A O   1 
HETATM 8629 O  O   . HOH F 6 .    ? 51.045 95.824  -26.029 1.00 45.67 ? 2417 HOH A O   1 
HETATM 8630 O  O   . HOH F 6 .    ? 56.367 92.879  -29.740 1.00 26.35 ? 2418 HOH A O   1 
HETATM 8631 O  O   . HOH F 6 .    ? 52.586 73.171  4.231   1.00 31.01 ? 2419 HOH A O   1 
HETATM 8632 O  O   . HOH F 6 .    ? 21.954 36.804  0.028   1.00 27.60 ? 2420 HOH A O   1 
HETATM 8633 O  O   . HOH F 6 .    ? 10.791 77.283  -5.327  1.00 22.71 ? 2421 HOH A O   1 
HETATM 8634 O  O   . HOH F 6 .    ? 72.734 64.074  -21.215 1.00 26.85 ? 2422 HOH A O   1 
HETATM 8635 O  O   . HOH F 6 .    ? 79.953 73.951  -17.694 1.00 36.80 ? 2423 HOH A O   1 
HETATM 8636 O  O   . HOH F 6 .    ? 66.777 74.640  -4.545  1.00 20.19 ? 2424 HOH A O   1 
HETATM 8637 O  O   . HOH F 6 .    ? 48.141 64.296  -28.621 1.00 20.19 ? 2425 HOH A O   1 
HETATM 8638 O  O   . HOH F 6 .    ? 42.483 39.295  -1.716  1.00 25.01 ? 2426 HOH A O   1 
HETATM 8639 O  O   . HOH F 6 .    ? 63.185 67.885  -31.923 1.00 28.02 ? 2427 HOH A O   1 
HETATM 8640 O  O   . HOH F 6 .    ? 24.158 42.088  -14.634 1.00 25.22 ? 2428 HOH A O   1 
HETATM 8641 O  O   . HOH F 6 .    ? 27.557 50.869  13.294  1.00 15.71 ? 2429 HOH A O   1 
HETATM 8642 O  O   . HOH F 6 .    ? 38.671 83.630  -39.891 1.00 36.19 ? 2430 HOH A O   1 
HETATM 8643 O  O   . HOH F 6 .    ? 76.605 74.080  -26.904 1.00 20.77 ? 2431 HOH A O   1 
HETATM 8644 O  O   . HOH F 6 .    ? 28.822 72.373  22.400  1.00 24.48 ? 2432 HOH A O   1 
HETATM 8645 O  O   . HOH F 6 .    ? 20.915 55.116  -35.739 1.00 31.89 ? 2433 HOH A O   1 
HETATM 8646 O  O   . HOH F 6 .    ? 23.940 57.537  38.985  1.00 30.30 ? 2434 HOH A O   1 
HETATM 8647 O  O   . HOH F 6 .    ? 23.533 82.505  -40.816 1.00 21.57 ? 2435 HOH A O   1 
HETATM 8648 O  O   . HOH F 6 .    ? 17.164 67.139  -25.824 1.00 31.07 ? 2436 HOH A O   1 
HETATM 8649 O  O   . HOH F 6 .    ? 65.971 84.748  -22.387 1.00 47.47 ? 2437 HOH A O   1 
HETATM 8650 O  O   . HOH F 6 .    ? 20.663 67.996  8.366   1.00 20.35 ? 2438 HOH A O   1 
HETATM 8651 O  O   . HOH F 6 .    ? 61.495 63.834  -31.244 1.00 35.85 ? 2439 HOH A O   1 
HETATM 8652 O  O   . HOH F 6 .    ? 9.913  59.962  6.805   1.00 43.68 ? 2440 HOH A O   1 
HETATM 8653 O  O   . HOH F 6 .    ? 31.669 85.967  -19.881 1.00 32.07 ? 2441 HOH A O   1 
HETATM 8654 O  O   . HOH F 6 .    ? 28.452 87.845  -41.694 1.00 30.04 ? 2442 HOH A O   1 
HETATM 8655 O  O   . HOH F 6 .    ? 44.780 82.531  -30.505 1.00 26.19 ? 2443 HOH A O   1 
HETATM 8656 O  O   . HOH F 6 .    ? 59.307 67.168  -34.624 1.00 31.57 ? 2444 HOH A O   1 
HETATM 8657 O  O   . HOH F 6 .    ? 70.207 56.363  -12.767 1.00 32.43 ? 2445 HOH A O   1 
HETATM 8658 O  O   . HOH F 6 .    ? 46.047 46.106  16.275  1.00 37.58 ? 2446 HOH A O   1 
HETATM 8659 O  O   . HOH F 6 .    ? 45.845 82.859  -25.486 1.00 30.07 ? 2447 HOH A O   1 
HETATM 8660 O  O   . HOH F 6 .    ? 57.029 87.600  -20.194 1.00 36.49 ? 2448 HOH A O   1 
HETATM 8661 O  O   . HOH F 6 .    ? 73.683 74.272  -5.870  1.00 21.14 ? 2449 HOH A O   1 
HETATM 8662 O  O   . HOH F 6 .    ? 19.892 43.412  33.983  1.00 30.04 ? 2450 HOH A O   1 
HETATM 8663 O  O   . HOH F 6 .    ? 79.146 51.242  -0.830  1.00 26.10 ? 2451 HOH A O   1 
HETATM 8664 O  O   . HOH F 6 .    ? 65.936 45.558  -3.395  1.00 22.67 ? 2452 HOH A O   1 
HETATM 8665 O  O   . HOH F 6 .    ? 48.349 77.684  -9.876  1.00 29.22 ? 2453 HOH A O   1 
HETATM 8666 O  O   . HOH F 6 .    ? 29.705 34.089  -1.567  1.00 31.27 ? 2454 HOH A O   1 
HETATM 8667 O  O   . HOH F 6 .    ? 16.140 74.869  -24.121 1.00 40.77 ? 2455 HOH A O   1 
HETATM 8668 O  O   . HOH F 6 .    ? 22.456 31.207  29.253  1.00 35.11 ? 2456 HOH A O   1 
HETATM 8669 O  O   . HOH F 6 .    ? 33.461 84.263  -18.385 1.00 16.80 ? 2457 HOH A O   1 
HETATM 8670 O  O   . HOH F 6 .    ? 41.290 94.845  -39.636 1.00 22.45 ? 2458 HOH A O   1 
HETATM 8671 O  O   . HOH F 6 .    ? 44.236 83.783  -27.709 1.00 21.79 ? 2459 HOH A O   1 
HETATM 8672 O  O   . HOH F 6 .    ? 30.875 57.318  4.532   1.00 16.08 ? 2460 HOH A O   1 
HETATM 8673 O  O   . HOH F 6 .    ? 66.032 66.282  -0.599  1.00 21.71 ? 2461 HOH A O   1 
HETATM 8674 O  O   . HOH F 6 .    ? 46.448 68.252  26.284  1.00 41.38 ? 2462 HOH A O   1 
HETATM 8675 O  O   . HOH F 6 .    ? 70.100 61.849  -20.861 1.00 29.23 ? 2463 HOH A O   1 
HETATM 8676 O  O   . HOH F 6 .    ? 23.589 90.896  -25.957 1.00 35.06 ? 2464 HOH A O   1 
HETATM 8677 O  O   . HOH F 6 .    ? 25.142 71.204  22.279  1.00 37.31 ? 2465 HOH A O   1 
HETATM 8678 O  O   . HOH F 6 .    ? 48.415 95.173  -26.976 1.00 25.07 ? 2466 HOH A O   1 
HETATM 8679 O  O   . HOH F 6 .    ? 62.117 80.859  -19.072 1.00 25.18 ? 2467 HOH A O   1 
HETATM 8680 O  O   . HOH F 6 .    ? 27.517 47.394  45.791  1.00 39.52 ? 2468 HOH A O   1 
HETATM 8681 O  O   . HOH F 6 .    ? 24.432 34.361  0.145   1.00 44.39 ? 2469 HOH A O   1 
HETATM 8682 O  O   . HOH F 6 .    ? 58.262 68.145  13.319  1.00 48.11 ? 2470 HOH A O   1 
HETATM 8683 O  O   . HOH F 6 .    ? 7.985  48.025  11.779  1.00 22.81 ? 2471 HOH A O   1 
HETATM 8684 O  O   . HOH F 6 .    ? 71.296 59.563  0.832   1.00 44.02 ? 2472 HOH A O   1 
HETATM 8685 O  O   . HOH F 6 .    ? 67.582 88.024  -23.493 1.00 26.32 ? 2473 HOH A O   1 
HETATM 8686 O  O   . HOH F 6 .    ? 12.221 75.190  -13.708 1.00 28.32 ? 2474 HOH A O   1 
HETATM 8687 O  O   . HOH F 6 .    ? 27.797 51.963  42.487  1.00 22.78 ? 2475 HOH A O   1 
HETATM 8688 O  O   . HOH F 6 .    ? 21.978 62.928  33.544  1.00 28.11 ? 2476 HOH A O   1 
HETATM 8689 O  O   . HOH F 6 .    ? 34.297 87.318  -10.525 1.00 27.81 ? 2477 HOH A O   1 
HETATM 8690 O  O   . HOH F 6 .    ? 30.065 36.739  29.086  1.00 28.02 ? 2478 HOH A O   1 
HETATM 8691 O  O   . HOH F 6 .    ? 8.679  49.601  5.661   1.00 49.91 ? 2479 HOH A O   1 
HETATM 8692 O  O   . HOH F 6 .    ? 42.253 67.137  29.079  1.00 29.39 ? 2480 HOH A O   1 
HETATM 8693 O  O   . HOH F 6 .    ? 72.482 75.944  -27.195 1.00 41.79 ? 2481 HOH A O   1 
HETATM 8694 O  O   . HOH F 6 .    ? 8.883  44.540  12.811  1.00 32.42 ? 2482 HOH A O   1 
HETATM 8695 O  O   . HOH F 6 .    ? 71.027 43.052  -15.330 1.00 30.19 ? 2483 HOH A O   1 
HETATM 8696 O  O   . HOH F 6 .    ? 41.598 44.794  -24.464 1.00 31.02 ? 2484 HOH A O   1 
HETATM 8697 O  O   . HOH F 6 .    ? 40.070 66.790  31.279  1.00 42.29 ? 2485 HOH A O   1 
HETATM 8698 O  O   . HOH F 6 .    ? 53.149 52.689  26.009  1.00 23.20 ? 2486 HOH A O   1 
HETATM 8699 O  O   . HOH F 6 .    ? 26.182 44.217  -27.173 1.00 44.24 ? 2487 HOH A O   1 
HETATM 8700 O  O   . HOH F 6 .    ? 19.423 52.510  -27.037 1.00 35.23 ? 2488 HOH A O   1 
HETATM 8701 O  O   . HOH F 6 .    ? 70.677 95.725  -34.877 1.00 43.10 ? 2489 HOH A O   1 
HETATM 8702 O  O   . HOH F 6 .    ? 48.044 64.683  -25.765 1.00 23.34 ? 2490 HOH A O   1 
HETATM 8703 O  O   . HOH F 6 .    ? 17.686 53.054  35.441  1.00 22.35 ? 2491 HOH A O   1 
HETATM 8704 O  O   . HOH F 6 .    ? 83.523 70.174  -20.352 1.00 25.34 ? 2492 HOH A O   1 
HETATM 8705 O  O   . HOH F 6 .    ? 43.803 79.534  -42.684 1.00 34.77 ? 2493 HOH A O   1 
HETATM 8706 O  O   . HOH F 6 .    ? 22.545 62.607  16.405  1.00 24.72 ? 2494 HOH A O   1 
HETATM 8707 O  O   . HOH F 6 .    ? 45.871 79.350  -8.198  1.00 26.47 ? 2495 HOH A O   1 
HETATM 8708 O  O   . HOH F 6 .    ? 38.787 42.028  -22.262 1.00 31.68 ? 2496 HOH A O   1 
HETATM 8709 O  O   . HOH F 6 .    ? 36.915 29.422  13.027  1.00 33.93 ? 2497 HOH A O   1 
HETATM 8710 O  O   . HOH F 6 .    ? 20.449 65.432  27.404  1.00 33.00 ? 2498 HOH A O   1 
HETATM 8711 O  O   . HOH F 6 .    ? 61.338 77.440  -13.065 1.00 21.61 ? 2499 HOH A O   1 
HETATM 8712 O  O   . HOH F 6 .    ? 27.880 49.382  38.504  1.00 24.11 ? 2500 HOH A O   1 
HETATM 8713 O  O   . HOH F 6 .    ? 29.142 40.957  -25.658 1.00 30.25 ? 2501 HOH A O   1 
HETATM 8714 O  O   . HOH F 6 .    ? 43.448 41.908  -7.618  1.00 26.40 ? 2502 HOH A O   1 
HETATM 8715 O  O   . HOH F 6 .    ? 48.925 55.130  -22.545 1.00 22.02 ? 2503 HOH A O   1 
HETATM 8716 O  O   . HOH F 6 .    ? 35.658 38.911  -16.103 1.00 27.98 ? 2504 HOH A O   1 
HETATM 8717 O  O   . HOH F 6 .    ? 58.561 51.371  22.357  1.00 24.59 ? 2505 HOH A O   1 
HETATM 8718 O  O   . HOH F 6 .    ? 46.451 80.349  -42.703 1.00 32.28 ? 2506 HOH A O   1 
HETATM 8719 O  O   . HOH F 6 .    ? 71.630 84.538  -20.203 1.00 30.12 ? 2507 HOH A O   1 
HETATM 8720 O  O   . HOH F 6 .    ? 61.308 67.500  -36.512 1.00 41.19 ? 2508 HOH A O   1 
HETATM 8721 O  O   . HOH F 6 .    ? 58.177 34.955  -12.059 1.00 36.30 ? 2509 HOH A O   1 
HETATM 8722 O  O   . HOH F 6 .    ? 21.015 79.676  -23.564 1.00 22.65 ? 2510 HOH A O   1 
HETATM 8723 O  O   . HOH F 6 .    ? 51.189 71.415  -20.342 1.00 20.30 ? 2511 HOH A O   1 
HETATM 8724 O  O   . HOH F 6 .    ? 32.266 85.230  -8.729  1.00 32.05 ? 2512 HOH A O   1 
HETATM 8725 O  O   . HOH F 6 .    ? 21.612 29.248  27.806  1.00 27.91 ? 2513 HOH A O   1 
HETATM 8726 O  O   . HOH F 6 .    ? 31.620 57.485  37.464  1.00 21.92 ? 2514 HOH A O   1 
HETATM 8727 O  O   . HOH F 6 .    ? 17.595 81.426  -17.391 1.00 43.76 ? 2515 HOH A O   1 
HETATM 8728 O  O   . HOH F 6 .    ? 22.159 80.051  -36.142 1.00 30.08 ? 2516 HOH A O   1 
HETATM 8729 O  O   . HOH F 6 .    ? 25.403 73.952  8.742   1.00 24.41 ? 2517 HOH A O   1 
HETATM 8730 O  O   . HOH F 6 .    ? 22.024 79.961  5.462   1.00 24.99 ? 2518 HOH A O   1 
HETATM 8731 O  O   . HOH F 6 .    ? 39.935 38.970  -3.504  1.00 28.48 ? 2519 HOH A O   1 
HETATM 8732 O  O   . HOH F 6 .    ? 36.915 34.979  -15.998 1.00 30.00 ? 2520 HOH A O   1 
HETATM 8733 O  O   . HOH F 6 .    ? 34.751 45.925  33.368  1.00 16.20 ? 2521 HOH A O   1 
HETATM 8734 O  O   . HOH F 6 .    ? 69.832 62.208  0.018   1.00 34.68 ? 2522 HOH A O   1 
HETATM 8735 O  O   . HOH F 6 .    ? 46.405 74.535  22.337  1.00 32.88 ? 2523 HOH A O   1 
HETATM 8736 O  O   . HOH F 6 .    ? 60.256 92.124  -28.878 1.00 22.01 ? 2524 HOH A O   1 
HETATM 8737 O  O   . HOH F 6 .    ? 37.993 62.216  35.255  1.00 31.33 ? 2525 HOH A O   1 
HETATM 8738 O  O   . HOH F 6 .    ? 62.056 83.071  -38.314 1.00 34.06 ? 2526 HOH A O   1 
HETATM 8739 O  O   . HOH F 6 .    ? 62.974 42.974  -21.049 1.00 30.43 ? 2527 HOH A O   1 
HETATM 8740 O  O   . HOH F 6 .    ? 53.147 44.737  22.696  1.00 33.16 ? 2528 HOH A O   1 
HETATM 8741 O  O   . HOH F 6 .    ? 30.820 34.737  -9.403  1.00 32.27 ? 2529 HOH A O   1 
HETATM 8742 O  O   . HOH F 6 .    ? 29.543 31.659  21.874  1.00 39.91 ? 2530 HOH A O   1 
HETATM 8743 O  O   . HOH F 6 .    ? 78.459 68.908  -12.238 1.00 27.45 ? 2531 HOH A O   1 
HETATM 8744 O  O   . HOH F 6 .    ? 31.091 69.344  -45.463 1.00 34.12 ? 2532 HOH A O   1 
HETATM 8745 O  O   . HOH F 6 .    ? 73.237 82.322  -21.568 1.00 24.93 ? 2533 HOH A O   1 
HETATM 8746 O  O   . HOH F 6 .    ? 20.421 37.835  12.043  1.00 31.17 ? 2534 HOH A O   1 
HETATM 8747 O  O   . HOH F 6 .    ? 35.236 95.101  -32.553 1.00 27.46 ? 2535 HOH A O   1 
HETATM 8748 O  O   . HOH F 6 .    ? 20.601 80.377  -33.869 1.00 38.40 ? 2536 HOH A O   1 
HETATM 8749 O  O   . HOH F 6 .    ? 49.247 91.805  -24.765 1.00 29.91 ? 2537 HOH A O   1 
HETATM 8750 O  O   . HOH F 6 .    ? 43.890 44.885  19.333  1.00 33.13 ? 2538 HOH A O   1 
HETATM 8751 O  O   . HOH F 6 .    ? 21.092 35.894  -4.805  1.00 40.42 ? 2539 HOH A O   1 
HETATM 8752 O  O   . HOH F 6 .    ? 71.211 62.997  -27.359 1.00 38.81 ? 2540 HOH A O   1 
HETATM 8753 O  O   . HOH F 6 .    ? 19.961 35.455  25.756  1.00 24.26 ? 2541 HOH A O   1 
HETATM 8754 O  O   . HOH F 6 .    ? 59.267 86.628  -46.083 1.00 35.45 ? 2542 HOH A O   1 
HETATM 8755 O  O   . HOH F 6 .    ? 28.625 69.644  -39.560 1.00 30.46 ? 2543 HOH A O   1 
HETATM 8756 O  O   . HOH F 6 .    ? 45.609 83.334  -43.427 1.00 45.73 ? 2544 HOH A O   1 
HETATM 8757 O  O   . HOH F 6 .    ? 29.713 81.970  -42.755 1.00 48.46 ? 2545 HOH A O   1 
HETATM 8758 O  O   . HOH F 6 .    ? 28.350 90.735  -42.723 1.00 34.12 ? 2546 HOH A O   1 
HETATM 8759 O  O   . HOH F 6 .    ? 20.894 41.455  34.998  1.00 38.75 ? 2547 HOH A O   1 
HETATM 8760 O  O   . HOH F 6 .    ? 39.533 31.004  12.812  1.00 52.72 ? 2548 HOH A O   1 
HETATM 8761 O  O   . HOH F 6 .    ? 62.171 85.484  -23.185 1.00 28.22 ? 2549 HOH A O   1 
HETATM 8762 O  O   . HOH F 6 .    ? 31.080 68.408  13.955  1.00 34.01 ? 2550 HOH A O   1 
HETATM 8763 O  O   . HOH F 6 .    ? 14.908 63.770  -25.673 1.00 27.86 ? 2551 HOH A O   1 
HETATM 8764 O  O   . HOH F 6 .    ? 29.795 72.424  12.323  1.00 19.67 ? 2552 HOH A O   1 
HETATM 8765 O  O   . HOH F 6 .    ? 60.630 93.254  -38.086 1.00 43.33 ? 2553 HOH A O   1 
HETATM 8766 O  O   . HOH F 6 .    ? 59.121 62.126  25.890  1.00 23.45 ? 2554 HOH A O   1 
HETATM 8767 O  O   . HOH F 6 .    ? 51.239 79.529  -1.589  1.00 40.32 ? 2555 HOH A O   1 
HETATM 8768 O  O   . HOH F 6 .    ? 59.429 91.172  -35.481 1.00 28.64 ? 2556 HOH A O   1 
HETATM 8769 O  O   . HOH F 6 .    ? 24.275 60.835  35.949  1.00 46.00 ? 2557 HOH A O   1 
HETATM 8770 O  O   . HOH F 6 .    ? 11.304 61.813  0.137   1.00 38.18 ? 2558 HOH A O   1 
HETATM 8771 O  O   . HOH F 6 .    ? 55.210 80.464  -19.529 1.00 23.12 ? 2559 HOH A O   1 
HETATM 8772 O  O   . HOH F 6 .    ? 40.837 40.452  -21.510 1.00 28.69 ? 2560 HOH A O   1 
HETATM 8773 O  O   . HOH F 6 .    ? 39.989 35.569  11.322  1.00 26.01 ? 2561 HOH A O   1 
HETATM 8774 O  O   . HOH F 6 .    ? 64.776 79.998  -9.085  1.00 40.61 ? 2562 HOH A O   1 
HETATM 8775 O  O   . HOH F 6 .    ? 73.169 43.901  -12.437 1.00 45.88 ? 2563 HOH A O   1 
HETATM 8776 O  O   . HOH F 6 .    ? 12.991 74.691  -19.126 1.00 33.60 ? 2564 HOH A O   1 
HETATM 8777 O  O   . HOH F 6 .    ? 57.334 75.744  -2.961  1.00 26.38 ? 2565 HOH A O   1 
HETATM 8778 O  O   . HOH F 6 .    ? 22.839 37.084  13.362  1.00 32.22 ? 2566 HOH A O   1 
HETATM 8779 O  O   . HOH F 6 .    ? 29.378 88.707  -26.251 1.00 10.06 ? 2567 HOH A O   1 
HETATM 8780 O  O   . HOH F 6 .    ? 37.288 33.793  5.904   1.00 40.97 ? 2568 HOH A O   1 
HETATM 8781 O  O   . HOH F 6 .    ? 34.094 70.529  -44.861 1.00 36.57 ? 2569 HOH A O   1 
HETATM 8782 O  O   . HOH F 6 .    ? 64.475 77.451  0.306   1.00 45.11 ? 2570 HOH A O   1 
HETATM 8783 O  O   . HOH F 6 .    ? 30.820 51.643  39.730  1.00 45.66 ? 2571 HOH A O   1 
HETATM 8784 O  O   . HOH F 6 .    ? 14.712 50.386  0.707   1.00 38.19 ? 2572 HOH A O   1 
HETATM 8785 O  O   . HOH F 6 .    ? 67.081 81.354  -11.472 1.00 27.78 ? 2573 HOH A O   1 
HETATM 8786 O  O   . HOH F 6 .    ? 43.621 56.941  33.439  1.00 21.34 ? 2574 HOH A O   1 
HETATM 8787 O  O   . HOH F 6 .    ? 56.407 50.090  -30.323 1.00 40.17 ? 2575 HOH A O   1 
HETATM 8788 O  O   . HOH F 6 .    ? 63.263 57.766  26.284  1.00 39.25 ? 2576 HOH A O   1 
HETATM 8789 O  O   . HOH F 6 .    ? 62.293 48.244  -21.125 1.00 40.91 ? 2577 HOH A O   1 
HETATM 8790 O  O   . HOH F 6 .    ? 26.681 91.737  -27.594 1.00 28.62 ? 2578 HOH A O   1 
HETATM 8791 O  O   . HOH F 6 .    ? 13.562 70.057  -9.784  1.00 31.80 ? 2579 HOH A O   1 
HETATM 8792 O  O   . HOH F 6 .    ? 60.526 78.770  -41.763 1.00 29.73 ? 2580 HOH A O   1 
HETATM 8793 O  O   . HOH F 6 .    ? 36.400 62.665  -38.475 1.00 31.90 ? 2581 HOH A O   1 
HETATM 8794 O  O   . HOH F 6 .    ? 37.647 80.558  -0.721  1.00 20.20 ? 2582 HOH A O   1 
HETATM 8795 O  O   . HOH F 6 .    ? 48.686 97.809  -34.090 1.00 26.27 ? 2583 HOH A O   1 
HETATM 8796 O  O   . HOH F 6 .    ? 60.444 73.283  -0.208  1.00 38.16 ? 2584 HOH A O   1 
HETATM 8797 O  O   . HOH F 6 .    ? 41.161 48.292  -29.459 1.00 46.35 ? 2585 HOH A O   1 
HETATM 8798 O  O   . HOH F 6 .    ? 63.270 52.034  -0.595  1.00 27.40 ? 2586 HOH A O   1 
HETATM 8799 O  O   . HOH F 6 .    ? 23.136 48.752  -36.126 1.00 36.23 ? 2587 HOH A O   1 
HETATM 8800 O  O   . HOH F 6 .    ? 18.315 70.957  -29.712 1.00 33.65 ? 2588 HOH A O   1 
HETATM 8801 O  O   . HOH F 6 .    ? 27.341 50.210  23.298  1.00 38.02 ? 2589 HOH A O   1 
HETATM 8802 O  O   . HOH F 6 .    ? 59.837 52.817  -30.666 1.00 32.82 ? 2590 HOH A O   1 
HETATM 8803 O  O   . HOH F 6 .    ? 33.867 47.740  36.362  1.00 40.21 ? 2591 HOH A O   1 
HETATM 8804 O  O   . HOH F 6 .    ? 27.322 82.044  3.058   1.00 22.74 ? 2592 HOH A O   1 
HETATM 8805 O  O   . HOH F 6 .    ? 53.117 71.214  -16.668 1.00 35.86 ? 2593 HOH A O   1 
HETATM 8806 O  O   . HOH F 6 .    ? 54.229 60.807  31.034  1.00 42.96 ? 2594 HOH A O   1 
HETATM 8807 O  O   . HOH F 6 .    ? 35.691 77.651  -43.240 1.00 37.91 ? 2595 HOH A O   1 
HETATM 8808 O  O   . HOH F 6 .    ? 61.001 45.416  -3.810  1.00 37.57 ? 2596 HOH A O   1 
HETATM 8809 O  O   . HOH F 6 .    ? 65.441 78.803  -5.851  1.00 23.91 ? 2597 HOH A O   1 
HETATM 8810 O  O   . HOH F 6 .    ? 49.580 50.828  32.482  1.00 21.73 ? 2598 HOH A O   1 
HETATM 8811 O  O   . HOH F 6 .    ? 17.442 45.864  -14.287 1.00 25.77 ? 2599 HOH A O   1 
HETATM 8812 O  O   . HOH F 6 .    ? 28.616 55.149  39.859  1.00 42.63 ? 2600 HOH A O   1 
HETATM 8813 O  O   . HOH F 6 .    ? 50.835 59.919  -9.051  1.00 8.39  ? 2601 HOH A O   1 
HETATM 8814 O  O   . HOH F 6 .    ? 43.823 63.095  -28.729 1.00 9.19  ? 2602 HOH A O   1 
HETATM 8815 O  O   . HOH F 6 .    ? 37.998 81.816  -31.536 1.00 10.96 ? 2603 HOH A O   1 
HETATM 8816 O  O   . HOH F 6 .    ? 32.364 39.187  -4.987  1.00 9.84  ? 2604 HOH A O   1 
HETATM 8817 O  O   . HOH F 6 .    ? 60.404 60.980  -18.268 1.00 10.82 ? 2605 HOH A O   1 
HETATM 8818 O  O   . HOH F 6 .    ? 63.238 58.619  -1.540  1.00 10.91 ? 2606 HOH A O   1 
HETATM 8819 O  O   . HOH F 6 .    ? 60.734 60.904  -3.644  1.00 11.67 ? 2607 HOH A O   1 
HETATM 8820 O  O   . HOH F 6 .    ? 46.807 74.493  7.606   1.00 10.78 ? 2608 HOH A O   1 
HETATM 8821 O  O   . HOH F 6 .    ? 54.972 57.500  -0.590  1.00 12.35 ? 2609 HOH A O   1 
HETATM 8822 O  O   . HOH F 6 .    ? 30.197 74.940  -29.344 1.00 13.94 ? 2610 HOH A O   1 
HETATM 8823 O  O   . HOH F 6 .    ? 58.918 56.766  -1.477  1.00 11.50 ? 2611 HOH A O   1 
HETATM 8824 O  O   . HOH F 6 .    ? 58.666 52.792  -0.110  1.00 14.27 ? 2612 HOH A O   1 
HETATM 8825 O  O   . HOH F 6 .    ? 63.159 61.130  -4.996  1.00 13.39 ? 2613 HOH A O   1 
HETATM 8826 O  O   . HOH F 6 .    ? 27.923 48.742  12.113  1.00 10.76 ? 2614 HOH A O   1 
HETATM 8827 O  O   . HOH F 6 .    ? 66.527 56.274  -20.320 1.00 13.53 ? 2615 HOH A O   1 
HETATM 8828 O  O   . HOH F 6 .    ? 19.830 46.863  -14.453 1.00 19.36 ? 2616 HOH A O   1 
HETATM 8829 O  O   . HOH F 6 .    ? 38.607 69.175  -38.238 1.00 13.06 ? 2617 HOH A O   1 
HETATM 8830 O  O   . HOH F 6 .    ? 33.701 60.368  23.362  1.00 20.79 ? 2618 HOH A O   1 
HETATM 8831 O  O   . HOH F 6 .    ? 39.686 55.909  3.031   1.00 10.45 ? 2619 HOH A O   1 
HETATM 8832 O  O   . HOH F 6 .    ? 24.600 61.449  9.248   1.00 18.06 ? 2620 HOH A O   1 
HETATM 8833 O  O   . HOH F 6 .    ? 16.739 57.167  12.946  1.00 16.41 ? 2621 HOH A O   1 
HETATM 8834 O  O   . HOH F 6 .    ? 39.417 69.209  -35.562 1.00 13.22 ? 2622 HOH A O   1 
HETATM 8835 O  O   . HOH F 6 .    ? 49.903 67.572  4.244   1.00 26.26 ? 2623 HOH A O   1 
HETATM 8836 O  O   . HOH F 6 .    ? 27.644 53.407  20.060  1.00 17.36 ? 2624 HOH A O   1 
HETATM 8837 O  O   . HOH F 6 .    ? 29.648 82.978  2.471   1.00 12.35 ? 2625 HOH A O   1 
HETATM 8838 O  O   . HOH F 6 .    ? 28.186 90.982  -25.411 1.00 18.43 ? 2626 HOH A O   1 
HETATM 8839 O  O   . HOH F 6 .    ? 46.095 77.687  9.474   1.00 11.79 ? 2627 HOH A O   1 
HETATM 8840 O  O   . HOH F 6 .    ? 12.560 49.309  17.619  1.00 18.54 ? 2628 HOH A O   1 
HETATM 8841 O  O   . HOH F 6 .    ? 12.357 68.564  -11.456 1.00 23.51 ? 2629 HOH A O   1 
HETATM 8842 O  O   . HOH F 6 .    ? 41.508 44.719  -6.901  1.00 18.54 ? 2630 HOH A O   1 
HETATM 8843 O  O   . HOH F 6 .    ? 45.551 67.790  -27.855 1.00 21.05 ? 2631 HOH A O   1 
HETATM 8844 O  O   . HOH F 6 .    ? 14.025 50.641  24.064  1.00 16.49 ? 2632 HOH A O   1 
HETATM 8845 O  O   . HOH F 6 .    ? 67.443 46.698  -1.535  1.00 21.76 ? 2633 HOH A O   1 
HETATM 8846 O  O   . HOH F 6 .    ? 8.984  50.433  8.024   1.00 25.02 ? 2634 HOH A O   1 
HETATM 8847 O  O   . HOH F 6 .    ? 48.447 41.001  -1.161  1.00 23.73 ? 2635 HOH A O   1 
HETATM 8848 O  O   . HOH F 6 .    ? 17.872 74.567  4.075   1.00 22.95 ? 2636 HOH A O   1 
HETATM 8849 O  O   . HOH F 6 .    ? 44.837 55.050  -18.301 1.00 13.82 ? 2637 HOH A O   1 
HETATM 8850 O  O   . HOH F 6 .    ? 83.287 66.538  -15.557 1.00 20.04 ? 2638 HOH A O   1 
HETATM 8851 O  O   . HOH F 6 .    ? 48.832 69.122  -36.936 1.00 23.22 ? 2639 HOH A O   1 
HETATM 8852 O  O   . HOH F 6 .    ? 51.713 70.211  -38.108 1.00 29.00 ? 2640 HOH A O   1 
HETATM 8853 O  O   . HOH F 6 .    ? 29.584 72.454  34.405  1.00 26.33 ? 2641 HOH A O   1 
HETATM 8854 O  O   . HOH F 6 .    ? 37.478 61.532  -32.551 1.00 27.52 ? 2642 HOH A O   1 
HETATM 8855 O  O   . HOH F 6 .    ? 57.218 48.980  21.387  1.00 22.69 ? 2643 HOH A O   1 
HETATM 8856 O  O   . HOH F 6 .    ? 42.937 59.484  -31.530 1.00 26.20 ? 2644 HOH A O   1 
HETATM 8857 O  O   . HOH F 6 .    ? 31.994 34.505  -3.167  1.00 23.67 ? 2645 HOH A O   1 
HETATM 8858 O  O   . HOH F 6 .    ? 36.954 59.090  -33.690 1.00 22.00 ? 2646 HOH A O   1 
HETATM 8859 O  O   . HOH F 6 .    ? 61.389 59.123  14.727  1.00 26.39 ? 2647 HOH A O   1 
HETATM 8860 O  O   . HOH F 6 .    ? 40.161 56.441  -19.082 1.00 28.48 ? 2648 HOH A O   1 
HETATM 8861 O  O   . HOH F 6 .    ? 61.672 76.490  -10.668 1.00 20.70 ? 2649 HOH A O   1 
HETATM 8862 O  O   . HOH F 6 .    ? 10.444 50.508  -11.268 1.00 48.59 ? 2650 HOH A O   1 
HETATM 8863 O  O   . HOH F 6 .    ? 37.595 51.579  -18.557 1.00 19.72 ? 2651 HOH A O   1 
HETATM 8864 O  O   . HOH F 6 .    ? 25.664 52.251  12.896  1.00 18.16 ? 2652 HOH A O   1 
HETATM 8865 O  O   . HOH F 6 .    ? 69.410 63.707  -28.933 1.00 25.92 ? 2653 HOH A O   1 
HETATM 8866 O  O   . HOH F 6 .    ? 72.854 66.567  -10.084 1.00 25.48 ? 2654 HOH A O   1 
HETATM 8867 O  O   . HOH F 6 .    ? 42.498 56.244  2.056   1.00 26.21 ? 2655 HOH A O   1 
HETATM 8868 O  O   . HOH F 6 .    ? 55.991 65.119  -36.231 1.00 19.11 ? 2656 HOH A O   1 
HETATM 8869 O  O   . HOH F 6 .    ? 17.824 66.252  27.925  1.00 20.09 ? 2657 HOH A O   1 
HETATM 8870 O  O   . HOH F 6 .    ? 11.693 63.674  -17.014 1.00 23.46 ? 2658 HOH A O   1 
HETATM 8871 O  O   . HOH F 6 .    ? 35.450 86.508  -18.156 1.00 25.45 ? 2659 HOH A O   1 
HETATM 8872 O  O   . HOH F 6 .    ? 9.955  60.271  -20.359 1.00 22.90 ? 2660 HOH A O   1 
HETATM 8873 O  O   . HOH F 6 .    ? 11.653 48.604  -2.557  1.00 27.69 ? 2661 HOH A O   1 
HETATM 8874 O  O   . HOH F 6 .    ? 39.902 52.957  36.233  1.00 32.13 ? 2662 HOH A O   1 
HETATM 8875 O  O   . HOH F 6 .    ? 49.753 47.496  28.923  1.00 23.67 ? 2663 HOH A O   1 
HETATM 8876 O  O   . HOH F 6 .    ? 24.126 34.590  15.234  1.00 26.92 ? 2664 HOH A O   1 
HETATM 8877 O  O   . HOH F 6 .    ? 59.285 51.070  24.921  1.00 26.01 ? 2665 HOH A O   1 
HETATM 8878 O  O   . HOH F 6 .    ? 38.028 83.082  -1.297  1.00 30.00 ? 2666 HOH A O   1 
HETATM 8879 O  O   . HOH F 6 .    ? 12.974 51.782  -12.375 1.00 31.53 ? 2667 HOH A O   1 
HETATM 8880 O  O   . HOH F 6 .    ? 48.231 50.725  35.185  1.00 39.26 ? 2668 HOH A O   1 
HETATM 8881 O  O   . HOH F 6 .    ? 48.127 41.405  -5.344  1.00 27.88 ? 2669 HOH A O   1 
HETATM 8882 O  O   . HOH F 6 .    ? 22.417 40.752  -11.301 1.00 34.05 ? 2670 HOH A O   1 
HETATM 8883 O  O   . HOH F 6 .    ? 16.148 36.486  16.476  1.00 22.56 ? 2671 HOH A O   1 
HETATM 8884 O  O   . HOH F 6 .    ? 22.341 68.172  20.444  1.00 25.19 ? 2672 HOH A O   1 
HETATM 8885 O  O   . HOH F 6 .    ? 72.040 47.041  -17.992 1.00 25.36 ? 2673 HOH A O   1 
HETATM 8886 O  O   . HOH F 6 .    ? 40.972 85.265  -12.049 1.00 21.29 ? 2674 HOH A O   1 
HETATM 8887 O  O   . HOH F 6 .    ? 57.107 46.912  15.895  1.00 24.33 ? 2675 HOH A O   1 
HETATM 8888 O  O   . HOH F 6 .    ? 51.687 64.201  24.584  1.00 19.55 ? 2676 HOH A O   1 
HETATM 8889 O  O   . HOH F 6 .    ? 56.684 58.611  1.268   1.00 30.03 ? 2677 HOH A O   1 
HETATM 8890 O  O   . HOH F 6 .    ? 57.676 58.448  5.448   1.00 35.99 ? 2678 HOH A O   1 
HETATM 8891 O  O   . HOH F 6 .    ? 74.625 64.629  -15.648 1.00 39.94 ? 2679 HOH A O   1 
HETATM 8892 O  O   . HOH F 6 .    ? 14.816 70.739  -22.970 1.00 22.66 ? 2680 HOH A O   1 
HETATM 8893 O  O   . HOH F 6 .    ? 13.052 52.165  -15.225 1.00 31.65 ? 2681 HOH A O   1 
HETATM 8894 O  O   . HOH F 6 .    ? 22.175 48.322  45.235  1.00 24.97 ? 2682 HOH A O   1 
HETATM 8895 O  O   . HOH F 6 .    ? 23.305 86.956  -32.686 1.00 32.66 ? 2683 HOH A O   1 
HETATM 8896 O  O   . HOH F 6 .    ? 66.632 81.709  -14.225 1.00 30.70 ? 2684 HOH A O   1 
HETATM 8897 O  O   . HOH F 6 .    ? 47.240 61.331  -29.052 1.00 20.50 ? 2685 HOH A O   1 
HETATM 8898 O  O   . HOH F 6 .    ? 52.680 70.876  5.510   1.00 33.14 ? 2686 HOH A O   1 
HETATM 8899 O  O   . HOH F 6 .    ? 40.806 55.778  -33.341 1.00 25.24 ? 2687 HOH A O   1 
HETATM 8900 O  O   . HOH F 6 .    ? 39.578 39.840  20.007  1.00 28.29 ? 2688 HOH A O   1 
HETATM 8901 O  O   . HOH F 6 .    ? 44.410 55.433  35.989  1.00 42.82 ? 2689 HOH A O   1 
HETATM 8902 O  O   . HOH F 6 .    ? 13.826 62.317  14.578  1.00 30.63 ? 2690 HOH A O   1 
HETATM 8903 O  O   . HOH F 6 .    ? 39.870 39.508  -0.075  1.00 33.80 ? 2691 HOH A O   1 
HETATM 8904 O  O   . HOH F 6 .    ? 31.332 70.745  22.169  1.00 45.64 ? 2692 HOH A O   1 
HETATM 8905 O  O   . HOH F 6 .    ? 27.063 41.623  -27.405 1.00 41.08 ? 2693 HOH A O   1 
HETATM 8906 O  O   . HOH F 6 .    ? 19.746 41.738  -5.052  1.00 27.31 ? 2694 HOH A O   1 
HETATM 8907 O  O   . HOH F 6 .    ? 13.527 61.175  7.442   1.00 46.69 ? 2695 HOH A O   1 
HETATM 8908 O  O   . HOH F 6 .    ? 46.785 46.026  11.582  1.00 29.12 ? 2696 HOH A O   1 
HETATM 8909 O  O   . HOH F 6 .    ? 42.895 68.497  -30.270 1.00 21.45 ? 2697 HOH A O   1 
HETATM 8910 O  O   . HOH F 6 .    ? 47.723 69.907  -16.695 1.00 28.51 ? 2698 HOH A O   1 
HETATM 8911 O  O   . HOH F 6 .    ? 58.468 93.583  -27.648 1.00 36.68 ? 2699 HOH A O   1 
HETATM 8912 O  O   . HOH F 6 .    ? 31.327 79.177  -42.789 1.00 26.75 ? 2700 HOH A O   1 
HETATM 8913 O  O   . HOH F 6 .    ? 22.260 42.657  -13.067 1.00 31.01 ? 2701 HOH A O   1 
HETATM 8914 O  O   . HOH F 6 .    ? 52.696 92.217  -23.489 1.00 34.87 ? 2702 HOH A O   1 
HETATM 8915 O  O   . HOH F 6 .    ? 59.936 51.060  20.372  1.00 25.85 ? 2703 HOH A O   1 
HETATM 8916 O  O   . HOH F 6 .    ? 14.609 51.215  32.466  1.00 25.58 ? 2704 HOH A O   1 
HETATM 8917 O  O   . HOH F 6 .    ? 26.572 66.991  19.467  1.00 33.07 ? 2705 HOH A O   1 
HETATM 8918 O  O   . HOH F 6 .    ? 11.994 41.655  19.905  1.00 30.79 ? 2706 HOH A O   1 
HETATM 8919 O  O   . HOH F 6 .    ? 69.288 77.034  -34.215 1.00 32.17 ? 2707 HOH A O   1 
HETATM 8920 O  O   . HOH F 6 .    ? 16.543 43.101  -2.535  1.00 23.52 ? 2708 HOH A O   1 
HETATM 8921 O  O   . HOH F 6 .    ? 34.335 66.249  -42.542 1.00 35.04 ? 2709 HOH A O   1 
HETATM 8922 O  O   . HOH F 6 .    ? 57.141 36.088  -14.178 1.00 31.14 ? 2710 HOH A O   1 
HETATM 8923 O  O   . HOH F 6 .    ? 37.201 37.512  2.926   1.00 26.26 ? 2711 HOH A O   1 
HETATM 8924 O  O   . HOH F 6 .    ? 51.294 66.563  8.417   1.00 27.10 ? 2712 HOH A O   1 
HETATM 8925 O  O   . HOH F 6 .    ? 10.469 51.269  21.158  1.00 31.01 ? 2713 HOH A O   1 
HETATM 8926 O  O   . HOH F 6 .    ? 30.316 87.307  -14.994 1.00 28.13 ? 2714 HOH A O   1 
HETATM 8927 O  O   . HOH F 6 .    ? 42.288 54.942  -17.328 1.00 33.25 ? 2715 HOH A O   1 
HETATM 8928 O  O   . HOH F 6 .    ? 29.619 75.705  10.979  1.00 18.55 ? 2716 HOH A O   1 
HETATM 8929 O  O   . HOH F 6 .    ? 43.158 98.264  -37.344 1.00 27.61 ? 2717 HOH A O   1 
HETATM 8930 O  O   . HOH F 6 .    ? 64.809 78.943  -1.679  1.00 29.66 ? 2718 HOH A O   1 
HETATM 8931 O  O   . HOH F 6 .    ? 43.286 40.384  -23.208 1.00 29.72 ? 2719 HOH A O   1 
HETATM 8932 O  O   . HOH F 6 .    ? 59.467 48.936  2.118   1.00 27.76 ? 2720 HOH A O   1 
HETATM 8933 O  O   . HOH F 6 .    ? 69.138 41.754  -17.119 1.00 31.62 ? 2721 HOH A O   1 
HETATM 8934 O  O   . HOH F 6 .    ? 24.515 71.893  -39.734 1.00 25.90 ? 2722 HOH A O   1 
HETATM 8935 O  O   . HOH F 6 .    ? 23.755 48.466  -24.330 1.00 37.92 ? 2723 HOH A O   1 
HETATM 8936 O  O   . HOH F 6 .    ? 47.103 68.027  -24.848 1.00 26.87 ? 2724 HOH A O   1 
HETATM 8937 O  O   . HOH F 6 .    ? 53.272 53.225  -30.094 1.00 31.96 ? 2725 HOH A O   1 
HETATM 8938 O  O   . HOH F 6 .    ? 24.902 34.290  35.664  1.00 38.05 ? 2726 HOH A O   1 
HETATM 8939 O  O   . HOH F 6 .    ? 12.973 52.323  25.753  1.00 30.52 ? 2727 HOH A O   1 
HETATM 8940 O  O   . HOH F 6 .    ? 51.606 44.423  2.842   1.00 25.25 ? 2728 HOH A O   1 
HETATM 8941 O  O   . HOH F 6 .    ? 21.827 55.264  40.203  1.00 34.49 ? 2729 HOH A O   1 
HETATM 8942 O  O   . HOH F 6 .    ? 64.122 70.704  -5.267  1.00 15.88 ? 2730 HOH A O   1 
HETATM 8943 O  O   . HOH F 6 .    ? 47.003 89.380  -23.162 1.00 45.71 ? 2731 HOH A O   1 
HETATM 8944 O  O   . HOH F 6 .    ? 7.998  53.049  -7.666  1.00 17.09 ? 2732 HOH A O   1 
HETATM 8945 O  O   . HOH F 6 .    ? 22.300 80.808  -42.612 1.00 29.55 ? 2733 HOH A O   1 
HETATM 8946 O  O   . HOH F 6 .    ? 63.683 65.448  -30.583 1.00 43.47 ? 2734 HOH A O   1 
HETATM 8947 O  O   . HOH F 6 .    ? 18.152 48.615  -19.730 1.00 28.53 ? 2735 HOH A O   1 
HETATM 8948 O  O   . HOH F 6 .    ? 59.635 76.838  -4.361  1.00 31.57 ? 2736 HOH A O   1 
HETATM 8949 O  O   . HOH F 6 .    ? 21.122 84.101  -12.465 1.00 25.88 ? 2737 HOH A O   1 
HETATM 8950 O  O   . HOH F 6 .    ? 19.015 52.698  -32.041 1.00 37.60 ? 2738 HOH A O   1 
HETATM 8951 O  O   . HOH F 6 .    ? 67.216 85.551  -36.273 1.00 35.91 ? 2739 HOH A O   1 
HETATM 8952 O  O   . HOH F 6 .    ? 64.044 89.692  -22.406 1.00 26.70 ? 2740 HOH A O   1 
HETATM 8953 O  O   . HOH F 6 .    ? 32.986 84.176  0.501   1.00 26.60 ? 2741 HOH A O   1 
HETATM 8954 O  O   . HOH F 6 .    ? 45.807 65.355  -28.638 1.00 27.51 ? 2742 HOH A O   1 
HETATM 8955 O  O   . HOH F 6 .    ? 12.886 62.085  -2.333  1.00 23.62 ? 2743 HOH A O   1 
HETATM 8956 O  O   . HOH F 6 .    ? 25.525 63.032  13.741  1.00 20.03 ? 2744 HOH A O   1 
HETATM 8957 O  O   . HOH F 6 .    ? 28.411 34.878  32.359  1.00 44.41 ? 2745 HOH A O   1 
HETATM 8958 O  O   . HOH F 6 .    ? 35.795 68.474  23.662  1.00 24.56 ? 2746 HOH A O   1 
HETATM 8959 O  O   . HOH F 6 .    ? 31.864 33.894  17.099  1.00 37.11 ? 2747 HOH A O   1 
HETATM 8960 O  O   . HOH F 6 .    ? 40.017 100.282 -32.029 1.00 35.94 ? 2748 HOH A O   1 
HETATM 8961 O  O   . HOH F 6 .    ? 54.044 82.990  -44.787 1.00 40.20 ? 2749 HOH A O   1 
HETATM 8962 O  O   . HOH F 6 .    ? 70.153 53.609  -10.495 1.00 35.38 ? 2750 HOH A O   1 
HETATM 8963 O  O   . HOH F 6 .    ? 12.490 64.768  -12.451 1.00 27.46 ? 2751 HOH A O   1 
HETATM 8964 O  O   . HOH F 6 .    ? 39.635 50.018  35.990  1.00 40.84 ? 2752 HOH A O   1 
HETATM 8965 O  O   . HOH F 6 .    ? 27.717 44.687  38.273  1.00 29.97 ? 2753 HOH A O   1 
HETATM 8966 O  O   . HOH F 6 .    ? 27.606 38.487  -22.541 1.00 45.89 ? 2754 HOH A O   1 
HETATM 8967 O  O   . HOH F 6 .    ? 72.193 95.638  -31.471 1.00 27.30 ? 2755 HOH A O   1 
HETATM 8968 O  O   . HOH F 6 .    ? 21.844 48.984  -39.312 1.00 43.32 ? 2756 HOH A O   1 
HETATM 8969 O  O   . HOH F 6 .    ? 20.697 31.675  31.423  1.00 43.99 ? 2757 HOH A O   1 
HETATM 8970 O  O   . HOH F 6 .    ? 43.068 47.598  -27.546 1.00 49.47 ? 2758 HOH A O   1 
HETATM 8971 O  O   . HOH F 6 .    ? 55.766 52.137  27.303  1.00 23.25 ? 2759 HOH A O   1 
HETATM 8972 O  O   . HOH F 6 .    ? 30.842 58.432  -40.432 1.00 40.67 ? 2760 HOH A O   1 
HETATM 8973 O  O   . HOH F 6 .    ? 18.482 43.197  27.208  1.00 36.92 ? 2761 HOH A O   1 
HETATM 8974 O  O   . HOH F 6 .    ? 62.082 81.169  -43.908 1.00 45.01 ? 2762 HOH A O   1 
HETATM 8975 O  O   . HOH F 6 .    ? 7.720  54.419  17.557  1.00 33.13 ? 2763 HOH A O   1 
HETATM 8976 O  O   . HOH F 6 .    ? 17.900 41.702  25.143  1.00 30.83 ? 2764 HOH A O   1 
HETATM 8977 O  O   . HOH F 6 .    ? 11.681 67.296  2.263   1.00 44.12 ? 2765 HOH A O   1 
HETATM 8978 O  O   . HOH F 6 .    ? 4.456  56.675  -6.490  1.00 25.43 ? 2766 HOH A O   1 
HETATM 8979 O  O   . HOH F 6 .    ? 22.238 76.767  8.595   1.00 26.35 ? 2767 HOH A O   1 
HETATM 8980 O  O   . HOH F 6 .    ? 25.804 87.704  -42.934 1.00 35.01 ? 2768 HOH A O   1 
HETATM 8981 O  O   . HOH F 6 .    ? 10.798 62.593  -11.959 1.00 35.16 ? 2769 HOH A O   1 
HETATM 8982 O  O   . HOH F 6 .    ? 37.155 39.757  26.349  1.00 45.94 ? 2770 HOH A O   1 
HETATM 8983 O  O   . HOH F 6 .    ? 23.168 88.809  -38.175 1.00 34.85 ? 2771 HOH A O   1 
HETATM 8984 O  O   . HOH F 6 .    ? 70.134 62.747  -24.277 1.00 41.57 ? 2772 HOH A O   1 
HETATM 8985 O  O   . HOH F 6 .    ? 22.702 64.403  18.391  1.00 25.25 ? 2773 HOH A O   1 
HETATM 8986 O  O   . HOH F 6 .    ? 67.056 38.439  -10.008 1.00 31.39 ? 2774 HOH A O   1 
HETATM 8987 O  O   . HOH F 6 .    ? 65.083 87.597  -41.526 1.00 44.28 ? 2775 HOH A O   1 
HETATM 8988 O  O   . HOH F 6 .    ? 20.875 65.478  -39.949 1.00 39.43 ? 2776 HOH A O   1 
HETATM 8989 O  O   . HOH F 6 .    ? 13.622 48.317  1.334   1.00 43.84 ? 2777 HOH A O   1 
HETATM 8990 O  O   . HOH F 6 .    ? 55.557 69.539  -38.309 1.00 37.97 ? 2778 HOH A O   1 
HETATM 8991 O  O   . HOH F 6 .    ? 69.700 81.919  -34.213 1.00 38.18 ? 2779 HOH A O   1 
HETATM 8992 O  O   . HOH F 6 .    ? 31.038 29.685  5.502   1.00 47.68 ? 2780 HOH A O   1 
HETATM 8993 O  O   . HOH F 6 .    ? 27.933 86.235  -14.718 1.00 18.64 ? 2781 HOH A O   1 
HETATM 8994 O  O   . HOH F 6 .    ? 66.304 50.422  0.397   1.00 44.77 ? 2782 HOH A O   1 
HETATM 8995 O  O   . HOH F 6 .    ? 28.169 63.781  13.998  1.00 20.19 ? 2783 HOH A O   1 
HETATM 8996 O  O   . HOH F 6 .    ? 52.382 72.481  18.401  1.00 24.54 ? 2784 HOH A O   1 
HETATM 8997 O  O   . HOH F 6 .    ? 46.844 75.106  -26.405 1.00 32.80 ? 2785 HOH A O   1 
HETATM 8998 O  O   . HOH F 6 .    ? 65.543 81.578  -4.439  1.00 35.24 ? 2786 HOH A O   1 
HETATM 8999 O  O   . HOH F 6 .    ? 48.365 72.372  -26.395 1.00 41.47 ? 2787 HOH A O   1 
HETATM 9000 O  O   . HOH F 6 .    ? 59.001 55.577  27.190  1.00 28.26 ? 2788 HOH A O   1 
HETATM 9001 O  O   . HOH F 6 .    ? 44.179 87.577  -16.203 1.00 45.36 ? 2789 HOH A O   1 
HETATM 9002 O  O   . HOH F 6 .    ? 63.822 76.931  -40.636 1.00 33.92 ? 2790 HOH A O   1 
HETATM 9003 O  O   . HOH F 6 .    ? 14.052 58.212  16.306  1.00 15.83 ? 2791 HOH A O   1 
HETATM 9004 O  O   . HOH F 6 .    ? 13.861 57.608  18.919  1.00 14.42 ? 2792 HOH A O   1 
HETATM 9005 O  O   . HOH F 6 .    ? 28.105 39.783  11.311  1.00 12.08 ? 2793 HOH A O   1 
HETATM 9006 O  O   . HOH F 6 .    ? 28.892 81.925  -35.824 1.00 18.91 ? 2794 HOH A O   1 
HETATM 9007 O  O   . HOH F 6 .    ? 12.449 55.930  -15.008 1.00 22.92 ? 2795 HOH A O   1 
HETATM 9008 O  O   . HOH F 6 .    ? 81.556 67.145  -13.626 1.00 23.18 ? 2796 HOH A O   1 
HETATM 9009 O  O   . HOH F 6 .    ? 58.876 58.015  0.735   1.00 28.14 ? 2797 HOH A O   1 
HETATM 9010 O  O   . HOH F 6 .    ? 49.251 68.313  6.637   1.00 22.82 ? 2798 HOH A O   1 
HETATM 9011 O  O   . HOH F 6 .    ? 68.418 79.271  -28.789 1.00 31.77 ? 2799 HOH A O   1 
HETATM 9012 O  O   . HOH F 6 .    ? 26.070 32.796  28.740  1.00 19.53 ? 2800 HOH A O   1 
HETATM 9013 O  O   . HOH F 6 .    ? 32.194 69.514  24.286  1.00 21.64 ? 2801 HOH A O   1 
HETATM 9014 O  O   . HOH F 6 .    ? 28.006 102.526 -19.126 1.00 22.54 ? 2802 HOH A O   1 
HETATM 9015 O  O   . HOH F 6 .    ? 71.659 73.809  -29.323 1.00 29.64 ? 2803 HOH A O   1 
HETATM 9016 O  O   . HOH F 6 .    ? 10.424 50.605  -8.991  1.00 25.83 ? 2804 HOH A O   1 
HETATM 9017 O  O   . HOH F 6 .    ? 37.412 83.550  -3.964  1.00 23.52 ? 2805 HOH A O   1 
HETATM 9018 O  O   . HOH F 6 .    ? 59.343 51.999  2.542   1.00 25.73 ? 2806 HOH A O   1 
HETATM 9019 O  O   . HOH F 6 .    ? 19.706 84.134  -18.291 1.00 29.47 ? 2807 HOH A O   1 
HETATM 9020 O  O   . HOH F 6 .    ? 44.014 79.234  -21.629 1.00 27.31 ? 2808 HOH A O   1 
HETATM 9021 O  O   . HOH F 6 .    ? 57.878 52.815  26.098  1.00 31.07 ? 2809 HOH A O   1 
HETATM 9022 O  O   . HOH F 6 .    ? 17.330 52.639  32.804  1.00 32.85 ? 2810 HOH A O   1 
HETATM 9023 O  O   . HOH F 6 .    ? 46.585 42.766  9.614   1.00 39.03 ? 2811 HOH A O   1 
HETATM 9024 O  O   . HOH F 6 .    ? 27.353 71.894  34.027  1.00 31.60 ? 2812 HOH A O   1 
HETATM 9025 O  O   . HOH F 6 .    ? 7.494  54.006  -10.136 1.00 29.71 ? 2813 HOH A O   1 
HETATM 9026 O  O   . HOH F 6 .    ? 50.020 46.749  -30.717 1.00 24.89 ? 2814 HOH A O   1 
HETATM 9027 O  O   . HOH F 6 .    ? 42.536 78.774  -29.527 1.00 40.04 ? 2815 HOH A O   1 
HETATM 9028 O  O   . HOH F 6 .    ? 27.826 89.032  -12.113 1.00 28.27 ? 2816 HOH A O   1 
HETATM 9029 O  O   . HOH F 6 .    ? 56.833 89.919  -43.820 1.00 41.11 ? 2817 HOH A O   1 
HETATM 9030 O  O   . HOH F 6 .    ? 20.692 64.958  -42.331 1.00 31.82 ? 2818 HOH A O   1 
HETATM 9031 O  O   . HOH F 6 .    ? 69.565 83.774  -36.181 1.00 38.51 ? 2819 HOH A O   1 
HETATM 9032 O  O   . HOH F 6 .    ? 57.868 92.977  -25.443 1.00 38.34 ? 2820 HOH A O   1 
HETATM 9033 O  O   . HOH F 6 .    ? 46.139 39.774  -0.074  1.00 31.27 ? 2821 HOH A O   1 
HETATM 9034 O  O   . HOH F 6 .    ? 37.021 37.527  24.872  1.00 37.41 ? 2822 HOH A O   1 
HETATM 9035 O  O   . HOH F 6 .    ? 52.113 68.581  4.419   1.00 34.66 ? 2823 HOH A O   1 
HETATM 9036 O  O   . HOH F 6 .    ? 15.464 76.973  -13.777 1.00 33.73 ? 2824 HOH A O   1 
HETATM 9037 O  O   . HOH F 6 .    ? 49.348 45.678  31.001  1.00 29.92 ? 2825 HOH A O   1 
HETATM 9038 O  O   . HOH F 6 .    ? 47.117 72.540  -17.737 1.00 36.43 ? 2826 HOH A O   1 
HETATM 9039 O  O   . HOH F 6 .    ? 70.594 78.107  -26.463 1.00 49.58 ? 2827 HOH A O   1 
HETATM 9040 O  O   . HOH F 6 .    ? 58.562 52.808  4.625   1.00 28.44 ? 2828 HOH A O   1 
HETATM 9041 O  O   . HOH F 6 .    ? 35.343 55.521  -34.791 1.00 28.33 ? 2829 HOH A O   1 
HETATM 9042 O  O   . HOH F 6 .    ? 41.362 82.652  -28.831 1.00 28.42 ? 2830 HOH A O   1 
HETATM 9043 O  O   . HOH F 6 .    ? 47.958 66.051  26.801  1.00 35.20 ? 2831 HOH A O   1 
HETATM 9044 O  O   . HOH F 6 .    ? 39.857 81.910  -22.156 1.00 34.88 ? 2832 HOH A O   1 
HETATM 9045 O  O   . HOH F 6 .    ? 22.178 65.590  32.490  1.00 31.48 ? 2833 HOH A O   1 
HETATM 9046 O  O   . HOH F 6 .    ? 58.770 48.976  18.868  1.00 33.21 ? 2834 HOH A O   1 
HETATM 9047 O  O   . HOH F 6 .    ? 30.948 81.349  7.481   1.00 46.62 ? 2835 HOH A O   1 
HETATM 9048 O  O   . HOH F 6 .    ? 50.298 45.144  -24.957 1.00 32.18 ? 2836 HOH A O   1 
HETATM 9049 O  O   . HOH F 6 .    ? 62.603 60.649  0.198   1.00 35.15 ? 2837 HOH A O   1 
HETATM 9050 O  O   . HOH F 6 .    ? 67.803 75.197  -35.167 1.00 40.72 ? 2838 HOH A O   1 
HETATM 9051 O  O   . HOH F 6 .    ? 22.697 39.219  -15.504 1.00 37.68 ? 2839 HOH A O   1 
HETATM 9052 O  O   . HOH F 6 .    ? 36.279 93.844  -29.730 1.00 35.41 ? 2840 HOH A O   1 
HETATM 9053 O  O   . HOH F 6 .    ? 74.034 79.945  -11.110 1.00 34.02 ? 2841 HOH A O   1 
HETATM 9054 O  O   . HOH F 6 .    ? 41.107 81.578  -3.958  1.00 46.41 ? 2842 HOH A O   1 
HETATM 9055 O  O   . HOH F 6 .    ? 13.171 62.808  11.793  1.00 35.82 ? 2843 HOH A O   1 
HETATM 9056 O  O   . HOH F 6 .    ? 56.586 75.920  0.166   1.00 39.76 ? 2844 HOH A O   1 
HETATM 9057 O  O   . HOH F 6 .    ? 74.235 51.934  1.316   1.00 36.71 ? 2845 HOH A O   1 
HETATM 9058 O  O   . HOH F 6 .    ? 21.759 61.448  -34.780 1.00 19.66 ? 2846 HOH A O   1 
HETATM 9059 O  O   . HOH F 6 .    ? 77.506 65.257  -15.024 1.00 35.16 ? 2847 HOH A O   1 
HETATM 9060 O  O   . HOH F 6 .    ? 16.791 41.878  32.068  1.00 46.86 ? 2848 HOH A O   1 
HETATM 9061 O  O   . HOH F 6 .    ? 10.221 63.051  -14.817 1.00 31.10 ? 2849 HOH A O   1 
HETATM 9062 O  O   . HOH F 6 .    ? 45.927 79.905  4.700   1.00 31.36 ? 2850 HOH A O   1 
HETATM 9063 O  O   . HOH F 6 .    ? 14.572 47.233  32.726  1.00 30.37 ? 2851 HOH A O   1 
HETATM 9064 O  O   . HOH F 6 .    ? 47.744 40.254  5.946   1.00 32.97 ? 2852 HOH A O   1 
HETATM 9065 O  O   . HOH F 6 .    ? 19.744 39.270  -3.742  1.00 39.98 ? 2853 HOH A O   1 
HETATM 9066 O  O   . HOH F 6 .    ? 25.982 58.955  -38.884 1.00 30.42 ? 2854 HOH A O   1 
HETATM 9067 O  O   . HOH F 6 .    ? 10.754 57.939  -21.044 1.00 44.38 ? 2855 HOH A O   1 
HETATM 9068 O  O   . HOH F 6 .    ? 78.031 72.187  -10.291 1.00 22.15 ? 2856 HOH A O   1 
HETATM 9069 O  O   . HOH F 6 .    ? 35.420 62.357  33.918  1.00 30.26 ? 2857 HOH A O   1 
HETATM 9070 O  O   . HOH F 6 .    ? 26.429 91.439  -31.949 1.00 40.21 ? 2858 HOH A O   1 
HETATM 9071 O  O   . HOH F 6 .    ? 49.191 41.818  8.044   1.00 31.03 ? 2859 HOH A O   1 
HETATM 9072 O  O   . HOH F 6 .    ? 44.787 92.509  -25.027 1.00 32.65 ? 2860 HOH A O   1 
HETATM 9073 O  O   . HOH F 6 .    ? 52.225 49.149  25.691  1.00 28.98 ? 2861 HOH A O   1 
HETATM 9074 O  O   . HOH F 6 .    ? 9.912  53.192  -12.158 1.00 31.93 ? 2862 HOH A O   1 
HETATM 9075 O  O   . HOH F 6 .    ? 59.169 50.867  14.793  1.00 34.09 ? 2863 HOH A O   1 
HETATM 9076 O  O   . HOH F 6 .    ? 51.984 50.636  27.230  1.00 33.12 ? 2864 HOH A O   1 
HETATM 9077 O  O   . HOH F 6 .    ? 7.532  58.242  -0.003  1.00 33.97 ? 2865 HOH A O   1 
HETATM 9078 O  O   . HOH F 6 .    ? 11.387 58.293  19.984  1.00 33.05 ? 2866 HOH A O   1 
HETATM 9079 O  O   . HOH F 6 .    ? 15.663 49.243  31.426  1.00 24.74 ? 2867 HOH A O   1 
HETATM 9080 O  O   . HOH F 6 .    ? 45.521 60.200  -31.684 1.00 33.65 ? 2868 HOH A O   1 
HETATM 9081 O  O   . HOH F 6 .    ? 5.439  57.057  6.473   1.00 29.22 ? 2869 HOH A O   1 
HETATM 9082 O  O   . HOH F 6 .    ? 47.177 81.559  -17.210 1.00 29.45 ? 2870 HOH A O   1 
HETATM 9083 O  O   . HOH F 6 .    ? 28.427 68.008  12.233  1.00 29.54 ? 2871 HOH A O   1 
HETATM 9084 O  O   . HOH F 6 .    ? 31.847 71.424  13.366  1.00 30.56 ? 2872 HOH A O   1 
HETATM 9085 O  O   . HOH F 6 .    ? 25.695 66.350  17.132  1.00 28.07 ? 2873 HOH A O   1 
HETATM 9086 O  O   . HOH F 6 .    ? 78.873 62.601  -22.973 1.00 30.04 ? 2874 HOH A O   1 
HETATM 9087 O  O   . HOH F 6 .    ? 29.492 65.980  10.575  1.00 16.73 ? 2875 HOH A O   1 
HETATM 9088 O  O   . HOH F 6 .    ? 28.500 63.513  11.126  1.00 21.44 ? 2876 HOH A O   1 
HETATM 9089 O  O   . HOH F 6 .    ? 27.840 66.496  14.508  1.00 35.81 ? 2877 HOH A O   1 
HETATM 9090 O  O   . HOH F 6 .    ? 36.473 56.548  -32.709 1.00 24.67 ? 2878 HOH A O   1 
HETATM 9091 O  O   . HOH F 6 .    ? 47.094 41.588  -14.779 1.00 20.01 ? 2879 HOH A O   1 
HETATM 9092 O  O   . HOH F 6 .    ? 24.762 33.068  6.537   1.00 23.93 ? 2880 HOH A O   1 
HETATM 9093 O  O   . HOH F 6 .    ? 25.698 36.475  -15.389 1.00 26.25 ? 2881 HOH A O   1 
HETATM 9094 O  O   . HOH F 6 .    ? 44.323 95.302  -30.552 1.00 35.57 ? 2882 HOH A O   1 
HETATM 9095 O  O   . HOH F 6 .    ? 56.595 66.983  4.970   1.00 25.48 ? 2883 HOH A O   1 
HETATM 9096 O  O   . HOH F 6 .    ? 29.890 59.220  35.151  1.00 30.81 ? 2884 HOH A O   1 
HETATM 9097 O  O   . HOH F 6 .    ? 47.400 78.394  11.641  1.00 30.46 ? 2885 HOH A O   1 
HETATM 9098 O  O   . HOH F 6 .    ? 19.696 63.005  35.040  1.00 33.08 ? 2886 HOH A O   1 
HETATM 9099 O  O   . HOH F 6 .    ? 9.985  58.071  -3.406  1.00 25.17 ? 2887 HOH A O   1 
HETATM 9100 O  O   . HOH F 6 .    ? 31.110 87.091  -3.184  1.00 34.17 ? 2888 HOH A O   1 
HETATM 9101 O  O   . HOH F 6 .    ? 18.167 59.540  31.546  1.00 26.74 ? 2889 HOH A O   1 
HETATM 9102 O  O   . HOH F 6 .    ? 41.854 40.933  27.364  1.00 36.25 ? 2890 HOH A O   1 
HETATM 9103 O  O   . HOH F 6 .    ? 57.632 48.482  25.351  1.00 28.21 ? 2891 HOH A O   1 
HETATM 9104 O  O   . HOH F 6 .    ? 15.756 73.502  5.339   1.00 28.91 ? 2892 HOH A O   1 
HETATM 9105 O  O   . HOH F 6 .    ? 31.742 96.603  -27.482 1.00 29.71 ? 2893 HOH A O   1 
HETATM 9106 O  O   . HOH F 6 .    ? 37.465 52.817  -32.287 1.00 34.66 ? 2894 HOH A O   1 
HETATM 9107 O  O   . HOH F 6 .    ? 49.540 41.188  1.133   1.00 33.90 ? 2895 HOH A O   1 
HETATM 9108 O  O   . HOH F 6 .    ? 35.262 85.226  -0.978  1.00 31.14 ? 2896 HOH A O   1 
HETATM 9109 O  O   . HOH F 6 .    ? 70.535 72.355  -34.424 1.00 35.83 ? 2897 HOH A O   1 
HETATM 9110 O  O   . HOH F 6 .    ? 13.931 88.395  -19.861 1.00 31.44 ? 2898 HOH A O   1 
HETATM 9111 O  O   . HOH F 6 .    ? 54.173 93.586  -24.919 1.00 31.24 ? 2899 HOH A O   1 
HETATM 9112 O  O   . HOH F 6 .    ? 22.009 68.251  -39.755 1.00 33.22 ? 2900 HOH A O   1 
HETATM 9113 O  O   . HOH F 6 .    ? 60.356 91.478  -31.446 1.00 30.86 ? 2901 HOH A O   1 
HETATM 9114 O  O   . HOH F 6 .    ? 52.103 69.158  9.132   1.00 33.94 ? 2902 HOH A O   1 
HETATM 9115 O  O   . HOH F 6 .    ? 11.371 62.159  5.539   1.00 31.80 ? 2903 HOH A O   1 
HETATM 9116 O  O   . HOH F 6 .    ? 21.323 63.725  14.643  1.00 35.09 ? 2904 HOH A O   1 
HETATM 9117 O  O   . HOH F 6 .    ? 40.888 83.587  -25.427 1.00 31.70 ? 2905 HOH A O   1 
HETATM 9118 O  O   . HOH F 6 .    ? 63.853 78.725  -38.027 1.00 32.34 ? 2906 HOH A O   1 
HETATM 9119 O  O   . HOH F 6 .    ? 22.277 34.584  12.692  1.00 39.14 ? 2907 HOH A O   1 
HETATM 9120 O  O   . HOH F 6 .    ? 30.577 43.466  40.338  1.00 40.05 ? 2908 HOH A O   1 
HETATM 9121 O  O   . HOH F 6 .    ? 10.996 66.139  -5.983  1.00 34.67 ? 2909 HOH A O   1 
HETATM 9122 O  O   . HOH F 6 .    ? 30.250 70.588  35.943  1.00 33.20 ? 2910 HOH A O   1 
HETATM 9123 O  O   . HOH F 6 .    ? 22.951 66.058  -43.193 1.00 34.73 ? 2911 HOH A O   1 
HETATM 9124 O  O   . HOH F 6 .    ? 63.373 59.631  16.997  1.00 27.91 ? 2912 HOH A O   1 
HETATM 9125 O  O   . HOH F 6 .    ? 49.724 58.252  -31.083 1.00 39.11 ? 2913 HOH A O   1 
HETATM 9126 O  O   . HOH F 6 .    ? 57.479 49.414  16.443  1.00 32.99 ? 2914 HOH A O   1 
HETATM 9127 O  O   . HOH F 6 .    ? 14.594 54.873  -26.339 1.00 30.99 ? 2915 HOH A O   1 
HETATM 9128 O  O   . HOH F 6 .    ? 47.425 99.740  -33.030 1.00 35.13 ? 2916 HOH A O   1 
HETATM 9129 O  O   . HOH F 6 .    ? 29.443 34.878  -16.262 1.00 40.88 ? 2917 HOH A O   1 
HETATM 9130 O  O   . HOH F 6 .    ? 60.848 61.406  13.548  1.00 39.32 ? 2918 HOH A O   1 
HETATM 9131 O  O   . HOH F 6 .    ? 26.703 99.160  -26.272 1.00 33.08 ? 2919 HOH A O   1 
HETATM 9132 O  O   . HOH F 6 .    ? 8.080  81.224  -4.501  1.00 38.53 ? 2920 HOH A O   1 
HETATM 9133 O  O   . HOH F 6 .    ? 35.452 63.382  -33.780 1.00 29.73 ? 2921 HOH A O   1 
HETATM 9134 O  O   . HOH F 6 .    ? 21.587 47.002  -34.616 1.00 38.85 ? 2922 HOH A O   1 
HETATM 9135 O  O   . HOH F 6 .    ? 14.893 73.673  -22.034 1.00 36.94 ? 2923 HOH A O   1 
HETATM 9136 O  O   . HOH F 6 .    ? 77.271 76.537  -12.240 1.00 34.44 ? 2924 HOH A O   1 
HETATM 9137 O  O   . HOH F 6 .    ? 45.124 43.516  17.744  1.00 30.48 ? 2925 HOH A O   1 
HETATM 9138 O  O   . HOH F 6 .    ? 62.767 82.698  -17.330 1.00 31.71 ? 2926 HOH A O   1 
HETATM 9139 O  O   . HOH F 6 .    ? 47.974 44.953  -30.948 1.00 34.25 ? 2927 HOH A O   1 
HETATM 9140 O  O   . HOH F 6 .    ? 33.386 32.421  -12.879 1.00 42.06 ? 2928 HOH A O   1 
HETATM 9141 O  O   . HOH F 6 .    ? 26.211 75.102  10.753  1.00 38.30 ? 2929 HOH A O   1 
HETATM 9142 O  O   . HOH F 6 .    ? 34.981 35.386  23.390  1.00 40.42 ? 2930 HOH A O   1 
HETATM 9143 O  O   . HOH F 6 .    ? 70.323 60.215  -23.040 1.00 38.82 ? 2931 HOH A O   1 
HETATM 9144 O  O   . HOH F 6 .    ? 68.099 88.403  -35.401 1.00 38.41 ? 2932 HOH A O   1 
HETATM 9145 O  O   . HOH F 6 .    ? 52.690 45.641  -27.372 1.00 40.90 ? 2933 HOH A O   1 
HETATM 9146 O  O   . HOH F 6 .    ? 24.358 63.681  11.563  1.00 41.08 ? 2934 HOH A O   1 
HETATM 9147 O  O   . HOH F 6 .    ? 14.564 39.747  12.827  1.00 32.53 ? 2935 HOH A O   1 
HETATM 9148 O  O   . HOH F 6 .    ? 33.375 57.168  -38.990 1.00 35.75 ? 2936 HOH A O   1 
HETATM 9149 O  O   . HOH F 6 .    ? 28.628 64.525  30.180  1.00 31.89 ? 2937 HOH A O   1 
HETATM 9150 O  O   . HOH F 6 .    ? 46.717 80.490  -22.471 1.00 27.85 ? 2938 HOH A O   1 
HETATM 9151 O  O   . HOH F 6 .    ? 36.339 36.212  -18.347 1.00 38.76 ? 2939 HOH A O   1 
HETATM 9152 O  O   . HOH F 6 .    ? 63.794 57.475  1.082   1.00 40.12 ? 2940 HOH A O   1 
HETATM 9153 O  O   . HOH F 6 .    ? 6.935  51.735  9.105   1.00 32.54 ? 2941 HOH A O   1 
HETATM 9154 O  O   . HOH F 6 .    ? 53.532 92.903  -40.458 1.00 38.06 ? 2942 HOH A O   1 
HETATM 9155 O  O   . HOH F 6 .    ? 64.472 49.824  -21.991 1.00 39.06 ? 2943 HOH A O   1 
HETATM 9156 O  O   . HOH F 6 .    ? 33.384 88.310  -18.942 1.00 50.62 ? 2944 HOH A O   1 
HETATM 9157 O  O   . HOH F 6 .    ? 35.341 73.644  15.101  1.00 33.06 ? 2945 HOH A O   1 
HETATM 9158 O  O   . HOH F 6 .    ? 62.591 83.140  -21.420 1.00 38.22 ? 2946 HOH A O   1 
HETATM 9159 O  O   . HOH F 6 .    ? 26.340 89.951  -21.989 1.00 41.05 ? 2947 HOH A O   1 
HETATM 9160 O  O   . HOH F 6 .    ? 53.999 45.202  -36.990 1.00 41.60 ? 2948 HOH A O   1 
HETATM 9161 O  O   . HOH F 6 .    ? 46.033 70.442  -39.780 1.00 30.97 ? 2949 HOH A O   1 
HETATM 9162 O  O   . HOH F 6 .    ? 12.722 70.908  24.867  1.00 39.40 ? 2950 HOH A O   1 
HETATM 9163 O  O   . HOH F 6 .    ? 56.058 53.366  29.902  1.00 36.50 ? 2951 HOH A O   1 
HETATM 9164 O  O   . HOH F 6 .    ? 46.612 43.087  -22.655 1.00 43.47 ? 2952 HOH A O   1 
HETATM 9165 O  O   . HOH F 6 .    ? 36.405 42.164  -26.914 1.00 46.76 ? 2953 HOH A O   1 
HETATM 9166 O  O   . HOH F 6 .    ? 21.695 35.271  34.451  1.00 40.97 ? 2954 HOH A O   1 
HETATM 9167 O  O   . HOH F 6 .    ? 19.768 81.858  -42.523 1.00 36.35 ? 2955 HOH A O   1 
HETATM 9168 O  O   . HOH F 6 .    ? 36.663 92.363  -17.866 1.00 34.09 ? 2956 HOH A O   1 
HETATM 9169 O  O   . HOH F 6 .    ? 35.572 86.006  -8.296  1.00 40.00 ? 2957 HOH A O   1 
HETATM 9170 O  O   . HOH F 6 .    ? 38.971 86.546  -41.576 1.00 27.34 ? 2958 HOH A O   1 
HETATM 9171 O  O   . HOH F 6 .    ? 22.676 48.922  -26.982 1.00 45.95 ? 2959 HOH A O   1 
HETATM 9172 O  O   . HOH F 6 .    ? 65.461 41.259  -21.093 1.00 43.04 ? 2960 HOH A O   1 
HETATM 9173 O  O   . HOH F 6 .    ? 60.343 51.476  5.989   1.00 32.17 ? 2961 HOH A O   1 
HETATM 9174 O  O   . HOH F 6 .    ? 35.000 36.240  3.150   1.00 37.73 ? 2962 HOH A O   1 
HETATM 9175 O  O   . HOH F 6 .    ? 65.046 77.068  -4.007  1.00 31.43 ? 2963 HOH A O   1 
HETATM 9176 O  O   . HOH F 6 .    ? 5.362  81.061  -3.510  1.00 33.02 ? 2964 HOH A O   1 
HETATM 9177 O  O   . HOH F 6 .    ? 40.637 35.901  8.334   1.00 45.55 ? 2965 HOH A O   1 
HETATM 9178 O  O   . HOH F 6 .    ? 24.575 87.116  -0.923  1.00 36.26 ? 2966 HOH A O   1 
HETATM 9179 O  O   . HOH F 6 .    ? 47.331 82.551  -20.189 1.00 40.84 ? 2967 HOH A O   1 
HETATM 9180 O  O   . HOH F 6 .    ? 75.554 48.215  -5.820  1.00 45.85 ? 2968 HOH A O   1 
HETATM 9181 O  O   . HOH F 6 .    ? 60.367 83.566  -16.789 1.00 46.01 ? 2969 HOH A O   1 
HETATM 9182 O  O   . HOH F 6 .    ? 74.707 77.501  -20.982 1.00 45.65 ? 2970 HOH A O   1 
HETATM 9183 O  O   . HOH F 6 .    ? 70.116 77.175  -31.718 1.00 35.28 ? 2971 HOH A O   1 
HETATM 9184 O  O   . HOH F 6 .    ? 47.318 58.105  -32.335 1.00 32.90 ? 2972 HOH A O   1 
HETATM 9185 O  O   . HOH F 6 .    ? 45.584 56.365  -32.776 1.00 35.82 ? 2973 HOH A O   1 
HETATM 9186 O  O   . HOH F 6 .    ? 36.551 66.761  25.528  1.00 27.39 ? 2974 HOH A O   1 
HETATM 9187 O  O   . HOH F 6 .    ? 9.727  53.499  21.871  1.00 39.30 ? 2975 HOH A O   1 
HETATM 9188 O  O   . HOH F 6 .    ? 43.161 69.459  -27.760 1.00 38.36 ? 2976 HOH A O   1 
HETATM 9189 O  O   . HOH F 6 .    ? 37.601 55.307  -36.521 1.00 37.13 ? 2977 HOH A O   1 
HETATM 9190 O  O   . HOH F 6 .    ? 16.231 30.890  18.064  1.00 37.17 ? 2978 HOH A O   1 
HETATM 9191 O  O   . HOH F 6 .    ? 22.648 59.916  38.421  1.00 42.50 ? 2979 HOH A O   1 
HETATM 9192 O  O   . HOH F 6 .    ? 21.543 48.726  -22.392 1.00 35.14 ? 2980 HOH A O   1 
HETATM 9193 O  O   . HOH F 6 .    ? 22.918 85.016  -17.039 1.00 37.10 ? 2981 HOH A O   1 
HETATM 9194 O  O   . HOH F 6 .    ? 30.025 89.789  -13.072 1.00 36.96 ? 2982 HOH A O   1 
HETATM 9195 O  O   . HOH F 6 .    ? 55.348 68.516  3.376   1.00 39.12 ? 2983 HOH A O   1 
HETATM 9196 O  O   . HOH F 6 .    ? 73.293 62.877  -0.764  1.00 37.80 ? 2984 HOH A O   1 
HETATM 9197 O  O   . HOH F 6 .    ? 76.754 49.911  -10.893 1.00 41.15 ? 2985 HOH A O   1 
HETATM 9198 O  O   . HOH F 6 .    ? 38.507 73.820  18.235  1.00 43.16 ? 2986 HOH A O   1 
HETATM 9199 O  O   . HOH F 6 .    ? 23.173 78.374  -42.256 1.00 38.89 ? 2987 HOH A O   1 
HETATM 9200 O  O   . HOH F 6 .    ? 10.498 62.015  -4.865  1.00 35.45 ? 2988 HOH A O   1 
HETATM 9201 O  O   . HOH F 6 .    ? 73.791 79.050  -13.479 1.00 42.17 ? 2989 HOH A O   1 
HETATM 9202 O  O   . HOH F 6 .    ? 49.978 80.998  -3.390  1.00 51.45 ? 2990 HOH A O   1 
HETATM 9203 O  O   . HOH F 6 .    ? 10.202 56.107  26.197  1.00 34.82 ? 2991 HOH A O   1 
HETATM 9204 O  O   . HOH F 6 .    ? 58.319 64.440  26.613  1.00 43.20 ? 2992 HOH A O   1 
HETATM 9205 O  O   . HOH F 6 .    ? 8.081  48.420  19.561  1.00 39.92 ? 2993 HOH A O   1 
HETATM 9206 O  O   . HOH F 6 .    ? 57.501 55.355  29.385  1.00 35.17 ? 2994 HOH A O   1 
HETATM 9207 O  O   . HOH F 6 .    ? 43.303 64.617  -31.607 1.00 36.91 ? 2995 HOH A O   1 
HETATM 9208 O  O   . HOH F 6 .    ? 50.935 90.459  -21.677 1.00 44.23 ? 2996 HOH A O   1 
HETATM 9209 O  O   . HOH F 6 .    ? 38.713 80.345  -3.204  1.00 39.13 ? 2997 HOH A O   1 
HETATM 9210 O  O   . HOH F 6 .    ? 74.607 62.805  -8.431  1.00 43.64 ? 2998 HOH A O   1 
HETATM 9211 O  O   . HOH F 6 .    ? 74.383 60.204  -9.818  1.00 35.61 ? 2999 HOH A O   1 
HETATM 9212 O  O   . HOH F 6 .    ? 61.608 55.476  27.370  1.00 38.21 ? 3000 HOH A O   1 
HETATM 9213 O  O   . HOH F 6 .    ? 14.125 68.626  5.200   1.00 38.32 ? 3001 HOH A O   1 
HETATM 9214 O  O   . HOH F 6 .    ? 51.887 60.454  28.100  1.00 35.51 ? 3002 HOH A O   1 
HETATM 9215 O  O   . HOH F 6 .    ? 18.183 36.764  5.583   1.00 34.86 ? 3003 HOH A O   1 
HETATM 9216 O  O   . HOH F 6 .    ? 64.952 87.881  -24.360 1.00 35.11 ? 3004 HOH A O   1 
HETATM 9217 O  O   . HOH F 6 .    ? 24.281 66.537  10.313  1.00 47.92 ? 3005 HOH A O   1 
HETATM 9218 O  O   . HOH F 6 .    ? 10.845 53.699  4.073   1.00 44.76 ? 3006 HOH A O   1 
HETATM 9219 O  O   . HOH F 6 .    ? 12.093 47.054  -12.038 1.00 43.02 ? 3007 HOH A O   1 
HETATM 9220 O  O   . HOH F 6 .    ? 27.020 47.535  -23.882 1.00 33.90 ? 3008 HOH A O   1 
HETATM 9221 O  O   . HOH F 6 .    ? 48.992 46.210  26.530  1.00 38.54 ? 3009 HOH A O   1 
HETATM 9222 O  O   . HOH F 6 .    ? 38.041 34.685  -6.666  1.00 46.58 ? 3010 HOH A O   1 
HETATM 9223 O  O   . HOH F 6 .    ? 32.416 31.036  16.122  1.00 37.46 ? 3011 HOH A O   1 
HETATM 9224 O  O   . HOH F 6 .    ? 39.536 38.404  -10.605 1.00 45.21 ? 3012 HOH A O   1 
HETATM 9225 O  O   . HOH F 6 .    ? 67.133 52.846  1.481   1.00 37.15 ? 3013 HOH A O   1 
HETATM 9226 O  O   . HOH F 6 .    ? 23.682 36.949  15.760  1.00 33.04 ? 3014 HOH A O   1 
HETATM 9227 O  O   . HOH F 6 .    ? 51.010 70.841  7.197   1.00 42.74 ? 3015 HOH A O   1 
HETATM 9228 O  O   . HOH F 6 .    ? 56.711 47.049  23.171  1.00 44.47 ? 3016 HOH A O   1 
HETATM 9229 O  O   . HOH F 6 .    ? 31.143 61.544  35.683  1.00 40.66 ? 3017 HOH A O   1 
HETATM 9230 O  O   . HOH F 6 .    ? 17.067 41.336  9.054   1.00 39.68 ? 3018 HOH A O   1 
HETATM 9231 O  O   . HOH F 6 .    ? 69.631 84.091  -17.873 1.00 47.05 ? 3019 HOH A O   1 
HETATM 9232 O  O   . HOH F 6 .    ? 10.241 41.836  11.951  1.00 36.37 ? 3020 HOH A O   1 
HETATM 9233 O  O   . HOH F 6 .    ? 13.073 62.398  -25.842 1.00 36.54 ? 3021 HOH A O   1 
HETATM 9234 O  O   . HOH F 6 .    ? 34.204 86.834  -44.039 1.00 35.69 ? 3022 HOH A O   1 
HETATM 9235 O  O   . HOH F 6 .    ? 31.672 57.007  -30.540 1.00 34.75 ? 3023 HOH A O   1 
HETATM 9236 O  O   . HOH F 6 .    ? 43.609 79.715  -27.718 1.00 39.13 ? 3024 HOH A O   1 
HETATM 9237 O  O   . HOH F 6 .    ? 37.796 34.999  -19.873 1.00 43.75 ? 3025 HOH A O   1 
HETATM 9238 O  O   . HOH F 6 .    ? 34.521 53.867  -33.433 1.00 45.79 ? 3026 HOH A O   1 
HETATM 9239 O  O   . HOH F 6 .    ? 43.580 92.733  -22.947 1.00 45.53 ? 3027 HOH A O   1 
HETATM 9240 O  O   . HOH F 6 .    ? 35.806 34.050  -21.916 1.00 44.64 ? 3028 HOH A O   1 
HETATM 9241 O  O   . HOH F 6 .    ? 44.794 45.665  32.288  1.00 45.66 ? 3029 HOH A O   1 
# 
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    ARG 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    SER 3    3    ?    ?   ?   A . n 
A 1 4    HIS 4    4    ?    ?   ?   A . n 
A 1 5    HIS 5    5    ?    ?   ?   A . n 
A 1 6    HIS 6    6    ?    ?   ?   A . n 
A 1 7    HIS 7    7    ?    ?   ?   A . n 
A 1 8    HIS 8    8    ?    ?   ?   A . n 
A 1 9    HIS 9    9    ?    ?   ?   A . n 
A 1 10   GLY 10   10   ?    ?   ?   A . n 
A 1 11   GLU 11   11   ?    ?   ?   A . n 
A 1 12   PHE 12   12   ?    ?   ?   A . n 
A 1 13   ASP 13   13   ?    ?   ?   A . n 
A 1 14   ASP 14   14   ?    ?   ?   A . n 
A 1 15   PRO 15   15   ?    ?   ?   A . n 
A 1 16   ILE 16   16   ?    ?   ?   A . n 
A 1 17   ARG 17   17   ?    ?   ?   A . n 
A 1 18   PRO 18   18   ?    ?   ?   A . n 
A 1 19   PRO 19   19   ?    ?   ?   A . n 
A 1 20   LEU 20   20   ?    ?   ?   A . n 
A 1 21   LYS 21   21   ?    ?   ?   A . n 
A 1 22   VAL 22   22   ?    ?   ?   A . n 
A 1 23   ALA 23   23   ?    ?   ?   A . n 
A 1 24   ARG 24   24   ?    ?   ?   A . n 
A 1 25   SER 25   25   ?    ?   ?   A . n 
A 1 26   PRO 26   26   ?    ?   ?   A . n 
A 1 27   ARG 27   27   ?    ?   ?   A . n 
A 1 28   PRO 28   28   ?    ?   ?   A . n 
A 1 29   GLY 29   29   ?    ?   ?   A . n 
A 1 30   GLN 30   30   ?    ?   ?   A . n 
A 1 31   CYS 31   31   31   CYS CYS A . n 
A 1 32   GLN 32   32   32   GLN GLN A . n 
A 1 33   ASP 33   33   33   ASP ASP A . n 
A 1 34   VAL 34   34   34   VAL VAL A . n 
A 1 35   VAL 35   35   35   VAL VAL A . n 
A 1 36   GLN 36   36   36   GLN GLN A . n 
A 1 37   ASP 37   37   37   ASP ASP A . n 
A 1 38   VAL 38   38   38   VAL VAL A . n 
A 1 39   PRO 39   39   39   PRO PRO A . n 
A 1 40   ASN 40   40   40   ASN ASN A . n 
A 1 41   VAL 41   41   41   VAL VAL A . n 
A 1 42   ASP 42   42   42   ASP ASP A . n 
A 1 43   VAL 43   43   43   VAL VAL A . n 
A 1 44   GLN 44   44   44   GLN GLN A . n 
A 1 45   MET 45   45   45   MET MET A . n 
A 1 46   LEU 46   46   46   LEU LEU A . n 
A 1 47   GLU 47   47   47   GLU GLU A . n 
A 1 48   LEU 48   48   48   LEU LEU A . n 
A 1 49   TYR 49   49   49   TYR TYR A . n 
A 1 50   ASP 50   50   50   ASP ASP A . n 
A 1 51   ARG 51   51   51   ARG ARG A . n 
A 1 52   MET 52   52   52   MET MET A . n 
A 1 53   SER 53   53   53   SER SER A . n 
A 1 54   PHE 54   54   54   PHE PHE A . n 
A 1 55   LYS 55   55   55   LYS LYS A . n 
A 1 56   ASP 56   56   56   ASP ASP A . n 
A 1 57   ILE 57   57   57   ILE ILE A . n 
A 1 58   ASP 58   58   58   ASP ASP A . n 
A 1 59   GLY 59   59   59   GLY GLY A . n 
A 1 60   GLY 60   60   60   GLY GLY A . n 
A 1 61   VAL 61   61   61   VAL VAL A . n 
A 1 62   TRP 62   62   62   TRP TRP A . n 
A 1 63   LYS 63   63   63   LYS LYS A . n 
A 1 64   GLN 64   64   64   GLN GLN A . n 
A 1 65   GLY 65   65   65   GLY GLY A . n 
A 1 66   TRP 66   66   66   TRP TRP A . n 
A 1 67   ASN 67   67   67   ASN ASN A . n 
A 1 68   ILE 68   68   68   ILE ILE A . n 
A 1 69   LYS 69   69   69   LYS LYS A . n 
A 1 70   TYR 70   70   70   TYR TYR A . n 
A 1 71   ASP 71   71   71   ASP ASP A . n 
A 1 72   PRO 72   72   72   PRO PRO A . n 
A 1 73   LEU 73   73   73   LEU LEU A . n 
A 1 74   LYS 74   74   74   LYS LYS A . n 
A 1 75   TYR 75   75   75   TYR TYR A . n 
A 1 76   ASN 76   76   76   ASN ASN A . n 
A 1 77   ALA 77   77   77   ALA ALA A . n 
A 1 78   HIS 78   78   78   HIS HIS A . n 
A 1 79   HIS 79   79   79   HIS HIS A . n 
A 1 80   LYS 80   80   80   LYS LYS A . n 
A 1 81   LEU 81   81   81   LEU LEU A . n 
A 1 82   LYS 82   82   82   LYS LYS A . n 
A 1 83   VAL 83   83   83   VAL VAL A . n 
A 1 84   PHE 84   84   84   PHE PHE A . n 
A 1 85   VAL 85   85   85   VAL VAL A . n 
A 1 86   VAL 86   86   86   VAL VAL A . n 
A 1 87   PRO 87   87   87   PRO PRO A . n 
A 1 88   HIS 88   88   88   HIS HIS A . n 
A 1 89   SER 89   89   89   SER SER A . n 
A 1 90   HIS 90   90   90   HIS HIS A . n 
A 1 91   ASN 91   91   91   ASN ASN A . n 
A 1 92   ASP 92   92   92   ASP ASP A . n 
A 1 93   PRO 93   93   93   PRO PRO A . n 
A 1 94   GLY 94   94   94   GLY GLY A . n 
A 1 95   TRP 95   95   95   TRP TRP A . n 
A 1 96   ILE 96   96   96   ILE ILE A . n 
A 1 97   GLN 97   97   97   GLN GLN A . n 
A 1 98   THR 98   98   98   THR THR A . n 
A 1 99   PHE 99   99   99   PHE PHE A . n 
A 1 100  GLU 100  100  100  GLU GLU A . n 
A 1 101  GLU 101  101  101  GLU GLU A . n 
A 1 102  TYR 102  102  102  TYR TYR A . n 
A 1 103  TYR 103  103  103  TYR TYR A . n 
A 1 104  GLN 104  104  104  GLN GLN A . n 
A 1 105  HIS 105  105  105  HIS HIS A . n 
A 1 106  ASP 106  106  106  ASP ASP A . n 
A 1 107  THR 107  107  107  THR THR A . n 
A 1 108  LYS 108  108  108  LYS LYS A . n 
A 1 109  HIS 109  109  109  HIS HIS A . n 
A 1 110  ILE 110  110  110  ILE ILE A . n 
A 1 111  LEU 111  111  111  LEU LEU A . n 
A 1 112  SER 112  112  112  SER SER A . n 
A 1 113  ASN 113  113  113  ASN ASN A . n 
A 1 114  ALA 114  114  114  ALA ALA A . n 
A 1 115  LEU 115  115  115  LEU LEU A . n 
A 1 116  ARG 116  116  116  ARG ARG A . n 
A 1 117  HIS 117  117  117  HIS HIS A . n 
A 1 118  LEU 118  118  118  LEU LEU A . n 
A 1 119  HIS 119  119  119  HIS HIS A . n 
A 1 120  ASP 120  120  120  ASP ASP A . n 
A 1 121  ASN 121  121  121  ASN ASN A . n 
A 1 122  PRO 122  122  122  PRO PRO A . n 
A 1 123  GLU 123  123  123  GLU GLU A . n 
A 1 124  MET 124  124  124  MET MET A . n 
A 1 125  LYS 125  125  125  LYS LYS A . n 
A 1 126  PHE 126  126  126  PHE PHE A . n 
A 1 127  ILE 127  127  127  ILE ILE A . n 
A 1 128  TRP 128  128  128  TRP TRP A . n 
A 1 129  ALA 129  129  129  ALA ALA A . n 
A 1 130  GLU 130  130  130  GLU GLU A . n 
A 1 131  ILE 131  131  131  ILE ILE A . n 
A 1 132  SER 132  132  132  SER SER A . n 
A 1 133  TYR 133  133  133  TYR TYR A . n 
A 1 134  PHE 134  134  134  PHE PHE A . n 
A 1 135  ALA 135  135  135  ALA ALA A . n 
A 1 136  ARG 136  136  136  ARG ARG A . n 
A 1 137  PHE 137  137  137  PHE PHE A . n 
A 1 138  TYR 138  138  138  TYR TYR A . n 
A 1 139  HIS 139  139  139  HIS HIS A . n 
A 1 140  ASP 140  140  140  ASP ASP A . n 
A 1 141  LEU 141  141  141  LEU LEU A . n 
A 1 142  GLY 142  142  142  GLY GLY A . n 
A 1 143  GLU 143  143  143  GLU GLU A . n 
A 1 144  ASN 144  144  144  ASN ASN A . n 
A 1 145  LYS 145  145  145  LYS LYS A . n 
A 1 146  LYS 146  146  146  LYS LYS A . n 
A 1 147  LEU 147  147  147  LEU LEU A . n 
A 1 148  GLN 148  148  148  GLN GLN A . n 
A 1 149  MET 149  149  149  MET MET A . n 
A 1 150  LYS 150  150  150  LYS LYS A . n 
A 1 151  SER 151  151  151  SER SER A . n 
A 1 152  ILE 152  152  152  ILE ILE A . n 
A 1 153  VAL 153  153  153  VAL VAL A . n 
A 1 154  LYS 154  154  154  LYS LYS A . n 
A 1 155  ASN 155  155  155  ASN ASN A . n 
A 1 156  GLY 156  156  156  GLY GLY A . n 
A 1 157  GLN 157  157  157  GLN GLN A . n 
A 1 158  LEU 158  158  158  LEU LEU A . n 
A 1 159  GLU 159  159  159  GLU GLU A . n 
A 1 160  PHE 160  160  160  PHE PHE A . n 
A 1 161  VAL 161  161  161  VAL VAL A . n 
A 1 162  THR 162  162  162  THR THR A . n 
A 1 163  GLY 163  163  163  GLY GLY A . n 
A 1 164  GLY 164  164  164  GLY GLY A . n 
A 1 165  TRP 165  165  165  TRP TRP A . n 
A 1 166  VAL 166  166  166  VAL VAL A . n 
A 1 167  MET 167  167  167  MET MET A . n 
A 1 168  PRO 168  168  168  PRO PRO A . n 
A 1 169  ASP 169  169  169  ASP ASP A . n 
A 1 170  GLU 170  170  170  GLU GLU A . n 
A 1 171  ALA 171  171  171  ALA ALA A . n 
A 1 172  ASN 172  172  172  ASN ASN A . n 
A 1 173  SER 173  173  173  SER SER A . n 
A 1 174  HIS 174  174  174  HIS HIS A . n 
A 1 175  TRP 175  175  175  TRP TRP A . n 
A 1 176  ARG 176  176  176  ARG ARG A . n 
A 1 177  ASN 177  177  177  ASN ASN A . n 
A 1 178  VAL 178  178  178  VAL VAL A . n 
A 1 179  LEU 179  179  179  LEU LEU A . n 
A 1 180  LEU 180  180  180  LEU LEU A . n 
A 1 181  GLN 181  181  181  GLN GLN A . n 
A 1 182  LEU 182  182  182  LEU LEU A . n 
A 1 183  THR 183  183  183  THR THR A . n 
A 1 184  GLU 184  184  184  GLU GLU A . n 
A 1 185  GLY 185  185  185  GLY GLY A . n 
A 1 186  GLN 186  186  186  GLN GLN A . n 
A 1 187  THR 187  187  187  THR THR A . n 
A 1 188  TRP 188  188  188  TRP TRP A . n 
A 1 189  LEU 189  189  189  LEU LEU A . n 
A 1 190  LYS 190  190  190  LYS LYS A . n 
A 1 191  GLN 191  191  191  GLN GLN A . n 
A 1 192  PHE 192  192  192  PHE PHE A . n 
A 1 193  MET 193  193  193  MET MET A . n 
A 1 194  ASN 194  194  194  ASN ASN A . n 
A 1 195  VAL 195  195  195  VAL VAL A . n 
A 1 196  THR 196  196  196  THR THR A . n 
A 1 197  PRO 197  197  197  PRO PRO A . n 
A 1 198  THR 198  198  198  THR THR A . n 
A 1 199  ALA 199  199  199  ALA ALA A . n 
A 1 200  SER 200  200  200  SER SER A . n 
A 1 201  TRP 201  201  201  TRP TRP A . n 
A 1 202  ALA 202  202  202  ALA ALA A . n 
A 1 203  ILE 203  203  203  ILE ILE A . n 
A 1 204  ASP 204  204  204  ASP ASP A . n 
A 1 205  PRO 205  205  205  PRO PRO A . n 
A 1 206  PHE 206  206  206  PHE PHE A . n 
A 1 207  GLY 207  207  207  GLY GLY A . n 
A 1 208  HIS 208  208  208  HIS HIS A . n 
A 1 209  SER 209  209  209  SER SER A . n 
A 1 210  PRO 210  210  210  PRO PRO A . n 
A 1 211  THR 211  211  211  THR THR A . n 
A 1 212  MET 212  212  212  MET MET A . n 
A 1 213  PRO 213  213  213  PRO PRO A . n 
A 1 214  TYR 214  214  214  TYR TYR A . n 
A 1 215  ILE 215  215  215  ILE ILE A . n 
A 1 216  LEU 216  216  216  LEU LEU A . n 
A 1 217  GLN 217  217  217  GLN GLN A . n 
A 1 218  LYS 218  218  218  LYS LYS A . n 
A 1 219  SER 219  219  219  SER SER A . n 
A 1 220  GLY 220  220  220  GLY GLY A . n 
A 1 221  PHE 221  221  221  PHE PHE A . n 
A 1 222  LYS 222  222  222  LYS LYS A . n 
A 1 223  ASN 223  223  223  ASN ASN A . n 
A 1 224  MET 224  224  224  MET MET A . n 
A 1 225  LEU 225  225  225  LEU LEU A . n 
A 1 226  ILE 226  226  226  ILE ILE A . n 
A 1 227  GLN 227  227  227  GLN GLN A . n 
A 1 228  ARG 228  228  228  ARG ARG A . n 
A 1 229  THR 229  229  229  THR THR A . n 
A 1 230  HIS 230  230  230  HIS HIS A . n 
A 1 231  TYR 231  231  231  TYR TYR A . n 
A 1 232  SER 232  232  232  SER SER A . n 
A 1 233  VAL 233  233  233  VAL VAL A . n 
A 1 234  LYS 234  234  234  LYS LYS A . n 
A 1 235  LYS 235  235  235  LYS LYS A . n 
A 1 236  GLU 236  236  236  GLU GLU A . n 
A 1 237  LEU 237  237  237  LEU LEU A . n 
A 1 238  ALA 238  238  238  ALA ALA A . n 
A 1 239  GLN 239  239  239  GLN GLN A . n 
A 1 240  GLN 240  240  240  GLN GLN A . n 
A 1 241  ARG 241  241  241  ARG ARG A . n 
A 1 242  GLN 242  242  242  GLN GLN A . n 
A 1 243  LEU 243  243  243  LEU LEU A . n 
A 1 244  GLU 244  244  244  GLU GLU A . n 
A 1 245  PHE 245  245  245  PHE PHE A . n 
A 1 246  LEU 246  246  246  LEU LEU A . n 
A 1 247  TRP 247  247  247  TRP TRP A . n 
A 1 248  ARG 248  248  248  ARG ARG A . n 
A 1 249  GLN 249  249  249  GLN GLN A . n 
A 1 250  ILE 250  250  250  ILE ILE A . n 
A 1 251  TRP 251  251  251  TRP TRP A . n 
A 1 252  ASP 252  252  252  ASP ASP A . n 
A 1 253  ASN 253  253  253  ASN ASN A . n 
A 1 254  LYS 254  254  254  LYS LYS A . n 
A 1 255  GLY 255  255  255  GLY GLY A . n 
A 1 256  ASP 256  256  256  ASP ASP A . n 
A 1 257  THR 257  257  257  THR THR A . n 
A 1 258  ALA 258  258  258  ALA ALA A . n 
A 1 259  LEU 259  259  259  LEU LEU A . n 
A 1 260  PHE 260  260  260  PHE PHE A . n 
A 1 261  THR 261  261  261  THR THR A . n 
A 1 262  HIS 262  262  262  HIS HIS A . n 
A 1 263  MET 263  263  263  MET MET A . n 
A 1 264  MET 264  264  264  MET MET A . n 
A 1 265  PRO 265  265  265  PRO PRO A . n 
A 1 266  PHE 266  266  266  PHE PHE A . n 
A 1 267  TYR 267  267  267  TYR TYR A . n 
A 1 268  SER 268  268  268  SER SER A . n 
A 1 269  TYR 269  269  269  TYR TYR A . n 
A 1 270  ASP 270  270  270  ASP ASP A . n 
A 1 271  ILE 271  271  271  ILE ILE A . n 
A 1 272  PRO 272  272  272  PRO PRO A . n 
A 1 273  HIS 273  273  273  HIS HIS A . n 
A 1 274  THR 274  274  274  THR THR A . n 
A 1 275  CYS 275  275  275  CYS CYS A . n 
A 1 276  GLY 276  276  276  GLY GLY A . n 
A 1 277  PRO 277  277  277  PRO PRO A . n 
A 1 278  ASP 278  278  278  ASP ASP A . n 
A 1 279  PRO 279  279  279  PRO PRO A . n 
A 1 280  LYS 280  280  280  LYS LYS A . n 
A 1 281  VAL 281  281  281  VAL VAL A . n 
A 1 282  CYS 282  282  282  CYS CYS A . n 
A 1 283  CYS 283  283  283  CYS CYS A . n 
A 1 284  GLN 284  284  284  GLN GLN A . n 
A 1 285  PHE 285  285  285  PHE PHE A . n 
A 1 286  ASP 286  286  286  ASP ASP A . n 
A 1 287  PHE 287  287  287  PHE PHE A . n 
A 1 288  LYS 288  288  288  LYS LYS A . n 
A 1 289  ARG 289  289  289  ARG ARG A . n 
A 1 290  MET 290  290  290  MET MET A . n 
A 1 291  GLY 291  291  291  GLY GLY A . n 
A 1 292  SER 292  292  292  SER SER A . n 
A 1 293  PHE 293  293  293  PHE PHE A . n 
A 1 294  GLY 294  294  294  GLY GLY A . n 
A 1 295  LEU 295  295  295  LEU LEU A . n 
A 1 296  SER 296  296  296  SER SER A . n 
A 1 297  CYS 297  297  297  CYS CYS A . n 
A 1 298  PRO 298  298  298  PRO PRO A . n 
A 1 299  TRP 299  299  299  TRP TRP A . n 
A 1 300  LYS 300  300  300  LYS LYS A . n 
A 1 301  VAL 301  301  301  VAL VAL A . n 
A 1 302  PRO 302  302  302  PRO PRO A . n 
A 1 303  PRO 303  303  303  PRO PRO A . n 
A 1 304  ARG 304  304  304  ARG ARG A . n 
A 1 305  THR 305  305  305  THR THR A . n 
A 1 306  ILE 306  306  306  ILE ILE A . n 
A 1 307  SER 307  307  307  SER SER A . n 
A 1 308  ASP 308  308  308  ASP ASP A . n 
A 1 309  GLN 309  309  309  GLN GLN A . n 
A 1 310  ASN 310  310  310  ASN ASN A . n 
A 1 311  VAL 311  311  311  VAL VAL A . n 
A 1 312  ALA 312  312  312  ALA ALA A . n 
A 1 313  ALA 313  313  313  ALA ALA A . n 
A 1 314  ARG 314  314  314  ARG ARG A . n 
A 1 315  SER 315  315  315  SER SER A . n 
A 1 316  ASP 316  316  316  ASP ASP A . n 
A 1 317  LEU 317  317  317  LEU LEU A . n 
A 1 318  LEU 318  318  318  LEU LEU A . n 
A 1 319  VAL 319  319  319  VAL VAL A . n 
A 1 320  ASP 320  320  320  ASP ASP A . n 
A 1 321  GLN 321  321  321  GLN GLN A . n 
A 1 322  TRP 322  322  322  TRP TRP A . n 
A 1 323  LYS 323  323  323  LYS LYS A . n 
A 1 324  LYS 324  324  324  LYS LYS A . n 
A 1 325  LYS 325  325  325  LYS LYS A . n 
A 1 326  ALA 326  326  326  ALA ALA A . n 
A 1 327  GLU 327  327  327  GLU GLU A . n 
A 1 328  LEU 328  328  328  LEU LEU A . n 
A 1 329  TYR 329  329  329  TYR TYR A . n 
A 1 330  ARG 330  330  330  ARG ARG A . n 
A 1 331  THR 331  331  331  THR THR A . n 
A 1 332  ASN 332  332  332  ASN ASN A . n 
A 1 333  VAL 333  333  333  VAL VAL A . n 
A 1 334  LEU 334  334  334  LEU LEU A . n 
A 1 335  LEU 335  335  335  LEU LEU A . n 
A 1 336  ILE 336  336  336  ILE ILE A . n 
A 1 337  PRO 337  337  337  PRO PRO A . n 
A 1 338  LEU 338  338  338  LEU LEU A . n 
A 1 339  GLY 339  339  339  GLY GLY A . n 
A 1 340  ASP 340  340  340  ASP ASP A . n 
A 1 341  ASN 341  341  341  ASN ASN A . n 
A 1 342  PHE 342  342  342  PHE PHE A . n 
A 1 343  ARG 343  343  343  ARG ARG A . n 
A 1 344  PHE 344  344  344  PHE PHE A . n 
A 1 345  LYS 345  345  345  LYS LYS A . n 
A 1 346  GLN 346  346  346  GLN GLN A . n 
A 1 347  ASN 347  347  347  ASN ASN A . n 
A 1 348  THR 348  348  348  THR THR A . n 
A 1 349  GLU 349  349  349  GLU GLU A . n 
A 1 350  TRP 350  350  350  TRP TRP A . n 
A 1 351  ASP 351  351  351  ASP ASP A . n 
A 1 352  VAL 352  352  352  VAL VAL A . n 
A 1 353  GLN 353  353  353  GLN GLN A . n 
A 1 354  ARG 354  354  354  ARG ARG A . n 
A 1 355  VAL 355  355  355  VAL VAL A . n 
A 1 356  ASN 356  356  356  ASN ASN A . n 
A 1 357  TYR 357  357  357  TYR TYR A . n 
A 1 358  GLU 358  358  358  GLU GLU A . n 
A 1 359  ARG 359  359  359  ARG ARG A . n 
A 1 360  LEU 360  360  360  LEU LEU A . n 
A 1 361  PHE 361  361  361  PHE PHE A . n 
A 1 362  GLU 362  362  362  GLU GLU A . n 
A 1 363  HIS 363  363  363  HIS HIS A . n 
A 1 364  ILE 364  364  364  ILE ILE A . n 
A 1 365  ASN 365  365  365  ASN ASN A . n 
A 1 366  SER 366  366  366  SER SER A . n 
A 1 367  GLN 367  367  367  GLN GLN A . n 
A 1 368  ALA 368  368  368  ALA ALA A . n 
A 1 369  HIS 369  369  369  HIS HIS A . n 
A 1 370  PHE 370  370  370  PHE PHE A . n 
A 1 371  ASN 371  371  371  ASN ASN A . n 
A 1 372  VAL 372  372  372  VAL VAL A . n 
A 1 373  GLN 373  373  373  GLN GLN A . n 
A 1 374  ALA 374  374  374  ALA ALA A . n 
A 1 375  GLN 375  375  375  GLN GLN A . n 
A 1 376  PHE 376  376  376  PHE PHE A . n 
A 1 377  GLY 377  377  377  GLY GLY A . n 
A 1 378  THR 378  378  378  THR THR A . n 
A 1 379  LEU 379  379  379  LEU LEU A . n 
A 1 380  GLN 380  380  380  GLN GLN A . n 
A 1 381  GLU 381  381  381  GLU GLU A . n 
A 1 382  TYR 382  382  382  TYR TYR A . n 
A 1 383  PHE 383  383  383  PHE PHE A . n 
A 1 384  ASP 384  384  384  ASP ASP A . n 
A 1 385  ALA 385  385  385  ALA ALA A . n 
A 1 386  VAL 386  386  386  VAL VAL A . n 
A 1 387  HIS 387  387  387  HIS HIS A . n 
A 1 388  GLN 388  388  388  GLN GLN A . n 
A 1 389  ALA 389  389  389  ALA ALA A . n 
A 1 390  GLU 390  390  390  GLU GLU A . n 
A 1 391  ARG 391  391  391  ARG ARG A . n 
A 1 392  ALA 392  392  392  ALA ALA A . n 
A 1 393  GLY 393  393  393  GLY GLY A . n 
A 1 394  GLN 394  394  394  GLN GLN A . n 
A 1 395  ALA 395  395  395  ALA ALA A . n 
A 1 396  GLU 396  396  396  GLU GLU A . n 
A 1 397  PHE 397  397  397  PHE PHE A . n 
A 1 398  PRO 398  398  398  PRO PRO A . n 
A 1 399  THR 399  399  399  THR THR A . n 
A 1 400  LEU 400  400  400  LEU LEU A . n 
A 1 401  SER 401  401  401  SER SER A . n 
A 1 402  GLY 402  402  402  GLY GLY A . n 
A 1 403  ASP 403  403  403  ASP ASP A . n 
A 1 404  PHE 404  404  404  PHE PHE A . n 
A 1 405  PHE 405  405  405  PHE PHE A . n 
A 1 406  THR 406  406  406  THR THR A . n 
A 1 407  TYR 407  407  407  TYR TYR A . n 
A 1 408  ALA 408  408  408  ALA ALA A . n 
A 1 409  ASP 409  409  409  ASP ASP A . n 
A 1 410  ARG 410  410  410  ARG ARG A . n 
A 1 411  SER 411  411  411  SER SER A . n 
A 1 412  ASP 412  412  412  ASP ASP A . n 
A 1 413  ASN 413  413  413  ASN ASN A . n 
A 1 414  TYR 414  414  414  TYR TYR A . n 
A 1 415  TRP 415  415  415  TRP TRP A . n 
A 1 416  SER 416  416  416  SER SER A . n 
A 1 417  GLY 417  417  417  GLY GLY A . n 
A 1 418  TYR 418  418  418  TYR TYR A . n 
A 1 419  TYR 419  419  419  TYR TYR A . n 
A 1 420  THR 420  420  420  THR THR A . n 
A 1 421  SER 421  421  421  SER SER A . n 
A 1 422  ARG 422  422  422  ARG ARG A . n 
A 1 423  PRO 423  423  423  PRO PRO A . n 
A 1 424  TYR 424  424  424  TYR TYR A . n 
A 1 425  HIS 425  425  425  HIS HIS A . n 
A 1 426  LYS 426  426  426  LYS LYS A . n 
A 1 427  ARG 427  427  427  ARG ARG A . n 
A 1 428  MET 428  428  428  MET MET A . n 
A 1 429  ASP 429  429  429  ASP ASP A . n 
A 1 430  ARG 430  430  430  ARG ARG A . n 
A 1 431  VAL 431  431  431  VAL VAL A . n 
A 1 432  LEU 432  432  432  LEU LEU A . n 
A 1 433  MET 433  433  433  MET MET A . n 
A 1 434  HIS 434  434  434  HIS HIS A . n 
A 1 435  TYR 435  435  435  TYR TYR A . n 
A 1 436  VAL 436  436  436  VAL VAL A . n 
A 1 437  ARG 437  437  437  ARG ARG A . n 
A 1 438  ALA 438  438  438  ALA ALA A . n 
A 1 439  ALA 439  439  439  ALA ALA A . n 
A 1 440  GLU 440  440  440  GLU GLU A . n 
A 1 441  MET 441  441  441  MET MET A . n 
A 1 442  LEU 442  442  442  LEU LEU A . n 
A 1 443  SER 443  443  443  SER SER A . n 
A 1 444  ALA 444  444  444  ALA ALA A . n 
A 1 445  TRP 445  445  445  TRP TRP A . n 
A 1 446  HIS 446  446  446  HIS HIS A . n 
A 1 447  SER 447  447  447  SER SER A . n 
A 1 448  TRP 448  448  448  TRP TRP A . n 
A 1 449  ASP 449  449  449  ASP ASP A . n 
A 1 450  GLY 450  450  450  GLY GLY A . n 
A 1 451  MET 451  451  451  MET MET A . n 
A 1 452  ALA 452  452  452  ALA ALA A . n 
A 1 453  ARG 453  453  453  ARG ARG A . n 
A 1 454  ILE 454  454  454  ILE ILE A . n 
A 1 455  GLU 455  455  455  GLU GLU A . n 
A 1 456  GLU 456  456  456  GLU GLU A . n 
A 1 457  ARG 457  457  457  ARG ARG A . n 
A 1 458  LEU 458  458  458  LEU LEU A . n 
A 1 459  GLU 459  459  459  GLU GLU A . n 
A 1 460  GLN 460  460  460  GLN GLN A . n 
A 1 461  ALA 461  461  461  ALA ALA A . n 
A 1 462  ARG 462  462  462  ARG ARG A . n 
A 1 463  ARG 463  463  463  ARG ARG A . n 
A 1 464  GLU 464  464  464  GLU GLU A . n 
A 1 465  LEU 465  465  465  LEU LEU A . n 
A 1 466  SER 466  466  466  SER SER A . n 
A 1 467  LEU 467  467  467  LEU LEU A . n 
A 1 468  PHE 468  468  468  PHE PHE A . n 
A 1 469  GLN 469  469  469  GLN GLN A . n 
A 1 470  HIS 470  470  470  HIS HIS A . n 
A 1 471  HIS 471  471  471  HIS HIS A . n 
A 1 472  ASP 472  472  472  ASP ASP A . n 
A 1 473  GLY 473  473  473  GLY GLY A . n 
A 1 474  ILE 474  474  474  ILE ILE A . n 
A 1 475  THR 475  475  475  THR THR A . n 
A 1 476  GLY 476  476  476  GLY GLY A . n 
A 1 477  THR 477  477  477  THR THR A . n 
A 1 478  ALA 478  478  478  ALA ALA A . n 
A 1 479  LYS 479  479  479  LYS LYS A . n 
A 1 480  THR 480  480  480  THR THR A . n 
A 1 481  HIS 481  481  481  HIS HIS A . n 
A 1 482  VAL 482  482  482  VAL VAL A . n 
A 1 483  VAL 483  483  483  VAL VAL A . n 
A 1 484  VAL 484  484  484  VAL VAL A . n 
A 1 485  ASP 485  485  485  ASP ASP A . n 
A 1 486  TYR 486  486  486  TYR TYR A . n 
A 1 487  GLU 487  487  487  GLU GLU A . n 
A 1 488  GLN 488  488  488  GLN GLN A . n 
A 1 489  ARG 489  489  489  ARG ARG A . n 
A 1 490  MET 490  490  490  MET MET A . n 
A 1 491  GLN 491  491  491  GLN GLN A . n 
A 1 492  GLU 492  492  492  GLU GLU A . n 
A 1 493  ALA 493  493  493  ALA ALA A . n 
A 1 494  LEU 494  494  494  LEU LEU A . n 
A 1 495  LYS 495  495  495  LYS LYS A . n 
A 1 496  ALA 496  496  496  ALA ALA A . n 
A 1 497  CYS 497  497  497  CYS CYS A . n 
A 1 498  GLN 498  498  498  GLN GLN A . n 
A 1 499  MET 499  499  499  MET MET A . n 
A 1 500  VAL 500  500  500  VAL VAL A . n 
A 1 501  MET 501  501  501  MET MET A . n 
A 1 502  GLN 502  502  502  GLN GLN A . n 
A 1 503  GLN 503  503  503  GLN GLN A . n 
A 1 504  SER 504  504  504  SER SER A . n 
A 1 505  VAL 505  505  505  VAL VAL A . n 
A 1 506  TYR 506  506  506  TYR TYR A . n 
A 1 507  ARG 507  507  507  ARG ARG A . n 
A 1 508  LEU 508  508  508  LEU LEU A . n 
A 1 509  LEU 509  509  509  LEU LEU A . n 
A 1 510  THR 510  510  510  THR THR A . n 
A 1 511  LYS 511  511  511  LYS LYS A . n 
A 1 512  PRO 512  512  512  PRO PRO A . n 
A 1 513  SER 513  513  513  SER SER A . n 
A 1 514  ILE 514  514  514  ILE ILE A . n 
A 1 515  TYR 515  515  515  TYR TYR A . n 
A 1 516  SER 516  516  516  SER SER A . n 
A 1 517  PRO 517  517  517  PRO PRO A . n 
A 1 518  ASP 518  518  518  ASP ASP A . n 
A 1 519  PHE 519  519  519  PHE PHE A . n 
A 1 520  SER 520  520  520  SER SER A . n 
A 1 521  PHE 521  521  521  PHE PHE A . n 
A 1 522  SER 522  522  522  SER SER A . n 
A 1 523  TYR 523  523  523  TYR TYR A . n 
A 1 524  PHE 524  524  524  PHE PHE A . n 
A 1 525  THR 525  525  525  THR THR A . n 
A 1 526  LEU 526  526  526  LEU LEU A . n 
A 1 527  ASP 527  527  527  ASP ASP A . n 
A 1 528  ASP 528  528  528  ASP ASP A . n 
A 1 529  SER 529  529  529  SER SER A . n 
A 1 530  ARG 530  530  530  ARG ARG A . n 
A 1 531  TRP 531  531  531  TRP TRP A . n 
A 1 532  PRO 532  532  532  PRO PRO A . n 
A 1 533  GLY 533  533  533  GLY GLY A . n 
A 1 534  SER 534  534  534  SER SER A . n 
A 1 535  GLY 535  535  535  GLY GLY A . n 
A 1 536  VAL 536  536  536  VAL VAL A . n 
A 1 537  GLU 537  537  537  GLU GLU A . n 
A 1 538  ASP 538  538  538  ASP ASP A . n 
A 1 539  SER 539  539  539  SER SER A . n 
A 1 540  ARG 540  540  540  ARG ARG A . n 
A 1 541  THR 541  541  541  THR THR A . n 
A 1 542  THR 542  542  542  THR THR A . n 
A 1 543  ILE 543  543  543  ILE ILE A . n 
A 1 544  ILE 544  544  544  ILE ILE A . n 
A 1 545  LEU 545  545  545  LEU LEU A . n 
A 1 546  GLY 546  546  546  GLY GLY A . n 
A 1 547  GLU 547  547  547  GLU GLU A . n 
A 1 548  ASP 548  548  548  ASP ASP A . n 
A 1 549  ILE 549  549  549  ILE ILE A . n 
A 1 550  LEU 550  550  550  LEU LEU A . n 
A 1 551  PRO 551  551  551  PRO PRO A . n 
A 1 552  SER 552  552  552  SER SER A . n 
A 1 553  LYS 553  553  553  LYS LYS A . n 
A 1 554  HIS 554  554  554  HIS HIS A . n 
A 1 555  VAL 555  555  555  VAL VAL A . n 
A 1 556  VAL 556  556  556  VAL VAL A . n 
A 1 557  MET 557  557  557  MET MET A . n 
A 1 558  HIS 558  558  558  HIS HIS A . n 
A 1 559  ASN 559  559  559  ASN ASN A . n 
A 1 560  THR 560  560  560  THR THR A . n 
A 1 561  LEU 561  561  561  LEU LEU A . n 
A 1 562  PRO 562  562  562  PRO PRO A . n 
A 1 563  HIS 563  563  563  HIS HIS A . n 
A 1 564  TRP 564  564  564  TRP TRP A . n 
A 1 565  ARG 565  565  565  ARG ARG A . n 
A 1 566  GLU 566  566  566  GLU GLU A . n 
A 1 567  GLN 567  567  567  GLN GLN A . n 
A 1 568  LEU 568  568  568  LEU LEU A . n 
A 1 569  VAL 569  569  569  VAL VAL A . n 
A 1 570  ASP 570  570  570  ASP ASP A . n 
A 1 571  PHE 571  571  571  PHE PHE A . n 
A 1 572  TYR 572  572  572  TYR TYR A . n 
A 1 573  VAL 573  573  573  VAL VAL A . n 
A 1 574  SER 574  574  574  SER SER A . n 
A 1 575  SER 575  575  575  SER SER A . n 
A 1 576  PRO 576  576  576  PRO PRO A . n 
A 1 577  PHE 577  577  577  PHE PHE A . n 
A 1 578  VAL 578  578  578  VAL VAL A . n 
A 1 579  SER 579  579  579  SER SER A . n 
A 1 580  VAL 580  580  580  VAL VAL A . n 
A 1 581  THR 581  581  581  THR THR A . n 
A 1 582  ASP 582  582  582  ASP ASP A . n 
A 1 583  LEU 583  583  583  LEU LEU A . n 
A 1 584  ALA 584  584  584  ALA ALA A . n 
A 1 585  ASN 585  585  585  ASN ASN A . n 
A 1 586  ASN 586  586  586  ASN ASN A . n 
A 1 587  PRO 587  587  587  PRO PRO A . n 
A 1 588  VAL 588  588  588  VAL VAL A . n 
A 1 589  GLU 589  589  589  GLU GLU A . n 
A 1 590  ALA 590  590  590  ALA ALA A . n 
A 1 591  GLN 591  591  591  GLN GLN A . n 
A 1 592  VAL 592  592  592  VAL VAL A . n 
A 1 593  SER 593  593  593  SER SER A . n 
A 1 594  PRO 594  594  594  PRO PRO A . n 
A 1 595  VAL 595  595  595  VAL VAL A . n 
A 1 596  TRP 596  596  596  TRP TRP A . n 
A 1 597  SER 597  597  597  SER SER A . n 
A 1 598  TRP 598  598  598  TRP TRP A . n 
A 1 599  HIS 599  599  599  HIS HIS A . n 
A 1 600  HIS 600  600  600  HIS HIS A . n 
A 1 601  ASP 601  601  601  ASP ASP A . n 
A 1 602  THR 602  602  602  THR THR A . n 
A 1 603  LEU 603  603  603  LEU LEU A . n 
A 1 604  THR 604  604  604  THR THR A . n 
A 1 605  LYS 605  605  605  LYS LYS A . n 
A 1 606  THR 606  606  606  THR THR A . n 
A 1 607  ILE 607  607  607  ILE ILE A . n 
A 1 608  HIS 608  608  608  HIS HIS A . n 
A 1 609  PRO 609  609  609  PRO PRO A . n 
A 1 610  GLN 610  610  610  GLN GLN A . n 
A 1 611  GLY 611  611  611  GLY GLY A . n 
A 1 612  SER 612  612  612  SER SER A . n 
A 1 613  THR 613  613  613  THR THR A . n 
A 1 614  THR 614  614  614  THR THR A . n 
A 1 615  LYS 615  615  615  LYS LYS A . n 
A 1 616  TYR 616  616  616  TYR TYR A . n 
A 1 617  ARG 617  617  617  ARG ARG A . n 
A 1 618  ILE 618  618  618  ILE ILE A . n 
A 1 619  ILE 619  619  619  ILE ILE A . n 
A 1 620  PHE 620  620  620  PHE PHE A . n 
A 1 621  LYS 621  621  621  LYS LYS A . n 
A 1 622  ALA 622  622  622  ALA ALA A . n 
A 1 623  ARG 623  623  623  ARG ARG A . n 
A 1 624  VAL 624  624  624  VAL VAL A . n 
A 1 625  PRO 625  625  625  PRO PRO A . n 
A 1 626  PRO 626  626  626  PRO PRO A . n 
A 1 627  MET 627  627  627  MET MET A . n 
A 1 628  GLY 628  628  628  GLY GLY A . n 
A 1 629  LEU 629  629  629  LEU LEU A . n 
A 1 630  ALA 630  630  630  ALA ALA A . n 
A 1 631  THR 631  631  631  THR THR A . n 
A 1 632  TYR 632  632  632  TYR TYR A . n 
A 1 633  VAL 633  633  633  VAL VAL A . n 
A 1 634  LEU 634  634  634  LEU LEU A . n 
A 1 635  THR 635  635  635  THR THR A . n 
A 1 636  ILE 636  636  636  ILE ILE A . n 
A 1 637  SER 637  637  637  SER SER A . n 
A 1 638  ASP 638  638  638  ASP ASP A . n 
A 1 639  SER 639  639  639  SER SER A . n 
A 1 640  LYS 640  640  640  LYS LYS A . n 
A 1 641  PRO 641  641  641  PRO PRO A . n 
A 1 642  GLU 642  642  642  GLU GLU A . n 
A 1 643  HIS 643  643  643  HIS HIS A . n 
A 1 644  THR 644  644  644  THR THR A . n 
A 1 645  SER 645  645  645  SER SER A . n 
A 1 646  TYR 646  646  646  TYR TYR A . n 
A 1 647  ALA 647  647  647  ALA ALA A . n 
A 1 648  SER 648  648  648  SER SER A . n 
A 1 649  ASN 649  649  649  ASN ASN A . n 
A 1 650  LEU 650  650  650  LEU LEU A . n 
A 1 651  LEU 651  651  651  LEU LEU A . n 
A 1 652  LEU 652  652  652  LEU LEU A . n 
A 1 653  ARG 653  653  653  ARG ARG A . n 
A 1 654  LYS 654  654  654  LYS LYS A . n 
A 1 655  ASN 655  655  655  ASN ASN A . n 
A 1 656  PRO 656  656  656  PRO PRO A . n 
A 1 657  THR 657  657  657  THR THR A . n 
A 1 658  SER 658  658  658  SER SER A . n 
A 1 659  LEU 659  659  659  LEU LEU A . n 
A 1 660  PRO 660  660  660  PRO PRO A . n 
A 1 661  LEU 661  661  661  LEU LEU A . n 
A 1 662  GLY 662  662  662  GLY GLY A . n 
A 1 663  GLN 663  663  663  GLN GLN A . n 
A 1 664  TYR 664  664  664  TYR TYR A . n 
A 1 665  PRO 665  665  665  PRO PRO A . n 
A 1 666  GLU 666  666  666  GLU GLU A . n 
A 1 667  ASP 667  667  667  ASP ASP A . n 
A 1 668  VAL 668  668  668  VAL VAL A . n 
A 1 669  LYS 669  669  669  LYS LYS A . n 
A 1 670  PHE 670  670  670  PHE PHE A . n 
A 1 671  GLY 671  671  671  GLY GLY A . n 
A 1 672  ASP 672  672  672  ASP ASP A . n 
A 1 673  PRO 673  673  673  PRO PRO A . n 
A 1 674  ARG 674  674  674  ARG ARG A . n 
A 1 675  GLU 675  675  675  GLU GLU A . n 
A 1 676  ILE 676  676  676  ILE ILE A . n 
A 1 677  SER 677  677  677  SER SER A . n 
A 1 678  LEU 678  678  678  LEU LEU A . n 
A 1 679  ARG 679  679  679  ARG ARG A . n 
A 1 680  VAL 680  680  680  VAL VAL A . n 
A 1 681  GLY 681  681  681  GLY GLY A . n 
A 1 682  ASN 682  682  682  ASN ASN A . n 
A 1 683  GLY 683  683  683  GLY GLY A . n 
A 1 684  PRO 684  684  684  PRO PRO A . n 
A 1 685  THR 685  685  685  THR THR A . n 
A 1 686  LEU 686  686  686  LEU LEU A . n 
A 1 687  ALA 687  687  687  ALA ALA A . n 
A 1 688  PHE 688  688  688  PHE PHE A . n 
A 1 689  SER 689  689  689  SER SER A . n 
A 1 690  GLU 690  690  690  GLU GLU A . n 
A 1 691  GLN 691  691  691  GLN GLN A . n 
A 1 692  GLY 692  692  692  GLY GLY A . n 
A 1 693  LEU 693  693  693  LEU LEU A . n 
A 1 694  LEU 694  694  694  LEU LEU A . n 
A 1 695  LYS 695  695  695  LYS LYS A . n 
A 1 696  SER 696  696  696  SER SER A . n 
A 1 697  ILE 697  697  697  ILE ILE A . n 
A 1 698  GLN 698  698  698  GLN GLN A . n 
A 1 699  LEU 699  699  699  LEU LEU A . n 
A 1 700  THR 700  700  700  THR THR A . n 
A 1 701  GLN 701  701  701  GLN GLN A . n 
A 1 702  ASP 702  702  702  ASP ASP A . n 
A 1 703  SER 703  703  703  SER SER A . n 
A 1 704  PRO 704  704  704  PRO PRO A . n 
A 1 705  HIS 705  705  705  HIS HIS A . n 
A 1 706  VAL 706  706  706  VAL VAL A . n 
A 1 707  PRO 707  707  707  PRO PRO A . n 
A 1 708  VAL 708  708  708  VAL VAL A . n 
A 1 709  HIS 709  709  709  HIS HIS A . n 
A 1 710  PHE 710  710  710  PHE PHE A . n 
A 1 711  LYS 711  711  711  LYS LYS A . n 
A 1 712  PHE 712  712  712  PHE PHE A . n 
A 1 713  LEU 713  713  713  LEU LEU A . n 
A 1 714  LYS 714  714  714  LYS LYS A . n 
A 1 715  TYR 715  715  715  TYR TYR A . n 
A 1 716  GLY 716  716  716  GLY GLY A . n 
A 1 717  VAL 717  717  717  VAL VAL A . n 
A 1 718  ARG 718  718  718  ARG ARG A . n 
A 1 719  SER 719  719  719  SER SER A . n 
A 1 720  HIS 720  720  720  HIS HIS A . n 
A 1 721  GLY 721  721  721  GLY GLY A . n 
A 1 722  ASP 722  722  722  ASP ASP A . n 
A 1 723  ARG 723  723  723  ARG ARG A . n 
A 1 724  SER 724  724  724  SER SER A . n 
A 1 725  GLY 725  725  725  GLY GLY A . n 
A 1 726  ALA 726  726  726  ALA ALA A . n 
A 1 727  TYR 727  727  727  TYR TYR A . n 
A 1 728  LEU 728  728  728  LEU LEU A . n 
A 1 729  PHE 729  729  729  PHE PHE A . n 
A 1 730  LEU 730  730  730  LEU LEU A . n 
A 1 731  PRO 731  731  731  PRO PRO A . n 
A 1 732  ASN 732  732  732  ASN ASN A . n 
A 1 733  GLY 733  733  733  GLY GLY A . n 
A 1 734  PRO 734  734  734  PRO PRO A . n 
A 1 735  ALA 735  735  735  ALA ALA A . n 
A 1 736  SER 736  736  736  SER SER A . n 
A 1 737  PRO 737  737  737  PRO PRO A . n 
A 1 738  VAL 738  738  738  VAL VAL A . n 
A 1 739  GLU 739  739  739  GLU GLU A . n 
A 1 740  LEU 740  740  740  LEU LEU A . n 
A 1 741  GLY 741  741  741  GLY GLY A . n 
A 1 742  GLN 742  742  742  GLN GLN A . n 
A 1 743  PRO 743  743  743  PRO PRO A . n 
A 1 744  VAL 744  744  744  VAL VAL A . n 
A 1 745  VAL 745  745  745  VAL VAL A . n 
A 1 746  LEU 746  746  746  LEU LEU A . n 
A 1 747  VAL 747  747  747  VAL VAL A . n 
A 1 748  THR 748  748  748  THR THR A . n 
A 1 749  LYS 749  749  749  LYS LYS A . n 
A 1 750  GLY 750  750  750  GLY GLY A . n 
A 1 751  LYS 751  751  751  LYS LYS A . n 
A 1 752  LEU 752  752  752  LEU LEU A . n 
A 1 753  GLU 753  753  753  GLU GLU A . n 
A 1 754  SER 754  754  754  SER SER A . n 
A 1 755  SER 755  755  755  SER SER A . n 
A 1 756  VAL 756  756  756  VAL VAL A . n 
A 1 757  SER 757  757  757  SER SER A . n 
A 1 758  VAL 758  758  758  VAL VAL A . n 
A 1 759  GLY 759  759  759  GLY GLY A . n 
A 1 760  LEU 760  760  760  LEU LEU A . n 
A 1 761  PRO 761  761  761  PRO PRO A . n 
A 1 762  SER 762  762  762  SER SER A . n 
A 1 763  VAL 763  763  763  VAL VAL A . n 
A 1 764  VAL 764  764  764  VAL VAL A . n 
A 1 765  HIS 765  765  765  HIS HIS A . n 
A 1 766  GLN 766  766  766  GLN GLN A . n 
A 1 767  THR 767  767  767  THR THR A . n 
A 1 768  ILE 768  768  768  ILE ILE A . n 
A 1 769  MET 769  769  769  MET MET A . n 
A 1 770  ARG 770  770  770  ARG ARG A . n 
A 1 771  GLY 771  771  771  GLY GLY A . n 
A 1 772  GLY 772  772  772  GLY GLY A . n 
A 1 773  ALA 773  773  773  ALA ALA A . n 
A 1 774  PRO 774  774  774  PRO PRO A . n 
A 1 775  GLU 775  775  775  GLU GLU A . n 
A 1 776  ILE 776  776  776  ILE ILE A . n 
A 1 777  ARG 777  777  777  ARG ARG A . n 
A 1 778  ASN 778  778  778  ASN ASN A . n 
A 1 779  LEU 779  779  779  LEU LEU A . n 
A 1 780  VAL 780  780  780  VAL VAL A . n 
A 1 781  ASP 781  781  781  ASP ASP A . n 
A 1 782  ILE 782  782  782  ILE ILE A . n 
A 1 783  GLY 783  783  783  GLY GLY A . n 
A 1 784  SER 784  784  784  SER SER A . n 
A 1 785  LEU 785  785  785  LEU LEU A . n 
A 1 786  ASP 786  786  786  ASP ASP A . n 
A 1 787  ASN 787  787  787  ASN ASN A . n 
A 1 788  THR 788  788  788  THR THR A . n 
A 1 789  GLU 789  789  789  GLU GLU A . n 
A 1 790  ILE 790  790  790  ILE ILE A . n 
A 1 791  VAL 791  791  791  VAL VAL A . n 
A 1 792  MET 792  792  792  MET MET A . n 
A 1 793  ARG 793  793  793  ARG ARG A . n 
A 1 794  LEU 794  794  794  LEU LEU A . n 
A 1 795  GLU 795  795  795  GLU GLU A . n 
A 1 796  THR 796  796  796  THR THR A . n 
A 1 797  HIS 797  797  797  HIS HIS A . n 
A 1 798  ILE 798  798  798  ILE ILE A . n 
A 1 799  ASP 799  799  799  ASP ASP A . n 
A 1 800  SER 800  800  800  SER SER A . n 
A 1 801  GLY 801  801  801  GLY GLY A . n 
A 1 802  ASP 802  802  802  ASP ASP A . n 
A 1 803  ILE 803  803  803  ILE ILE A . n 
A 1 804  PHE 804  804  804  PHE PHE A . n 
A 1 805  TYR 805  805  805  TYR TYR A . n 
A 1 806  THR 806  806  806  THR THR A . n 
A 1 807  ASP 807  807  807  ASP ASP A . n 
A 1 808  LEU 808  808  808  LEU LEU A . n 
A 1 809  ASN 809  809  809  ASN ASN A . n 
A 1 810  GLY 810  810  810  GLY GLY A . n 
A 1 811  LEU 811  811  811  LEU LEU A . n 
A 1 812  GLN 812  812  812  GLN GLN A . n 
A 1 813  PHE 813  813  813  PHE PHE A . n 
A 1 814  ILE 814  814  814  ILE ILE A . n 
A 1 815  LYS 815  815  815  LYS LYS A . n 
A 1 816  ARG 816  816  816  ARG ARG A . n 
A 1 817  ARG 817  817  817  ARG ARG A . n 
A 1 818  ARG 818  818  818  ARG ARG A . n 
A 1 819  LEU 819  819  819  LEU LEU A . n 
A 1 820  ASP 820  820  820  ASP ASP A . n 
A 1 821  LYS 821  821  821  LYS LYS A . n 
A 1 822  LEU 822  822  822  LEU LEU A . n 
A 1 823  PRO 823  823  823  PRO PRO A . n 
A 1 824  LEU 824  824  824  LEU LEU A . n 
A 1 825  GLN 825  825  825  GLN GLN A . n 
A 1 826  ALA 826  826  826  ALA ALA A . n 
A 1 827  ASN 827  827  827  ASN ASN A . n 
A 1 828  TYR 828  828  828  TYR TYR A . n 
A 1 829  TYR 829  829  829  TYR TYR A . n 
A 1 830  PRO 830  830  830  PRO PRO A . n 
A 1 831  ILE 831  831  831  ILE ILE A . n 
A 1 832  PRO 832  832  832  PRO PRO A . n 
A 1 833  SER 833  833  833  SER SER A . n 
A 1 834  GLY 834  834  834  GLY GLY A . n 
A 1 835  MET 835  835  835  MET MET A . n 
A 1 836  PHE 836  836  836  PHE PHE A . n 
A 1 837  ILE 837  837  837  ILE ILE A . n 
A 1 838  GLU 838  838  838  GLU GLU A . n 
A 1 839  ASP 839  839  839  ASP ASP A . n 
A 1 840  ALA 840  840  840  ALA ALA A . n 
A 1 841  ASN 841  841  841  ASN ASN A . n 
A 1 842  THR 842  842  842  THR THR A . n 
A 1 843  ARG 843  843  843  ARG ARG A . n 
A 1 844  LEU 844  844  844  LEU LEU A . n 
A 1 845  THR 845  845  845  THR THR A . n 
A 1 846  LEU 846  846  846  LEU LEU A . n 
A 1 847  LEU 847  847  847  LEU LEU A . n 
A 1 848  THR 848  848  848  THR THR A . n 
A 1 849  GLY 849  849  849  GLY GLY A . n 
A 1 850  GLN 850  850  850  GLN GLN A . n 
A 1 851  PRO 851  851  851  PRO PRO A . n 
A 1 852  LEU 852  852  852  LEU LEU A . n 
A 1 853  GLY 853  853  853  GLY GLY A . n 
A 1 854  GLY 854  854  854  GLY GLY A . n 
A 1 855  SER 855  855  855  SER SER A . n 
A 1 856  SER 856  856  856  SER SER A . n 
A 1 857  LEU 857  857  857  LEU LEU A . n 
A 1 858  ALA 858  858  858  ALA ALA A . n 
A 1 859  SER 859  859  859  SER SER A . n 
A 1 860  GLY 860  860  860  GLY GLY A . n 
A 1 861  GLU 861  861  861  GLU GLU A . n 
A 1 862  LEU 862  862  862  LEU LEU A . n 
A 1 863  GLU 863  863  863  GLU GLU A . n 
A 1 864  ILE 864  864  864  ILE ILE A . n 
A 1 865  MET 865  865  865  MET MET A . n 
A 1 866  GLN 866  866  866  GLN GLN A . n 
A 1 867  ASP 867  867  867  ASP ASP A . n 
A 1 868  ARG 868  868  868  ARG ARG A . n 
A 1 869  ARG 869  869  869  ARG ARG A . n 
A 1 870  LEU 870  870  870  LEU LEU A . n 
A 1 871  ALA 871  871  871  ALA ALA A . n 
A 1 872  SER 872  872  872  SER SER A . n 
A 1 873  ASP 873  873  873  ASP ASP A . n 
A 1 874  ASP 874  874  874  ASP ASP A . n 
A 1 875  GLU 875  875  875  GLU GLU A . n 
A 1 876  ARG 876  876  876  ARG ARG A . n 
A 1 877  GLY 877  877  877  GLY GLY A . n 
A 1 878  LEU 878  878  878  LEU LEU A . n 
A 1 879  GLY 879  879  879  GLY GLY A . n 
A 1 880  GLN 880  880  880  GLN GLN A . n 
A 1 881  GLY 881  881  881  GLY GLY A . n 
A 1 882  VAL 882  882  882  VAL VAL A . n 
A 1 883  LEU 883  883  883  LEU LEU A . n 
A 1 884  ASP 884  884  884  ASP ASP A . n 
A 1 885  ASN 885  885  885  ASN ASN A . n 
A 1 886  LYS 886  886  886  LYS LYS A . n 
A 1 887  PRO 887  887  887  PRO PRO A . n 
A 1 888  VAL 888  888  888  VAL VAL A . n 
A 1 889  LEU 889  889  889  LEU LEU A . n 
A 1 890  HIS 890  890  890  HIS HIS A . n 
A 1 891  ILE 891  891  891  ILE ILE A . n 
A 1 892  TYR 892  892  892  TYR TYR A . n 
A 1 893  ARG 893  893  893  ARG ARG A . n 
A 1 894  LEU 894  894  894  LEU LEU A . n 
A 1 895  VAL 895  895  895  VAL VAL A . n 
A 1 896  LEU 896  896  896  LEU LEU A . n 
A 1 897  GLU 897  897  897  GLU GLU A . n 
A 1 898  LYS 898  898  898  LYS LYS A . n 
A 1 899  VAL 899  899  899  VAL VAL A . n 
A 1 900  ASN 900  900  900  ASN ASN A . n 
A 1 901  ASN 901  901  901  ASN ASN A . n 
A 1 902  CYS 902  902  902  CYS CYS A . n 
A 1 903  VAL 903  903  903  VAL VAL A . n 
A 1 904  ARG 904  904  904  ARG ARG A . n 
A 1 905  PRO 905  905  905  PRO PRO A . n 
A 1 906  SER 906  906  906  SER SER A . n 
A 1 907  LYS 907  907  907  LYS LYS A . n 
A 1 908  LEU 908  908  908  LEU LEU A . n 
A 1 909  HIS 909  909  909  HIS HIS A . n 
A 1 910  PRO 910  910  910  PRO PRO A . n 
A 1 911  ALA 911  911  911  ALA ALA A . n 
A 1 912  GLY 912  912  912  GLY GLY A . n 
A 1 913  TYR 913  913  913  TYR TYR A . n 
A 1 914  LEU 914  914  914  LEU LEU A . n 
A 1 915  THR 915  915  915  THR THR A . n 
A 1 916  SER 916  916  916  SER SER A . n 
A 1 917  ALA 917  917  917  ALA ALA A . n 
A 1 918  ALA 918  918  918  ALA ALA A . n 
A 1 919  HIS 919  919  919  HIS HIS A . n 
A 1 920  LYS 920  920  920  LYS LYS A . n 
A 1 921  ALA 921  921  921  ALA ALA A . n 
A 1 922  SER 922  922  922  SER SER A . n 
A 1 923  GLN 923  923  923  GLN GLN A . n 
A 1 924  SER 924  924  924  SER SER A . n 
A 1 925  LEU 925  925  925  LEU LEU A . n 
A 1 926  LEU 926  926  926  LEU LEU A . n 
A 1 927  ASP 927  927  927  ASP ASP A . n 
A 1 928  PRO 928  928  928  PRO PRO A . n 
A 1 929  LEU 929  929  929  LEU LEU A . n 
A 1 930  ASP 930  930  930  ASP ASP A . n 
A 1 931  LYS 931  931  931  LYS LYS A . n 
A 1 932  PHE 932  932  932  PHE PHE A . n 
A 1 933  ILE 933  933  933  ILE ILE A . n 
A 1 934  PHE 934  934  934  PHE PHE A . n 
A 1 935  ALA 935  935  935  ALA ALA A . n 
A 1 936  GLU 936  936  936  GLU GLU A . n 
A 1 937  ASN 937  937  937  ASN ASN A . n 
A 1 938  GLU 938  938  938  GLU GLU A . n 
A 1 939  TRP 939  939  939  TRP TRP A . n 
A 1 940  ILE 940  940  940  ILE ILE A . n 
A 1 941  GLY 941  941  941  GLY GLY A . n 
A 1 942  ALA 942  942  942  ALA ALA A . n 
A 1 943  GLN 943  943  943  GLN GLN A . n 
A 1 944  GLY 944  944  944  GLY GLY A . n 
A 1 945  GLN 945  945  945  GLN GLN A . n 
A 1 946  PHE 946  946  946  PHE PHE A . n 
A 1 947  GLY 947  947  947  GLY GLY A . n 
A 1 948  GLY 948  948  948  GLY GLY A . n 
A 1 949  ASP 949  949  949  ASP ASP A . n 
A 1 950  HIS 950  950  950  HIS HIS A . n 
A 1 951  PRO 951  951  951  PRO PRO A . n 
A 1 952  SER 952  952  952  SER SER A . n 
A 1 953  ALA 953  953  953  ALA ALA A . n 
A 1 954  ARG 954  954  954  ARG ARG A . n 
A 1 955  GLU 955  955  955  GLU GLU A . n 
A 1 956  ASP 956  956  956  ASP ASP A . n 
A 1 957  LEU 957  957  957  LEU LEU A . n 
A 1 958  ASP 958  958  958  ASP ASP A . n 
A 1 959  VAL 959  959  959  VAL VAL A . n 
A 1 960  SER 960  960  960  SER SER A . n 
A 1 961  VAL 961  961  961  VAL VAL A . n 
A 1 962  MET 962  962  962  MET MET A . n 
A 1 963  ARG 963  963  963  ARG ARG A . n 
A 1 964  ARG 964  964  964  ARG ARG A . n 
A 1 965  LEU 965  965  965  LEU LEU A . n 
A 1 966  THR 966  966  966  THR THR A . n 
A 1 967  LYS 967  967  967  LYS LYS A . n 
A 1 968  SER 968  968  968  SER SER A . n 
A 1 969  SER 969  969  969  SER SER A . n 
A 1 970  ALA 970  970  970  ALA ALA A . n 
A 1 971  LYS 971  971  971  LYS LYS A . n 
A 1 972  THR 972  972  972  THR THR A . n 
A 1 973  GLN 973  973  973  GLN GLN A . n 
A 1 974  ARG 974  974  974  ARG ARG A . n 
A 1 975  VAL 975  975  975  VAL VAL A . n 
A 1 976  GLY 976  976  976  GLY GLY A . n 
A 1 977  TYR 977  977  977  TYR TYR A . n 
A 1 978  VAL 978  978  978  VAL VAL A . n 
A 1 979  LEU 979  979  979  LEU LEU A . n 
A 1 980  HIS 980  980  980  HIS HIS A . n 
A 1 981  ARG 981  981  981  ARG ARG A . n 
A 1 982  THR 982  982  982  THR THR A . n 
A 1 983  ASN 983  983  983  ASN ASN A . n 
A 1 984  LEU 984  984  984  LEU LEU A . n 
A 1 985  MET 985  985  985  MET MET A . n 
A 1 986  GLN 986  986  986  GLN GLN A . n 
A 1 987  CYS 987  987  987  CYS CYS A . n 
A 1 988  GLY 988  988  988  GLY GLY A . n 
A 1 989  THR 989  989  989  THR THR A . n 
A 1 990  PRO 990  990  990  PRO PRO A . n 
A 1 991  GLU 991  991  991  GLU GLU A . n 
A 1 992  GLU 992  992  992  GLU GLU A . n 
A 1 993  HIS 993  993  993  HIS HIS A . n 
A 1 994  THR 994  994  994  THR THR A . n 
A 1 995  GLN 995  995  995  GLN GLN A . n 
A 1 996  LYS 996  996  996  LYS LYS A . n 
A 1 997  LEU 997  997  997  LEU LEU A . n 
A 1 998  ASP 998  998  998  ASP ASP A . n 
A 1 999  VAL 999  999  999  VAL VAL A . n 
A 1 1000 CYS 1000 1000 1000 CYS CYS A . n 
A 1 1001 HIS 1001 1001 1001 HIS HIS A . n 
A 1 1002 LEU 1002 1002 1002 LEU LEU A . n 
A 1 1003 LEU 1003 1003 1003 LEU LEU A . n 
A 1 1004 PRO 1004 1004 1004 PRO PRO A . n 
A 1 1005 ASN 1005 1005 1005 ASN ASN A . n 
A 1 1006 VAL 1006 1006 1006 VAL VAL A . n 
A 1 1007 ALA 1007 1007 1007 ALA ALA A . n 
A 1 1008 ARG 1008 1008 1008 ARG ARG A . n 
A 1 1009 CYS 1009 1009 1009 CYS CYS A . n 
A 1 1010 GLU 1010 1010 1010 GLU GLU A . n 
A 1 1011 ARG 1011 1011 1011 ARG ARG A . n 
A 1 1012 THR 1012 1012 1012 THR THR A . n 
A 1 1013 THR 1013 1013 1013 THR THR A . n 
A 1 1014 LEU 1014 1014 1014 LEU LEU A . n 
A 1 1015 THR 1015 1015 1015 THR THR A . n 
A 1 1016 PHE 1016 1016 1016 PHE PHE A . n 
A 1 1017 LEU 1017 1017 1017 LEU LEU A . n 
A 1 1018 GLN 1018 1018 1018 GLN GLN A . n 
A 1 1019 ASN 1019 1019 1019 ASN ASN A . n 
A 1 1020 LEU 1020 1020 1020 LEU LEU A . n 
A 1 1021 GLU 1021 1021 1021 GLU GLU A . n 
A 1 1022 HIS 1022 1022 1022 HIS HIS A . n 
A 1 1023 LEU 1023 1023 1023 LEU LEU A . n 
A 1 1024 ASP 1024 1024 1024 ASP ASP A . n 
A 1 1025 GLY 1025 1025 1025 GLY GLY A . n 
A 1 1026 MET 1026 1026 1026 MET MET A . n 
A 1 1027 VAL 1027 1027 1027 VAL VAL A . n 
A 1 1028 ALA 1028 1028 1028 ALA ALA A . n 
A 1 1029 PRO 1029 1029 1029 PRO PRO A . n 
A 1 1030 GLU 1030 1030 1030 GLU GLU A . n 
A 1 1031 VAL 1031 1031 1031 VAL VAL A . n 
A 1 1032 CYS 1032 1032 1032 CYS CYS A . n 
A 1 1033 PRO 1033 1033 1033 PRO PRO A . n 
A 1 1034 MET 1034 1034 1034 MET MET A . n 
A 1 1035 GLU 1035 1035 1035 GLU GLU A . n 
A 1 1036 THR 1036 1036 1036 THR THR A . n 
A 1 1037 ALA 1037 1037 1037 ALA ALA A . n 
A 1 1038 ALA 1038 1038 1038 ALA ALA A . n 
A 1 1039 TYR 1039 1039 1039 TYR TYR A . n 
A 1 1040 VAL 1040 1040 1040 VAL VAL A . n 
A 1 1041 SER 1041 1041 1041 SER SER A . n 
A 1 1042 SER 1042 1042 1042 SER SER A . n 
A 1 1043 HIS 1043 1043 1043 HIS HIS A . n 
A 1 1044 SER 1044 1044 1044 SER SER A . n 
A 1 1045 SER 1045 1045 ?    ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NAG 1    2001 1    NAG NAG A . 
C 3 ZN  1    2004 1    ZN  ZN  A . 
D 4 GUL 1    2003 1    GUL GUL A . 
E 5 MPD 1    2002 1    MPD MPD A . 
F 6 HOH 1    2005 1    HOH WAT A . 
F 6 HOH 2    2006 2    HOH WAT A . 
F 6 HOH 3    2007 3    HOH WAT A . 
F 6 HOH 4    2008 4    HOH WAT A . 
F 6 HOH 5    2009 5    HOH WAT A . 
F 6 HOH 6    2010 6    HOH WAT A . 
F 6 HOH 7    2011 7    HOH WAT A . 
F 6 HOH 8    2012 8    HOH WAT A . 
F 6 HOH 9    2013 9    HOH WAT A . 
F 6 HOH 10   2014 10   HOH WAT A . 
F 6 HOH 11   2015 11   HOH WAT A . 
F 6 HOH 12   2016 12   HOH WAT A . 
F 6 HOH 13   2017 13   HOH WAT A . 
F 6 HOH 14   2018 14   HOH WAT A . 
F 6 HOH 15   2019 15   HOH WAT A . 
F 6 HOH 16   2020 16   HOH WAT A . 
F 6 HOH 17   2021 17   HOH WAT A . 
F 6 HOH 18   2022 18   HOH WAT A . 
F 6 HOH 19   2023 19   HOH WAT A . 
F 6 HOH 20   2024 20   HOH WAT A . 
F 6 HOH 21   2025 21   HOH WAT A . 
F 6 HOH 22   2026 22   HOH WAT A . 
F 6 HOH 23   2027 23   HOH WAT A . 
F 6 HOH 24   2028 24   HOH WAT A . 
F 6 HOH 25   2029 25   HOH WAT A . 
F 6 HOH 26   2030 26   HOH WAT A . 
F 6 HOH 27   2031 27   HOH WAT A . 
F 6 HOH 28   2032 28   HOH WAT A . 
F 6 HOH 29   2033 29   HOH WAT A . 
F 6 HOH 30   2034 30   HOH WAT A . 
F 6 HOH 31   2035 31   HOH WAT A . 
F 6 HOH 32   2036 32   HOH WAT A . 
F 6 HOH 33   2037 33   HOH WAT A . 
F 6 HOH 34   2038 34   HOH WAT A . 
F 6 HOH 35   2039 35   HOH WAT A . 
F 6 HOH 36   2040 36   HOH WAT A . 
F 6 HOH 37   2041 37   HOH WAT A . 
F 6 HOH 38   2042 38   HOH WAT A . 
F 6 HOH 39   2043 39   HOH WAT A . 
F 6 HOH 40   2044 40   HOH WAT A . 
F 6 HOH 41   2045 41   HOH WAT A . 
F 6 HOH 42   2046 42   HOH WAT A . 
F 6 HOH 43   2047 43   HOH WAT A . 
F 6 HOH 44   2048 44   HOH WAT A . 
F 6 HOH 45   2049 45   HOH WAT A . 
F 6 HOH 46   2050 46   HOH WAT A . 
F 6 HOH 47   2051 47   HOH WAT A . 
F 6 HOH 48   2052 48   HOH WAT A . 
F 6 HOH 49   2053 49   HOH WAT A . 
F 6 HOH 50   2054 50   HOH WAT A . 
F 6 HOH 51   2055 51   HOH WAT A . 
F 6 HOH 52   2056 52   HOH WAT A . 
F 6 HOH 53   2057 53   HOH WAT A . 
F 6 HOH 54   2058 54   HOH WAT A . 
F 6 HOH 55   2059 55   HOH WAT A . 
F 6 HOH 56   2060 56   HOH WAT A . 
F 6 HOH 57   2061 57   HOH WAT A . 
F 6 HOH 58   2062 58   HOH WAT A . 
F 6 HOH 59   2063 59   HOH WAT A . 
F 6 HOH 60   2064 60   HOH WAT A . 
F 6 HOH 61   2065 61   HOH WAT A . 
F 6 HOH 62   2066 62   HOH WAT A . 
F 6 HOH 63   2067 63   HOH WAT A . 
F 6 HOH 64   2068 64   HOH WAT A . 
F 6 HOH 65   2069 65   HOH WAT A . 
F 6 HOH 66   2070 66   HOH WAT A . 
F 6 HOH 67   2071 67   HOH WAT A . 
F 6 HOH 68   2072 68   HOH WAT A . 
F 6 HOH 69   2073 69   HOH WAT A . 
F 6 HOH 70   2074 70   HOH WAT A . 
F 6 HOH 71   2075 71   HOH WAT A . 
F 6 HOH 72   2076 72   HOH WAT A . 
F 6 HOH 73   2077 73   HOH WAT A . 
F 6 HOH 74   2078 74   HOH WAT A . 
F 6 HOH 75   2079 75   HOH WAT A . 
F 6 HOH 76   2080 76   HOH WAT A . 
F 6 HOH 77   2081 77   HOH WAT A . 
F 6 HOH 78   2082 78   HOH WAT A . 
F 6 HOH 79   2083 79   HOH WAT A . 
F 6 HOH 80   2084 80   HOH WAT A . 
F 6 HOH 81   2085 81   HOH WAT A . 
F 6 HOH 82   2086 82   HOH WAT A . 
F 6 HOH 83   2087 83   HOH WAT A . 
F 6 HOH 84   2088 84   HOH WAT A . 
F 6 HOH 85   2089 85   HOH WAT A . 
F 6 HOH 86   2090 86   HOH WAT A . 
F 6 HOH 87   2091 87   HOH WAT A . 
F 6 HOH 88   2092 88   HOH WAT A . 
F 6 HOH 89   2093 89   HOH WAT A . 
F 6 HOH 90   2094 90   HOH WAT A . 
F 6 HOH 91   2095 91   HOH WAT A . 
F 6 HOH 92   2096 92   HOH WAT A . 
F 6 HOH 93   2097 93   HOH WAT A . 
F 6 HOH 94   2098 94   HOH WAT A . 
F 6 HOH 95   2099 95   HOH WAT A . 
F 6 HOH 96   2100 96   HOH WAT A . 
F 6 HOH 97   2101 97   HOH WAT A . 
F 6 HOH 98   2102 98   HOH WAT A . 
F 6 HOH 99   2103 99   HOH WAT A . 
F 6 HOH 100  2104 100  HOH WAT A . 
F 6 HOH 101  2105 101  HOH WAT A . 
F 6 HOH 102  2106 102  HOH WAT A . 
F 6 HOH 103  2107 103  HOH WAT A . 
F 6 HOH 104  2108 104  HOH WAT A . 
F 6 HOH 105  2109 105  HOH WAT A . 
F 6 HOH 106  2110 106  HOH WAT A . 
F 6 HOH 107  2111 107  HOH WAT A . 
F 6 HOH 108  2112 108  HOH WAT A . 
F 6 HOH 109  2113 109  HOH WAT A . 
F 6 HOH 110  2114 110  HOH WAT A . 
F 6 HOH 111  2115 111  HOH WAT A . 
F 6 HOH 112  2116 112  HOH WAT A . 
F 6 HOH 113  2117 113  HOH WAT A . 
F 6 HOH 114  2118 114  HOH WAT A . 
F 6 HOH 115  2119 115  HOH WAT A . 
F 6 HOH 116  2120 116  HOH WAT A . 
F 6 HOH 117  2121 117  HOH WAT A . 
F 6 HOH 118  2122 118  HOH WAT A . 
F 6 HOH 119  2123 119  HOH WAT A . 
F 6 HOH 120  2124 120  HOH WAT A . 
F 6 HOH 121  2125 121  HOH WAT A . 
F 6 HOH 122  2126 122  HOH WAT A . 
F 6 HOH 123  2127 123  HOH WAT A . 
F 6 HOH 124  2128 124  HOH WAT A . 
F 6 HOH 125  2129 125  HOH WAT A . 
F 6 HOH 126  2130 126  HOH WAT A . 
F 6 HOH 127  2131 127  HOH WAT A . 
F 6 HOH 128  2132 128  HOH WAT A . 
F 6 HOH 129  2133 129  HOH WAT A . 
F 6 HOH 130  2134 130  HOH WAT A . 
F 6 HOH 131  2135 131  HOH WAT A . 
F 6 HOH 132  2136 132  HOH WAT A . 
F 6 HOH 133  2137 133  HOH WAT A . 
F 6 HOH 134  2138 134  HOH WAT A . 
F 6 HOH 135  2139 135  HOH WAT A . 
F 6 HOH 136  2140 136  HOH WAT A . 
F 6 HOH 137  2141 137  HOH WAT A . 
F 6 HOH 138  2142 138  HOH WAT A . 
F 6 HOH 139  2143 139  HOH WAT A . 
F 6 HOH 140  2144 140  HOH WAT A . 
F 6 HOH 141  2145 141  HOH WAT A . 
F 6 HOH 142  2146 142  HOH WAT A . 
F 6 HOH 143  2147 143  HOH WAT A . 
F 6 HOH 144  2148 144  HOH WAT A . 
F 6 HOH 145  2149 145  HOH WAT A . 
F 6 HOH 146  2150 146  HOH WAT A . 
F 6 HOH 147  2151 147  HOH WAT A . 
F 6 HOH 148  2152 148  HOH WAT A . 
F 6 HOH 149  2153 149  HOH WAT A . 
F 6 HOH 150  2154 150  HOH WAT A . 
F 6 HOH 151  2155 151  HOH WAT A . 
F 6 HOH 152  2156 152  HOH WAT A . 
F 6 HOH 153  2157 153  HOH WAT A . 
F 6 HOH 154  2158 154  HOH WAT A . 
F 6 HOH 155  2159 155  HOH WAT A . 
F 6 HOH 156  2160 156  HOH WAT A . 
F 6 HOH 157  2161 157  HOH WAT A . 
F 6 HOH 158  2162 158  HOH WAT A . 
F 6 HOH 159  2163 159  HOH WAT A . 
F 6 HOH 160  2164 160  HOH WAT A . 
F 6 HOH 161  2165 161  HOH WAT A . 
F 6 HOH 162  2166 162  HOH WAT A . 
F 6 HOH 163  2167 163  HOH WAT A . 
F 6 HOH 164  2168 164  HOH WAT A . 
F 6 HOH 165  2169 165  HOH WAT A . 
F 6 HOH 166  2170 166  HOH WAT A . 
F 6 HOH 167  2171 167  HOH WAT A . 
F 6 HOH 168  2172 168  HOH WAT A . 
F 6 HOH 169  2173 169  HOH WAT A . 
F 6 HOH 170  2174 170  HOH WAT A . 
F 6 HOH 171  2175 171  HOH WAT A . 
F 6 HOH 172  2176 172  HOH WAT A . 
F 6 HOH 173  2177 173  HOH WAT A . 
F 6 HOH 174  2178 174  HOH WAT A . 
F 6 HOH 175  2179 175  HOH WAT A . 
F 6 HOH 176  2180 176  HOH WAT A . 
F 6 HOH 177  2181 177  HOH WAT A . 
F 6 HOH 178  2182 178  HOH WAT A . 
F 6 HOH 179  2183 179  HOH WAT A . 
F 6 HOH 180  2184 180  HOH WAT A . 
F 6 HOH 181  2185 181  HOH WAT A . 
F 6 HOH 182  2186 182  HOH WAT A . 
F 6 HOH 183  2187 183  HOH WAT A . 
F 6 HOH 184  2188 184  HOH WAT A . 
F 6 HOH 185  2189 185  HOH WAT A . 
F 6 HOH 186  2190 186  HOH WAT A . 
F 6 HOH 187  2191 187  HOH WAT A . 
F 6 HOH 188  2192 188  HOH WAT A . 
F 6 HOH 189  2193 189  HOH WAT A . 
F 6 HOH 190  2194 190  HOH WAT A . 
F 6 HOH 191  2195 191  HOH WAT A . 
F 6 HOH 192  2196 192  HOH WAT A . 
F 6 HOH 193  2197 193  HOH WAT A . 
F 6 HOH 194  2198 194  HOH WAT A . 
F 6 HOH 195  2199 195  HOH WAT A . 
F 6 HOH 196  2200 196  HOH WAT A . 
F 6 HOH 197  2201 197  HOH WAT A . 
F 6 HOH 198  2202 198  HOH WAT A . 
F 6 HOH 199  2203 199  HOH WAT A . 
F 6 HOH 200  2204 200  HOH WAT A . 
F 6 HOH 201  2205 201  HOH WAT A . 
F 6 HOH 202  2206 202  HOH WAT A . 
F 6 HOH 203  2207 203  HOH WAT A . 
F 6 HOH 204  2208 204  HOH WAT A . 
F 6 HOH 205  2209 205  HOH WAT A . 
F 6 HOH 206  2210 206  HOH WAT A . 
F 6 HOH 207  2211 207  HOH WAT A . 
F 6 HOH 208  2212 208  HOH WAT A . 
F 6 HOH 209  2213 209  HOH WAT A . 
F 6 HOH 210  2214 210  HOH WAT A . 
F 6 HOH 211  2215 211  HOH WAT A . 
F 6 HOH 212  2216 212  HOH WAT A . 
F 6 HOH 213  2217 213  HOH WAT A . 
F 6 HOH 214  2218 214  HOH WAT A . 
F 6 HOH 215  2219 215  HOH WAT A . 
F 6 HOH 216  2220 216  HOH WAT A . 
F 6 HOH 217  2221 217  HOH WAT A . 
F 6 HOH 218  2222 218  HOH WAT A . 
F 6 HOH 219  2223 219  HOH WAT A . 
F 6 HOH 220  2224 220  HOH WAT A . 
F 6 HOH 221  2225 221  HOH WAT A . 
F 6 HOH 222  2226 222  HOH WAT A . 
F 6 HOH 223  2227 223  HOH WAT A . 
F 6 HOH 224  2228 224  HOH WAT A . 
F 6 HOH 225  2229 225  HOH WAT A . 
F 6 HOH 226  2230 226  HOH WAT A . 
F 6 HOH 227  2231 227  HOH WAT A . 
F 6 HOH 228  2232 228  HOH WAT A . 
F 6 HOH 229  2233 229  HOH WAT A . 
F 6 HOH 230  2234 230  HOH WAT A . 
F 6 HOH 231  2235 231  HOH WAT A . 
F 6 HOH 232  2236 232  HOH WAT A . 
F 6 HOH 233  2237 233  HOH WAT A . 
F 6 HOH 234  2238 234  HOH WAT A . 
F 6 HOH 235  2239 235  HOH WAT A . 
F 6 HOH 236  2240 236  HOH WAT A . 
F 6 HOH 237  2241 237  HOH WAT A . 
F 6 HOH 238  2242 238  HOH WAT A . 
F 6 HOH 239  2243 239  HOH WAT A . 
F 6 HOH 240  2244 240  HOH WAT A . 
F 6 HOH 241  2245 241  HOH WAT A . 
F 6 HOH 242  2246 242  HOH WAT A . 
F 6 HOH 243  2247 243  HOH WAT A . 
F 6 HOH 244  2248 244  HOH WAT A . 
F 6 HOH 245  2249 245  HOH WAT A . 
F 6 HOH 246  2250 246  HOH WAT A . 
F 6 HOH 247  2251 247  HOH WAT A . 
F 6 HOH 248  2252 248  HOH WAT A . 
F 6 HOH 249  2253 249  HOH WAT A . 
F 6 HOH 250  2254 250  HOH WAT A . 
F 6 HOH 251  2255 251  HOH WAT A . 
F 6 HOH 252  2256 252  HOH WAT A . 
F 6 HOH 253  2257 253  HOH WAT A . 
F 6 HOH 254  2258 254  HOH WAT A . 
F 6 HOH 255  2259 255  HOH WAT A . 
F 6 HOH 256  2260 256  HOH WAT A . 
F 6 HOH 257  2261 257  HOH WAT A . 
F 6 HOH 258  2262 258  HOH WAT A . 
F 6 HOH 259  2263 259  HOH WAT A . 
F 6 HOH 260  2264 260  HOH WAT A . 
F 6 HOH 261  2265 261  HOH WAT A . 
F 6 HOH 262  2266 262  HOH WAT A . 
F 6 HOH 263  2267 263  HOH WAT A . 
F 6 HOH 264  2268 264  HOH WAT A . 
F 6 HOH 265  2269 265  HOH WAT A . 
F 6 HOH 266  2270 266  HOH WAT A . 
F 6 HOH 267  2271 267  HOH WAT A . 
F 6 HOH 268  2272 268  HOH WAT A . 
F 6 HOH 269  2273 269  HOH WAT A . 
F 6 HOH 270  2274 270  HOH WAT A . 
F 6 HOH 271  2275 271  HOH WAT A . 
F 6 HOH 272  2276 272  HOH WAT A . 
F 6 HOH 273  2277 273  HOH WAT A . 
F 6 HOH 274  2278 274  HOH WAT A . 
F 6 HOH 275  2279 275  HOH WAT A . 
F 6 HOH 276  2280 276  HOH WAT A . 
F 6 HOH 277  2281 277  HOH WAT A . 
F 6 HOH 278  2282 278  HOH WAT A . 
F 6 HOH 279  2283 279  HOH WAT A . 
F 6 HOH 280  2284 280  HOH WAT A . 
F 6 HOH 281  2285 281  HOH WAT A . 
F 6 HOH 282  2286 282  HOH WAT A . 
F 6 HOH 283  2287 283  HOH WAT A . 
F 6 HOH 284  2288 284  HOH WAT A . 
F 6 HOH 285  2289 285  HOH WAT A . 
F 6 HOH 286  2290 286  HOH WAT A . 
F 6 HOH 287  2291 287  HOH WAT A . 
F 6 HOH 288  2292 288  HOH WAT A . 
F 6 HOH 289  2293 289  HOH WAT A . 
F 6 HOH 290  2294 290  HOH WAT A . 
F 6 HOH 291  2295 291  HOH WAT A . 
F 6 HOH 292  2296 292  HOH WAT A . 
F 6 HOH 293  2297 293  HOH WAT A . 
F 6 HOH 294  2298 294  HOH WAT A . 
F 6 HOH 295  2299 295  HOH WAT A . 
F 6 HOH 296  2300 296  HOH WAT A . 
F 6 HOH 297  2301 297  HOH WAT A . 
F 6 HOH 298  2302 298  HOH WAT A . 
F 6 HOH 299  2303 299  HOH WAT A . 
F 6 HOH 300  2304 300  HOH WAT A . 
F 6 HOH 301  2305 301  HOH WAT A . 
F 6 HOH 302  2306 302  HOH WAT A . 
F 6 HOH 303  2307 303  HOH WAT A . 
F 6 HOH 304  2308 304  HOH WAT A . 
F 6 HOH 305  2309 305  HOH WAT A . 
F 6 HOH 306  2310 306  HOH WAT A . 
F 6 HOH 307  2311 307  HOH WAT A . 
F 6 HOH 308  2312 308  HOH WAT A . 
F 6 HOH 309  2313 309  HOH WAT A . 
F 6 HOH 310  2314 310  HOH WAT A . 
F 6 HOH 311  2315 311  HOH WAT A . 
F 6 HOH 312  2316 312  HOH WAT A . 
F 6 HOH 313  2317 313  HOH WAT A . 
F 6 HOH 314  2318 314  HOH WAT A . 
F 6 HOH 315  2319 315  HOH WAT A . 
F 6 HOH 316  2320 316  HOH WAT A . 
F 6 HOH 317  2321 317  HOH WAT A . 
F 6 HOH 318  2322 318  HOH WAT A . 
F 6 HOH 319  2323 319  HOH WAT A . 
F 6 HOH 320  2324 320  HOH WAT A . 
F 6 HOH 321  2325 321  HOH WAT A . 
F 6 HOH 322  2326 322  HOH WAT A . 
F 6 HOH 323  2327 323  HOH WAT A . 
F 6 HOH 324  2328 324  HOH WAT A . 
F 6 HOH 325  2329 325  HOH WAT A . 
F 6 HOH 326  2330 326  HOH WAT A . 
F 6 HOH 327  2331 327  HOH WAT A . 
F 6 HOH 328  2332 328  HOH WAT A . 
F 6 HOH 329  2333 329  HOH WAT A . 
F 6 HOH 330  2334 330  HOH WAT A . 
F 6 HOH 331  2335 331  HOH WAT A . 
F 6 HOH 332  2336 332  HOH WAT A . 
F 6 HOH 333  2337 333  HOH WAT A . 
F 6 HOH 334  2338 334  HOH WAT A . 
F 6 HOH 335  2339 335  HOH WAT A . 
F 6 HOH 336  2340 336  HOH WAT A . 
F 6 HOH 337  2341 337  HOH WAT A . 
F 6 HOH 338  2342 338  HOH WAT A . 
F 6 HOH 339  2343 339  HOH WAT A . 
F 6 HOH 340  2344 340  HOH WAT A . 
F 6 HOH 341  2345 341  HOH WAT A . 
F 6 HOH 342  2346 342  HOH WAT A . 
F 6 HOH 343  2347 343  HOH WAT A . 
F 6 HOH 344  2348 344  HOH WAT A . 
F 6 HOH 345  2349 345  HOH WAT A . 
F 6 HOH 346  2350 346  HOH WAT A . 
F 6 HOH 347  2351 347  HOH WAT A . 
F 6 HOH 348  2352 348  HOH WAT A . 
F 6 HOH 349  2353 349  HOH WAT A . 
F 6 HOH 350  2354 350  HOH WAT A . 
F 6 HOH 351  2355 351  HOH WAT A . 
F 6 HOH 352  2356 352  HOH WAT A . 
F 6 HOH 353  2357 353  HOH WAT A . 
F 6 HOH 354  2358 354  HOH WAT A . 
F 6 HOH 355  2359 355  HOH WAT A . 
F 6 HOH 356  2360 356  HOH WAT A . 
F 6 HOH 357  2361 357  HOH WAT A . 
F 6 HOH 358  2362 358  HOH WAT A . 
F 6 HOH 359  2363 359  HOH WAT A . 
F 6 HOH 360  2364 360  HOH WAT A . 
F 6 HOH 361  2365 361  HOH WAT A . 
F 6 HOH 362  2366 362  HOH WAT A . 
F 6 HOH 363  2367 363  HOH WAT A . 
F 6 HOH 364  2368 364  HOH WAT A . 
F 6 HOH 365  2369 365  HOH WAT A . 
F 6 HOH 366  2370 366  HOH WAT A . 
F 6 HOH 367  2371 367  HOH WAT A . 
F 6 HOH 368  2372 368  HOH WAT A . 
F 6 HOH 369  2373 369  HOH WAT A . 
F 6 HOH 370  2374 370  HOH WAT A . 
F 6 HOH 371  2375 371  HOH WAT A . 
F 6 HOH 372  2376 372  HOH WAT A . 
F 6 HOH 373  2377 373  HOH WAT A . 
F 6 HOH 374  2378 374  HOH WAT A . 
F 6 HOH 375  2379 375  HOH WAT A . 
F 6 HOH 376  2380 376  HOH WAT A . 
F 6 HOH 377  2381 377  HOH WAT A . 
F 6 HOH 378  2382 378  HOH WAT A . 
F 6 HOH 379  2383 379  HOH WAT A . 
F 6 HOH 380  2384 380  HOH WAT A . 
F 6 HOH 381  2385 381  HOH WAT A . 
F 6 HOH 382  2386 382  HOH WAT A . 
F 6 HOH 383  2387 383  HOH WAT A . 
F 6 HOH 384  2388 384  HOH WAT A . 
F 6 HOH 385  2389 385  HOH WAT A . 
F 6 HOH 386  2390 386  HOH WAT A . 
F 6 HOH 387  2391 387  HOH WAT A . 
F 6 HOH 388  2392 388  HOH WAT A . 
F 6 HOH 389  2393 389  HOH WAT A . 
F 6 HOH 390  2394 390  HOH WAT A . 
F 6 HOH 391  2395 391  HOH WAT A . 
F 6 HOH 392  2396 392  HOH WAT A . 
F 6 HOH 393  2397 393  HOH WAT A . 
F 6 HOH 394  2398 394  HOH WAT A . 
F 6 HOH 395  2399 395  HOH WAT A . 
F 6 HOH 396  2400 396  HOH WAT A . 
F 6 HOH 397  2401 397  HOH WAT A . 
F 6 HOH 398  2402 398  HOH WAT A . 
F 6 HOH 399  2403 399  HOH WAT A . 
F 6 HOH 400  2404 400  HOH WAT A . 
F 6 HOH 401  2405 401  HOH WAT A . 
F 6 HOH 402  2406 402  HOH WAT A . 
F 6 HOH 403  2407 403  HOH WAT A . 
F 6 HOH 404  2408 404  HOH WAT A . 
F 6 HOH 405  2409 405  HOH WAT A . 
F 6 HOH 406  2410 406  HOH WAT A . 
F 6 HOH 407  2411 407  HOH WAT A . 
F 6 HOH 408  2412 408  HOH WAT A . 
F 6 HOH 409  2413 409  HOH WAT A . 
F 6 HOH 410  2414 410  HOH WAT A . 
F 6 HOH 411  2415 411  HOH WAT A . 
F 6 HOH 412  2416 412  HOH WAT A . 
F 6 HOH 413  2417 413  HOH WAT A . 
F 6 HOH 414  2418 414  HOH WAT A . 
F 6 HOH 415  2419 415  HOH WAT A . 
F 6 HOH 416  2420 416  HOH WAT A . 
F 6 HOH 417  2421 417  HOH WAT A . 
F 6 HOH 418  2422 418  HOH WAT A . 
F 6 HOH 419  2423 419  HOH WAT A . 
F 6 HOH 420  2424 420  HOH WAT A . 
F 6 HOH 421  2425 421  HOH WAT A . 
F 6 HOH 422  2426 422  HOH WAT A . 
F 6 HOH 423  2427 423  HOH WAT A . 
F 6 HOH 424  2428 424  HOH WAT A . 
F 6 HOH 425  2429 425  HOH WAT A . 
F 6 HOH 426  2430 426  HOH WAT A . 
F 6 HOH 427  2431 427  HOH WAT A . 
F 6 HOH 428  2432 428  HOH WAT A . 
F 6 HOH 429  2433 429  HOH WAT A . 
F 6 HOH 430  2434 430  HOH WAT A . 
F 6 HOH 431  2435 431  HOH WAT A . 
F 6 HOH 432  2436 432  HOH WAT A . 
F 6 HOH 433  2437 433  HOH WAT A . 
F 6 HOH 434  2438 434  HOH WAT A . 
F 6 HOH 435  2439 435  HOH WAT A . 
F 6 HOH 436  2440 436  HOH WAT A . 
F 6 HOH 437  2441 437  HOH WAT A . 
F 6 HOH 438  2442 438  HOH WAT A . 
F 6 HOH 439  2443 439  HOH WAT A . 
F 6 HOH 440  2444 440  HOH WAT A . 
F 6 HOH 441  2445 441  HOH WAT A . 
F 6 HOH 442  2446 442  HOH WAT A . 
F 6 HOH 443  2447 443  HOH WAT A . 
F 6 HOH 444  2448 444  HOH WAT A . 
F 6 HOH 445  2449 445  HOH WAT A . 
F 6 HOH 446  2450 446  HOH WAT A . 
F 6 HOH 447  2451 447  HOH WAT A . 
F 6 HOH 448  2452 448  HOH WAT A . 
F 6 HOH 449  2453 449  HOH WAT A . 
F 6 HOH 450  2454 450  HOH WAT A . 
F 6 HOH 451  2455 451  HOH WAT A . 
F 6 HOH 452  2456 452  HOH WAT A . 
F 6 HOH 453  2457 453  HOH WAT A . 
F 6 HOH 454  2458 454  HOH WAT A . 
F 6 HOH 455  2459 455  HOH WAT A . 
F 6 HOH 456  2460 456  HOH WAT A . 
F 6 HOH 457  2461 457  HOH WAT A . 
F 6 HOH 458  2462 458  HOH WAT A . 
F 6 HOH 459  2463 459  HOH WAT A . 
F 6 HOH 460  2464 460  HOH WAT A . 
F 6 HOH 461  2465 461  HOH WAT A . 
F 6 HOH 462  2466 462  HOH WAT A . 
F 6 HOH 463  2467 463  HOH WAT A . 
F 6 HOH 464  2468 464  HOH WAT A . 
F 6 HOH 465  2469 465  HOH WAT A . 
F 6 HOH 466  2470 466  HOH WAT A . 
F 6 HOH 467  2471 467  HOH WAT A . 
F 6 HOH 468  2472 468  HOH WAT A . 
F 6 HOH 469  2473 469  HOH WAT A . 
F 6 HOH 470  2474 470  HOH WAT A . 
F 6 HOH 471  2475 471  HOH WAT A . 
F 6 HOH 472  2476 472  HOH WAT A . 
F 6 HOH 473  2477 473  HOH WAT A . 
F 6 HOH 474  2478 474  HOH WAT A . 
F 6 HOH 475  2479 475  HOH WAT A . 
F 6 HOH 476  2480 476  HOH WAT A . 
F 6 HOH 477  2481 477  HOH WAT A . 
F 6 HOH 478  2482 478  HOH WAT A . 
F 6 HOH 479  2483 479  HOH WAT A . 
F 6 HOH 480  2484 480  HOH WAT A . 
F 6 HOH 481  2485 481  HOH WAT A . 
F 6 HOH 482  2486 482  HOH WAT A . 
F 6 HOH 483  2487 483  HOH WAT A . 
F 6 HOH 484  2488 484  HOH WAT A . 
F 6 HOH 485  2489 485  HOH WAT A . 
F 6 HOH 486  2490 486  HOH WAT A . 
F 6 HOH 487  2491 487  HOH WAT A . 
F 6 HOH 488  2492 488  HOH WAT A . 
F 6 HOH 489  2493 489  HOH WAT A . 
F 6 HOH 490  2494 490  HOH WAT A . 
F 6 HOH 491  2495 491  HOH WAT A . 
F 6 HOH 492  2496 492  HOH WAT A . 
F 6 HOH 493  2497 493  HOH WAT A . 
F 6 HOH 494  2498 494  HOH WAT A . 
F 6 HOH 495  2499 495  HOH WAT A . 
F 6 HOH 496  2500 496  HOH WAT A . 
F 6 HOH 497  2501 497  HOH WAT A . 
F 6 HOH 498  2502 498  HOH WAT A . 
F 6 HOH 499  2503 499  HOH WAT A . 
F 6 HOH 500  2504 500  HOH WAT A . 
F 6 HOH 501  2505 501  HOH WAT A . 
F 6 HOH 502  2506 502  HOH WAT A . 
F 6 HOH 503  2507 503  HOH WAT A . 
F 6 HOH 504  2508 504  HOH WAT A . 
F 6 HOH 505  2509 505  HOH WAT A . 
F 6 HOH 506  2510 506  HOH WAT A . 
F 6 HOH 507  2511 507  HOH WAT A . 
F 6 HOH 508  2512 508  HOH WAT A . 
F 6 HOH 509  2513 509  HOH WAT A . 
F 6 HOH 510  2514 510  HOH WAT A . 
F 6 HOH 511  2515 511  HOH WAT A . 
F 6 HOH 512  2516 512  HOH WAT A . 
F 6 HOH 513  2517 513  HOH WAT A . 
F 6 HOH 514  2518 514  HOH WAT A . 
F 6 HOH 515  2519 515  HOH WAT A . 
F 6 HOH 516  2520 516  HOH WAT A . 
F 6 HOH 517  2521 517  HOH WAT A . 
F 6 HOH 518  2522 518  HOH WAT A . 
F 6 HOH 519  2523 519  HOH WAT A . 
F 6 HOH 520  2524 520  HOH WAT A . 
F 6 HOH 521  2525 521  HOH WAT A . 
F 6 HOH 522  2526 522  HOH WAT A . 
F 6 HOH 523  2527 523  HOH WAT A . 
F 6 HOH 524  2528 524  HOH WAT A . 
F 6 HOH 525  2529 525  HOH WAT A . 
F 6 HOH 526  2530 526  HOH WAT A . 
F 6 HOH 527  2531 527  HOH WAT A . 
F 6 HOH 528  2532 528  HOH WAT A . 
F 6 HOH 529  2533 529  HOH WAT A . 
F 6 HOH 530  2534 530  HOH WAT A . 
F 6 HOH 531  2535 531  HOH WAT A . 
F 6 HOH 532  2536 532  HOH WAT A . 
F 6 HOH 533  2537 533  HOH WAT A . 
F 6 HOH 534  2538 534  HOH WAT A . 
F 6 HOH 535  2539 535  HOH WAT A . 
F 6 HOH 536  2540 536  HOH WAT A . 
F 6 HOH 537  2541 537  HOH WAT A . 
F 6 HOH 538  2542 538  HOH WAT A . 
F 6 HOH 539  2543 539  HOH WAT A . 
F 6 HOH 540  2544 540  HOH WAT A . 
F 6 HOH 541  2545 541  HOH WAT A . 
F 6 HOH 542  2546 542  HOH WAT A . 
F 6 HOH 543  2547 543  HOH WAT A . 
F 6 HOH 544  2548 544  HOH WAT A . 
F 6 HOH 545  2549 545  HOH WAT A . 
F 6 HOH 546  2550 546  HOH WAT A . 
F 6 HOH 547  2551 547  HOH WAT A . 
F 6 HOH 548  2552 548  HOH WAT A . 
F 6 HOH 549  2553 549  HOH WAT A . 
F 6 HOH 550  2554 550  HOH WAT A . 
F 6 HOH 551  2555 551  HOH WAT A . 
F 6 HOH 552  2556 552  HOH WAT A . 
F 6 HOH 553  2557 553  HOH WAT A . 
F 6 HOH 554  2558 554  HOH WAT A . 
F 6 HOH 555  2559 555  HOH WAT A . 
F 6 HOH 556  2560 556  HOH WAT A . 
F 6 HOH 557  2561 557  HOH WAT A . 
F 6 HOH 558  2562 558  HOH WAT A . 
F 6 HOH 559  2563 559  HOH WAT A . 
F 6 HOH 560  2564 560  HOH WAT A . 
F 6 HOH 561  2565 561  HOH WAT A . 
F 6 HOH 562  2566 562  HOH WAT A . 
F 6 HOH 563  2567 563  HOH WAT A . 
F 6 HOH 564  2568 564  HOH WAT A . 
F 6 HOH 565  2569 565  HOH WAT A . 
F 6 HOH 566  2570 566  HOH WAT A . 
F 6 HOH 567  2571 567  HOH WAT A . 
F 6 HOH 568  2572 568  HOH WAT A . 
F 6 HOH 569  2573 569  HOH WAT A . 
F 6 HOH 570  2574 570  HOH WAT A . 
F 6 HOH 571  2575 571  HOH WAT A . 
F 6 HOH 572  2576 572  HOH WAT A . 
F 6 HOH 573  2577 573  HOH WAT A . 
F 6 HOH 574  2578 574  HOH WAT A . 
F 6 HOH 575  2579 575  HOH WAT A . 
F 6 HOH 576  2580 576  HOH WAT A . 
F 6 HOH 577  2581 577  HOH WAT A . 
F 6 HOH 578  2582 578  HOH WAT A . 
F 6 HOH 579  2583 579  HOH WAT A . 
F 6 HOH 580  2584 580  HOH WAT A . 
F 6 HOH 581  2585 581  HOH WAT A . 
F 6 HOH 582  2586 582  HOH WAT A . 
F 6 HOH 583  2587 583  HOH WAT A . 
F 6 HOH 584  2588 584  HOH WAT A . 
F 6 HOH 585  2589 585  HOH WAT A . 
F 6 HOH 586  2590 586  HOH WAT A . 
F 6 HOH 587  2591 587  HOH WAT A . 
F 6 HOH 588  2592 588  HOH WAT A . 
F 6 HOH 589  2593 589  HOH WAT A . 
F 6 HOH 590  2594 590  HOH WAT A . 
F 6 HOH 591  2595 591  HOH WAT A . 
F 6 HOH 592  2596 592  HOH WAT A . 
F 6 HOH 593  2597 593  HOH WAT A . 
F 6 HOH 594  2598 594  HOH WAT A . 
F 6 HOH 595  2599 595  HOH WAT A . 
F 6 HOH 596  2600 596  HOH WAT A . 
F 6 HOH 597  2601 597  HOH WAT A . 
F 6 HOH 598  2602 598  HOH WAT A . 
F 6 HOH 599  2603 599  HOH WAT A . 
F 6 HOH 600  2604 600  HOH WAT A . 
F 6 HOH 601  2605 601  HOH WAT A . 
F 6 HOH 602  2606 602  HOH WAT A . 
F 6 HOH 603  2607 603  HOH WAT A . 
F 6 HOH 604  2608 604  HOH WAT A . 
F 6 HOH 605  2609 605  HOH WAT A . 
F 6 HOH 606  2610 606  HOH WAT A . 
F 6 HOH 607  2611 607  HOH WAT A . 
F 6 HOH 608  2612 608  HOH WAT A . 
F 6 HOH 609  2613 609  HOH WAT A . 
F 6 HOH 610  2614 610  HOH WAT A . 
F 6 HOH 611  2615 611  HOH WAT A . 
F 6 HOH 612  2616 612  HOH WAT A . 
F 6 HOH 613  2617 613  HOH WAT A . 
F 6 HOH 614  2618 614  HOH WAT A . 
F 6 HOH 615  2619 615  HOH WAT A . 
F 6 HOH 616  2620 616  HOH WAT A . 
F 6 HOH 617  2621 617  HOH WAT A . 
F 6 HOH 618  2622 618  HOH WAT A . 
F 6 HOH 619  2623 619  HOH WAT A . 
F 6 HOH 620  2624 620  HOH WAT A . 
F 6 HOH 621  2625 621  HOH WAT A . 
F 6 HOH 622  2626 622  HOH WAT A . 
F 6 HOH 623  2627 623  HOH WAT A . 
F 6 HOH 624  2628 624  HOH WAT A . 
F 6 HOH 625  2629 625  HOH WAT A . 
F 6 HOH 626  2630 626  HOH WAT A . 
F 6 HOH 627  2631 627  HOH WAT A . 
F 6 HOH 628  2632 628  HOH WAT A . 
F 6 HOH 629  2633 629  HOH WAT A . 
F 6 HOH 630  2634 630  HOH WAT A . 
F 6 HOH 631  2635 631  HOH WAT A . 
F 6 HOH 632  2636 632  HOH WAT A . 
F 6 HOH 633  2637 633  HOH WAT A . 
F 6 HOH 634  2638 634  HOH WAT A . 
F 6 HOH 635  2639 635  HOH WAT A . 
F 6 HOH 636  2640 636  HOH WAT A . 
F 6 HOH 637  2641 637  HOH WAT A . 
F 6 HOH 638  2642 638  HOH WAT A . 
F 6 HOH 639  2643 639  HOH WAT A . 
F 6 HOH 640  2644 640  HOH WAT A . 
F 6 HOH 641  2645 641  HOH WAT A . 
F 6 HOH 642  2646 642  HOH WAT A . 
F 6 HOH 643  2647 643  HOH WAT A . 
F 6 HOH 644  2648 644  HOH WAT A . 
F 6 HOH 645  2649 645  HOH WAT A . 
F 6 HOH 646  2650 646  HOH WAT A . 
F 6 HOH 647  2651 647  HOH WAT A . 
F 6 HOH 648  2652 648  HOH WAT A . 
F 6 HOH 649  2653 649  HOH WAT A . 
F 6 HOH 650  2654 650  HOH WAT A . 
F 6 HOH 651  2655 651  HOH WAT A . 
F 6 HOH 652  2656 652  HOH WAT A . 
F 6 HOH 653  2657 653  HOH WAT A . 
F 6 HOH 654  2658 654  HOH WAT A . 
F 6 HOH 655  2659 655  HOH WAT A . 
F 6 HOH 656  2660 656  HOH WAT A . 
F 6 HOH 657  2661 657  HOH WAT A . 
F 6 HOH 658  2662 658  HOH WAT A . 
F 6 HOH 659  2663 659  HOH WAT A . 
F 6 HOH 660  2664 660  HOH WAT A . 
F 6 HOH 661  2665 661  HOH WAT A . 
F 6 HOH 662  2666 662  HOH WAT A . 
F 6 HOH 663  2667 663  HOH WAT A . 
F 6 HOH 664  2668 664  HOH WAT A . 
F 6 HOH 665  2669 665  HOH WAT A . 
F 6 HOH 666  2670 666  HOH WAT A . 
F 6 HOH 667  2671 667  HOH WAT A . 
F 6 HOH 668  2672 668  HOH WAT A . 
F 6 HOH 669  2673 669  HOH WAT A . 
F 6 HOH 670  2674 670  HOH WAT A . 
F 6 HOH 671  2675 671  HOH WAT A . 
F 6 HOH 672  2676 672  HOH WAT A . 
F 6 HOH 673  2677 673  HOH WAT A . 
F 6 HOH 674  2678 674  HOH WAT A . 
F 6 HOH 675  2679 675  HOH WAT A . 
F 6 HOH 676  2680 676  HOH WAT A . 
F 6 HOH 677  2681 677  HOH WAT A . 
F 6 HOH 678  2682 678  HOH WAT A . 
F 6 HOH 679  2683 679  HOH WAT A . 
F 6 HOH 680  2684 680  HOH WAT A . 
F 6 HOH 681  2685 681  HOH WAT A . 
F 6 HOH 682  2686 682  HOH WAT A . 
F 6 HOH 683  2687 683  HOH WAT A . 
F 6 HOH 684  2688 684  HOH WAT A . 
F 6 HOH 685  2689 685  HOH WAT A . 
F 6 HOH 686  2690 686  HOH WAT A . 
F 6 HOH 687  2691 687  HOH WAT A . 
F 6 HOH 688  2692 688  HOH WAT A . 
F 6 HOH 689  2693 689  HOH WAT A . 
F 6 HOH 690  2694 690  HOH WAT A . 
F 6 HOH 691  2695 691  HOH WAT A . 
F 6 HOH 692  2696 692  HOH WAT A . 
F 6 HOH 693  2697 693  HOH WAT A . 
F 6 HOH 694  2698 694  HOH WAT A . 
F 6 HOH 695  2699 695  HOH WAT A . 
F 6 HOH 696  2700 696  HOH WAT A . 
F 6 HOH 697  2701 697  HOH WAT A . 
F 6 HOH 698  2702 698  HOH WAT A . 
F 6 HOH 699  2703 699  HOH WAT A . 
F 6 HOH 700  2704 700  HOH WAT A . 
F 6 HOH 701  2705 701  HOH WAT A . 
F 6 HOH 702  2706 702  HOH WAT A . 
F 6 HOH 703  2707 703  HOH WAT A . 
F 6 HOH 704  2708 704  HOH WAT A . 
F 6 HOH 705  2709 705  HOH WAT A . 
F 6 HOH 706  2710 706  HOH WAT A . 
F 6 HOH 707  2711 707  HOH WAT A . 
F 6 HOH 708  2712 708  HOH WAT A . 
F 6 HOH 709  2713 709  HOH WAT A . 
F 6 HOH 710  2714 710  HOH WAT A . 
F 6 HOH 711  2715 711  HOH WAT A . 
F 6 HOH 712  2716 712  HOH WAT A . 
F 6 HOH 713  2717 713  HOH WAT A . 
F 6 HOH 714  2718 714  HOH WAT A . 
F 6 HOH 715  2719 715  HOH WAT A . 
F 6 HOH 716  2720 716  HOH WAT A . 
F 6 HOH 717  2721 717  HOH WAT A . 
F 6 HOH 718  2722 718  HOH WAT A . 
F 6 HOH 719  2723 719  HOH WAT A . 
F 6 HOH 720  2724 720  HOH WAT A . 
F 6 HOH 721  2725 721  HOH WAT A . 
F 6 HOH 722  2726 722  HOH WAT A . 
F 6 HOH 723  2727 723  HOH WAT A . 
F 6 HOH 724  2728 724  HOH WAT A . 
F 6 HOH 725  2729 725  HOH WAT A . 
F 6 HOH 726  2730 726  HOH WAT A . 
F 6 HOH 727  2731 727  HOH WAT A . 
F 6 HOH 728  2732 728  HOH WAT A . 
F 6 HOH 729  2733 729  HOH WAT A . 
F 6 HOH 730  2734 730  HOH WAT A . 
F 6 HOH 731  2735 731  HOH WAT A . 
F 6 HOH 732  2736 732  HOH WAT A . 
F 6 HOH 733  2737 733  HOH WAT A . 
F 6 HOH 734  2738 734  HOH WAT A . 
F 6 HOH 735  2739 735  HOH WAT A . 
F 6 HOH 736  2740 736  HOH WAT A . 
F 6 HOH 737  2741 737  HOH WAT A . 
F 6 HOH 738  2742 738  HOH WAT A . 
F 6 HOH 739  2743 739  HOH WAT A . 
F 6 HOH 740  2744 740  HOH WAT A . 
F 6 HOH 741  2745 741  HOH WAT A . 
F 6 HOH 742  2746 742  HOH WAT A . 
F 6 HOH 743  2747 743  HOH WAT A . 
F 6 HOH 744  2748 744  HOH WAT A . 
F 6 HOH 745  2749 745  HOH WAT A . 
F 6 HOH 746  2750 746  HOH WAT A . 
F 6 HOH 747  2751 747  HOH WAT A . 
F 6 HOH 748  2752 748  HOH WAT A . 
F 6 HOH 749  2753 749  HOH WAT A . 
F 6 HOH 750  2754 750  HOH WAT A . 
F 6 HOH 751  2755 751  HOH WAT A . 
F 6 HOH 752  2756 752  HOH WAT A . 
F 6 HOH 753  2757 753  HOH WAT A . 
F 6 HOH 754  2758 754  HOH WAT A . 
F 6 HOH 755  2759 755  HOH WAT A . 
F 6 HOH 756  2760 756  HOH WAT A . 
F 6 HOH 757  2761 757  HOH WAT A . 
F 6 HOH 758  2762 758  HOH WAT A . 
F 6 HOH 759  2763 759  HOH WAT A . 
F 6 HOH 760  2764 760  HOH WAT A . 
F 6 HOH 761  2765 761  HOH WAT A . 
F 6 HOH 762  2766 762  HOH WAT A . 
F 6 HOH 763  2767 763  HOH WAT A . 
F 6 HOH 764  2768 764  HOH WAT A . 
F 6 HOH 765  2769 765  HOH WAT A . 
F 6 HOH 766  2770 766  HOH WAT A . 
F 6 HOH 767  2771 767  HOH WAT A . 
F 6 HOH 768  2772 768  HOH WAT A . 
F 6 HOH 769  2773 769  HOH WAT A . 
F 6 HOH 770  2774 770  HOH WAT A . 
F 6 HOH 771  2775 771  HOH WAT A . 
F 6 HOH 772  2776 772  HOH WAT A . 
F 6 HOH 773  2777 773  HOH WAT A . 
F 6 HOH 774  2778 774  HOH WAT A . 
F 6 HOH 775  2779 775  HOH WAT A . 
F 6 HOH 776  2780 776  HOH WAT A . 
F 6 HOH 777  2781 777  HOH WAT A . 
F 6 HOH 778  2782 778  HOH WAT A . 
F 6 HOH 779  2783 779  HOH WAT A . 
F 6 HOH 780  2784 780  HOH WAT A . 
F 6 HOH 781  2785 781  HOH WAT A . 
F 6 HOH 782  2786 782  HOH WAT A . 
F 6 HOH 783  2787 783  HOH WAT A . 
F 6 HOH 784  2788 784  HOH WAT A . 
F 6 HOH 785  2789 785  HOH WAT A . 
F 6 HOH 786  2790 786  HOH WAT A . 
F 6 HOH 787  2791 787  HOH WAT A . 
F 6 HOH 788  2792 788  HOH WAT A . 
F 6 HOH 789  2793 789  HOH WAT A . 
F 6 HOH 790  2794 790  HOH WAT A . 
F 6 HOH 791  2795 791  HOH WAT A . 
F 6 HOH 792  2796 792  HOH WAT A . 
F 6 HOH 793  2797 793  HOH WAT A . 
F 6 HOH 794  2798 794  HOH WAT A . 
F 6 HOH 795  2799 795  HOH WAT A . 
F 6 HOH 796  2800 796  HOH WAT A . 
F 6 HOH 797  2801 797  HOH WAT A . 
F 6 HOH 798  2802 798  HOH WAT A . 
F 6 HOH 799  2803 799  HOH WAT A . 
F 6 HOH 800  2804 800  HOH WAT A . 
F 6 HOH 801  2805 801  HOH WAT A . 
F 6 HOH 802  2806 802  HOH WAT A . 
F 6 HOH 803  2807 803  HOH WAT A . 
F 6 HOH 804  2808 804  HOH WAT A . 
F 6 HOH 805  2809 805  HOH WAT A . 
F 6 HOH 806  2810 806  HOH WAT A . 
F 6 HOH 807  2811 807  HOH WAT A . 
F 6 HOH 808  2812 808  HOH WAT A . 
F 6 HOH 809  2813 809  HOH WAT A . 
F 6 HOH 810  2814 810  HOH WAT A . 
F 6 HOH 811  2815 811  HOH WAT A . 
F 6 HOH 812  2816 812  HOH WAT A . 
F 6 HOH 813  2817 813  HOH WAT A . 
F 6 HOH 814  2818 814  HOH WAT A . 
F 6 HOH 815  2819 815  HOH WAT A . 
F 6 HOH 816  2820 816  HOH WAT A . 
F 6 HOH 817  2821 817  HOH WAT A . 
F 6 HOH 818  2822 818  HOH WAT A . 
F 6 HOH 819  2823 819  HOH WAT A . 
F 6 HOH 820  2824 820  HOH WAT A . 
F 6 HOH 821  2825 821  HOH WAT A . 
F 6 HOH 822  2826 822  HOH WAT A . 
F 6 HOH 823  2827 823  HOH WAT A . 
F 6 HOH 824  2828 824  HOH WAT A . 
F 6 HOH 825  2829 825  HOH WAT A . 
F 6 HOH 826  2830 826  HOH WAT A . 
F 6 HOH 827  2831 827  HOH WAT A . 
F 6 HOH 828  2832 828  HOH WAT A . 
F 6 HOH 829  2833 829  HOH WAT A . 
F 6 HOH 830  2834 830  HOH WAT A . 
F 6 HOH 831  2835 831  HOH WAT A . 
F 6 HOH 832  2836 832  HOH WAT A . 
F 6 HOH 833  2837 833  HOH WAT A . 
F 6 HOH 834  2838 834  HOH WAT A . 
F 6 HOH 835  2839 835  HOH WAT A . 
F 6 HOH 836  2840 836  HOH WAT A . 
F 6 HOH 837  2841 837  HOH WAT A . 
F 6 HOH 838  2842 838  HOH WAT A . 
F 6 HOH 839  2843 839  HOH WAT A . 
F 6 HOH 840  2844 840  HOH WAT A . 
F 6 HOH 841  2845 841  HOH WAT A . 
F 6 HOH 842  2846 842  HOH WAT A . 
F 6 HOH 843  2847 843  HOH WAT A . 
F 6 HOH 844  2848 844  HOH WAT A . 
F 6 HOH 845  2849 845  HOH WAT A . 
F 6 HOH 846  2850 846  HOH WAT A . 
F 6 HOH 847  2851 847  HOH WAT A . 
F 6 HOH 848  2852 848  HOH WAT A . 
F 6 HOH 849  2853 849  HOH WAT A . 
F 6 HOH 850  2854 850  HOH WAT A . 
F 6 HOH 851  2855 851  HOH WAT A . 
F 6 HOH 852  2856 852  HOH WAT A . 
F 6 HOH 853  2857 853  HOH WAT A . 
F 6 HOH 854  2858 854  HOH WAT A . 
F 6 HOH 855  2859 855  HOH WAT A . 
F 6 HOH 856  2860 856  HOH WAT A . 
F 6 HOH 857  2861 857  HOH WAT A . 
F 6 HOH 858  2862 858  HOH WAT A . 
F 6 HOH 859  2863 859  HOH WAT A . 
F 6 HOH 860  2864 860  HOH WAT A . 
F 6 HOH 861  2865 861  HOH WAT A . 
F 6 HOH 862  2866 862  HOH WAT A . 
F 6 HOH 863  2867 863  HOH WAT A . 
F 6 HOH 864  2868 864  HOH WAT A . 
F 6 HOH 865  2869 865  HOH WAT A . 
F 6 HOH 866  2870 866  HOH WAT A . 
F 6 HOH 867  2871 867  HOH WAT A . 
F 6 HOH 868  2872 868  HOH WAT A . 
F 6 HOH 869  2873 869  HOH WAT A . 
F 6 HOH 870  2874 870  HOH WAT A . 
F 6 HOH 871  2875 871  HOH WAT A . 
F 6 HOH 872  2876 872  HOH WAT A . 
F 6 HOH 873  2877 873  HOH WAT A . 
F 6 HOH 874  2878 874  HOH WAT A . 
F 6 HOH 875  2879 875  HOH WAT A . 
F 6 HOH 876  2880 876  HOH WAT A . 
F 6 HOH 877  2881 877  HOH WAT A . 
F 6 HOH 878  2882 878  HOH WAT A . 
F 6 HOH 879  2883 879  HOH WAT A . 
F 6 HOH 880  2884 880  HOH WAT A . 
F 6 HOH 881  2885 881  HOH WAT A . 
F 6 HOH 882  2886 882  HOH WAT A . 
F 6 HOH 883  2887 883  HOH WAT A . 
F 6 HOH 884  2888 884  HOH WAT A . 
F 6 HOH 885  2889 885  HOH WAT A . 
F 6 HOH 886  2890 886  HOH WAT A . 
F 6 HOH 887  2891 887  HOH WAT A . 
F 6 HOH 888  2892 888  HOH WAT A . 
F 6 HOH 889  2893 889  HOH WAT A . 
F 6 HOH 890  2894 890  HOH WAT A . 
F 6 HOH 891  2895 891  HOH WAT A . 
F 6 HOH 892  2896 892  HOH WAT A . 
F 6 HOH 893  2897 893  HOH WAT A . 
F 6 HOH 894  2898 894  HOH WAT A . 
F 6 HOH 895  2899 895  HOH WAT A . 
F 6 HOH 896  2900 896  HOH WAT A . 
F 6 HOH 897  2901 897  HOH WAT A . 
F 6 HOH 898  2902 898  HOH WAT A . 
F 6 HOH 899  2903 899  HOH WAT A . 
F 6 HOH 900  2904 900  HOH WAT A . 
F 6 HOH 901  2905 901  HOH WAT A . 
F 6 HOH 902  2906 902  HOH WAT A . 
F 6 HOH 903  2907 903  HOH WAT A . 
F 6 HOH 904  2908 904  HOH WAT A . 
F 6 HOH 905  2909 905  HOH WAT A . 
F 6 HOH 906  2910 906  HOH WAT A . 
F 6 HOH 907  2911 907  HOH WAT A . 
F 6 HOH 908  2912 908  HOH WAT A . 
F 6 HOH 909  2913 909  HOH WAT A . 
F 6 HOH 910  2914 910  HOH WAT A . 
F 6 HOH 911  2915 911  HOH WAT A . 
F 6 HOH 912  2916 912  HOH WAT A . 
F 6 HOH 913  2917 913  HOH WAT A . 
F 6 HOH 914  2918 914  HOH WAT A . 
F 6 HOH 915  2919 915  HOH WAT A . 
F 6 HOH 916  2920 916  HOH WAT A . 
F 6 HOH 917  2921 917  HOH WAT A . 
F 6 HOH 918  2922 918  HOH WAT A . 
F 6 HOH 919  2923 919  HOH WAT A . 
F 6 HOH 920  2924 920  HOH WAT A . 
F 6 HOH 921  2925 921  HOH WAT A . 
F 6 HOH 922  2926 922  HOH WAT A . 
F 6 HOH 923  2927 923  HOH WAT A . 
F 6 HOH 924  2928 924  HOH WAT A . 
F 6 HOH 925  2929 925  HOH WAT A . 
F 6 HOH 926  2930 926  HOH WAT A . 
F 6 HOH 927  2931 927  HOH WAT A . 
F 6 HOH 928  2932 928  HOH WAT A . 
F 6 HOH 929  2933 929  HOH WAT A . 
F 6 HOH 930  2934 930  HOH WAT A . 
F 6 HOH 931  2935 931  HOH WAT A . 
F 6 HOH 932  2936 932  HOH WAT A . 
F 6 HOH 933  2937 933  HOH WAT A . 
F 6 HOH 934  2938 934  HOH WAT A . 
F 6 HOH 935  2939 935  HOH WAT A . 
F 6 HOH 936  2940 936  HOH WAT A . 
F 6 HOH 937  2941 937  HOH WAT A . 
F 6 HOH 938  2942 938  HOH WAT A . 
F 6 HOH 939  2943 939  HOH WAT A . 
F 6 HOH 940  2944 940  HOH WAT A . 
F 6 HOH 941  2945 941  HOH WAT A . 
F 6 HOH 942  2946 942  HOH WAT A . 
F 6 HOH 943  2947 943  HOH WAT A . 
F 6 HOH 944  2948 944  HOH WAT A . 
F 6 HOH 945  2949 945  HOH WAT A . 
F 6 HOH 946  2950 946  HOH WAT A . 
F 6 HOH 947  2951 947  HOH WAT A . 
F 6 HOH 948  2952 948  HOH WAT A . 
F 6 HOH 949  2953 949  HOH WAT A . 
F 6 HOH 950  2954 950  HOH WAT A . 
F 6 HOH 951  2955 951  HOH WAT A . 
F 6 HOH 952  2956 952  HOH WAT A . 
F 6 HOH 953  2957 953  HOH WAT A . 
F 6 HOH 954  2958 954  HOH WAT A . 
F 6 HOH 955  2959 955  HOH WAT A . 
F 6 HOH 956  2960 956  HOH WAT A . 
F 6 HOH 957  2961 957  HOH WAT A . 
F 6 HOH 958  2962 958  HOH WAT A . 
F 6 HOH 959  2963 959  HOH WAT A . 
F 6 HOH 960  2964 960  HOH WAT A . 
F 6 HOH 961  2965 961  HOH WAT A . 
F 6 HOH 962  2966 962  HOH WAT A . 
F 6 HOH 963  2967 963  HOH WAT A . 
F 6 HOH 964  2968 964  HOH WAT A . 
F 6 HOH 965  2969 965  HOH WAT A . 
F 6 HOH 966  2970 966  HOH WAT A . 
F 6 HOH 967  2971 967  HOH WAT A . 
F 6 HOH 968  2972 968  HOH WAT A . 
F 6 HOH 969  2973 969  HOH WAT A . 
F 6 HOH 970  2974 970  HOH WAT A . 
F 6 HOH 971  2975 971  HOH WAT A . 
F 6 HOH 972  2976 972  HOH WAT A . 
F 6 HOH 973  2977 973  HOH WAT A . 
F 6 HOH 974  2978 974  HOH WAT A . 
F 6 HOH 975  2979 975  HOH WAT A . 
F 6 HOH 976  2980 976  HOH WAT A . 
F 6 HOH 977  2981 977  HOH WAT A . 
F 6 HOH 978  2982 978  HOH WAT A . 
F 6 HOH 979  2983 979  HOH WAT A . 
F 6 HOH 980  2984 980  HOH WAT A . 
F 6 HOH 981  2985 981  HOH WAT A . 
F 6 HOH 982  2986 982  HOH WAT A . 
F 6 HOH 983  2987 983  HOH WAT A . 
F 6 HOH 984  2988 984  HOH WAT A . 
F 6 HOH 985  2989 985  HOH WAT A . 
F 6 HOH 986  2990 986  HOH WAT A . 
F 6 HOH 987  2991 987  HOH WAT A . 
F 6 HOH 988  2992 988  HOH WAT A . 
F 6 HOH 989  2993 989  HOH WAT A . 
F 6 HOH 990  2994 990  HOH WAT A . 
F 6 HOH 991  2995 991  HOH WAT A . 
F 6 HOH 992  2996 992  HOH WAT A . 
F 6 HOH 993  2997 993  HOH WAT A . 
F 6 HOH 994  2998 994  HOH WAT A . 
F 6 HOH 995  2999 995  HOH WAT A . 
F 6 HOH 996  3000 996  HOH WAT A . 
F 6 HOH 997  3001 997  HOH WAT A . 
F 6 HOH 998  3002 998  HOH WAT A . 
F 6 HOH 999  3003 999  HOH WAT A . 
F 6 HOH 1000 3004 1000 HOH WAT A . 
F 6 HOH 1001 3005 1001 HOH WAT A . 
F 6 HOH 1002 3006 1002 HOH WAT A . 
F 6 HOH 1003 3007 1003 HOH WAT A . 
F 6 HOH 1004 3008 1004 HOH WAT A . 
F 6 HOH 1005 3009 1005 HOH WAT A . 
F 6 HOH 1006 3010 1006 HOH WAT A . 
F 6 HOH 1007 3011 1007 HOH WAT A . 
F 6 HOH 1008 3012 1008 HOH WAT A . 
F 6 HOH 1009 3013 1009 HOH WAT A . 
F 6 HOH 1010 3014 1010 HOH WAT A . 
F 6 HOH 1011 3015 1011 HOH WAT A . 
F 6 HOH 1012 3016 1012 HOH WAT A . 
F 6 HOH 1013 3017 1013 HOH WAT A . 
F 6 HOH 1014 3018 1014 HOH WAT A . 
F 6 HOH 1015 3019 1015 HOH WAT A . 
F 6 HOH 1016 3020 1016 HOH WAT A . 
F 6 HOH 1017 3021 1017 HOH WAT A . 
F 6 HOH 1018 3022 1018 HOH WAT A . 
F 6 HOH 1019 3023 1019 HOH WAT A . 
F 6 HOH 1020 3024 1020 HOH WAT A . 
F 6 HOH 1021 3025 1021 HOH WAT A . 
F 6 HOH 1022 3026 1022 HOH WAT A . 
F 6 HOH 1023 3027 1023 HOH WAT A . 
F 6 HOH 1024 3028 1024 HOH WAT A . 
F 6 HOH 1025 3029 1025 HOH WAT A . 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    ASN 
_pdbx_struct_mod_residue.label_seq_id     194 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     ASN 
_pdbx_struct_mod_residue.auth_seq_id      194 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   ASN 
_pdbx_struct_mod_residue.details          'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 O2  ? D GUL .   ? A GUL 2003 ? 1_555 91.0  ? 
2  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 98.4  ? 
3  O2  ? D GUL .   ? A GUL 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 92.4  ? 
4  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 98.3  ? 
5  O2  ? D GUL .   ? A GUL 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 163.4 ? 
6  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 99.7  ? 
7  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 O3  ? D GUL .   ? A GUL 2003 ? 1_555 164.8 ? 
8  O2  ? D GUL .   ? A GUL 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 O3  ? D GUL .   ? A GUL 2003 ? 1_555 75.0  ? 
9  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 O3  ? D GUL .   ? A GUL 2003 ? 1_555 88.4  ? 
10 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 O3  ? D GUL .   ? A GUL 2003 ? 1_555 93.9  ? 
11 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 204 ? A ASP 204  ? 1_555 89.8  ? 
12 O2  ? D GUL .   ? A GUL 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 204 ? A ASP 204  ? 1_555 70.0  ? 
13 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 204 ? A ASP 204  ? 1_555 160.8 ? 
14 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 204 ? A ASP 204  ? 1_555 96.2  ? 
15 O3  ? D GUL .   ? A GUL 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 204 ? A ASP 204  ? 1_555 79.8  ? 
# 
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 
1 'Structure model' 1 0 2003-10-07 
2 'Structure model' 1 1 2008-04-29 
3 'Structure model' 1 2 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Non-polymer description'   
3 3 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CNS       refinement       1.0 ? 1 
DENZO     'data reduction' .   ? 2 
SCALEPACK 'data scaling'   .   ? 3 
CNS       phasing          .   ? 4 
# 
_pdbx_database_remark.id     999 
_pdbx_database_remark.text   
;SEQUENCE
The E -> K conflict for residue 970
is noted in Swiss-Prot entry Q24451.
;
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OH A TYR 75   ? ? O A HOH 3014 ? ? 2.08 
2 1 O  A HOH 2861 ? ? O A HOH 2864 ? ? 2.15 
3 1 O  A HOH 2338 ? ? O A HOH 2589 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     2682 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     3021 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_565 
_pdbx_validate_symm_contact.dist              2.10 
# 
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 HIS A 79  ? ? -154.15 88.41   
2  1 TRP A 95  ? ? -170.64 -83.04  
3  1 ASP A 106 ? ? -134.59 -58.87  
4  1 THR A 162 ? ? 67.17   -62.44  
5  1 GLN A 227 ? ? -133.67 -51.78  
6  1 PHE A 287 ? ? -69.01  0.89    
7  1 SER A 411 ? ? 35.25   -118.63 
8  1 ILE A 549 ? ? -143.32 -49.54  
9  1 PRO A 562 ? ? -82.45  44.36   
10 1 SER A 703 ? ? -41.09  160.18  
11 1 ASN A 732 ? ? -93.53  59.15   
12 1 SER A 762 ? ? 78.25   -8.40   
13 1 SER A 833 ? ? -154.29 -11.12  
14 1 ASP A 839 ? ? -129.05 -159.76 
15 1 SER A 855 ? ? -170.82 -174.55 
16 1 GLU A 991 ? ? 36.42   97.55   
17 1 GLU A 992 ? ? -118.09 -151.11 
18 1 HIS A 993 ? ? 21.57   85.11   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 TYR A 407 ? ? 0.071 'SIDE CHAIN' 
2 1 TYR A 646 ? ? 0.069 'SIDE CHAIN' 
# 
loop_
_pdbx_validate_chiral.id 
_pdbx_validate_chiral.PDB_model_num 
_pdbx_validate_chiral.auth_atom_id 
_pdbx_validate_chiral.label_alt_id 
_pdbx_validate_chiral.auth_asym_id 
_pdbx_validate_chiral.auth_comp_id 
_pdbx_validate_chiral.auth_seq_id 
_pdbx_validate_chiral.PDB_ins_code 
_pdbx_validate_chiral.details 
_pdbx_validate_chiral.omega 
1 1 C1 ? A NAG 2001 ? 'WRONG HAND' . 
2 1 C4 ? A MPD 2002 ? 'WRONG HAND' . 
# 
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 ARG 1    ? A ARG 1    
2  1 Y 1 A SER 2    ? A SER 2    
3  1 Y 1 A SER 3    ? A SER 3    
4  1 Y 1 A HIS 4    ? A HIS 4    
5  1 Y 1 A HIS 5    ? A HIS 5    
6  1 Y 1 A HIS 6    ? A HIS 6    
7  1 Y 1 A HIS 7    ? A HIS 7    
8  1 Y 1 A HIS 8    ? A HIS 8    
9  1 Y 1 A HIS 9    ? A HIS 9    
10 1 Y 1 A GLY 10   ? A GLY 10   
11 1 Y 1 A GLU 11   ? A GLU 11   
12 1 Y 1 A PHE 12   ? A PHE 12   
13 1 Y 1 A ASP 13   ? A ASP 13   
14 1 Y 1 A ASP 14   ? A ASP 14   
15 1 Y 1 A PRO 15   ? A PRO 15   
16 1 Y 1 A ILE 16   ? A ILE 16   
17 1 Y 1 A ARG 17   ? A ARG 17   
18 1 Y 1 A PRO 18   ? A PRO 18   
19 1 Y 1 A PRO 19   ? A PRO 19   
20 1 Y 1 A LEU 20   ? A LEU 20   
21 1 Y 1 A LYS 21   ? A LYS 21   
22 1 Y 1 A VAL 22   ? A VAL 22   
23 1 Y 1 A ALA 23   ? A ALA 23   
24 1 Y 1 A ARG 24   ? A ARG 24   
25 1 Y 1 A SER 25   ? A SER 25   
26 1 Y 1 A PRO 26   ? A PRO 26   
27 1 Y 1 A ARG 27   ? A ARG 27   
28 1 Y 1 A PRO 28   ? A PRO 28   
29 1 Y 1 A GLY 29   ? A GLY 29   
30 1 Y 1 A GLN 30   ? A GLN 30   
31 1 Y 1 A SER 1045 ? A SER 1045 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE             NAG 
3 'ZINC ION'                         ZN  
4 '5-FLUORO-BETA-L-GULOSYL FLUORIDE' GUL 
5 '(4S)-2-METHYL-2,4-PENTANEDIOL'    MPD 
6 water                              HOH 
# 
