data_2F18
# 
_entry.id   2F18 
# 
_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   2F18         
RCSB  RCSB035326   
WWPDB D_1000035326 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1HTY . unspecified 
PDB 1HWW . unspecified 
PDB 1HXK . unspecified 
PDB 1PS2 . unspecified 
PDB 1QWN . unspecified 
PDB 1QX1 . unspecified 
PDB 1R33 . unspecified 
PDB 1R34 . unspecified 
PDB 1TQS . unspecified 
PDB 1TQT . unspecified 
PDB 1TQU . unspecified 
PDB 1TQV . unspecified 
PDB 1TQW . unspecified 
PDB 2ALW . unspecified 
PDB 2F1A . unspecified 
PDB 2F1B . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2F18 
_pdbx_database_status.recvd_initial_deposition_date   2005-11-14 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Kuntz, D.A.' 1 
'Rose, D.R.'  2 
# 
_citation.id                        primary 
_citation.title                     
'Evaluation of docking programs for predicting binding of Golgi alpha-mannosidase II inhibitors: a comparison with crystallography.' 
_citation.journal_abbrev            Proteins 
_citation.journal_volume            69 
_citation.page_first                160 
_citation.page_last                 176 
_citation.year                      2007 
_citation.journal_id_ASTM           PSFGEY 
_citation.country                   US 
_citation.journal_id_ISSN           0887-3585 
_citation.journal_id_CSD            0867 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   17557336 
_citation.pdbx_database_id_DOI      10.1002/prot.21479 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Englebienne, P.'    1 
primary 'Fiaux, H.'          2 
primary 'Kuntz, D.A.'        3 
primary 'Corbeil, C.R.'      4 
primary 'Gerber-Lemaire, S.' 5 
primary 'Rose, D.R.'         6 
primary 'Moitessier, N.'     7 
# 
_cell.entry_id           2F18 
_cell.length_a           68.965 
_cell.length_b           109.724 
_cell.length_c           138.911 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2F18 
_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 
_symmetry.space_group_name_Hall            ? 
# 
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'                                                           119701.617 1    3.2.1.114 ? 
'CATALYTIC DOMAIN' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE                                                           221.208    1    ?         ? ? ? 
3 non-polymer syn 'PHOSPHATE ION'                                                                  94.971     1    ?         ? ? ? 
4 non-polymer syn 'ZINC ION'                                                                       65.409     1    ?         ? ? ? 
5 non-polymer syn '(2R,3R,4S)-2-({[(1R)-2-HYDROXY-1-PHENYLETHYL]AMINO}METHYL)PYRROLIDINE-3,4-DIOL' 252.309    1    ?         ? ? ? 
6 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'                                                  118.174    1    ?         ? ? ? 
7 water       nat water                                                                            18.015     1172 ?         ? ? ? 
# 
_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
QWKKKAELYRTNVLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTL
SGDFFTYADRSDNYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKT
HVVVDYEQRMQEALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNT
LPHWREQLVDFYVSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSK
PEHTSYASNLLLRKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSH
GDRSGAYLFLPNGPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDS
GDIFYTDLNGLQFIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQ
GVLDNKPVLHIYRLVLEKVNNCVRPSKLHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVS
VMRRLTKSSAKTQRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYV
SSHSS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;RSSHHHHHHGEFDDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHK
LKVFVVPHSHNDPGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEF
VTGGWVMPDEANSHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQ
RQLEFLWRQIWDNKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVD
QWKKKAELYRTNVLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTL
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  ASP 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, GmII' 
_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 cell' 
_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          'Stable transfection plasmid' 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pMTBIP_NHIS 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    GB 
_struct_ref.db_code                    CAA54732 
_struct_ref.pdbx_db_accession          517481 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHKLKVFVVPHSHND
PGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEFVTGGWVMPDEAN
SHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQRQLEFLWRQIWD
NKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVDQWKKKAELYRTN
VLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTLSGDFFTYADRSD
NYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKTHVVVDYEQRMQE
ALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNTLPHWREQLVDFY
VSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSKPEHTSYASNLLL
RKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSHGDRSGAYLFLPN
GPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDSGDIFYTDLNGLQ
FIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQGVLDNKPVLHIY
RLVLEKVNNCVRPSKLHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVSVMRRLTKSSAKT
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              2F18 
_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             517481 
_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 2F18 ARG A 1  ? GB 517481 ? ? 'EXPRESSION TAG' 1  1  
1 2F18 SER A 2  ? GB 517481 ? ? 'EXPRESSION TAG' 2  2  
1 2F18 SER A 3  ? GB 517481 ? ? 'EXPRESSION TAG' 3  3  
1 2F18 HIS A 4  ? GB 517481 ? ? 'EXPRESSION TAG' 4  4  
1 2F18 HIS A 5  ? GB 517481 ? ? 'EXPRESSION TAG' 5  5  
1 2F18 HIS A 6  ? GB 517481 ? ? 'EXPRESSION TAG' 6  6  
1 2F18 HIS A 7  ? GB 517481 ? ? 'EXPRESSION TAG' 7  7  
1 2F18 HIS A 8  ? GB 517481 ? ? 'EXPRESSION TAG' 8  8  
1 2F18 HIS A 9  ? GB 517481 ? ? 'EXPRESSION TAG' 9  9  
1 2F18 GLY A 10 ? GB 517481 ? ? 'EXPRESSION TAG' 10 10 
1 2F18 GLU A 11 ? GB 517481 ? ? 'EXPRESSION TAG' 11 11 
1 2F18 PHE A 12 ? GB 517481 ? ? 'EXPRESSION TAG' 12 12 
# 
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 
GB1 non-polymer         . '(2R,3R,4S)-2-({[(1R)-2-HYDROXY-1-PHENYLETHYL]AMINO}METHYL)PYRROLIDINE-3,4-DIOL' ? 'C13 H20 N2 O3'  
252.309 
GLN 'L-peptide linking' y GLUTAMINE                                                                        ? 'C5 H10 N2 O3'   
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                  ? 'C5 H9 N O4'     
147.129 
GLY 'peptide linking'   y GLYCINE                                                                          ? 'C2 H5 N O2'     
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                        ? 'C6 H10 N3 O2 1' 
156.162 
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 
PO4 non-polymer         . 'PHOSPHATE ION'                                                                  ? 'O4 P -3'        
94.971  
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          2F18 
_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   43.94 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_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    'Tris, PEG 6K, MPD, NaCl, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   2004-12-10 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9793376 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 19-ID' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9793376 
# 
_reflns.entry_id                     2F18 
_reflns.observed_criterion_sigma_I   2 
_reflns.observed_criterion_sigma_F   2 
_reflns.d_resolution_low             30 
_reflns.d_resolution_high            1.3 
_reflns.number_obs                   257516 
_reflns.number_all                   257854 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.066 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        39 
_reflns.B_iso_Wilson_estimate        13.0 
_reflns.pdbx_redundancy              10.8 
_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_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.3 
_reflns_shell.d_res_low              1.35 
_reflns_shell.percent_possible_all   99.6 
_reflns_shell.Rmerge_I_obs           0.35 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    5.1 
_reflns_shell.pdbx_redundancy        5 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      25391 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2F18 
_refine.ls_number_reflns_obs                     252466 
_refine.ls_number_reflns_all                     258145 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               536245.31 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             29.85 
_refine.ls_d_res_high                            1.30 
_refine.ls_percent_reflns_obs                    97.8 
_refine.ls_R_factor_obs                          0.168 
_refine.ls_R_factor_all                          0.168 
_refine.ls_R_factor_R_work                       0.168 
_refine.ls_R_factor_R_free                       0.18 
_refine.ls_R_factor_R_free_error                 0.003 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 1.9 
_refine.ls_number_reflns_R_free                  4740 
_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                               15.8 
_refine.aniso_B[1][1]                            -0.81 
_refine.aniso_B[2][2]                            0.89 
_refine.aniso_B[3][3]                            -0.08 
_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                 0.325707 
_refine.solvent_model_param_bsol                 43.9992 
_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                                  
;The data was collected to 1.21, but since the I/sigmaI was not great in the last shell, data was only refined to a 1.3 A stucture. However sf file contains all the data. The difference in unique reflections is a difference in the way good reflections are assessed between scalepack and CNS.
;
_refine.pdbx_starting_model                      'PDB ENTRY 1HWW' 
_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.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_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                        2F18 
_refine_analyze.Luzzati_coordinate_error_obs    0.13 
_refine_analyze.Luzzati_sigma_a_obs             0.10 
_refine_analyze.Luzzati_d_res_low_obs           30.00 
_refine_analyze.Luzzati_coordinate_error_free   0.14 
_refine_analyze.Luzzati_sigma_a_free            0.10 
_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         46 
_refine_hist.number_atoms_solvent             1172 
_refine_hist.number_atoms_total               9399 
_refine_hist.d_res_high                       1.30 
_refine_hist.d_res_low                        29.85 
# 
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                0.019 ?    ? ? '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             1.9   ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      25.4  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      1.31  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             0.97  1.50 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            1.59  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             1.88  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            2.92  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       1.30 
_refine_ls_shell.d_res_low                        1.38 
_refine_ls_shell.number_reflns_R_work             38928 
_refine_ls_shell.R_factor_R_work                  0.226 
_refine_ls_shell.percent_reflns_obs               93.6 
_refine_ls_shell.R_factor_R_free                  0.231 
_refine_ls_shell.R_factor_R_free_error            0.008 
_refine_ls_shell.percent_reflns_R_free            2.4 
_refine_ls_shell.number_reflns_R_free             945 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
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.param  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' 
6 po4.par            po4.top          'X-RAY DIFFRACTION' 
7 GB1.par            GB1.top          'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2F18 
_struct.title                     
'GOLGI ALPHA-MANNOSIDASE II complex with (2R,3R,4S)-2-({[(1R)-2-hydroxy-1-phenylethyl]amino}methyl)pyrrolidine-3,4-diol' 
_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        2F18 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'GLYCOSYL HYDROLASE FAMILY 38, 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 ? 
G N N 7 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  ? HIS A 139  ? GLU A 130  HIS A 139  1 ? 10 
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  ? MET A 290  ? GLN A 284  MET A 290  5 ? 7  
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 ? ? ? ? ? ? ? 2.062 ? 
disulf2 disulf ? ? A CYS 275  SG  ? ? ? 1_555 A CYS 282  SG ? ? A CYS 275  A CYS 282  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf3 disulf ? ? A CYS 283  SG  ? ? ? 1_555 A CYS 297  SG ? ? A CYS 283  A CYS 297  1_555 ? ? ? ? ? ? ? 2.058 ? 
disulf4 disulf ? ? A CYS 902  SG  ? ? ? 1_555 A CYS 987  SG ? ? A CYS 902  A CYS 987  1_555 ? ? ? ? ? ? ? 2.056 ? 
disulf5 disulf ? ? A CYS 1000 SG  ? ? ? 1_555 A CYS 1009 SG ? ? A CYS 1000 A CYS 1009 1_555 ? ? ? ? ? ? ? 2.000 ? 
covale1 covale ? ? A ASN 194  ND2 ? ? ? 1_555 B NAG .    C1 ? ? A ASN 194  A NAG 1802 1_555 ? ? ? ? ? ? ? 1.459 ? 
metalc1 metalc ? ? A HIS 90   NE2 ? ? ? 1_555 D ZN  .    ZN ? ? A HIS 90   A ZN  1805 1_555 ? ? ? ? ? ? ? 2.116 ? 
metalc2 metalc ? ? A ASP 92   OD1 ? ? ? 1_555 D ZN  .    ZN ? ? A ASP 92   A ZN  1805 1_555 ? ? ? ? ? ? ? 2.129 ? 
metalc3 metalc ? ? A ASP 204  OD2 ? ? ? 1_555 D ZN  .    ZN ? ? A ASP 204  A ZN  1805 1_555 ? ? ? ? ? ? ? 2.086 ? 
metalc4 metalc ? ? A HIS 471  NE2 ? ? ? 1_555 D ZN  .    ZN ? ? A HIS 471  A ZN  1805 1_555 ? ? ? ? ? ? ? 2.112 ? 
metalc5 metalc ? ? D ZN  .    ZN  ? ? ? 1_555 E GB1 .    O3 ? ? A ZN  1805 A GB1 1804 1_555 ? ? ? ? ? ? ? 2.178 ? 
metalc6 metalc ? ? D ZN  .    ZN  ? ? ? 1_555 E GB1 .    O4 ? ? A ZN  1805 A GB1 1804 1_555 ? ? ? ? ? ? ? 2.261 ? 
# 
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 -4.30 
2 TRP 531 A . ? TRP 531 A PRO 532 A ? PRO 532 A 1 -0.18 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 6  ? 
B ? 3  ? 
C ? 2  ? 
D ? 6  ? 
E ? 5  ? 
F ? 5  ? 
G ? 12 ? 
H ? 5  ? 
I ? 8  ? 
J ? 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 
D 2  3  ? anti-parallel 
D 3  4  ? anti-parallel 
D 4  5  ? anti-parallel 
D 5  6  ? anti-parallel 
E 1  2  ? anti-parallel 
E 2  3  ? anti-parallel 
E 3  4  ? anti-parallel 
E 4  5  ? anti-parallel 
F 1  2  ? parallel      
F 2  3  ? anti-parallel 
F 3  4  ? anti-parallel 
F 4  5  ? parallel      
G 1  2  ? parallel      
G 2  3  ? anti-parallel 
G 3  4  ? anti-parallel 
G 4  5  ? anti-parallel 
G 5  6  ? anti-parallel 
G 6  7  ? anti-parallel 
G 7  8  ? anti-parallel 
G 8  9  ? anti-parallel 
G 9  10 ? anti-parallel 
G 10 11 ? anti-parallel 
G 11 12 ? anti-parallel 
H 1  2  ? anti-parallel 
H 2  3  ? anti-parallel 
H 3  4  ? anti-parallel 
H 4  5  ? anti-parallel 
I 1  2  ? anti-parallel 
I 2  3  ? anti-parallel 
I 3  4  ? anti-parallel 
I 4  5  ? anti-parallel 
I 5  6  ? anti-parallel 
I 6  7  ? anti-parallel 
I 7  8  ? anti-parallel 
J 1  2  ? anti-parallel 
J 2  3  ? anti-parallel 
J 3  4  ? anti-parallel 
J 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  ? ASP A 341  ? VAL A 333  ASP 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  PHE A 524  ? ASP A 527  ? PHE A 524  ASP A 527  
D 2  ASP A 930  ? PHE A 934  ? ASP A 930  PHE A 934  
D 3  SER A 552  ? ASN A 559  ? SER A 552  ASN A 559  
D 4  GLY A 628  ? ILE A 636  ? GLY A 628  ILE A 636  
D 5  VAL A 578  ? ASP A 582  ? VAL A 578  ASP A 582  
D 6  PRO A 587  ? VAL A 588  ? PRO A 587  VAL A 588  
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  GLN A 945  ? PHE A 946  ? GLN A 945  PHE A 946  
F 1  THR A 542  ? ILE A 543  ? THR A 542  ILE A 543  
F 2  ARG A 565  ? VAL A 573  ? ARG A 565  VAL A 573  
F 3  THR A 606  ? VAL A 624  ? THR A 606  VAL A 624  
F 4  ALA A 590  ? ASP A 601  ? ALA A 590  ASP A 601  
F 5  THR A 644  ? TYR A 646  ? THR A 644  TYR A 646  
G 1  LYS A 669  ? GLY A 671  ? LYS A 669  GLY A 671  
G 2  SER A 648  ? LEU A 652  ? SER A 648  LEU A 652  
G 3  VAL A 745  ? LYS A 749  ? VAL A 745  LYS A 749  
G 4  SER A 754  ? LEU A 760  ? SER A 754  LEU A 760  
G 5  VAL A 763  ? MET A 769  ? VAL A 763  MET A 769  
G 6  GLU A 775  ? VAL A 780  ? GLU A 775  VAL A 780  
G 7  VAL A 888  ? LYS A 898  ? VAL A 888  LYS A 898  
G 8  THR A 842  ? THR A 848  ? THR A 842  THR A 848  
G 9  GLY A 834  ? GLU A 838  ? GLY A 834  GLU A 838  
G 10 ILE A 803  ? LEU A 808  ? ILE A 803  LEU A 808  
G 11 GLN A 812  ? ARG A 817  ? GLN A 812  ARG A 817  
G 12 ALA A 911  ? GLY A 912  ? ALA A 911  GLY A 912  
H 1  ILE A 676  ? ARG A 679  ? ILE A 676  ARG A 679  
H 2  THR A 685  ? PHE A 688  ? THR A 685  PHE A 688  
H 3  LEU A 694  ? GLN A 698  ? LEU A 694  GLN A 698  
H 4  HIS A 705  ? TYR A 715  ? HIS A 705  TYR A 715  
H 5  SER A 736  ? PRO A 737  ? SER A 736  PRO A 737  
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  HIS A 705  ? TYR A 715  ? HIS A 705  TYR A 715  
I 5  THR A 788  ? THR A 796  ? THR A 788  THR A 796  
I 6  GLU A 861  ? ARG A 869  ? GLU A 861  ARG A 869  
I 7  LEU A 852  ? SER A 855  ? LEU A 852  SER A 855  
I 8  TYR A 829  ? ILE A 831  ? TYR A 829  ILE A 831  
J 1  LEU A 957  ? ARG A 964  ? LEU A 957  ARG A 964  
J 2  GLN A 973  ? ARG A 981  ? GLN A 973  ARG A 981  
J 3  THR A 1036 ? HIS A 1043 ? THR A 1036 HIS A 1043 
J 4  VAL A 1006 ? THR A 1012 ? VAL A 1006 THR A 1012 
J 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 SER A 401  ? O SER A 401  
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 LEU A 225  ? O LEU A 225  N ALA A 202  ? N ALA A 202  
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 85   ? N VAL A 85   O GLN A 375  ? O GLN A 375  
C 1  2  N PHE A 126  ? N PHE A 126  O GLU A 159  ? O GLU A 159  
D 1  2  N THR A 525  ? N THR A 525  O ILE A 933  ? O ILE A 933  
D 2  3  O PHE A 932  ? O PHE A 932  N VAL A 556  ? N VAL A 556  
D 3  4  N VAL A 555  ? N VAL A 555  O TYR A 632  ? O TYR A 632  
D 4  5  O VAL A 633  ? O VAL A 633  N THR A 581  ? N THR A 581  
D 5  6  N VAL A 580  ? N VAL A 580  O VAL A 588  ? O VAL A 588  
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  N LEU A 629  ? N LEU A 629  O PHE A 946  ? O PHE A 946  
F 1  2  N ILE A 543  ? N ILE A 543  O TYR A 572  ? O TYR A 572  
F 2  3  N ARG A 565  ? N ARG A 565  O VAL A 624  ? O VAL A 624  
F 3  4  O GLN A 610  ? O GLN A 610  N SER A 597  ? N SER A 597  
F 4  5  N VAL A 592  ? N VAL A 592  O SER A 645  ? O SER A 645  
G 1  2  O LYS A 669  ? O LYS A 669  N LEU A 651  ? N LEU A 651  
G 2  3  N LEU A 652  ? N LEU A 652  O VAL A 745  ? O VAL A 745  
G 3  4  N LEU A 746  ? N LEU A 746  O SER A 757  ? O SER A 757  
G 4  5  N SER A 754  ? N SER A 754  O MET A 769  ? O MET A 769  
G 5  6  N ILE A 768  ? N ILE A 768  O GLU A 775  ? O GLU A 775  
G 6  7  N VAL A 780  ? N VAL A 780  O VAL A 888  ? O VAL A 888  
G 7  8  O VAL A 895  ? O VAL A 895  N THR A 845  ? N THR A 845  
G 8  9  O LEU A 846  ? O LEU A 846  N MET A 835  ? N MET A 835  
G 9  10 O PHE A 836  ? O PHE A 836  N TYR A 805  ? N TYR A 805  
G 10 11 N PHE A 804  ? N PHE A 804  O ARG A 816  ? O ARG A 816  
G 11 12 N PHE A 813  ? N PHE A 813  O GLY A 912  ? O GLY A 912  
H 1  2  N ILE A 676  ? N ILE A 676  O PHE A 688  ? O PHE A 688  
H 2  3  N ALA A 687  ? N ALA A 687  O LYS A 695  ? O LYS A 695  
H 3  4  N ILE A 697  ? N ILE A 697  O VAL A 706  ? O VAL A 706  
H 4  5  N LYS A 714  ? N LYS A 714  O SER A 736  ? O SER A 736  
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 711  ? N LYS A 711  O ARG A 793  ? O ARG A 793  
I 5  6  N ILE A 790  ? N ILE A 790  O GLN A 866  ? O GLN A 866  
I 6  7  O MET A 865  ? O MET A 865  N GLY A 853  ? N GLY A 853  
I 7  8  O GLY A 854  ? O GLY A 854  N TYR A 829  ? N TYR A 829  
J 1  2  N ARG A 963  ? N ARG A 963  O GLY A 976  ? O GLY A 976  
J 2  3  N LEU A 979  ? N LEU A 979  O ALA A 1037 ? O ALA A 1037 
J 3  4  O SER A 1042 ? O SER A 1042 N ALA A 1007 ? N ALA A 1007 
J 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 ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG A 1802' 
AC2 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE PO4 A 1803' 
AC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN A 1805'  
AC4 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE GB1 A 1804' 
AC5 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MPD A 1801' 
# 
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 1  ASN A 194 ? ASN A 194  . ? 1_555 ? 
2  AC2 9  ARG A 770 ? ARG A 770  . ? 1_555 ? 
3  AC2 9  ARG A 893 ? ARG A 893  . ? 1_555 ? 
4  AC2 9  SER A 924 ? SER A 924  . ? 1_555 ? 
5  AC2 9  HOH G .   ? HOH A 1939 . ? 1_555 ? 
6  AC2 9  HOH G .   ? HOH A 1941 . ? 1_555 ? 
7  AC2 9  HOH G .   ? HOH A 1942 . ? 1_555 ? 
8  AC2 9  HOH G .   ? HOH A 2909 . ? 1_555 ? 
9  AC2 9  HOH G .   ? HOH A 2926 . ? 1_555 ? 
10 AC2 9  HOH G .   ? HOH A 2933 . ? 1_555 ? 
11 AC3 5  HIS A 90  ? HIS A 90   . ? 1_555 ? 
12 AC3 5  ASP A 92  ? ASP A 92   . ? 1_555 ? 
13 AC3 5  ASP A 204 ? ASP A 204  . ? 1_555 ? 
14 AC3 5  HIS A 471 ? HIS A 471  . ? 1_555 ? 
15 AC3 5  GB1 E .   ? GB1 A 1804 . ? 1_555 ? 
16 AC4 15 HIS A 90  ? HIS A 90   . ? 1_555 ? 
17 AC4 15 ASP A 92  ? ASP A 92   . ? 1_555 ? 
18 AC4 15 TRP A 95  ? TRP A 95   . ? 1_555 ? 
19 AC4 15 ASP A 204 ? ASP A 204  . ? 1_555 ? 
20 AC4 15 ARG A 228 ? ARG A 228  . ? 1_555 ? 
21 AC4 15 TYR A 269 ? TYR A 269  . ? 1_555 ? 
22 AC4 15 ASP A 340 ? ASP A 340  . ? 1_555 ? 
23 AC4 15 ASP A 341 ? ASP A 341  . ? 1_555 ? 
24 AC4 15 HIS A 471 ? HIS A 471  . ? 1_555 ? 
25 AC4 15 ASP A 472 ? ASP A 472  . ? 1_555 ? 
26 AC4 15 TYR A 727 ? TYR A 727  . ? 1_555 ? 
27 AC4 15 GLY A 877 ? GLY A 877  . ? 1_555 ? 
28 AC4 15 ZN  D .   ? ZN  A 1805 . ? 1_555 ? 
29 AC4 15 HOH G .   ? HOH A 2498 . ? 1_555 ? 
30 AC4 15 HOH G .   ? HOH A 2723 . ? 1_555 ? 
31 AC5 7  LYS A 63  ? LYS A 63   . ? 1_555 ? 
32 AC5 7  GLN A 64  ? GLN A 64   . ? 1_555 ? 
33 AC5 7  HIS A 273 ? HIS A 273  . ? 1_555 ? 
34 AC5 7  HOH G .   ? HOH A 2362 . ? 1_555 ? 
35 AC5 7  HOH G .   ? HOH A 2513 . ? 1_555 ? 
36 AC5 7  HOH G .   ? HOH A 2514 . ? 1_555 ? 
37 AC5 7  HOH G .   ? HOH A 2516 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2F18 
_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                    2F18 
_atom_sites.fract_transf_matrix[1][1]   0.014500 
_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]   0.009114 
_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]   0.007199 
_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  
N  
O  
P  
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   ? 44.158 35.938  -18.994 1.00 23.70 ? 31   CYS A N   1 
ATOM   2    C  CA  . CYS A 1 31   ? 43.409 37.162  -18.573 1.00 21.88 ? 31   CYS A CA  1 
ATOM   3    C  C   . CYS A 1 31   ? 41.909 36.957  -18.632 1.00 20.75 ? 31   CYS A C   1 
ATOM   4    O  O   . CYS A 1 31   ? 41.396 36.384  -19.619 1.00 21.80 ? 31   CYS A O   1 
ATOM   5    C  CB  . CYS A 1 31   ? 43.715 38.327  -19.514 1.00 21.45 ? 31   CYS A CB  1 
ATOM   6    S  SG  . CYS A 1 31   ? 45.415 38.987  -19.520 1.00 23.16 ? 31   CYS A SG  1 
ATOM   7    N  N   . GLN A 1 32   ? 41.196 37.485  -17.642 1.00 19.69 ? 32   GLN A N   1 
ATOM   8    C  CA  . GLN A 1 32   ? 39.740 37.416  -17.614 1.00 19.41 ? 32   GLN A CA  1 
ATOM   9    C  C   . GLN A 1 32   ? 39.227 38.341  -18.722 1.00 17.41 ? 32   GLN A C   1 
ATOM   10   O  O   . GLN A 1 32   ? 39.822 39.398  -19.013 1.00 15.53 ? 32   GLN A O   1 
ATOM   11   C  CB  . GLN A 1 32   ? 39.162 37.968  -16.306 1.00 21.41 ? 32   GLN A CB  1 
ATOM   12   C  CG  . GLN A 1 32   ? 39.303 37.107  -15.086 1.00 23.15 ? 32   GLN A CG  1 
ATOM   13   C  CD  . GLN A 1 32   ? 38.210 37.416  -14.050 1.00 24.58 ? 32   GLN A CD  1 
ATOM   14   O  OE1 . GLN A 1 32   ? 37.101 36.866  -14.120 1.00 25.63 ? 32   GLN A OE1 1 
ATOM   15   N  NE2 . GLN A 1 32   ? 38.515 38.314  -13.098 1.00 25.11 ? 32   GLN A NE2 1 
ATOM   16   N  N   . ASP A 1 33   ? 38.114 37.941  -19.336 1.00 17.53 ? 33   ASP A N   1 
ATOM   17   C  CA  . ASP A 1 33   ? 37.478 38.750  -20.375 1.00 15.89 ? 33   ASP A CA  1 
ATOM   18   C  C   . ASP A 1 33   ? 36.564 39.742  -19.624 1.00 16.10 ? 33   ASP A C   1 
ATOM   19   O  O   . ASP A 1 33   ? 35.588 39.350  -18.983 1.00 18.04 ? 33   ASP A O   1 
ATOM   20   C  CB  . ASP A 1 33   ? 36.664 37.812  -21.284 1.00 16.78 ? 33   ASP A CB  1 
ATOM   21   C  CG  . ASP A 1 33   ? 36.008 38.521  -22.451 1.00 18.63 ? 33   ASP A CG  1 
ATOM   22   O  OD1 . ASP A 1 33   ? 35.554 39.683  -22.326 1.00 18.36 ? 33   ASP A OD1 1 
ATOM   23   O  OD2 . ASP A 1 33   ? 35.885 37.872  -23.529 1.00 20.60 ? 33   ASP A OD2 1 
ATOM   24   N  N   . VAL A 1 34   ? 36.832 41.041  -19.743 1.00 12.28 ? 34   VAL A N   1 
ATOM   25   C  CA  . VAL A 1 34   ? 36.036 42.006  -19.012 1.00 10.78 ? 34   VAL A CA  1 
ATOM   26   C  C   . VAL A 1 34   ? 34.857 42.578  -19.765 1.00 9.90  ? 34   VAL A C   1 
ATOM   27   O  O   . VAL A 1 34   ? 34.160 43.434  -19.261 1.00 10.31 ? 34   VAL A O   1 
ATOM   28   C  CB  . VAL A 1 34   ? 36.915 43.165  -18.512 1.00 11.39 ? 34   VAL A CB  1 
ATOM   29   C  CG1 . VAL A 1 34   ? 38.169 42.593  -17.807 1.00 13.47 ? 34   VAL A CG1 1 
ATOM   30   C  CG2 . VAL A 1 34   ? 37.381 44.074  -19.719 1.00 11.97 ? 34   VAL A CG2 1 
ATOM   31   N  N   . VAL A 1 35   ? 34.611 42.002  -20.954 1.00 11.22 ? 35   VAL A N   1 
ATOM   32   C  CA  . VAL A 1 35   ? 33.506 42.462  -21.795 1.00 11.28 ? 35   VAL A CA  1 
ATOM   33   C  C   . VAL A 1 35   ? 32.330 41.512  -21.999 1.00 11.49 ? 35   VAL A C   1 
ATOM   34   O  O   . VAL A 1 35   ? 31.170 41.898  -21.910 1.00 11.16 ? 35   VAL A O   1 
ATOM   35   C  CB  . VAL A 1 35   ? 34.018 42.785  -23.198 1.00 11.48 ? 35   VAL A CB  1 
ATOM   36   C  CG1 . VAL A 1 35   ? 32.870 43.199  -24.127 1.00 12.59 ? 35   VAL A CG1 1 
ATOM   37   C  CG2 . VAL A 1 35   ? 35.103 43.929  -23.090 1.00 13.23 ? 35   VAL A CG2 1 
ATOM   38   N  N   . GLN A 1 36   ? 32.661 40.250  -22.264 1.00 12.89 ? 36   GLN A N   1 
ATOM   39   C  CA  . GLN A 1 36   ? 31.670 39.263  -22.714 1.00 14.33 ? 36   GLN A CA  1 
ATOM   40   C  C   . GLN A 1 36   ? 31.066 38.360  -21.676 1.00 16.54 ? 36   GLN A C   1 
ATOM   41   O  O   . GLN A 1 36   ? 30.121 37.654  -21.972 1.00 19.92 ? 36   GLN A O   1 
ATOM   42   C  CB  . GLN A 1 36   ? 32.349 38.419  -23.794 1.00 14.51 ? 36   GLN A CB  1 
ATOM   43   C  CG  . GLN A 1 36   ? 33.010 39.264  -24.879 1.00 16.16 ? 36   GLN A CG  1 
ATOM   44   C  CD  . GLN A 1 36   ? 33.474 38.441  -26.041 1.00 15.89 ? 36   GLN A CD  1 
ATOM   45   O  OE1 . GLN A 1 36   ? 32.730 38.254  -26.991 1.00 17.56 ? 36   GLN A OE1 1 
ATOM   46   N  NE2 . GLN A 1 36   ? 34.708 37.977  -25.988 1.00 16.63 ? 36   GLN A NE2 1 
ATOM   47   N  N   . ASP A 1 37   ? 31.610 38.357  -20.467 1.00 16.91 ? 37   ASP A N   1 
ATOM   48   C  CA  . ASP A 1 37   ? 31.097 37.502  -19.406 1.00 18.32 ? 37   ASP A CA  1 
ATOM   49   C  C   . ASP A 1 37   ? 30.380 38.328  -18.304 1.00 16.55 ? 37   ASP A C   1 
ATOM   50   O  O   . ASP A 1 37   ? 31.069 38.956  -17.481 1.00 19.67 ? 37   ASP A O   1 
ATOM   51   C  CB  . ASP A 1 37   ? 32.274 36.692  -18.771 1.00 20.47 ? 37   ASP A CB  1 
ATOM   52   C  CG  . ASP A 1 37   ? 32.905 35.651  -19.740 1.00 22.36 ? 37   ASP A CG  1 
ATOM   53   O  OD1 . ASP A 1 37   ? 32.136 34.983  -20.444 1.00 24.76 ? 37   ASP A OD1 1 
ATOM   54   O  OD2 . ASP A 1 37   ? 34.154 35.491  -19.784 1.00 23.84 ? 37   ASP A OD2 1 
ATOM   55   N  N   . VAL A 1 38   ? 29.061 38.299  -18.259 1.00 16.08 ? 38   VAL A N   1 
ATOM   56   C  CA  . VAL A 1 38   ? 28.319 39.040  -17.208 1.00 14.84 ? 38   VAL A CA  1 
ATOM   57   C  C   . VAL A 1 38   ? 28.501 38.340  -15.860 1.00 15.18 ? 38   VAL A C   1 
ATOM   58   O  O   . VAL A 1 38   ? 28.114 37.181  -15.711 1.00 15.47 ? 38   VAL A O   1 
ATOM   59   C  CB  . VAL A 1 38   ? 26.809 39.153  -17.505 1.00 15.46 ? 38   VAL A CB  1 
ATOM   60   C  CG1 . VAL A 1 38   ? 26.080 39.883  -16.321 1.00 14.32 ? 38   VAL A CG1 1 
ATOM   61   C  CG2 . VAL A 1 38   ? 26.596 39.897  -18.876 1.00 16.84 ? 38   VAL A CG2 1 
ATOM   62   N  N   . PRO A 1 39   ? 29.111 38.997  -14.866 1.00 13.88 ? 39   PRO A N   1 
ATOM   63   C  CA  . PRO A 1 39   ? 29.276 38.297  -13.584 1.00 12.74 ? 39   PRO A CA  1 
ATOM   64   C  C   . PRO A 1 39   ? 27.981 37.956  -12.920 1.00 12.72 ? 39   PRO A C   1 
ATOM   65   O  O   . PRO A 1 39   ? 27.022 38.688  -12.992 1.00 13.60 ? 39   PRO A O   1 
ATOM   66   C  CB  . PRO A 1 39   ? 30.050 39.293  -12.723 1.00 12.92 ? 39   PRO A CB  1 
ATOM   67   C  CG  . PRO A 1 39   ? 30.818 40.134  -13.742 1.00 12.30 ? 39   PRO A CG  1 
ATOM   68   C  CD  . PRO A 1 39   ? 29.837 40.287  -14.897 1.00 13.85 ? 39   PRO A CD  1 
ATOM   69   N  N   . ASN A 1 40   ? 27.973 36.798  -12.236 1.00 13.76 ? 40   ASN A N   1 
ATOM   70   C  CA  . ASN A 1 40   ? 26.821 36.404  -11.468 1.00 14.52 ? 40   ASN A CA  1 
ATOM   71   C  C   . ASN A 1 40   ? 27.102 36.754  -10.000 1.00 13.51 ? 40   ASN A C   1 
ATOM   72   O  O   . ASN A 1 40   ? 28.016 36.193  -9.356  1.00 14.97 ? 40   ASN A O   1 
ATOM   73   C  CB  . ASN A 1 40   ? 26.550 34.900  -11.659 1.00 18.61 ? 40   ASN A CB  1 
ATOM   74   C  CG  . ASN A 1 40   ? 25.507 34.369  -10.724 1.00 22.27 ? 40   ASN A CG  1 
ATOM   75   O  OD1 . ASN A 1 40   ? 24.455 34.991  -10.490 1.00 25.13 ? 40   ASN A OD1 1 
ATOM   76   N  ND2 . ASN A 1 40   ? 25.783 33.196  -10.164 1.00 25.68 ? 40   ASN A ND2 1 
ATOM   77   N  N   . VAL A 1 41   ? 26.364 37.748  -9.528  1.00 12.30 ? 41   VAL A N   1 
ATOM   78   C  CA  . VAL A 1 41   ? 26.514 38.229  -8.131  1.00 11.21 ? 41   VAL A CA  1 
ATOM   79   C  C   . VAL A 1 41   ? 25.166 38.217  -7.453  1.00 11.42 ? 41   VAL A C   1 
ATOM   80   O  O   . VAL A 1 41   ? 24.099 38.327  -8.075  1.00 12.81 ? 41   VAL A O   1 
ATOM   81   C  CB  . VAL A 1 41   ? 27.137 39.671  -8.067  1.00 10.72 ? 41   VAL A CB  1 
ATOM   82   C  CG1 . VAL A 1 41   ? 28.583 39.616  -8.506  1.00 12.81 ? 41   VAL A CG1 1 
ATOM   83   C  CG2 . VAL A 1 41   ? 26.276 40.697  -8.931  1.00 11.66 ? 41   VAL A CG2 1 
ATOM   84   N  N   . ASP A 1 42   ? 25.186 38.130  -6.120  1.00 10.59 ? 42   ASP A N   1 
ATOM   85   C  CA  . ASP A 1 42   ? 23.925 38.123  -5.394  1.00 10.93 ? 42   ASP A CA  1 
ATOM   86   C  C   . ASP A 1 42   ? 23.218 39.479  -5.401  1.00 11.09 ? 42   ASP A C   1 
ATOM   87   O  O   . ASP A 1 42   ? 21.962 39.579  -5.407  1.00 12.24 ? 42   ASP A O   1 
ATOM   88   C  CB  . ASP A 1 42   ? 24.134 37.674  -3.929  1.00 11.89 ? 42   ASP A CB  1 
ATOM   89   C  CG  . ASP A 1 42   ? 24.699 36.281  -3.839  1.00 14.11 ? 42   ASP A CG  1 
ATOM   90   O  OD1 . ASP A 1 42   ? 24.073 35.357  -4.462  1.00 17.60 ? 42   ASP A OD1 1 
ATOM   91   O  OD2 . ASP A 1 42   ? 25.761 36.025  -3.214  1.00 14.36 ? 42   ASP A OD2 1 
ATOM   92   N  N   . VAL A 1 43   ? 24.012 40.561  -5.329  1.00 10.26 ? 43   VAL A N   1 
ATOM   93   C  CA  . VAL A 1 43   ? 23.478 41.916  -5.333  1.00 10.21 ? 43   VAL A CA  1 
ATOM   94   C  C   . VAL A 1 43   ? 24.232 42.690  -6.421  1.00 9.72  ? 43   VAL A C   1 
ATOM   95   O  O   . VAL A 1 43   ? 25.480 42.755  -6.394  1.00 10.15 ? 43   VAL A O   1 
ATOM   96   C  CB  . VAL A 1 43   ? 23.713 42.625  -3.992  1.00 9.30  ? 43   VAL A CB  1 
ATOM   97   C  CG1 . VAL A 1 43   ? 23.092 44.017  -4.035  1.00 11.29 ? 43   VAL A CG1 1 
ATOM   98   C  CG2 . VAL A 1 43   ? 23.039 41.820  -2.839  1.00 11.78 ? 43   VAL A CG2 1 
ATOM   99   N  N   . GLN A 1 44   ? 23.505 43.234  -7.399  1.00 9.14  ? 44   GLN A N   1 
ATOM   100  C  CA  . GLN A 1 44   ? 24.131 44.038  -8.453  1.00 9.36  ? 44   GLN A CA  1 
ATOM   101  C  C   . GLN A 1 44   ? 23.403 45.352  -8.308  1.00 8.83  ? 44   GLN A C   1 
ATOM   102  O  O   . GLN A 1 44   ? 22.209 45.425  -8.452  1.00 9.35  ? 44   GLN A O   1 
ATOM   103  C  CB  . GLN A 1 44   ? 23.932 43.377  -9.813  1.00 10.24 ? 44   GLN A CB  1 
ATOM   104  C  CG  . GLN A 1 44   ? 25.010 43.802  -10.819 1.00 9.05  ? 44   GLN A CG  1 
ATOM   105  C  CD  . GLN A 1 44   ? 25.068 45.309  -10.958 1.00 8.85  ? 44   GLN A CD  1 
ATOM   106  O  OE1 . GLN A 1 44   ? 24.058 45.950  -11.306 1.00 10.08 ? 44   GLN A OE1 1 
ATOM   107  N  NE2 . GLN A 1 44   ? 26.255 45.900  -10.668 1.00 8.63  ? 44   GLN A NE2 1 
ATOM   108  N  N   . MET A 1 45   ? 24.138 46.417  -7.972  1.00 8.73  ? 45   MET A N   1 
ATOM   109  C  CA  . MET A 1 45   ? 23.453 47.638  -7.596  1.00 8.59  ? 45   MET A CA  1 
ATOM   110  C  C   . MET A 1 45   ? 22.535 48.318  -8.615  1.00 7.54  ? 45   MET A C   1 
ATOM   111  O  O   . MET A 1 45   ? 21.556 48.946  -8.223  1.00 9.29  ? 45   MET A O   1 
ATOM   112  C  CB  . MET A 1 45   ? 24.481 48.634  -7.017  1.00 8.13  ? 45   MET A CB  1 
ATOM   113  C  CG  . MET A 1 45   ? 25.091 48.172  -5.681  1.00 9.51  ? 45   MET A CG  1 
ATOM   114  S  SD  . MET A 1 45   ? 23.877 47.903  -4.364  1.00 10.70 ? 45   MET A SD  1 
ATOM   115  C  CE  . MET A 1 45   ? 23.192 49.611  -4.226  1.00 12.98 ? 45   MET A CE  1 
ATOM   116  N  N   . LEU A 1 46   ? 22.888 48.213  -9.888  1.00 8.52  ? 46   LEU A N   1 
ATOM   117  C  CA  . LEU A 1 46   ? 22.024 48.813  -10.914 1.00 9.29  ? 46   LEU A CA  1 
ATOM   118  C  C   . LEU A 1 46   ? 20.705 47.996  -10.933 1.00 9.98  ? 46   LEU A C   1 
ATOM   119  O  O   . LEU A 1 46   ? 19.641 48.570  -11.056 1.00 10.02 ? 46   LEU A O   1 
ATOM   120  C  CB  . LEU A 1 46   ? 22.714 48.759  -12.274 1.00 10.42 ? 46   LEU A CB  1 
ATOM   121  C  CG  . LEU A 1 46   ? 21.896 49.498  -13.356 1.00 10.86 ? 46   LEU A CG  1 
ATOM   122  C  CD1 . LEU A 1 46   ? 21.946 51.049  -13.129 1.00 11.41 ? 46   LEU A CD1 1 
ATOM   123  C  CD2 . LEU A 1 46   ? 22.467 49.103  -14.705 1.00 11.10 ? 46   LEU A CD2 1 
ATOM   124  N  N   . GLU A 1 47   ? 20.793 46.669  -10.795 1.00 9.98  ? 47   GLU A N   1 
ATOM   125  C  CA  . GLU A 1 47   ? 19.571 45.836  -10.822 1.00 11.23 ? 47   GLU A CA  1 
ATOM   126  C  C   . GLU A 1 47   ? 18.755 46.147  -9.596  1.00 11.49 ? 47   GLU A C   1 
ATOM   127  O  O   . GLU A 1 47   ? 17.525 46.307  -9.649  1.00 12.15 ? 47   GLU A O   1 
ATOM   128  C  CB  . GLU A 1 47   ? 19.975 44.366  -10.868 1.00 12.13 ? 47   GLU A CB  1 
ATOM   129  C  CG  . GLU A 1 47   ? 18.823 43.385  -11.043 1.00 16.12 ? 47   GLU A CG  1 
ATOM   130  C  CD  . GLU A 1 47   ? 18.038 43.109  -9.799  1.00 18.93 ? 47   GLU A CD  1 
ATOM   131  O  OE1 . GLU A 1 47   ? 18.532 43.238  -8.662  1.00 18.25 ? 47   GLU A OE1 1 
ATOM   132  O  OE2 . GLU A 1 47   ? 16.853 42.710  -9.918  1.00 21.93 ? 47   GLU A OE2 1 
ATOM   133  N  N   . LEU A 1 48   ? 19.427 46.283  -8.462  1.00 10.41 ? 48   LEU A N   1 
ATOM   134  C  CA  . LEU A 1 48   ? 18.740 46.591  -7.224  1.00 11.44 ? 48   LEU A CA  1 
ATOM   135  C  C   . LEU A 1 48   ? 18.003 47.922  -7.343  1.00 10.95 ? 48   LEU A C   1 
ATOM   136  O  O   . LEU A 1 48   ? 16.844 48.072  -6.977  1.00 12.98 ? 48   LEU A O   1 
ATOM   137  C  CB  . LEU A 1 48   ? 19.730 46.654  -6.040  1.00 12.59 ? 48   LEU A CB  1 
ATOM   138  C  CG  . LEU A 1 48   ? 19.050 46.786  -4.686  1.00 12.68 ? 48   LEU A CG  1 
ATOM   139  C  CD1 . LEU A 1 48   ? 18.160 45.555  -4.451  1.00 18.11 ? 48   LEU A CD1 1 
ATOM   140  C  CD2 . LEU A 1 48   ? 20.097 46.878  -3.551  1.00 16.69 ? 48   LEU A CD2 1 
ATOM   141  N  N   . TYR A 1 49   ? 18.672 48.926  -7.880  1.00 10.26 ? 49   TYR A N   1 
ATOM   142  C  CA  . TYR A 1 49   ? 18.017 50.202  -8.078  1.00 10.54 ? 49   TYR A CA  1 
ATOM   143  C  C   . TYR A 1 49   ? 16.798 50.112  -8.995  1.00 11.00 ? 49   TYR A C   1 
ATOM   144  O  O   . TYR A 1 49   ? 15.823 50.839  -8.775  1.00 11.37 ? 49   TYR A O   1 
ATOM   145  C  CB  . TYR A 1 49   ? 19.062 51.191  -8.683  1.00 9.41  ? 49   TYR A CB  1 
ATOM   146  C  CG  . TYR A 1 49   ? 19.649 52.120  -7.669  1.00 8.71  ? 49   TYR A CG  1 
ATOM   147  C  CD1 . TYR A 1 49   ? 20.079 51.628  -6.441  1.00 9.58  ? 49   TYR A CD1 1 
ATOM   148  C  CD2 . TYR A 1 49   ? 19.686 53.491  -7.903  1.00 9.99  ? 49   TYR A CD2 1 
ATOM   149  C  CE1 . TYR A 1 49   ? 20.513 52.488  -5.445  1.00 9.24  ? 49   TYR A CE1 1 
ATOM   150  C  CE2 . TYR A 1 49   ? 20.126 54.389  -6.897  1.00 9.13  ? 49   TYR A CE2 1 
ATOM   151  C  CZ  . TYR A 1 49   ? 20.523 53.860  -5.671  1.00 9.03  ? 49   TYR A CZ  1 
ATOM   152  O  OH  . TYR A 1 49   ? 20.887 54.701  -4.644  1.00 9.90  ? 49   TYR A OH  1 
ATOM   153  N  N   . ASP A 1 50   ? 16.852 49.266  -10.021 1.00 10.88 ? 50   ASP A N   1 
ATOM   154  C  CA  . ASP A 1 50   ? 15.719 49.197  -10.948 1.00 13.67 ? 50   ASP A CA  1 
ATOM   155  C  C   . ASP A 1 50   ? 14.505 48.647  -10.199 1.00 14.20 ? 50   ASP A C   1 
ATOM   156  O  O   . ASP A 1 50   ? 13.389 49.096  -10.504 1.00 14.90 ? 50   ASP A O   1 
ATOM   157  C  CB  . ASP A 1 50   ? 16.123 48.276  -12.086 1.00 15.53 ? 50   ASP A CB  1 
ATOM   158  C  CG  . ASP A 1 50   ? 15.329 48.464  -13.337 1.00 18.17 ? 50   ASP A CG  1 
ATOM   159  O  OD1 . ASP A 1 50   ? 14.624 49.468  -13.482 1.00 19.95 ? 50   ASP A OD1 1 
ATOM   160  O  OD2 . ASP A 1 50   ? 15.482 47.556  -14.189 1.00 22.44 ? 50   ASP A OD2 1 
ATOM   161  N  N   . ARG A 1 51   ? 14.716 47.686  -9.303  1.00 14.10 ? 51   ARG A N   1 
ATOM   162  C  CA  . ARG A 1 51   ? 13.606 47.029  -8.543  1.00 15.74 ? 51   ARG A CA  1 
ATOM   163  C  C   . ARG A 1 51   ? 13.100 47.779  -7.309  1.00 15.90 ? 51   ARG A C   1 
ATOM   164  O  O   . ARG A 1 51   ? 11.924 47.694  -6.978  1.00 17.83 ? 51   ARG A O   1 
ATOM   165  C  CB  . ARG A 1 51   ? 14.021 45.636  -8.028  1.00 19.23 ? 51   ARG A CB  1 
ATOM   166  C  CG  . ARG A 1 51   ? 14.645 44.714  -8.996  1.00 25.42 ? 51   ARG A CG  1 
ATOM   167  C  CD  . ARG A 1 51   ? 14.923 43.316  -8.335  1.00 29.58 ? 51   ARG A CD  1 
ATOM   168  N  NE  . ARG A 1 51   ? 14.840 43.359  -6.882  1.00 31.63 ? 51   ARG A NE  1 
ATOM   169  C  CZ  . ARG A 1 51   ? 15.850 43.176  -6.034  1.00 32.76 ? 51   ARG A CZ  1 
ATOM   170  N  NH1 . ARG A 1 51   ? 17.084 42.916  -6.466  1.00 33.25 ? 51   ARG A NH1 1 
ATOM   171  N  NH2 . ARG A 1 51   ? 15.615 43.278  -4.729  1.00 33.58 ? 51   ARG A NH2 1 
ATOM   172  N  N   . MET A 1 52   ? 13.993 48.507  -6.650  1.00 14.48 ? 52   MET A N   1 
ATOM   173  C  CA  . MET A 1 52   ? 13.654 49.233  -5.437  1.00 14.08 ? 52   MET A CA  1 
ATOM   174  C  C   . MET A 1 52   ? 12.626 50.310  -5.604  1.00 13.61 ? 52   MET A C   1 
ATOM   175  O  O   . MET A 1 52   ? 12.612 51.010  -6.619  1.00 14.55 ? 52   MET A O   1 
ATOM   176  C  CB  A MET A 1 52   ? 14.908 49.878  -4.846  0.50 12.75 ? 52   MET A CB  1 
ATOM   177  C  CB  B MET A 1 52   ? 14.730 49.718  -4.571  0.50 15.75 ? 52   MET A CB  1 
ATOM   178  C  CG  A MET A 1 52   ? 15.817 48.883  -4.208  0.50 12.51 ? 52   MET A CG  1 
ATOM   179  C  CG  B MET A 1 52   ? 15.425 48.628  -3.783  0.50 17.44 ? 52   MET A CG  1 
ATOM   180  S  SD  A MET A 1 52   ? 17.340 49.672  -3.603  0.50 11.81 ? 52   MET A SD  1 
ATOM   181  S  SD  B MET A 1 52   ? 16.547 49.282  -2.579  0.50 19.47 ? 52   MET A SD  1 
ATOM   182  C  CE  A MET A 1 52   ? 16.742 50.995  -2.533  0.50 11.47 ? 52   MET A CE  1 
ATOM   183  C  CE  B MET A 1 52   ? 17.694 49.958  -3.742  0.50 18.64 ? 52   MET A CE  1 
ATOM   184  N  N   . SER A 1 53   ? 11.787 50.481  -4.574  1.00 14.09 ? 53   SER A N   1 
ATOM   185  C  CA  . SER A 1 53   ? 10.757 51.512  -4.611  1.00 14.87 ? 53   SER A CA  1 
ATOM   186  C  C   . SER A 1 53   ? 11.177 52.866  -4.005  1.00 14.66 ? 53   SER A C   1 
ATOM   187  O  O   . SER A 1 53   ? 10.561 53.907  -4.271  1.00 15.35 ? 53   SER A O   1 
ATOM   188  C  CB  A SER A 1 53   ? 9.504  50.978  -3.896  0.50 15.18 ? 53   SER A CB  1 
ATOM   189  C  CB  B SER A 1 53   ? 9.329  51.237  -4.105  0.50 15.23 ? 53   SER A CB  1 
ATOM   190  O  OG  A SER A 1 53   ? 8.984  49.904  -4.648  0.50 17.95 ? 53   SER A OG  1 
ATOM   191  O  OG  B SER A 1 53   ? 9.411  50.957  -2.720  0.50 16.66 ? 53   SER A OG  1 
ATOM   192  N  N   . PHE A 1 54   ? 12.196 52.847  -3.155  1.00 13.87 ? 54   PHE A N   1 
ATOM   193  C  CA  . PHE A 1 54   ? 12.680 54.045  -2.510  1.00 12.73 ? 54   PHE A CA  1 
ATOM   194  C  C   . PHE A 1 54   ? 11.643 54.839  -1.712  1.00 13.40 ? 54   PHE A C   1 
ATOM   195  O  O   . PHE A 1 54   ? 11.716 56.079  -1.572  1.00 13.84 ? 54   PHE A O   1 
ATOM   196  C  CB  . PHE A 1 54   ? 13.354 55.005  -3.536  1.00 12.84 ? 54   PHE A CB  1 
ATOM   197  C  CG  . PHE A 1 54   ? 14.617 54.452  -4.178  1.00 10.68 ? 54   PHE A CG  1 
ATOM   198  C  CD1 . PHE A 1 54   ? 14.545 53.615  -5.273  1.00 12.34 ? 54   PHE A CD1 1 
ATOM   199  C  CD2 . PHE A 1 54   ? 15.864 54.796  -3.675  1.00 11.33 ? 54   PHE A CD2 1 
ATOM   200  C  CE1 . PHE A 1 54   ? 15.723 53.121  -5.864  1.00 11.19 ? 54   PHE A CE1 1 
ATOM   201  C  CE2 . PHE A 1 54   ? 17.035 54.324  -4.268  1.00 12.81 ? 54   PHE A CE2 1 
ATOM   202  C  CZ  . PHE A 1 54   ? 16.971 53.486  -5.358  1.00 11.86 ? 54   PHE A CZ  1 
ATOM   203  N  N   . LYS A 1 55   ? 10.656 54.131  -1.159  1.00 14.96 ? 55   LYS A N   1 
ATOM   204  C  CA  . LYS A 1 55   ? 9.693  54.881  -0.356  1.00 15.49 ? 55   LYS A CA  1 
ATOM   205  C  C   . LYS A 1 55   ? 10.266 55.325  0.953   1.00 15.18 ? 55   LYS A C   1 
ATOM   206  O  O   . LYS A 1 55   ? 10.961 54.569  1.622   1.00 17.79 ? 55   LYS A O   1 
ATOM   207  C  CB  . LYS A 1 55   ? 8.452  54.034  -0.037  1.00 16.38 ? 55   LYS A CB  1 
ATOM   208  C  CG  . LYS A 1 55   ? 7.702  53.589  -1.246  1.00 18.60 ? 55   LYS A CG  1 
ATOM   209  C  CD  . LYS A 1 55   ? 7.427  54.748  -2.218  1.00 19.82 ? 55   LYS A CD  1 
ATOM   210  C  CE  . LYS A 1 55   ? 6.579  54.269  -3.417  1.00 21.17 ? 55   LYS A CE  1 
ATOM   211  N  NZ  . LYS A 1 55   ? 6.243  55.420  -4.341  1.00 22.93 ? 55   LYS A NZ  1 
ATOM   212  N  N   . ASP A 1 56   ? 9.989  56.558  1.322   1.00 15.08 ? 56   ASP A N   1 
ATOM   213  C  CA  . ASP A 1 56   ? 10.500 57.137  2.529   1.00 15.90 ? 56   ASP A CA  1 
ATOM   214  C  C   . ASP A 1 56   ? 9.460  57.149  3.662   1.00 16.80 ? 56   ASP A C   1 
ATOM   215  O  O   . ASP A 1 56   ? 8.839  58.163  3.969   1.00 19.03 ? 56   ASP A O   1 
ATOM   216  C  CB  . ASP A 1 56   ? 11.010 58.549  2.185   1.00 15.80 ? 56   ASP A CB  1 
ATOM   217  C  CG  . ASP A 1 56   ? 11.671 59.253  3.361   1.00 15.67 ? 56   ASP A CG  1 
ATOM   218  O  OD1 . ASP A 1 56   ? 12.203 58.617  4.296   1.00 15.52 ? 56   ASP A OD1 1 
ATOM   219  O  OD2 . ASP A 1 56   ? 11.651 60.506  3.312   1.00 18.28 ? 56   ASP A OD2 1 
ATOM   220  N  N   . ILE A 1 57   ? 9.293  56.011  4.297   1.00 17.44 ? 57   ILE A N   1 
ATOM   221  C  CA  . ILE A 1 57   ? 8.301  55.958  5.352   1.00 19.08 ? 57   ILE A CA  1 
ATOM   222  C  C   . ILE A 1 57   ? 8.898  55.942  6.716   1.00 19.00 ? 57   ILE A C   1 
ATOM   223  O  O   . ILE A 1 57   ? 10.031 55.503  6.922   1.00 18.34 ? 57   ILE A O   1 
ATOM   224  C  CB  . ILE A 1 57   ? 7.347  54.731  5.201   1.00 21.21 ? 57   ILE A CB  1 
ATOM   225  C  CG1 . ILE A 1 57   ? 8.128  53.443  5.247   1.00 22.27 ? 57   ILE A CG1 1 
ATOM   226  C  CG2 . ILE A 1 57   ? 6.512  54.827  3.864   1.00 21.00 ? 57   ILE A CG2 1 
ATOM   227  C  CD1 . ILE A 1 57   ? 7.289  52.316  5.846   1.00 23.16 ? 57   ILE A CD1 1 
ATOM   228  N  N   . ASP A 1 58   ? 8.117  56.425  7.664   1.00 18.39 ? 58   ASP A N   1 
ATOM   229  C  CA  . ASP A 1 58   ? 8.504  56.501  9.048   1.00 18.97 ? 58   ASP A CA  1 
ATOM   230  C  C   . ASP A 1 58   ? 8.530  55.094  9.613   1.00 18.48 ? 58   ASP A C   1 
ATOM   231  O  O   . ASP A 1 58   ? 7.485  54.482  9.792   1.00 18.85 ? 58   ASP A O   1 
ATOM   232  C  CB  . ASP A 1 58   ? 7.468  57.350  9.769   1.00 20.13 ? 58   ASP A CB  1 
ATOM   233  C  CG  . ASP A 1 58   ? 7.843  57.643  11.183  1.00 22.79 ? 58   ASP A CG  1 
ATOM   234  O  OD1 . ASP A 1 58   ? 8.649  56.889  11.786  1.00 21.24 ? 58   ASP A OD1 1 
ATOM   235  O  OD2 . ASP A 1 58   ? 7.320  58.668  11.706  1.00 25.86 ? 58   ASP A OD2 1 
ATOM   236  N  N   . GLY A 1 59   ? 9.711  54.550  9.872   1.00 17.24 ? 59   GLY A N   1 
ATOM   237  C  CA  . GLY A 1 59   ? 9.806  53.195  10.397  1.00 16.64 ? 59   GLY A CA  1 
ATOM   238  C  C   . GLY A 1 59   ? 9.753  53.080  11.922  1.00 14.89 ? 59   GLY A C   1 
ATOM   239  O  O   . GLY A 1 59   ? 9.984  51.993  12.453  1.00 15.83 ? 59   GLY A O   1 
ATOM   240  N  N   . GLY A 1 60   ? 9.479  54.194  12.595  1.00 14.90 ? 60   GLY A N   1 
ATOM   241  C  CA  . GLY A 1 60   ? 9.462  54.202  14.050  1.00 14.42 ? 60   GLY A CA  1 
ATOM   242  C  C   . GLY A 1 60   ? 10.748 54.805  14.650  1.00 13.27 ? 60   GLY A C   1 
ATOM   243  O  O   . GLY A 1 60   ? 11.299 55.774  14.096  1.00 15.02 ? 60   GLY A O   1 
ATOM   244  N  N   . VAL A 1 61   ? 11.206 54.282  15.790  1.00 13.85 ? 61   VAL A N   1 
ATOM   245  C  CA  . VAL A 1 61   ? 12.410 54.850  16.396  1.00 12.97 ? 61   VAL A CA  1 
ATOM   246  C  C   . VAL A 1 61   ? 13.572 54.727  15.371  1.00 12.79 ? 61   VAL A C   1 
ATOM   247  O  O   . VAL A 1 61   ? 14.430 55.624  15.341  1.00 12.86 ? 61   VAL A O   1 
ATOM   248  C  CB  . VAL A 1 61   ? 12.775 54.192  17.745  1.00 13.63 ? 61   VAL A CB  1 
ATOM   249  C  CG1 . VAL A 1 61   ? 11.719 54.567  18.811  1.00 14.38 ? 61   VAL A CG1 1 
ATOM   250  C  CG2 . VAL A 1 61   ? 12.917 52.702  17.600  1.00 15.27 ? 61   VAL A CG2 1 
ATOM   251  N  N   . TRP A 1 62   ? 13.627 53.657  14.589  1.00 12.26 ? 62   TRP A N   1 
ATOM   252  C  CA  . TRP A 1 62   ? 14.657 53.581  13.502  1.00 11.66 ? 62   TRP A CA  1 
ATOM   253  C  C   . TRP A 1 62   ? 13.862 54.228  12.392  1.00 11.55 ? 62   TRP A C   1 
ATOM   254  O  O   . TRP A 1 62   ? 13.077 53.560  11.679  1.00 12.46 ? 62   TRP A O   1 
ATOM   255  C  CB  . TRP A 1 62   ? 15.007 52.137  13.157  1.00 11.01 ? 62   TRP A CB  1 
ATOM   256  C  CG  . TRP A 1 62   ? 15.983 52.015  12.052  1.00 10.18 ? 62   TRP A CG  1 
ATOM   257  C  CD1 . TRP A 1 62   ? 16.671 53.056  11.432  1.00 10.50 ? 62   TRP A CD1 1 
ATOM   258  C  CD2 . TRP A 1 62   ? 16.337 50.822  11.379  1.00 10.59 ? 62   TRP A CD2 1 
ATOM   259  N  NE1 . TRP A 1 62   ? 17.408 52.544  10.412  1.00 10.75 ? 62   TRP A NE1 1 
ATOM   260  C  CE2 . TRP A 1 62   ? 17.243 51.181  10.348  1.00 10.36 ? 62   TRP A CE2 1 
ATOM   261  C  CE3 . TRP A 1 62   ? 15.979 49.477  11.531  1.00 10.36 ? 62   TRP A CE3 1 
ATOM   262  C  CZ2 . TRP A 1 62   ? 17.801 50.230  9.464   1.00 10.89 ? 62   TRP A CZ2 1 
ATOM   263  C  CZ3 . TRP A 1 62   ? 16.514 48.537  10.673  1.00 9.94  ? 62   TRP A CZ3 1 
ATOM   264  C  CH2 . TRP A 1 62   ? 17.434 48.914  9.635   1.00 11.12 ? 62   TRP A CH2 1 
ATOM   265  N  N   . LYS A 1 63   ? 14.065 55.533  12.210  1.00 11.88 ? 63   LYS A N   1 
ATOM   266  C  CA  . LYS A 1 63   ? 13.200 56.273  11.276  1.00 13.49 ? 63   LYS A CA  1 
ATOM   267  C  C   . LYS A 1 63   ? 13.152 55.783  9.851   1.00 13.22 ? 63   LYS A C   1 
ATOM   268  O  O   . LYS A 1 63   ? 12.119 55.878  9.158   1.00 14.10 ? 63   LYS A O   1 
ATOM   269  C  CB  . LYS A 1 63   ? 13.555 57.756  11.300  1.00 14.15 ? 63   LYS A CB  1 
ATOM   270  C  CG  . LYS A 1 63   ? 13.132 58.494  12.607  1.00 18.82 ? 63   LYS A CG  1 
ATOM   271  C  CD  . LYS A 1 63   ? 11.602 58.852  12.645  1.00 21.32 ? 63   LYS A CD  1 
ATOM   272  C  CE  . LYS A 1 63   ? 11.108 59.434  14.034  1.00 24.98 ? 63   LYS A CE  1 
ATOM   273  N  NZ  . LYS A 1 63   ? 11.376 58.692  15.387  1.00 26.21 ? 63   LYS A NZ  1 
ATOM   274  N  N   . GLN A 1 64   ? 14.260 55.240  9.390   1.00 11.98 ? 64   GLN A N   1 
ATOM   275  C  CA  . GLN A 1 64   ? 14.342 54.775  8.019   1.00 11.10 ? 64   GLN A CA  1 
ATOM   276  C  C   . GLN A 1 64   ? 14.424 53.278  7.868   1.00 11.20 ? 64   GLN A C   1 
ATOM   277  O  O   . GLN A 1 64   ? 14.735 52.766  6.799   1.00 11.17 ? 64   GLN A O   1 
ATOM   278  C  CB  . GLN A 1 64   ? 15.558 55.467  7.327   1.00 11.48 ? 64   GLN A CB  1 
ATOM   279  C  CG  . GLN A 1 64   ? 15.432 56.975  7.326   1.00 12.20 ? 64   GLN A CG  1 
ATOM   280  C  CD  . GLN A 1 64   ? 16.817 57.653  7.181   1.00 10.46 ? 64   GLN A CD  1 
ATOM   281  O  OE1 . GLN A 1 64   ? 17.751 57.313  7.907   1.00 11.04 ? 64   GLN A OE1 1 
ATOM   282  N  NE2 . GLN A 1 64   ? 16.896 58.633  6.285   1.00 11.09 ? 64   GLN A NE2 1 
ATOM   283  N  N   . GLY A 1 65   ? 14.044 52.579  8.947   1.00 11.66 ? 65   GLY A N   1 
ATOM   284  C  CA  . GLY A 1 65   ? 14.009 51.119  8.960   1.00 12.10 ? 65   GLY A CA  1 
ATOM   285  C  C   . GLY A 1 65   ? 12.656 50.555  9.386   1.00 12.61 ? 65   GLY A C   1 
ATOM   286  O  O   . GLY A 1 65   ? 11.633 50.886  8.776   1.00 14.19 ? 65   GLY A O   1 
ATOM   287  N  N   . TRP A 1 66   ? 12.704 49.686  10.381  1.00 13.22 ? 66   TRP A N   1 
ATOM   288  C  CA  . TRP A 1 66   ? 11.445 49.088  10.908  1.00 12.68 ? 66   TRP A CA  1 
ATOM   289  C  C   . TRP A 1 66   ? 11.721 48.714  12.340  1.00 13.58 ? 66   TRP A C   1 
ATOM   290  O  O   . TRP A 1 66   ? 12.846 48.830  12.828  1.00 13.38 ? 66   TRP A O   1 
ATOM   291  C  CB  . TRP A 1 66   ? 11.051 47.866  10.056  1.00 12.56 ? 66   TRP A CB  1 
ATOM   292  C  CG  . TRP A 1 66   ? 11.998 46.710  10.211  1.00 12.30 ? 66   TRP A CG  1 
ATOM   293  C  CD1 . TRP A 1 66   ? 11.894 45.679  11.102  1.00 13.40 ? 66   TRP A CD1 1 
ATOM   294  C  CD2 . TRP A 1 66   ? 13.220 46.467  9.480   1.00 13.05 ? 66   TRP A CD2 1 
ATOM   295  N  NE1 . TRP A 1 66   ? 12.950 44.826  10.994  1.00 13.87 ? 66   TRP A NE1 1 
ATOM   296  C  CE2 . TRP A 1 66   ? 13.782 45.281  9.998   1.00 12.32 ? 66   TRP A CE2 1 
ATOM   297  C  CE3 . TRP A 1 66   ? 13.907 47.136  8.438   1.00 12.34 ? 66   TRP A CE3 1 
ATOM   298  C  CZ2 . TRP A 1 66   ? 14.981 44.739  9.530   1.00 14.31 ? 66   TRP A CZ2 1 
ATOM   299  C  CZ3 . TRP A 1 66   ? 15.100 46.584  7.984   1.00 13.25 ? 66   TRP A CZ3 1 
ATOM   300  C  CH2 . TRP A 1 66   ? 15.627 45.409  8.520   1.00 13.41 ? 66   TRP A CH2 1 
ATOM   301  N  N   . ASN A 1 67   ? 10.690 48.264  13.074  1.00 14.53 ? 67   ASN A N   1 
ATOM   302  C  CA  . ASN A 1 67   ? 10.877 47.858  14.483  1.00 14.47 ? 67   ASN A CA  1 
ATOM   303  C  C   . ASN A 1 67   ? 11.478 46.452  14.494  1.00 14.56 ? 67   ASN A C   1 
ATOM   304  O  O   . ASN A 1 67   ? 10.788 45.446  14.198  1.00 15.21 ? 67   ASN A O   1 
ATOM   305  C  CB  . ASN A 1 67   ? 9.508  47.815  15.197  1.00 16.42 ? 67   ASN A CB  1 
ATOM   306  C  CG  . ASN A 1 67   ? 8.907  49.162  15.393  1.00 19.06 ? 67   ASN A CG  1 
ATOM   307  O  OD1 . ASN A 1 67   ? 9.587  50.188  15.501  1.00 20.22 ? 67   ASN A OD1 1 
ATOM   308  N  ND2 . ASN A 1 67   ? 7.585  49.178  15.486  1.00 21.99 ? 67   ASN A ND2 1 
ATOM   309  N  N   . ILE A 1 68   ? 12.775 46.382  14.771  1.00 13.09 ? 68   ILE A N   1 
ATOM   310  C  CA  . ILE A 1 68   ? 13.473 45.126  14.768  1.00 14.13 ? 68   ILE A CA  1 
ATOM   311  C  C   . ILE A 1 68   ? 13.015 44.225  15.922  1.00 15.10 ? 68   ILE A C   1 
ATOM   312  O  O   . ILE A 1 68   ? 12.930 44.659  17.054  1.00 15.77 ? 68   ILE A O   1 
ATOM   313  C  CB  . ILE A 1 68   ? 15.042 45.320  14.870  1.00 13.12 ? 68   ILE A CB  1 
ATOM   314  C  CG1 . ILE A 1 68   ? 15.543 46.157  13.667  1.00 12.82 ? 68   ILE A CG1 1 
ATOM   315  C  CG2 . ILE A 1 68   ? 15.731 43.952  14.909  1.00 14.04 ? 68   ILE A CG2 1 
ATOM   316  C  CD1 . ILE A 1 68   ? 17.030 46.626  13.892  1.00 12.47 ? 68   ILE A CD1 1 
ATOM   317  N  N   . LYS A 1 69   ? 12.786 42.967  15.593  1.00 16.70 ? 69   LYS A N   1 
ATOM   318  C  CA  . LYS A 1 69   ? 12.406 41.999  16.627  1.00 17.44 ? 69   LYS A CA  1 
ATOM   319  C  C   . LYS A 1 69   ? 13.436 40.878  16.653  1.00 17.56 ? 69   LYS A C   1 
ATOM   320  O  O   . LYS A 1 69   ? 14.022 40.549  15.630  1.00 17.23 ? 69   LYS A O   1 
ATOM   321  C  CB  . LYS A 1 69   ? 11.013 41.426  16.311  1.00 21.00 ? 69   LYS A CB  1 
ATOM   322  C  CG  . LYS A 1 69   ? 9.890  42.424  16.685  1.00 24.33 ? 69   LYS A CG  1 
ATOM   323  C  CD  . LYS A 1 69   ? 8.494  42.012  16.137  1.00 29.04 ? 69   LYS A CD  1 
ATOM   324  C  CE  . LYS A 1 69   ? 8.158  40.507  16.351  1.00 31.40 ? 69   LYS A CE  1 
ATOM   325  N  NZ  . LYS A 1 69   ? 6.822  40.105  15.751  1.00 33.39 ? 69   LYS A NZ  1 
ATOM   326  N  N   . TYR A 1 70   ? 13.703 40.311  17.830  1.00 17.54 ? 70   TYR A N   1 
ATOM   327  C  CA  . TYR A 1 70   ? 14.638 39.178  17.853  1.00 17.67 ? 70   TYR A CA  1 
ATOM   328  C  C   . TYR A 1 70   ? 14.102 38.106  18.808  1.00 18.95 ? 70   TYR A C   1 
ATOM   329  O  O   . TYR A 1 70   ? 13.295 38.423  19.683  1.00 19.63 ? 70   TYR A O   1 
ATOM   330  C  CB  . TYR A 1 70   ? 16.049 39.608  18.302  1.00 17.10 ? 70   TYR A CB  1 
ATOM   331  C  CG  . TYR A 1 70   ? 16.113 40.237  19.660  1.00 16.01 ? 70   TYR A CG  1 
ATOM   332  C  CD1 . TYR A 1 70   ? 15.853 41.572  19.819  1.00 17.30 ? 70   TYR A CD1 1 
ATOM   333  C  CD2 . TYR A 1 70   ? 16.449 39.480  20.804  1.00 16.75 ? 70   TYR A CD2 1 
ATOM   334  C  CE1 . TYR A 1 70   ? 15.924 42.190  21.070  1.00 18.70 ? 70   TYR A CE1 1 
ATOM   335  C  CE2 . TYR A 1 70   ? 16.514 40.092  22.058  1.00 18.49 ? 70   TYR A CE2 1 
ATOM   336  C  CZ  . TYR A 1 70   ? 16.250 41.438  22.189  1.00 18.76 ? 70   TYR A CZ  1 
ATOM   337  O  OH  . TYR A 1 70   ? 16.263 42.060  23.435  1.00 20.98 ? 70   TYR A OH  1 
ATOM   338  N  N   . ASP A 1 71   ? 14.541 36.873  18.579  1.00 20.80 ? 71   ASP A N   1 
ATOM   339  C  CA  . ASP A 1 71   ? 14.181 35.734  19.413  1.00 22.65 ? 71   ASP A CA  1 
ATOM   340  C  C   . ASP A 1 71   ? 15.149 35.710  20.586  1.00 23.36 ? 71   ASP A C   1 
ATOM   341  O  O   . ASP A 1 71   ? 16.328 35.406  20.420  1.00 22.68 ? 71   ASP A O   1 
ATOM   342  C  CB  . ASP A 1 71   ? 14.344 34.453  18.637  1.00 24.49 ? 71   ASP A CB  1 
ATOM   343  C  CG  . ASP A 1 71   ? 13.897 33.231  19.453  1.00 26.61 ? 71   ASP A CG  1 
ATOM   344  O  OD1 . ASP A 1 71   ? 13.680 33.374  20.693  1.00 26.81 ? 71   ASP A OD1 1 
ATOM   345  O  OD2 . ASP A 1 71   ? 13.778 32.160  18.839  1.00 28.57 ? 71   ASP A OD2 1 
ATOM   346  N  N   . PRO A 1 72   ? 14.668 36.021  21.803  1.00 24.84 ? 72   PRO A N   1 
ATOM   347  C  CA  . PRO A 1 72   ? 15.610 36.000  22.924  1.00 25.35 ? 72   PRO A CA  1 
ATOM   348  C  C   . PRO A 1 72   ? 16.379 34.691  23.109  1.00 25.33 ? 72   PRO A C   1 
ATOM   349  O  O   . PRO A 1 72   ? 17.493 34.671  23.635  1.00 26.24 ? 72   PRO A O   1 
ATOM   350  C  CB  . PRO A 1 72   ? 14.739 36.395  24.128  1.00 25.39 ? 72   PRO A CB  1 
ATOM   351  C  CG  . PRO A 1 72   ? 13.348 35.977  23.714  1.00 26.66 ? 72   PRO A CG  1 
ATOM   352  C  CD  . PRO A 1 72   ? 13.295 36.327  22.246  1.00 25.27 ? 72   PRO A CD  1 
ATOM   353  N  N   . LEU A 1 73   ? 15.819 33.598  22.608  1.00 25.51 ? 73   LEU A N   1 
ATOM   354  C  CA  . LEU A 1 73   ? 16.471 32.312  22.735  1.00 25.92 ? 73   LEU A CA  1 
ATOM   355  C  C   . LEU A 1 73   ? 17.547 32.048  21.704  1.00 25.51 ? 73   LEU A C   1 
ATOM   356  O  O   . LEU A 1 73   ? 18.146 30.987  21.703  1.00 25.78 ? 73   LEU A O   1 
ATOM   357  C  CB  . LEU A 1 73   ? 15.427 31.204  22.634  1.00 26.38 ? 73   LEU A CB  1 
ATOM   358  C  CG  . LEU A 1 73   ? 14.337 31.332  23.688  1.00 27.65 ? 73   LEU A CG  1 
ATOM   359  C  CD1 . LEU A 1 73   ? 13.275 30.232  23.466  1.00 28.37 ? 73   LEU A CD1 1 
ATOM   360  C  CD2 . LEU A 1 73   ? 15.003 31.229  25.059  1.00 28.43 ? 73   LEU A CD2 1 
ATOM   361  N  N   . LYS A 1 74   ? 17.801 33.014  20.815  1.00 25.18 ? 74   LYS A N   1 
ATOM   362  C  CA  . LYS A 1 74   ? 18.821 32.842  19.792  1.00 24.45 ? 74   LYS A CA  1 
ATOM   363  C  C   . LYS A 1 74   ? 20.200 32.708  20.427  1.00 23.79 ? 74   LYS A C   1 
ATOM   364  O  O   . LYS A 1 74   ? 21.074 31.992  19.928  1.00 23.34 ? 74   LYS A O   1 
ATOM   365  C  CB  . LYS A 1 74   ? 18.820 34.054  18.864  1.00 24.73 ? 74   LYS A CB  1 
ATOM   366  C  CG  . LYS A 1 74   ? 19.792 33.963  17.705  1.00 26.45 ? 74   LYS A CG  1 
ATOM   367  C  CD  . LYS A 1 74   ? 19.627 35.245  16.863  1.00 27.79 ? 74   LYS A CD  1 
ATOM   368  C  CE  . LYS A 1 74   ? 20.433 35.238  15.590  1.00 28.99 ? 74   LYS A CE  1 
ATOM   369  N  NZ  . LYS A 1 74   ? 19.810 36.189  14.627  1.00 30.60 ? 74   LYS A NZ  1 
ATOM   370  N  N   . TYR A 1 75   ? 20.446 33.458  21.494  1.00 24.18 ? 75   TYR A N   1 
ATOM   371  C  CA  . TYR A 1 75   ? 21.745 33.380  22.160  1.00 23.75 ? 75   TYR A CA  1 
ATOM   372  C  C   A TYR A 1 75   ? 21.534 32.667  23.509  0.50 23.82 ? 75   TYR A C   1 
ATOM   373  C  C   B TYR A 1 75   ? 21.417 32.490  23.490  0.50 23.89 ? 75   TYR A C   1 
ATOM   374  O  O   A TYR A 1 75   ? 20.537 32.899  24.184  0.50 24.15 ? 75   TYR A O   1 
ATOM   375  O  O   B TYR A 1 75   ? 20.331 32.457  24.064  0.50 24.04 ? 75   TYR A O   1 
ATOM   376  C  CB  A TYR A 1 75   ? 22.356 34.793  22.314  0.50 23.46 ? 75   TYR A CB  1 
ATOM   377  C  CB  B TYR A 1 75   ? 22.044 34.724  22.712  0.50 23.73 ? 75   TYR A CB  1 
ATOM   378  C  CG  A TYR A 1 75   ? 22.713 35.423  20.973  0.50 22.40 ? 75   TYR A CG  1 
ATOM   379  C  CG  B TYR A 1 75   ? 22.037 35.649  21.562  0.50 22.86 ? 75   TYR A CG  1 
ATOM   380  C  CD1 A TYR A 1 75   ? 21.926 36.445  20.409  0.50 22.80 ? 75   TYR A CD1 1 
ATOM   381  C  CD1 B TYR A 1 75   ? 20.982 36.530  21.367  0.50 22.98 ? 75   TYR A CD1 1 
ATOM   382  C  CD2 A TYR A 1 75   ? 23.780 34.935  20.224  0.50 22.31 ? 75   TYR A CD2 1 
ATOM   383  C  CD2 B TYR A 1 75   ? 23.049 35.598  20.617  0.50 22.04 ? 75   TYR A CD2 1 
ATOM   384  C  CE1 A TYR A 1 75   ? 22.196 36.954  19.126  0.50 22.55 ? 75   TYR A CE1 1 
ATOM   385  C  CE1 B TYR A 1 75   ? 20.933 37.344  20.252  0.50 22.08 ? 75   TYR A CE1 1 
ATOM   386  C  CE2 A TYR A 1 75   ? 24.059 35.426  18.937  0.50 23.10 ? 75   TYR A CE2 1 
ATOM   387  C  CE2 B TYR A 1 75   ? 23.013 36.408  19.494  0.50 22.15 ? 75   TYR A CE2 1 
ATOM   388  C  CZ  A TYR A 1 75   ? 23.268 36.429  18.391  0.50 22.42 ? 75   TYR A CZ  1 
ATOM   389  C  CZ  B TYR A 1 75   ? 21.952 37.276  19.322  0.50 21.68 ? 75   TYR A CZ  1 
ATOM   390  O  OH  A TYR A 1 75   ? 23.545 36.868  17.096  0.50 23.09 ? 75   TYR A OH  1 
ATOM   391  O  OH  B TYR A 1 75   ? 21.924 38.069  18.215  0.50 20.71 ? 75   TYR A OH  1 
ATOM   392  N  N   . ASN A 1 76   ? 22.465 31.774  23.845  1.00 23.21 ? 76   ASN A N   1 
ATOM   393  C  CA  . ASN A 1 76   ? 22.429 30.952  25.053  1.00 24.37 ? 76   ASN A CA  1 
ATOM   394  C  C   . ASN A 1 76   ? 23.878 30.658  25.498  1.00 24.67 ? 76   ASN A C   1 
ATOM   395  O  O   . ASN A 1 76   ? 24.818 31.200  24.930  1.00 24.48 ? 76   ASN A O   1 
ATOM   396  C  CB  . ASN A 1 76   ? 21.646 29.655  24.774  1.00 25.07 ? 76   ASN A CB  1 
ATOM   397  C  CG  . ASN A 1 76   ? 22.145 28.915  23.563  1.00 24.91 ? 76   ASN A CG  1 
ATOM   398  O  OD1 . ASN A 1 76   ? 23.317 28.608  23.460  1.00 25.11 ? 76   ASN A OD1 1 
ATOM   399  N  ND2 . ASN A 1 76   ? 21.232 28.620  22.623  1.00 27.32 ? 76   ASN A ND2 1 
ATOM   400  N  N   . ALA A 1 77   ? 24.087 29.807  26.512  1.00 25.62 ? 77   ALA A N   1 
ATOM   401  C  CA  . ALA A 1 77   ? 25.455 29.575  26.995  1.00 26.63 ? 77   ALA A CA  1 
ATOM   402  C  C   . ALA A 1 77   ? 26.432 29.074  25.946  1.00 27.23 ? 77   ALA A C   1 
ATOM   403  O  O   . ALA A 1 77   ? 27.632 29.323  26.026  1.00 27.71 ? 77   ALA A O   1 
ATOM   404  C  CB  . ALA A 1 77   ? 25.439 28.599  28.164  1.00 26.94 ? 77   ALA A CB  1 
ATOM   405  N  N   . HIS A 1 78   ? 25.900 28.390  24.945  1.00 28.31 ? 78   HIS A N   1 
ATOM   406  C  CA  . HIS A 1 78   ? 26.720 27.805  23.899  1.00 29.39 ? 78   HIS A CA  1 
ATOM   407  C  C   . HIS A 1 78   ? 26.841 28.672  22.665  1.00 28.29 ? 78   HIS A C   1 
ATOM   408  O  O   . HIS A 1 78   ? 27.656 28.402  21.767  1.00 28.75 ? 78   HIS A O   1 
ATOM   409  C  CB  . HIS A 1 78   ? 26.143 26.434  23.545  1.00 32.62 ? 78   HIS A CB  1 
ATOM   410  C  CG  . HIS A 1 78   ? 26.028 25.531  24.732  1.00 36.33 ? 78   HIS A CG  1 
ATOM   411  N  ND1 . HIS A 1 78   ? 27.131 25.080  25.431  1.00 38.27 ? 78   HIS A ND1 1 
ATOM   412  C  CD2 . HIS A 1 78   ? 24.943 25.058  25.393  1.00 37.75 ? 78   HIS A CD2 1 
ATOM   413  C  CE1 . HIS A 1 78   ? 26.731 24.369  26.472  1.00 39.14 ? 78   HIS A CE1 1 
ATOM   414  N  NE2 . HIS A 1 78   ? 25.407 24.341  26.473  1.00 39.46 ? 78   HIS A NE2 1 
ATOM   415  N  N   . HIS A 1 79   ? 26.021 29.716  22.625  1.00 25.76 ? 79   HIS A N   1 
ATOM   416  C  CA  . HIS A 1 79   ? 26.040 30.621  21.489  1.00 22.71 ? 79   HIS A CA  1 
ATOM   417  C  C   . HIS A 1 79   ? 25.846 32.031  22.016  1.00 19.39 ? 79   HIS A C   1 
ATOM   418  O  O   . HIS A 1 79   ? 24.733 32.495  22.101  1.00 18.96 ? 79   HIS A O   1 
ATOM   419  C  CB  . HIS A 1 79   ? 24.913 30.283  20.550  1.00 23.55 ? 79   HIS A CB  1 
ATOM   420  C  CG  . HIS A 1 79   ? 25.089 30.902  19.203  1.00 24.13 ? 79   HIS A CG  1 
ATOM   421  N  ND1 . HIS A 1 79   ? 24.206 31.828  18.687  1.00 25.56 ? 79   HIS A ND1 1 
ATOM   422  C  CD2 . HIS A 1 79   ? 26.082 30.773  18.289  1.00 24.80 ? 79   HIS A CD2 1 
ATOM   423  C  CE1 . HIS A 1 79   ? 24.651 32.249  17.516  1.00 24.80 ? 79   HIS A CE1 1 
ATOM   424  N  NE2 . HIS A 1 79   ? 25.786 31.626  17.251  1.00 24.44 ? 79   HIS A NE2 1 
ATOM   425  N  N   . LYS A 1 80   ? 26.951 32.677  22.375  1.00 17.81 ? 80   LYS A N   1 
ATOM   426  C  CA  . LYS A 1 80   ? 26.848 34.014  22.951  1.00 15.82 ? 80   LYS A CA  1 
ATOM   427  C  C   . LYS A 1 80   ? 27.071 35.076  21.882  1.00 15.00 ? 80   LYS A C   1 
ATOM   428  O  O   . LYS A 1 80   ? 27.659 34.794  20.815  1.00 16.30 ? 80   LYS A O   1 
ATOM   429  C  CB  . LYS A 1 80   ? 27.904 34.216  24.021  1.00 17.57 ? 80   LYS A CB  1 
ATOM   430  C  CG  . LYS A 1 80   ? 27.713 33.258  25.204  1.00 19.80 ? 80   LYS A CG  1 
ATOM   431  C  CD  . LYS A 1 80   ? 28.896 33.315  26.113  1.00 22.73 ? 80   LYS A CD  1 
ATOM   432  C  CE  . LYS A 1 80   ? 29.062 34.608  26.854  1.00 22.45 ? 80   LYS A CE  1 
ATOM   433  N  NZ  . LYS A 1 80   ? 29.954 34.328  28.055  1.00 25.33 ? 80   LYS A NZ  1 
ATOM   434  N  N   . LEU A 1 81   ? 26.556 36.261  22.153  1.00 12.99 ? 81   LEU A N   1 
ATOM   435  C  CA  . LEU A 1 81   ? 26.787 37.397  21.254  1.00 11.77 ? 81   LEU A CA  1 
ATOM   436  C  C   . LEU A 1 81   ? 28.082 38.063  21.722  1.00 12.42 ? 81   LEU A C   1 
ATOM   437  O  O   . LEU A 1 81   ? 28.202 38.482  22.893  1.00 12.78 ? 81   LEU A O   1 
ATOM   438  C  CB  . LEU A 1 81   ? 25.649 38.371  21.379  1.00 12.96 ? 81   LEU A CB  1 
ATOM   439  C  CG  . LEU A 1 81   ? 25.793 39.642  20.508  1.00 12.16 ? 81   LEU A CG  1 
ATOM   440  C  CD1 . LEU A 1 81   ? 25.718 39.283  18.991  1.00 13.68 ? 81   LEU A CD1 1 
ATOM   441  C  CD2 . LEU A 1 81   ? 24.650 40.620  20.843  1.00 14.56 ? 81   LEU A CD2 1 
ATOM   442  N  N   . LYS A 1 82   ? 29.066 38.179  20.826  1.00 10.76 ? 82   LYS A N   1 
ATOM   443  C  CA  . LYS A 1 82   ? 30.355 38.770  21.130  1.00 10.92 ? 82   LYS A CA  1 
ATOM   444  C  C   . LYS A 1 82   ? 30.296 40.194  20.609  1.00 11.45 ? 82   LYS A C   1 
ATOM   445  O  O   . LYS A 1 82   ? 30.066 40.397  19.405  1.00 12.49 ? 82   LYS A O   1 
ATOM   446  C  CB  . LYS A 1 82   ? 31.465 37.972  20.426  1.00 13.28 ? 82   LYS A CB  1 
ATOM   447  C  CG  . LYS A 1 82   ? 32.871 38.493  20.641  1.00 20.17 ? 82   LYS A CG  1 
ATOM   448  C  CD  . LYS A 1 82   ? 33.337 38.473  22.115  1.00 23.46 ? 82   LYS A CD  1 
ATOM   449  C  CE  . LYS A 1 82   ? 34.851 38.103  22.180  1.00 25.31 ? 82   LYS A CE  1 
ATOM   450  N  NZ  . LYS A 1 82   ? 35.399 38.171  23.573  1.00 27.97 ? 82   LYS A NZ  1 
ATOM   451  N  N   . VAL A 1 83   ? 30.440 41.162  21.513  1.00 10.11 ? 83   VAL A N   1 
ATOM   452  C  CA  . VAL A 1 83   ? 30.310 42.575  21.150  1.00 10.46 ? 83   VAL A CA  1 
ATOM   453  C  C   . VAL A 1 83   ? 31.631 43.298  21.292  1.00 10.38 ? 83   VAL A C   1 
ATOM   454  O  O   . VAL A 1 83   ? 32.261 43.292  22.350  1.00 10.80 ? 83   VAL A O   1 
ATOM   455  C  CB  . VAL A 1 83   ? 29.279 43.243  22.073  1.00 8.82  ? 83   VAL A CB  1 
ATOM   456  C  CG1 . VAL A 1 83   ? 29.054 44.756  21.730  1.00 11.24 ? 83   VAL A CG1 1 
ATOM   457  C  CG2 . VAL A 1 83   ? 27.924 42.510  21.938  1.00 11.50 ? 83   VAL A CG2 1 
ATOM   458  N  N   . PHE A 1 84   ? 32.049 43.970  20.213  1.00 9.90  ? 84   PHE A N   1 
ATOM   459  C  CA  . PHE A 1 84   ? 33.275 44.773  20.230  1.00 9.92  ? 84   PHE A CA  1 
ATOM   460  C  C   . PHE A 1 84   ? 32.910 46.230  20.154  1.00 9.79  ? 84   PHE A C   1 
ATOM   461  O  O   . PHE A 1 84   ? 32.368 46.691  19.138  1.00 9.46  ? 84   PHE A O   1 
ATOM   462  C  CB  . PHE A 1 84   ? 34.164 44.410  19.053  1.00 10.67 ? 84   PHE A CB  1 
ATOM   463  C  CG  . PHE A 1 84   ? 34.773 43.089  19.201  1.00 11.71 ? 84   PHE A CG  1 
ATOM   464  C  CD1 . PHE A 1 84   ? 35.873 42.901  20.050  1.00 15.26 ? 84   PHE A CD1 1 
ATOM   465  C  CD2 . PHE A 1 84   ? 34.293 42.001  18.501  1.00 14.24 ? 84   PHE A CD2 1 
ATOM   466  C  CE1 . PHE A 1 84   ? 36.501 41.665  20.192  1.00 16.18 ? 84   PHE A CE1 1 
ATOM   467  C  CE2 . PHE A 1 84   ? 34.895 40.743  18.629  1.00 16.23 ? 84   PHE A CE2 1 
ATOM   468  C  CZ  . PHE A 1 84   ? 36.017 40.553  19.466  1.00 15.67 ? 84   PHE A CZ  1 
ATOM   469  N  N   . VAL A 1 85   ? 33.180 46.961  21.231  1.00 9.19  ? 85   VAL A N   1 
ATOM   470  C  CA  . VAL A 1 85   ? 32.941 48.401  21.272  1.00 9.21  ? 85   VAL A CA  1 
ATOM   471  C  C   . VAL A 1 85   ? 34.256 49.038  20.863  1.00 8.74  ? 85   VAL A C   1 
ATOM   472  O  O   . VAL A 1 85   ? 35.269 48.867  21.516  1.00 9.42  ? 85   VAL A O   1 
ATOM   473  C  CB  . VAL A 1 85   ? 32.507 48.862  22.692  1.00 8.82  ? 85   VAL A CB  1 
ATOM   474  C  CG1 . VAL A 1 85   ? 32.301 50.376  22.716  1.00 11.73 ? 85   VAL A CG1 1 
ATOM   475  C  CG2 . VAL A 1 85   ? 31.211 48.140  23.056  1.00 10.80 ? 85   VAL A CG2 1 
ATOM   476  N  N   . VAL A 1 86   ? 34.228 49.795  19.747  1.00 8.96  ? 86   VAL A N   1 
ATOM   477  C  CA  . VAL A 1 86   ? 35.457 50.307  19.135  1.00 8.48  ? 86   VAL A CA  1 
ATOM   478  C  C   . VAL A 1 86   ? 35.532 51.834  19.229  1.00 8.01  ? 86   VAL A C   1 
ATOM   479  O  O   . VAL A 1 86   ? 34.889 52.553  18.450  1.00 8.39  ? 86   VAL A O   1 
ATOM   480  C  CB  . VAL A 1 86   ? 35.458 49.853  17.660  1.00 8.63  ? 86   VAL A CB  1 
ATOM   481  C  CG1 . VAL A 1 86   ? 36.794 50.369  16.984  1.00 9.65  ? 86   VAL A CG1 1 
ATOM   482  C  CG2 . VAL A 1 86   ? 35.427 48.312  17.567  1.00 10.77 ? 86   VAL A CG2 1 
ATOM   483  N  N   . PRO A 1 87   ? 36.290 52.358  20.200  1.00 8.24  ? 87   PRO A N   1 
ATOM   484  C  CA  . PRO A 1 87   ? 36.414 53.829  20.372  1.00 8.48  ? 87   PRO A CA  1 
ATOM   485  C  C   . PRO A 1 87   ? 37.145 54.445  19.181  1.00 7.63  ? 87   PRO A C   1 
ATOM   486  O  O   . PRO A 1 87   ? 38.153 53.889  18.698  1.00 7.85  ? 87   PRO A O   1 
ATOM   487  C  CB  . PRO A 1 87   ? 37.224 53.975  21.698  1.00 8.11  ? 87   PRO A CB  1 
ATOM   488  C  CG  . PRO A 1 87   ? 36.933 52.624  22.395  1.00 10.02 ? 87   PRO A CG  1 
ATOM   489  C  CD  . PRO A 1 87   ? 36.986 51.621  21.269  1.00 9.22  ? 87   PRO A CD  1 
ATOM   490  N  N   . HIS A 1 88   ? 36.636 55.585  18.739  1.00 7.28  ? 88   HIS A N   1 
ATOM   491  C  CA  . HIS A 1 88   ? 37.219 56.275  17.562  1.00 8.08  ? 88   HIS A CA  1 
ATOM   492  C  C   . HIS A 1 88   ? 36.977 57.752  17.639  1.00 7.85  ? 88   HIS A C   1 
ATOM   493  O  O   . HIS A 1 88   ? 36.153 58.215  18.448  1.00 8.24  ? 88   HIS A O   1 
ATOM   494  C  CB  . HIS A 1 88   ? 36.624 55.664  16.258  1.00 7.89  ? 88   HIS A CB  1 
ATOM   495  C  CG  . HIS A 1 88   ? 35.193 56.001  16.013  1.00 6.65  ? 88   HIS A CG  1 
ATOM   496  N  ND1 . HIS A 1 88   ? 34.789 57.064  15.220  1.00 7.52  ? 88   HIS A ND1 1 
ATOM   497  C  CD2 . HIS A 1 88   ? 34.059 55.410  16.460  1.00 7.15  ? 88   HIS A CD2 1 
ATOM   498  C  CE1 . HIS A 1 88   ? 33.463 57.100  15.180  1.00 8.64  ? 88   HIS A CE1 1 
ATOM   499  N  NE2 . HIS A 1 88   ? 33.000 56.102  15.939  1.00 8.79  ? 88   HIS A NE2 1 
ATOM   500  N  N   . SER A 1 89   ? 37.693 58.529  16.813  1.00 8.16  ? 89   SER A N   1 
ATOM   501  C  CA  . SER A 1 89   ? 37.574 59.988  16.809  1.00 8.01  ? 89   SER A CA  1 
ATOM   502  C  C   . SER A 1 89   ? 37.740 60.410  15.349  1.00 7.32  ? 89   SER A C   1 
ATOM   503  O  O   . SER A 1 89   ? 38.831 60.215  14.786  1.00 8.07  ? 89   SER A O   1 
ATOM   504  C  CB  . SER A 1 89   ? 38.718 60.530  17.674  1.00 9.10  ? 89   SER A CB  1 
ATOM   505  O  OG  . SER A 1 89   ? 38.717 61.943  17.696  1.00 8.56  ? 89   SER A OG  1 
ATOM   506  N  N   . HIS A 1 90   ? 36.698 60.983  14.783  1.00 7.12  ? 90   HIS A N   1 
ATOM   507  C  CA  . HIS A 1 90   ? 36.755 61.388  13.371  1.00 7.04  ? 90   HIS A CA  1 
ATOM   508  C  C   . HIS A 1 90   ? 37.430 62.770  13.276  1.00 7.20  ? 90   HIS A C   1 
ATOM   509  O  O   . HIS A 1 90   ? 36.908 63.774  13.767  1.00 7.59  ? 90   HIS A O   1 
ATOM   510  C  CB  . HIS A 1 90   ? 35.331 61.377  12.788  1.00 7.80  ? 90   HIS A CB  1 
ATOM   511  C  CG  . HIS A 1 90   ? 35.292 61.730  11.333  1.00 6.78  ? 90   HIS A CG  1 
ATOM   512  N  ND1 . HIS A 1 90   ? 35.887 60.941  10.359  1.00 7.10  ? 90   HIS A ND1 1 
ATOM   513  C  CD2 . HIS A 1 90   ? 34.721 62.769  10.707  1.00 6.93  ? 90   HIS A CD2 1 
ATOM   514  C  CE1 . HIS A 1 90   ? 35.643 61.505  9.171   1.00 7.30  ? 90   HIS A CE1 1 
ATOM   515  N  NE2 . HIS A 1 90   ? 34.947 62.615  9.360   1.00 6.62  ? 90   HIS A NE2 1 
ATOM   516  N  N   . ASN A 1 91   ? 38.615 62.798  12.666  1.00 7.52  ? 91   ASN A N   1 
ATOM   517  C  CA  . ASN A 1 91   ? 39.380 64.064  12.629  1.00 8.01  ? 91   ASN A CA  1 
ATOM   518  C  C   . ASN A 1 91   ? 39.537 64.547  11.197  1.00 8.60  ? 91   ASN A C   1 
ATOM   519  O  O   . ASN A 1 91   ? 40.388 64.037  10.440  1.00 10.93 ? 91   ASN A O   1 
ATOM   520  C  CB  . ASN A 1 91   ? 40.787 63.831  13.234  1.00 8.15  ? 91   ASN A CB  1 
ATOM   521  C  CG  . ASN A 1 91   ? 40.763 63.715  14.739  1.00 8.00  ? 91   ASN A CG  1 
ATOM   522  O  OD1 . ASN A 1 91   ? 40.141 62.781  15.284  1.00 10.43 ? 91   ASN A OD1 1 
ATOM   523  N  ND2 . ASN A 1 91   ? 41.416 64.608  15.405  1.00 6.78  ? 91   ASN A ND2 1 
ATOM   524  N  N   . ASP A 1 92   ? 38.730 65.511  10.820  1.00 7.42  ? 92   ASP A N   1 
ATOM   525  C  CA  . ASP A 1 92   ? 38.812 66.035  9.457   1.00 7.43  ? 92   ASP A CA  1 
ATOM   526  C  C   . ASP A 1 92   ? 40.067 66.858  9.249   1.00 7.04  ? 92   ASP A C   1 
ATOM   527  O  O   . ASP A 1 92   ? 40.301 67.809  10.002  1.00 8.15  ? 92   ASP A O   1 
ATOM   528  C  CB  . ASP A 1 92   ? 37.620 66.952  9.230   1.00 7.82  ? 92   ASP A CB  1 
ATOM   529  C  CG  . ASP A 1 92   ? 36.319 66.213  9.244   1.00 8.05  ? 92   ASP A CG  1 
ATOM   530  O  OD1 . ASP A 1 92   ? 36.158 65.257  8.449   1.00 7.79  ? 92   ASP A OD1 1 
ATOM   531  O  OD2 . ASP A 1 92   ? 35.447 66.562  10.080  1.00 9.31  ? 92   ASP A OD2 1 
ATOM   532  N  N   . PRO A 1 93   ? 40.904 66.524  8.248   1.00 7.27  ? 93   PRO A N   1 
ATOM   533  C  CA  . PRO A 1 93   ? 42.145 67.312  7.951   1.00 7.25  ? 93   PRO A CA  1 
ATOM   534  C  C   . PRO A 1 93   ? 41.736 68.597  7.172   1.00 7.83  ? 93   PRO A C   1 
ATOM   535  O  O   . PRO A 1 93   ? 42.062 68.773  5.967   1.00 9.40  ? 93   PRO A O   1 
ATOM   536  C  CB  . PRO A 1 93   ? 43.002 66.349  7.116   1.00 8.57  ? 93   PRO A CB  1 
ATOM   537  C  CG  . PRO A 1 93   ? 42.424 64.953  7.402   1.00 9.00  ? 93   PRO A CG  1 
ATOM   538  C  CD  . PRO A 1 93   ? 40.893 65.251  7.504   1.00 7.43  ? 93   PRO A CD  1 
ATOM   539  N  N   . GLY A 1 94   ? 41.017 69.484  7.885   1.00 8.41  ? 94   GLY A N   1 
ATOM   540  C  CA  . GLY A 1 94   ? 40.469 70.720  7.338   1.00 7.83  ? 94   GLY A CA  1 
ATOM   541  C  C   . GLY A 1 94   ? 38.974 70.527  7.091   1.00 8.46  ? 94   GLY A C   1 
ATOM   542  O  O   . GLY A 1 94   ? 38.549 69.460  6.559   1.00 9.20  ? 94   GLY A O   1 
ATOM   543  N  N   . TRP A 1 95   ? 38.176 71.507  7.498   1.00 7.92  ? 95   TRP A N   1 
ATOM   544  C  CA  . TRP A 1 95   ? 36.722 71.523  7.218   1.00 7.61  ? 95   TRP A CA  1 
ATOM   545  C  C   . TRP A 1 95   ? 36.206 72.905  7.660   1.00 7.96  ? 95   TRP A C   1 
ATOM   546  O  O   . TRP A 1 95   ? 36.190 73.828  6.848   1.00 9.29  ? 95   TRP A O   1 
ATOM   547  C  CB  . TRP A 1 95   ? 35.984 70.354  7.920   1.00 7.08  ? 95   TRP A CB  1 
ATOM   548  C  CG  . TRP A 1 95   ? 34.495 70.483  7.606   1.00 7.31  ? 95   TRP A CG  1 
ATOM   549  C  CD1 . TRP A 1 95   ? 33.917 70.887  6.414   1.00 7.42  ? 95   TRP A CD1 1 
ATOM   550  C  CD2 . TRP A 1 95   ? 33.400 70.131  8.466   1.00 7.65  ? 95   TRP A CD2 1 
ATOM   551  N  NE1 . TRP A 1 95   ? 32.539 70.805  6.488   1.00 8.16  ? 95   TRP A NE1 1 
ATOM   552  C  CE2 . TRP A 1 95   ? 32.201 70.332  7.726   1.00 8.03  ? 95   TRP A CE2 1 
ATOM   553  C  CE3 . TRP A 1 95   ? 33.323 69.651  9.798   1.00 8.72  ? 95   TRP A CE3 1 
ATOM   554  C  CZ2 . TRP A 1 95   ? 30.909 70.044  8.264   1.00 8.87  ? 95   TRP A CZ2 1 
ATOM   555  C  CZ3 . TRP A 1 95   ? 32.033 69.370  10.332  1.00 9.71  ? 95   TRP A CZ3 1 
ATOM   556  C  CH2 . TRP A 1 95   ? 30.856 69.567  9.552   1.00 10.47 ? 95   TRP A CH2 1 
ATOM   557  N  N   . ILE A 1 96   ? 35.891 73.056  8.944   1.00 8.70  ? 96   ILE A N   1 
ATOM   558  C  CA  . ILE A 1 96   ? 35.467 74.329  9.538   1.00 11.01 ? 96   ILE A CA  1 
ATOM   559  C  C   . ILE A 1 96   ? 36.701 75.114  10.012  1.00 9.39  ? 96   ILE A C   1 
ATOM   560  O  O   . ILE A 1 96   ? 36.603 76.313  10.250  1.00 12.23 ? 96   ILE A O   1 
ATOM   561  C  CB  . ILE A 1 96   ? 34.580 74.115  10.799  1.00 15.19 ? 96   ILE A CB  1 
ATOM   562  C  CG1 . ILE A 1 96   ? 33.384 73.303  10.455  1.00 19.20 ? 96   ILE A CG1 1 
ATOM   563  C  CG2 . ILE A 1 96   ? 34.126 75.449  11.401  1.00 18.72 ? 96   ILE A CG2 1 
ATOM   564  C  CD1 . ILE A 1 96   ? 32.828 73.787  9.205   1.00 16.36 ? 96   ILE A CD1 1 
ATOM   565  N  N   . GLN A 1 97   ? 37.808 74.414  10.204  1.00 8.39  ? 97   GLN A N   1 
ATOM   566  C  CA  . GLN A 1 97   ? 39.100 74.998  10.586  1.00 8.03  ? 97   GLN A CA  1 
ATOM   567  C  C   . GLN A 1 97   ? 40.143 74.410  9.629   1.00 8.16  ? 97   GLN A C   1 
ATOM   568  O  O   . GLN A 1 97   ? 39.902 73.386  8.985   1.00 8.28  ? 97   GLN A O   1 
ATOM   569  C  CB  A GLN A 1 97   ? 39.458 74.596  12.021  0.50 9.50  ? 97   GLN A CB  1 
ATOM   570  C  CB  B GLN A 1 97   ? 39.520 74.809  12.033  0.50 10.64 ? 97   GLN A CB  1 
ATOM   571  C  CG  . GLN A 1 97   ? 38.565 75.257  13.081  1.00 10.91 ? 97   GLN A CG  1 
ATOM   572  C  CD  A GLN A 1 97   ? 38.883 76.727  13.242  0.50 10.21 ? 97   GLN A CD  1 
ATOM   573  C  CD  B GLN A 1 97   ? 39.017 74.987  14.545  0.50 15.73 ? 97   GLN A CD  1 
ATOM   574  O  OE1 A GLN A 1 97   ? 39.746 77.104  14.032  0.50 13.01 ? 97   GLN A OE1 1 
ATOM   575  O  OE1 B GLN A 1 97   ? 38.330 74.358  15.355  0.50 17.09 ? 97   GLN A OE1 1 
ATOM   576  N  NE2 A GLN A 1 97   ? 38.211 77.562  12.473  0.50 11.72 ? 97   GLN A NE2 1 
ATOM   577  N  NE2 B GLN A 1 97   ? 40.210 75.477  14.856  0.50 17.02 ? 97   GLN A NE2 1 
ATOM   578  N  N   . THR A 1 98   ? 41.286 75.056  9.511   1.00 8.08  ? 98   THR A N   1 
ATOM   579  C  CA  . THR A 1 98   ? 42.329 74.487  8.652   1.00 8.09  ? 98   THR A CA  1 
ATOM   580  C  C   . THR A 1 98   ? 42.938 73.275  9.372   1.00 7.94  ? 98   THR A C   1 
ATOM   581  O  O   . THR A 1 98   ? 42.704 73.043  10.574  1.00 8.31  ? 98   THR A O   1 
ATOM   582  C  CB  . THR A 1 98   ? 43.460 75.456  8.423   1.00 7.55  ? 98   THR A CB  1 
ATOM   583  O  OG1 . THR A 1 98   ? 44.058 75.744  9.678   1.00 9.05  ? 98   THR A OG1 1 
ATOM   584  C  CG2 . THR A 1 98   ? 42.982 76.725  7.775   1.00 9.42  ? 98   THR A CG2 1 
ATOM   585  N  N   . PHE A 1 99   ? 43.690 72.460  8.637   1.00 8.18  ? 99   PHE A N   1 
ATOM   586  C  CA  . PHE A 1 99   ? 44.413 71.356  9.230   1.00 7.84  ? 99   PHE A CA  1 
ATOM   587  C  C   . PHE A 1 99   ? 45.229 71.820  10.446  1.00 7.73  ? 99   PHE A C   1 
ATOM   588  O  O   . PHE A 1 99   ? 45.148 71.216  11.514  1.00 8.46  ? 99   PHE A O   1 
ATOM   589  C  CB  . PHE A 1 99   ? 45.383 70.789  8.170   1.00 8.25  ? 99   PHE A CB  1 
ATOM   590  C  CG  . PHE A 1 99   ? 46.274 69.693  8.681   1.00 7.97  ? 99   PHE A CG  1 
ATOM   591  C  CD1 . PHE A 1 99   ? 47.505 69.978  9.274   1.00 8.93  ? 99   PHE A CD1 1 
ATOM   592  C  CD2 . PHE A 1 99   ? 45.879 68.355  8.598   1.00 9.07  ? 99   PHE A CD2 1 
ATOM   593  C  CE1 . PHE A 1 99   ? 48.321 68.942  9.768   1.00 10.36 ? 99   PHE A CE1 1 
ATOM   594  C  CE2 . PHE A 1 99   ? 46.685 67.307  9.090   1.00 8.73  ? 99   PHE A CE2 1 
ATOM   595  C  CZ  . PHE A 1 99   ? 47.908 67.605  9.673   1.00 8.87  ? 99   PHE A CZ  1 
ATOM   596  N  N   . GLU A 1 100  ? 45.996 72.910  10.311  1.00 8.18  ? 100  GLU A N   1 
ATOM   597  C  CA  . GLU A 1 100  ? 46.838 73.313  11.432  1.00 8.00  ? 100  GLU A CA  1 
ATOM   598  C  C   . GLU A 1 100  ? 46.015 73.860  12.584  1.00 7.96  ? 100  GLU A C   1 
ATOM   599  O  O   . GLU A 1 100  ? 46.403 73.601  13.742  1.00 8.72  ? 100  GLU A O   1 
ATOM   600  C  CB  . GLU A 1 100  ? 47.851 74.336  10.930  1.00 9.54  ? 100  GLU A CB  1 
ATOM   601  C  CG  . GLU A 1 100  ? 48.904 74.715  11.993  1.00 10.70 ? 100  GLU A CG  1 
ATOM   602  C  CD  . GLU A 1 100  ? 49.776 73.568  12.448  1.00 11.86 ? 100  GLU A CD  1 
ATOM   603  O  OE1 . GLU A 1 100  ? 49.977 72.530  11.796  1.00 12.13 ? 100  GLU A OE1 1 
ATOM   604  O  OE2 . GLU A 1 100  ? 50.415 73.752  13.533  1.00 13.84 ? 100  GLU A OE2 1 
ATOM   605  N  N   . GLU A 1 101  ? 44.929 74.574  12.296  1.00 8.53  ? 101  GLU A N   1 
ATOM   606  C  CA  . GLU A 1 101  ? 44.075 75.066  13.394  1.00 9.29  ? 101  GLU A CA  1 
ATOM   607  C  C   . GLU A 1 101  ? 43.457 73.904  14.170  1.00 8.95  ? 101  GLU A C   1 
ATOM   608  O  O   . GLU A 1 101  ? 43.452 73.911  15.423  1.00 9.27  ? 101  GLU A O   1 
ATOM   609  C  CB  . GLU A 1 101  ? 42.962 75.901  12.830  1.00 10.13 ? 101  GLU A CB  1 
ATOM   610  C  CG  . GLU A 1 101  ? 43.393 77.291  12.398  1.00 13.40 ? 101  GLU A CG  1 
ATOM   611  C  CD  . GLU A 1 101  ? 42.311 78.045  11.576  1.00 14.44 ? 101  GLU A CD  1 
ATOM   612  O  OE1 . GLU A 1 101  ? 41.359 77.508  10.978  1.00 12.29 ? 101  GLU A OE1 1 
ATOM   613  O  OE2 . GLU A 1 101  ? 42.418 79.287  11.477  1.00 19.19 ? 101  GLU A OE2 1 
ATOM   614  N  N   . TYR A 1 102  ? 42.925 72.904  13.473  1.00 8.50  ? 102  TYR A N   1 
ATOM   615  C  CA  . TYR A 1 102  ? 42.408 71.745  14.194  1.00 8.72  ? 102  TYR A CA  1 
ATOM   616  C  C   . TYR A 1 102  ? 43.524 71.014  14.929  1.00 8.81  ? 102  TYR A C   1 
ATOM   617  O  O   . TYR A 1 102  ? 43.283 70.482  16.040  1.00 8.71  ? 102  TYR A O   1 
ATOM   618  C  CB  . TYR A 1 102  ? 41.784 70.705  13.231  1.00 9.09  ? 102  TYR A CB  1 
ATOM   619  C  CG  . TYR A 1 102  ? 40.383 70.977  12.758  1.00 8.39  ? 102  TYR A CG  1 
ATOM   620  C  CD1 . TYR A 1 102  ? 39.318 71.200  13.645  1.00 8.61  ? 102  TYR A CD1 1 
ATOM   621  C  CD2 . TYR A 1 102  ? 40.085 70.842  11.394  1.00 8.21  ? 102  TYR A CD2 1 
ATOM   622  C  CE1 . TYR A 1 102  ? 37.984 71.293  13.159  1.00 8.76  ? 102  TYR A CE1 1 
ATOM   623  C  CE2 . TYR A 1 102  ? 38.792 70.878  10.907  1.00 7.99  ? 102  TYR A CE2 1 
ATOM   624  C  CZ  . TYR A 1 102  ? 37.742 71.108  11.792  1.00 8.18  ? 102  TYR A CZ  1 
ATOM   625  O  OH  . TYR A 1 102  ? 36.448 71.147  11.278  1.00 9.53  ? 102  TYR A OH  1 
ATOM   626  N  N   . TYR A 1 103  ? 44.699 70.883  14.340  1.00 8.68  ? 103  TYR A N   1 
ATOM   627  C  CA  . TYR A 1 103  ? 45.745 70.200  15.044  1.00 8.68  ? 103  TYR A CA  1 
ATOM   628  C  C   . TYR A 1 103  ? 46.061 70.884  16.380  1.00 9.29  ? 103  TYR A C   1 
ATOM   629  O  O   . TYR A 1 103  ? 46.229 70.215  17.385  1.00 9.79  ? 103  TYR A O   1 
ATOM   630  C  CB  . TYR A 1 103  ? 47.017 70.150  14.202  1.00 9.06  ? 103  TYR A CB  1 
ATOM   631  C  CG  . TYR A 1 103  ? 48.163 69.527  14.915  1.00 9.80  ? 103  TYR A CG  1 
ATOM   632  C  CD1 . TYR A 1 103  ? 48.198 68.155  15.213  1.00 10.03 ? 103  TYR A CD1 1 
ATOM   633  C  CD2 . TYR A 1 103  ? 49.215 70.339  15.385  1.00 10.29 ? 103  TYR A CD2 1 
ATOM   634  C  CE1 . TYR A 1 103  ? 49.203 67.604  15.945  1.00 10.27 ? 103  TYR A CE1 1 
ATOM   635  C  CE2 . TYR A 1 103  ? 50.236 69.783  16.138  1.00 10.82 ? 103  TYR A CE2 1 
ATOM   636  C  CZ  . TYR A 1 103  ? 50.234 68.422  16.419  1.00 10.53 ? 103  TYR A CZ  1 
ATOM   637  O  OH  . TYR A 1 103  ? 51.232 67.851  17.243  1.00 12.33 ? 103  TYR A OH  1 
ATOM   638  N  N   . GLN A 1 104  ? 46.169 72.206  16.353  1.00 9.50  ? 104  GLN A N   1 
ATOM   639  C  CA  . GLN A 1 104  ? 46.520 72.942  17.573  1.00 10.31 ? 104  GLN A CA  1 
ATOM   640  C  C   . GLN A 1 104  ? 45.423 72.968  18.580  1.00 10.86 ? 104  GLN A C   1 
ATOM   641  O  O   . GLN A 1 104  ? 45.708 72.861  19.787  1.00 12.25 ? 104  GLN A O   1 
ATOM   642  C  CB  . GLN A 1 104  ? 46.869 74.402  17.229  1.00 10.58 ? 104  GLN A CB  1 
ATOM   643  C  CG  . GLN A 1 104  ? 48.193 74.552  16.461  1.00 11.45 ? 104  GLN A CG  1 
ATOM   644  C  CD  . GLN A 1 104  ? 49.380 74.050  17.241  1.00 11.87 ? 104  GLN A CD  1 
ATOM   645  O  OE1 . GLN A 1 104  ? 49.409 74.150  18.490  1.00 13.34 ? 104  GLN A OE1 1 
ATOM   646  N  NE2 . GLN A 1 104  ? 50.389 73.531  16.528  1.00 13.01 ? 104  GLN A NE2 1 
ATOM   647  N  N   . HIS A 1 105  ? 44.176 73.078  18.154  1.00 10.67 ? 105  HIS A N   1 
ATOM   648  C  CA  . HIS A 1 105  ? 43.096 73.201  19.134  1.00 11.65 ? 105  HIS A CA  1 
ATOM   649  C  C   A HIS A 1 105  ? 42.583 71.864  19.620  0.50 11.45 ? 105  HIS A C   1 
ATOM   650  C  C   B HIS A 1 105  ? 42.418 71.938  19.527  0.50 11.63 ? 105  HIS A C   1 
ATOM   651  O  O   A HIS A 1 105  ? 42.252 71.703  20.797  0.50 11.34 ? 105  HIS A O   1 
ATOM   652  O  O   B HIS A 1 105  ? 41.785 71.904  20.577  0.50 11.67 ? 105  HIS A O   1 
ATOM   653  C  CB  . HIS A 1 105  ? 41.919 73.969  18.522  1.00 14.54 ? 105  HIS A CB  1 
ATOM   654  C  CG  A HIS A 1 105  ? 42.291 75.310  17.953  0.50 17.78 ? 105  HIS A CG  1 
ATOM   655  C  CG  B HIS A 1 105  ? 40.937 74.518  19.548  0.50 16.28 ? 105  HIS A CG  1 
ATOM   656  N  ND1 A HIS A 1 105  ? 41.606 75.893  16.907  0.50 19.96 ? 105  HIS A ND1 1 
ATOM   657  N  ND1 B HIS A 1 105  ? 39.860 73.727  19.884  0.50 17.40 ? 105  HIS A ND1 1 
ATOM   658  C  CD2 A HIS A 1 105  ? 43.273 76.178  18.288  0.50 19.59 ? 105  HIS A CD2 1 
ATOM   659  C  CD2 B HIS A 1 105  ? 40.857 75.617  20.335  0.50 18.50 ? 105  HIS A CD2 1 
ATOM   660  C  CE1 A HIS A 1 105  ? 42.155 77.061  16.621  0.50 20.75 ? 105  HIS A CE1 1 
ATOM   661  C  CE1 B HIS A 1 105  ? 39.161 74.321  20.836  0.50 18.68 ? 105  HIS A CE1 1 
ATOM   662  N  NE2 A HIS A 1 105  ? 43.168 77.257  17.443  0.50 20.57 ? 105  HIS A NE2 1 
ATOM   663  N  NE2 B HIS A 1 105  ? 39.746 75.469  21.128  0.50 19.03 ? 105  HIS A NE2 1 
ATOM   664  N  N   . ASP A 1 106  ? 42.565 70.882  18.716  1.00 11.06 ? 106  ASP A N   1 
ATOM   665  C  CA  . ASP A 1 106  ? 41.969 69.603  19.045  1.00 10.95 ? 106  ASP A CA  1 
ATOM   666  C  C   . ASP A 1 106  ? 42.786 68.354  18.905  1.00 9.71  ? 106  ASP A C   1 
ATOM   667  O  O   . ASP A 1 106  ? 43.028 67.630  19.898  1.00 10.09 ? 106  ASP A O   1 
ATOM   668  C  CB  . ASP A 1 106  ? 40.668 69.412  18.219  1.00 13.09 ? 106  ASP A CB  1 
ATOM   669  C  CG  . ASP A 1 106  ? 39.668 70.476  18.543  1.00 15.78 ? 106  ASP A CG  1 
ATOM   670  O  OD1 . ASP A 1 106  ? 38.928 70.300  19.524  1.00 16.95 ? 106  ASP A OD1 1 
ATOM   671  O  OD2 . ASP A 1 106  ? 39.654 71.501  17.842  1.00 19.73 ? 106  ASP A OD2 1 
ATOM   672  N  N   . THR A 1 107  ? 43.295 68.094  17.707  1.00 9.65  ? 107  THR A N   1 
ATOM   673  C  CA  . THR A 1 107  ? 43.915 66.814  17.464  1.00 8.30  ? 107  THR A CA  1 
ATOM   674  C  C   . THR A 1 107  ? 45.172 66.537  18.274  1.00 8.60  ? 107  THR A C   1 
ATOM   675  O  O   . THR A 1 107  ? 45.408 65.402  18.693  1.00 8.85  ? 107  THR A O   1 
ATOM   676  C  CB  . THR A 1 107  ? 44.171 66.653  15.949  1.00 8.04  ? 107  THR A CB  1 
ATOM   677  O  OG1 . THR A 1 107  ? 42.943 66.908  15.276  1.00 8.65  ? 107  THR A OG1 1 
ATOM   678  C  CG2 . THR A 1 107  ? 44.667 65.222  15.624  1.00 9.15  ? 107  THR A CG2 1 
ATOM   679  N  N   . LYS A 1 108  ? 45.981 67.577  18.538  1.00 9.09  ? 108  LYS A N   1 
ATOM   680  C  CA  . LYS A 1 108  ? 47.178 67.253  19.317  1.00 9.14  ? 108  LYS A CA  1 
ATOM   681  C  C   . LYS A 1 108  ? 46.818 66.811  20.735  1.00 8.66  ? 108  LYS A C   1 
ATOM   682  O  O   . LYS A 1 108  ? 47.541 66.009  21.278  1.00 10.11 ? 108  LYS A O   1 
ATOM   683  C  CB  . LYS A 1 108  ? 48.177 68.452  19.308  1.00 10.85 ? 108  LYS A CB  1 
ATOM   684  C  CG  . LYS A 1 108  ? 47.866 69.594  20.219  1.00 12.39 ? 108  LYS A CG  1 
ATOM   685  C  CD  . LYS A 1 108  ? 48.989 70.641  20.020  1.00 14.21 ? 108  LYS A CD  1 
ATOM   686  C  CE  . LYS A 1 108  ? 48.836 71.720  21.031  1.00 15.48 ? 108  LYS A CE  1 
ATOM   687  N  NZ  . LYS A 1 108  ? 49.979 72.698  20.893  1.00 17.27 ? 108  LYS A NZ  1 
ATOM   688  N  N   . HIS A 1 109  ? 45.714 67.325  21.258  1.00 8.79  ? 109  HIS A N   1 
ATOM   689  C  CA  . HIS A 1 109  ? 45.271 66.949  22.602  1.00 9.50  ? 109  HIS A CA  1 
ATOM   690  C  C   . HIS A 1 109  ? 44.650 65.586  22.581  1.00 10.01 ? 109  HIS A C   1 
ATOM   691  O  O   . HIS A 1 109  ? 44.871 64.774  23.498  1.00 10.21 ? 109  HIS A O   1 
ATOM   692  C  CB  . HIS A 1 109  ? 44.292 67.997  23.110  1.00 12.17 ? 109  HIS A CB  1 
ATOM   693  C  CG  . HIS A 1 109  ? 44.893 69.353  23.150  1.00 13.93 ? 109  HIS A CG  1 
ATOM   694  N  ND1 . HIS A 1 109  ? 45.917 69.663  24.023  1.00 17.03 ? 109  HIS A ND1 1 
ATOM   695  C  CD2 . HIS A 1 109  ? 44.666 70.456  22.406  1.00 16.17 ? 109  HIS A CD2 1 
ATOM   696  C  CE1 . HIS A 1 109  ? 46.295 70.914  23.811  1.00 16.47 ? 109  HIS A CE1 1 
ATOM   697  N  NE2 . HIS A 1 109  ? 45.551 71.415  22.840  1.00 18.25 ? 109  HIS A NE2 1 
ATOM   698  N  N   . ILE A 1 110  ? 43.879 65.283  21.530  1.00 9.74  ? 110  ILE A N   1 
ATOM   699  C  CA  . ILE A 1 110  ? 43.285 63.947  21.420  1.00 8.96  ? 110  ILE A CA  1 
ATOM   700  C  C   . ILE A 1 110  ? 44.380 62.893  21.396  1.00 8.87  ? 110  ILE A C   1 
ATOM   701  O  O   . ILE A 1 110  ? 44.335 61.883  22.120  1.00 10.05 ? 110  ILE A O   1 
ATOM   702  C  CB  . ILE A 1 110  ? 42.447 63.860  20.105  1.00 9.02  ? 110  ILE A CB  1 
ATOM   703  C  CG1 . ILE A 1 110  ? 41.234 64.763  20.189  1.00 9.03  ? 110  ILE A CG1 1 
ATOM   704  C  CG2 . ILE A 1 110  ? 42.081 62.384  19.773  1.00 9.42  ? 110  ILE A CG2 1 
ATOM   705  C  CD1 . ILE A 1 110  ? 40.546 64.986  18.801  1.00 9.06  ? 110  ILE A CD1 1 
ATOM   706  N  N   . LEU A 1 111  ? 45.412 63.092  20.581  1.00 9.10  ? 111  LEU A N   1 
ATOM   707  C  CA  . LEU A 1 111  ? 46.474 62.112  20.516  1.00 9.13  ? 111  LEU A CA  1 
ATOM   708  C  C   . LEU A 1 111  ? 47.348 62.021  21.763  1.00 9.20  ? 111  LEU A C   1 
ATOM   709  O  O   . LEU A 1 111  ? 47.761 60.933  22.167  1.00 10.31 ? 111  LEU A O   1 
ATOM   710  C  CB  . LEU A 1 111  ? 47.323 62.369  19.236  1.00 8.88  ? 111  LEU A CB  1 
ATOM   711  C  CG  . LEU A 1 111  ? 46.565 62.004  17.946  1.00 8.80  ? 111  LEU A CG  1 
ATOM   712  C  CD1 . LEU A 1 111  ? 47.379 62.499  16.768  1.00 10.57 ? 111  LEU A CD1 1 
ATOM   713  C  CD2 . LEU A 1 111  ? 46.309 60.517  17.883  1.00 11.26 ? 111  LEU A CD2 1 
ATOM   714  N  N   . SER A 1 112  ? 47.634 63.170  22.362  1.00 9.72  ? 112  SER A N   1 
ATOM   715  C  CA  . SER A 1 112  ? 48.465 63.138  23.564  1.00 9.90  ? 112  SER A CA  1 
ATOM   716  C  C   . SER A 1 112  ? 47.673 62.464  24.706  1.00 10.02 ? 112  SER A C   1 
ATOM   717  O  O   . SER A 1 112  ? 48.249 61.684  25.495  1.00 11.08 ? 112  SER A O   1 
ATOM   718  C  CB  A SER A 1 112  ? 48.860 64.559  23.914  0.50 9.44  ? 112  SER A CB  1 
ATOM   719  C  CB  B SER A 1 112  ? 48.510 64.670  24.056  0.50 11.80 ? 112  SER A CB  1 
ATOM   720  O  OG  A SER A 1 112  ? 49.546 64.589  25.146  0.50 10.86 ? 112  SER A OG  1 
ATOM   721  O  OG  B SER A 1 112  ? 49.354 65.377  23.211  0.50 16.45 ? 112  SER A OG  1 
ATOM   722  N  N   . ASN A 1 113  ? 46.369 62.739  24.789  1.00 9.82  ? 113  ASN A N   1 
ATOM   723  C  CA  . ASN A 1 113  ? 45.583 62.100  25.844  1.00 11.15 ? 113  ASN A CA  1 
ATOM   724  C  C   . ASN A 1 113  ? 45.327 60.641  25.515  1.00 11.65 ? 113  ASN A C   1 
ATOM   725  O  O   . ASN A 1 113  ? 45.241 59.803  26.445  1.00 12.19 ? 113  ASN A O   1 
ATOM   726  C  CB  . ASN A 1 113  ? 44.342 62.896  26.176  1.00 12.50 ? 113  ASN A CB  1 
ATOM   727  C  CG  . ASN A 1 113  ? 44.728 64.250  26.845  1.00 11.84 ? 113  ASN A CG  1 
ATOM   728  O  OD1 . ASN A 1 113  ? 45.856 64.371  27.437  1.00 16.82 ? 113  ASN A OD1 1 
ATOM   729  N  ND2 . ASN A 1 113  ? 43.886 65.242  26.722  1.00 14.17 ? 113  ASN A ND2 1 
ATOM   730  N  N   . ALA A 1 114  ? 45.228 60.278  24.229  1.00 10.79 ? 114  ALA A N   1 
ATOM   731  C  CA  . ALA A 1 114  ? 45.084 58.866  23.898  1.00 11.95 ? 114  ALA A CA  1 
ATOM   732  C  C   . ALA A 1 114  ? 46.322 58.099  24.343  1.00 10.83 ? 114  ALA A C   1 
ATOM   733  O  O   . ALA A 1 114  ? 46.252 56.962  24.882  1.00 11.54 ? 114  ALA A O   1 
ATOM   734  C  CB  . ALA A 1 114  ? 44.926 58.726  22.374  1.00 11.80 ? 114  ALA A CB  1 
ATOM   735  N  N   . LEU A 1 115  ? 47.496 58.696  24.152  1.00 10.98 ? 115  LEU A N   1 
ATOM   736  C  CA  . LEU A 1 115  ? 48.727 58.033  24.546  1.00 11.06 ? 115  LEU A CA  1 
ATOM   737  C  C   . LEU A 1 115  ? 48.736 57.770  26.068  1.00 11.96 ? 115  LEU A C   1 
ATOM   738  O  O   . LEU A 1 115  ? 49.003 56.649  26.509  1.00 13.27 ? 115  LEU A O   1 
ATOM   739  C  CB  . LEU A 1 115  ? 49.935 58.869  24.103  1.00 11.96 ? 115  LEU A CB  1 
ATOM   740  C  CG  . LEU A 1 115  ? 51.296 58.321  24.554  1.00 12.89 ? 115  LEU A CG  1 
ATOM   741  C  CD1 . LEU A 1 115  ? 51.571 56.875  24.104  1.00 15.49 ? 115  LEU A CD1 1 
ATOM   742  C  CD2 . LEU A 1 115  ? 52.350 59.260  23.964  1.00 15.85 ? 115  LEU A CD2 1 
ATOM   743  N  N   . ARG A 1 116  ? 48.365 58.800  26.804  1.00 12.51 ? 116  ARG A N   1 
ATOM   744  C  CA  . ARG A 1 116  ? 48.345 58.663  28.255  1.00 13.70 ? 116  ARG A CA  1 
ATOM   745  C  C   . ARG A 1 116  ? 47.278 57.654  28.706  1.00 12.43 ? 116  ARG A C   1 
ATOM   746  O  O   . ARG A 1 116  ? 47.582 56.734  29.482  1.00 13.51 ? 116  ARG A O   1 
ATOM   747  C  CB  . ARG A 1 116  ? 48.078 60.007  28.882  1.00 16.36 ? 116  ARG A CB  1 
ATOM   748  C  CG  . ARG A 1 116  ? 47.713 59.942  30.406  1.00 20.91 ? 116  ARG A CG  1 
ATOM   749  C  CD  . ARG A 1 116  ? 46.876 61.182  30.814  1.00 24.94 ? 116  ARG A CD  1 
ATOM   750  N  NE  . ARG A 1 116  ? 46.443 61.167  32.218  1.00 27.81 ? 116  ARG A NE  1 
ATOM   751  C  CZ  . ARG A 1 116  ? 46.096 62.262  32.895  1.00 29.94 ? 116  ARG A CZ  1 
ATOM   752  N  NH1 . ARG A 1 116  ? 46.138 63.451  32.304  1.00 29.84 ? 116  ARG A NH1 1 
ATOM   753  N  NH2 . ARG A 1 116  ? 45.701 62.165  34.169  1.00 31.53 ? 116  ARG A NH2 1 
ATOM   754  N  N   . HIS A 1 117  ? 46.048 57.813  28.231  1.00 12.38 ? 117  HIS A N   1 
ATOM   755  C  CA  . HIS A 1 117  ? 44.990 56.917  28.694  1.00 12.75 ? 117  HIS A CA  1 
ATOM   756  C  C   . HIS A 1 117  ? 45.146 55.510  28.275  1.00 13.07 ? 117  HIS A C   1 
ATOM   757  O  O   . HIS A 1 117  ? 44.850 54.612  29.062  1.00 13.41 ? 117  HIS A O   1 
ATOM   758  C  CB  . HIS A 1 117  ? 43.631 57.464  28.346  1.00 14.01 ? 117  HIS A CB  1 
ATOM   759  C  CG  . HIS A 1 117  ? 43.275 58.655  29.171  1.00 15.76 ? 117  HIS A CG  1 
ATOM   760  N  ND1 . HIS A 1 117  ? 42.639 58.544  30.399  1.00 16.29 ? 117  HIS A ND1 1 
ATOM   761  C  CD2 . HIS A 1 117  ? 43.580 59.965  29.013  1.00 16.96 ? 117  HIS A CD2 1 
ATOM   762  C  CE1 . HIS A 1 117  ? 42.578 59.745  30.959  1.00 16.41 ? 117  HIS A CE1 1 
ATOM   763  N  NE2 . HIS A 1 117  ? 43.145 60.621  30.145  1.00 17.48 ? 117  HIS A NE2 1 
ATOM   764  N  N   . LEU A 1 118  ? 45.571 55.235  27.043  1.00 11.59 ? 118  LEU A N   1 
ATOM   765  C  CA  . LEU A 1 118  ? 45.784 53.857  26.648  1.00 11.90 ? 118  LEU A CA  1 
ATOM   766  C  C   . LEU A 1 118  ? 46.955 53.251  27.430  1.00 12.37 ? 118  LEU A C   1 
ATOM   767  O  O   . LEU A 1 118  ? 46.886 52.101  27.885  1.00 13.08 ? 118  LEU A O   1 
ATOM   768  C  CB  . LEU A 1 118  ? 46.012 53.804  25.105  1.00 11.35 ? 118  LEU A CB  1 
ATOM   769  C  CG  . LEU A 1 118  ? 44.749 54.242  24.300  1.00 13.15 ? 118  LEU A CG  1 
ATOM   770  C  CD1 . LEU A 1 118  ? 45.213 54.406  22.794  1.00 14.12 ? 118  LEU A CD1 1 
ATOM   771  C  CD2 . LEU A 1 118  ? 43.626 53.229  24.425  1.00 14.05 ? 118  LEU A CD2 1 
ATOM   772  N  N   . HIS A 1 119  ? 48.019 54.017  27.621  1.00 12.73 ? 119  HIS A N   1 
ATOM   773  C  CA  . HIS A 1 119  ? 49.123 53.467  28.381  1.00 12.83 ? 119  HIS A CA  1 
ATOM   774  C  C   . HIS A 1 119  ? 48.648 53.052  29.774  1.00 14.30 ? 119  HIS A C   1 
ATOM   775  O  O   . HIS A 1 119  ? 48.978 51.976  30.245  1.00 15.08 ? 119  HIS A O   1 
ATOM   776  C  CB  . HIS A 1 119  ? 50.207 54.525  28.534  1.00 16.71 ? 119  HIS A CB  1 
ATOM   777  C  CG  . HIS A 1 119  ? 51.335 54.101  29.410  1.00 19.83 ? 119  HIS A CG  1 
ATOM   778  N  ND1 . HIS A 1 119  ? 51.406 54.448  30.742  1.00 22.81 ? 119  HIS A ND1 1 
ATOM   779  C  CD2 . HIS A 1 119  ? 52.402 53.306  29.161  1.00 22.25 ? 119  HIS A CD2 1 
ATOM   780  C  CE1 . HIS A 1 119  ? 52.478 53.881  31.278  1.00 23.27 ? 119  HIS A CE1 1 
ATOM   781  N  NE2 . HIS A 1 119  ? 53.096 53.185  30.341  1.00 24.01 ? 119  HIS A NE2 1 
ATOM   782  N  N   . ASP A 1 120  ? 47.870 53.905  30.402  1.00 14.42 ? 120  ASP A N   1 
ATOM   783  C  CA  . ASP A 1 120  ? 47.419 53.628  31.785  1.00 15.49 ? 120  ASP A CA  1 
ATOM   784  C  C   . ASP A 1 120  ? 46.260 52.638  31.950  1.00 16.60 ? 120  ASP A C   1 
ATOM   785  O  O   . ASP A 1 120  ? 46.010 52.180  33.083  1.00 17.05 ? 120  ASP A O   1 
ATOM   786  C  CB  . ASP A 1 120  ? 47.006 54.937  32.461  1.00 16.16 ? 120  ASP A CB  1 
ATOM   787  C  CG  . ASP A 1 120  ? 48.196 55.851  32.762  1.00 17.64 ? 120  ASP A CG  1 
ATOM   788  O  OD1 . ASP A 1 120  ? 49.360 55.410  32.673  1.00 20.78 ? 120  ASP A OD1 1 
ATOM   789  O  OD2 . ASP A 1 120  ? 47.982 57.026  33.084  1.00 20.60 ? 120  ASP A OD2 1 
ATOM   790  N  N   . ASN A 1 121  ? 45.551 52.280  30.875  1.00 14.76 ? 121  ASN A N   1 
ATOM   791  C  CA  . ASN A 1 121  ? 44.360 51.412  30.951  1.00 13.62 ? 121  ASN A CA  1 
ATOM   792  C  C   . ASN A 1 121  ? 44.568 50.374  29.889  1.00 14.13 ? 121  ASN A C   1 
ATOM   793  O  O   . ASN A 1 121  ? 44.084 50.518  28.767  1.00 14.07 ? 121  ASN A O   1 
ATOM   794  C  CB  . ASN A 1 121  ? 43.115 52.234  30.701  1.00 12.95 ? 121  ASN A CB  1 
ATOM   795  C  CG  . ASN A 1 121  ? 42.943 53.323  31.743  1.00 13.56 ? 121  ASN A CG  1 
ATOM   796  O  OD1 . ASN A 1 121  ? 43.320 54.503  31.543  1.00 16.29 ? 121  ASN A OD1 1 
ATOM   797  N  ND2 . ASN A 1 121  ? 42.386 52.925  32.890  1.00 12.83 ? 121  ASN A ND2 1 
ATOM   798  N  N   . PRO A 1 122  ? 45.278 49.300  30.205  1.00 13.18 ? 122  PRO A N   1 
ATOM   799  C  CA  . PRO A 1 122  ? 45.586 48.260  29.219  1.00 13.32 ? 122  PRO A CA  1 
ATOM   800  C  C   . PRO A 1 122  ? 44.471 47.624  28.408  1.00 13.68 ? 122  PRO A C   1 
ATOM   801  O  O   . PRO A 1 122  ? 44.768 47.113  27.280  1.00 14.67 ? 122  PRO A O   1 
ATOM   802  C  CB  . PRO A 1 122  ? 46.397 47.221  30.019  1.00 14.21 ? 122  PRO A CB  1 
ATOM   803  C  CG  . PRO A 1 122  ? 46.937 48.031  31.182  1.00 16.15 ? 122  PRO A CG  1 
ATOM   804  C  CD  . PRO A 1 122  ? 45.801 48.933  31.556  1.00 14.26 ? 122  PRO A CD  1 
ATOM   805  N  N   . GLU A 1 123  ? 43.235 47.615  28.911  1.00 13.10 ? 123  GLU A N   1 
ATOM   806  C  CA  . GLU A 1 123  ? 42.145 47.006  28.140  1.00 14.12 ? 123  GLU A CA  1 
ATOM   807  C  C   . GLU A 1 123  ? 41.444 48.001  27.220  1.00 13.09 ? 123  GLU A C   1 
ATOM   808  O  O   . GLU A 1 123  ? 40.593 47.601  26.429  1.00 14.08 ? 123  GLU A O   1 
ATOM   809  C  CB  . GLU A 1 123  ? 41.093 46.337  29.052  1.00 15.58 ? 123  GLU A CB  1 
ATOM   810  C  CG  . GLU A 1 123  ? 41.663 45.233  29.962  1.00 21.10 ? 123  GLU A CG  1 
ATOM   811  C  CD  . GLU A 1 123  ? 42.325 44.139  29.200  1.00 23.87 ? 123  GLU A CD  1 
ATOM   812  O  OE1 . GLU A 1 123  ? 41.697 43.590  28.263  1.00 26.03 ? 123  GLU A OE1 1 
ATOM   813  O  OE2 . GLU A 1 123  ? 43.491 43.806  29.548  1.00 28.34 ? 123  GLU A OE2 1 
ATOM   814  N  N   . MET A 1 124  ? 41.741 49.291  27.373  1.00 12.11 ? 124  MET A N   1 
ATOM   815  C  CA  . MET A 1 124  ? 41.108 50.312  26.540  1.00 11.85 ? 124  MET A CA  1 
ATOM   816  C  C   . MET A 1 124  ? 41.762 50.217  25.143  1.00 10.98 ? 124  MET A C   1 
ATOM   817  O  O   . MET A 1 124  ? 42.927 49.864  25.016  1.00 11.07 ? 124  MET A O   1 
ATOM   818  C  CB  . MET A 1 124  ? 41.348 51.682  27.167  1.00 13.19 ? 124  MET A CB  1 
ATOM   819  C  CG  . MET A 1 124  ? 40.631 52.862  26.484  1.00 13.75 ? 124  MET A CG  1 
ATOM   820  S  SD  . MET A 1 124  ? 38.869 52.575  26.315  1.00 13.84 ? 124  MET A SD  1 
ATOM   821  C  CE  . MET A 1 124  ? 38.365 54.140  25.444  1.00 14.84 ? 124  MET A CE  1 
ATOM   822  N  N   . LYS A 1 125  ? 40.968 50.545  24.110  1.00 10.34 ? 125  LYS A N   1 
ATOM   823  C  CA  . LYS A 1 125  ? 41.394 50.473  22.719  1.00 10.78 ? 125  LYS A CA  1 
ATOM   824  C  C   . LYS A 1 125  ? 40.974 51.746  21.996  1.00 10.55 ? 125  LYS A C   1 
ATOM   825  O  O   . LYS A 1 125  ? 40.101 52.498  22.450  1.00 10.83 ? 125  LYS A O   1 
ATOM   826  C  CB  . LYS A 1 125  ? 40.690 49.316  22.015  1.00 12.82 ? 125  LYS A CB  1 
ATOM   827  C  CG  . LYS A 1 125  ? 40.875 47.960  22.710  1.00 16.19 ? 125  LYS A CG  1 
ATOM   828  C  CD  . LYS A 1 125  ? 42.246 47.462  22.479  1.00 19.12 ? 125  LYS A CD  1 
ATOM   829  C  CE  . LYS A 1 125  ? 42.578 46.207  23.297  1.00 22.32 ? 125  LYS A CE  1 
ATOM   830  N  NZ  . LYS A 1 125  ? 41.614 45.145  23.060  1.00 24.00 ? 125  LYS A NZ  1 
ATOM   831  N  N   . PHE A 1 126  ? 41.610 51.978  20.825  1.00 9.46  ? 126  PHE A N   1 
ATOM   832  C  CA  . PHE A 1 126  ? 41.307 53.188  20.051  1.00 8.83  ? 126  PHE A CA  1 
ATOM   833  C  C   . PHE A 1 126  ? 41.804 52.941  18.628  1.00 7.75  ? 126  PHE A C   1 
ATOM   834  O  O   . PHE A 1 126  ? 42.853 52.372  18.443  1.00 9.93  ? 126  PHE A O   1 
ATOM   835  C  CB  . PHE A 1 126  ? 42.080 54.371  20.686  1.00 9.33  ? 126  PHE A CB  1 
ATOM   836  C  CG  . PHE A 1 126  ? 41.691 55.751  20.189  1.00 8.45  ? 126  PHE A CG  1 
ATOM   837  C  CD1 . PHE A 1 126  ? 40.379 56.185  20.206  1.00 8.77  ? 126  PHE A CD1 1 
ATOM   838  C  CD2 . PHE A 1 126  ? 42.724 56.665  19.840  1.00 9.34  ? 126  PHE A CD2 1 
ATOM   839  C  CE1 . PHE A 1 126  ? 40.074 57.560  19.876  1.00 9.76  ? 126  PHE A CE1 1 
ATOM   840  C  CE2 . PHE A 1 126  ? 42.426 58.018  19.527  1.00 9.13  ? 126  PHE A CE2 1 
ATOM   841  C  CZ  . PHE A 1 126  ? 41.124 58.474  19.541  1.00 8.81  ? 126  PHE A CZ  1 
ATOM   842  N  N   . ILE A 1 127  ? 41.007 53.388  17.649  1.00 8.49  ? 127  ILE A N   1 
ATOM   843  C  CA  . ILE A 1 127  ? 41.429 53.260  16.242  1.00 7.98  ? 127  ILE A CA  1 
ATOM   844  C  C   . ILE A 1 127  ? 41.671 54.653  15.687  1.00 7.77  ? 127  ILE A C   1 
ATOM   845  O  O   . ILE A 1 127  ? 41.077 55.653  16.123  1.00 8.18  ? 127  ILE A O   1 
ATOM   846  C  CB  . ILE A 1 127  ? 40.408 52.524  15.335  1.00 8.45  ? 127  ILE A CB  1 
ATOM   847  C  CG1 . ILE A 1 127  ? 39.000 53.147  15.355  1.00 8.57  ? 127  ILE A CG1 1 
ATOM   848  C  CG2 . ILE A 1 127  ? 40.367 51.055  15.785  1.00 8.99  ? 127  ILE A CG2 1 
ATOM   849  C  CD1 . ILE A 1 127  ? 38.073 52.537  14.238  1.00 8.71  ? 127  ILE A CD1 1 
ATOM   850  N  N   . TRP A 1 128  ? 42.624 54.717  14.775  1.00 7.83  ? 128  TRP A N   1 
ATOM   851  C  CA  . TRP A 1 128  ? 43.015 56.007  14.152  1.00 7.33  ? 128  TRP A CA  1 
ATOM   852  C  C   . TRP A 1 128  ? 43.135 55.889  12.648  1.00 6.54  ? 128  TRP A C   1 
ATOM   853  O  O   . TRP A 1 128  ? 43.799 54.972  12.156  1.00 7.26  ? 128  TRP A O   1 
ATOM   854  C  CB  . TRP A 1 128  ? 44.361 56.479  14.731  1.00 7.69  ? 128  TRP A CB  1 
ATOM   855  C  CG  . TRP A 1 128  ? 44.647 57.931  14.393  1.00 7.33  ? 128  TRP A CG  1 
ATOM   856  C  CD1 . TRP A 1 128  ? 45.338 58.436  13.295  1.00 7.13  ? 128  TRP A CD1 1 
ATOM   857  C  CD2 . TRP A 1 128  ? 44.069 59.037  15.050  1.00 7.33  ? 128  TRP A CD2 1 
ATOM   858  N  NE1 . TRP A 1 128  ? 45.211 59.788  13.252  1.00 7.80  ? 128  TRP A NE1 1 
ATOM   859  C  CE2 . TRP A 1 128  ? 44.434 60.202  14.317  1.00 7.03  ? 128  TRP A CE2 1 
ATOM   860  C  CE3 . TRP A 1 128  ? 43.250 59.168  16.207  1.00 8.84  ? 128  TRP A CE3 1 
ATOM   861  C  CZ2 . TRP A 1 128  ? 44.028 61.478  14.687  1.00 7.68  ? 128  TRP A CZ2 1 
ATOM   862  C  CZ3 . TRP A 1 128  ? 42.844 60.438  16.569  1.00 9.19  ? 128  TRP A CZ3 1 
ATOM   863  C  CH2 . TRP A 1 128  ? 43.239 61.593  15.798  1.00 8.20  ? 128  TRP A CH2 1 
ATOM   864  N  N   . ALA A 1 129  ? 42.536 56.841  11.928  1.00 7.34  ? 129  ALA A N   1 
ATOM   865  C  CA  . ALA A 1 129  ? 42.507 56.772  10.462  1.00 7.18  ? 129  ALA A CA  1 
ATOM   866  C  C   . ALA A 1 129  ? 43.397 57.755  9.711   1.00 8.41  ? 129  ALA A C   1 
ATOM   867  O  O   . ALA A 1 129  ? 43.977 57.368  8.714   1.00 9.41  ? 129  ALA A O   1 
ATOM   868  C  CB  . ALA A 1 129  ? 41.068 57.017  9.972   1.00 8.97  ? 129  ALA A CB  1 
ATOM   869  N  N   . GLU A 1 130  ? 43.505 58.997  10.168  1.00 7.82  ? 130  GLU A N   1 
ATOM   870  C  CA  . GLU A 1 130  ? 44.131 60.056  9.347   1.00 7.61  ? 130  GLU A CA  1 
ATOM   871  C  C   . GLU A 1 130  ? 45.605 60.205  9.673   1.00 7.05  ? 130  GLU A C   1 
ATOM   872  O  O   . GLU A 1 130  ? 46.012 60.819  10.714  1.00 7.71  ? 130  GLU A O   1 
ATOM   873  C  CB  . GLU A 1 130  ? 43.382 61.358  9.603   1.00 8.95  ? 130  GLU A CB  1 
ATOM   874  C  CG  . GLU A 1 130  ? 41.838 61.300  9.335   1.00 9.22  ? 130  GLU A CG  1 
ATOM   875  C  CD  . GLU A 1 130  ? 41.020 60.892  10.534  1.00 9.42  ? 130  GLU A CD  1 
ATOM   876  O  OE1 . GLU A 1 130  ? 41.615 60.635  11.590  1.00 10.92 ? 130  GLU A OE1 1 
ATOM   877  O  OE2 . GLU A 1 130  ? 39.776 60.860  10.390  1.00 11.65 ? 130  GLU A OE2 1 
ATOM   878  N  N   . ILE A 1 131  ? 46.452 59.668  8.806   1.00 6.30  ? 131  ILE A N   1 
ATOM   879  C  CA  . ILE A 1 131  ? 47.898 59.686  9.101   1.00 7.24  ? 131  ILE A CA  1 
ATOM   880  C  C   . ILE A 1 131  ? 48.519 61.055  8.954   1.00 7.61  ? 131  ILE A C   1 
ATOM   881  O  O   . ILE A 1 131  ? 49.529 61.306  9.615   1.00 8.84  ? 131  ILE A O   1 
ATOM   882  C  CB  . ILE A 1 131  ? 48.604 58.604  8.265   1.00 7.13  ? 131  ILE A CB  1 
ATOM   883  C  CG1 . ILE A 1 131  ? 47.980 57.241  8.558   1.00 7.68  ? 131  ILE A CG1 1 
ATOM   884  C  CG2 . ILE A 1 131  ? 50.096 58.539  8.613   1.00 8.80  ? 131  ILE A CG2 1 
ATOM   885  C  CD1 . ILE A 1 131  ? 47.785 56.937  10.101  1.00 10.53 ? 131  ILE A CD1 1 
ATOM   886  N  N   . SER A 1 132  ? 47.945 61.946  8.163   1.00 7.24  ? 132  SER A N   1 
ATOM   887  C  CA  . SER A 1 132  ? 48.460 63.321  8.088   1.00 7.50  ? 132  SER A CA  1 
ATOM   888  C  C   . SER A 1 132  ? 48.555 63.918  9.509   1.00 7.82  ? 132  SER A C   1 
ATOM   889  O  O   . SER A 1 132  ? 49.621 64.461  9.871   1.00 8.59  ? 132  SER A O   1 
ATOM   890  C  CB  . SER A 1 132  ? 47.543 64.211  7.227   1.00 7.84  ? 132  SER A CB  1 
ATOM   891  O  OG  . SER A 1 132  ? 46.185 64.112  7.664   1.00 7.70  ? 132  SER A OG  1 
ATOM   892  N  N   . TYR A 1 133  ? 47.489 63.772  10.319  1.00 7.46  ? 133  TYR A N   1 
ATOM   893  C  CA  . TYR A 1 133  ? 47.530 64.293  11.686  1.00 7.36  ? 133  TYR A CA  1 
ATOM   894  C  C   . TYR A 1 133  ? 48.473 63.465  12.546  1.00 7.05  ? 133  TYR A C   1 
ATOM   895  O  O   . TYR A 1 133  ? 49.145 64.060  13.418  1.00 8.92  ? 133  TYR A O   1 
ATOM   896  C  CB  . TYR A 1 133  ? 46.160 64.183  12.353  1.00 7.38  ? 133  TYR A CB  1 
ATOM   897  C  CG  . TYR A 1 133  ? 45.215 65.310  12.000  1.00 6.80  ? 133  TYR A CG  1 
ATOM   898  C  CD1 . TYR A 1 133  ? 45.555 66.644  12.268  1.00 8.27  ? 133  TYR A CD1 1 
ATOM   899  C  CD2 . TYR A 1 133  ? 43.980 65.071  11.430  1.00 7.27  ? 133  TYR A CD2 1 
ATOM   900  C  CE1 . TYR A 1 133  ? 44.703 67.697  11.972  1.00 7.80  ? 133  TYR A CE1 1 
ATOM   901  C  CE2 . TYR A 1 133  ? 43.087 66.135  11.124  1.00 7.06  ? 133  TYR A CE2 1 
ATOM   902  C  CZ  . TYR A 1 133  ? 43.462 67.443  11.398  1.00 8.15  ? 133  TYR A CZ  1 
ATOM   903  O  OH  . TYR A 1 133  ? 42.642 68.503  11.116  1.00 8.81  ? 133  TYR A OH  1 
ATOM   904  N  N   . PHE A 1 134  ? 48.502 62.145  12.393  1.00 7.42  ? 134  PHE A N   1 
ATOM   905  C  CA  . PHE A 1 134  ? 49.339 61.343  13.270  1.00 8.30  ? 134  PHE A CA  1 
ATOM   906  C  C   . PHE A 1 134  ? 50.803 61.660  13.026  1.00 9.18  ? 134  PHE A C   1 
ATOM   907  O  O   . PHE A 1 134  ? 51.585 61.774  14.004  1.00 9.51  ? 134  PHE A O   1 
ATOM   908  C  CB  . PHE A 1 134  ? 49.065 59.848  13.085  1.00 8.32  ? 134  PHE A CB  1 
ATOM   909  C  CG  . PHE A 1 134  ? 49.624 59.029  14.207  1.00 8.93  ? 134  PHE A CG  1 
ATOM   910  C  CD1 . PHE A 1 134  ? 48.853 58.832  15.373  1.00 9.45  ? 134  PHE A CD1 1 
ATOM   911  C  CD2 . PHE A 1 134  ? 50.924 58.526  14.125  1.00 10.63 ? 134  PHE A CD2 1 
ATOM   912  C  CE1 . PHE A 1 134  ? 49.421 58.102  16.497  1.00 11.60 ? 134  PHE A CE1 1 
ATOM   913  C  CE2 . PHE A 1 134  ? 51.505 57.801  15.219  1.00 11.75 ? 134  PHE A CE2 1 
ATOM   914  C  CZ  . PHE A 1 134  ? 50.726 57.603  16.399  1.00 11.55 ? 134  PHE A CZ  1 
ATOM   915  N  N   . ALA A 1 135  ? 51.194 61.836  11.759  1.00 9.17  ? 135  ALA A N   1 
ATOM   916  C  CA  . ALA A 1 135  ? 52.593 62.169  11.460  1.00 9.54  ? 135  ALA A CA  1 
ATOM   917  C  C   . ALA A 1 135  ? 52.899 63.595  11.998  1.00 10.09 ? 135  ALA A C   1 
ATOM   918  O  O   . ALA A 1 135  ? 54.025 63.792  12.525  1.00 12.19 ? 135  ALA A O   1 
ATOM   919  C  CB  . ALA A 1 135  ? 52.827 62.095  9.964   1.00 10.93 ? 135  ALA A CB  1 
ATOM   920  N  N   . ARG A 1 136  ? 51.988 64.545  11.882  1.00 10.31 ? 136  ARG A N   1 
ATOM   921  C  CA  . ARG A 1 136  ? 52.190 65.929  12.400  1.00 11.20 ? 136  ARG A CA  1 
ATOM   922  C  C   . ARG A 1 136  ? 52.443 65.863  13.932  1.00 12.36 ? 136  ARG A C   1 
ATOM   923  O  O   . ARG A 1 136  ? 53.307 66.572  14.466  1.00 14.50 ? 136  ARG A O   1 
ATOM   924  C  CB  . ARG A 1 136  ? 50.958 66.784  12.085  1.00 11.73 ? 136  ARG A CB  1 
ATOM   925  C  CG  . ARG A 1 136  ? 50.946 68.156  12.770  1.00 11.18 ? 136  ARG A CG  1 
ATOM   926  C  CD  . ARG A 1 136  ? 51.860 69.162  12.018  1.00 13.44 ? 136  ARG A CD  1 
ATOM   927  N  NE  . ARG A 1 136  ? 51.803 70.479  12.680  1.00 12.92 ? 136  ARG A NE  1 
ATOM   928  C  CZ  . ARG A 1 136  ? 52.559 70.778  13.732  1.00 13.86 ? 136  ARG A CZ  1 
ATOM   929  N  NH1 . ARG A 1 136  ? 53.423 69.858  14.185  1.00 14.99 ? 136  ARG A NH1 1 
ATOM   930  N  NH2 . ARG A 1 136  ? 52.410 71.975  14.324  1.00 12.37 ? 136  ARG A NH2 1 
ATOM   931  N  N   . PHE A 1 137  ? 51.732 64.982  14.618  1.00 11.09 ? 137  PHE A N   1 
ATOM   932  C  CA  . PHE A 1 137  ? 51.852 64.820  16.051  1.00 11.33 ? 137  PHE A CA  1 
ATOM   933  C  C   . PHE A 1 137  ? 53.130 64.092  16.433  1.00 11.71 ? 137  PHE A C   1 
ATOM   934  O  O   . PHE A 1 137  ? 53.914 64.590  17.290  1.00 12.01 ? 137  PHE A O   1 
ATOM   935  C  CB  . PHE A 1 137  ? 50.666 63.997  16.542  1.00 10.87 ? 137  PHE A CB  1 
ATOM   936  C  CG  . PHE A 1 137  ? 50.686 63.729  18.037  1.00 11.80 ? 137  PHE A CG  1 
ATOM   937  C  CD1 . PHE A 1 137  ? 50.367 64.761  18.892  1.00 11.21 ? 137  PHE A CD1 1 
ATOM   938  C  CD2 . PHE A 1 137  ? 51.021 62.482  18.542  1.00 12.24 ? 137  PHE A CD2 1 
ATOM   939  C  CE1 . PHE A 1 137  ? 50.372 64.579  20.276  1.00 13.05 ? 137  PHE A CE1 1 
ATOM   940  C  CE2 . PHE A 1 137  ? 51.051 62.295  19.984  1.00 12.71 ? 137  PHE A CE2 1 
ATOM   941  C  CZ  . PHE A 1 137  ? 50.720 63.351  20.794  1.00 12.61 ? 137  PHE A CZ  1 
ATOM   942  N  N   . TYR A 1 138  ? 53.379 62.944  15.810  1.00 12.67 ? 138  TYR A N   1 
ATOM   943  C  CA  . TYR A 1 138  ? 54.516 62.116  16.153  1.00 14.65 ? 138  TYR A CA  1 
ATOM   944  C  C   . TYR A 1 138  ? 55.873 62.788  15.993  1.00 15.47 ? 138  TYR A C   1 
ATOM   945  O  O   . TYR A 1 138  ? 56.780 62.590  16.832  1.00 15.64 ? 138  TYR A O   1 
ATOM   946  C  CB  A TYR A 1 138  ? 54.447 60.804  15.354  0.50 14.37 ? 138  TYR A CB  1 
ATOM   947  C  CB  B TYR A 1 138  ? 54.587 60.903  15.169  0.50 14.37 ? 138  TYR A CB  1 
ATOM   948  C  CG  A TYR A 1 138  ? 55.444 59.750  15.776  0.50 14.29 ? 138  TYR A CG  1 
ATOM   949  C  CG  B TYR A 1 138  ? 55.778 59.981  15.386  0.50 14.16 ? 138  TYR A CG  1 
ATOM   950  C  CD1 A TYR A 1 138  ? 55.158 58.869  16.802  0.50 13.20 ? 138  TYR A CD1 1 
ATOM   951  C  CD1 B TYR A 1 138  ? 55.699 58.934  16.299  0.50 14.90 ? 138  TYR A CD1 1 
ATOM   952  C  CD2 A TYR A 1 138  ? 56.664 59.633  15.124  0.50 13.82 ? 138  TYR A CD2 1 
ATOM   953  C  CD2 B TYR A 1 138  ? 56.961 60.149  14.669  0.50 14.75 ? 138  TYR A CD2 1 
ATOM   954  C  CE1 A TYR A 1 138  ? 56.074 57.882  17.173  0.50 14.33 ? 138  TYR A CE1 1 
ATOM   955  C  CE1 B TYR A 1 138  ? 56.778 58.073  16.498  0.50 14.88 ? 138  TYR A CE1 1 
ATOM   956  C  CE2 A TYR A 1 138  ? 57.598 58.647  15.482  0.50 13.53 ? 138  TYR A CE2 1 
ATOM   957  C  CE2 B TYR A 1 138  ? 58.053 59.274  14.864  0.50 15.05 ? 138  TYR A CE2 1 
ATOM   958  C  CZ  A TYR A 1 138  ? 57.287 57.778  16.501  0.50 13.70 ? 138  TYR A CZ  1 
ATOM   959  C  CZ  B TYR A 1 138  ? 57.937 58.256  15.779  0.50 14.71 ? 138  TYR A CZ  1 
ATOM   960  O  OH  A TYR A 1 138  ? 58.187 56.779  16.834  0.50 14.70 ? 138  TYR A OH  1 
ATOM   961  O  OH  B TYR A 1 138  ? 58.992 57.412  16.015  0.50 15.81 ? 138  TYR A OH  1 
ATOM   962  N  N   . HIS A 1 139  ? 56.046 63.595  14.960  1.00 15.84 ? 139  HIS A N   1 
ATOM   963  C  CA  . HIS A 1 139  ? 57.321 64.243  14.770  1.00 17.90 ? 139  HIS A CA  1 
ATOM   964  C  C   . HIS A 1 139  ? 57.582 65.331  15.807  1.00 18.90 ? 139  HIS A C   1 
ATOM   965  O  O   . HIS A 1 139  ? 58.736 65.755  15.957  1.00 20.35 ? 139  HIS A O   1 
ATOM   966  C  CB  . HIS A 1 139  ? 57.417 64.696  13.302  1.00 18.48 ? 139  HIS A CB  1 
ATOM   967  C  CG  . HIS A 1 139  ? 57.613 63.554  12.337  1.00 19.74 ? 139  HIS A CG  1 
ATOM   968  N  ND1 . HIS A 1 139  ? 58.679 62.682  12.425  1.00 21.07 ? 139  HIS A ND1 1 
ATOM   969  C  CD2 . HIS A 1 139  ? 56.869 63.138  11.277  1.00 19.98 ? 139  HIS A CD2 1 
ATOM   970  C  CE1 . HIS A 1 139  ? 58.587 61.776  11.459  1.00 21.77 ? 139  HIS A CE1 1 
ATOM   971  N  NE2 . HIS A 1 139  ? 57.501 62.032  10.745  1.00 20.87 ? 139  HIS A NE2 1 
ATOM   972  N  N   . ASP A 1 140  ? 56.551 65.772  16.529  1.00 18.60 ? 140  ASP A N   1 
ATOM   973  C  CA  . ASP A 1 140  ? 56.720 66.764  17.610  1.00 18.90 ? 140  ASP A CA  1 
ATOM   974  C  C   . ASP A 1 140  ? 56.921 66.126  18.990  1.00 17.29 ? 140  ASP A C   1 
ATOM   975  O  O   . ASP A 1 140  ? 57.137 66.830  19.982  1.00 18.67 ? 140  ASP A O   1 
ATOM   976  C  CB  . ASP A 1 140  ? 55.544 67.688  17.669  1.00 19.46 ? 140  ASP A CB  1 
ATOM   977  C  CG  . ASP A 1 140  ? 55.706 68.851  16.698  1.00 21.80 ? 140  ASP A CG  1 
ATOM   978  O  OD1 . ASP A 1 140  ? 56.603 68.767  15.835  1.00 23.30 ? 140  ASP A OD1 1 
ATOM   979  O  OD2 . ASP A 1 140  ? 54.965 69.825  16.815  1.00 22.68 ? 140  ASP A OD2 1 
ATOM   980  N  N   . LEU A 1 141  ? 56.858 64.811  19.045  1.00 16.93 ? 141  LEU A N   1 
ATOM   981  C  CA  . LEU A 1 141  ? 57.059 64.101  20.310  1.00 16.79 ? 141  LEU A CA  1 
ATOM   982  C  C   . LEU A 1 141  ? 58.525 63.898  20.643  1.00 17.75 ? 141  LEU A C   1 
ATOM   983  O  O   . LEU A 1 141  ? 59.358 63.743  19.774  1.00 18.45 ? 141  LEU A O   1 
ATOM   984  C  CB  . LEU A 1 141  ? 56.458 62.692  20.262  1.00 16.40 ? 141  LEU A CB  1 
ATOM   985  C  CG  . LEU A 1 141  ? 54.949 62.541  20.212  1.00 17.34 ? 141  LEU A CG  1 
ATOM   986  C  CD1 . LEU A 1 141  ? 54.575 61.022  20.127  1.00 17.19 ? 141  LEU A CD1 1 
ATOM   987  C  CD2 . LEU A 1 141  ? 54.342 63.187  21.440  1.00 17.44 ? 141  LEU A CD2 1 
ATOM   988  N  N   . GLY A 1 142  ? 58.805 63.890  21.945  1.00 18.74 ? 142  GLY A N   1 
ATOM   989  C  CA  . GLY A 1 142  ? 60.137 63.583  22.401  1.00 20.79 ? 142  GLY A CA  1 
ATOM   990  C  C   . GLY A 1 142  ? 60.301 62.073  22.286  1.00 20.74 ? 142  GLY A C   1 
ATOM   991  O  O   . GLY A 1 142  ? 59.304 61.328  22.205  1.00 20.28 ? 142  GLY A O   1 
ATOM   992  N  N   . GLU A 1 143  ? 61.539 61.607  22.300  1.00 20.62 ? 143  GLU A N   1 
ATOM   993  C  CA  . GLU A 1 143  ? 61.830 60.193  22.181  1.00 21.32 ? 143  GLU A CA  1 
ATOM   994  C  C   . GLU A 1 143  ? 61.116 59.316  23.211  1.00 21.32 ? 143  GLU A C   1 
ATOM   995  O  O   . GLU A 1 143  ? 60.655 58.206  22.891  1.00 20.93 ? 143  GLU A O   1 
ATOM   996  C  CB  . GLU A 1 143  ? 63.342 59.964  22.280  1.00 23.74 ? 143  GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 143  ? 63.810 58.612  21.772  1.00 27.05 ? 143  GLU A CG  1 
ATOM   998  C  CD  . GLU A 1 143  ? 63.579 58.412  20.253  1.00 29.02 ? 143  GLU A CD  1 
ATOM   999  O  OE1 . GLU A 1 143  ? 63.360 59.399  19.485  1.00 31.40 ? 143  GLU A OE1 1 
ATOM   1000 O  OE2 . GLU A 1 143  ? 63.630 57.248  19.820  1.00 31.48 ? 143  GLU A OE2 1 
ATOM   1001 N  N   . ASN A 1 144  ? 61.007 59.772  24.445  1.00 21.17 ? 144  ASN A N   1 
ATOM   1002 C  CA  . ASN A 1 144  ? 60.366 58.950  25.446  1.00 22.40 ? 144  ASN A CA  1 
ATOM   1003 C  C   . ASN A 1 144  ? 58.915 58.645  25.020  1.00 20.28 ? 144  ASN A C   1 
ATOM   1004 O  O   . ASN A 1 144  ? 58.479 57.494  25.085  1.00 19.69 ? 144  ASN A O   1 
ATOM   1005 C  CB  . ASN A 1 144  ? 60.462 59.688  26.804  1.00 25.90 ? 144  ASN A CB  1 
ATOM   1006 C  CG  . ASN A 1 144  ? 59.604 59.068  27.905  1.00 30.12 ? 144  ASN A CG  1 
ATOM   1007 O  OD1 . ASN A 1 144  ? 58.382 59.332  28.004  1.00 33.33 ? 144  ASN A OD1 1 
ATOM   1008 N  ND2 . ASN A 1 144  ? 60.237 58.241  28.755  1.00 32.08 ? 144  ASN A ND2 1 
ATOM   1009 N  N   . LYS A 1 145  ? 58.211 59.673  24.557  1.00 19.54 ? 145  LYS A N   1 
ATOM   1010 C  CA  . LYS A 1 145  ? 56.826 59.503  24.123  1.00 18.22 ? 145  LYS A CA  1 
ATOM   1011 C  C   . LYS A 1 145  ? 56.733 58.707  22.801  1.00 17.01 ? 145  LYS A C   1 
ATOM   1012 O  O   . LYS A 1 145  ? 55.778 57.917  22.663  1.00 16.75 ? 145  LYS A O   1 
ATOM   1013 C  CB  . LYS A 1 145  ? 56.116 60.853  23.987  1.00 19.85 ? 145  LYS A CB  1 
ATOM   1014 C  CG  . LYS A 1 145  ? 55.852 61.556  25.326  1.00 23.31 ? 145  LYS A CG  1 
ATOM   1015 C  CD  . LYS A 1 145  ? 54.770 60.837  26.110  1.00 27.13 ? 145  LYS A CD  1 
ATOM   1016 C  CE  . LYS A 1 145  ? 54.371 61.610  27.373  1.00 29.97 ? 145  LYS A CE  1 
ATOM   1017 N  NZ  . LYS A 1 145  ? 55.451 61.573  28.401  1.00 32.19 ? 145  LYS A NZ  1 
ATOM   1018 N  N   . LYS A 1 146  ? 57.683 58.893  21.873  1.00 16.74 ? 146  LYS A N   1 
ATOM   1019 C  CA  . LYS A 1 146  ? 57.656 58.132  20.616  1.00 16.67 ? 146  LYS A CA  1 
ATOM   1020 C  C   . LYS A 1 146  ? 57.724 56.653  20.973  1.00 16.65 ? 146  LYS A C   1 
ATOM   1021 O  O   . LYS A 1 146  ? 57.018 55.822  20.400  1.00 16.78 ? 146  LYS A O   1 
ATOM   1022 C  CB  . LYS A 1 146  ? 58.833 58.482  19.704  1.00 16.13 ? 146  LYS A CB  1 
ATOM   1023 C  CG  . LYS A 1 146  ? 58.724 59.810  19.000  1.00 16.17 ? 146  LYS A CG  1 
ATOM   1024 C  CD  . LYS A 1 146  ? 59.973 60.030  18.135  1.00 16.88 ? 146  LYS A CD  1 
ATOM   1025 C  CE  A LYS A 1 146  ? 59.810 61.247  17.226  0.50 17.51 ? 146  LYS A CE  1 
ATOM   1026 C  CE  B LYS A 1 146  ? 59.862 61.036  17.043  0.50 17.44 ? 146  LYS A CE  1 
ATOM   1027 N  NZ  A LYS A 1 146  ? 61.066 61.566  16.501  0.50 18.49 ? 146  LYS A NZ  1 
ATOM   1028 N  NZ  B LYS A 1 146  ? 59.851 62.415  17.579  0.50 18.43 ? 146  LYS A NZ  1 
ATOM   1029 N  N   . LEU A 1 147  ? 58.578 56.306  21.929  1.00 17.25 ? 147  LEU A N   1 
ATOM   1030 C  CA  . LEU A 1 147  ? 58.699 54.909  22.341  1.00 16.96 ? 147  LEU A CA  1 
ATOM   1031 C  C   . LEU A 1 147  ? 57.408 54.405  23.034  1.00 16.40 ? 147  LEU A C   1 
ATOM   1032 O  O   . LEU A 1 147  ? 56.981 53.272  22.782  1.00 16.26 ? 147  LEU A O   1 
ATOM   1033 C  CB  . LEU A 1 147  ? 59.902 54.757  23.293  1.00 18.15 ? 147  LEU A CB  1 
ATOM   1034 C  CG  . LEU A 1 147  ? 61.263 54.845  22.612  1.00 20.16 ? 147  LEU A CG  1 
ATOM   1035 C  CD1 . LEU A 1 147  ? 62.317 54.953  23.714  1.00 21.76 ? 147  LEU A CD1 1 
ATOM   1036 C  CD2 . LEU A 1 147  ? 61.552 53.597  21.766  1.00 21.28 ? 147  LEU A CD2 1 
ATOM   1037 N  N   . GLN A 1 148  ? 56.797 55.222  23.886  1.00 15.74 ? 148  GLN A N   1 
ATOM   1038 C  CA  . GLN A 1 148  ? 55.540 54.819  24.512  1.00 17.34 ? 148  GLN A CA  1 
ATOM   1039 C  C   . GLN A 1 148  ? 54.469 54.593  23.413  1.00 16.41 ? 148  GLN A C   1 
ATOM   1040 O  O   . GLN A 1 148  ? 53.700 53.659  23.489  1.00 16.64 ? 148  GLN A O   1 
ATOM   1041 C  CB  . GLN A 1 148  ? 55.037 55.895  25.456  1.00 19.52 ? 148  GLN A CB  1 
ATOM   1042 C  CG  . GLN A 1 148  ? 55.800 55.967  26.740  1.00 23.84 ? 148  GLN A CG  1 
ATOM   1043 C  CD  . GLN A 1 148  ? 55.076 56.835  27.750  1.00 26.37 ? 148  GLN A CD  1 
ATOM   1044 O  OE1 . GLN A 1 148  ? 55.307 56.713  28.972  1.00 30.03 ? 148  GLN A OE1 1 
ATOM   1045 N  NE2 . GLN A 1 148  ? 54.199 57.722  27.256  1.00 27.71 ? 148  GLN A NE2 1 
ATOM   1046 N  N   . MET A 1 149  ? 54.454 55.479  22.425  1.00 15.15 ? 149  MET A N   1 
ATOM   1047 C  CA  . MET A 1 149  ? 53.474 55.353  21.342  1.00 14.05 ? 149  MET A CA  1 
ATOM   1048 C  C   . MET A 1 149  ? 53.709 54.067  20.570  1.00 14.01 ? 149  MET A C   1 
ATOM   1049 O  O   . MET A 1 149  ? 52.753 53.330  20.264  1.00 13.90 ? 149  MET A O   1 
ATOM   1050 C  CB  . MET A 1 149  ? 53.589 56.559  20.408  1.00 14.42 ? 149  MET A CB  1 
ATOM   1051 C  CG  . MET A 1 149  ? 52.554 56.574  19.297  1.00 14.34 ? 149  MET A CG  1 
ATOM   1052 S  SD  . MET A 1 149  ? 50.859 56.769  19.929  1.00 15.46 ? 149  MET A SD  1 
ATOM   1053 C  CE  . MET A 1 149  ? 50.642 58.506  20.066  1.00 18.08 ? 149  MET A CE  1 
ATOM   1054 N  N   . LYS A 1 150  ? 54.961 53.785  20.211  1.00 14.40 ? 150  LYS A N   1 
ATOM   1055 C  CA  . LYS A 1 150  ? 55.232 52.564  19.467  1.00 16.00 ? 150  LYS A CA  1 
ATOM   1056 C  C   . LYS A 1 150  ? 54.773 51.344  20.255  1.00 15.54 ? 150  LYS A C   1 
ATOM   1057 O  O   . LYS A 1 150  ? 54.284 50.362  19.657  1.00 15.83 ? 150  LYS A O   1 
ATOM   1058 C  CB  . LYS A 1 150  ? 56.720 52.428  19.119  1.00 17.29 ? 150  LYS A CB  1 
ATOM   1059 C  CG  . LYS A 1 150  ? 57.125 53.369  18.016  1.00 19.99 ? 150  LYS A CG  1 
ATOM   1060 C  CD  . LYS A 1 150  ? 58.490 53.038  17.430  1.00 24.27 ? 150  LYS A CD  1 
ATOM   1061 C  CE  . LYS A 1 150  ? 59.537 53.749  18.179  1.00 26.13 ? 150  LYS A CE  1 
ATOM   1062 N  NZ  . LYS A 1 150  ? 60.722 53.920  17.296  1.00 28.18 ? 150  LYS A NZ  1 
ATOM   1063 N  N   . SER A 1 151  ? 54.886 51.411  21.580  1.00 15.64 ? 151  SER A N   1 
ATOM   1064 C  CA  . SER A 1 151  ? 54.497 50.306  22.444  1.00 16.02 ? 151  SER A CA  1 
ATOM   1065 C  C   . SER A 1 151  ? 52.986 50.054  22.457  1.00 15.29 ? 151  SER A C   1 
ATOM   1066 O  O   . SER A 1 151  ? 52.564 48.902  22.400  1.00 16.15 ? 151  SER A O   1 
ATOM   1067 C  CB  . SER A 1 151  ? 55.017 50.542  23.874  1.00 16.68 ? 151  SER A CB  1 
ATOM   1068 O  OG  A SER A 1 151  ? 54.273 51.552  24.522  0.50 17.96 ? 151  SER A OG  1 
ATOM   1069 O  OG  B SER A 1 151  ? 54.817 49.304  24.600  0.50 17.92 ? 151  SER A OG  1 
ATOM   1070 N  N   . ILE A 1 152  ? 52.166 51.107  22.511  1.00 14.81 ? 152  ILE A N   1 
ATOM   1071 C  CA  . ILE A 1 152  ? 50.725 50.868  22.507  1.00 13.53 ? 152  ILE A CA  1 
ATOM   1072 C  C   . ILE A 1 152  ? 50.216 50.453  21.111  1.00 12.60 ? 152  ILE A C   1 
ATOM   1073 O  O   . ILE A 1 152  ? 49.114 49.905  21.011  1.00 13.43 ? 152  ILE A O   1 
ATOM   1074 C  CB  . ILE A 1 152  ? 49.851 52.013  23.090  1.00 14.12 ? 152  ILE A CB  1 
ATOM   1075 C  CG1 . ILE A 1 152  ? 50.096 53.324  22.378  1.00 14.40 ? 152  ILE A CG1 1 
ATOM   1076 C  CG2 . ILE A 1 152  ? 50.182 52.209  24.597  1.00 15.48 ? 152  ILE A CG2 1 
ATOM   1077 C  CD1 . ILE A 1 152  ? 49.084 54.437  22.742  1.00 15.15 ? 152  ILE A CD1 1 
ATOM   1078 N  N   . VAL A 1 153  ? 50.998 50.718  20.068  1.00 12.51 ? 153  VAL A N   1 
ATOM   1079 C  CA  . VAL A 1 153  ? 50.641 50.245  18.727  1.00 13.01 ? 153  VAL A CA  1 
ATOM   1080 C  C   . VAL A 1 153  ? 51.064 48.785  18.602  1.00 14.07 ? 153  VAL A C   1 
ATOM   1081 O  O   . VAL A 1 153  ? 50.277 47.921  18.204  1.00 14.74 ? 153  VAL A O   1 
ATOM   1082 C  CB  . VAL A 1 153  ? 51.305 51.128  17.660  1.00 13.22 ? 153  VAL A CB  1 
ATOM   1083 C  CG1 . VAL A 1 153  ? 51.117 50.471  16.266  1.00 14.60 ? 153  VAL A CG1 1 
ATOM   1084 C  CG2 . VAL A 1 153  ? 50.724 52.500  17.711  1.00 12.77 ? 153  VAL A CG2 1 
ATOM   1085 N  N   . LYS A 1 154  ? 52.293 48.477  19.046  1.00 14.38 ? 154  LYS A N   1 
ATOM   1086 C  CA  . LYS A 1 154  ? 52.750 47.103  18.972  1.00 15.97 ? 154  LYS A CA  1 
ATOM   1087 C  C   . LYS A 1 154  ? 51.898 46.126  19.786  1.00 15.95 ? 154  LYS A C   1 
ATOM   1088 O  O   . LYS A 1 154  ? 51.676 44.993  19.347  1.00 17.69 ? 154  LYS A O   1 
ATOM   1089 C  CB  . LYS A 1 154  ? 54.209 47.033  19.416  1.00 17.27 ? 154  LYS A CB  1 
ATOM   1090 C  CG  . LYS A 1 154  ? 54.829 45.674  19.123  1.00 21.94 ? 154  LYS A CG  1 
ATOM   1091 C  CD  . LYS A 1 154  ? 56.291 45.695  19.465  1.00 25.06 ? 154  LYS A CD  1 
ATOM   1092 C  CE  . LYS A 1 154  ? 56.884 44.278  19.341  1.00 27.60 ? 154  LYS A CE  1 
ATOM   1093 N  NZ  . LYS A 1 154  ? 58.065 44.124  20.253  1.00 29.97 ? 154  LYS A NZ  1 
ATOM   1094 N  N   . ASN A 1 155  ? 51.392 46.549  20.952  1.00 15.89 ? 155  ASN A N   1 
ATOM   1095 C  CA  . ASN A 1 155  ? 50.546 45.666  21.792  1.00 15.65 ? 155  ASN A CA  1 
ATOM   1096 C  C   A ASN A 1 155  ? 49.079 45.604  21.340  0.50 15.69 ? 155  ASN A C   1 
ATOM   1097 C  C   B ASN A 1 155  ? 49.084 45.773  21.461  0.50 16.84 ? 155  ASN A C   1 
ATOM   1098 O  O   A ASN A 1 155  ? 48.285 44.844  21.889  0.50 15.37 ? 155  ASN A O   1 
ATOM   1099 O  O   B ASN A 1 155  ? 48.272 45.290  22.243  0.50 16.82 ? 155  ASN A O   1 
ATOM   1100 C  CB  A ASN A 1 155  ? 50.626 46.038  23.305  0.50 15.73 ? 155  ASN A CB  1 
ATOM   1101 C  CB  B ASN A 1 155  ? 51.116 45.893  23.158  0.50 19.10 ? 155  ASN A CB  1 
ATOM   1102 C  CG  A ASN A 1 155  ? 49.823 47.289  23.696  0.50 14.87 ? 155  ASN A CG  1 
ATOM   1103 C  CG  B ASN A 1 155  ? 52.640 45.534  23.280  0.50 20.13 ? 155  ASN A CG  1 
ATOM   1104 O  OD1 A ASN A 1 155  ? 49.128 47.866  22.895  0.50 14.30 ? 155  ASN A OD1 1 
ATOM   1105 O  OD1 B ASN A 1 155  ? 53.033 44.372  23.052  0.50 21.97 ? 155  ASN A OD1 1 
ATOM   1106 N  ND2 A ASN A 1 155  ? 49.922 47.693  24.969  0.50 15.11 ? 155  ASN A ND2 1 
ATOM   1107 N  ND2 B ASN A 1 155  ? 53.491 46.530  23.591  0.50 21.38 ? 155  ASN A ND2 1 
ATOM   1108 N  N   . GLY A 1 156  ? 48.738 46.374  20.315  1.00 15.41 ? 156  GLY A N   1 
ATOM   1109 C  CA  . GLY A 1 156  ? 47.350 46.395  19.819  1.00 15.13 ? 156  GLY A CA  1 
ATOM   1110 C  C   . GLY A 1 156  ? 46.306 47.301  20.429  1.00 14.77 ? 156  GLY A C   1 
ATOM   1111 O  O   . GLY A 1 156  ? 45.143 47.204  20.056  1.00 15.74 ? 156  GLY A O   1 
ATOM   1112 N  N   . GLN A 1 157  ? 46.684 48.178  21.352  1.00 12.05 ? 157  GLN A N   1 
ATOM   1113 C  CA  . GLN A 1 157  ? 45.694 49.027  21.938  1.00 10.79 ? 157  GLN A CA  1 
ATOM   1114 C  C   . GLN A 1 157  ? 45.312 50.151  20.974  1.00 9.96  ? 157  GLN A C   1 
ATOM   1115 O  O   . GLN A 1 157  ? 44.146 50.512  20.916  1.00 11.12 ? 157  GLN A O   1 
ATOM   1116 C  CB  . GLN A 1 157  ? 46.230 49.646  23.224  1.00 10.60 ? 157  GLN A CB  1 
ATOM   1117 C  CG  . GLN A 1 157  ? 46.193 48.687  24.417  1.00 11.85 ? 157  GLN A CG  1 
ATOM   1118 C  CD  . GLN A 1 157  ? 46.498 49.482  25.677  1.00 11.70 ? 157  GLN A CD  1 
ATOM   1119 O  OE1 . GLN A 1 157  ? 45.631 50.158  26.250  1.00 14.56 ? 157  GLN A OE1 1 
ATOM   1120 N  NE2 . GLN A 1 157  ? 47.749 49.454  26.062  1.00 11.96 ? 157  GLN A NE2 1 
ATOM   1121 N  N   . LEU A 1 158  ? 46.324 50.740  20.309  1.00 9.98  ? 158  LEU A N   1 
ATOM   1122 C  CA  . LEU A 1 158  ? 46.067 51.801  19.325  1.00 10.18 ? 158  LEU A CA  1 
ATOM   1123 C  C   . LEU A 1 158  ? 46.268 51.117  17.959  1.00 9.68  ? 158  LEU A C   1 
ATOM   1124 O  O   . LEU A 1 158  ? 47.336 50.568  17.692  1.00 11.08 ? 158  LEU A O   1 
ATOM   1125 C  CB  . LEU A 1 158  ? 47.065 52.952  19.484  1.00 11.88 ? 158  LEU A CB  1 
ATOM   1126 C  CG  . LEU A 1 158  ? 47.010 53.996  18.374  1.00 13.46 ? 158  LEU A CG  1 
ATOM   1127 C  CD1 . LEU A 1 158  ? 45.718 54.642  18.424  1.00 15.34 ? 158  LEU A CD1 1 
ATOM   1128 C  CD2 . LEU A 1 158  ? 48.144 55.045  18.594  1.00 15.07 ? 158  LEU A CD2 1 
ATOM   1129 N  N   . GLU A 1 159  ? 45.197 51.094  17.156  1.00 9.05  ? 159  GLU A N   1 
ATOM   1130 C  CA  . GLU A 1 159  ? 45.272 50.434  15.846  1.00 9.01  ? 159  GLU A CA  1 
ATOM   1131 C  C   . GLU A 1 159  ? 44.922 51.404  14.732  1.00 8.19  ? 159  GLU A C   1 
ATOM   1132 O  O   . GLU A 1 159  ? 43.889 52.084  14.759  1.00 9.10  ? 159  GLU A O   1 
ATOM   1133 C  CB  . GLU A 1 159  ? 44.288 49.280  15.835  1.00 9.38  ? 159  GLU A CB  1 
ATOM   1134 C  CG  . GLU A 1 159  ? 44.234 48.538  14.501  1.00 10.02 ? 159  GLU A CG  1 
ATOM   1135 C  CD  . GLU A 1 159  ? 43.234 47.390  14.564  1.00 12.57 ? 159  GLU A CD  1 
ATOM   1136 O  OE1 . GLU A 1 159  ? 43.524 46.365  15.288  1.00 11.97 ? 159  GLU A OE1 1 
ATOM   1137 O  OE2 . GLU A 1 159  ? 42.171 47.530  13.917  1.00 10.93 ? 159  GLU A OE2 1 
ATOM   1138 N  N   . PHE A 1 160  ? 45.784 51.412  13.727  1.00 8.29  ? 160  PHE A N   1 
ATOM   1139 C  CA  . PHE A 1 160  ? 45.533 52.248  12.534  1.00 7.54  ? 160  PHE A CA  1 
ATOM   1140 C  C   . PHE A 1 160  ? 44.593 51.521  11.588  1.00 7.71  ? 160  PHE A C   1 
ATOM   1141 O  O   . PHE A 1 160  ? 44.736 50.314  11.340  1.00 8.31  ? 160  PHE A O   1 
ATOM   1142 C  CB  . PHE A 1 160  ? 46.885 52.560  11.868  1.00 8.49  ? 160  PHE A CB  1 
ATOM   1143 C  CG  . PHE A 1 160  ? 47.766 53.412  12.726  1.00 8.56  ? 160  PHE A CG  1 
ATOM   1144 C  CD1 . PHE A 1 160  ? 47.464 54.762  12.909  1.00 9.57  ? 160  PHE A CD1 1 
ATOM   1145 C  CD2 . PHE A 1 160  ? 48.846 52.836  13.415  1.00 9.42  ? 160  PHE A CD2 1 
ATOM   1146 C  CE1 . PHE A 1 160  ? 48.249 55.549  13.780  1.00 10.39 ? 160  PHE A CE1 1 
ATOM   1147 C  CE2 . PHE A 1 160  ? 49.616 53.607  14.263  1.00 10.59 ? 160  PHE A CE2 1 
ATOM   1148 C  CZ  . PHE A 1 160  ? 49.334 54.934  14.445  1.00 10.84 ? 160  PHE A CZ  1 
ATOM   1149 N  N   . VAL A 1 161  ? 43.607 52.274  11.128  1.00 7.75  ? 161  VAL A N   1 
ATOM   1150 C  CA  . VAL A 1 161  ? 42.627 51.757  10.166  1.00 7.76  ? 161  VAL A CA  1 
ATOM   1151 C  C   . VAL A 1 161  ? 42.826 52.564  8.892   1.00 7.65  ? 161  VAL A C   1 
ATOM   1152 O  O   . VAL A 1 161  ? 42.920 53.795  8.893   1.00 8.25  ? 161  VAL A O   1 
ATOM   1153 C  CB  . VAL A 1 161  ? 41.168 51.849  10.730  1.00 6.94  ? 161  VAL A CB  1 
ATOM   1154 C  CG1 . VAL A 1 161  ? 41.034 50.846  11.917  1.00 8.64  ? 161  VAL A CG1 1 
ATOM   1155 C  CG2 . VAL A 1 161  ? 40.825 53.242  11.202  1.00 7.89  ? 161  VAL A CG2 1 
ATOM   1156 N  N   . THR A 1 162  ? 42.864 51.789  7.799   1.00 7.67  ? 162  THR A N   1 
ATOM   1157 C  CA  . THR A 1 162  ? 43.185 52.259  6.409   1.00 8.10  ? 162  THR A CA  1 
ATOM   1158 C  C   . THR A 1 162  ? 44.648 52.715  6.350   1.00 7.41  ? 162  THR A C   1 
ATOM   1159 O  O   . THR A 1 162  ? 45.459 52.139  5.614   1.00 8.34  ? 162  THR A O   1 
ATOM   1160 C  CB  . THR A 1 162  ? 42.326 53.391  5.913   1.00 7.80  ? 162  THR A CB  1 
ATOM   1161 O  OG1 . THR A 1 162  ? 40.934 53.061  6.005   1.00 9.12  ? 162  THR A OG1 1 
ATOM   1162 C  CG2 . THR A 1 162  ? 42.646 53.629  4.415   1.00 9.28  ? 162  THR A CG2 1 
ATOM   1163 N  N   . GLY A 1 163  ? 44.983 53.778  7.078   1.00 7.51  ? 163  GLY A N   1 
ATOM   1164 C  CA  . GLY A 1 163  ? 46.370 54.238  7.076   1.00 7.74  ? 163  GLY A CA  1 
ATOM   1165 C  C   . GLY A 1 163  ? 46.694 55.194  5.960   1.00 7.26  ? 163  GLY A C   1 
ATOM   1166 O  O   . GLY A 1 163  ? 47.867 55.384  5.648   1.00 7.84  ? 163  GLY A O   1 
ATOM   1167 N  N   . GLY A 1 164  ? 45.664 55.764  5.318   1.00 6.73  ? 164  GLY A N   1 
ATOM   1168 C  CA  . GLY A 1 164  ? 45.970 56.797  4.299   1.00 7.07  ? 164  GLY A CA  1 
ATOM   1169 C  C   . GLY A 1 164  ? 46.272 58.133  4.949   1.00 6.59  ? 164  GLY A C   1 
ATOM   1170 O  O   . GLY A 1 164  ? 45.991 58.351  6.147   1.00 7.03  ? 164  GLY A O   1 
ATOM   1171 N  N   . TRP A 1 165  ? 46.877 59.035  4.186   1.00 6.44  ? 165  TRP A N   1 
ATOM   1172 C  CA  . TRP A 1 165  ? 47.119 60.384  4.682   1.00 6.37  ? 165  TRP A CA  1 
ATOM   1173 C  C   . TRP A 1 165  ? 45.788 60.999  5.161   1.00 6.39  ? 165  TRP A C   1 
ATOM   1174 O  O   . TRP A 1 165  ? 45.761 61.753  6.171   1.00 6.99  ? 165  TRP A O   1 
ATOM   1175 C  CB  . TRP A 1 165  ? 47.727 61.190  3.536   1.00 7.01  ? 165  TRP A CB  1 
ATOM   1176 C  CG  . TRP A 1 165  ? 48.556 62.302  3.986   1.00 7.29  ? 165  TRP A CG  1 
ATOM   1177 C  CD1 . TRP A 1 165  ? 48.364 63.610  3.659   1.00 8.40  ? 165  TRP A CD1 1 
ATOM   1178 C  CD2 . TRP A 1 165  ? 49.762 62.248  4.793   1.00 8.28  ? 165  TRP A CD2 1 
ATOM   1179 N  NE1 . TRP A 1 165  ? 49.387 64.397  4.216   1.00 9.75  ? 165  TRP A NE1 1 
ATOM   1180 C  CE2 . TRP A 1 165  ? 50.229 63.581  4.912   1.00 8.39  ? 165  TRP A CE2 1 
ATOM   1181 C  CE3 . TRP A 1 165  ? 50.472 61.203  5.391   1.00 8.63  ? 165  TRP A CE3 1 
ATOM   1182 C  CZ2 . TRP A 1 165  ? 51.427 63.902  5.665   1.00 10.90 ? 165  TRP A CZ2 1 
ATOM   1183 C  CZ3 . TRP A 1 165  ? 51.651 61.511  6.108   1.00 11.06 ? 165  TRP A CZ3 1 
ATOM   1184 C  CH2 . TRP A 1 165  ? 52.095 62.860  6.223   1.00 11.78 ? 165  TRP A CH2 1 
ATOM   1185 N  N   . VAL A 1 166  ? 44.708 60.707  4.441   1.00 6.15  ? 166  VAL A N   1 
ATOM   1186 C  CA  . VAL A 1 166  ? 43.369 61.207  4.763   1.00 6.38  ? 166  VAL A CA  1 
ATOM   1187 C  C   . VAL A 1 166  ? 42.365 60.054  4.582   1.00 6.45  ? 166  VAL A C   1 
ATOM   1188 O  O   . VAL A 1 166  ? 42.756 58.924  4.318   1.00 7.52  ? 166  VAL A O   1 
ATOM   1189 C  CB  . VAL A 1 166  ? 42.951 62.374  3.828   1.00 5.98  ? 166  VAL A CB  1 
ATOM   1190 C  CG1 . VAL A 1 166  ? 43.960 63.534  3.955   1.00 7.33  ? 166  VAL A CG1 1 
ATOM   1191 C  CG2 . VAL A 1 166  ? 42.832 61.880  2.361   1.00 7.25  ? 166  VAL A CG2 1 
ATOM   1192 N  N   . MET A 1 167  ? 41.061 60.350  4.816   1.00 7.76  ? 167  MET A N   1 
ATOM   1193 C  CA  . MET A 1 167  ? 39.943 59.400  4.507   1.00 6.36  ? 167  MET A CA  1 
ATOM   1194 C  C   . MET A 1 167  ? 39.413 60.154  3.255   1.00 6.74  ? 167  MET A C   1 
ATOM   1195 O  O   . MET A 1 167  ? 38.635 61.112  3.344   1.00 7.01  ? 167  MET A O   1 
ATOM   1196 C  CB  . MET A 1 167  ? 38.969 59.403  5.660   1.00 6.83  ? 167  MET A CB  1 
ATOM   1197 C  CG  . MET A 1 167  ? 37.683 58.633  5.333   1.00 6.51  ? 167  MET A CG  1 
ATOM   1198 S  SD  . MET A 1 167  ? 36.520 58.721  6.698   1.00 7.82  ? 167  MET A SD  1 
ATOM   1199 C  CE  . MET A 1 167  ? 37.488 57.959  8.055   1.00 8.90  ? 167  MET A CE  1 
ATOM   1200 N  N   . PRO A 1 168  ? 39.800 59.694  2.053   1.00 6.07  ? 168  PRO A N   1 
ATOM   1201 C  CA  . PRO A 1 168  ? 39.414 60.445  0.871   1.00 6.72  ? 168  PRO A CA  1 
ATOM   1202 C  C   . PRO A 1 168  ? 37.995 60.462  0.409   1.00 5.63  ? 168  PRO A C   1 
ATOM   1203 O  O   . PRO A 1 168  ? 37.245 59.540  0.633   1.00 6.64  ? 168  PRO A O   1 
ATOM   1204 C  CB  . PRO A 1 168  ? 40.318 59.848  -0.245  1.00 6.61  ? 168  PRO A CB  1 
ATOM   1205 C  CG  . PRO A 1 168  ? 40.446 58.422  0.168   1.00 7.46  ? 168  PRO A CG  1 
ATOM   1206 C  CD  . PRO A 1 168  ? 40.630 58.516  1.715   1.00 6.37  ? 168  PRO A CD  1 
ATOM   1207 N  N   . ASP A 1 169  ? 37.651 61.551  -0.264  1.00 6.69  ? 169  ASP A N   1 
ATOM   1208 C  CA  . ASP A 1 169  ? 36.406 61.577  -1.044  1.00 6.12  ? 169  ASP A CA  1 
ATOM   1209 C  C   . ASP A 1 169  ? 36.543 60.401  -2.025  1.00 6.25  ? 169  ASP A C   1 
ATOM   1210 O  O   . ASP A 1 169  ? 37.643 60.070  -2.500  1.00 6.48  ? 169  ASP A O   1 
ATOM   1211 C  CB  . ASP A 1 169  ? 36.389 62.871  -1.860  1.00 6.32  ? 169  ASP A CB  1 
ATOM   1212 C  CG  . ASP A 1 169  ? 35.217 62.931  -2.812  1.00 6.58  ? 169  ASP A CG  1 
ATOM   1213 O  OD1 . ASP A 1 169  ? 34.135 62.411  -2.501  1.00 7.52  ? 169  ASP A OD1 1 
ATOM   1214 O  OD2 . ASP A 1 169  ? 35.368 63.536  -3.903  1.00 8.68  ? 169  ASP A OD2 1 
ATOM   1215 N  N   . GLU A 1 170  ? 35.423 59.811  -2.364  1.00 5.88  ? 170  GLU A N   1 
ATOM   1216 C  CA  . GLU A 1 170  ? 35.386 58.675  -3.328  1.00 6.21  ? 170  GLU A CA  1 
ATOM   1217 C  C   . GLU A 1 170  ? 34.659 59.041  -4.618  1.00 5.97  ? 170  GLU A C   1 
ATOM   1218 O  O   . GLU A 1 170  ? 34.680 58.241  -5.558  1.00 6.45  ? 170  GLU A O   1 
ATOM   1219 C  CB  . GLU A 1 170  ? 34.765 57.444  -2.643  1.00 6.90  ? 170  GLU A CB  1 
ATOM   1220 C  CG  . GLU A 1 170  ? 35.548 57.042  -1.362  1.00 7.04  ? 170  GLU A CG  1 
ATOM   1221 C  CD  . GLU A 1 170  ? 34.993 55.802  -0.703  1.00 8.06  ? 170  GLU A CD  1 
ATOM   1222 O  OE1 . GLU A 1 170  ? 34.229 55.037  -1.324  1.00 7.94  ? 170  GLU A OE1 1 
ATOM   1223 O  OE2 . GLU A 1 170  ? 35.380 55.554  0.458   1.00 8.72  ? 170  GLU A OE2 1 
ATOM   1224 N  N   . ALA A 1 171  ? 34.084 60.247  -4.699  1.00 6.39  ? 171  ALA A N   1 
ATOM   1225 C  CA  . ALA A 1 171  ? 33.355 60.663  -5.919  1.00 5.61  ? 171  ALA A CA  1 
ATOM   1226 C  C   . ALA A 1 171  ? 34.212 61.419  -6.912  1.00 6.03  ? 171  ALA A C   1 
ATOM   1227 O  O   . ALA A 1 171  ? 34.239 61.085  -8.081  1.00 6.86  ? 171  ALA A O   1 
ATOM   1228 C  CB  . ALA A 1 171  ? 32.157 61.526  -5.553  1.00 6.72  ? 171  ALA A CB  1 
ATOM   1229 N  N   . ASN A 1 172  ? 34.912 62.441  -6.439  1.00 5.97  ? 172  ASN A N   1 
ATOM   1230 C  CA  . ASN A 1 172  ? 35.656 63.309  -7.358  1.00 6.09  ? 172  ASN A CA  1 
ATOM   1231 C  C   . ASN A 1 172  ? 37.112 62.925  -7.494  1.00 6.11  ? 172  ASN A C   1 
ATOM   1232 O  O   . ASN A 1 172  ? 37.793 63.368  -8.431  1.00 6.38  ? 172  ASN A O   1 
ATOM   1233 C  CB  . ASN A 1 172  ? 35.636 64.739  -6.795  1.00 6.34  ? 172  ASN A CB  1 
ATOM   1234 C  CG  . ASN A 1 172  ? 34.234 65.284  -6.656  1.00 7.48  ? 172  ASN A CG  1 
ATOM   1235 O  OD1 . ASN A 1 172  ? 33.565 65.495  -7.650  1.00 9.24  ? 172  ASN A OD1 1 
ATOM   1236 N  ND2 . ASN A 1 172  ? 33.802 65.546  -5.429  1.00 8.50  ? 172  ASN A ND2 1 
ATOM   1237 N  N   . SER A 1 173  ? 37.612 62.120  -6.582  1.00 5.82  ? 173  SER A N   1 
ATOM   1238 C  CA  . SER A 1 173  ? 39.056 61.779  -6.562  1.00 6.13  ? 173  SER A CA  1 
ATOM   1239 C  C   . SER A 1 173  ? 39.434 60.874  -7.702  1.00 6.16  ? 173  SER A C   1 
ATOM   1240 O  O   . SER A 1 173  ? 38.721 59.951  -8.094  1.00 6.86  ? 173  SER A O   1 
ATOM   1241 C  CB  . SER A 1 173  ? 39.373 61.120  -5.218  1.00 6.38  ? 173  SER A CB  1 
ATOM   1242 O  OG  . SER A 1 173  ? 38.478 59.988  -5.033  1.00 6.92  ? 173  SER A OG  1 
ATOM   1243 N  N   . HIS A 1 174  ? 40.608 61.155  -8.246  1.00 5.71  ? 174  HIS A N   1 
ATOM   1244 C  CA  . HIS A 1 174  ? 41.142 60.263  -9.269  1.00 5.29  ? 174  HIS A CA  1 
ATOM   1245 C  C   . HIS A 1 174  ? 41.779 59.072  -8.584  1.00 5.05  ? 174  HIS A C   1 
ATOM   1246 O  O   . HIS A 1 174  ? 42.448 59.252  -7.562  1.00 5.40  ? 174  HIS A O   1 
ATOM   1247 C  CB  . HIS A 1 174  ? 42.188 60.988  -10.122 1.00 6.27  ? 174  HIS A CB  1 
ATOM   1248 C  CG  . HIS A 1 174  ? 42.431 60.311  -11.427 1.00 6.05  ? 174  HIS A CG  1 
ATOM   1249 N  ND1 . HIS A 1 174  ? 43.139 59.134  -11.534 1.00 6.87  ? 174  HIS A ND1 1 
ATOM   1250 C  CD2 . HIS A 1 174  ? 41.980 60.615  -12.664 1.00 6.98  ? 174  HIS A CD2 1 
ATOM   1251 C  CE1 . HIS A 1 174  ? 43.114 58.738  -12.792 1.00 7.03  ? 174  HIS A CE1 1 
ATOM   1252 N  NE2 . HIS A 1 174  ? 42.416 59.616  -13.492 1.00 7.50  ? 174  HIS A NE2 1 
ATOM   1253 N  N   . TRP A 1 175  ? 41.641 57.865  -9.129  1.00 5.46  ? 175  TRP A N   1 
ATOM   1254 C  CA  . TRP A 1 175  ? 42.256 56.698  -8.479  1.00 4.94  ? 175  TRP A CA  1 
ATOM   1255 C  C   . TRP A 1 175  ? 43.755 56.857  -8.285  1.00 5.60  ? 175  TRP A C   1 
ATOM   1256 O  O   . TRP A 1 175  ? 44.287 56.352  -7.299  1.00 5.88  ? 175  TRP A O   1 
ATOM   1257 C  CB  . TRP A 1 175  ? 41.944 55.414  -9.295  1.00 6.17  ? 175  TRP A CB  1 
ATOM   1258 C  CG  . TRP A 1 175  ? 42.795 55.196  -10.566 1.00 6.05  ? 175  TRP A CG  1 
ATOM   1259 C  CD1 . TRP A 1 175  ? 42.440 55.573  -11.854 1.00 6.18  ? 175  TRP A CD1 1 
ATOM   1260 C  CD2 . TRP A 1 175  ? 44.101 54.580  -10.660 1.00 6.47  ? 175  TRP A CD2 1 
ATOM   1261 N  NE1 . TRP A 1 175  ? 43.490 55.203  -12.712 1.00 7.21  ? 175  TRP A NE1 1 
ATOM   1262 C  CE2 . TRP A 1 175  ? 44.489 54.608  -11.991 1.00 6.57  ? 175  TRP A CE2 1 
ATOM   1263 C  CE3 . TRP A 1 175  ? 44.972 53.997  -9.714  1.00 7.54  ? 175  TRP A CE3 1 
ATOM   1264 C  CZ2 . TRP A 1 175  ? 45.719 54.090  -12.423 1.00 7.54  ? 175  TRP A CZ2 1 
ATOM   1265 C  CZ3 . TRP A 1 175  ? 46.172 53.462  -10.150 1.00 8.04  ? 175  TRP A CZ3 1 
ATOM   1266 C  CH2 . TRP A 1 175  ? 46.535 53.519  -11.488 1.00 8.07  ? 175  TRP A CH2 1 
ATOM   1267 N  N   . ARG A 1 176  ? 44.423 57.572  -9.187  1.00 6.39  ? 176  ARG A N   1 
ATOM   1268 C  CA  . ARG A 1 176  ? 45.882 57.746  -8.985  1.00 5.65  ? 176  ARG A CA  1 
ATOM   1269 C  C   . ARG A 1 176  ? 46.150 58.518  -7.697  1.00 5.50  ? 176  ARG A C   1 
ATOM   1270 O  O   . ARG A 1 176  ? 47.139 58.223  -7.016  1.00 6.33  ? 176  ARG A O   1 
ATOM   1271 C  CB  . ARG A 1 176  ? 46.457 58.516  -10.206 1.00 7.13  ? 176  ARG A CB  1 
ATOM   1272 C  CG  . ARG A 1 176  ? 46.447 57.633  -11.455 1.00 8.26  ? 176  ARG A CG  1 
ATOM   1273 C  CD  . ARG A 1 176  ? 46.399 58.465  -12.744 1.00 9.72  ? 176  ARG A CD  1 
ATOM   1274 N  NE  . ARG A 1 176  ? 47.550 59.340  -12.867 1.00 9.12  ? 176  ARG A NE  1 
ATOM   1275 C  CZ  . ARG A 1 176  ? 47.675 60.180  -13.906 1.00 8.84  ? 176  ARG A CZ  1 
ATOM   1276 N  NH1 . ARG A 1 176  ? 46.727 60.218  -14.861 1.00 8.67  ? 176  ARG A NH1 1 
ATOM   1277 N  NH2 . ARG A 1 176  ? 48.639 61.104  -13.907 1.00 10.13 ? 176  ARG A NH2 1 
ATOM   1278 N  N   . ASN A 1 177  ? 45.297 59.495  -7.347  1.00 5.39  ? 177  ASN A N   1 
ATOM   1279 C  CA  . ASN A 1 177  ? 45.522 60.264  -6.113  1.00 5.63  ? 177  ASN A CA  1 
ATOM   1280 C  C   . ASN A 1 177  ? 45.015 59.506  -4.902  1.00 5.89  ? 177  ASN A C   1 
ATOM   1281 O  O   . ASN A 1 177  ? 45.529 59.721  -3.781  1.00 6.22  ? 177  ASN A O   1 
ATOM   1282 C  CB  . ASN A 1 177  ? 44.895 61.643  -6.212  1.00 6.04  ? 177  ASN A CB  1 
ATOM   1283 C  CG  . ASN A 1 177  ? 45.573 62.488  -7.251  1.00 6.85  ? 177  ASN A CG  1 
ATOM   1284 O  OD1 . ASN A 1 177  ? 46.753 62.296  -7.557  1.00 7.69  ? 177  ASN A OD1 1 
ATOM   1285 N  ND2 . ASN A 1 177  ? 44.855 63.463  -7.773  1.00 9.46  ? 177  ASN A ND2 1 
ATOM   1286 N  N   . VAL A 1 178  ? 44.014 58.637  -5.071  1.00 6.05  ? 178  VAL A N   1 
ATOM   1287 C  CA  . VAL A 1 178  ? 43.609 57.804  -3.927  1.00 5.77  ? 178  VAL A CA  1 
ATOM   1288 C  C   . VAL A 1 178  ? 44.811 56.906  -3.593  1.00 5.42  ? 178  VAL A C   1 
ATOM   1289 O  O   . VAL A 1 178  ? 45.141 56.746  -2.410  1.00 6.59  ? 178  VAL A O   1 
ATOM   1290 C  CB  . VAL A 1 178  ? 42.376 56.946  -4.309  1.00 5.65  ? 178  VAL A CB  1 
ATOM   1291 C  CG1 . VAL A 1 178  ? 42.080 55.941  -3.193  1.00 7.65  ? 178  VAL A CG1 1 
ATOM   1292 C  CG2 . VAL A 1 178  ? 41.132 57.840  -4.520  1.00 7.34  ? 178  VAL A CG2 1 
ATOM   1293 N  N   . LEU A 1 179  ? 45.457 56.319  -4.606  1.00 6.16  ? 179  LEU A N   1 
ATOM   1294 C  CA  . LEU A 1 179  ? 46.646 55.498  -4.335  1.00 6.24  ? 179  LEU A CA  1 
ATOM   1295 C  C   . LEU A 1 179  ? 47.768 56.335  -3.768  1.00 5.98  ? 179  LEU A C   1 
ATOM   1296 O  O   . LEU A 1 179  ? 48.438 55.888  -2.831  1.00 6.59  ? 179  LEU A O   1 
ATOM   1297 C  CB  . LEU A 1 179  ? 47.086 54.821  -5.656  1.00 6.71  ? 179  LEU A CB  1 
ATOM   1298 C  CG  . LEU A 1 179  ? 48.406 53.981  -5.489  1.00 6.98  ? 179  LEU A CG  1 
ATOM   1299 C  CD1 . LEU A 1 179  ? 48.270 52.833  -4.428  1.00 8.34  ? 179  LEU A CD1 1 
ATOM   1300 C  CD2 . LEU A 1 179  ? 48.810 53.433  -6.863  1.00 8.48  ? 179  LEU A CD2 1 
ATOM   1301 N  N   . LEU A 1 180  ? 47.947 57.553  -4.266  1.00 6.17  ? 180  LEU A N   1 
ATOM   1302 C  CA  . LEU A 1 180  ? 49.062 58.407  -3.763  1.00 6.52  ? 180  LEU A CA  1 
ATOM   1303 C  C   . LEU A 1 180  ? 48.885 58.644  -2.273  1.00 5.88  ? 180  LEU A C   1 
ATOM   1304 O  O   . LEU A 1 180  ? 49.836 58.456  -1.489  1.00 6.34  ? 180  LEU A O   1 
ATOM   1305 C  CB  . LEU A 1 180  ? 49.029 59.767  -4.506  1.00 6.33  ? 180  LEU A CB  1 
ATOM   1306 C  CG  . LEU A 1 180  ? 50.177 60.730  -4.167  1.00 7.97  ? 180  LEU A CG  1 
ATOM   1307 C  CD1 . LEU A 1 180  ? 51.446 60.214  -4.841  1.00 8.89  ? 180  LEU A CD1 1 
ATOM   1308 C  CD2 . LEU A 1 180  ? 49.853 62.147  -4.663  1.00 8.51  ? 180  LEU A CD2 1 
ATOM   1309 N  N   . GLN A 1 181  ? 47.684 59.045  -1.854  1.00 5.90  ? 181  GLN A N   1 
ATOM   1310 C  CA  . GLN A 1 181  ? 47.545 59.352  -0.425  1.00 5.96  ? 181  GLN A CA  1 
ATOM   1311 C  C   . GLN A 1 181  ? 47.584 58.106  0.447   1.00 6.04  ? 181  GLN A C   1 
ATOM   1312 O  O   . GLN A 1 181  ? 48.071 58.178  1.588   1.00 6.08  ? 181  GLN A O   1 
ATOM   1313 C  CB  . GLN A 1 181  ? 46.261 60.201  -0.215  1.00 6.20  ? 181  GLN A CB  1 
ATOM   1314 C  CG  . GLN A 1 181  ? 44.920 59.460  -0.438  1.00 6.10  ? 181  GLN A CG  1 
ATOM   1315 C  CD  . GLN A 1 181  ? 44.532 58.525  0.702   1.00 6.43  ? 181  GLN A CD  1 
ATOM   1316 O  OE1 . GLN A 1 181  ? 44.755 58.851  1.876   1.00 8.04  ? 181  GLN A OE1 1 
ATOM   1317 N  NE2 . GLN A 1 181  ? 43.909 57.406  0.357   1.00 7.30  ? 181  GLN A NE2 1 
ATOM   1318 N  N   . LEU A 1 182  ? 47.094 56.976  -0.054  1.00 6.59  ? 182  LEU A N   1 
ATOM   1319 C  CA  . LEU A 1 182  ? 47.166 55.728  0.696   1.00 6.44  ? 182  LEU A CA  1 
ATOM   1320 C  C   . LEU A 1 182  ? 48.638 55.384  0.861   1.00 6.34  ? 182  LEU A C   1 
ATOM   1321 O  O   . LEU A 1 182  ? 49.066 55.000  1.972   1.00 6.82  ? 182  LEU A O   1 
ATOM   1322 C  CB  . LEU A 1 182  ? 46.418 54.606  -0.065  1.00 6.46  ? 182  LEU A CB  1 
ATOM   1323 C  CG  . LEU A 1 182  ? 46.497 53.232  0.602   1.00 6.74  ? 182  LEU A CG  1 
ATOM   1324 C  CD1 . LEU A 1 182  ? 45.740 53.212  1.979   1.00 9.22  ? 182  LEU A CD1 1 
ATOM   1325 C  CD2 . LEU A 1 182  ? 45.892 52.161  -0.343  1.00 8.20  ? 182  LEU A CD2 1 
ATOM   1326 N  N   . THR A 1 183  ? 49.411 55.488  -0.203  1.00 6.26  ? 183  THR A N   1 
ATOM   1327 C  CA  . THR A 1 183  ? 50.825 55.178  -0.126  1.00 6.03  ? 183  THR A CA  1 
ATOM   1328 C  C   . THR A 1 183  ? 51.554 56.156  0.813   1.00 6.40  ? 183  THR A C   1 
ATOM   1329 O  O   . THR A 1 183  ? 52.455 55.720  1.577   1.00 6.74  ? 183  THR A O   1 
ATOM   1330 C  CB  . THR A 1 183  ? 51.435 55.243  -1.548  1.00 6.85  ? 183  THR A CB  1 
ATOM   1331 O  OG1 . THR A 1 183  ? 50.747 54.309  -2.390  1.00 6.95  ? 183  THR A OG1 1 
ATOM   1332 C  CG2 . THR A 1 183  ? 52.915 54.818  -1.504  1.00 8.11  ? 183  THR A CG2 1 
ATOM   1333 N  N   . GLU A 1 184  ? 51.193 57.431  0.821   1.00 6.21  ? 184  GLU A N   1 
ATOM   1334 C  CA  . GLU A 1 184  ? 51.897 58.392  1.679   1.00 7.26  ? 184  GLU A CA  1 
ATOM   1335 C  C   . GLU A 1 184  ? 51.677 57.998  3.128   1.00 7.26  ? 184  GLU A C   1 
ATOM   1336 O  O   . GLU A 1 184  ? 52.621 57.976  3.923   1.00 8.21  ? 184  GLU A O   1 
ATOM   1337 C  CB  . GLU A 1 184  ? 51.332 59.777  1.428   1.00 8.17  ? 184  GLU A CB  1 
ATOM   1338 C  CG  . GLU A 1 184  ? 52.191 60.940  1.928   1.00 9.80  ? 184  GLU A CG  1 
ATOM   1339 C  CD  . GLU A 1 184  ? 53.607 60.992  1.271   1.00 9.21  ? 184  GLU A CD  1 
ATOM   1340 O  OE1 . GLU A 1 184  ? 53.792 60.619  0.117   1.00 10.08 ? 184  GLU A OE1 1 
ATOM   1341 O  OE2 . GLU A 1 184  ? 54.512 61.440  1.971   1.00 12.23 ? 184  GLU A OE2 1 
ATOM   1342 N  N   . GLY A 1 185  ? 50.448 57.695  3.516   1.00 6.99  ? 185  GLY A N   1 
ATOM   1343 C  CA  . GLY A 1 185  ? 50.205 57.326  4.910   1.00 6.74  ? 185  GLY A CA  1 
ATOM   1344 C  C   . GLY A 1 185  ? 50.791 55.991  5.251   1.00 7.22  ? 185  GLY A C   1 
ATOM   1345 O  O   . GLY A 1 185  ? 51.384 55.865  6.344   1.00 7.90  ? 185  GLY A O   1 
ATOM   1346 N  N   . GLN A 1 186  ? 50.649 54.997  4.403   1.00 7.32  ? 186  GLN A N   1 
ATOM   1347 C  CA  . GLN A 1 186  ? 51.156 53.665  4.792   1.00 7.81  ? 186  GLN A CA  1 
ATOM   1348 C  C   . GLN A 1 186  ? 52.673 53.632  4.759   1.00 7.52  ? 186  GLN A C   1 
ATOM   1349 O  O   . GLN A 1 186  ? 53.270 52.877  5.542   1.00 7.82  ? 186  GLN A O   1 
ATOM   1350 C  CB  . GLN A 1 186  ? 50.581 52.553  3.901   1.00 6.46  ? 186  GLN A CB  1 
ATOM   1351 C  CG  . GLN A 1 186  ? 49.051 52.399  4.077   1.00 8.84  ? 186  GLN A CG  1 
ATOM   1352 C  CD  . GLN A 1 186  ? 48.637 50.994  3.851   1.00 8.56  ? 186  GLN A CD  1 
ATOM   1353 O  OE1 . GLN A 1 186  ? 49.270 50.301  3.073   1.00 11.56 ? 186  GLN A OE1 1 
ATOM   1354 N  NE2 . GLN A 1 186  ? 47.599 50.535  4.530   1.00 9.27  ? 186  GLN A NE2 1 
ATOM   1355 N  N   . THR A 1 187  ? 53.335 54.405  3.881   1.00 7.99  ? 187  THR A N   1 
ATOM   1356 C  CA  . THR A 1 187  ? 54.810 54.370  3.874   1.00 8.04  ? 187  THR A CA  1 
ATOM   1357 C  C   . THR A 1 187  ? 55.270 54.972  5.191   1.00 8.78  ? 187  THR A C   1 
ATOM   1358 O  O   . THR A 1 187  ? 56.215 54.437  5.796   1.00 8.98  ? 187  THR A O   1 
ATOM   1359 C  CB  . THR A 1 187  ? 55.294 55.136  2.683   1.00 7.03  ? 187  THR A CB  1 
ATOM   1360 O  OG1 . THR A 1 187  ? 54.832 54.462  1.502   1.00 8.63  ? 187  THR A OG1 1 
ATOM   1361 C  CG2 . THR A 1 187  ? 56.869 55.132  2.660   1.00 9.55  ? 187  THR A CG2 1 
ATOM   1362 N  N   . TRP A 1 188  ? 54.617 56.028  5.650   1.00 8.04  ? 188  TRP A N   1 
ATOM   1363 C  CA  . TRP A 1 188  ? 54.964 56.647  6.937   1.00 8.72  ? 188  TRP A CA  1 
ATOM   1364 C  C   . TRP A 1 188  ? 54.736 55.628  8.075   1.00 8.72  ? 188  TRP A C   1 
ATOM   1365 O  O   . TRP A 1 188  ? 55.617 55.416  8.962   1.00 9.15  ? 188  TRP A O   1 
ATOM   1366 C  CB  . TRP A 1 188  ? 54.106 57.880  7.174   1.00 9.00  ? 188  TRP A CB  1 
ATOM   1367 C  CG  . TRP A 1 188  ? 54.541 58.680  8.402   1.00 9.45  ? 188  TRP A CG  1 
ATOM   1368 C  CD1 . TRP A 1 188  ? 55.408 59.707  8.390   1.00 10.43 ? 188  TRP A CD1 1 
ATOM   1369 C  CD2 . TRP A 1 188  ? 54.208 58.416  9.775   1.00 9.76  ? 188  TRP A CD2 1 
ATOM   1370 N  NE1 . TRP A 1 188  ? 55.692 60.114  9.685   1.00 10.74 ? 188  TRP A NE1 1 
ATOM   1371 C  CE2 . TRP A 1 188  ? 54.969 59.342  10.557  1.00 10.17 ? 188  TRP A CE2 1 
ATOM   1372 C  CE3 . TRP A 1 188  ? 53.389 57.494  10.409  1.00 8.86  ? 188  TRP A CE3 1 
ATOM   1373 C  CZ2 . TRP A 1 188  ? 54.928 59.349  11.968  1.00 10.59 ? 188  TRP A CZ2 1 
ATOM   1374 C  CZ3 . TRP A 1 188  ? 53.360 57.485  11.807  1.00 9.76  ? 188  TRP A CZ3 1 
ATOM   1375 C  CH2 . TRP A 1 188  ? 54.124 58.408  12.563  1.00 9.97  ? 188  TRP A CH2 1 
ATOM   1376 N  N   . LEU A 1 189  ? 53.611 54.922  8.054   1.00 7.66  ? 189  LEU A N   1 
ATOM   1377 C  CA  . LEU A 1 189  ? 53.342 53.944  9.101   1.00 8.35  ? 189  LEU A CA  1 
ATOM   1378 C  C   . LEU A 1 189  ? 54.331 52.820  9.114   1.00 8.96  ? 189  LEU A C   1 
ATOM   1379 O  O   . LEU A 1 189  ? 54.705 52.340  10.219  1.00 9.97  ? 189  LEU A O   1 
ATOM   1380 C  CB  . LEU A 1 189  ? 51.941 53.310  8.959   1.00 8.43  ? 189  LEU A CB  1 
ATOM   1381 C  CG  . LEU A 1 189  ? 50.826 54.227  9.417   1.00 8.55  ? 189  LEU A CG  1 
ATOM   1382 C  CD1 . LEU A 1 189  ? 49.458 53.529  9.090   1.00 9.61  ? 189  LEU A CD1 1 
ATOM   1383 C  CD2 . LEU A 1 189  ? 50.888 54.452  11.001  1.00 9.36  ? 189  LEU A CD2 1 
ATOM   1384 N  N   . LYS A 1 190  ? 54.782 52.342  7.967   1.00 8.78  ? 190  LYS A N   1 
ATOM   1385 C  CA  . LYS A 1 190  ? 55.713 51.220  7.978   1.00 9.78  ? 190  LYS A CA  1 
ATOM   1386 C  C   . LYS A 1 190  ? 57.046 51.678  8.551   1.00 10.22 ? 190  LYS A C   1 
ATOM   1387 O  O   . LYS A 1 190  ? 57.655 50.957  9.351   1.00 11.49 ? 190  LYS A O   1 
ATOM   1388 C  CB  . LYS A 1 190  ? 55.937 50.640  6.569   1.00 11.63 ? 190  LYS A CB  1 
ATOM   1389 C  CG  . LYS A 1 190  ? 56.852 49.405  6.576   1.00 14.20 ? 190  LYS A CG  1 
ATOM   1390 C  CD  . LYS A 1 190  ? 57.048 48.857  5.210   1.00 18.10 ? 190  LYS A CD  1 
ATOM   1391 C  CE  . LYS A 1 190  ? 57.887 47.573  5.210   1.00 21.16 ? 190  LYS A CE  1 
ATOM   1392 N  NZ  . LYS A 1 190  ? 58.129 47.150  3.767   1.00 21.51 ? 190  LYS A NZ  1 
ATOM   1393 N  N   . GLN A 1 191  ? 57.465 52.858  8.152   1.00 10.51 ? 191  GLN A N   1 
ATOM   1394 C  CA  . GLN A 1 191  ? 58.754 53.403  8.599   1.00 12.65 ? 191  GLN A CA  1 
ATOM   1395 C  C   . GLN A 1 191  ? 58.792 53.692  10.091  1.00 13.56 ? 191  GLN A C   1 
ATOM   1396 O  O   . GLN A 1 191  ? 59.740 53.273  10.783  1.00 15.36 ? 191  GLN A O   1 
ATOM   1397 C  CB  . GLN A 1 191  ? 59.061 54.689  7.841   1.00 14.15 ? 191  GLN A CB  1 
ATOM   1398 C  CG  . GLN A 1 191  ? 60.426 55.270  8.248   1.00 19.65 ? 191  GLN A CG  1 
ATOM   1399 C  CD  . GLN A 1 191  ? 60.902 56.433  7.334   1.00 22.74 ? 191  GLN A CD  1 
ATOM   1400 O  OE1 . GLN A 1 191  ? 61.978 57.006  7.577   1.00 27.22 ? 191  GLN A OE1 1 
ATOM   1401 N  NE2 . GLN A 1 191  ? 60.128 56.771  6.308   1.00 24.72 ? 191  GLN A NE2 1 
ATOM   1402 N  N   . PHE A 1 192  ? 57.784 54.364  10.596  1.00 11.56 ? 192  PHE A N   1 
ATOM   1403 C  CA  . PHE A 1 192  ? 57.785 54.785  11.994  1.00 12.27 ? 192  PHE A CA  1 
ATOM   1404 C  C   . PHE A 1 192  ? 57.021 53.946  12.999  1.00 12.89 ? 192  PHE A C   1 
ATOM   1405 O  O   . PHE A 1 192  ? 57.357 53.969  14.194  1.00 15.26 ? 192  PHE A O   1 
ATOM   1406 C  CB  . PHE A 1 192  ? 57.316 56.227  12.080  1.00 11.42 ? 192  PHE A CB  1 
ATOM   1407 C  CG  . PHE A 1 192  ? 58.211 57.183  11.344  1.00 11.71 ? 192  PHE A CG  1 
ATOM   1408 C  CD1 . PHE A 1 192  ? 59.447 57.537  11.901  1.00 13.48 ? 192  PHE A CD1 1 
ATOM   1409 C  CD2 . PHE A 1 192  ? 57.884 57.662  10.064  1.00 12.56 ? 192  PHE A CD2 1 
ATOM   1410 C  CE1 . PHE A 1 192  ? 60.346 58.350  11.191  1.00 14.74 ? 192  PHE A CE1 1 
ATOM   1411 C  CE2 . PHE A 1 192  ? 58.755 58.464  9.352   1.00 12.82 ? 192  PHE A CE2 1 
ATOM   1412 C  CZ  . PHE A 1 192  ? 60.015 58.816  9.929   1.00 14.43 ? 192  PHE A CZ  1 
ATOM   1413 N  N   . MET A 1 193  ? 56.000 53.226  12.564  1.00 11.63 ? 193  MET A N   1 
ATOM   1414 C  CA  . MET A 1 193  ? 55.223 52.415  13.496  1.00 11.46 ? 193  MET A CA  1 
ATOM   1415 C  C   . MET A 1 193  ? 55.350 50.921  13.224  1.00 11.95 ? 193  MET A C   1 
ATOM   1416 O  O   . MET A 1 193  ? 54.814 50.095  13.995  1.00 13.85 ? 193  MET A O   1 
ATOM   1417 C  CB  . MET A 1 193  ? 53.733 52.814  13.411  1.00 11.31 ? 193  MET A CB  1 
ATOM   1418 C  CG  A MET A 1 193  ? 53.379 54.177  14.048  0.50 10.37 ? 193  MET A CG  1 
ATOM   1419 C  CG  B MET A 1 193  ? 53.598 54.400  13.679  0.50 15.69 ? 193  MET A CG  1 
ATOM   1420 S  SD  A MET A 1 193  ? 53.521 54.157  15.870  0.50 11.45 ? 193  MET A SD  1 
ATOM   1421 S  SD  B MET A 1 193  ? 54.607 55.180  14.928  0.50 18.20 ? 193  MET A SD  1 
ATOM   1422 C  CE  A MET A 1 193  ? 54.734 55.453  16.160  0.50 12.66 ? 193  MET A CE  1 
ATOM   1423 C  CE  B MET A 1 193  ? 53.832 54.504  16.398  0.50 16.90 ? 193  MET A CE  1 
ATOM   1424 N  N   . ASN A 1 194  ? 56.007 50.565  12.119  1.00 12.47 ? 194  ASN A N   1 
ATOM   1425 C  CA  . ASN A 1 194  ? 56.182 49.182  11.718  1.00 13.18 ? 194  ASN A CA  1 
ATOM   1426 C  C   . ASN A 1 194  ? 54.885 48.392  11.610  1.00 13.36 ? 194  ASN A C   1 
ATOM   1427 O  O   . ASN A 1 194  ? 54.777 47.229  12.049  1.00 14.37 ? 194  ASN A O   1 
ATOM   1428 C  CB  . ASN A 1 194  ? 57.098 48.453  12.740  1.00 15.66 ? 194  ASN A CB  1 
ATOM   1429 C  CG  . ASN A 1 194  ? 57.610 47.144  12.211  1.00 21.62 ? 194  ASN A CG  1 
ATOM   1430 O  OD1 . ASN A 1 194  ? 57.812 46.987  11.014  1.00 20.44 ? 194  ASN A OD1 1 
ATOM   1431 N  ND2 . ASN A 1 194  ? 57.837 46.211  13.128  1.00 26.61 ? 194  ASN A ND2 1 
ATOM   1432 N  N   . VAL A 1 195  ? 53.872 49.026  11.023  1.00 11.85 ? 195  VAL A N   1 
ATOM   1433 C  CA  . VAL A 1 195  ? 52.599 48.344  10.829  1.00 11.88 ? 195  VAL A CA  1 
ATOM   1434 C  C   . VAL A 1 195  ? 52.016 48.800  9.498   1.00 10.79 ? 195  VAL A C   1 
ATOM   1435 O  O   . VAL A 1 195  ? 52.281 49.902  9.047   1.00 10.32 ? 195  VAL A O   1 
ATOM   1436 C  CB  . VAL A 1 195  ? 51.530 48.692  11.939  1.00 12.25 ? 195  VAL A CB  1 
ATOM   1437 C  CG1 . VAL A 1 195  ? 52.003 48.262  13.316  1.00 16.71 ? 195  VAL A CG1 1 
ATOM   1438 C  CG2 . VAL A 1 195  ? 51.176 50.172  11.954  1.00 13.90 ? 195  VAL A CG2 1 
ATOM   1439 N  N   . THR A 1 196  ? 51.260 47.890  8.891   1.00 10.00 ? 196  THR A N   1 
ATOM   1440 C  CA  . THR A 1 196  ? 50.533 48.152  7.617   1.00 10.25 ? 196  THR A CA  1 
ATOM   1441 C  C   . THR A 1 196  ? 49.105 47.651  7.813   1.00 9.87  ? 196  THR A C   1 
ATOM   1442 O  O   . THR A 1 196  ? 48.863 46.443  7.864   1.00 10.37 ? 196  THR A O   1 
ATOM   1443 C  CB  . THR A 1 196  ? 51.141 47.409  6.421   1.00 10.57 ? 196  THR A CB  1 
ATOM   1444 O  OG1 . THR A 1 196  ? 52.525 47.792  6.276   1.00 12.83 ? 196  THR A OG1 1 
ATOM   1445 C  CG2 . THR A 1 196  ? 50.404 47.789  5.146   1.00 13.21 ? 196  THR A CG2 1 
ATOM   1446 N  N   . PRO A 1 197  ? 48.116 48.569  7.911   1.00 8.77  ? 197  PRO A N   1 
ATOM   1447 C  CA  . PRO A 1 197  ? 46.732 48.152  8.109   1.00 8.67  ? 197  PRO A CA  1 
ATOM   1448 C  C   . PRO A 1 197  ? 46.215 47.294  6.972   1.00 9.15  ? 197  PRO A C   1 
ATOM   1449 O  O   . PRO A 1 197  ? 46.574 47.536  5.793   1.00 8.96  ? 197  PRO A O   1 
ATOM   1450 C  CB  . PRO A 1 197  ? 45.988 49.485  8.153   1.00 10.45 ? 197  PRO A CB  1 
ATOM   1451 C  CG  . PRO A 1 197  ? 47.008 50.476  8.656   1.00 9.89  ? 197  PRO A CG  1 
ATOM   1452 C  CD  . PRO A 1 197  ? 48.292 50.022  8.078   1.00 9.52  ? 197  PRO A CD  1 
ATOM   1453 N  N   . THR A 1 198  ? 45.389 46.324  7.318   1.00 8.16  ? 198  THR A N   1 
ATOM   1454 C  CA  . THR A 1 198  ? 44.738 45.488  6.306   1.00 8.87  ? 198  THR A CA  1 
ATOM   1455 C  C   . THR A 1 198  ? 43.226 45.637  6.398   1.00 8.01  ? 198  THR A C   1 
ATOM   1456 O  O   . THR A 1 198  ? 42.495 44.936  5.698   1.00 8.55  ? 198  THR A O   1 
ATOM   1457 C  CB  . THR A 1 198  ? 45.076 43.995  6.454   1.00 10.03 ? 198  THR A CB  1 
ATOM   1458 O  OG1 . THR A 1 198  ? 44.672 43.583  7.757   1.00 11.90 ? 198  THR A OG1 1 
ATOM   1459 C  CG2 . THR A 1 198  ? 46.594 43.741  6.277   1.00 11.76 ? 198  THR A CG2 1 
ATOM   1460 N  N   . ALA A 1 199  ? 42.738 46.516  7.275   1.00 7.81  ? 199  ALA A N   1 
ATOM   1461 C  CA  . ALA A 1 199  ? 41.290 46.806  7.380   1.00 7.25  ? 199  ALA A CA  1 
ATOM   1462 C  C   . ALA A 1 199  ? 41.130 48.310  7.142   1.00 8.06  ? 199  ALA A C   1 
ATOM   1463 O  O   . ALA A 1 199  ? 41.890 49.116  7.718   1.00 7.55  ? 199  ALA A O   1 
ATOM   1464 C  CB  . ALA A 1 199  ? 40.756 46.462  8.821   1.00 8.67  ? 199  ALA A CB  1 
ATOM   1465 N  N   . SER A 1 200  ? 40.150 48.684  6.327   1.00 7.27  ? 200  SER A N   1 
ATOM   1466 C  CA  . SER A 1 200  ? 39.861 50.070  6.017   1.00 7.14  ? 200  SER A CA  1 
ATOM   1467 C  C   . SER A 1 200  ? 38.604 50.552  6.723   1.00 6.91  ? 200  SER A C   1 
ATOM   1468 O  O   . SER A 1 200  ? 37.627 49.771  6.884   1.00 7.55  ? 200  SER A O   1 
ATOM   1469 C  CB  . SER A 1 200  ? 39.726 50.202  4.504   1.00 7.79  ? 200  SER A CB  1 
ATOM   1470 O  OG  . SER A 1 200  ? 39.555 51.575  4.124   1.00 10.37 ? 200  SER A OG  1 
ATOM   1471 N  N   . TRP A 1 201  ? 38.615 51.827  7.103   1.00 7.56  ? 201  TRP A N   1 
ATOM   1472 C  CA  . TRP A 1 201  ? 37.524 52.510  7.808   1.00 6.70  ? 201  TRP A CA  1 
ATOM   1473 C  C   . TRP A 1 201  ? 37.173 53.768  7.048   1.00 6.48  ? 201  TRP A C   1 
ATOM   1474 O  O   . TRP A 1 201  ? 37.986 54.712  7.044   1.00 8.34  ? 201  TRP A O   1 
ATOM   1475 C  CB  . TRP A 1 201  ? 38.076 52.848  9.190   1.00 7.13  ? 201  TRP A CB  1 
ATOM   1476 C  CG  . TRP A 1 201  ? 37.235 53.672  10.136  1.00 6.93  ? 201  TRP A CG  1 
ATOM   1477 C  CD1 . TRP A 1 201  ? 37.381 55.006  10.446  1.00 7.55  ? 201  TRP A CD1 1 
ATOM   1478 C  CD2 . TRP A 1 201  ? 36.264 53.165  11.066  1.00 8.01  ? 201  TRP A CD2 1 
ATOM   1479 N  NE1 . TRP A 1 201  ? 36.567 55.334  11.505  1.00 8.06  ? 201  TRP A NE1 1 
ATOM   1480 C  CE2 . TRP A 1 201  ? 35.876 54.240  11.913  1.00 8.26  ? 201  TRP A CE2 1 
ATOM   1481 C  CE3 . TRP A 1 201  ? 35.699 51.904  11.283  1.00 8.53  ? 201  TRP A CE3 1 
ATOM   1482 C  CZ2 . TRP A 1 201  ? 34.955 54.102  12.959  1.00 8.81  ? 201  TRP A CZ2 1 
ATOM   1483 C  CZ3 . TRP A 1 201  ? 34.766 51.749  12.343  1.00 9.08  ? 201  TRP A CZ3 1 
ATOM   1484 C  CH2 . TRP A 1 201  ? 34.414 52.852  13.161  1.00 9.86  ? 201  TRP A CH2 1 
ATOM   1485 N  N   . ALA A 1 202  ? 35.988 53.791  6.428   1.00 6.97  ? 202  ALA A N   1 
ATOM   1486 C  CA  . ALA A 1 202  ? 35.570 54.997  5.692   1.00 6.87  ? 202  ALA A CA  1 
ATOM   1487 C  C   . ALA A 1 202  ? 34.148 55.373  6.101   1.00 7.19  ? 202  ALA A C   1 
ATOM   1488 O  O   . ALA A 1 202  ? 33.153 54.992  5.488   1.00 7.81  ? 202  ALA A O   1 
ATOM   1489 C  CB  . ALA A 1 202  ? 35.674 54.733  4.187   1.00 8.49  ? 202  ALA A CB  1 
ATOM   1490 N  N   . ILE A 1 203  ? 34.072 56.068  7.233   1.00 7.08  ? 203  ILE A N   1 
ATOM   1491 C  CA  . ILE A 1 203  ? 32.778 56.403  7.828   1.00 6.77  ? 203  ILE A CA  1 
ATOM   1492 C  C   . ILE A 1 203  ? 32.133 57.664  7.316   1.00 7.10  ? 203  ILE A C   1 
ATOM   1493 O  O   . ILE A 1 203  ? 30.946 57.877  7.590   1.00 8.17  ? 203  ILE A O   1 
ATOM   1494 C  CB  . ILE A 1 203  ? 32.861 56.503  9.401   1.00 7.46  ? 203  ILE A CB  1 
ATOM   1495 C  CG1 . ILE A 1 203  ? 34.008 57.427  9.858   1.00 7.92  ? 203  ILE A CG1 1 
ATOM   1496 C  CG2 . ILE A 1 203  ? 33.125 55.065  9.943   1.00 8.48  ? 203  ILE A CG2 1 
ATOM   1497 C  CD1 . ILE A 1 203  ? 33.913 57.816  11.383  1.00 8.41  ? 203  ILE A CD1 1 
ATOM   1498 N  N   . ASP A 1 204  ? 32.887 58.512  6.618   1.00 7.12  ? 204  ASP A N   1 
ATOM   1499 C  CA  . ASP A 1 204  ? 32.327 59.802  6.219   1.00 7.13  ? 204  ASP A CA  1 
ATOM   1500 C  C   . ASP A 1 204  ? 32.272 60.197  4.723   1.00 6.69  ? 204  ASP A C   1 
ATOM   1501 O  O   . ASP A 1 204  ? 31.562 61.134  4.429   1.00 8.36  ? 204  ASP A O   1 
ATOM   1502 C  CB  . ASP A 1 204  ? 33.017 60.939  6.998   1.00 7.65  ? 204  ASP A CB  1 
ATOM   1503 C  CG  . ASP A 1 204  ? 32.103 62.165  7.216   1.00 7.84  ? 204  ASP A CG  1 
ATOM   1504 O  OD1 . ASP A 1 204  ? 30.874 62.047  7.334   1.00 8.65  ? 204  ASP A OD1 1 
ATOM   1505 O  OD2 . ASP A 1 204  ? 32.632 63.303  7.291   1.00 7.72  ? 204  ASP A OD2 1 
ATOM   1506 N  N   . PRO A 1 205  ? 33.003 59.531  3.783   1.00 6.43  ? 205  PRO A N   1 
ATOM   1507 C  CA  . PRO A 1 205  ? 32.827 60.012  2.380   1.00 6.92  ? 205  PRO A CA  1 
ATOM   1508 C  C   . PRO A 1 205  ? 31.360 59.964  1.967   1.00 6.88  ? 205  PRO A C   1 
ATOM   1509 O  O   . PRO A 1 205  ? 30.606 59.080  2.410   1.00 7.64  ? 205  PRO A O   1 
ATOM   1510 C  CB  . PRO A 1 205  ? 33.741 59.085  1.555   1.00 8.49  ? 205  PRO A CB  1 
ATOM   1511 C  CG  . PRO A 1 205  ? 34.844 58.610  2.590   1.00 9.78  ? 205  PRO A CG  1 
ATOM   1512 C  CD  . PRO A 1 205  ? 33.991 58.428  3.896   1.00 8.41  ? 205  PRO A CD  1 
ATOM   1513 N  N   . PHE A 1 206  ? 30.940 60.883  1.100   1.00 6.83  ? 206  PHE A N   1 
ATOM   1514 C  CA  . PHE A 1 206  ? 29.468 61.045  0.828   1.00 7.14  ? 206  PHE A CA  1 
ATOM   1515 C  C   . PHE A 1 206  ? 29.018 60.161  -0.348  1.00 7.31  ? 206  PHE A C   1 
ATOM   1516 O  O   . PHE A 1 206  ? 28.804 60.589  -1.482  1.00 7.64  ? 206  PHE A O   1 
ATOM   1517 C  CB  . PHE A 1 206  ? 29.177 62.536  0.579   1.00 7.59  ? 206  PHE A CB  1 
ATOM   1518 C  CG  . PHE A 1 206  ? 30.036 63.488  1.420   1.00 6.58  ? 206  PHE A CG  1 
ATOM   1519 C  CD1 . PHE A 1 206  ? 30.228 63.254  2.772   1.00 7.53  ? 206  PHE A CD1 1 
ATOM   1520 C  CD2 . PHE A 1 206  ? 30.651 64.583  0.809   1.00 7.22  ? 206  PHE A CD2 1 
ATOM   1521 C  CE1 . PHE A 1 206  ? 31.018 64.095  3.532   1.00 8.10  ? 206  PHE A CE1 1 
ATOM   1522 C  CE2 . PHE A 1 206  ? 31.458 65.454  1.553   1.00 6.49  ? 206  PHE A CE2 1 
ATOM   1523 C  CZ  . PHE A 1 206  ? 31.644 65.225  2.925   1.00 8.18  ? 206  PHE A CZ  1 
ATOM   1524 N  N   . GLY A 1 207  ? 28.892 58.892  -0.008  1.00 6.82  ? 207  GLY A N   1 
ATOM   1525 C  CA  . GLY A 1 207  ? 28.687 57.835  -1.004  1.00 6.82  ? 207  GLY A CA  1 
ATOM   1526 C  C   . GLY A 1 207  ? 30.019 57.122  -1.210  1.00 6.80  ? 207  GLY A C   1 
ATOM   1527 O  O   . GLY A 1 207  ? 31.127 57.662  -0.909  1.00 7.28  ? 207  GLY A O   1 
ATOM   1528 N  N   . HIS A 1 208  ? 29.950 55.922  -1.796  1.00 6.90  ? 208  HIS A N   1 
ATOM   1529 C  CA  . HIS A 1 208  ? 31.156 55.061  -1.860  1.00 7.13  ? 208  HIS A CA  1 
ATOM   1530 C  C   . HIS A 1 208  ? 31.368 54.433  -3.213  1.00 6.40  ? 208  HIS A C   1 
ATOM   1531 O  O   . HIS A 1 208  ? 30.392 54.075  -3.915  1.00 7.31  ? 208  HIS A O   1 
ATOM   1532 C  CB  . HIS A 1 208  ? 31.048 53.947  -0.786  1.00 7.78  ? 208  HIS A CB  1 
ATOM   1533 C  CG  . HIS A 1 208  ? 31.123 54.460  0.635   1.00 7.57  ? 208  HIS A CG  1 
ATOM   1534 N  ND1 . HIS A 1 208  ? 32.337 54.754  1.250   1.00 9.01  ? 208  HIS A ND1 1 
ATOM   1535 C  CD2 . HIS A 1 208  ? 30.153 54.744  1.529   1.00 9.09  ? 208  HIS A CD2 1 
ATOM   1536 C  CE1 . HIS A 1 208  ? 32.073 55.181  2.480   1.00 9.17  ? 208  HIS A CE1 1 
ATOM   1537 N  NE2 . HIS A 1 208  ? 30.771 55.184  2.674   1.00 10.13 ? 208  HIS A NE2 1 
ATOM   1538 N  N   . SER A 1 209  ? 32.638 54.301  -3.591  1.00 6.73  ? 209  SER A N   1 
ATOM   1539 C  CA  . SER A 1 209  ? 33.041 53.811  -4.919  1.00 5.58  ? 209  SER A CA  1 
ATOM   1540 C  C   . SER A 1 209  ? 33.760 52.509  -4.855  1.00 6.26  ? 209  SER A C   1 
ATOM   1541 O  O   . SER A 1 209  ? 34.567 52.269  -3.958  1.00 6.45  ? 209  SER A O   1 
ATOM   1542 C  CB  . SER A 1 209  ? 34.011 54.863  -5.496  1.00 7.42  ? 209  SER A CB  1 
ATOM   1543 O  OG  . SER A 1 209  ? 34.541 54.337  -6.714  1.00 6.90  ? 209  SER A OG  1 
ATOM   1544 N  N   . PRO A 1 210  ? 33.515 51.614  -5.844  1.00 6.13  ? 210  PRO A N   1 
ATOM   1545 C  CA  . PRO A 1 210  ? 34.211 50.312  -5.878  1.00 6.63  ? 210  PRO A CA  1 
ATOM   1546 C  C   . PRO A 1 210  ? 35.693 50.513  -6.225  1.00 6.48  ? 210  PRO A C   1 
ATOM   1547 O  O   . PRO A 1 210  ? 36.475 49.548  -6.156  1.00 6.59  ? 210  PRO A O   1 
ATOM   1548 C  CB  . PRO A 1 210  ? 33.490 49.521  -6.983  1.00 7.14  ? 210  PRO A CB  1 
ATOM   1549 C  CG  . PRO A 1 210  ? 32.903 50.642  -7.857  1.00 7.61  ? 210  PRO A CG  1 
ATOM   1550 C  CD  . PRO A 1 210  ? 32.505 51.745  -6.915  1.00 6.22  ? 210  PRO A CD  1 
ATOM   1551 N  N   . THR A 1 211  ? 36.131 51.745  -6.612  1.00 6.50  ? 211  THR A N   1 
ATOM   1552 C  CA  . THR A 1 211  ? 37.559 51.954  -6.798  1.00 7.57  ? 211  THR A CA  1 
ATOM   1553 C  C   . THR A 1 211  ? 38.297 51.700  -5.493  1.00 6.90  ? 211  THR A C   1 
ATOM   1554 O  O   . THR A 1 211  ? 39.477 51.296  -5.517  1.00 7.24  ? 211  THR A O   1 
ATOM   1555 C  CB  . THR A 1 211  ? 37.774 53.389  -7.280  1.00 7.05  ? 211  THR A CB  1 
ATOM   1556 O  OG1 . THR A 1 211  ? 37.203 53.440  -8.611  1.00 7.58  ? 211  THR A OG1 1 
ATOM   1557 C  CG2 . THR A 1 211  ? 39.245 53.788  -7.313  1.00 8.77  ? 211  THR A CG2 1 
ATOM   1558 N  N   . MET A 1 212  ? 37.628 51.960  -4.354  1.00 6.62  ? 212  MET A N   1 
ATOM   1559 C  CA  . MET A 1 212  ? 38.305 51.698  -3.086  1.00 7.12  ? 212  MET A CA  1 
ATOM   1560 C  C   . MET A 1 212  ? 38.660 50.220  -2.870  1.00 6.98  ? 212  MET A C   1 
ATOM   1561 O  O   . MET A 1 212  ? 39.838 49.907  -2.654  1.00 6.70  ? 212  MET A O   1 
ATOM   1562 C  CB  . MET A 1 212  ? 37.500 52.271  -1.923  1.00 7.76  ? 212  MET A CB  1 
ATOM   1563 C  CG  . MET A 1 212  ? 37.249 53.745  -2.024  1.00 8.39  ? 212  MET A CG  1 
ATOM   1564 S  SD  . MET A 1 212  ? 38.702 54.737  -2.336  1.00 11.81 ? 212  MET A SD  1 
ATOM   1565 C  CE  . MET A 1 212  ? 39.496 54.715  -0.751  1.00 12.94 ? 212  MET A CE  1 
ATOM   1566 N  N   . PRO A 1 213  ? 37.697 49.275  -2.892  1.00 7.12  ? 213  PRO A N   1 
ATOM   1567 C  CA  . PRO A 1 213  ? 38.128 47.873  -2.718  1.00 7.41  ? 213  PRO A CA  1 
ATOM   1568 C  C   . PRO A 1 213  ? 39.100 47.470  -3.847  1.00 7.35  ? 213  PRO A C   1 
ATOM   1569 O  O   . PRO A 1 213  ? 39.986 46.638  -3.626  1.00 8.34  ? 213  PRO A O   1 
ATOM   1570 C  CB  . PRO A 1 213  ? 36.813 47.069  -2.769  1.00 7.90  ? 213  PRO A CB  1 
ATOM   1571 C  CG  . PRO A 1 213  ? 35.795 48.045  -3.442  1.00 7.60  ? 213  PRO A CG  1 
ATOM   1572 C  CD  . PRO A 1 213  ? 36.221 49.415  -2.892  1.00 7.11  ? 213  PRO A CD  1 
ATOM   1573 N  N   . TYR A 1 214  ? 38.953 48.047  -5.061  1.00 7.21  ? 214  TYR A N   1 
ATOM   1574 C  CA  . TYR A 1 214  ? 39.912 47.677  -6.108  1.00 7.12  ? 214  TYR A CA  1 
ATOM   1575 C  C   . TYR A 1 214  ? 41.362 47.966  -5.664  1.00 7.30  ? 214  TYR A C   1 
ATOM   1576 O  O   . TYR A 1 214  ? 42.262 47.086  -5.766  1.00 7.93  ? 214  TYR A O   1 
ATOM   1577 C  CB  . TYR A 1 214  ? 39.607 48.488  -7.389  1.00 7.79  ? 214  TYR A CB  1 
ATOM   1578 C  CG  . TYR A 1 214  ? 40.582 48.235  -8.544  1.00 10.12 ? 214  TYR A CG  1 
ATOM   1579 C  CD1 . TYR A 1 214  ? 40.345 47.165  -9.407  1.00 12.87 ? 214  TYR A CD1 1 
ATOM   1580 C  CD2 . TYR A 1 214  ? 41.654 49.092  -8.785  1.00 9.33  ? 214  TYR A CD2 1 
ATOM   1581 C  CE1 . TYR A 1 214  ? 41.158 46.970  -10.523 1.00 13.95 ? 214  TYR A CE1 1 
ATOM   1582 C  CE2 . TYR A 1 214  ? 42.458 48.913  -9.878  1.00 10.01 ? 214  TYR A CE2 1 
ATOM   1583 C  CZ  . TYR A 1 214  ? 42.191 47.873  -10.743 1.00 12.29 ? 214  TYR A CZ  1 
ATOM   1584 O  OH  . TYR A 1 214  ? 42.924 47.774  -11.927 1.00 12.60 ? 214  TYR A OH  1 
ATOM   1585 N  N   . ILE A 1 215  ? 41.626 49.197  -5.239  1.00 6.66  ? 215  ILE A N   1 
ATOM   1586 C  CA  . ILE A 1 215  ? 42.975 49.589  -4.825  1.00 6.89  ? 215  ILE A CA  1 
ATOM   1587 C  C   . ILE A 1 215  ? 43.372 48.886  -3.510  1.00 6.59  ? 215  ILE A C   1 
ATOM   1588 O  O   . ILE A 1 215  ? 44.470 48.370  -3.391  1.00 7.52  ? 215  ILE A O   1 
ATOM   1589 C  CB  . ILE A 1 215  ? 43.038 51.123  -4.617  1.00 7.50  ? 215  ILE A CB  1 
ATOM   1590 C  CG1 . ILE A 1 215  ? 42.865 51.829  -5.961  1.00 8.53  ? 215  ILE A CG1 1 
ATOM   1591 C  CG2 . ILE A 1 215  ? 44.379 51.531  -3.886  1.00 8.82  ? 215  ILE A CG2 1 
ATOM   1592 C  CD1 . ILE A 1 215  ? 42.732 53.351  -5.814  1.00 11.27 ? 215  ILE A CD1 1 
ATOM   1593 N  N   . LEU A 1 216  ? 42.465 48.829  -2.566  1.00 7.24  ? 216  LEU A N   1 
ATOM   1594 C  CA  . LEU A 1 216  ? 42.788 48.210  -1.255  1.00 6.82  ? 216  LEU A CA  1 
ATOM   1595 C  C   . LEU A 1 216  ? 43.118 46.729  -1.406  1.00 7.55  ? 216  LEU A C   1 
ATOM   1596 O  O   . LEU A 1 216  ? 44.114 46.269  -0.823  1.00 7.54  ? 216  LEU A O   1 
ATOM   1597 C  CB  . LEU A 1 216  ? 41.601 48.386  -0.293  1.00 7.03  ? 216  LEU A CB  1 
ATOM   1598 C  CG  . LEU A 1 216  ? 41.230 49.822  0.075   1.00 7.63  ? 216  LEU A CG  1 
ATOM   1599 C  CD1 . LEU A 1 216  ? 39.922 49.785  0.840   1.00 9.28  ? 216  LEU A CD1 1 
ATOM   1600 C  CD2 . LEU A 1 216  ? 42.353 50.467  0.961   1.00 9.34  ? 216  LEU A CD2 1 
ATOM   1601 N  N   . GLN A 1 217  ? 42.331 45.997  -2.213  1.00 7.25  ? 217  GLN A N   1 
ATOM   1602 C  CA  . GLN A 1 217  ? 42.617 44.571  -2.381  1.00 8.09  ? 217  GLN A CA  1 
ATOM   1603 C  C   . GLN A 1 217  ? 43.984 44.327  -3.059  1.00 9.08  ? 217  GLN A C   1 
ATOM   1604 O  O   . GLN A 1 217  ? 44.617 43.317  -2.800  1.00 10.35 ? 217  GLN A O   1 
ATOM   1605 C  CB  . GLN A 1 217  ? 41.434 43.957  -3.144  1.00 9.33  ? 217  GLN A CB  1 
ATOM   1606 C  CG  . GLN A 1 217  ? 41.443 42.403  -3.189  1.00 10.70 ? 217  GLN A CG  1 
ATOM   1607 C  CD  . GLN A 1 217  ? 42.350 41.843  -4.242  1.00 13.74 ? 217  GLN A CD  1 
ATOM   1608 O  OE1 . GLN A 1 217  ? 42.496 42.416  -5.289  1.00 15.51 ? 217  GLN A OE1 1 
ATOM   1609 N  NE2 . GLN A 1 217  ? 42.918 40.667  -3.987  1.00 14.74 ? 217  GLN A NE2 1 
ATOM   1610 N  N   . LYS A 1 218  ? 44.446 45.263  -3.884  1.00 8.04  ? 218  LYS A N   1 
ATOM   1611 C  CA  . LYS A 1 218  ? 45.756 45.150  -4.534  1.00 8.32  ? 218  LYS A CA  1 
ATOM   1612 C  C   . LYS A 1 218  ? 46.862 45.774  -3.671  1.00 8.12  ? 218  LYS A C   1 
ATOM   1613 O  O   . LYS A 1 218  ? 48.025 45.849  -4.107  1.00 8.49  ? 218  LYS A O   1 
ATOM   1614 C  CB  . LYS A 1 218  ? 45.680 45.875  -5.883  1.00 8.37  ? 218  LYS A CB  1 
ATOM   1615 C  CG  . LYS A 1 218  ? 44.892 45.052  -6.904  1.00 9.61  ? 218  LYS A CG  1 
ATOM   1616 C  CD  . LYS A 1 218  ? 44.588 45.935  -8.158  1.00 10.01 ? 218  LYS A CD  1 
ATOM   1617 C  CE  . LYS A 1 218  ? 44.145 45.123  -9.355  1.00 14.10 ? 218  LYS A CE  1 
ATOM   1618 N  NZ  . LYS A 1 218  ? 43.084 44.073  -9.184  1.00 13.70 ? 218  LYS A NZ  1 
ATOM   1619 N  N   . SER A 1 219  ? 46.514 46.204  -2.465  1.00 7.96  ? 219  SER A N   1 
ATOM   1620 C  CA  . SER A 1 219  ? 47.428 46.798  -1.487  1.00 8.05  ? 219  SER A CA  1 
ATOM   1621 C  C   . SER A 1 219  ? 47.437 46.032  -0.174  1.00 7.80  ? 219  SER A C   1 
ATOM   1622 O  O   . SER A 1 219  ? 47.746 46.610  0.849   1.00 8.34  ? 219  SER A O   1 
ATOM   1623 C  CB  . SER A 1 219  ? 47.057 48.266  -1.242  1.00 8.22  ? 219  SER A CB  1 
ATOM   1624 O  OG  . SER A 1 219  ? 47.093 48.989  -2.494  1.00 8.63  ? 219  SER A OG  1 
ATOM   1625 N  N   . GLY A 1 220  ? 47.086 44.738  -0.255  1.00 7.64  ? 220  GLY A N   1 
ATOM   1626 C  CA  . GLY A 1 220  ? 47.155 43.865  0.930   1.00 9.21  ? 220  GLY A CA  1 
ATOM   1627 C  C   . GLY A 1 220  ? 45.950 43.824  1.853   1.00 8.91  ? 220  GLY A C   1 
ATOM   1628 O  O   . GLY A 1 220  ? 45.963 43.072  2.835   1.00 10.12 ? 220  GLY A O   1 
ATOM   1629 N  N   . PHE A 1 221  ? 44.907 44.596  1.557   1.00 7.99  ? 221  PHE A N   1 
ATOM   1630 C  CA  . PHE A 1 221  ? 43.784 44.605  2.472   1.00 8.05  ? 221  PHE A CA  1 
ATOM   1631 C  C   . PHE A 1 221  ? 42.940 43.372  2.397   1.00 8.32  ? 221  PHE A C   1 
ATOM   1632 O  O   . PHE A 1 221  ? 42.853 42.697  1.357   1.00 9.30  ? 221  PHE A O   1 
ATOM   1633 C  CB  . PHE A 1 221  ? 42.889 45.838  2.248   1.00 7.17  ? 221  PHE A CB  1 
ATOM   1634 C  CG  . PHE A 1 221  ? 43.459 47.095  2.773   1.00 6.71  ? 221  PHE A CG  1 
ATOM   1635 C  CD1 . PHE A 1 221  ? 44.583 47.703  2.173   1.00 7.73  ? 221  PHE A CD1 1 
ATOM   1636 C  CD2 . PHE A 1 221  ? 42.866 47.716  3.884   1.00 7.59  ? 221  PHE A CD2 1 
ATOM   1637 C  CE1 . PHE A 1 221  ? 45.078 48.857  2.668   1.00 7.71  ? 221  PHE A CE1 1 
ATOM   1638 C  CE2 . PHE A 1 221  ? 43.377 48.916  4.379   1.00 8.28  ? 221  PHE A CE2 1 
ATOM   1639 C  CZ  . PHE A 1 221  ? 44.496 49.495  3.770   1.00 7.42  ? 221  PHE A CZ  1 
ATOM   1640 N  N   . LYS A 1 222  ? 42.313 43.092  3.529   1.00 8.75  ? 222  LYS A N   1 
ATOM   1641 C  CA  . LYS A 1 222  ? 41.430 41.955  3.641   1.00 9.38  ? 222  LYS A CA  1 
ATOM   1642 C  C   . LYS A 1 222  ? 40.013 42.355  4.011   1.00 9.20  ? 222  LYS A C   1 
ATOM   1643 O  O   . LYS A 1 222  ? 39.106 41.570  3.807   1.00 9.26  ? 222  LYS A O   1 
ATOM   1644 C  CB  . LYS A 1 222  ? 41.951 40.980  4.702   1.00 11.58 ? 222  LYS A CB  1 
ATOM   1645 C  CG  . LYS A 1 222  ? 43.361 40.480  4.471   1.00 14.83 ? 222  LYS A CG  1 
ATOM   1646 C  CD  . LYS A 1 222  ? 43.563 39.852  3.110   1.00 18.77 ? 222  LYS A CD  1 
ATOM   1647 C  CE  . LYS A 1 222  ? 44.971 39.244  3.023   1.00 21.01 ? 222  LYS A CE  1 
ATOM   1648 N  NZ  A LYS A 1 222  ? 45.180 38.298  4.158   0.50 21.75 ? 222  LYS A NZ  1 
ATOM   1649 N  NZ  B LYS A 1 222  ? 45.120 38.391  1.681   0.50 21.30 ? 222  LYS A NZ  1 
ATOM   1650 N  N   . ASN A 1 223  ? 39.798 43.573  4.510   1.00 7.48  ? 223  ASN A N   1 
ATOM   1651 C  CA  . ASN A 1 223  ? 38.454 43.978  4.939   1.00 7.66  ? 223  ASN A CA  1 
ATOM   1652 C  C   . ASN A 1 223  ? 38.307 45.490  4.834   1.00 7.18  ? 223  ASN A C   1 
ATOM   1653 O  O   . ASN A 1 223  ? 39.284 46.216  4.932   1.00 7.73  ? 223  ASN A O   1 
ATOM   1654 C  CB  . ASN A 1 223  ? 38.233 43.625  6.454   1.00 8.59  ? 223  ASN A CB  1 
ATOM   1655 C  CG  . ASN A 1 223  ? 38.302 42.152  6.733   1.00 9.07  ? 223  ASN A CG  1 
ATOM   1656 O  OD1 . ASN A 1 223  ? 39.351 41.642  7.209   1.00 11.45 ? 223  ASN A OD1 1 
ATOM   1657 N  ND2 . ASN A 1 223  ? 37.251 41.444  6.424   1.00 7.71  ? 223  ASN A ND2 1 
ATOM   1658 N  N   . MET A 1 224  ? 37.067 45.916  4.672   1.00 6.77  ? 224  MET A N   1 
ATOM   1659 C  CA  . MET A 1 224  ? 36.782 47.368  4.650   1.00 6.97  ? 224  MET A CA  1 
ATOM   1660 C  C   . MET A 1 224  ? 35.384 47.648  5.216   1.00 7.48  ? 224  MET A C   1 
ATOM   1661 O  O   . MET A 1 224  ? 34.479 46.762  5.220   1.00 7.74  ? 224  MET A O   1 
ATOM   1662 C  CB  . MET A 1 224  ? 36.907 47.980  3.234   1.00 8.16  ? 224  MET A CB  1 
ATOM   1663 C  CG  . MET A 1 224  ? 35.896 47.384  2.235   1.00 8.16  ? 224  MET A CG  1 
ATOM   1664 S  SD  . MET A 1 224  ? 36.048 48.182  0.609   1.00 9.27  ? 224  MET A SD  1 
ATOM   1665 C  CE  . MET A 1 224  ? 35.593 49.765  1.048   1.00 13.60 ? 224  MET A CE  1 
ATOM   1666 N  N   . LEU A 1 225  ? 35.216 48.878  5.696   1.00 7.56  ? 225  LEU A N   1 
ATOM   1667 C  CA  . LEU A 1 225  ? 33.978 49.328  6.284   1.00 7.02  ? 225  LEU A CA  1 
ATOM   1668 C  C   . LEU A 1 225  ? 33.554 50.627  5.629   1.00 6.77  ? 225  LEU A C   1 
ATOM   1669 O  O   . LEU A 1 225  ? 34.349 51.533  5.437   1.00 7.07  ? 225  LEU A O   1 
ATOM   1670 C  CB  . LEU A 1 225  ? 34.153 49.478  7.814   1.00 7.85  ? 225  LEU A CB  1 
ATOM   1671 C  CG  . LEU A 1 225  ? 32.935 50.076  8.519   1.00 7.42  ? 225  LEU A CG  1 
ATOM   1672 C  CD1 . LEU A 1 225  ? 32.839 49.491  9.965   1.00 8.49  ? 225  LEU A CD1 1 
ATOM   1673 C  CD2 . LEU A 1 225  ? 32.997 51.625  8.594   1.00 8.73  ? 225  LEU A CD2 1 
ATOM   1674 N  N   . ILE A 1 226  ? 32.262 50.726  5.375   1.00 6.88  ? 226  ILE A N   1 
ATOM   1675 C  CA  . ILE A 1 226  ? 31.641 51.936  4.782   1.00 7.34  ? 226  ILE A CA  1 
ATOM   1676 C  C   . ILE A 1 226  ? 30.392 52.313  5.544   1.00 6.61  ? 226  ILE A C   1 
ATOM   1677 O  O   . ILE A 1 226  ? 29.836 51.488  6.296   1.00 8.40  ? 226  ILE A O   1 
ATOM   1678 C  CB  . ILE A 1 226  ? 31.353 51.759  3.251   1.00 7.18  ? 226  ILE A CB  1 
ATOM   1679 C  CG1 . ILE A 1 226  ? 30.287 50.670  3.035   1.00 8.27  ? 226  ILE A CG1 1 
ATOM   1680 C  CG2 . ILE A 1 226  ? 32.685 51.388  2.517   1.00 8.20  ? 226  ILE A CG2 1 
ATOM   1681 C  CD1 . ILE A 1 226  ? 29.902 50.499  1.519   1.00 9.21  ? 226  ILE A CD1 1 
ATOM   1682 N  N   . GLN A 1 227  ? 29.967 53.564  5.387   1.00 8.24  ? 227  GLN A N   1 
ATOM   1683 C  CA  . GLN A 1 227  ? 28.795 54.107  6.126   1.00 7.93  ? 227  GLN A CA  1 
ATOM   1684 C  C   . GLN A 1 227  ? 27.803 54.930  5.350   1.00 8.14  ? 227  GLN A C   1 
ATOM   1685 O  O   . GLN A 1 227  ? 26.605 54.708  5.504   1.00 8.92  ? 227  GLN A O   1 
ATOM   1686 C  CB  . GLN A 1 227  ? 29.318 54.939  7.335   1.00 8.78  ? 227  GLN A CB  1 
ATOM   1687 C  CG  . GLN A 1 227  ? 28.344 56.000  7.909   1.00 9.52  ? 227  GLN A CG  1 
ATOM   1688 C  CD  . GLN A 1 227  ? 27.009 55.460  8.424   1.00 9.10  ? 227  GLN A CD  1 
ATOM   1689 O  OE1 . GLN A 1 227  ? 26.902 54.281  8.817   1.00 10.61 ? 227  GLN A OE1 1 
ATOM   1690 N  NE2 . GLN A 1 227  ? 25.993 56.317  8.421   1.00 10.33 ? 227  GLN A NE2 1 
ATOM   1691 N  N   . ARG A 1 228  ? 28.234 55.857  4.504   1.00 7.91  ? 228  ARG A N   1 
ATOM   1692 C  CA  . ARG A 1 228  ? 27.251 56.740  3.891   1.00 7.45  ? 228  ARG A CA  1 
ATOM   1693 C  C   . ARG A 1 228  ? 26.721 56.180  2.595   1.00 7.72  ? 228  ARG A C   1 
ATOM   1694 O  O   . ARG A 1 228  ? 27.285 56.409  1.538   1.00 8.30  ? 228  ARG A O   1 
ATOM   1695 C  CB  . ARG A 1 228  ? 27.867 58.155  3.687   1.00 7.75  ? 228  ARG A CB  1 
ATOM   1696 C  CG  . ARG A 1 228  ? 28.072 58.917  4.978   1.00 7.87  ? 228  ARG A CG  1 
ATOM   1697 C  CD  . ARG A 1 228  ? 28.338 60.403  4.636   1.00 8.16  ? 228  ARG A CD  1 
ATOM   1698 N  NE  . ARG A 1 228  ? 28.672 61.247  5.794   1.00 8.43  ? 228  ARG A NE  1 
ATOM   1699 C  CZ  . ARG A 1 228  ? 27.783 61.936  6.505   1.00 9.67  ? 228  ARG A CZ  1 
ATOM   1700 N  NH1 . ARG A 1 228  ? 26.485 61.841  6.209   1.00 10.30 ? 228  ARG A NH1 1 
ATOM   1701 N  NH2 . ARG A 1 228  ? 28.200 62.790  7.429   1.00 10.95 ? 228  ARG A NH2 1 
ATOM   1702 N  N   . THR A 1 229  ? 25.684 55.356  2.724   1.00 7.82  ? 229  THR A N   1 
ATOM   1703 C  CA  . THR A 1 229  ? 24.966 54.835  1.580   1.00 7.91  ? 229  THR A CA  1 
ATOM   1704 C  C   . THR A 1 229  ? 23.494 55.235  1.792   1.00 7.58  ? 229  THR A C   1 
ATOM   1705 O  O   . THR A 1 229  ? 23.025 55.525  2.905   1.00 8.48  ? 229  THR A O   1 
ATOM   1706 C  CB  . THR A 1 229  ? 25.065 53.303  1.465   1.00 7.43  ? 229  THR A CB  1 
ATOM   1707 O  OG1 . THR A 1 229  ? 24.483 52.739  2.629   1.00 9.50  ? 229  THR A OG1 1 
ATOM   1708 C  CG2 . THR A 1 229  ? 26.528 52.898  1.410   1.00 8.85  ? 229  THR A CG2 1 
ATOM   1709 N  N   . HIS A 1 230  ? 22.815 55.328  0.661   1.00 7.92  ? 230  HIS A N   1 
ATOM   1710 C  CA  . HIS A 1 230  ? 21.406 55.782  0.689   1.00 8.65  ? 230  HIS A CA  1 
ATOM   1711 C  C   . HIS A 1 230  ? 20.572 55.036  1.738   1.00 8.34  ? 230  HIS A C   1 
ATOM   1712 O  O   . HIS A 1 230  ? 20.640 53.803  1.811   1.00 8.59  ? 230  HIS A O   1 
ATOM   1713 C  CB  . HIS A 1 230  ? 20.858 55.549  -0.738  1.00 8.49  ? 230  HIS A CB  1 
ATOM   1714 C  CG  . HIS A 1 230  ? 19.564 56.246  -1.038  1.00 8.63  ? 230  HIS A CG  1 
ATOM   1715 N  ND1 . HIS A 1 230  ? 18.390 55.986  -0.370  1.00 9.30  ? 230  HIS A ND1 1 
ATOM   1716 C  CD2 . HIS A 1 230  ? 19.257 57.159  -2.003  1.00 9.57  ? 230  HIS A CD2 1 
ATOM   1717 C  CE1 . HIS A 1 230  ? 17.418 56.707  -0.897  1.00 9.72  ? 230  HIS A CE1 1 
ATOM   1718 N  NE2 . HIS A 1 230  ? 17.910 57.429  -1.894  1.00 8.84  ? 230  HIS A NE2 1 
ATOM   1719 N  N   . TYR A 1 231  ? 19.773 55.797  2.504   1.00 8.77  ? 231  TYR A N   1 
ATOM   1720 C  CA  . TYR A 1 231  ? 18.960 55.159  3.538   1.00 8.79  ? 231  TYR A CA  1 
ATOM   1721 C  C   . TYR A 1 231  ? 18.070 54.038  2.973   1.00 9.54  ? 231  TYR A C   1 
ATOM   1722 O  O   . TYR A 1 231  ? 17.819 53.068  3.679   1.00 9.60  ? 231  TYR A O   1 
ATOM   1723 C  CB  . TYR A 1 231  ? 18.127 56.207  4.272   1.00 10.15 ? 231  TYR A CB  1 
ATOM   1724 C  CG  . TYR A 1 231  ? 17.135 56.984  3.385   1.00 10.41 ? 231  TYR A CG  1 
ATOM   1725 C  CD1 . TYR A 1 231  ? 15.839 56.492  3.142   1.00 10.36 ? 231  TYR A CD1 1 
ATOM   1726 C  CD2 . TYR A 1 231  ? 17.479 58.230  2.795   1.00 10.01 ? 231  TYR A CD2 1 
ATOM   1727 C  CE1 . TYR A 1 231  ? 14.938 57.204  2.379   1.00 11.15 ? 231  TYR A CE1 1 
ATOM   1728 C  CE2 . TYR A 1 231  ? 16.611 58.924  2.025   1.00 10.36 ? 231  TYR A CE2 1 
ATOM   1729 C  CZ  . TYR A 1 231  ? 15.309 58.412  1.814   1.00 10.24 ? 231  TYR A CZ  1 
ATOM   1730 O  OH  . TYR A 1 231  ? 14.392 59.151  1.059   1.00 12.27 ? 231  TYR A OH  1 
ATOM   1731 N  N   . SER A 1 232  ? 17.642 54.129  1.719   1.00 8.97  ? 232  SER A N   1 
ATOM   1732 C  CA  . SER A 1 232  ? 16.801 53.063  1.147   1.00 10.50 ? 232  SER A CA  1 
ATOM   1733 C  C   . SER A 1 232  ? 17.625 51.796  0.887   1.00 9.94  ? 232  SER A C   1 
ATOM   1734 O  O   . SER A 1 232  ? 17.131 50.666  1.016   1.00 10.39 ? 232  SER A O   1 
ATOM   1735 C  CB  . SER A 1 232  ? 16.172 53.494  -0.153  1.00 11.67 ? 232  SER A CB  1 
ATOM   1736 O  OG  . SER A 1 232  ? 15.208 54.504  0.060   1.00 13.04 ? 232  SER A OG  1 
ATOM   1737 N  N   . VAL A 1 233  ? 18.902 51.972  0.516   1.00 10.09 ? 233  VAL A N   1 
ATOM   1738 C  CA  . VAL A 1 233  ? 19.794 50.837  0.320   1.00 9.72  ? 233  VAL A CA  1 
ATOM   1739 C  C   . VAL A 1 233  ? 20.091 50.157  1.679   1.00 9.62  ? 233  VAL A C   1 
ATOM   1740 O  O   . VAL A 1 233  ? 20.090 48.921  1.775   1.00 9.84  ? 233  VAL A O   1 
ATOM   1741 C  CB  . VAL A 1 233  ? 21.135 51.326  -0.363  1.00 9.43  ? 233  VAL A CB  1 
ATOM   1742 C  CG1 . VAL A 1 233  ? 22.189 50.219  -0.347  1.00 9.79  ? 233  VAL A CG1 1 
ATOM   1743 C  CG2 . VAL A 1 233  ? 20.834 51.713  -1.829  1.00 9.82  ? 233  VAL A CG2 1 
ATOM   1744 N  N   . LYS A 1 234  ? 20.375 50.939  2.721   1.00 8.80  ? 234  LYS A N   1 
ATOM   1745 C  CA  . LYS A 1 234  ? 20.564 50.322  4.039   1.00 9.74  ? 234  LYS A CA  1 
ATOM   1746 C  C   . LYS A 1 234  ? 19.353 49.479  4.435   1.00 9.88  ? 234  LYS A C   1 
ATOM   1747 O  O   . LYS A 1 234  ? 19.515 48.379  4.941   1.00 9.91  ? 234  LYS A O   1 
ATOM   1748 C  CB  . LYS A 1 234  ? 20.782 51.408  5.091   1.00 8.97  ? 234  LYS A CB  1 
ATOM   1749 C  CG  . LYS A 1 234  ? 22.183 52.057  5.005   1.00 9.24  ? 234  LYS A CG  1 
ATOM   1750 C  CD  . LYS A 1 234  ? 22.190 53.355  5.780   1.00 9.19  ? 234  LYS A CD  1 
ATOM   1751 C  CE  . LYS A 1 234  ? 23.609 54.058  5.730   1.00 8.45  ? 234  LYS A CE  1 
ATOM   1752 N  NZ  . LYS A 1 234  ? 24.501 53.499  6.848   1.00 9.01  ? 234  LYS A NZ  1 
ATOM   1753 N  N   . LYS A 1 235  ? 18.153 50.017  4.230   1.00 10.06 ? 235  LYS A N   1 
ATOM   1754 C  CA  . LYS A 1 235  ? 16.944 49.242  4.621   1.00 10.42 ? 235  LYS A CA  1 
ATOM   1755 C  C   . LYS A 1 235  ? 16.834 47.959  3.810   1.00 10.07 ? 235  LYS A C   1 
ATOM   1756 O  O   . LYS A 1 235  ? 16.605 46.873  4.389   1.00 11.21 ? 235  LYS A O   1 
ATOM   1757 C  CB  . LYS A 1 235  ? 15.718 50.123  4.447   1.00 11.34 ? 235  LYS A CB  1 
ATOM   1758 C  CG  . LYS A 1 235  ? 14.392 49.391  4.861   1.00 11.32 ? 235  LYS A CG  1 
ATOM   1759 C  CD  . LYS A 1 235  ? 13.240 50.358  4.764   1.00 13.41 ? 235  LYS A CD  1 
ATOM   1760 C  CE  . LYS A 1 235  ? 11.921 49.708  5.247   1.00 14.79 ? 235  LYS A CE  1 
ATOM   1761 N  NZ  . LYS A 1 235  ? 10.811 50.691  5.029   1.00 20.51 ? 235  LYS A NZ  1 
ATOM   1762 N  N   . GLU A 1 236  ? 17.027 48.040  2.509   1.00 10.25 ? 236  GLU A N   1 
ATOM   1763 C  CA  . GLU A 1 236  ? 16.909 46.886  1.660   1.00 11.11 ? 236  GLU A CA  1 
ATOM   1764 C  C   . GLU A 1 236  ? 17.937 45.804  1.991   1.00 11.43 ? 236  GLU A C   1 
ATOM   1765 O  O   . GLU A 1 236  ? 17.643 44.606  2.099   1.00 12.27 ? 236  GLU A O   1 
ATOM   1766 C  CB  . GLU A 1 236  ? 17.073 47.341  0.210   1.00 14.09 ? 236  GLU A CB  1 
ATOM   1767 C  CG  . GLU A 1 236  ? 16.839 46.279  -0.864  1.00 18.45 ? 236  GLU A CG  1 
ATOM   1768 C  CD  . GLU A 1 236  ? 15.347 45.967  -1.084  1.00 21.57 ? 236  GLU A CD  1 
ATOM   1769 O  OE1 . GLU A 1 236  ? 14.454 46.759  -0.669  1.00 24.77 ? 236  GLU A OE1 1 
ATOM   1770 O  OE2 . GLU A 1 236  ? 15.089 44.915  -1.687  1.00 25.37 ? 236  GLU A OE2 1 
ATOM   1771 N  N   . LEU A 1 237  ? 19.198 46.204  2.153   1.00 10.19 ? 237  LEU A N   1 
ATOM   1772 C  CA  . LEU A 1 237  ? 20.224 45.199  2.414   1.00 10.78 ? 237  LEU A CA  1 
ATOM   1773 C  C   . LEU A 1 237  ? 20.045 44.691  3.854   1.00 10.21 ? 237  LEU A C   1 
ATOM   1774 O  O   . LEU A 1 237  ? 20.285 43.490  4.103   1.00 10.84 ? 237  LEU A O   1 
ATOM   1775 C  CB  . LEU A 1 237  ? 21.620 45.803  2.217   1.00 10.24 ? 237  LEU A CB  1 
ATOM   1776 C  CG  . LEU A 1 237  ? 21.953 46.268  0.779   1.00 9.82  ? 237  LEU A CG  1 
ATOM   1777 C  CD1 . LEU A 1 237  ? 23.388 46.846  0.797   1.00 11.88 ? 237  LEU A CD1 1 
ATOM   1778 C  CD2 . LEU A 1 237  ? 21.906 45.103  -0.241  1.00 11.94 ? 237  LEU A CD2 1 
ATOM   1779 N  N   . ALA A 1 238  ? 19.616 45.548  4.793   1.00 10.10 ? 238  ALA A N   1 
ATOM   1780 C  CA  . ALA A 1 238  ? 19.419 45.060  6.154   1.00 10.29 ? 238  ALA A CA  1 
ATOM   1781 C  C   . ALA A 1 238  ? 18.338 43.965  6.184   1.00 11.28 ? 238  ALA A C   1 
ATOM   1782 O  O   . ALA A 1 238  ? 18.501 42.963  6.917   1.00 11.77 ? 238  ALA A O   1 
ATOM   1783 C  CB  . ALA A 1 238  ? 19.031 46.223  7.077   1.00 11.01 ? 238  ALA A CB  1 
ATOM   1784 N  N   . GLN A 1 239  ? 17.254 44.197  5.440   1.00 11.49 ? 239  GLN A N   1 
ATOM   1785 C  CA  . GLN A 1 239  ? 16.181 43.179  5.427   1.00 13.25 ? 239  GLN A CA  1 
ATOM   1786 C  C   . GLN A 1 239  ? 16.661 41.815  4.952   1.00 14.05 ? 239  GLN A C   1 
ATOM   1787 O  O   . GLN A 1 239  ? 16.134 40.786  5.384   1.00 16.18 ? 239  GLN A O   1 
ATOM   1788 C  CB  . GLN A 1 239  ? 15.027 43.667  4.574   1.00 15.08 ? 239  GLN A CB  1 
ATOM   1789 C  CG  . GLN A 1 239  ? 14.229 44.764  5.271   1.00 18.49 ? 239  GLN A CG  1 
ATOM   1790 C  CD  . GLN A 1 239  ? 13.211 45.461  4.375   1.00 21.87 ? 239  GLN A CD  1 
ATOM   1791 O  OE1 . GLN A 1 239  ? 13.338 45.510  3.142   1.00 24.52 ? 239  GLN A OE1 1 
ATOM   1792 N  NE2 . GLN A 1 239  ? 12.205 46.053  5.010   1.00 23.91 ? 239  GLN A NE2 1 
ATOM   1793 N  N   . GLN A 1 240  ? 17.654 41.769  4.073   1.00 12.54 ? 240  GLN A N   1 
ATOM   1794 C  CA  . GLN A 1 240  ? 18.172 40.505  3.561   1.00 12.76 ? 240  GLN A CA  1 
ATOM   1795 C  C   . GLN A 1 240  ? 19.467 40.076  4.227   1.00 11.33 ? 240  GLN A C   1 
ATOM   1796 O  O   . GLN A 1 240  ? 20.077 39.118  3.816   1.00 11.36 ? 240  GLN A O   1 
ATOM   1797 C  CB  . GLN A 1 240  ? 18.437 40.645  2.059   1.00 14.21 ? 240  GLN A CB  1 
ATOM   1798 C  CG  . GLN A 1 240  ? 17.262 41.178  1.232   1.00 17.32 ? 240  GLN A CG  1 
ATOM   1799 C  CD  . GLN A 1 240  ? 16.061 40.325  1.396   1.00 19.74 ? 240  GLN A CD  1 
ATOM   1800 O  OE1 . GLN A 1 240  ? 14.922 40.836  1.484   1.00 23.80 ? 240  GLN A OE1 1 
ATOM   1801 N  NE2 . GLN A 1 240  ? 16.273 39.034  1.450   1.00 20.63 ? 240  GLN A NE2 1 
ATOM   1802 N  N   . ARG A 1 241  ? 19.851 40.789  5.303   1.00 11.48 ? 241  ARG A N   1 
ATOM   1803 C  CA  . ARG A 1 241  ? 21.146 40.541  5.955   1.00 10.93 ? 241  ARG A CA  1 
ATOM   1804 C  C   . ARG A 1 241  ? 22.280 40.515  4.921   1.00 9.99  ? 241  ARG A C   1 
ATOM   1805 O  O   . ARG A 1 241  ? 23.124 39.638  4.895   1.00 10.37 ? 241  ARG A O   1 
ATOM   1806 C  CB  . ARG A 1 241  ? 21.171 39.250  6.796   1.00 11.94 ? 241  ARG A CB  1 
ATOM   1807 C  CG  . ARG A 1 241  ? 20.139 39.367  7.911   1.00 13.71 ? 241  ARG A CG  1 
ATOM   1808 C  CD  . ARG A 1 241  ? 20.293 38.225  8.920   1.00 16.13 ? 241  ARG A CD  1 
ATOM   1809 N  NE  . ARG A 1 241  ? 20.237 36.932  8.281   1.00 21.51 ? 241  ARG A NE  1 
ATOM   1810 C  CZ  . ARG A 1 241  ? 20.633 35.817  8.885   1.00 23.06 ? 241  ARG A CZ  1 
ATOM   1811 N  NH1 . ARG A 1 241  ? 21.090 35.888  10.132  1.00 23.32 ? 241  ARG A NH1 1 
ATOM   1812 N  NH2 . ARG A 1 241  ? 20.624 34.657  8.223   1.00 24.54 ? 241  ARG A NH2 1 
ATOM   1813 N  N   . GLN A 1 242  ? 22.263 41.548  4.055   1.00 10.18 ? 242  GLN A N   1 
ATOM   1814 C  CA  . GLN A 1 242  ? 23.290 41.703  3.010   1.00 9.85  ? 242  GLN A CA  1 
ATOM   1815 C  C   . GLN A 1 242  ? 24.147 42.949  3.259   1.00 9.81  ? 242  GLN A C   1 
ATOM   1816 O  O   . GLN A 1 242  ? 24.708 43.522  2.318   1.00 10.43 ? 242  GLN A O   1 
ATOM   1817 C  CB  . GLN A 1 242  ? 22.654 41.750  1.622   1.00 10.20 ? 242  GLN A CB  1 
ATOM   1818 C  CG  . GLN A 1 242  ? 22.030 40.362  1.239   1.00 11.68 ? 242  GLN A CG  1 
ATOM   1819 C  CD  . GLN A 1 242  ? 21.203 40.465  -0.031  1.00 12.31 ? 242  GLN A CD  1 
ATOM   1820 O  OE1 . GLN A 1 242  ? 20.644 41.515  -0.326  1.00 12.38 ? 242  GLN A OE1 1 
ATOM   1821 N  NE2 . GLN A 1 242  ? 21.158 39.367  -0.794  1.00 13.50 ? 242  GLN A NE2 1 
ATOM   1822 N  N   . LEU A 1 243  ? 24.282 43.336  4.545   1.00 9.19  ? 243  LEU A N   1 
ATOM   1823 C  CA  . LEU A 1 243  ? 25.101 44.504  4.891   1.00 8.67  ? 243  LEU A CA  1 
ATOM   1824 C  C   . LEU A 1 243  ? 26.580 44.138  4.904   1.00 8.89  ? 243  LEU A C   1 
ATOM   1825 O  O   . LEU A 1 243  ? 27.409 45.027  4.925   1.00 9.23  ? 243  LEU A O   1 
ATOM   1826 C  CB  . LEU A 1 243  ? 24.668 45.067  6.247   1.00 9.16  ? 243  LEU A CB  1 
ATOM   1827 C  CG  . LEU A 1 243  ? 23.284 45.751  6.224   1.00 10.54 ? 243  LEU A CG  1 
ATOM   1828 C  CD1 . LEU A 1 243  ? 22.848 45.963  7.677   1.00 10.96 ? 243  LEU A CD1 1 
ATOM   1829 C  CD2 . LEU A 1 243  ? 23.317 47.120  5.470   1.00 10.97 ? 243  LEU A CD2 1 
ATOM   1830 N  N   . GLU A 1 244  ? 26.928 42.855  4.999   1.00 8.14  ? 244  GLU A N   1 
ATOM   1831 C  CA  . GLU A 1 244  ? 28.315 42.411  4.866   1.00 8.30  ? 244  GLU A CA  1 
ATOM   1832 C  C   . GLU A 1 244  ? 28.327 41.610  3.579   1.00 8.87  ? 244  GLU A C   1 
ATOM   1833 O  O   . GLU A 1 244  ? 27.514 40.693  3.397   1.00 9.25  ? 244  GLU A O   1 
ATOM   1834 C  CB  . GLU A 1 244  ? 28.783 41.550  6.059   1.00 8.14  ? 244  GLU A CB  1 
ATOM   1835 C  CG  . GLU A 1 244  ? 29.088 42.488  7.250   1.00 9.63  ? 244  GLU A CG  1 
ATOM   1836 C  CD  . GLU A 1 244  ? 29.390 41.805  8.566   1.00 9.12  ? 244  GLU A CD  1 
ATOM   1837 O  OE1 . GLU A 1 244  ? 28.811 40.725  8.846   1.00 9.74  ? 244  GLU A OE1 1 
ATOM   1838 O  OE2 . GLU A 1 244  ? 30.198 42.369  9.327   1.00 9.20  ? 244  GLU A OE2 1 
ATOM   1839 N  N   . PHE A 1 245  ? 29.282 41.907  2.691   1.00 8.38  ? 245  PHE A N   1 
ATOM   1840 C  CA  . PHE A 1 245  ? 29.314 41.289  1.371   1.00 7.99  ? 245  PHE A CA  1 
ATOM   1841 C  C   . PHE A 1 245  ? 30.717 41.252  0.817   1.00 8.42  ? 245  PHE A C   1 
ATOM   1842 O  O   . PHE A 1 245  ? 31.601 42.006  1.257   1.00 8.72  ? 245  PHE A O   1 
ATOM   1843 C  CB  . PHE A 1 245  ? 28.366 42.074  0.416   1.00 8.38  ? 245  PHE A CB  1 
ATOM   1844 C  CG  . PHE A 1 245  ? 28.529 43.546  0.473   1.00 7.99  ? 245  PHE A CG  1 
ATOM   1845 C  CD1 . PHE A 1 245  ? 29.472 44.193  -0.338  1.00 8.48  ? 245  PHE A CD1 1 
ATOM   1846 C  CD2 . PHE A 1 245  ? 27.720 44.298  1.316   1.00 8.82  ? 245  PHE A CD2 1 
ATOM   1847 C  CE1 . PHE A 1 245  ? 29.617 45.622  -0.335  1.00 8.27  ? 245  PHE A CE1 1 
ATOM   1848 C  CE2 . PHE A 1 245  ? 27.848 45.726  1.360   1.00 8.82  ? 245  PHE A CE2 1 
ATOM   1849 C  CZ  . PHE A 1 245  ? 28.816 46.367  0.505   1.00 8.35  ? 245  PHE A CZ  1 
ATOM   1850 N  N   . LEU A 1 246  ? 30.940 40.398  -0.169  1.00 8.01  ? 246  LEU A N   1 
ATOM   1851 C  CA  . LEU A 1 246  ? 32.216 40.328  -0.882  1.00 8.14  ? 246  LEU A CA  1 
ATOM   1852 C  C   . LEU A 1 246  ? 32.045 41.248  -2.083  1.00 7.74  ? 246  LEU A C   1 
ATOM   1853 O  O   . LEU A 1 246  ? 31.381 40.920  -3.089  1.00 8.34  ? 246  LEU A O   1 
ATOM   1854 C  CB  . LEU A 1 246  ? 32.505 38.862  -1.300  1.00 9.55  ? 246  LEU A CB  1 
ATOM   1855 C  CG  . LEU A 1 246  ? 32.818 38.029  -0.033  1.00 12.22 ? 246  LEU A CG  1 
ATOM   1856 C  CD1 . LEU A 1 246  ? 32.666 36.534  -0.372  1.00 15.68 ? 246  LEU A CD1 1 
ATOM   1857 C  CD2 . LEU A 1 246  ? 34.261 38.333  0.378   1.00 15.63 ? 246  LEU A CD2 1 
ATOM   1858 N  N   . TRP A 1 247  ? 32.668 42.415  -1.992  1.00 8.06  ? 247  TRP A N   1 
ATOM   1859 C  CA  . TRP A 1 247  ? 32.494 43.454  -3.027  1.00 7.85  ? 247  TRP A CA  1 
ATOM   1860 C  C   . TRP A 1 247  ? 33.524 43.262  -4.121  1.00 7.40  ? 247  TRP A C   1 
ATOM   1861 O  O   . TRP A 1 247  ? 34.725 43.459  -3.903  1.00 7.67  ? 247  TRP A O   1 
ATOM   1862 C  CB  . TRP A 1 247  ? 32.634 44.815  -2.325  1.00 7.37  ? 247  TRP A CB  1 
ATOM   1863 C  CG  . TRP A 1 247  ? 32.212 46.003  -3.180  1.00 5.99  ? 247  TRP A CG  1 
ATOM   1864 C  CD1 . TRP A 1 247  ? 31.673 45.991  -4.426  1.00 6.79  ? 247  TRP A CD1 1 
ATOM   1865 C  CD2 . TRP A 1 247  ? 32.220 47.366  -2.757  1.00 7.40  ? 247  TRP A CD2 1 
ATOM   1866 N  NE1 . TRP A 1 247  ? 31.310 47.299  -4.816  1.00 6.86  ? 247  TRP A NE1 1 
ATOM   1867 C  CE2 . TRP A 1 247  ? 31.640 48.147  -3.800  1.00 6.63  ? 247  TRP A CE2 1 
ATOM   1868 C  CE3 . TRP A 1 247  ? 32.664 48.016  -1.598  1.00 7.81  ? 247  TRP A CE3 1 
ATOM   1869 C  CZ2 . TRP A 1 247  ? 31.506 49.527  -3.712  1.00 7.85  ? 247  TRP A CZ2 1 
ATOM   1870 C  CZ3 . TRP A 1 247  ? 32.528 49.390  -1.522  1.00 6.84  ? 247  TRP A CZ3 1 
ATOM   1871 C  CH2 . TRP A 1 247  ? 31.966 50.135  -2.553  1.00 6.93  ? 247  TRP A CH2 1 
ATOM   1872 N  N   . ARG A 1 248  ? 33.028 42.829  -5.297  1.00 7.98  ? 248  ARG A N   1 
ATOM   1873 C  CA  . ARG A 1 248  ? 33.910 42.668  -6.459  1.00 7.87  ? 248  ARG A CA  1 
ATOM   1874 C  C   . ARG A 1 248  ? 33.623 43.739  -7.489  1.00 6.37  ? 248  ARG A C   1 
ATOM   1875 O  O   . ARG A 1 248  ? 32.591 44.388  -7.453  1.00 7.55  ? 248  ARG A O   1 
ATOM   1876 C  CB  . ARG A 1 248  ? 33.686 41.287  -7.128  1.00 8.22  ? 248  ARG A CB  1 
ATOM   1877 C  CG  . ARG A 1 248  ? 32.298 41.123  -7.754  1.00 8.94  ? 248  ARG A CG  1 
ATOM   1878 C  CD  . ARG A 1 248  ? 32.254 39.809  -8.582  1.00 10.80 ? 248  ARG A CD  1 
ATOM   1879 N  NE  . ARG A 1 248  ? 32.299 38.654  -7.697  1.00 11.02 ? 248  ARG A NE  1 
ATOM   1880 C  CZ  . ARG A 1 248  ? 32.247 37.402  -8.129  1.00 12.26 ? 248  ARG A CZ  1 
ATOM   1881 N  NH1 . ARG A 1 248  ? 32.194 37.165  -9.444  1.00 13.37 ? 248  ARG A NH1 1 
ATOM   1882 N  NH2 . ARG A 1 248  ? 32.172 36.419  -7.247  1.00 13.35 ? 248  ARG A NH2 1 
ATOM   1883 N  N   . GLN A 1 249  ? 34.551 43.855  -8.445  1.00 7.53  ? 249  GLN A N   1 
ATOM   1884 C  CA  . GLN A 1 249  ? 34.356 44.852  -9.516  1.00 7.75  ? 249  GLN A CA  1 
ATOM   1885 C  C   . GLN A 1 249  ? 33.242 44.394  -10.471 1.00 7.88  ? 249  GLN A C   1 
ATOM   1886 O  O   . GLN A 1 249  ? 32.990 43.184  -10.644 1.00 8.60  ? 249  GLN A O   1 
ATOM   1887 C  CB  . GLN A 1 249  ? 35.686 45.034  -10.289 1.00 8.41  ? 249  GLN A CB  1 
ATOM   1888 C  CG  . GLN A 1 249  ? 36.823 45.536  -9.337  1.00 8.20  ? 249  GLN A CG  1 
ATOM   1889 C  CD  . GLN A 1 249  ? 36.420 46.836  -8.612  1.00 7.93  ? 249  GLN A CD  1 
ATOM   1890 O  OE1 . GLN A 1 249  ? 36.402 46.893  -7.333  1.00 9.68  ? 249  GLN A OE1 1 
ATOM   1891 N  NE2 . GLN A 1 249  ? 36.074 47.846  -9.348  1.00 6.94  ? 249  GLN A NE2 1 
ATOM   1892 N  N   . ILE A 1 250  ? 32.594 45.368  -11.108 1.00 8.43  ? 250  ILE A N   1 
ATOM   1893 C  CA  . ILE A 1 250  ? 31.465 45.078  -11.982 1.00 8.84  ? 250  ILE A CA  1 
ATOM   1894 C  C   . ILE A 1 250  ? 31.776 44.140  -13.154 1.00 9.11  ? 250  ILE A C   1 
ATOM   1895 O  O   . ILE A 1 250  ? 30.849 43.483  -13.616 1.00 10.41 ? 250  ILE A O   1 
ATOM   1896 C  CB  . ILE A 1 250  ? 30.766 46.395  -12.508 1.00 9.28  ? 250  ILE A CB  1 
ATOM   1897 C  CG1 . ILE A 1 250  ? 31.769 47.276  -13.230 1.00 9.96  ? 250  ILE A CG1 1 
ATOM   1898 C  CG2 . ILE A 1 250  ? 30.073 47.121  -11.352 1.00 10.55 ? 250  ILE A CG2 1 
ATOM   1899 C  CD1 . ILE A 1 250  ? 31.125 48.598  -13.745 1.00 12.23 ? 250  ILE A CD1 1 
ATOM   1900 N  N   . TRP A 1 251  ? 33.025 44.080  -13.592 1.00 9.91  ? 251  TRP A N   1 
ATOM   1901 C  CA  . TRP A 1 251  ? 33.378 43.212  -14.739 1.00 11.63 ? 251  TRP A CA  1 
ATOM   1902 C  C   . TRP A 1 251  ? 34.017 41.921  -14.305 1.00 13.89 ? 251  TRP A C   1 
ATOM   1903 O  O   . TRP A 1 251  ? 34.331 41.093  -15.147 1.00 14.38 ? 251  TRP A O   1 
ATOM   1904 C  CB  . TRP A 1 251  ? 34.375 43.939  -15.635 1.00 12.48 ? 251  TRP A CB  1 
ATOM   1905 C  CG  . TRP A 1 251  ? 35.613 44.092  -14.938 1.00 14.72 ? 251  TRP A CG  1 
ATOM   1906 C  CD1 . TRP A 1 251  ? 36.588 43.124  -14.741 1.00 16.07 ? 251  TRP A CD1 1 
ATOM   1907 C  CD2 . TRP A 1 251  ? 36.028 45.225  -14.252 1.00 14.58 ? 251  TRP A CD2 1 
ATOM   1908 N  NE1 . TRP A 1 251  ? 37.568 43.616  -13.966 1.00 15.23 ? 251  TRP A NE1 1 
ATOM   1909 C  CE2 . TRP A 1 251  ? 37.268 44.911  -13.640 1.00 13.94 ? 251  TRP A CE2 1 
ATOM   1910 C  CE3 . TRP A 1 251  ? 35.487 46.480  -14.064 1.00 13.63 ? 251  TRP A CE3 1 
ATOM   1911 C  CZ2 . TRP A 1 251  ? 37.976 45.811  -12.856 1.00 14.49 ? 251  TRP A CZ2 1 
ATOM   1912 C  CZ3 . TRP A 1 251  ? 36.178 47.395  -13.263 1.00 15.34 ? 251  TRP A CZ3 1 
ATOM   1913 C  CH2 . TRP A 1 251  ? 37.412 47.053  -12.676 1.00 16.28 ? 251  TRP A CH2 1 
ATOM   1914 N  N   . ASP A 1 252  ? 34.163 41.691  -13.003 1.00 12.88 ? 252  ASP A N   1 
ATOM   1915 C  CA  . ASP A 1 252  ? 34.901 40.524  -12.497 1.00 13.76 ? 252  ASP A CA  1 
ATOM   1916 C  C   . ASP A 1 252  ? 34.075 39.256  -12.379 1.00 13.73 ? 252  ASP A C   1 
ATOM   1917 O  O   . ASP A 1 252  ? 33.343 39.021  -11.450 1.00 14.07 ? 252  ASP A O   1 
ATOM   1918 C  CB  . ASP A 1 252  ? 35.542 40.942  -11.160 1.00 13.45 ? 252  ASP A CB  1 
ATOM   1919 C  CG  . ASP A 1 252  ? 36.282 39.815  -10.499 1.00 15.81 ? 252  ASP A CG  1 
ATOM   1920 O  OD1 . ASP A 1 252  ? 36.547 38.796  -11.191 1.00 17.56 ? 252  ASP A OD1 1 
ATOM   1921 O  OD2 . ASP A 1 252  ? 36.574 39.960  -9.295  1.00 13.57 ? 252  ASP A OD2 1 
ATOM   1922 N  N   . ASN A 1 253  ? 34.220 38.396  -13.377 1.00 15.04 ? 253  ASN A N   1 
ATOM   1923 C  CA  . ASN A 1 253  ? 33.451 37.194  -13.446 1.00 15.45 ? 253  ASN A CA  1 
ATOM   1924 C  C   . ASN A 1 253  ? 33.852 36.149  -12.411 1.00 15.54 ? 253  ASN A C   1 
ATOM   1925 O  O   . ASN A 1 253  ? 33.003 35.492  -11.834 1.00 16.88 ? 253  ASN A O   1 
ATOM   1926 C  CB  . ASN A 1 253  ? 33.647 36.598  -14.840 1.00 18.46 ? 253  ASN A CB  1 
ATOM   1927 C  CG  . ASN A 1 253  ? 32.841 35.386  -15.048 1.00 21.46 ? 253  ASN A CG  1 
ATOM   1928 O  OD1 . ASN A 1 253  ? 33.383 34.345  -15.482 1.00 24.92 ? 253  ASN A OD1 1 
ATOM   1929 N  ND2 . ASN A 1 253  ? 31.548 35.462  -14.765 1.00 20.73 ? 253  ASN A ND2 1 
ATOM   1930 N  N   . LYS A 1 254  ? 35.140 36.063  -12.184 1.00 18.16 ? 254  LYS A N   1 
ATOM   1931 C  CA  . LYS A 1 254  ? 35.725 35.066  -11.278 1.00 19.39 ? 254  LYS A CA  1 
ATOM   1932 C  C   . LYS A 1 254  ? 35.637 35.422  -9.801  1.00 19.31 ? 254  LYS A C   1 
ATOM   1933 O  O   . LYS A 1 254  ? 35.438 34.547  -8.945  1.00 20.52 ? 254  LYS A O   1 
ATOM   1934 C  CB  . LYS A 1 254  ? 37.192 34.875  -11.668 1.00 23.08 ? 254  LYS A CB  1 
ATOM   1935 C  CG  . LYS A 1 254  ? 37.829 33.615  -11.157 1.00 26.56 ? 254  LYS A CG  1 
ATOM   1936 C  CD  . LYS A 1 254  ? 39.250 33.489  -11.724 1.00 28.96 ? 254  LYS A CD  1 
ATOM   1937 C  CE  . LYS A 1 254  ? 40.056 32.360  -11.047 1.00 29.92 ? 254  LYS A CE  1 
ATOM   1938 N  NZ  . LYS A 1 254  ? 40.033 32.382  -9.545  1.00 31.35 ? 254  LYS A NZ  1 
ATOM   1939 N  N   . GLY A 1 255  ? 35.787 36.709  -9.519  1.00 17.48 ? 255  GLY A N   1 
ATOM   1940 C  CA  . GLY A 1 255  ? 35.741 37.183  -8.146  1.00 15.81 ? 255  GLY A CA  1 
ATOM   1941 C  C   . GLY A 1 255  ? 37.103 37.442  -7.503  1.00 15.46 ? 255  GLY A C   1 
ATOM   1942 O  O   . GLY A 1 255  ? 37.134 37.701  -6.307  1.00 14.80 ? 255  GLY A O   1 
ATOM   1943 N  N   . ASP A 1 256  ? 38.205 37.426  -8.243  1.00 15.26 ? 256  ASP A N   1 
ATOM   1944 C  CA  . ASP A 1 256  ? 39.502 37.655  -7.611  1.00 16.23 ? 256  ASP A CA  1 
ATOM   1945 C  C   . ASP A 1 256  ? 39.698 39.065  -7.069  1.00 14.63 ? 256  ASP A C   1 
ATOM   1946 O  O   . ASP A 1 256  ? 40.602 39.304  -6.265  1.00 15.04 ? 256  ASP A O   1 
ATOM   1947 C  CB  . ASP A 1 256  ? 40.659 37.338  -8.567  1.00 18.82 ? 256  ASP A CB  1 
ATOM   1948 C  CG  A ASP A 1 256  ? 40.667 35.893  -9.023  0.50 20.65 ? 256  ASP A CG  1 
ATOM   1949 C  CG  B ASP A 1 256  ? 40.147 37.362  -10.107 0.50 20.80 ? 256  ASP A CG  1 
ATOM   1950 O  OD1 A ASP A 1 256  ? 40.167 35.024  -8.280  0.50 22.41 ? 256  ASP A OD1 1 
ATOM   1951 O  OD1 B ASP A 1 256  ? 39.567 38.370  -10.552 0.50 21.58 ? 256  ASP A OD1 1 
ATOM   1952 O  OD2 A ASP A 1 256  ? 41.197 35.643  -10.123 0.50 21.95 ? 256  ASP A OD2 1 
ATOM   1953 O  OD2 B ASP A 1 256  ? 40.368 36.344  -10.804 0.50 23.20 ? 256  ASP A OD2 1 
ATOM   1954 N  N   . THR A 1 257  ? 38.862 40.010  -7.495  1.00 12.89 ? 257  THR A N   1 
ATOM   1955 C  CA  . THR A 1 257  ? 38.996 41.363  -6.963  1.00 11.88 ? 257  THR A CA  1 
ATOM   1956 C  C   . THR A 1 257  ? 38.189 41.552  -5.666  1.00 11.30 ? 257  THR A C   1 
ATOM   1957 O  O   . THR A 1 257  ? 38.294 42.630  -5.045  1.00 11.26 ? 257  THR A O   1 
ATOM   1958 C  CB  . THR A 1 257  ? 38.459 42.460  -7.935  1.00 11.30 ? 257  THR A CB  1 
ATOM   1959 O  OG1 . THR A 1 257  ? 37.039 42.268  -8.149  1.00 10.96 ? 257  THR A OG1 1 
ATOM   1960 C  CG2 . THR A 1 257  ? 39.222 42.342  -9.274  1.00 13.46 ? 257  THR A CG2 1 
ATOM   1961 N  N   . ALA A 1 258  ? 37.435 40.527  -5.239  1.00 11.06 ? 258  ALA A N   1 
ATOM   1962 C  CA  . ALA A 1 258  ? 36.565 40.671  -4.063  1.00 10.67 ? 258  ALA A CA  1 
ATOM   1963 C  C   . ALA A 1 258  ? 37.244 41.057  -2.790  1.00 9.62  ? 258  ALA A C   1 
ATOM   1964 O  O   . ALA A 1 258  ? 38.323 40.568  -2.469  1.00 10.73 ? 258  ALA A O   1 
ATOM   1965 C  CB  . ALA A 1 258  ? 35.795 39.395  -3.756  1.00 12.01 ? 258  ALA A CB  1 
ATOM   1966 N  N   . LEU A 1 259  ? 36.604 41.968  -2.078  1.00 8.15  ? 259  LEU A N   1 
ATOM   1967 C  CA  . LEU A 1 259  ? 37.079 42.395  -0.747  1.00 7.79  ? 259  LEU A CA  1 
ATOM   1968 C  C   . LEU A 1 259  ? 35.887 42.390  0.207   1.00 7.40  ? 259  LEU A C   1 
ATOM   1969 O  O   . LEU A 1 259  ? 34.842 43.019  -0.062  1.00 7.37  ? 259  LEU A O   1 
ATOM   1970 C  CB  . LEU A 1 259  ? 37.681 43.814  -0.814  1.00 9.16  ? 259  LEU A CB  1 
ATOM   1971 C  CG  . LEU A 1 259  ? 38.424 44.234  0.470   1.00 8.32  ? 259  LEU A CG  1 
ATOM   1972 C  CD1 . LEU A 1 259  ? 39.697 43.343  0.725   1.00 10.05 ? 259  LEU A CD1 1 
ATOM   1973 C  CD2 . LEU A 1 259  ? 38.877 45.721  0.287   1.00 9.65  ? 259  LEU A CD2 1 
ATOM   1974 N  N   . PHE A 1 260  ? 36.040 41.738  1.363   1.00 7.57  ? 260  PHE A N   1 
ATOM   1975 C  CA  . PHE A 1 260  ? 34.962 41.697  2.335   1.00 7.31  ? 260  PHE A CA  1 
ATOM   1976 C  C   . PHE A 1 260  ? 34.656 43.112  2.819   1.00 7.24  ? 260  PHE A C   1 
ATOM   1977 O  O   . PHE A 1 260  ? 35.588 43.852  3.247   1.00 7.65  ? 260  PHE A O   1 
ATOM   1978 C  CB  . PHE A 1 260  ? 35.404 40.811  3.519   1.00 8.03  ? 260  PHE A CB  1 
ATOM   1979 C  CG  . PHE A 1 260  ? 34.298 40.640  4.546   1.00 8.89  ? 260  PHE A CG  1 
ATOM   1980 C  CD1 . PHE A 1 260  ? 33.309 39.666  4.333   1.00 10.01 ? 260  PHE A CD1 1 
ATOM   1981 C  CD2 . PHE A 1 260  ? 34.227 41.424  5.682   1.00 8.65  ? 260  PHE A CD2 1 
ATOM   1982 C  CE1 . PHE A 1 260  ? 32.253 39.481  5.283   1.00 11.24 ? 260  PHE A CE1 1 
ATOM   1983 C  CE2 . PHE A 1 260  ? 33.188 41.263  6.630   1.00 10.36 ? 260  PHE A CE2 1 
ATOM   1984 C  CZ  . PHE A 1 260  ? 32.219 40.303  6.435   1.00 11.04 ? 260  PHE A CZ  1 
ATOM   1985 N  N   . THR A 1 261  ? 33.378 43.479  2.813   1.00 6.72  ? 261  THR A N   1 
ATOM   1986 C  CA  . THR A 1 261  ? 32.965 44.833  3.130   1.00 7.29  ? 261  THR A CA  1 
ATOM   1987 C  C   . THR A 1 261  ? 31.846 44.787  4.146   1.00 7.06  ? 261  THR A C   1 
ATOM   1988 O  O   . THR A 1 261  ? 30.899 43.996  4.028   1.00 8.07  ? 261  THR A O   1 
ATOM   1989 C  CB  . THR A 1 261  ? 32.441 45.544  1.844   1.00 8.16  ? 261  THR A CB  1 
ATOM   1990 O  OG1 . THR A 1 261  ? 33.516 45.587  0.885   1.00 8.06  ? 261  THR A OG1 1 
ATOM   1991 C  CG2 . THR A 1 261  ? 31.932 46.956  2.144   1.00 8.39  ? 261  THR A CG2 1 
ATOM   1992 N  N   . HIS A 1 262  ? 31.955 45.650  5.154   1.00 7.15  ? 262  HIS A N   1 
ATOM   1993 C  CA  . HIS A 1 262  ? 30.902 45.837  6.150   1.00 7.31  ? 262  HIS A CA  1 
ATOM   1994 C  C   . HIS A 1 262  ? 30.253 47.192  5.958   1.00 7.51  ? 262  HIS A C   1 
ATOM   1995 O  O   . HIS A 1 262  ? 30.956 48.226  6.060   1.00 7.84  ? 262  HIS A O   1 
ATOM   1996 C  CB  . HIS A 1 262  ? 31.528 45.788  7.564   1.00 7.71  ? 262  HIS A CB  1 
ATOM   1997 C  CG  . HIS A 1 262  ? 30.569 46.148  8.674   1.00 7.05  ? 262  HIS A CG  1 
ATOM   1998 N  ND1 . HIS A 1 262  ? 29.934 45.185  9.442   1.00 7.98  ? 262  HIS A ND1 1 
ATOM   1999 C  CD2 . HIS A 1 262  ? 30.141 47.354  9.146   1.00 7.83  ? 262  HIS A CD2 1 
ATOM   2000 C  CE1 . HIS A 1 262  ? 29.167 45.803  10.351  1.00 9.03  ? 262  HIS A CE1 1 
ATOM   2001 N  NE2 . HIS A 1 262  ? 29.265 47.108  10.189  1.00 8.68  ? 262  HIS A NE2 1 
ATOM   2002 N  N   . MET A 1 263  ? 28.950 47.240  5.679   1.00 7.19  ? 263  MET A N   1 
ATOM   2003 C  CA  . MET A 1 263  ? 28.250 48.509  5.614   1.00 7.17  ? 263  MET A CA  1 
ATOM   2004 C  C   . MET A 1 263  ? 27.504 48.708  6.939   1.00 7.71  ? 263  MET A C   1 
ATOM   2005 O  O   . MET A 1 263  ? 26.733 47.795  7.369   1.00 8.50  ? 263  MET A O   1 
ATOM   2006 C  CB  . MET A 1 263  ? 27.216 48.468  4.476   1.00 8.03  ? 263  MET A CB  1 
ATOM   2007 C  CG  . MET A 1 263  ? 26.420 49.777  4.329   1.00 8.53  ? 263  MET A CG  1 
ATOM   2008 S  SD  . MET A 1 263  ? 25.039 49.585  3.110   1.00 8.69  ? 263  MET A SD  1 
ATOM   2009 C  CE  . MET A 1 263  ? 25.917 49.150  1.579   1.00 10.51 ? 263  MET A CE  1 
ATOM   2010 N  N   . MET A 1 264  ? 27.721 49.850  7.584   1.00 7.44  ? 264  MET A N   1 
ATOM   2011 C  CA  . MET A 1 264  ? 27.022 50.142  8.842   1.00 8.43  ? 264  MET A CA  1 
ATOM   2012 C  C   . MET A 1 264  ? 25.553 50.371  8.440   1.00 8.42  ? 264  MET A C   1 
ATOM   2013 O  O   . MET A 1 264  ? 25.244 50.835  7.323   1.00 8.76  ? 264  MET A O   1 
ATOM   2014 C  CB  . MET A 1 264  ? 27.694 51.292  9.581   1.00 8.53  ? 264  MET A CB  1 
ATOM   2015 C  CG  A MET A 1 264  ? 29.045 51.132  9.936   0.50 7.86  ? 264  MET A CG  1 
ATOM   2016 C  CG  B MET A 1 264  ? 29.140 50.888  9.943   0.50 9.16  ? 264  MET A CG  1 
ATOM   2017 S  SD  A MET A 1 264  ? 30.066 52.598  10.387  0.50 7.76  ? 264  MET A SD  1 
ATOM   2018 S  SD  B MET A 1 264  ? 29.737 51.596  11.486  0.50 11.33 ? 264  MET A SD  1 
ATOM   2019 C  CE  A MET A 1 264  ? 28.962 53.515  11.546  0.50 10.44 ? 264  MET A CE  1 
ATOM   2020 C  CE  B MET A 1 264  ? 29.483 53.366  11.075  0.50 10.79 ? 264  MET A CE  1 
ATOM   2021 N  N   . PRO A 1 265  ? 24.613 50.079  9.349   1.00 8.17  ? 265  PRO A N   1 
ATOM   2022 C  CA  . PRO A 1 265  ? 23.199 50.187  9.034   1.00 8.93  ? 265  PRO A CA  1 
ATOM   2023 C  C   . PRO A 1 265  ? 22.357 51.378  9.203   1.00 8.74  ? 265  PRO A C   1 
ATOM   2024 O  O   . PRO A 1 265  ? 21.264 51.463  8.635   1.00 9.47  ? 265  PRO A O   1 
ATOM   2025 C  CB  . PRO A 1 265  ? 22.556 49.178  9.987   1.00 10.45 ? 265  PRO A CB  1 
ATOM   2026 C  CG  . PRO A 1 265  ? 23.469 49.144  11.165  1.00 10.40 ? 265  PRO A CG  1 
ATOM   2027 C  CD  . PRO A 1 265  ? 24.839 49.472  10.641  1.00 8.10  ? 265  PRO A CD  1 
ATOM   2028 N  N   . PHE A 1 266  ? 22.881 52.299  9.986   1.00 9.08  ? 266  PHE A N   1 
ATOM   2029 C  CA  . PHE A 1 266  ? 22.100 53.432  10.435  1.00 9.61  ? 266  PHE A CA  1 
ATOM   2030 C  C   . PHE A 1 266  ? 22.461 54.768  9.856   1.00 8.73  ? 266  PHE A C   1 
ATOM   2031 O  O   . PHE A 1 266  ? 23.355 54.846  9.011   1.00 9.43  ? 266  PHE A O   1 
ATOM   2032 C  CB  . PHE A 1 266  ? 22.101 53.417  11.979  1.00 10.00 ? 266  PHE A CB  1 
ATOM   2033 C  CG  . PHE A 1 266  ? 21.549 52.111  12.592  1.00 9.51  ? 266  PHE A CG  1 
ATOM   2034 C  CD1 . PHE A 1 266  ? 20.393 51.480  12.074  1.00 10.14 ? 266  PHE A CD1 1 
ATOM   2035 C  CD2 . PHE A 1 266  ? 22.184 51.549  13.680  1.00 9.46  ? 266  PHE A CD2 1 
ATOM   2036 C  CE1 . PHE A 1 266  ? 19.911 50.283  12.674  1.00 10.59 ? 266  PHE A CE1 1 
ATOM   2037 C  CE2 . PHE A 1 266  ? 21.707 50.356  14.270  1.00 10.40 ? 266  PHE A CE2 1 
ATOM   2038 C  CZ  . PHE A 1 266  ? 20.565 49.739  13.748  1.00 10.00 ? 266  PHE A CZ  1 
ATOM   2039 N  N   . TYR A 1 267  ? 21.802 55.810  10.297  1.00 9.08  ? 267  TYR A N   1 
ATOM   2040 C  CA  . TYR A 1 267  ? 21.909 57.114  9.669   1.00 8.83  ? 267  TYR A CA  1 
ATOM   2041 C  C   . TYR A 1 267  ? 23.241 57.826  9.847   1.00 8.59  ? 267  TYR A C   1 
ATOM   2042 O  O   . TYR A 1 267  ? 23.589 58.668  9.002   1.00 8.41  ? 267  TYR A O   1 
ATOM   2043 C  CB  . TYR A 1 267  ? 20.752 57.956  10.234  1.00 10.19 ? 267  TYR A CB  1 
ATOM   2044 C  CG  . TYR A 1 267  ? 20.842 59.469  10.084  1.00 10.32 ? 267  TYR A CG  1 
ATOM   2045 C  CD1 . TYR A 1 267  ? 20.515 60.104  8.881   1.00 12.28 ? 267  TYR A CD1 1 
ATOM   2046 C  CD2 . TYR A 1 267  ? 21.226 60.251  11.171  1.00 12.64 ? 267  TYR A CD2 1 
ATOM   2047 C  CE1 . TYR A 1 267  ? 20.595 61.517  8.769   1.00 13.44 ? 267  TYR A CE1 1 
ATOM   2048 C  CE2 . TYR A 1 267  ? 21.291 61.621  11.085  1.00 13.62 ? 267  TYR A CE2 1 
ATOM   2049 C  CZ  . TYR A 1 267  ? 20.978 62.232  9.901   1.00 14.02 ? 267  TYR A CZ  1 
ATOM   2050 O  OH  . TYR A 1 267  ? 21.037 63.630  9.890   1.00 18.28 ? 267  TYR A OH  1 
ATOM   2051 N  N   . SER A 1 268  ? 23.913 57.562  10.937  1.00 8.31  ? 268  SER A N   1 
ATOM   2052 C  CA  . SER A 1 268  ? 25.192 58.239  11.220  1.00 8.89  ? 268  SER A CA  1 
ATOM   2053 C  C   . SER A 1 268  ? 26.177 57.293  11.894  1.00 9.04  ? 268  SER A C   1 
ATOM   2054 O  O   . SER A 1 268  ? 25.832 56.193  12.327  1.00 8.97  ? 268  SER A O   1 
ATOM   2055 C  CB  . SER A 1 268  ? 24.911 59.427  12.146  1.00 9.92  ? 268  SER A CB  1 
ATOM   2056 O  OG  . SER A 1 268  ? 26.119 60.090  12.515  1.00 12.53 ? 268  SER A OG  1 
ATOM   2057 N  N   . TYR A 1 269  ? 27.457 57.682  11.899  1.00 8.83  ? 269  TYR A N   1 
ATOM   2058 C  CA  . TYR A 1 269  ? 28.468 56.979  12.680  1.00 8.18  ? 269  TYR A CA  1 
ATOM   2059 C  C   . TYR A 1 269  ? 28.577 57.523  14.164  1.00 8.55  ? 269  TYR A C   1 
ATOM   2060 O  O   . TYR A 1 269  ? 29.436 57.049  14.918  1.00 9.06  ? 269  TYR A O   1 
ATOM   2061 C  CB  . TYR A 1 269  ? 29.851 57.164  11.993  1.00 7.68  ? 269  TYR A CB  1 
ATOM   2062 C  CG  . TYR A 1 269  ? 30.248 58.616  11.771  1.00 8.52  ? 269  TYR A CG  1 
ATOM   2063 C  CD1 . TYR A 1 269  ? 30.704 59.429  12.842  1.00 8.88  ? 269  TYR A CD1 1 
ATOM   2064 C  CD2 . TYR A 1 269  ? 30.158 59.178  10.489  1.00 8.63  ? 269  TYR A CD2 1 
ATOM   2065 C  CE1 . TYR A 1 269  ? 31.057 60.789  12.614  1.00 9.93  ? 269  TYR A CE1 1 
ATOM   2066 C  CE2 . TYR A 1 269  ? 30.512 60.522  10.246  1.00 8.86  ? 269  TYR A CE2 1 
ATOM   2067 C  CZ  . TYR A 1 269  ? 30.958 61.302  11.328  1.00 9.32  ? 269  TYR A CZ  1 
ATOM   2068 O  OH  . TYR A 1 269  ? 31.285 62.599  11.101  1.00 9.25  ? 269  TYR A OH  1 
ATOM   2069 N  N   . ASP A 1 270  ? 27.742 58.496  14.553  1.00 8.70  ? 270  ASP A N   1 
ATOM   2070 C  CA  . ASP A 1 270  ? 27.796 59.041  15.918  1.00 9.02  ? 270  ASP A CA  1 
ATOM   2071 C  C   . ASP A 1 270  ? 27.242 58.007  16.904  1.00 8.23  ? 270  ASP A C   1 
ATOM   2072 O  O   . ASP A 1 270  ? 26.712 56.950  16.503  1.00 9.28  ? 270  ASP A O   1 
ATOM   2073 C  CB  . ASP A 1 270  ? 27.124 60.437  15.961  1.00 9.85  ? 270  ASP A CB  1 
ATOM   2074 C  CG  . ASP A 1 270  ? 25.640 60.423  15.757  1.00 10.28 ? 270  ASP A CG  1 
ATOM   2075 O  OD1 . ASP A 1 270  ? 25.015 59.345  15.710  1.00 11.41 ? 270  ASP A OD1 1 
ATOM   2076 O  OD2 . ASP A 1 270  ? 25.088 61.557  15.678  1.00 12.94 ? 270  ASP A OD2 1 
ATOM   2077 N  N   . ILE A 1 271  ? 27.458 58.262  18.186  1.00 8.97  ? 271  ILE A N   1 
ATOM   2078 C  CA  . ILE A 1 271  ? 27.053 57.251  19.194  1.00 9.31  ? 271  ILE A CA  1 
ATOM   2079 C  C   . ILE A 1 271  ? 25.553 56.991  19.175  1.00 8.75  ? 271  ILE A C   1 
ATOM   2080 O  O   . ILE A 1 271  ? 25.158 55.814  19.196  1.00 9.20  ? 271  ILE A O   1 
ATOM   2081 C  CB  . ILE A 1 271  ? 27.624 57.631  20.553  1.00 9.43  ? 271  ILE A CB  1 
ATOM   2082 C  CG1 . ILE A 1 271  ? 29.141 57.499  20.454  1.00 9.69  ? 271  ILE A CG1 1 
ATOM   2083 C  CG2 . ILE A 1 271  ? 27.058 56.671  21.663  1.00 10.38 ? 271  ILE A CG2 1 
ATOM   2084 C  CD1 . ILE A 1 271  ? 29.891 58.164  21.634  1.00 9.88  ? 271  ILE A CD1 1 
ATOM   2085 N  N   . PRO A 1 272  ? 24.701 58.021  19.007  1.00 9.00  ? 272  PRO A N   1 
ATOM   2086 C  CA  . PRO A 1 272  ? 23.243 57.722  18.969  1.00 9.89  ? 272  PRO A CA  1 
ATOM   2087 C  C   . PRO A 1 272  ? 22.838 56.792  17.845  1.00 10.63 ? 272  PRO A C   1 
ATOM   2088 O  O   . PRO A 1 272  ? 21.792 56.118  17.942  1.00 11.02 ? 272  PRO A O   1 
ATOM   2089 C  CB  . PRO A 1 272  ? 22.565 59.093  18.798  1.00 10.92 ? 272  PRO A CB  1 
ATOM   2090 C  CG  . PRO A 1 272  ? 23.567 60.032  19.503  1.00 11.01 ? 272  PRO A CG  1 
ATOM   2091 C  CD  . PRO A 1 272  ? 24.959 59.476  19.106  1.00 9.96  ? 272  PRO A CD  1 
ATOM   2092 N  N   . HIS A 1 273  ? 23.650 56.702  16.781  1.00 9.66  ? 273  HIS A N   1 
ATOM   2093 C  CA  . HIS A 1 273  ? 23.274 55.837  15.637  1.00 9.05  ? 273  HIS A CA  1 
ATOM   2094 C  C   . HIS A 1 273  ? 24.201 54.658  15.444  1.00 9.45  ? 273  HIS A C   1 
ATOM   2095 O  O   . HIS A 1 273  ? 24.244 54.050  14.349  1.00 10.07 ? 273  HIS A O   1 
ATOM   2096 C  CB  . HIS A 1 273  ? 23.133 56.666  14.328  1.00 9.33  ? 273  HIS A CB  1 
ATOM   2097 C  CG  . HIS A 1 273  ? 22.137 57.779  14.450  1.00 9.56  ? 273  HIS A CG  1 
ATOM   2098 N  ND1 . HIS A 1 273  ? 20.787 57.694  14.115  1.00 11.76 ? 273  HIS A ND1 1 
ATOM   2099 C  CD2 . HIS A 1 273  ? 22.325 59.020  14.948  1.00 8.60  ? 273  HIS A CD2 1 
ATOM   2100 C  CE1 . HIS A 1 273  ? 20.206 58.849  14.412  1.00 7.91  ? 273  HIS A CE1 1 
ATOM   2101 N  NE2 . HIS A 1 273  ? 21.108 59.667  14.923  1.00 12.20 ? 273  HIS A NE2 1 
ATOM   2102 N  N   . THR A 1 274  ? 24.922 54.285  16.498  1.00 8.96  ? 274  THR A N   1 
ATOM   2103 C  CA  . THR A 1 274  ? 25.771 53.119  16.405  1.00 9.28  ? 274  THR A CA  1 
ATOM   2104 C  C   . THR A 1 274  ? 25.560 52.026  17.452  1.00 9.11  ? 274  THR A C   1 
ATOM   2105 O  O   . THR A 1 274  ? 26.084 50.952  17.316  1.00 10.36 ? 274  THR A O   1 
ATOM   2106 C  CB  . THR A 1 274  ? 27.275 53.511  16.361  1.00 9.89  ? 274  THR A CB  1 
ATOM   2107 O  OG1 . THR A 1 274  ? 27.550 54.468  17.397  1.00 9.82  ? 274  THR A OG1 1 
ATOM   2108 C  CG2 . THR A 1 274  ? 27.644 54.105  14.988  1.00 10.44 ? 274  THR A CG2 1 
ATOM   2109 N  N   . CYS A 1 275  ? 24.779 52.291  18.503  1.00 10.42 ? 275  CYS A N   1 
ATOM   2110 C  CA  . CYS A 1 275  ? 24.584 51.195  19.452  1.00 10.78 ? 275  CYS A CA  1 
ATOM   2111 C  C   . CYS A 1 275  ? 23.408 50.276  19.082  1.00 10.04 ? 275  CYS A C   1 
ATOM   2112 O  O   . CYS A 1 275  ? 23.350 49.135  19.558  1.00 11.82 ? 275  CYS A O   1 
ATOM   2113 C  CB  . CYS A 1 275  ? 24.314 51.781  20.861  1.00 11.70 ? 275  CYS A CB  1 
ATOM   2114 S  SG  . CYS A 1 275  ? 22.582 51.887  21.439  1.00 13.29 ? 275  CYS A SG  1 
ATOM   2115 N  N   . GLY A 1 276  ? 22.534 50.744  18.220  1.00 10.18 ? 276  GLY A N   1 
ATOM   2116 C  CA  . GLY A 1 276  ? 21.310 50.003  17.949  1.00 10.02 ? 276  GLY A CA  1 
ATOM   2117 C  C   . GLY A 1 276  ? 20.390 50.900  17.190  1.00 10.16 ? 276  GLY A C   1 
ATOM   2118 O  O   . GLY A 1 276  ? 20.742 52.056  16.925  1.00 10.97 ? 276  GLY A O   1 
ATOM   2119 N  N   . PRO A 1 277  ? 19.161 50.458  16.882  1.00 10.43 ? 277  PRO A N   1 
ATOM   2120 C  CA  . PRO A 1 277  ? 18.205 51.217  16.113  1.00 11.33 ? 277  PRO A CA  1 
ATOM   2121 C  C   . PRO A 1 277  ? 17.523 52.416  16.702  1.00 10.75 ? 277  PRO A C   1 
ATOM   2122 O  O   . PRO A 1 277  ? 16.953 53.175  15.957  1.00 11.46 ? 277  PRO A O   1 
ATOM   2123 C  CB  . PRO A 1 277  ? 17.169 50.151  15.689  1.00 11.61 ? 277  PRO A CB  1 
ATOM   2124 C  CG  . PRO A 1 277  ? 17.184 49.216  16.954  1.00 11.40 ? 277  PRO A CG  1 
ATOM   2125 C  CD  . PRO A 1 277  ? 18.663 49.105  17.242  1.00 11.31 ? 277  PRO A CD  1 
ATOM   2126 N  N   . ASP A 1 278  ? 17.594 52.557  18.026  1.00 11.21 ? 278  ASP A N   1 
ATOM   2127 C  CA  . ASP A 1 278  ? 16.858 53.664  18.659  1.00 12.39 ? 278  ASP A CA  1 
ATOM   2128 C  C   . ASP A 1 278  ? 17.807 54.713  19.208  1.00 10.94 ? 278  ASP A C   1 
ATOM   2129 O  O   . ASP A 1 278  ? 18.396 54.525  20.275  1.00 12.00 ? 278  ASP A O   1 
ATOM   2130 C  CB  . ASP A 1 278  ? 15.970 53.130  19.805  1.00 13.15 ? 278  ASP A CB  1 
ATOM   2131 C  CG  . ASP A 1 278  ? 15.079 54.219  20.381  1.00 13.90 ? 278  ASP A CG  1 
ATOM   2132 O  OD1 . ASP A 1 278  ? 15.200 55.413  20.026  1.00 14.69 ? 278  ASP A OD1 1 
ATOM   2133 O  OD2 . ASP A 1 278  ? 14.211 53.875  21.233  1.00 16.31 ? 278  ASP A OD2 1 
ATOM   2134 N  N   . PRO A 1 279  ? 17.948 55.833  18.476  1.00 11.86 ? 279  PRO A N   1 
ATOM   2135 C  CA  . PRO A 1 279  ? 18.880 56.881  18.955  1.00 12.97 ? 279  PRO A CA  1 
ATOM   2136 C  C   . PRO A 1 279  ? 18.505 57.513  20.280  1.00 13.11 ? 279  PRO A C   1 
ATOM   2137 O  O   . PRO A 1 279  ? 19.379 58.007  20.948  1.00 12.47 ? 279  PRO A O   1 
ATOM   2138 C  CB  . PRO A 1 279  ? 18.923 57.890  17.780  1.00 12.88 ? 279  PRO A CB  1 
ATOM   2139 C  CG  . PRO A 1 279  ? 17.555 57.797  17.205  1.00 12.58 ? 279  PRO A CG  1 
ATOM   2140 C  CD  . PRO A 1 279  ? 17.215 56.270  17.282  1.00 12.11 ? 279  PRO A CD  1 
ATOM   2141 N  N   . LYS A 1 280  ? 17.215 57.500  20.658  1.00 12.51 ? 280  LYS A N   1 
ATOM   2142 C  CA  . LYS A 1 280  ? 16.852 58.061  21.974  1.00 13.98 ? 280  LYS A CA  1 
ATOM   2143 C  C   . LYS A 1 280  ? 17.482 57.228  23.101  1.00 13.32 ? 280  LYS A C   1 
ATOM   2144 O  O   . LYS A 1 280  ? 17.904 57.748  24.158  1.00 14.33 ? 280  LYS A O   1 
ATOM   2145 C  CB  . LYS A 1 280  ? 15.339 58.067  22.118  1.00 15.66 ? 280  LYS A CB  1 
ATOM   2146 C  CG  . LYS A 1 280  ? 14.834 58.507  23.509  1.00 17.37 ? 280  LYS A CG  1 
ATOM   2147 C  CD  . LYS A 1 280  ? 13.297 58.550  23.394  1.00 20.36 ? 280  LYS A CD  1 
ATOM   2148 C  CE  . LYS A 1 280  ? 12.626 59.047  24.670  1.00 24.55 ? 280  LYS A CE  1 
ATOM   2149 N  NZ  . LYS A 1 280  ? 11.192 59.403  24.366  1.00 26.65 ? 280  LYS A NZ  1 
ATOM   2150 N  N   . VAL A 1 281  ? 17.639 55.918  22.877  1.00 12.80 ? 281  VAL A N   1 
ATOM   2151 C  CA  . VAL A 1 281  ? 18.285 55.063  23.849  1.00 13.31 ? 281  VAL A CA  1 
ATOM   2152 C  C   . VAL A 1 281  ? 19.822 55.127  23.717  1.00 12.35 ? 281  VAL A C   1 
ATOM   2153 O  O   . VAL A 1 281  ? 20.566 55.286  24.696  1.00 11.65 ? 281  VAL A O   1 
ATOM   2154 C  CB  . VAL A 1 281  ? 17.859 53.583  23.675  1.00 13.44 ? 281  VAL A CB  1 
ATOM   2155 C  CG1 . VAL A 1 281  ? 18.699 52.669  24.591  1.00 13.00 ? 281  VAL A CG1 1 
ATOM   2156 C  CG2 . VAL A 1 281  ? 16.307 53.480  23.909  1.00 13.73 ? 281  VAL A CG2 1 
ATOM   2157 N  N   . CYS A 1 282  ? 20.329 55.045  22.466  1.00 12.10 ? 282  CYS A N   1 
ATOM   2158 C  CA  . CYS A 1 282  ? 21.800 55.043  22.304  1.00 12.62 ? 282  CYS A CA  1 
ATOM   2159 C  C   . CYS A 1 282  ? 22.465 56.332  22.793  1.00 10.60 ? 282  CYS A C   1 
ATOM   2160 O  O   . CYS A 1 282  ? 23.612 56.289  23.297  1.00 11.43 ? 282  CYS A O   1 
ATOM   2161 C  CB  . CYS A 1 282  ? 22.185 54.827  20.829  1.00 12.09 ? 282  CYS A CB  1 
ATOM   2162 S  SG  . CYS A 1 282  ? 21.732 53.215  20.158  1.00 12.64 ? 282  CYS A SG  1 
ATOM   2163 N  N   . CYS A 1 283  ? 21.746 57.452  22.628  1.00 11.21 ? 283  CYS A N   1 
ATOM   2164 C  CA  . CYS A 1 283  ? 22.306 58.716  23.059  1.00 11.58 ? 283  CYS A CA  1 
ATOM   2165 C  C   . CYS A 1 283  ? 22.594 58.698  24.553  1.00 12.06 ? 283  CYS A C   1 
ATOM   2166 O  O   . CYS A 1 283  ? 23.472 59.385  25.007  1.00 11.37 ? 283  CYS A O   1 
ATOM   2167 C  CB  . CYS A 1 283  ? 21.335 59.843  22.683  1.00 11.63 ? 283  CYS A CB  1 
ATOM   2168 S  SG  . CYS A 1 283  ? 22.150 61.479  22.815  1.00 13.00 ? 283  CYS A SG  1 
ATOM   2169 N  N   . GLN A 1 284  ? 21.855 57.869  25.309  1.00 11.82 ? 284  GLN A N   1 
ATOM   2170 C  CA  . GLN A 1 284  ? 22.079 57.781  26.739  1.00 11.44 ? 284  GLN A CA  1 
ATOM   2171 C  C   . GLN A 1 284  ? 23.366 57.025  27.114  1.00 11.77 ? 284  GLN A C   1 
ATOM   2172 O  O   . GLN A 1 284  ? 23.736 56.936  28.277  1.00 13.02 ? 284  GLN A O   1 
ATOM   2173 C  CB  . GLN A 1 284  ? 20.869 57.085  27.419  1.00 12.15 ? 284  GLN A CB  1 
ATOM   2174 C  CG  . GLN A 1 284  ? 19.593 57.844  27.254  1.00 14.26 ? 284  GLN A CG  1 
ATOM   2175 C  CD  . GLN A 1 284  ? 18.419 57.048  27.777  1.00 14.10 ? 284  GLN A CD  1 
ATOM   2176 O  OE1 . GLN A 1 284  ? 18.457 56.574  28.911  1.00 17.10 ? 284  GLN A OE1 1 
ATOM   2177 N  NE2 . GLN A 1 284  ? 17.422 56.856  26.945  1.00 15.38 ? 284  GLN A NE2 1 
ATOM   2178 N  N   . PHE A 1 285  ? 24.072 56.499  26.088  1.00 11.19 ? 285  PHE A N   1 
ATOM   2179 C  CA  . PHE A 1 285  ? 25.306 55.793  26.294  1.00 10.55 ? 285  PHE A CA  1 
ATOM   2180 C  C   . PHE A 1 285  ? 26.456 56.564  25.649  1.00 10.62 ? 285  PHE A C   1 
ATOM   2181 O  O   . PHE A 1 285  ? 27.520 56.004  25.432  1.00 10.72 ? 285  PHE A O   1 
ATOM   2182 C  CB  . PHE A 1 285  ? 25.179 54.340  25.836  1.00 11.51 ? 285  PHE A CB  1 
ATOM   2183 C  CG  . PHE A 1 285  ? 24.170 53.575  26.680  1.00 11.68 ? 285  PHE A CG  1 
ATOM   2184 C  CD1 . PHE A 1 285  ? 24.559 52.946  27.868  1.00 11.76 ? 285  PHE A CD1 1 
ATOM   2185 C  CD2 . PHE A 1 285  ? 22.830 53.590  26.315  1.00 12.24 ? 285  PHE A CD2 1 
ATOM   2186 C  CE1 . PHE A 1 285  ? 23.557 52.342  28.690  1.00 12.62 ? 285  PHE A CE1 1 
ATOM   2187 C  CE2 . PHE A 1 285  ? 21.831 52.986  27.128  1.00 12.89 ? 285  PHE A CE2 1 
ATOM   2188 C  CZ  . PHE A 1 285  ? 22.220 52.371  28.312  1.00 13.90 ? 285  PHE A CZ  1 
ATOM   2189 N  N   . ASP A 1 286  ? 26.192 57.841  25.369  1.00 10.22 ? 286  ASP A N   1 
ATOM   2190 C  CA  . ASP A 1 286  ? 27.297 58.758  24.938  1.00 10.22 ? 286  ASP A CA  1 
ATOM   2191 C  C   . ASP A 1 286  ? 27.561 59.594  26.225  1.00 8.74  ? 286  ASP A C   1 
ATOM   2192 O  O   . ASP A 1 286  ? 26.874 60.609  26.437  1.00 11.17 ? 286  ASP A O   1 
ATOM   2193 C  CB  . ASP A 1 286  ? 26.856 59.634  23.796  1.00 10.16 ? 286  ASP A CB  1 
ATOM   2194 C  CG  . ASP A 1 286  ? 27.999 60.508  23.277  1.00 9.16  ? 286  ASP A CG  1 
ATOM   2195 O  OD1 . ASP A 1 286  ? 29.042 60.572  23.986  1.00 9.56  ? 286  ASP A OD1 1 
ATOM   2196 O  OD2 . ASP A 1 286  ? 27.805 61.146  22.203  1.00 10.37 ? 286  ASP A OD2 1 
ATOM   2197 N  N   . PHE A 1 287  ? 28.539 59.165  27.025  1.00 9.75  ? 287  PHE A N   1 
ATOM   2198 C  CA  . PHE A 1 287  ? 28.714 59.815  28.323  1.00 10.72 ? 287  PHE A CA  1 
ATOM   2199 C  C   . PHE A 1 287  ? 29.263 61.195  28.268  1.00 12.28 ? 287  PHE A C   1 
ATOM   2200 O  O   . PHE A 1 287  ? 29.381 61.842  29.297  1.00 13.02 ? 287  PHE A O   1 
ATOM   2201 C  CB  . PHE A 1 287  ? 29.426 58.859  29.312  1.00 11.31 ? 287  PHE A CB  1 
ATOM   2202 C  CG  . PHE A 1 287  ? 28.622 57.575  29.544  1.00 10.56 ? 287  PHE A CG  1 
ATOM   2203 C  CD1 . PHE A 1 287  ? 27.623 57.543  30.530  1.00 11.95 ? 287  PHE A CD1 1 
ATOM   2204 C  CD2 . PHE A 1 287  ? 28.812 56.429  28.786  1.00 11.97 ? 287  PHE A CD2 1 
ATOM   2205 C  CE1 . PHE A 1 287  ? 26.849 56.386  30.733  1.00 12.70 ? 287  PHE A CE1 1 
ATOM   2206 C  CE2 . PHE A 1 287  ? 28.035 55.281  28.991  1.00 12.80 ? 287  PHE A CE2 1 
ATOM   2207 C  CZ  . PHE A 1 287  ? 27.048 55.261  29.980  1.00 13.06 ? 287  PHE A CZ  1 
ATOM   2208 N  N   . LYS A 1 288  ? 29.597 61.694  27.063  1.00 12.40 ? 288  LYS A N   1 
ATOM   2209 C  CA  . LYS A 1 288  ? 29.997 63.096  26.967  1.00 11.97 ? 288  LYS A CA  1 
ATOM   2210 C  C   . LYS A 1 288  ? 28.798 64.026  26.922  1.00 12.68 ? 288  LYS A C   1 
ATOM   2211 O  O   . LYS A 1 288  ? 28.961 65.263  26.946  1.00 13.33 ? 288  LYS A O   1 
ATOM   2212 C  CB  . LYS A 1 288  ? 30.845 63.312  25.672  1.00 12.34 ? 288  LYS A CB  1 
ATOM   2213 C  CG  . LYS A 1 288  ? 31.710 64.599  25.734  1.00 10.25 ? 288  LYS A CG  1 
ATOM   2214 C  CD  . LYS A 1 288  ? 32.447 64.799  24.384  1.00 10.41 ? 288  LYS A CD  1 
ATOM   2215 C  CE  . LYS A 1 288  ? 33.153 66.127  24.558  1.00 11.99 ? 288  LYS A CE  1 
ATOM   2216 N  NZ  . LYS A 1 288  ? 33.909 66.423  23.219  1.00 16.39 ? 288  LYS A NZ  1 
ATOM   2217 N  N   . ARG A 1 289  ? 27.578 63.508  26.856  1.00 13.12 ? 289  ARG A N   1 
ATOM   2218 C  CA  . ARG A 1 289  ? 26.394 64.347  26.751  1.00 15.11 ? 289  ARG A CA  1 
ATOM   2219 C  C   . ARG A 1 289  ? 25.623 64.644  28.077  1.00 16.42 ? 289  ARG A C   1 
ATOM   2220 O  O   . ARG A 1 289  ? 24.430 64.852  28.023  1.00 16.87 ? 289  ARG A O   1 
ATOM   2221 C  CB  . ARG A 1 289  ? 25.431 63.711  25.743  1.00 13.18 ? 289  ARG A CB  1 
ATOM   2222 C  CG  . ARG A 1 289  ? 26.075 63.564  24.352  1.00 13.14 ? 289  ARG A CG  1 
ATOM   2223 C  CD  . ARG A 1 289  ? 25.049 63.136  23.373  1.00 12.49 ? 289  ARG A CD  1 
ATOM   2224 N  NE  . ARG A 1 289  ? 25.590 62.827  22.037  1.00 12.43 ? 289  ARG A NE  1 
ATOM   2225 C  CZ  . ARG A 1 289  ? 25.147 63.378  20.925  1.00 12.50 ? 289  ARG A CZ  1 
ATOM   2226 N  NH1 . ARG A 1 289  ? 24.169 64.287  20.902  1.00 13.97 ? 289  ARG A NH1 1 
ATOM   2227 N  NH2 . ARG A 1 289  ? 25.672 62.977  19.771  1.00 13.28 ? 289  ARG A NH2 1 
ATOM   2228 N  N   . MET A 1 290  ? 26.265 64.659  29.245  1.00 19.93 ? 290  MET A N   1 
ATOM   2229 C  CA  . MET A 1 290  ? 25.426 64.949  30.431  1.00 21.76 ? 290  MET A CA  1 
ATOM   2230 C  C   . MET A 1 290  ? 25.335 66.469  30.846  1.00 22.69 ? 290  MET A C   1 
ATOM   2231 O  O   . MET A 1 290  ? 24.550 66.820  31.802  1.00 24.44 ? 290  MET A O   1 
ATOM   2232 C  CB  . MET A 1 290  ? 25.809 64.002  31.619  1.00 21.51 ? 290  MET A CB  1 
ATOM   2233 C  CG  . MET A 1 290  ? 25.785 62.566  31.287  1.00 22.94 ? 290  MET A CG  1 
ATOM   2234 S  SD  . MET A 1 290  ? 26.276 61.378  32.654  1.00 24.52 ? 290  MET A SD  1 
ATOM   2235 C  CE  . MET A 1 290  ? 28.079 61.438  32.505  1.00 25.47 ? 290  MET A CE  1 
ATOM   2236 N  N   . GLY A 1 291  ? 26.078 67.373  30.148  1.00 23.29 ? 291  GLY A N   1 
ATOM   2237 C  CA  . GLY A 1 291  ? 26.020 68.815  30.438  1.00 21.49 ? 291  GLY A CA  1 
ATOM   2238 C  C   . GLY A 1 291  ? 27.299 69.699  30.587  1.00 21.13 ? 291  GLY A C   1 
ATOM   2239 O  O   . GLY A 1 291  ? 27.406 70.804  30.005  1.00 21.49 ? 291  GLY A O   1 
ATOM   2240 N  N   . SER A 1 292  ? 28.275 69.214  31.361  1.00 19.74 ? 292  SER A N   1 
ATOM   2241 C  CA  . SER A 1 292  ? 29.516 69.951  31.620  1.00 16.22 ? 292  SER A CA  1 
ATOM   2242 C  C   . SER A 1 292  ? 30.380 70.143  30.349  1.00 14.39 ? 292  SER A C   1 
ATOM   2243 O  O   . SER A 1 292  ? 31.272 71.010  30.292  1.00 13.26 ? 292  SER A O   1 
ATOM   2244 C  CB  . SER A 1 292  ? 30.302 69.194  32.692  1.00 17.38 ? 292  SER A CB  1 
ATOM   2245 O  OG  . SER A 1 292  ? 30.804 67.951  32.212  1.00 19.09 ? 292  SER A OG  1 
ATOM   2246 N  N   . PHE A 1 293  ? 30.113 69.319  29.341  1.00 12.76 ? 293  PHE A N   1 
ATOM   2247 C  CA  . PHE A 1 293  ? 30.826 69.415  28.067  1.00 11.99 ? 293  PHE A CA  1 
ATOM   2248 C  C   . PHE A 1 293  ? 30.080 70.235  27.052  1.00 12.75 ? 293  PHE A C   1 
ATOM   2249 O  O   . PHE A 1 293  ? 30.533 70.310  25.902  1.00 12.88 ? 293  PHE A O   1 
ATOM   2250 C  CB  . PHE A 1 293  ? 31.097 67.996  27.434  1.00 13.10 ? 293  PHE A CB  1 
ATOM   2251 C  CG  . PHE A 1 293  ? 32.042 67.129  28.231  1.00 12.93 ? 293  PHE A CG  1 
ATOM   2252 C  CD1 . PHE A 1 293  ? 33.402 67.257  28.066  1.00 13.46 ? 293  PHE A CD1 1 
ATOM   2253 C  CD2 . PHE A 1 293  ? 31.534 66.202  29.141  1.00 14.99 ? 293  PHE A CD2 1 
ATOM   2254 C  CE1 . PHE A 1 293  ? 34.292 66.432  28.818  1.00 15.41 ? 293  PHE A CE1 1 
ATOM   2255 C  CE2 . PHE A 1 293  ? 32.421 65.389  29.894  1.00 16.16 ? 293  PHE A CE2 1 
ATOM   2256 C  CZ  . PHE A 1 293  ? 33.780 65.529  29.706  1.00 15.53 ? 293  PHE A CZ  1 
ATOM   2257 N  N   . GLY A 1 294  ? 28.927 70.778  27.457  1.00 13.20 ? 294  GLY A N   1 
ATOM   2258 C  CA  . GLY A 1 294  ? 28.178 71.602  26.527  1.00 13.98 ? 294  GLY A CA  1 
ATOM   2259 C  C   . GLY A 1 294  ? 27.428 70.808  25.460  1.00 13.32 ? 294  GLY A C   1 
ATOM   2260 O  O   . GLY A 1 294  ? 27.100 71.326  24.379  1.00 13.75 ? 294  GLY A O   1 
ATOM   2261 N  N   . LEU A 1 295  ? 27.168 69.523  25.750  1.00 13.75 ? 295  LEU A N   1 
ATOM   2262 C  CA  . LEU A 1 295  ? 26.447 68.661  24.846  1.00 13.53 ? 295  LEU A CA  1 
ATOM   2263 C  C   . LEU A 1 295  ? 25.208 68.117  25.534  1.00 14.50 ? 295  LEU A C   1 
ATOM   2264 O  O   . LEU A 1 295  ? 25.128 68.078  26.756  1.00 15.59 ? 295  LEU A O   1 
ATOM   2265 C  CB  . LEU A 1 295  ? 27.345 67.499  24.393  1.00 13.75 ? 295  LEU A CB  1 
ATOM   2266 C  CG  . LEU A 1 295  ? 28.666 67.895  23.700  1.00 14.23 ? 295  LEU A CG  1 
ATOM   2267 C  CD1 . LEU A 1 295  ? 29.466 66.648  23.367  1.00 16.25 ? 295  LEU A CD1 1 
ATOM   2268 C  CD2 . LEU A 1 295  ? 28.359 68.653  22.416  1.00 14.95 ? 295  LEU A CD2 1 
ATOM   2269 N  N   . SER A 1 296  ? 24.244 67.719  24.719  1.00 14.88 ? 296  SER A N   1 
ATOM   2270 C  CA  . SER A 1 296  ? 22.999 67.119  25.225  1.00 16.10 ? 296  SER A CA  1 
ATOM   2271 C  C   . SER A 1 296  ? 22.449 66.145  24.183  1.00 16.29 ? 296  SER A C   1 
ATOM   2272 O  O   . SER A 1 296  ? 23.002 66.018  23.084  1.00 14.45 ? 296  SER A O   1 
ATOM   2273 C  CB  . SER A 1 296  ? 21.998 68.254  25.553  1.00 17.21 ? 296  SER A CB  1 
ATOM   2274 O  OG  . SER A 1 296  ? 21.666 69.015  24.403  1.00 18.66 ? 296  SER A OG  1 
ATOM   2275 N  N   . CYS A 1 297  ? 21.394 65.412  24.545  1.00 14.65 ? 297  CYS A N   1 
ATOM   2276 C  CA  . CYS A 1 297  ? 20.723 64.448  23.664  1.00 15.35 ? 297  CYS A CA  1 
ATOM   2277 C  C   . CYS A 1 297  ? 19.484 65.107  23.062  1.00 15.97 ? 297  CYS A C   1 
ATOM   2278 O  O   . CYS A 1 297  ? 18.585 65.507  23.808  1.00 17.42 ? 297  CYS A O   1 
ATOM   2279 C  CB  . CYS A 1 297  ? 20.311 63.195  24.493  1.00 15.90 ? 297  CYS A CB  1 
ATOM   2280 S  SG  . CYS A 1 297  ? 21.740 62.082  24.739  1.00 15.42 ? 297  CYS A SG  1 
ATOM   2281 N  N   . PRO A 1 298  ? 19.384 65.198  21.729  1.00 15.92 ? 298  PRO A N   1 
ATOM   2282 C  CA  . PRO A 1 298  ? 18.195 65.846  21.155  1.00 16.96 ? 298  PRO A CA  1 
ATOM   2283 C  C   . PRO A 1 298  ? 16.914 65.095  21.408  1.00 16.42 ? 298  PRO A C   1 
ATOM   2284 O  O   . PRO A 1 298  ? 15.841 65.706  21.314  1.00 17.12 ? 298  PRO A O   1 
ATOM   2285 C  CB  . PRO A 1 298  ? 18.508 66.022  19.663  1.00 18.80 ? 298  PRO A CB  1 
ATOM   2286 C  CG  . PRO A 1 298  ? 19.771 65.261  19.410  1.00 17.50 ? 298  PRO A CG  1 
ATOM   2287 C  CD  . PRO A 1 298  ? 20.471 65.010  20.725  1.00 16.57 ? 298  PRO A CD  1 
ATOM   2288 N  N   . TRP A 1 299  ? 17.022 63.833  21.810  1.00 15.69 ? 299  TRP A N   1 
ATOM   2289 C  CA  . TRP A 1 299  ? 15.798 63.038  22.065  1.00 16.04 ? 299  TRP A CA  1 
ATOM   2290 C  C   . TRP A 1 299  ? 15.299 63.280  23.469  1.00 17.48 ? 299  TRP A C   1 
ATOM   2291 O  O   . TRP A 1 299  ? 14.332 62.643  23.916  1.00 18.50 ? 299  TRP A O   1 
ATOM   2292 C  CB  . TRP A 1 299  ? 16.070 61.541  21.810  1.00 15.44 ? 299  TRP A CB  1 
ATOM   2293 C  CG  . TRP A 1 299  ? 16.459 61.323  20.356  1.00 15.00 ? 299  TRP A CG  1 
ATOM   2294 C  CD1 . TRP A 1 299  ? 15.619 61.141  19.307  1.00 14.02 ? 299  TRP A CD1 1 
ATOM   2295 C  CD2 . TRP A 1 299  ? 17.792 61.424  19.802  1.00 14.36 ? 299  TRP A CD2 1 
ATOM   2296 N  NE1 . TRP A 1 299  ? 16.327 61.121  18.128  1.00 15.33 ? 299  TRP A NE1 1 
ATOM   2297 C  CE2 . TRP A 1 299  ? 17.658 61.298  18.408  1.00 14.36 ? 299  TRP A CE2 1 
ATOM   2298 C  CE3 . TRP A 1 299  ? 19.062 61.608  20.362  1.00 13.75 ? 299  TRP A CE3 1 
ATOM   2299 C  CZ2 . TRP A 1 299  ? 18.762 61.361  17.543  1.00 15.15 ? 299  TRP A CZ2 1 
ATOM   2300 C  CZ3 . TRP A 1 299  ? 20.172 61.668  19.505  1.00 13.14 ? 299  TRP A CZ3 1 
ATOM   2301 C  CH2 . TRP A 1 299  ? 19.995 61.550  18.108  1.00 13.96 ? 299  TRP A CH2 1 
ATOM   2302 N  N   . LYS A 1 300  ? 16.004 64.156  24.181  1.00 17.64 ? 300  LYS A N   1 
ATOM   2303 C  CA  . LYS A 1 300  ? 15.587 64.622  25.517  1.00 19.07 ? 300  LYS A CA  1 
ATOM   2304 C  C   . LYS A 1 300  ? 15.733 63.713  26.720  1.00 19.17 ? 300  LYS A C   1 
ATOM   2305 O  O   . LYS A 1 300  ? 15.237 64.034  27.828  1.00 20.55 ? 300  LYS A O   1 
ATOM   2306 C  CB  . LYS A 1 300  ? 14.154 65.159  25.445  1.00 20.66 ? 300  LYS A CB  1 
ATOM   2307 C  CG  . LYS A 1 300  ? 13.986 66.341  24.558  1.00 22.93 ? 300  LYS A CG  1 
ATOM   2308 C  CD  . LYS A 1 300  ? 12.493 66.696  24.419  1.00 25.88 ? 300  LYS A CD  1 
ATOM   2309 C  CE  . LYS A 1 300  ? 12.254 68.009  23.653  1.00 28.12 ? 300  LYS A CE  1 
ATOM   2310 N  NZ  . LYS A 1 300  ? 13.282 68.255  22.622  1.00 29.55 ? 300  LYS A NZ  1 
ATOM   2311 N  N   . VAL A 1 301  ? 16.427 62.601  26.568  1.00 18.28 ? 301  VAL A N   1 
ATOM   2312 C  CA  . VAL A 1 301  ? 16.695 61.754  27.715  1.00 17.44 ? 301  VAL A CA  1 
ATOM   2313 C  C   . VAL A 1 301  ? 18.217 61.762  27.810  1.00 17.01 ? 301  VAL A C   1 
ATOM   2314 O  O   . VAL A 1 301  ? 18.910 61.264  26.901  1.00 17.54 ? 301  VAL A O   1 
ATOM   2315 C  CB  . VAL A 1 301  ? 16.179 60.298  27.553  1.00 17.57 ? 301  VAL A CB  1 
ATOM   2316 C  CG1 . VAL A 1 301  ? 16.496 59.520  28.821  1.00 17.99 ? 301  VAL A CG1 1 
ATOM   2317 C  CG2 . VAL A 1 301  ? 14.655 60.293  27.257  1.00 19.48 ? 301  VAL A CG2 1 
ATOM   2318 N  N   . PRO A 1 302  ? 18.780 62.285  28.896  1.00 15.40 ? 302  PRO A N   1 
ATOM   2319 C  CA  . PRO A 1 302  ? 20.223 62.347  29.018  1.00 15.65 ? 302  PRO A CA  1 
ATOM   2320 C  C   . PRO A 1 302  ? 20.901 61.081  29.469  1.00 15.62 ? 302  PRO A C   1 
ATOM   2321 O  O   . PRO A 1 302  ? 20.279 60.143  29.972  1.00 15.84 ? 302  PRO A O   1 
ATOM   2322 C  CB  . PRO A 1 302  ? 20.427 63.484  30.038  1.00 16.85 ? 302  PRO A CB  1 
ATOM   2323 C  CG  . PRO A 1 302  ? 19.208 63.291  30.963  1.00 18.15 ? 302  PRO A CG  1 
ATOM   2324 C  CD  . PRO A 1 302  ? 18.099 62.973  30.026  1.00 16.19 ? 302  PRO A CD  1 
ATOM   2325 N  N   . PRO A 1 303  ? 22.210 60.976  29.217  1.00 14.17 ? 303  PRO A N   1 
ATOM   2326 C  CA  . PRO A 1 303  ? 22.908 59.785  29.698  1.00 15.30 ? 303  PRO A CA  1 
ATOM   2327 C  C   . PRO A 1 303  ? 22.908 59.918  31.244  1.00 16.67 ? 303  PRO A C   1 
ATOM   2328 O  O   . PRO A 1 303  ? 22.834 61.036  31.807  1.00 17.30 ? 303  PRO A O   1 
ATOM   2329 C  CB  . PRO A 1 303  ? 24.364 59.974  29.227  1.00 14.65 ? 303  PRO A CB  1 
ATOM   2330 C  CG  . PRO A 1 303  ? 24.302 61.132  28.242  1.00 15.23 ? 303  PRO A CG  1 
ATOM   2331 C  CD  . PRO A 1 303  ? 23.122 61.976  28.634  1.00 14.80 ? 303  PRO A CD  1 
ATOM   2332 N  N   . ARG A 1 304  ? 23.038 58.779  31.920  1.00 18.26 ? 304  ARG A N   1 
ATOM   2333 C  CA  . ARG A 1 304  ? 23.169 58.798  33.367  1.00 19.46 ? 304  ARG A CA  1 
ATOM   2334 C  C   . ARG A 1 304  ? 24.367 57.991  33.779  1.00 17.55 ? 304  ARG A C   1 
ATOM   2335 O  O   . ARG A 1 304  ? 24.620 56.899  33.211  1.00 16.35 ? 304  ARG A O   1 
ATOM   2336 C  CB  . ARG A 1 304  ? 21.927 58.203  34.021  1.00 23.53 ? 304  ARG A CB  1 
ATOM   2337 C  CG  . ARG A 1 304  ? 20.810 59.232  34.179  1.00 29.53 ? 304  ARG A CG  1 
ATOM   2338 C  CD  . ARG A 1 304  ? 19.645 58.609  34.905  1.00 34.59 ? 304  ARG A CD  1 
ATOM   2339 N  NE  . ARG A 1 304  ? 19.237 57.381  34.215  1.00 39.24 ? 304  ARG A NE  1 
ATOM   2340 C  CZ  . ARG A 1 304  ? 19.055 56.204  34.816  1.00 41.45 ? 304  ARG A CZ  1 
ATOM   2341 N  NH1 . ARG A 1 304  ? 19.233 56.066  36.138  1.00 42.71 ? 304  ARG A NH1 1 
ATOM   2342 N  NH2 . ARG A 1 304  ? 18.716 55.149  34.083  1.00 43.03 ? 304  ARG A NH2 1 
ATOM   2343 N  N   . THR A 1 305  ? 25.124 58.488  34.747  1.00 16.84 ? 305  THR A N   1 
ATOM   2344 C  CA  . THR A 1 305  ? 26.272 57.780  35.226  1.00 16.74 ? 305  THR A CA  1 
ATOM   2345 C  C   . THR A 1 305  ? 25.893 56.373  35.684  1.00 15.74 ? 305  THR A C   1 
ATOM   2346 O  O   . THR A 1 305  ? 24.894 56.210  36.396  1.00 16.66 ? 305  THR A O   1 
ATOM   2347 C  CB  . THR A 1 305  ? 26.931 58.565  36.384  1.00 17.09 ? 305  THR A CB  1 
ATOM   2348 O  OG1 . THR A 1 305  ? 27.403 59.806  35.836  1.00 20.79 ? 305  THR A OG1 1 
ATOM   2349 C  CG2 . THR A 1 305  ? 28.045 57.817  37.036  1.00 18.55 ? 305  THR A CG2 1 
ATOM   2350 N  N   . ILE A 1 306  ? 26.652 55.372  35.274  1.00 14.45 ? 306  ILE A N   1 
ATOM   2351 C  CA  . ILE A 1 306  ? 26.343 53.990  35.643  1.00 14.23 ? 306  ILE A CA  1 
ATOM   2352 C  C   . ILE A 1 306  ? 26.784 53.781  37.087  1.00 15.60 ? 306  ILE A C   1 
ATOM   2353 O  O   . ILE A 1 306  ? 27.890 54.165  37.493  1.00 16.27 ? 306  ILE A O   1 
ATOM   2354 C  CB  . ILE A 1 306  ? 27.068 52.999  34.672  1.00 13.77 ? 306  ILE A CB  1 
ATOM   2355 C  CG1 . ILE A 1 306  ? 26.720 53.305  33.203  1.00 12.85 ? 306  ILE A CG1 1 
ATOM   2356 C  CG2 . ILE A 1 306  ? 26.703 51.529  35.111  1.00 14.12 ? 306  ILE A CG2 1 
ATOM   2357 C  CD1 . ILE A 1 306  ? 25.282 53.222  32.832  1.00 13.72 ? 306  ILE A CD1 1 
ATOM   2358 N  N   . SER A 1 307  ? 25.903 53.122  37.856  1.00 16.78 ? 307  SER A N   1 
ATOM   2359 C  CA  . SER A 1 307  ? 26.131 52.851  39.291  1.00 17.48 ? 307  SER A CA  1 
ATOM   2360 C  C   . SER A 1 307  ? 25.642 51.460  39.574  1.00 18.25 ? 307  SER A C   1 
ATOM   2361 O  O   . SER A 1 307  ? 24.925 50.869  38.770  1.00 17.36 ? 307  SER A O   1 
ATOM   2362 C  CB  . SER A 1 307  ? 25.262 53.784  40.146  1.00 17.80 ? 307  SER A CB  1 
ATOM   2363 O  OG  . SER A 1 307  ? 23.871 53.515  39.993  1.00 17.51 ? 307  SER A OG  1 
ATOM   2364 N  N   . ASP A 1 308  ? 25.954 50.977  40.766  1.00 19.80 ? 308  ASP A N   1 
ATOM   2365 C  CA  . ASP A 1 308  ? 25.447 49.660  41.112  1.00 20.59 ? 308  ASP A CA  1 
ATOM   2366 C  C   . ASP A 1 308  ? 23.900 49.610  41.172  1.00 20.23 ? 308  ASP A C   1 
ATOM   2367 O  O   . ASP A 1 308  ? 23.350 48.532  40.912  1.00 19.74 ? 308  ASP A O   1 
ATOM   2368 C  CB  . ASP A 1 308  ? 26.072 49.163  42.423  1.00 23.85 ? 308  ASP A CB  1 
ATOM   2369 C  CG  . ASP A 1 308  ? 27.571 48.897  42.310  1.00 26.25 ? 308  ASP A CG  1 
ATOM   2370 O  OD1 . ASP A 1 308  ? 28.150 48.896  41.197  1.00 28.23 ? 308  ASP A OD1 1 
ATOM   2371 O  OD2 . ASP A 1 308  ? 28.228 48.648  43.351  1.00 29.33 ? 308  ASP A OD2 1 
ATOM   2372 N  N   . GLN A 1 309  ? 23.196 50.720  41.460  1.00 19.24 ? 309  GLN A N   1 
ATOM   2373 C  CA  . GLN A 1 309  ? 21.714 50.741  41.537  1.00 19.12 ? 309  GLN A CA  1 
ATOM   2374 C  C   A GLN A 1 309  ? 20.977 50.925  40.210  0.50 18.68 ? 309  GLN A C   1 
ATOM   2375 C  C   B GLN A 1 309  ? 21.084 50.684  40.179  0.50 20.28 ? 309  GLN A C   1 
ATOM   2376 O  O   A GLN A 1 309  ? 19.727 50.820  40.132  0.50 17.50 ? 309  GLN A O   1 
ATOM   2377 O  O   B GLN A 1 309  ? 19.978 50.165  40.044  0.50 20.51 ? 309  GLN A O   1 
ATOM   2378 C  CB  A GLN A 1 309  ? 21.188 51.810  42.517  0.50 18.11 ? 309  GLN A CB  1 
ATOM   2379 C  CB  B GLN A 1 309  ? 21.196 52.046  42.154  0.50 21.09 ? 309  GLN A CB  1 
ATOM   2380 C  CG  A GLN A 1 309  ? 21.682 51.664  43.956  0.50 17.15 ? 309  GLN A CG  1 
ATOM   2381 C  CG  B GLN A 1 309  ? 21.028 52.247  43.634  0.50 22.78 ? 309  GLN A CG  1 
ATOM   2382 C  CD  A GLN A 1 309  ? 23.171 51.874  44.073  0.50 17.18 ? 309  GLN A CD  1 
ATOM   2383 C  CD  B GLN A 1 309  ? 20.671 53.708  43.881  0.50 22.47 ? 309  GLN A CD  1 
ATOM   2384 O  OE1 A GLN A 1 309  ? 23.714 52.836  43.521  0.50 16.78 ? 309  GLN A OE1 1 
ATOM   2385 O  OE1 B GLN A 1 309  ? 19.880 54.318  43.129  0.50 22.43 ? 309  GLN A OE1 1 
ATOM   2386 N  NE2 A GLN A 1 309  ? 23.839 50.988  44.808  0.50 16.92 ? 309  GLN A NE2 1 
ATOM   2387 N  NE2 B GLN A 1 309  ? 21.270 54.291  44.900  0.50 24.57 ? 309  GLN A NE2 1 
ATOM   2388 N  N   . ASN A 1 310  ? 21.723 51.262  39.167  1.00 18.87 ? 310  ASN A N   1 
ATOM   2389 C  CA  . ASN A 1 310  ? 21.085 51.345  37.875  1.00 17.16 ? 310  ASN A CA  1 
ATOM   2390 C  C   . ASN A 1 310  ? 21.758 50.466  36.825  1.00 15.55 ? 310  ASN A C   1 
ATOM   2391 O  O   . ASN A 1 310  ? 21.183 50.380  35.768  1.00 16.03 ? 310  ASN A O   1 
ATOM   2392 C  CB  . ASN A 1 310  ? 21.027 52.799  37.369  1.00 17.62 ? 310  ASN A CB  1 
ATOM   2393 C  CG  . ASN A 1 310  ? 22.412 53.371  37.005  1.00 16.43 ? 310  ASN A CG  1 
ATOM   2394 O  OD1 . ASN A 1 310  ? 23.372 52.644  36.758  1.00 16.44 ? 310  ASN A OD1 1 
ATOM   2395 N  ND2 . ASN A 1 310  ? 22.489 54.697  36.984  1.00 18.84 ? 310  ASN A ND2 1 
ATOM   2396 N  N   . VAL A 1 311  ? 22.853 49.802  37.150  1.00 14.76 ? 311  VAL A N   1 
ATOM   2397 C  CA  . VAL A 1 311  ? 23.580 49.055  36.061  1.00 14.91 ? 311  VAL A CA  1 
ATOM   2398 C  C   . VAL A 1 311  ? 22.721 47.937  35.471  1.00 16.35 ? 311  VAL A C   1 
ATOM   2399 O  O   . VAL A 1 311  ? 22.742 47.699  34.255  1.00 16.43 ? 311  VAL A O   1 
ATOM   2400 C  CB  . VAL A 1 311  ? 24.963 48.547  36.504  1.00 14.99 ? 311  VAL A CB  1 
ATOM   2401 C  CG1 . VAL A 1 311  ? 24.847 47.433  37.535  1.00 17.04 ? 311  VAL A CG1 1 
ATOM   2402 C  CG2 . VAL A 1 311  ? 25.764 48.019  35.257  1.00 15.00 ? 311  VAL A CG2 1 
ATOM   2403 N  N   . ALA A 1 312  ? 21.915 47.255  36.272  1.00 16.18 ? 312  ALA A N   1 
ATOM   2404 C  CA  . ALA A 1 312  ? 21.103 46.215  35.666  1.00 15.94 ? 312  ALA A CA  1 
ATOM   2405 C  C   . ALA A 1 312  ? 20.097 46.777  34.684  1.00 16.63 ? 312  ALA A C   1 
ATOM   2406 O  O   . ALA A 1 312  ? 19.920 46.223  33.590  1.00 17.31 ? 312  ALA A O   1 
ATOM   2407 C  CB  . ALA A 1 312  ? 20.359 45.375  36.776  1.00 16.71 ? 312  ALA A CB  1 
ATOM   2408 N  N   . ALA A 1 313  ? 19.400 47.859  35.016  1.00 15.90 ? 313  ALA A N   1 
ATOM   2409 C  CA  . ALA A 1 313  ? 18.438 48.450  34.117  1.00 16.91 ? 313  ALA A CA  1 
ATOM   2410 C  C   . ALA A 1 313  ? 19.135 49.061  32.915  1.00 17.11 ? 313  ALA A C   1 
ATOM   2411 O  O   . ALA A 1 313  ? 18.633 48.929  31.825  1.00 16.72 ? 313  ALA A O   1 
ATOM   2412 C  CB  . ALA A 1 313  ? 17.553 49.536  34.827  1.00 17.46 ? 313  ALA A CB  1 
ATOM   2413 N  N   . ARG A 1 314  ? 20.263 49.714  33.141  1.00 16.64 ? 314  ARG A N   1 
ATOM   2414 C  CA  . ARG A 1 314  ? 20.961 50.337  31.993  1.00 16.04 ? 314  ARG A CA  1 
ATOM   2415 C  C   . ARG A 1 314  ? 21.457 49.247  31.049  1.00 15.31 ? 314  ARG A C   1 
ATOM   2416 O  O   . ARG A 1 314  ? 21.379 49.420  29.821  1.00 15.59 ? 314  ARG A O   1 
ATOM   2417 C  CB  . ARG A 1 314  ? 22.146 51.157  32.500  1.00 15.50 ? 314  ARG A CB  1 
ATOM   2418 C  CG  . ARG A 1 314  ? 21.796 52.341  33.373  1.00 16.86 ? 314  ARG A CG  1 
ATOM   2419 C  CD  . ARG A 1 314  ? 21.481 53.566  32.549  1.00 20.01 ? 314  ARG A CD  1 
ATOM   2420 N  NE  . ARG A 1 314  ? 20.110 53.609  32.084  1.00 21.93 ? 314  ARG A NE  1 
ATOM   2421 C  CZ  . ARG A 1 314  ? 19.624 54.477  31.197  1.00 21.76 ? 314  ARG A CZ  1 
ATOM   2422 N  NH1 . ARG A 1 314  ? 20.418 55.402  30.624  1.00 22.69 ? 314  ARG A NH1 1 
ATOM   2423 N  NH2 . ARG A 1 314  ? 18.324 54.497  30.926  1.00 22.61 ? 314  ARG A NH2 1 
ATOM   2424 N  N   . SER A 1 315  ? 21.943 48.156  31.615  1.00 15.08 ? 315  SER A N   1 
ATOM   2425 C  CA  . SER A 1 315  ? 22.429 47.000  30.800  1.00 16.42 ? 315  SER A CA  1 
ATOM   2426 C  C   . SER A 1 315  ? 21.320 46.381  30.022  1.00 17.68 ? 315  SER A C   1 
ATOM   2427 O  O   . SER A 1 315  ? 21.509 45.955  28.871  1.00 18.22 ? 315  SER A O   1 
ATOM   2428 C  CB  . SER A 1 315  ? 23.055 45.932  31.665  1.00 15.81 ? 315  SER A CB  1 
ATOM   2429 O  OG  . SER A 1 315  ? 24.229 46.409  32.216  1.00 16.39 ? 315  SER A OG  1 
ATOM   2430 N  N   . ASP A 1 316  ? 20.134 46.272  30.604  1.00 17.42 ? 316  ASP A N   1 
ATOM   2431 C  CA  . ASP A 1 316  ? 19.015 45.682  29.866  1.00 17.18 ? 316  ASP A CA  1 
ATOM   2432 C  C   . ASP A 1 316  ? 18.577 46.541  28.658  1.00 16.91 ? 316  ASP A C   1 
ATOM   2433 O  O   A ASP A 1 316  ? 18.107 46.040  27.623  0.50 15.22 ? 316  ASP A O   1 
ATOM   2434 O  O   B ASP A 1 316  ? 18.667 45.894  27.618  0.50 16.45 ? 316  ASP A O   1 
ATOM   2435 C  CB  A ASP A 1 316  ? 17.840 45.475  30.803  0.50 17.60 ? 316  ASP A CB  1 
ATOM   2436 C  CB  B ASP A 1 316  ? 17.725 46.000  30.817  0.50 19.97 ? 316  ASP A CB  1 
ATOM   2437 C  CG  A ASP A 1 316  ? 16.905 44.420  30.304  0.50 17.64 ? 316  ASP A CG  1 
ATOM   2438 C  CG  B ASP A 1 316  ? 17.161 44.743  31.355  0.50 21.89 ? 316  ASP A CG  1 
ATOM   2439 O  OD1 A ASP A 1 316  ? 15.708 44.738  30.119  0.50 19.43 ? 316  ASP A OD1 1 
ATOM   2440 O  OD1 B ASP A 1 316  ? 17.882 44.095  32.118  0.50 21.24 ? 316  ASP A OD1 1 
ATOM   2441 O  OD2 A ASP A 1 316  ? 17.391 43.286  30.102  0.50 17.95 ? 316  ASP A OD2 1 
ATOM   2442 O  OD2 B ASP A 1 316  ? 16.000 44.412  31.002  0.50 23.00 ? 316  ASP A OD2 1 
ATOM   2443 N  N   . LEU A 1 317  ? 18.681 47.851  28.791  1.00 16.60 ? 317  LEU A N   1 
ATOM   2444 C  CA  . LEU A 1 317  ? 18.358 48.726  27.659  1.00 16.88 ? 317  LEU A CA  1 
ATOM   2445 C  C   . LEU A 1 317  ? 19.423 48.601  26.582  1.00 14.21 ? 317  LEU A C   1 
ATOM   2446 O  O   . LEU A 1 317  ? 19.106 48.464  25.406  1.00 14.44 ? 317  LEU A O   1 
ATOM   2447 C  CB  . LEU A 1 317  ? 18.297 50.211  28.101  1.00 18.50 ? 317  LEU A CB  1 
ATOM   2448 C  CG  . LEU A 1 317  ? 16.937 50.733  28.525  1.00 20.87 ? 317  LEU A CG  1 
ATOM   2449 C  CD1 . LEU A 1 317  ? 17.162 52.032  29.326  1.00 22.68 ? 317  LEU A CD1 1 
ATOM   2450 C  CD2 . LEU A 1 317  ? 16.001 50.972  27.321  1.00 22.49 ? 317  LEU A CD2 1 
ATOM   2451 N  N   . LEU A 1 318  ? 20.664 48.608  27.029  1.00 13.33 ? 318  LEU A N   1 
ATOM   2452 C  CA  . LEU A 1 318  ? 21.778 48.563  26.066  1.00 12.55 ? 318  LEU A CA  1 
ATOM   2453 C  C   . LEU A 1 318  ? 21.885 47.241  25.351  1.00 12.94 ? 318  LEU A C   1 
ATOM   2454 O  O   . LEU A 1 318  ? 22.019 47.186  24.094  1.00 12.93 ? 318  LEU A O   1 
ATOM   2455 C  CB  . LEU A 1 318  ? 23.088 48.900  26.764  1.00 12.70 ? 318  LEU A CB  1 
ATOM   2456 C  CG  . LEU A 1 318  ? 24.315 48.992  25.824  1.00 13.13 ? 318  LEU A CG  1 
ATOM   2457 C  CD1 . LEU A 1 318  ? 24.066 50.120  24.785  1.00 13.23 ? 318  LEU A CD1 1 
ATOM   2458 C  CD2 . LEU A 1 318  ? 25.577 49.288  26.646  1.00 13.75 ? 318  LEU A CD2 1 
ATOM   2459 N  N   . VAL A 1 319  ? 21.796 46.152  26.090  1.00 12.94 ? 319  VAL A N   1 
ATOM   2460 C  CA  . VAL A 1 319  ? 21.919 44.831  25.469  1.00 12.84 ? 319  VAL A CA  1 
ATOM   2461 C  C   . VAL A 1 319  ? 20.749 44.626  24.490  1.00 12.72 ? 319  VAL A C   1 
ATOM   2462 O  O   . VAL A 1 319  ? 20.901 43.970  23.463  1.00 12.86 ? 319  VAL A O   1 
ATOM   2463 C  CB  . VAL A 1 319  ? 21.947 43.699  26.529  1.00 13.26 ? 319  VAL A CB  1 
ATOM   2464 C  CG1 . VAL A 1 319  ? 21.789 42.336  25.798  1.00 13.26 ? 319  VAL A CG1 1 
ATOM   2465 C  CG2 . VAL A 1 319  ? 23.248 43.696  27.282  1.00 14.38 ? 319  VAL A CG2 1 
ATOM   2466 N  N   . ASP A 1 320  ? 19.568 45.142  24.802  1.00 12.84 ? 320  ASP A N   1 
ATOM   2467 C  CA  . ASP A 1 320  ? 18.432 45.036  23.890  1.00 13.20 ? 320  ASP A CA  1 
ATOM   2468 C  C   . ASP A 1 320  ? 18.743 45.782  22.557  1.00 12.63 ? 320  ASP A C   1 
ATOM   2469 O  O   . ASP A 1 320  ? 18.392 45.288  21.478  1.00 12.01 ? 320  ASP A O   1 
ATOM   2470 C  CB  . ASP A 1 320  ? 17.160 45.580  24.579  1.00 14.99 ? 320  ASP A CB  1 
ATOM   2471 C  CG  . ASP A 1 320  ? 15.973 45.651  23.676  1.00 13.97 ? 320  ASP A CG  1 
ATOM   2472 O  OD1 . ASP A 1 320  ? 15.445 44.569  23.311  1.00 18.13 ? 320  ASP A OD1 1 
ATOM   2473 O  OD2 . ASP A 1 320  ? 15.486 46.732  23.303  1.00 16.32 ? 320  ASP A OD2 1 
ATOM   2474 N  N   . GLN A 1 321  ? 19.363 46.961  22.626  1.00 11.58 ? 321  GLN A N   1 
ATOM   2475 C  CA  . GLN A 1 321  ? 19.758 47.649  21.363  1.00 10.81 ? 321  GLN A CA  1 
ATOM   2476 C  C   . GLN A 1 321  ? 20.779 46.796  20.613  1.00 10.02 ? 321  GLN A C   1 
ATOM   2477 O  O   . GLN A 1 321  ? 20.675 46.669  19.384  1.00 10.90 ? 321  GLN A O   1 
ATOM   2478 C  CB  . GLN A 1 321  ? 20.396 48.993  21.717  1.00 10.52 ? 321  GLN A CB  1 
ATOM   2479 C  CG  . GLN A 1 321  ? 19.398 50.046  22.181  1.00 12.33 ? 321  GLN A CG  1 
ATOM   2480 C  CD  . GLN A 1 321  ? 18.349 50.257  21.102  1.00 12.75 ? 321  GLN A CD  1 
ATOM   2481 O  OE1 . GLN A 1 321  ? 18.654 50.662  19.989  1.00 13.12 ? 321  GLN A OE1 1 
ATOM   2482 N  NE2 . GLN A 1 321  ? 17.077 49.963  21.415  1.00 13.85 ? 321  GLN A NE2 1 
ATOM   2483 N  N   . TRP A 1 322  ? 21.764 46.246  21.313  1.00 10.33 ? 322  TRP A N   1 
ATOM   2484 C  CA  . TRP A 1 322  ? 22.764 45.420  20.647  1.00 11.25 ? 322  TRP A CA  1 
ATOM   2485 C  C   . TRP A 1 322  ? 22.136 44.220  19.956  1.00 12.00 ? 322  TRP A C   1 
ATOM   2486 O  O   . TRP A 1 322  ? 22.507 43.873  18.822  1.00 11.79 ? 322  TRP A O   1 
ATOM   2487 C  CB  . TRP A 1 322  ? 23.788 44.903  21.650  1.00 10.75 ? 322  TRP A CB  1 
ATOM   2488 C  CG  . TRP A 1 322  ? 24.742 45.971  22.206  1.00 11.16 ? 322  TRP A CG  1 
ATOM   2489 C  CD1 . TRP A 1 322  ? 24.961 47.247  21.741  1.00 11.17 ? 322  TRP A CD1 1 
ATOM   2490 C  CD2 . TRP A 1 322  ? 25.622 45.794  23.324  1.00 11.08 ? 322  TRP A CD2 1 
ATOM   2491 N  NE1 . TRP A 1 322  ? 25.941 47.871  22.516  1.00 11.43 ? 322  TRP A NE1 1 
ATOM   2492 C  CE2 . TRP A 1 322  ? 26.354 47.003  23.487  1.00 11.50 ? 322  TRP A CE2 1 
ATOM   2493 C  CE3 . TRP A 1 322  ? 25.871 44.720  24.212  1.00 12.57 ? 322  TRP A CE3 1 
ATOM   2494 C  CZ2 . TRP A 1 322  ? 27.319 47.181  24.505  1.00 12.79 ? 322  TRP A CZ2 1 
ATOM   2495 C  CZ3 . TRP A 1 322  ? 26.832 44.894  25.233  1.00 12.63 ? 322  TRP A CZ3 1 
ATOM   2496 C  CH2 . TRP A 1 322  ? 27.539 46.103  25.372  1.00 13.53 ? 322  TRP A CH2 1 
ATOM   2497 N  N   . LYS A 1 323  ? 21.188 43.564  20.631  1.00 11.90 ? 323  LYS A N   1 
ATOM   2498 C  CA  . LYS A 1 323  ? 20.606 42.351  20.020  1.00 12.52 ? 323  LYS A CA  1 
ATOM   2499 C  C   . LYS A 1 323  ? 19.752 42.700  18.839  1.00 12.42 ? 323  LYS A C   1 
ATOM   2500 O  O   . LYS A 1 323  ? 19.648 41.926  17.896  1.00 13.05 ? 323  LYS A O   1 
ATOM   2501 C  CB  . LYS A 1 323  ? 19.848 41.518  21.097  1.00 13.21 ? 323  LYS A CB  1 
ATOM   2502 C  CG  . LYS A 1 323  ? 20.848 40.744  21.973  1.00 13.97 ? 323  LYS A CG  1 
ATOM   2503 C  CD  . LYS A 1 323  ? 20.179 39.947  23.109  1.00 14.73 ? 323  LYS A CD  1 
ATOM   2504 C  CE  . LYS A 1 323  ? 21.191 39.077  23.765  1.00 15.65 ? 323  LYS A CE  1 
ATOM   2505 N  NZ  . LYS A 1 323  ? 20.492 38.267  24.776  1.00 19.05 ? 323  LYS A NZ  1 
ATOM   2506 N  N   . LYS A 1 324  ? 19.123 43.858  18.851  1.00 11.22 ? 324  LYS A N   1 
ATOM   2507 C  CA  . LYS A 1 324  ? 18.385 44.324  17.674  1.00 11.45 ? 324  LYS A CA  1 
ATOM   2508 C  C   . LYS A 1 324  ? 19.378 44.593  16.511  1.00 11.77 ? 324  LYS A C   1 
ATOM   2509 O  O   . LYS A 1 324  ? 19.160 44.170  15.383  1.00 11.67 ? 324  LYS A O   1 
ATOM   2510 C  CB  . LYS A 1 324  ? 17.608 45.589  18.021  1.00 11.04 ? 324  LYS A CB  1 
ATOM   2511 C  CG  . LYS A 1 324  ? 16.348 45.214  18.837  1.00 11.63 ? 324  LYS A CG  1 
ATOM   2512 C  CD  . LYS A 1 324  ? 15.765 46.464  19.434  1.00 13.32 ? 324  LYS A CD  1 
ATOM   2513 C  CE  . LYS A 1 324  ? 14.453 46.020  20.132  1.00 14.72 ? 324  LYS A CE  1 
ATOM   2514 N  NZ  . LYS A 1 324  ? 13.899 47.095  21.007  1.00 16.67 ? 324  LYS A NZ  1 
ATOM   2515 N  N   . LYS A 1 325  ? 20.459 45.322  16.787  1.00 10.41 ? 325  LYS A N   1 
ATOM   2516 C  CA  . LYS A 1 325  ? 21.441 45.563  15.712  1.00 9.36  ? 325  LYS A CA  1 
ATOM   2517 C  C   . LYS A 1 325  ? 21.980 44.239  15.184  1.00 9.58  ? 325  LYS A C   1 
ATOM   2518 O  O   . LYS A 1 325  ? 22.179 44.071  13.970  1.00 9.57  ? 325  LYS A O   1 
ATOM   2519 C  CB  . LYS A 1 325  ? 22.580 46.424  16.268  1.00 9.71  ? 325  LYS A CB  1 
ATOM   2520 C  CG  . LYS A 1 325  ? 23.485 47.029  15.138  1.00 9.21  ? 325  LYS A CG  1 
ATOM   2521 C  CD  . LYS A 1 325  ? 24.602 47.850  15.730  1.00 10.56 ? 325  LYS A CD  1 
ATOM   2522 C  CE  . LYS A 1 325  ? 25.332 48.575  14.554  1.00 9.47  ? 325  LYS A CE  1 
ATOM   2523 N  NZ  . LYS A 1 325  ? 26.556 49.240  15.126  1.00 11.32 ? 325  LYS A NZ  1 
ATOM   2524 N  N   . ALA A 1 326  ? 22.229 43.268  16.066  1.00 10.68 ? 326  ALA A N   1 
ATOM   2525 C  CA  . ALA A 1 326  ? 22.777 41.978  15.642  1.00 10.33 ? 326  ALA A CA  1 
ATOM   2526 C  C   . ALA A 1 326  ? 21.833 41.217  14.692  1.00 11.31 ? 326  ALA A C   1 
ATOM   2527 O  O   . ALA A 1 326  ? 22.293 40.366  13.923  1.00 11.60 ? 326  ALA A O   1 
ATOM   2528 C  CB  . ALA A 1 326  ? 23.085 41.136  16.874  1.00 10.87 ? 326  ALA A CB  1 
ATOM   2529 N  N   . GLU A 1 327  ? 20.534 41.506  14.762  1.00 11.66 ? 327  GLU A N   1 
ATOM   2530 C  CA  . GLU A 1 327  ? 19.602 40.853  13.840  1.00 12.46 ? 327  GLU A CA  1 
ATOM   2531 C  C   . GLU A 1 327  ? 19.840 41.196  12.376  1.00 12.03 ? 327  GLU A C   1 
ATOM   2532 O  O   . GLU A 1 327  ? 19.373 40.486  11.471  1.00 13.31 ? 327  GLU A O   1 
ATOM   2533 C  CB  . GLU A 1 327  ? 18.143 41.230  14.161  1.00 14.44 ? 327  GLU A CB  1 
ATOM   2534 C  CG  . GLU A 1 327  ? 17.514 40.471  15.244  1.00 17.79 ? 327  GLU A CG  1 
ATOM   2535 C  CD  . GLU A 1 327  ? 17.522 38.970  14.958  1.00 17.97 ? 327  GLU A CD  1 
ATOM   2536 O  OE1 . GLU A 1 327  ? 16.859 38.454  14.019  1.00 21.33 ? 327  GLU A OE1 1 
ATOM   2537 O  OE2 . GLU A 1 327  ? 18.237 38.288  15.684  1.00 19.20 ? 327  GLU A OE2 1 
ATOM   2538 N  N   . LEU A 1 328  ? 20.553 42.288  12.139  1.00 10.86 ? 328  LEU A N   1 
ATOM   2539 C  CA  . LEU A 1 328  ? 20.780 42.739  10.763  1.00 10.92 ? 328  LEU A CA  1 
ATOM   2540 C  C   . LEU A 1 328  ? 21.990 42.091  10.124  1.00 10.89 ? 328  LEU A C   1 
ATOM   2541 O  O   . LEU A 1 328  ? 22.233 42.332  8.958   1.00 11.76 ? 328  LEU A O   1 
ATOM   2542 C  CB  . LEU A 1 328  ? 20.974 44.253  10.774  1.00 11.10 ? 328  LEU A CB  1 
ATOM   2543 C  CG  . LEU A 1 328  ? 19.865 45.022  11.503  1.00 10.22 ? 328  LEU A CG  1 
ATOM   2544 C  CD1 . LEU A 1 328  ? 20.104 46.536  11.286  1.00 11.22 ? 328  LEU A CD1 1 
ATOM   2545 C  CD2 . LEU A 1 328  ? 18.465 44.646  10.971  1.00 12.72 ? 328  LEU A CD2 1 
ATOM   2546 N  N   . TYR A 1 329  ? 22.714 41.273  10.870  1.00 10.13 ? 329  TYR A N   1 
ATOM   2547 C  CA  . TYR A 1 329  ? 23.947 40.653  10.411  1.00 10.11 ? 329  TYR A CA  1 
ATOM   2548 C  C   . TYR A 1 329  ? 23.947 39.149  10.590  1.00 11.45 ? 329  TYR A C   1 
ATOM   2549 O  O   . TYR A 1 329  ? 23.114 38.637  11.361  1.00 12.83 ? 329  TYR A O   1 
ATOM   2550 C  CB  . TYR A 1 329  ? 25.176 41.292  11.111  1.00 11.05 ? 329  TYR A CB  1 
ATOM   2551 C  CG  . TYR A 1 329  ? 25.390 42.748  10.761  1.00 9.33  ? 329  TYR A CG  1 
ATOM   2552 C  CD1 . TYR A 1 329  ? 26.118 43.103  9.641   1.00 10.12 ? 329  TYR A CD1 1 
ATOM   2553 C  CD2 . TYR A 1 329  ? 24.789 43.762  11.544  1.00 10.82 ? 329  TYR A CD2 1 
ATOM   2554 C  CE1 . TYR A 1 329  ? 26.240 44.460  9.272   1.00 9.85  ? 329  TYR A CE1 1 
ATOM   2555 C  CE2 . TYR A 1 329  ? 24.911 45.099  11.208  1.00 10.99 ? 329  TYR A CE2 1 
ATOM   2556 C  CZ  . TYR A 1 329  ? 25.637 45.429  10.056  1.00 9.14  ? 329  TYR A CZ  1 
ATOM   2557 O  OH  . TYR A 1 329  ? 25.729 46.769  9.709   1.00 10.64 ? 329  TYR A OH  1 
ATOM   2558 N  N   . ARG A 1 330  ? 24.876 38.452  9.942   1.00 11.22 ? 330  ARG A N   1 
ATOM   2559 C  CA  . ARG A 1 330  ? 24.825 36.993  9.919   1.00 11.69 ? 330  ARG A CA  1 
ATOM   2560 C  C   . ARG A 1 330  ? 25.618 36.265  10.959  1.00 12.39 ? 330  ARG A C   1 
ATOM   2561 O  O   . ARG A 1 330  ? 25.407 35.050  11.089  1.00 15.06 ? 330  ARG A O   1 
ATOM   2562 C  CB  . ARG A 1 330  ? 25.233 36.489  8.522   1.00 11.24 ? 330  ARG A CB  1 
ATOM   2563 C  CG  . ARG A 1 330  ? 24.269 36.957  7.437   1.00 12.49 ? 330  ARG A CG  1 
ATOM   2564 C  CD  . ARG A 1 330  ? 24.632 36.360  6.060   1.00 13.56 ? 330  ARG A CD  1 
ATOM   2565 N  NE  . ARG A 1 330  ? 23.679 36.924  5.130   1.00 14.56 ? 330  ARG A NE  1 
ATOM   2566 C  CZ  . ARG A 1 330  ? 23.333 36.420  3.952   1.00 16.93 ? 330  ARG A CZ  1 
ATOM   2567 N  NH1 . ARG A 1 330  ? 23.880 35.304  3.484   1.00 18.53 ? 330  ARG A NH1 1 
ATOM   2568 N  NH2 . ARG A 1 330  ? 22.392 37.036  3.254   1.00 18.01 ? 330  ARG A NH2 1 
ATOM   2569 N  N   . THR A 1 331  ? 26.533 36.912  11.667  1.00 11.86 ? 331  THR A N   1 
ATOM   2570 C  CA  . THR A 1 331  ? 27.304 36.172  12.661  1.00 11.55 ? 331  THR A CA  1 
ATOM   2571 C  C   . THR A 1 331  ? 26.902 36.584  14.073  1.00 12.01 ? 331  THR A C   1 
ATOM   2572 O  O   . THR A 1 331  ? 26.066 37.473  14.242  1.00 13.42 ? 331  THR A O   1 
ATOM   2573 C  CB  . THR A 1 331  ? 28.843 36.400  12.519  1.00 12.29 ? 331  THR A CB  1 
ATOM   2574 O  OG1 . THR A 1 331  ? 29.207 37.714  13.001  1.00 11.76 ? 331  THR A OG1 1 
ATOM   2575 C  CG2 . THR A 1 331  ? 29.278 36.160  11.025  1.00 12.55 ? 331  THR A CG2 1 
ATOM   2576 N  N   . ASN A 1 332  ? 27.548 35.940  15.061  1.00 12.67 ? 332  ASN A N   1 
ATOM   2577 C  CA  . ASN A 1 332  ? 27.319 36.323  16.465  1.00 12.69 ? 332  ASN A CA  1 
ATOM   2578 C  C   . ASN A 1 332  ? 28.395 37.263  16.974  1.00 11.33 ? 332  ASN A C   1 
ATOM   2579 O  O   . ASN A 1 332  ? 28.664 37.351  18.178  1.00 13.03 ? 332  ASN A O   1 
ATOM   2580 C  CB  . ASN A 1 332  ? 27.250 35.056  17.359  1.00 14.17 ? 332  ASN A CB  1 
ATOM   2581 C  CG  . ASN A 1 332  ? 28.606 34.355  17.504  1.00 18.17 ? 332  ASN A CG  1 
ATOM   2582 O  OD1 . ASN A 1 332  ? 29.419 34.371  16.593  1.00 19.01 ? 332  ASN A OD1 1 
ATOM   2583 N  ND2 . ASN A 1 332  ? 28.840 33.693  18.665  1.00 19.61 ? 332  ASN A ND2 1 
ATOM   2584 N  N   . VAL A 1 333  ? 29.004 38.005  16.048  1.00 11.06 ? 333  VAL A N   1 
ATOM   2585 C  CA  . VAL A 1 333  ? 30.052 38.967  16.390  1.00 10.87 ? 333  VAL A CA  1 
ATOM   2586 C  C   . VAL A 1 333  ? 29.499 40.327  15.955  1.00 9.61  ? 333  VAL A C   1 
ATOM   2587 O  O   . VAL A 1 333  ? 29.204 40.531  14.771  1.00 10.35 ? 333  VAL A O   1 
ATOM   2588 C  CB  . VAL A 1 333  ? 31.362 38.656  15.614  1.00 11.94 ? 333  VAL A CB  1 
ATOM   2589 C  CG1 . VAL A 1 333  ? 32.440 39.667  16.024  1.00 12.02 ? 333  VAL A CG1 1 
ATOM   2590 C  CG2 . VAL A 1 333  ? 31.791 37.204  15.863  1.00 14.18 ? 333  VAL A CG2 1 
ATOM   2591 N  N   . LEU A 1 334  ? 29.395 41.273  16.891  1.00 9.68  ? 334  LEU A N   1 
ATOM   2592 C  CA  . LEU A 1 334  ? 28.755 42.577  16.630  1.00 9.63  ? 334  LEU A CA  1 
ATOM   2593 C  C   . LEU A 1 334  ? 29.724 43.739  16.790  1.00 8.97  ? 334  LEU A C   1 
ATOM   2594 O  O   . LEU A 1 334  ? 30.465 43.846  17.778  1.00 9.90  ? 334  LEU A O   1 
ATOM   2595 C  CB  . LEU A 1 334  ? 27.590 42.769  17.611  1.00 9.05  ? 334  LEU A CB  1 
ATOM   2596 C  CG  . LEU A 1 334  ? 26.779 44.047  17.436  1.00 9.62  ? 334  LEU A CG  1 
ATOM   2597 C  CD1 . LEU A 1 334  ? 25.997 43.972  16.121  1.00 11.38 ? 334  LEU A CD1 1 
ATOM   2598 C  CD2 . LEU A 1 334  ? 25.807 44.190  18.629  1.00 11.05 ? 334  LEU A CD2 1 
ATOM   2599 N  N   . LEU A 1 335  ? 29.710 44.635  15.799  1.00 8.33  ? 335  LEU A N   1 
ATOM   2600 C  CA  . LEU A 1 335  ? 30.582 45.829  15.814  1.00 8.32  ? 335  LEU A CA  1 
ATOM   2601 C  C   . LEU A 1 335  ? 29.779 47.015  16.347  1.00 7.43  ? 335  LEU A C   1 
ATOM   2602 O  O   . LEU A 1 335  ? 28.732 47.363  15.797  1.00 9.56  ? 335  LEU A O   1 
ATOM   2603 C  CB  . LEU A 1 335  ? 31.038 46.130  14.364  1.00 8.81  ? 335  LEU A CB  1 
ATOM   2604 C  CG  . LEU A 1 335  ? 31.874 47.423  14.267  1.00 7.88  ? 335  LEU A CG  1 
ATOM   2605 C  CD1 . LEU A 1 335  ? 33.214 47.256  15.001  1.00 11.07 ? 335  LEU A CD1 1 
ATOM   2606 C  CD2 . LEU A 1 335  ? 32.126 47.712  12.762  1.00 10.90 ? 335  LEU A CD2 1 
ATOM   2607 N  N   . ILE A 1 336  ? 30.289 47.653  17.405  1.00 8.29  ? 336  ILE A N   1 
ATOM   2608 C  CA  . ILE A 1 336  ? 29.678 48.842  17.988  1.00 8.56  ? 336  ILE A CA  1 
ATOM   2609 C  C   . ILE A 1 336  ? 30.702 49.997  18.013  1.00 7.61  ? 336  ILE A C   1 
ATOM   2610 O  O   . ILE A 1 336  ? 31.507 50.114  18.924  1.00 8.86  ? 336  ILE A O   1 
ATOM   2611 C  CB  . ILE A 1 336  ? 29.158 48.598  19.422  1.00 9.14  ? 336  ILE A CB  1 
ATOM   2612 C  CG1 . ILE A 1 336  ? 28.123 47.469  19.431  1.00 9.01  ? 336  ILE A CG1 1 
ATOM   2613 C  CG2 . ILE A 1 336  ? 28.579 49.882  19.940  1.00 9.67  ? 336  ILE A CG2 1 
ATOM   2614 C  CD1 . ILE A 1 336  ? 26.825 47.771  18.695  1.00 10.06 ? 336  ILE A CD1 1 
ATOM   2615 N  N   . PRO A 1 337  ? 30.749 50.814  16.961  1.00 8.01  ? 337  PRO A N   1 
ATOM   2616 C  CA  . PRO A 1 337  ? 31.685 51.957  17.020  1.00 8.34  ? 337  PRO A CA  1 
ATOM   2617 C  C   . PRO A 1 337  ? 31.261 52.894  18.188  1.00 8.56  ? 337  PRO A C   1 
ATOM   2618 O  O   . PRO A 1 337  ? 30.068 53.017  18.494  1.00 9.42  ? 337  PRO A O   1 
ATOM   2619 C  CB  . PRO A 1 337  ? 31.426 52.691  15.689  1.00 8.83  ? 337  PRO A CB  1 
ATOM   2620 C  CG  . PRO A 1 337  ? 30.976 51.549  14.781  1.00 8.52  ? 337  PRO A CG  1 
ATOM   2621 C  CD  . PRO A 1 337  ? 30.058 50.722  15.654  1.00 8.81  ? 337  PRO A CD  1 
ATOM   2622 N  N   . LEU A 1 338  ? 32.245 53.520  18.837  1.00 9.22  ? 338  LEU A N   1 
ATOM   2623 C  CA  . LEU A 1 338  ? 31.986 54.449  19.934  1.00 8.63  ? 338  LEU A CA  1 
ATOM   2624 C  C   . LEU A 1 338  ? 32.824 55.735  19.692  1.00 8.47  ? 338  LEU A C   1 
ATOM   2625 O  O   . LEU A 1 338  ? 34.000 55.818  20.103  1.00 8.33  ? 338  LEU A O   1 
ATOM   2626 C  CB  . LEU A 1 338  ? 32.352 53.792  21.261  1.00 9.44  ? 338  LEU A CB  1 
ATOM   2627 C  CG  . LEU A 1 338  ? 32.009 54.708  22.437  1.00 10.17 ? 338  LEU A CG  1 
ATOM   2628 C  CD1 . LEU A 1 338  ? 30.495 54.617  22.727  1.00 12.18 ? 338  LEU A CD1 1 
ATOM   2629 C  CD2 . LEU A 1 338  ? 32.767 54.192  23.677  1.00 12.05 ? 338  LEU A CD2 1 
ATOM   2630 N  N   . GLY A 1 339  ? 32.208 56.707  18.992  1.00 8.05  ? 339  GLY A N   1 
ATOM   2631 C  CA  . GLY A 1 339  ? 32.956 57.941  18.705  1.00 8.55  ? 339  GLY A CA  1 
ATOM   2632 C  C   . GLY A 1 339  ? 32.165 58.920  17.888  1.00 8.47  ? 339  GLY A C   1 
ATOM   2633 O  O   . GLY A 1 339  ? 30.986 58.658  17.538  1.00 9.65  ? 339  GLY A O   1 
ATOM   2634 N  N   . ASP A 1 340  ? 32.817 60.050  17.527  1.00 8.74  ? 340  ASP A N   1 
ATOM   2635 C  CA  . ASP A 1 340  ? 32.186 61.108  16.781  1.00 7.99  ? 340  ASP A CA  1 
ATOM   2636 C  C   . ASP A 1 340  ? 33.333 62.059  16.411  1.00 7.99  ? 340  ASP A C   1 
ATOM   2637 O  O   . ASP A 1 340  ? 34.507 61.765  16.654  1.00 8.28  ? 340  ASP A O   1 
ATOM   2638 C  CB  . ASP A 1 340  ? 31.126 61.800  17.667  1.00 9.22  ? 340  ASP A CB  1 
ATOM   2639 C  CG  . ASP A 1 340  ? 30.029 62.481  16.875  1.00 10.93 ? 340  ASP A CG  1 
ATOM   2640 O  OD1 . ASP A 1 340  ? 30.222 62.787  15.660  1.00 10.91 ? 340  ASP A OD1 1 
ATOM   2641 O  OD2 . ASP A 1 340  ? 28.957 62.774  17.469  1.00 11.21 ? 340  ASP A OD2 1 
ATOM   2642 N  N   . ASP A 1 341  ? 32.955 63.202  15.854  1.00 8.37  ? 341  ASP A N   1 
ATOM   2643 C  CA  . ASP A 1 341  ? 33.964 64.175  15.344  1.00 8.31  ? 341  ASP A CA  1 
ATOM   2644 C  C   . ASP A 1 341  ? 34.843 64.693  16.484  1.00 8.00  ? 341  ASP A C   1 
ATOM   2645 O  O   . ASP A 1 341  ? 34.330 65.195  17.499  1.00 8.97  ? 341  ASP A O   1 
ATOM   2646 C  CB  . ASP A 1 341  ? 33.270 65.348  14.657  1.00 8.61  ? 341  ASP A CB  1 
ATOM   2647 C  CG  . ASP A 1 341  ? 32.599 64.965  13.358  1.00 8.64  ? 341  ASP A CG  1 
ATOM   2648 O  OD1 . ASP A 1 341  ? 32.493 63.756  13.068  1.00 9.17  ? 341  ASP A OD1 1 
ATOM   2649 O  OD2 . ASP A 1 341  ? 32.183 65.898  12.642  1.00 9.10  ? 341  ASP A OD2 1 
ATOM   2650 N  N   . PHE A 1 342  ? 36.166 64.603  16.315  1.00 7.58  ? 342  PHE A N   1 
ATOM   2651 C  CA  . PHE A 1 342  ? 37.105 65.136  17.297  1.00 8.51  ? 342  PHE A CA  1 
ATOM   2652 C  C   . PHE A 1 342  ? 36.792 64.757  18.747  1.00 8.64  ? 342  PHE A C   1 
ATOM   2653 O  O   . PHE A 1 342  ? 37.024 65.539  19.677  1.00 10.33 ? 342  PHE A O   1 
ATOM   2654 C  CB  . PHE A 1 342  ? 37.264 66.680  17.076  1.00 7.99  ? 342  PHE A CB  1 
ATOM   2655 C  CG  . PHE A 1 342  ? 37.821 67.035  15.723  1.00 7.67  ? 342  PHE A CG  1 
ATOM   2656 C  CD1 . PHE A 1 342  ? 39.209 67.029  15.496  1.00 7.79  ? 342  PHE A CD1 1 
ATOM   2657 C  CD2 . PHE A 1 342  ? 36.981 67.427  14.663  1.00 8.66  ? 342  PHE A CD2 1 
ATOM   2658 C  CE1 . PHE A 1 342  ? 39.753 67.417  14.263  1.00 7.87  ? 342  PHE A CE1 1 
ATOM   2659 C  CE2 . PHE A 1 342  ? 37.550 67.813  13.418  1.00 8.54  ? 342  PHE A CE2 1 
ATOM   2660 C  CZ  . PHE A 1 342  ? 38.922 67.807  13.239  1.00 8.32  ? 342  PHE A CZ  1 
ATOM   2661 N  N   . ARG A 1 343  ? 36.341 63.511  18.901  1.00 8.70  ? 343  ARG A N   1 
ATOM   2662 C  CA  . ARG A 1 343  ? 36.120 62.984  20.244  1.00 7.72  ? 343  ARG A CA  1 
ATOM   2663 C  C   . ARG A 1 343  ? 37.433 62.515  20.891  1.00 9.48  ? 343  ARG A C   1 
ATOM   2664 O  O   . ARG A 1 343  ? 38.524 62.426  20.287  1.00 8.96  ? 343  ARG A O   1 
ATOM   2665 C  CB  . ARG A 1 343  ? 35.101 61.821  20.200  1.00 8.56  ? 343  ARG A CB  1 
ATOM   2666 C  CG  . ARG A 1 343  ? 33.686 62.285  19.925  1.00 9.79  ? 343  ARG A CG  1 
ATOM   2667 C  CD  . ARG A 1 343  ? 33.214 63.311  21.023  1.00 9.83  ? 343  ARG A CD  1 
ATOM   2668 N  NE  . ARG A 1 343  ? 31.773 63.552  20.899  1.00 10.18 ? 343  ARG A NE  1 
ATOM   2669 C  CZ  . ARG A 1 343  ? 30.837 62.827  21.553  1.00 9.50  ? 343  ARG A CZ  1 
ATOM   2670 N  NH1 . ARG A 1 343  ? 31.202 61.801  22.337  1.00 9.77  ? 343  ARG A NH1 1 
ATOM   2671 N  NH2 . ARG A 1 343  ? 29.566 63.235  21.467  1.00 10.66 ? 343  ARG A NH2 1 
ATOM   2672 N  N   . PHE A 1 344  ? 37.298 62.206  22.190  1.00 8.92  ? 344  PHE A N   1 
ATOM   2673 C  CA  . PHE A 1 344  ? 38.384 61.744  23.041  1.00 9.21  ? 344  PHE A CA  1 
ATOM   2674 C  C   . PHE A 1 344  ? 39.490 62.767  23.158  1.00 10.63 ? 344  PHE A C   1 
ATOM   2675 O  O   . PHE A 1 344  ? 40.666 62.452  23.010  1.00 11.59 ? 344  PHE A O   1 
ATOM   2676 C  CB  . PHE A 1 344  ? 38.849 60.340  22.573  1.00 10.00 ? 344  PHE A CB  1 
ATOM   2677 C  CG  . PHE A 1 344  ? 37.789 59.297  22.728  1.00 10.06 ? 344  PHE A CG  1 
ATOM   2678 C  CD1 . PHE A 1 344  ? 37.560 58.718  23.994  1.00 11.87 ? 344  PHE A CD1 1 
ATOM   2679 C  CD2 . PHE A 1 344  ? 36.970 58.922  21.675  1.00 9.98  ? 344  PHE A CD2 1 
ATOM   2680 C  CE1 . PHE A 1 344  ? 36.518 57.788  24.164  1.00 10.86 ? 344  PHE A CE1 1 
ATOM   2681 C  CE2 . PHE A 1 344  ? 35.940 58.001  21.860  1.00 10.85 ? 344  PHE A CE2 1 
ATOM   2682 C  CZ  . PHE A 1 344  ? 35.731 57.443  23.126  1.00 11.32 ? 344  PHE A CZ  1 
ATOM   2683 N  N   . LYS A 1 345  ? 39.077 64.005  23.442  1.00 11.58 ? 345  LYS A N   1 
ATOM   2684 C  CA  . LYS A 1 345  ? 40.058 65.095  23.605  1.00 13.38 ? 345  LYS A CA  1 
ATOM   2685 C  C   . LYS A 1 345  ? 40.442 65.200  25.114  1.00 14.32 ? 345  LYS A C   1 
ATOM   2686 O  O   . LYS A 1 345  ? 41.498 64.697  25.540  1.00 15.92 ? 345  LYS A O   1 
ATOM   2687 C  CB  . LYS A 1 345  ? 39.412 66.389  23.094  1.00 14.44 ? 345  LYS A CB  1 
ATOM   2688 C  CG  . LYS A 1 345  ? 40.289 67.619  23.164  1.00 16.56 ? 345  LYS A CG  1 
ATOM   2689 C  CD  . LYS A 1 345  ? 39.491 68.833  22.708  1.00 19.46 ? 345  LYS A CD  1 
ATOM   2690 C  CE  . LYS A 1 345  ? 40.265 70.109  22.881  1.00 20.81 ? 345  LYS A CE  1 
ATOM   2691 N  NZ  . LYS A 1 345  ? 39.440 71.188  22.254  1.00 22.44 ? 345  LYS A NZ  1 
ATOM   2692 N  N   . GLN A 1 346  ? 39.513 65.688  25.902  1.00 14.60 ? 346  GLN A N   1 
ATOM   2693 C  CA  . GLN A 1 346  ? 39.860 65.881  27.292  1.00 16.18 ? 346  GLN A CA  1 
ATOM   2694 C  C   . GLN A 1 346  ? 40.016 64.644  28.138  1.00 15.55 ? 346  GLN A C   1 
ATOM   2695 O  O   . GLN A 1 346  ? 39.342 63.629  27.911  1.00 13.31 ? 346  GLN A O   1 
ATOM   2696 C  CB  . GLN A 1 346  ? 38.834 66.790  27.912  1.00 18.98 ? 346  GLN A CB  1 
ATOM   2697 C  CG  . GLN A 1 346  ? 38.858 68.173  27.275  1.00 22.75 ? 346  GLN A CG  1 
ATOM   2698 C  CD  . GLN A 1 346  ? 37.681 68.995  27.737  1.00 26.04 ? 346  GLN A CD  1 
ATOM   2699 O  OE1 . GLN A 1 346  ? 37.813 69.843  28.641  1.00 29.80 ? 346  GLN A OE1 1 
ATOM   2700 N  NE2 . GLN A 1 346  ? 36.518 68.752  27.136  1.00 29.09 ? 346  GLN A NE2 1 
ATOM   2701 N  N   . ASN A 1 347  ? 40.851 64.728  29.164  1.00 15.85 ? 347  ASN A N   1 
ATOM   2702 C  CA  . ASN A 1 347  ? 41.050 63.596  30.059  1.00 15.42 ? 347  ASN A CA  1 
ATOM   2703 C  C   . ASN A 1 347  ? 39.729 63.207  30.720  1.00 14.26 ? 347  ASN A C   1 
ATOM   2704 O  O   . ASN A 1 347  ? 39.430 62.014  30.841  1.00 14.03 ? 347  ASN A O   1 
ATOM   2705 C  CB  . ASN A 1 347  ? 42.051 63.975  31.153  1.00 17.70 ? 347  ASN A CB  1 
ATOM   2706 C  CG  . ASN A 1 347  ? 43.386 64.183  30.609  1.00 20.20 ? 347  ASN A CG  1 
ATOM   2707 O  OD1 . ASN A 1 347  ? 43.912 63.299  29.943  1.00 22.48 ? 347  ASN A OD1 1 
ATOM   2708 N  ND2 . ASN A 1 347  ? 43.982 65.363  30.868  1.00 23.25 ? 347  ASN A ND2 1 
ATOM   2709 N  N   . THR A 1 348  ? 38.904 64.194  31.100  1.00 13.46 ? 348  THR A N   1 
ATOM   2710 C  CA  . THR A 1 348  ? 37.621 63.896  31.721  1.00 14.58 ? 348  THR A CA  1 
ATOM   2711 C  C   . THR A 1 348  ? 36.701 63.130  30.776  1.00 13.90 ? 348  THR A C   1 
ATOM   2712 O  O   . THR A 1 348  ? 35.860 62.335  31.206  1.00 14.30 ? 348  THR A O   1 
ATOM   2713 C  CB  . THR A 1 348  ? 36.899 65.202  32.201  1.00 14.53 ? 348  THR A CB  1 
ATOM   2714 O  OG1 . THR A 1 348  ? 36.787 66.149  31.107  1.00 18.38 ? 348  THR A OG1 1 
ATOM   2715 C  CG2 . THR A 1 348  ? 37.725 65.871  33.338  1.00 16.61 ? 348  THR A CG2 1 
ATOM   2716 N  N   . GLU A 1 349  ? 36.852 63.359  29.461  1.00 11.14 ? 349  GLU A N   1 
ATOM   2717 C  CA  . GLU A 1 349  ? 36.028 62.642  28.483  1.00 10.87 ? 349  GLU A CA  1 
ATOM   2718 C  C   . GLU A 1 349  ? 36.511 61.206  28.350  1.00 9.95  ? 349  GLU A C   1 
ATOM   2719 O  O   . GLU A 1 349  ? 35.678 60.284  28.308  1.00 10.74 ? 349  GLU A O   1 
ATOM   2720 C  CB  . GLU A 1 349  ? 36.133 63.333  27.114  1.00 10.96 ? 349  GLU A CB  1 
ATOM   2721 C  CG  . GLU A 1 349  ? 35.312 62.633  26.039  1.00 10.28 ? 349  GLU A CG  1 
ATOM   2722 C  CD  . GLU A 1 349  ? 35.574 63.191  24.631  1.00 10.30 ? 349  GLU A CD  1 
ATOM   2723 O  OE1 . GLU A 1 349  ? 36.267 64.224  24.478  1.00 12.52 ? 349  GLU A OE1 1 
ATOM   2724 O  OE2 . GLU A 1 349  ? 35.061 62.532  23.725  1.00 11.44 ? 349  GLU A OE2 1 
ATOM   2725 N  N   . TRP A 1 350  ? 37.818 60.988  28.306  1.00 9.94  ? 350  TRP A N   1 
ATOM   2726 C  CA  . TRP A 1 350  ? 38.342 59.604  28.286  1.00 10.15 ? 350  TRP A CA  1 
ATOM   2727 C  C   . TRP A 1 350  ? 37.803 58.838  29.494  1.00 10.73 ? 350  TRP A C   1 
ATOM   2728 O  O   . TRP A 1 350  ? 37.297 57.710  29.366  1.00 12.16 ? 350  TRP A O   1 
ATOM   2729 C  CB  . TRP A 1 350  ? 39.858 59.561  28.352  1.00 10.65 ? 350  TRP A CB  1 
ATOM   2730 C  CG  . TRP A 1 350  ? 40.526 59.776  27.013  1.00 10.86 ? 350  TRP A CG  1 
ATOM   2731 C  CD1 . TRP A 1 350  ? 40.865 60.972  26.471  1.00 11.25 ? 350  TRP A CD1 1 
ATOM   2732 C  CD2 . TRP A 1 350  ? 40.827 58.775  26.043  1.00 10.94 ? 350  TRP A CD2 1 
ATOM   2733 N  NE1 . TRP A 1 350  ? 41.374 60.791  25.215  1.00 10.78 ? 350  TRP A NE1 1 
ATOM   2734 C  CE2 . TRP A 1 350  ? 41.359 59.458  24.913  1.00 11.21 ? 350  TRP A CE2 1 
ATOM   2735 C  CE3 . TRP A 1 350  ? 40.698 57.384  25.999  1.00 12.93 ? 350  TRP A CE3 1 
ATOM   2736 C  CZ2 . TRP A 1 350  ? 41.757 58.785  23.758  1.00 12.89 ? 350  TRP A CZ2 1 
ATOM   2737 C  CZ3 . TRP A 1 350  ? 41.110 56.705  24.829  1.00 13.51 ? 350  TRP A CZ3 1 
ATOM   2738 C  CH2 . TRP A 1 350  ? 41.628 57.416  23.734  1.00 13.78 ? 350  TRP A CH2 1 
ATOM   2739 N  N   . ASP A 1 351  ? 37.870 59.474  30.665  1.00 12.34 ? 351  ASP A N   1 
ATOM   2740 C  CA  . ASP A 1 351  ? 37.372 58.820  31.867  1.00 13.51 ? 351  ASP A CA  1 
ATOM   2741 C  C   . ASP A 1 351  ? 35.870 58.569  31.865  1.00 12.58 ? 351  ASP A C   1 
ATOM   2742 O  O   . ASP A 1 351  ? 35.422 57.455  32.241  1.00 13.47 ? 351  ASP A O   1 
ATOM   2743 C  CB  . ASP A 1 351  ? 37.653 59.694  33.096  1.00 16.32 ? 351  ASP A CB  1 
ATOM   2744 C  CG  . ASP A 1 351  ? 39.091 59.748  33.474  1.00 18.72 ? 351  ASP A CG  1 
ATOM   2745 O  OD1 . ASP A 1 351  ? 39.876 58.820  33.142  1.00 20.63 ? 351  ASP A OD1 1 
ATOM   2746 O  OD2 . ASP A 1 351  ? 39.439 60.737  34.178  1.00 21.85 ? 351  ASP A OD2 1 
ATOM   2747 N  N   . VAL A 1 352  ? 35.073 59.548  31.463  1.00 12.78 ? 352  VAL A N   1 
ATOM   2748 C  CA  . VAL A 1 352  ? 33.646 59.357  31.528  1.00 13.76 ? 352  VAL A CA  1 
ATOM   2749 C  C   . VAL A 1 352  ? 33.196 58.238  30.582  1.00 13.00 ? 352  VAL A C   1 
ATOM   2750 O  O   . VAL A 1 352  ? 32.339 57.433  30.909  1.00 14.95 ? 352  VAL A O   1 
ATOM   2751 C  CB  . VAL A 1 352  ? 32.892 60.704  31.326  1.00 15.03 ? 352  VAL A CB  1 
ATOM   2752 C  CG1 . VAL A 1 352  ? 32.698 61.040  29.907  1.00 14.77 ? 352  VAL A CG1 1 
ATOM   2753 C  CG2 . VAL A 1 352  ? 31.593 60.711  32.096  1.00 17.17 ? 352  VAL A CG2 1 
ATOM   2754 N  N   . GLN A 1 353  ? 33.784 58.122  29.405  1.00 12.13 ? 353  GLN A N   1 
ATOM   2755 C  CA  . GLN A 1 353  ? 33.360 57.034  28.544  1.00 11.15 ? 353  GLN A CA  1 
ATOM   2756 C  C   . GLN A 1 353  ? 33.925 55.697  29.041  1.00 11.11 ? 353  GLN A C   1 
ATOM   2757 O  O   . GLN A 1 353  ? 33.169 54.704  29.158  1.00 12.10 ? 353  GLN A O   1 
ATOM   2758 C  CB  . GLN A 1 353  ? 33.878 57.288  27.104  1.00 10.32 ? 353  GLN A CB  1 
ATOM   2759 C  CG  . GLN A 1 353  ? 33.343 58.582  26.399  1.00 10.60 ? 353  GLN A CG  1 
ATOM   2760 C  CD  . GLN A 1 353  ? 31.900 58.499  25.953  1.00 10.28 ? 353  GLN A CD  1 
ATOM   2761 O  OE1 . GLN A 1 353  ? 31.077 57.761  26.549  1.00 12.07 ? 353  GLN A OE1 1 
ATOM   2762 N  NE2 . GLN A 1 353  ? 31.544 59.242  24.922  1.00 10.56 ? 353  GLN A NE2 1 
ATOM   2763 N  N   . ARG A 1 354  ? 35.219 55.636  29.356  1.00 10.72 ? 354  ARG A N   1 
ATOM   2764 C  CA  . ARG A 1 354  ? 35.826 54.389  29.790  1.00 11.74 ? 354  ARG A CA  1 
ATOM   2765 C  C   . ARG A 1 354  ? 35.222 53.804  31.077  1.00 12.84 ? 354  ARG A C   1 
ATOM   2766 O  O   . ARG A 1 354  ? 34.865 52.630  31.107  1.00 12.37 ? 354  ARG A O   1 
ATOM   2767 C  CB  . ARG A 1 354  ? 37.334 54.537  30.015  1.00 11.44 ? 354  ARG A CB  1 
ATOM   2768 C  CG  . ARG A 1 354  ? 37.963 53.216  30.439  1.00 11.55 ? 354  ARG A CG  1 
ATOM   2769 C  CD  . ARG A 1 354  ? 39.480 53.390  30.723  1.00 12.92 ? 354  ARG A CD  1 
ATOM   2770 N  NE  . ARG A 1 354  ? 39.724 54.461  31.697  1.00 15.18 ? 354  ARG A NE  1 
ATOM   2771 C  CZ  . ARG A 1 354  ? 39.573 54.355  33.012  1.00 15.43 ? 354  ARG A CZ  1 
ATOM   2772 N  NH1 . ARG A 1 354  ? 39.144 53.227  33.565  1.00 15.80 ? 354  ARG A NH1 1 
ATOM   2773 N  NH2 . ARG A 1 354  ? 39.927 55.372  33.790  1.00 18.77 ? 354  ARG A NH2 1 
ATOM   2774 N  N   . VAL A 1 355  ? 35.099 54.613  32.114  1.00 13.23 ? 355  VAL A N   1 
ATOM   2775 C  CA  . VAL A 1 355  ? 34.600 54.049  33.374  1.00 13.57 ? 355  VAL A CA  1 
ATOM   2776 C  C   . VAL A 1 355  ? 33.181 53.582  33.270  1.00 12.64 ? 355  VAL A C   1 
ATOM   2777 O  O   . VAL A 1 355  ? 32.838 52.489  33.836  1.00 14.78 ? 355  VAL A O   1 
ATOM   2778 C  CB  . VAL A 1 355  ? 34.770 55.099  34.518  1.00 15.32 ? 355  VAL A CB  1 
ATOM   2779 C  CG1 . VAL A 1 355  ? 34.240 54.550  35.854  1.00 19.58 ? 355  VAL A CG1 1 
ATOM   2780 C  CG2 . VAL A 1 355  ? 36.257 55.432  34.716  1.00 16.65 ? 355  VAL A CG2 1 
ATOM   2781 N  N   . ASN A 1 356  ? 32.321 54.328  32.590  1.00 12.43 ? 356  ASN A N   1 
ATOM   2782 C  CA  . ASN A 1 356  ? 30.931 53.911  32.472  1.00 12.19 ? 356  ASN A CA  1 
ATOM   2783 C  C   . ASN A 1 356  ? 30.828 52.624  31.637  1.00 13.35 ? 356  ASN A C   1 
ATOM   2784 O  O   . ASN A 1 356  ? 30.093 51.672  32.026  1.00 12.92 ? 356  ASN A O   1 
ATOM   2785 C  CB  . ASN A 1 356  ? 30.038 55.045  31.992  1.00 13.25 ? 356  ASN A CB  1 
ATOM   2786 C  CG  . ASN A 1 356  ? 29.795 56.039  33.069  1.00 14.36 ? 356  ASN A CG  1 
ATOM   2787 O  OD1 . ASN A 1 356  ? 29.100 55.725  34.055  1.00 14.75 ? 356  ASN A OD1 1 
ATOM   2788 N  ND2 . ASN A 1 356  ? 30.389 57.237  32.949  1.00 14.47 ? 356  ASN A ND2 1 
ATOM   2789 N  N   . TYR A 1 357  ? 31.561 52.530  30.531  1.00 11.40 ? 357  TYR A N   1 
ATOM   2790 C  CA  . TYR A 1 357  ? 31.503 51.298  29.789  1.00 11.57 ? 357  TYR A CA  1 
ATOM   2791 C  C   . TYR A 1 357  ? 32.116 50.123  30.547  1.00 11.77 ? 357  TYR A C   1 
ATOM   2792 O  O   . TYR A 1 357  ? 31.572 49.001  30.449  1.00 11.97 ? 357  TYR A O   1 
ATOM   2793 C  CB  . TYR A 1 357  ? 32.131 51.466  28.367  1.00 10.50 ? 357  TYR A CB  1 
ATOM   2794 C  CG  . TYR A 1 357  ? 31.137 51.979  27.389  1.00 10.67 ? 357  TYR A CG  1 
ATOM   2795 C  CD1 . TYR A 1 357  ? 30.274 51.095  26.693  1.00 10.28 ? 357  TYR A CD1 1 
ATOM   2796 C  CD2 . TYR A 1 357  ? 30.999 53.350  27.191  1.00 10.17 ? 357  TYR A CD2 1 
ATOM   2797 C  CE1 . TYR A 1 357  ? 29.305 51.571  25.833  1.00 10.26 ? 357  TYR A CE1 1 
ATOM   2798 C  CE2 . TYR A 1 357  ? 30.005 53.862  26.332  1.00 10.72 ? 357  TYR A CE2 1 
ATOM   2799 C  CZ  . TYR A 1 357  ? 29.146 52.976  25.646  1.00 11.75 ? 357  TYR A CZ  1 
ATOM   2800 O  OH  . TYR A 1 357  ? 28.146 53.445  24.843  1.00 11.46 ? 357  TYR A OH  1 
ATOM   2801 N  N   . GLU A 1 358  ? 33.212 50.330  31.293  1.00 11.92 ? 358  GLU A N   1 
ATOM   2802 C  CA  . GLU A 1 358  ? 33.762 49.215  32.092  1.00 12.79 ? 358  GLU A CA  1 
ATOM   2803 C  C   . GLU A 1 358  ? 32.688 48.692  33.076  1.00 12.99 ? 358  GLU A C   1 
ATOM   2804 O  O   . GLU A 1 358  ? 32.591 47.481  33.278  1.00 13.03 ? 358  GLU A O   1 
ATOM   2805 C  CB  . GLU A 1 358  ? 34.961 49.664  32.905  1.00 13.78 ? 358  GLU A CB  1 
ATOM   2806 C  CG  . GLU A 1 358  ? 36.236 49.904  32.082  1.00 16.11 ? 358  GLU A CG  1 
ATOM   2807 C  CD  . GLU A 1 358  ? 37.448 50.300  32.928  1.00 18.33 ? 358  GLU A CD  1 
ATOM   2808 O  OE1 . GLU A 1 358  ? 37.364 50.293  34.173  1.00 21.27 ? 358  GLU A OE1 1 
ATOM   2809 O  OE2 . GLU A 1 358  ? 38.512 50.603  32.371  1.00 18.33 ? 358  GLU A OE2 1 
ATOM   2810 N  N   . ARG A 1 359  ? 31.904 49.577  33.671  1.00 12.52 ? 359  ARG A N   1 
ATOM   2811 C  CA  . ARG A 1 359  ? 30.873 49.092  34.624  1.00 14.31 ? 359  ARG A CA  1 
ATOM   2812 C  C   . ARG A 1 359  ? 29.804 48.295  33.894  1.00 14.14 ? 359  ARG A C   1 
ATOM   2813 O  O   . ARG A 1 359  ? 29.305 47.263  34.411  1.00 14.00 ? 359  ARG A O   1 
ATOM   2814 C  CB  . ARG A 1 359  ? 30.223 50.246  35.363  1.00 15.39 ? 359  ARG A CB  1 
ATOM   2815 C  CG  . ARG A 1 359  ? 31.089 50.943  36.401  1.00 18.10 ? 359  ARG A CG  1 
ATOM   2816 C  CD  . ARG A 1 359  ? 30.332 52.178  36.877  1.00 21.83 ? 359  ARG A CD  1 
ATOM   2817 N  NE  . ARG A 1 359  ? 31.191 53.105  37.615  1.00 24.87 ? 359  ARG A NE  1 
ATOM   2818 C  CZ  . ARG A 1 359  ? 31.208 54.437  37.438  1.00 25.24 ? 359  ARG A CZ  1 
ATOM   2819 N  NH1 . ARG A 1 359  ? 30.407 55.062  36.530  1.00 24.06 ? 359  ARG A NH1 1 
ATOM   2820 N  NH2 . ARG A 1 359  ? 32.048 55.163  38.191  1.00 29.05 ? 359  ARG A NH2 1 
ATOM   2821 N  N   . LEU A 1 360  ? 29.405 48.726  32.702  1.00 13.09 ? 360  LEU A N   1 
ATOM   2822 C  CA  . LEU A 1 360  ? 28.436 47.981  31.927  1.00 12.40 ? 360  LEU A CA  1 
ATOM   2823 C  C   . LEU A 1 360  ? 29.010 46.627  31.536  1.00 12.88 ? 360  LEU A C   1 
ATOM   2824 O  O   . LEU A 1 360  ? 28.315 45.602  31.670  1.00 14.31 ? 360  LEU A O   1 
ATOM   2825 C  CB  . LEU A 1 360  ? 28.064 48.785  30.676  1.00 12.36 ? 360  LEU A CB  1 
ATOM   2826 C  CG  . LEU A 1 360  ? 27.192 50.012  31.011  1.00 11.75 ? 360  LEU A CG  1 
ATOM   2827 C  CD1 . LEU A 1 360  ? 27.275 51.034  29.868  1.00 13.24 ? 360  LEU A CD1 1 
ATOM   2828 C  CD2 . LEU A 1 360  ? 25.717 49.628  31.204  1.00 13.43 ? 360  LEU A CD2 1 
ATOM   2829 N  N   . PHE A 1 361  ? 30.247 46.568  31.044  1.00 12.39 ? 361  PHE A N   1 
ATOM   2830 C  CA  . PHE A 1 361  ? 30.837 45.277  30.647  1.00 12.50 ? 361  PHE A CA  1 
ATOM   2831 C  C   . PHE A 1 361  ? 30.935 44.316  31.861  1.00 13.95 ? 361  PHE A C   1 
ATOM   2832 O  O   . PHE A 1 361  ? 30.671 43.117  31.721  1.00 13.60 ? 361  PHE A O   1 
ATOM   2833 C  CB  . PHE A 1 361  ? 32.263 45.440  30.091  1.00 12.10 ? 361  PHE A CB  1 
ATOM   2834 C  CG  . PHE A 1 361  ? 32.349 46.228  28.829  1.00 11.95 ? 361  PHE A CG  1 
ATOM   2835 C  CD1 . PHE A 1 361  ? 31.269 46.368  27.982  1.00 11.48 ? 361  PHE A CD1 1 
ATOM   2836 C  CD2 . PHE A 1 361  ? 33.542 46.865  28.549  1.00 11.43 ? 361  PHE A CD2 1 
ATOM   2837 C  CE1 . PHE A 1 361  ? 31.382 47.172  26.819  1.00 11.79 ? 361  PHE A CE1 1 
ATOM   2838 C  CE2 . PHE A 1 361  ? 33.667 47.678  27.370  1.00 12.27 ? 361  PHE A CE2 1 
ATOM   2839 C  CZ  . PHE A 1 361  ? 32.582 47.811  26.533  1.00 11.95 ? 361  PHE A CZ  1 
ATOM   2840 N  N   . GLU A 1 362  ? 31.378 44.819  33.020  1.00 14.20 ? 362  GLU A N   1 
ATOM   2841 C  CA  . GLU A 1 362  ? 31.509 43.886  34.146  1.00 14.27 ? 362  GLU A CA  1 
ATOM   2842 C  C   . GLU A 1 362  ? 30.121 43.294  34.499  1.00 13.76 ? 362  GLU A C   1 
ATOM   2843 O  O   . GLU A 1 362  ? 30.003 42.095  34.739  1.00 14.52 ? 362  GLU A O   1 
ATOM   2844 C  CB  . GLU A 1 362  ? 32.113 44.599  35.363  1.00 16.48 ? 362  GLU A CB  1 
ATOM   2845 C  CG  . GLU A 1 362  ? 32.221 43.603  36.499  1.00 19.73 ? 362  GLU A CG  1 
ATOM   2846 C  CD  . GLU A 1 362  ? 32.703 44.177  37.806  1.00 24.12 ? 362  GLU A CD  1 
ATOM   2847 O  OE1 . GLU A 1 362  ? 33.039 45.387  37.872  1.00 27.03 ? 362  GLU A OE1 1 
ATOM   2848 O  OE2 . GLU A 1 362  ? 32.722 43.373  38.768  1.00 25.55 ? 362  GLU A OE2 1 
ATOM   2849 N  N   . HIS A 1 363  ? 29.087 44.110  34.514  1.00 13.72 ? 363  HIS A N   1 
ATOM   2850 C  CA  . HIS A 1 363  ? 27.754 43.602  34.801  1.00 15.17 ? 363  HIS A CA  1 
ATOM   2851 C  C   . HIS A 1 363  ? 27.241 42.647  33.734  1.00 14.68 ? 363  HIS A C   1 
ATOM   2852 O  O   . HIS A 1 363  ? 26.865 41.490  34.003  1.00 15.22 ? 363  HIS A O   1 
ATOM   2853 C  CB  . HIS A 1 363  ? 26.749 44.740  34.994  1.00 15.58 ? 363  HIS A CB  1 
ATOM   2854 C  CG  . HIS A 1 363  ? 25.350 44.270  35.310  1.00 17.86 ? 363  HIS A CG  1 
ATOM   2855 N  ND1 . HIS A 1 363  ? 24.970 43.839  36.573  1.00 19.98 ? 363  HIS A ND1 1 
ATOM   2856 C  CD2 . HIS A 1 363  ? 24.263 44.129  34.521  1.00 18.73 ? 363  HIS A CD2 1 
ATOM   2857 C  CE1 . HIS A 1 363  ? 23.707 43.452  36.531  1.00 20.13 ? 363  HIS A CE1 1 
ATOM   2858 N  NE2 . HIS A 1 363  ? 23.246 43.618  35.306  1.00 20.48 ? 363  HIS A NE2 1 
ATOM   2859 N  N   . ILE A 1 364  ? 27.257 43.094  32.471  1.00 14.17 ? 364  ILE A N   1 
ATOM   2860 C  CA  . ILE A 1 364  ? 26.713 42.297  31.412  1.00 14.26 ? 364  ILE A CA  1 
ATOM   2861 C  C   . ILE A 1 364  ? 27.424 40.977  31.280  1.00 13.32 ? 364  ILE A C   1 
ATOM   2862 O  O   . ILE A 1 364  ? 26.760 39.912  31.149  1.00 14.93 ? 364  ILE A O   1 
ATOM   2863 C  CB  . ILE A 1 364  ? 26.818 43.075  30.050  1.00 13.62 ? 364  ILE A CB  1 
ATOM   2864 C  CG1 . ILE A 1 364  ? 25.787 44.218  30.028  1.00 13.65 ? 364  ILE A CG1 1 
ATOM   2865 C  CG2 . ILE A 1 364  ? 26.604 42.094  28.894  1.00 12.80 ? 364  ILE A CG2 1 
ATOM   2866 C  CD1 . ILE A 1 364  ? 26.079 45.341  29.013  1.00 13.83 ? 364  ILE A CD1 1 
ATOM   2867 N  N   . ASN A 1 365  ? 28.740 40.981  31.324  1.00 13.50 ? 365  ASN A N   1 
ATOM   2868 C  CA  . ASN A 1 365  ? 29.527 39.747  31.105  1.00 14.99 ? 365  ASN A CA  1 
ATOM   2869 C  C   . ASN A 1 365  ? 29.383 38.748  32.259  1.00 16.92 ? 365  ASN A C   1 
ATOM   2870 O  O   . ASN A 1 365  ? 29.701 37.575  32.095  1.00 16.99 ? 365  ASN A O   1 
ATOM   2871 C  CB  . ASN A 1 365  ? 31.009 40.031  30.875  1.00 13.35 ? 365  ASN A CB  1 
ATOM   2872 C  CG  . ASN A 1 365  ? 31.240 40.868  29.602  1.00 12.85 ? 365  ASN A CG  1 
ATOM   2873 O  OD1 . ASN A 1 365  ? 30.313 41.039  28.806  1.00 13.40 ? 365  ASN A OD1 1 
ATOM   2874 N  ND2 . ASN A 1 365  ? 32.449 41.399  29.456  1.00 12.50 ? 365  ASN A ND2 1 
ATOM   2875 N  N   . SER A 1 366  ? 28.890 39.240  33.394  1.00 18.53 ? 366  SER A N   1 
ATOM   2876 C  CA  . SER A 1 366  ? 28.736 38.371  34.579  1.00 21.13 ? 366  SER A CA  1 
ATOM   2877 C  C   . SER A 1 366  ? 27.324 37.853  34.747  1.00 21.96 ? 366  SER A C   1 
ATOM   2878 O  O   . SER A 1 366  ? 27.072 36.987  35.601  1.00 23.39 ? 366  SER A O   1 
ATOM   2879 C  CB  . SER A 1 366  ? 29.165 39.136  35.858  1.00 21.56 ? 366  SER A CB  1 
ATOM   2880 O  OG  . SER A 1 366  ? 28.158 40.064  36.238  1.00 24.15 ? 366  SER A OG  1 
ATOM   2881 N  N   . GLN A 1 367  ? 26.394 38.362  33.970  1.00 22.47 ? 367  GLN A N   1 
ATOM   2882 C  CA  . GLN A 1 367  ? 25.002 37.962  34.035  1.00 23.37 ? 367  GLN A CA  1 
ATOM   2883 C  C   . GLN A 1 367  ? 24.696 37.013  32.874  1.00 23.21 ? 367  GLN A C   1 
ATOM   2884 O  O   . GLN A 1 367  ? 24.310 37.427  31.767  1.00 22.26 ? 367  GLN A O   1 
ATOM   2885 C  CB  . GLN A 1 367  ? 24.105 39.180  33.940  1.00 25.23 ? 367  GLN A CB  1 
ATOM   2886 C  CG  . GLN A 1 367  ? 24.214 40.086  35.144  1.00 28.52 ? 367  GLN A CG  1 
ATOM   2887 C  CD  . GLN A 1 367  ? 23.493 39.476  36.319  1.00 30.15 ? 367  GLN A CD  1 
ATOM   2888 O  OE1 . GLN A 1 367  ? 22.275 39.250  36.249  1.00 31.42 ? 367  GLN A OE1 1 
ATOM   2889 N  NE2 . GLN A 1 367  ? 24.233 39.188  37.402  1.00 31.06 ? 367  GLN A NE2 1 
ATOM   2890 N  N   . ALA A 1 368  ? 24.779 35.722  33.171  1.00 21.99 ? 368  ALA A N   1 
ATOM   2891 C  CA  . ALA A 1 368  ? 24.557 34.693  32.168  1.00 21.01 ? 368  ALA A CA  1 
ATOM   2892 C  C   . ALA A 1 368  ? 23.311 34.853  31.305  1.00 20.46 ? 368  ALA A C   1 
ATOM   2893 O  O   . ALA A 1 368  ? 23.335 34.520  30.100  1.00 20.06 ? 368  ALA A O   1 
ATOM   2894 C  CB  . ALA A 1 368  ? 24.507 33.331  32.865  1.00 21.78 ? 368  ALA A CB  1 
ATOM   2895 N  N   . HIS A 1 369  ? 22.212 35.328  31.895  1.00 19.32 ? 369  HIS A N   1 
ATOM   2896 C  CA  . HIS A 1 369  ? 20.977 35.478  31.167  1.00 19.69 ? 369  HIS A CA  1 
ATOM   2897 C  C   . HIS A 1 369  ? 21.107 36.357  29.930  1.00 18.84 ? 369  HIS A C   1 
ATOM   2898 O  O   . HIS A 1 369  ? 20.296 36.232  29.029  1.00 19.98 ? 369  HIS A O   1 
ATOM   2899 C  CB  . HIS A 1 369  ? 19.843 35.999  32.084  1.00 21.82 ? 369  HIS A CB  1 
ATOM   2900 C  CG  . HIS A 1 369  ? 20.051 37.398  32.570  1.00 23.42 ? 369  HIS A CG  1 
ATOM   2901 N  ND1 . HIS A 1 369  ? 19.621 38.501  31.863  1.00 25.66 ? 369  HIS A ND1 1 
ATOM   2902 C  CD2 . HIS A 1 369  ? 20.698 37.877  33.656  1.00 24.74 ? 369  HIS A CD2 1 
ATOM   2903 C  CE1 . HIS A 1 369  ? 19.997 39.603  32.490  1.00 24.50 ? 369  HIS A CE1 1 
ATOM   2904 N  NE2 . HIS A 1 369  ? 20.655 39.254  33.581  1.00 25.28 ? 369  HIS A NE2 1 
ATOM   2905 N  N   . PHE A 1 370  ? 22.111 37.244  29.875  1.00 18.80 ? 370  PHE A N   1 
ATOM   2906 C  CA  . PHE A 1 370  ? 22.242 38.061  28.640  1.00 17.38 ? 370  PHE A CA  1 
ATOM   2907 C  C   . PHE A 1 370  ? 22.920 37.275  27.506  1.00 15.61 ? 370  PHE A C   1 
ATOM   2908 O  O   . PHE A 1 370  ? 22.696 37.574  26.328  1.00 16.03 ? 370  PHE A O   1 
ATOM   2909 C  CB  . PHE A 1 370  ? 23.123 39.307  28.837  1.00 18.64 ? 370  PHE A CB  1 
ATOM   2910 C  CG  . PHE A 1 370  ? 22.514 40.385  29.682  1.00 19.42 ? 370  PHE A CG  1 
ATOM   2911 C  CD1 . PHE A 1 370  ? 21.349 41.019  29.280  1.00 20.16 ? 370  PHE A CD1 1 
ATOM   2912 C  CD2 . PHE A 1 370  ? 23.157 40.808  30.824  1.00 20.20 ? 370  PHE A CD2 1 
ATOM   2913 C  CE1 . PHE A 1 370  ? 20.817 42.115  30.042  1.00 21.51 ? 370  PHE A CE1 1 
ATOM   2914 C  CE2 . PHE A 1 370  ? 22.643 41.889  31.577  1.00 21.75 ? 370  PHE A CE2 1 
ATOM   2915 C  CZ  . PHE A 1 370  ? 21.496 42.519  31.181  1.00 21.22 ? 370  PHE A CZ  1 
ATOM   2916 N  N   . ASN A 1 371  ? 23.767 36.314  27.875  1.00 14.49 ? 371  ASN A N   1 
ATOM   2917 C  CA  . ASN A 1 371  ? 24.527 35.502  26.939  1.00 13.62 ? 371  ASN A CA  1 
ATOM   2918 C  C   . ASN A 1 371  ? 25.304 36.414  26.004  1.00 13.65 ? 371  ASN A C   1 
ATOM   2919 O  O   . ASN A 1 371  ? 25.308 36.224  24.777  1.00 14.42 ? 371  ASN A O   1 
ATOM   2920 C  CB  . ASN A 1 371  ? 23.596 34.555  26.167  1.00 15.21 ? 371  ASN A CB  1 
ATOM   2921 C  CG  . ASN A 1 371  ? 22.921 33.554  27.096  1.00 15.66 ? 371  ASN A CG  1 
ATOM   2922 O  OD1 . ASN A 1 371  ? 23.597 32.743  27.746  1.00 17.18 ? 371  ASN A OD1 1 
ATOM   2923 N  ND2 . ASN A 1 371  ? 21.619 33.651  27.190  1.00 16.95 ? 371  ASN A ND2 1 
ATOM   2924 N  N   . VAL A 1 372  ? 25.973 37.388  26.617  1.00 12.27 ? 372  VAL A N   1 
ATOM   2925 C  CA  . VAL A 1 372  ? 26.810 38.367  25.888  1.00 13.11 ? 372  VAL A CA  1 
ATOM   2926 C  C   . VAL A 1 372  ? 28.179 38.445  26.503  1.00 13.21 ? 372  VAL A C   1 
ATOM   2927 O  O   . VAL A 1 372  ? 28.327 38.334  27.741  1.00 14.23 ? 372  VAL A O   1 
ATOM   2928 C  CB  . VAL A 1 372  ? 26.171 39.794  25.998  1.00 13.34 ? 372  VAL A CB  1 
ATOM   2929 C  CG1 . VAL A 1 372  ? 27.143 40.927  25.440  1.00 12.99 ? 372  VAL A CG1 1 
ATOM   2930 C  CG2 . VAL A 1 372  ? 24.838 39.841  25.218  1.00 13.54 ? 372  VAL A CG2 1 
ATOM   2931 N  N   . GLN A 1 373  ? 29.210 38.601  25.678  1.00 12.65 ? 373  GLN A N   1 
ATOM   2932 C  CA  . GLN A 1 373  ? 30.587 38.878  26.138  1.00 12.06 ? 373  GLN A CA  1 
ATOM   2933 C  C   . GLN A 1 373  ? 30.955 40.183  25.395  1.00 11.40 ? 373  GLN A C   1 
ATOM   2934 O  O   . GLN A 1 373  ? 31.137 40.173  24.149  1.00 11.61 ? 373  GLN A O   1 
ATOM   2935 C  CB  . GLN A 1 373  ? 31.563 37.759  25.779  1.00 13.44 ? 373  GLN A CB  1 
ATOM   2936 C  CG  . GLN A 1 373  ? 33.049 38.075  26.104  1.00 15.79 ? 373  GLN A CG  1 
ATOM   2937 C  CD  . GLN A 1 373  ? 33.303 38.443  27.575  1.00 17.38 ? 373  GLN A CD  1 
ATOM   2938 O  OE1 . GLN A 1 373  ? 32.565 37.990  28.476  1.00 18.88 ? 373  GLN A OE1 1 
ATOM   2939 N  NE2 . GLN A 1 373  ? 34.333 39.280  27.822  1.00 18.73 ? 373  GLN A NE2 1 
ATOM   2940 N  N   . ALA A 1 374  ? 31.035 41.296  26.112  1.00 11.27 ? 374  ALA A N   1 
ATOM   2941 C  CA  . ALA A 1 374  ? 31.322 42.599  25.526  1.00 11.65 ? 374  ALA A CA  1 
ATOM   2942 C  C   . ALA A 1 374  ? 32.620 43.153  26.000  1.00 11.43 ? 374  ALA A C   1 
ATOM   2943 O  O   . ALA A 1 374  ? 32.998 42.994  27.171  1.00 11.55 ? 374  ALA A O   1 
ATOM   2944 C  CB  . ALA A 1 374  ? 30.191 43.560  25.875  1.00 11.62 ? 374  ALA A CB  1 
ATOM   2945 N  N   . GLN A 1 375  ? 33.330 43.856  25.108  1.00 11.12 ? 375  GLN A N   1 
ATOM   2946 C  CA  . GLN A 1 375  ? 34.629 44.434  25.444  1.00 10.85 ? 375  GLN A CA  1 
ATOM   2947 C  C   . GLN A 1 375  ? 35.038 45.515  24.465  1.00 9.76  ? 375  GLN A C   1 
ATOM   2948 O  O   . GLN A 1 375  ? 34.490 45.591  23.381  1.00 11.07 ? 375  GLN A O   1 
ATOM   2949 C  CB  . GLN A 1 375  ? 35.710 43.363  25.356  1.00 12.10 ? 375  GLN A CB  1 
ATOM   2950 C  CG  . GLN A 1 375  ? 35.723 42.631  23.979  1.00 15.25 ? 375  GLN A CG  1 
ATOM   2951 C  CD  . GLN A 1 375  ? 35.044 41.275  24.082  1.00 18.77 ? 375  GLN A CD  1 
ATOM   2952 O  OE1 . GLN A 1 375  ? 35.490 40.414  24.869  1.00 21.87 ? 375  GLN A OE1 1 
ATOM   2953 N  NE2 . GLN A 1 375  ? 33.941 41.074  23.315  1.00 18.46 ? 375  GLN A NE2 1 
ATOM   2954 N  N   . PHE A 1 376  ? 35.969 46.371  24.894  1.00 10.03 ? 376  PHE A N   1 
ATOM   2955 C  CA  . PHE A 1 376  ? 36.548 47.310  23.930  1.00 10.36 ? 376  PHE A CA  1 
ATOM   2956 C  C   . PHE A 1 376  ? 37.357 46.464  22.942  1.00 11.54 ? 376  PHE A C   1 
ATOM   2957 O  O   . PHE A 1 376  ? 37.990 45.464  23.276  1.00 11.79 ? 376  PHE A O   1 
ATOM   2958 C  CB  . PHE A 1 376  ? 37.520 48.260  24.638  1.00 10.13 ? 376  PHE A CB  1 
ATOM   2959 C  CG  . PHE A 1 376  ? 36.844 49.199  25.556  1.00 10.45 ? 376  PHE A CG  1 
ATOM   2960 C  CD1 . PHE A 1 376  ? 35.823 50.052  25.106  1.00 11.30 ? 376  PHE A CD1 1 
ATOM   2961 C  CD2 . PHE A 1 376  ? 37.227 49.252  26.910  1.00 12.26 ? 376  PHE A CD2 1 
ATOM   2962 C  CE1 . PHE A 1 376  ? 35.186 50.960  26.046  1.00 12.59 ? 376  PHE A CE1 1 
ATOM   2963 C  CE2 . PHE A 1 376  ? 36.585 50.144  27.786  1.00 13.41 ? 376  PHE A CE2 1 
ATOM   2964 C  CZ  . PHE A 1 376  ? 35.602 50.973  27.376  1.00 13.96 ? 376  PHE A CZ  1 
ATOM   2965 N  N   . GLY A 1 377  ? 37.327 46.891  21.667  1.00 10.49 ? 377  GLY A N   1 
ATOM   2966 C  CA  . GLY A 1 377  ? 38.086 46.181  20.665  1.00 10.14 ? 377  GLY A CA  1 
ATOM   2967 C  C   . GLY A 1 377  ? 38.491 47.148  19.566  1.00 9.52  ? 377  GLY A C   1 
ATOM   2968 O  O   . GLY A 1 377  ? 38.188 48.319  19.590  1.00 10.31 ? 377  GLY A O   1 
ATOM   2969 N  N   . THR A 1 378  ? 39.241 46.584  18.619  1.00 11.07 ? 378  THR A N   1 
ATOM   2970 C  CA  . THR A 1 378  ? 39.670 47.344  17.436  1.00 10.86 ? 378  THR A CA  1 
ATOM   2971 C  C   . THR A 1 378  ? 38.917 46.782  16.221  1.00 10.07 ? 378  THR A C   1 
ATOM   2972 O  O   . THR A 1 378  ? 38.210 45.765  16.274  1.00 9.90  ? 378  THR A O   1 
ATOM   2973 C  CB  . THR A 1 378  ? 41.170 47.212  17.156  1.00 11.28 ? 378  THR A CB  1 
ATOM   2974 O  OG1 . THR A 1 378  ? 41.481 45.859  16.804  1.00 11.79 ? 378  THR A OG1 1 
ATOM   2975 C  CG2 . THR A 1 378  ? 42.018 47.594  18.396  1.00 13.23 ? 378  THR A CG2 1 
ATOM   2976 N  N   . LEU A 1 379  ? 39.071 47.459  15.080  1.00 9.55  ? 379  LEU A N   1 
ATOM   2977 C  CA  . LEU A 1 379  ? 38.399 47.038  13.854  1.00 9.02  ? 379  LEU A CA  1 
ATOM   2978 C  C   . LEU A 1 379  ? 38.896 45.708  13.367  1.00 8.45  ? 379  LEU A C   1 
ATOM   2979 O  O   . LEU A 1 379  ? 38.115 44.833  13.004  1.00 9.16  ? 379  LEU A O   1 
ATOM   2980 C  CB  . LEU A 1 379  ? 38.598 48.140  12.804  1.00 9.35  ? 379  LEU A CB  1 
ATOM   2981 C  CG  . LEU A 1 379  ? 37.848 47.899  11.496  1.00 9.27  ? 379  LEU A CG  1 
ATOM   2982 C  CD1 . LEU A 1 379  ? 36.298 47.926  11.764  1.00 9.70  ? 379  LEU A CD1 1 
ATOM   2983 C  CD2 . LEU A 1 379  ? 38.260 49.032  10.486  1.00 9.62  ? 379  LEU A CD2 1 
ATOM   2984 N  N   . GLN A 1 380  ? 40.222 45.510  13.400  1.00 8.69  ? 380  GLN A N   1 
ATOM   2985 C  CA  . GLN A 1 380  ? 40.784 44.221  12.948  1.00 9.82  ? 380  GLN A CA  1 
ATOM   2986 C  C   . GLN A 1 380  ? 40.272 43.091  13.850  1.00 10.33 ? 380  GLN A C   1 
ATOM   2987 O  O   . GLN A 1 380  ? 40.012 41.984  13.357  1.00 9.85  ? 380  GLN A O   1 
ATOM   2988 C  CB  . GLN A 1 380  ? 42.312 44.275  12.955  1.00 10.98 ? 380  GLN A CB  1 
ATOM   2989 C  CG  . GLN A 1 380  ? 42.923 42.956  12.425  1.00 12.54 ? 380  GLN A CG  1 
ATOM   2990 C  CD  . GLN A 1 380  ? 42.636 42.803  10.964  1.00 14.16 ? 380  GLN A CD  1 
ATOM   2991 O  OE1 . GLN A 1 380  ? 42.695 43.789  10.200  1.00 14.69 ? 380  GLN A OE1 1 
ATOM   2992 N  NE2 . GLN A 1 380  ? 42.320 41.557  10.532  1.00 17.65 ? 380  GLN A NE2 1 
ATOM   2993 N  N   . GLU A 1 381  ? 40.123 43.362  15.149  1.00 10.55 ? 381  GLU A N   1 
ATOM   2994 C  CA  . GLU A 1 381  ? 39.641 42.310  16.040  1.00 10.42 ? 381  GLU A CA  1 
ATOM   2995 C  C   . GLU A 1 381  ? 38.215 41.895  15.656  1.00 9.46  ? 381  GLU A C   1 
ATOM   2996 O  O   . GLU A 1 381  ? 37.885 40.719  15.669  1.00 11.11 ? 381  GLU A O   1 
ATOM   2997 C  CB  . GLU A 1 381  ? 39.623 42.800  17.486  1.00 12.16 ? 381  GLU A CB  1 
ATOM   2998 C  CG  . GLU A 1 381  ? 40.927 42.813  18.276  1.00 17.06 ? 381  GLU A CG  1 
ATOM   2999 C  CD  . GLU A 1 381  ? 40.538 43.132  19.737  1.00 19.57 ? 381  GLU A CD  1 
ATOM   3000 O  OE1 . GLU A 1 381  ? 40.359 44.285  20.019  1.00 20.09 ? 381  GLU A OE1 1 
ATOM   3001 O  OE2 . GLU A 1 381  ? 40.345 42.213  20.608  1.00 23.53 ? 381  GLU A OE2 1 
ATOM   3002 N  N   . TYR A 1 382  ? 37.370 42.864  15.306  1.00 9.85  ? 382  TYR A N   1 
ATOM   3003 C  CA  . TYR A 1 382  ? 36.044 42.551  14.871  1.00 8.76  ? 382  TYR A CA  1 
ATOM   3004 C  C   . TYR A 1 382  ? 36.096 41.656  13.629  1.00 8.80  ? 382  TYR A C   1 
ATOM   3005 O  O   . TYR A 1 382  ? 35.448 40.616  13.553  1.00 9.56  ? 382  TYR A O   1 
ATOM   3006 C  CB  . TYR A 1 382  ? 35.276 43.834  14.507  1.00 9.07  ? 382  TYR A CB  1 
ATOM   3007 C  CG  . TYR A 1 382  ? 33.952 43.552  13.818  1.00 8.76  ? 382  TYR A CG  1 
ATOM   3008 C  CD1 . TYR A 1 382  ? 32.881 42.959  14.506  1.00 9.34  ? 382  TYR A CD1 1 
ATOM   3009 C  CD2 . TYR A 1 382  ? 33.795 43.813  12.438  1.00 9.26  ? 382  TYR A CD2 1 
ATOM   3010 C  CE1 . TYR A 1 382  ? 31.694 42.633  13.850  1.00 9.87  ? 382  TYR A CE1 1 
ATOM   3011 C  CE2 . TYR A 1 382  ? 32.631 43.490  11.798  1.00 9.65  ? 382  TYR A CE2 1 
ATOM   3012 C  CZ  . TYR A 1 382  ? 31.584 42.891  12.510  1.00 9.15  ? 382  TYR A CZ  1 
ATOM   3013 O  OH  . TYR A 1 382  ? 30.405 42.516  11.889  1.00 10.09 ? 382  TYR A OH  1 
ATOM   3014 N  N   . PHE A 1 383  ? 36.792 42.118  12.593  1.00 8.72  ? 383  PHE A N   1 
ATOM   3015 C  CA  . PHE A 1 383  ? 36.839 41.316  11.373  1.00 8.93  ? 383  PHE A CA  1 
ATOM   3016 C  C   . PHE A 1 383  ? 37.447 39.930  11.582  1.00 9.18  ? 383  PHE A C   1 
ATOM   3017 O  O   . PHE A 1 383  ? 36.947 38.958  11.004  1.00 10.97 ? 383  PHE A O   1 
ATOM   3018 C  CB  . PHE A 1 383  ? 37.616 42.070  10.258  1.00 8.56  ? 383  PHE A CB  1 
ATOM   3019 C  CG  . PHE A 1 383  ? 36.841 43.220  9.641   1.00 8.90  ? 383  PHE A CG  1 
ATOM   3020 C  CD1 . PHE A 1 383  ? 35.615 43.002  8.990   1.00 8.81  ? 383  PHE A CD1 1 
ATOM   3021 C  CD2 . PHE A 1 383  ? 37.390 44.522  9.676   1.00 9.04  ? 383  PHE A CD2 1 
ATOM   3022 C  CE1 . PHE A 1 383  ? 34.920 44.079  8.364   1.00 9.56  ? 383  PHE A CE1 1 
ATOM   3023 C  CE2 . PHE A 1 383  ? 36.701 45.594  9.053   1.00 8.64  ? 383  PHE A CE2 1 
ATOM   3024 C  CZ  . PHE A 1 383  ? 35.484 45.365  8.408   1.00 9.08  ? 383  PHE A CZ  1 
ATOM   3025 N  N   . ASP A 1 384  ? 38.487 39.834  12.412  1.00 10.72 ? 384  ASP A N   1 
ATOM   3026 C  CA  . ASP A 1 384  ? 39.073 38.502  12.640  1.00 11.81 ? 384  ASP A CA  1 
ATOM   3027 C  C   . ASP A 1 384  ? 38.013 37.575  13.281  1.00 11.35 ? 384  ASP A C   1 
ATOM   3028 O  O   . ASP A 1 384  ? 37.908 36.381  12.903  1.00 12.02 ? 384  ASP A O   1 
ATOM   3029 C  CB  . ASP A 1 384  ? 40.276 38.582  13.580  1.00 12.92 ? 384  ASP A CB  1 
ATOM   3030 C  CG  . ASP A 1 384  ? 41.495 39.196  12.952  1.00 15.18 ? 384  ASP A CG  1 
ATOM   3031 O  OD1 . ASP A 1 384  ? 41.607 39.288  11.703  1.00 15.86 ? 384  ASP A OD1 1 
ATOM   3032 O  OD2 . ASP A 1 384  ? 42.356 39.563  13.795  1.00 17.79 ? 384  ASP A OD2 1 
ATOM   3033 N  N   . ALA A 1 385  ? 37.197 38.093  14.193  1.00 10.80 ? 385  ALA A N   1 
ATOM   3034 C  CA  . ALA A 1 385  ? 36.193 37.267  14.821  1.00 11.43 ? 385  ALA A CA  1 
ATOM   3035 C  C   . ALA A 1 385  ? 35.082 36.937  13.845  1.00 12.00 ? 385  ALA A C   1 
ATOM   3036 O  O   . ALA A 1 385  ? 34.571 35.823  13.857  1.00 12.01 ? 385  ALA A O   1 
ATOM   3037 C  CB  . ALA A 1 385  ? 35.675 37.969  16.093  1.00 11.40 ? 385  ALA A CB  1 
ATOM   3038 N  N   . VAL A 1 386  ? 34.711 37.863  12.951  1.00 10.84 ? 386  VAL A N   1 
ATOM   3039 C  CA  . VAL A 1 386  ? 33.674 37.538  11.985  1.00 11.09 ? 386  VAL A CA  1 
ATOM   3040 C  C   . VAL A 1 386  ? 34.163 36.405  11.078  1.00 11.71 ? 386  VAL A C   1 
ATOM   3041 O  O   . VAL A 1 386  ? 33.387 35.471  10.787  1.00 12.12 ? 386  VAL A O   1 
ATOM   3042 C  CB  . VAL A 1 386  ? 33.379 38.776  11.106  1.00 9.77  ? 386  VAL A CB  1 
ATOM   3043 C  CG1 . VAL A 1 386  ? 32.543 38.403  9.879   1.00 12.14 ? 386  VAL A CG1 1 
ATOM   3044 C  CG2 . VAL A 1 386  ? 32.629 39.806  11.934  1.00 12.24 ? 386  VAL A CG2 1 
ATOM   3045 N  N   . HIS A 1 387  ? 35.410 36.457  10.635  1.00 11.71 ? 387  HIS A N   1 
ATOM   3046 C  CA  . HIS A 1 387  ? 35.895 35.402  9.739   1.00 12.93 ? 387  HIS A CA  1 
ATOM   3047 C  C   . HIS A 1 387  ? 36.112 34.065  10.459  1.00 13.36 ? 387  HIS A C   1 
ATOM   3048 O  O   . HIS A 1 387  ? 35.984 33.006  9.822   1.00 13.97 ? 387  HIS A O   1 
ATOM   3049 C  CB  . HIS A 1 387  ? 37.141 35.856  8.972   1.00 12.88 ? 387  HIS A CB  1 
ATOM   3050 C  CG  . HIS A 1 387  ? 36.844 36.966  7.995   1.00 11.95 ? 387  HIS A CG  1 
ATOM   3051 N  ND1 . HIS A 1 387  ? 35.939 36.820  6.957   1.00 13.94 ? 387  HIS A ND1 1 
ATOM   3052 C  CD2 . HIS A 1 387  ? 37.274 38.250  7.950   1.00 12.51 ? 387  HIS A CD2 1 
ATOM   3053 C  CE1 . HIS A 1 387  ? 35.836 37.977  6.308   1.00 14.75 ? 387  HIS A CE1 1 
ATOM   3054 N  NE2 . HIS A 1 387  ? 36.640 38.856  6.890   1.00 12.52 ? 387  HIS A NE2 1 
ATOM   3055 N  N   . GLN A 1 388  ? 36.379 34.122  11.766  1.00 13.62 ? 388  GLN A N   1 
ATOM   3056 C  CA  . GLN A 1 388  ? 36.483 32.852  12.534  1.00 14.74 ? 388  GLN A CA  1 
ATOM   3057 C  C   . GLN A 1 388  ? 35.081 32.227  12.532  1.00 15.83 ? 388  GLN A C   1 
ATOM   3058 O  O   . GLN A 1 388  ? 34.951 31.014  12.379  1.00 16.28 ? 388  GLN A O   1 
ATOM   3059 C  CB  . GLN A 1 388  ? 36.993 33.169  13.927  1.00 16.20 ? 388  GLN A CB  1 
ATOM   3060 C  CG  . GLN A 1 388  ? 38.517 33.435  13.928  1.00 21.20 ? 388  GLN A CG  1 
ATOM   3061 C  CD  . GLN A 1 388  ? 39.023 34.251  15.167  1.00 24.91 ? 388  GLN A CD  1 
ATOM   3062 O  OE1 . GLN A 1 388  ? 40.222 34.631  15.256  1.00 27.34 ? 388  GLN A OE1 1 
ATOM   3063 N  NE2 . GLN A 1 388  ? 38.114 34.523  16.114  1.00 26.28 ? 388  GLN A NE2 1 
ATOM   3064 N  N   . ALA A 1 389  ? 34.029 33.026  12.675  1.00 15.74 ? 389  ALA A N   1 
ATOM   3065 C  CA  . ALA A 1 389  ? 32.634 32.537  12.680  1.00 16.93 ? 389  ALA A CA  1 
ATOM   3066 C  C   . ALA A 1 389  ? 32.322 31.932  11.319  1.00 18.21 ? 389  ALA A C   1 
ATOM   3067 O  O   . ALA A 1 389  ? 31.748 30.840  11.210  1.00 18.76 ? 389  ALA A O   1 
ATOM   3068 C  CB  . ALA A 1 389  ? 31.679 33.685  12.999  1.00 16.48 ? 389  ALA A CB  1 
ATOM   3069 N  N   . GLU A 1 390  ? 32.695 32.636  10.261  1.00 18.22 ? 390  GLU A N   1 
ATOM   3070 C  CA  . GLU A 1 390  ? 32.495 32.165  8.901   1.00 20.20 ? 390  GLU A CA  1 
ATOM   3071 C  C   . GLU A 1 390  ? 33.177 30.808  8.708   1.00 21.10 ? 390  GLU A C   1 
ATOM   3072 O  O   . GLU A 1 390  ? 32.549 29.872  8.180   1.00 21.88 ? 390  GLU A O   1 
ATOM   3073 C  CB  . GLU A 1 390  ? 33.080 33.202  7.932   1.00 19.62 ? 390  GLU A CB  1 
ATOM   3074 C  CG  . GLU A 1 390  ? 33.024 32.874  6.436   1.00 21.69 ? 390  GLU A CG  1 
ATOM   3075 C  CD  . GLU A 1 390  ? 33.755 33.926  5.606   1.00 22.57 ? 390  GLU A CD  1 
ATOM   3076 O  OE1 . GLU A 1 390  ? 34.603 34.653  6.172   1.00 22.32 ? 390  GLU A OE1 1 
ATOM   3077 O  OE2 . GLU A 1 390  ? 33.504 34.028  4.383   1.00 24.83 ? 390  GLU A OE2 1 
ATOM   3078 N  N   . ARG A 1 391  ? 34.436 30.691  9.123   1.00 21.89 ? 391  ARG A N   1 
ATOM   3079 C  CA  . ARG A 1 391  ? 35.165 29.428  8.958   1.00 23.51 ? 391  ARG A CA  1 
ATOM   3080 C  C   . ARG A 1 391  ? 34.527 28.311  9.780   1.00 23.35 ? 391  ARG A C   1 
ATOM   3081 O  O   . ARG A 1 391  ? 34.594 27.130  9.383   1.00 24.32 ? 391  ARG A O   1 
ATOM   3082 C  CB  . ARG A 1 391  ? 36.638 29.589  9.335   1.00 24.27 ? 391  ARG A CB  1 
ATOM   3083 C  CG  . ARG A 1 391  ? 37.417 30.458  8.338   1.00 27.36 ? 391  ARG A CG  1 
ATOM   3084 C  CD  . ARG A 1 391  ? 38.926 30.332  8.534   1.00 28.49 ? 391  ARG A CD  1 
ATOM   3085 N  NE  . ARG A 1 391  ? 39.373 30.810  9.842   1.00 30.80 ? 391  ARG A NE  1 
ATOM   3086 C  CZ  . ARG A 1 391  ? 39.562 32.094  10.157  1.00 31.23 ? 391  ARG A CZ  1 
ATOM   3087 N  NH1 . ARG A 1 391  ? 39.343 33.051  9.260   1.00 31.36 ? 391  ARG A NH1 1 
ATOM   3088 N  NH2 . ARG A 1 391  ? 39.972 32.409  11.375  1.00 32.33 ? 391  ARG A NH2 1 
ATOM   3089 N  N   . ALA A 1 392  ? 33.879 28.668  10.883  1.00 23.55 ? 392  ALA A N   1 
ATOM   3090 C  CA  . ALA A 1 392  ? 33.212 27.669  11.733  1.00 24.03 ? 392  ALA A CA  1 
ATOM   3091 C  C   . ALA A 1 392  ? 31.877 27.260  11.081  1.00 24.87 ? 392  ALA A C   1 
ATOM   3092 O  O   . ALA A 1 392  ? 31.073 26.505  11.691  1.00 26.58 ? 392  ALA A O   1 
ATOM   3093 C  CB  . ALA A 1 392  ? 32.960 28.242  13.118  1.00 24.01 ? 392  ALA A CB  1 
ATOM   3094 N  N   . GLY A 1 393  ? 31.620 27.776  9.873   1.00 24.89 ? 393  GLY A N   1 
ATOM   3095 C  CA  . GLY A 1 393  ? 30.391 27.453  9.166   1.00 24.23 ? 393  GLY A CA  1 
ATOM   3096 C  C   . GLY A 1 393  ? 29.160 28.150  9.669   1.00 23.73 ? 393  GLY A C   1 
ATOM   3097 O  O   . GLY A 1 393  ? 28.042 27.761  9.339   1.00 24.33 ? 393  GLY A O   1 
ATOM   3098 N  N   . GLN A 1 394  ? 29.326 29.228  10.431  1.00 23.27 ? 394  GLN A N   1 
ATOM   3099 C  CA  . GLN A 1 394  ? 28.132 29.855  10.940  1.00 23.89 ? 394  GLN A CA  1 
ATOM   3100 C  C   . GLN A 1 394  ? 27.497 30.896  10.024  1.00 22.54 ? 394  GLN A C   1 
ATOM   3101 O  O   . GLN A 1 394  ? 26.359 31.328  10.273  1.00 23.94 ? 394  GLN A O   1 
ATOM   3102 C  CB  . GLN A 1 394  ? 28.365 30.351  12.387  1.00 25.90 ? 394  GLN A CB  1 
ATOM   3103 C  CG  . GLN A 1 394  ? 28.934 31.699  12.569  1.00 28.17 ? 394  GLN A CG  1 
ATOM   3104 C  CD  . GLN A 1 394  ? 28.732 32.204  14.008  1.00 27.79 ? 394  GLN A CD  1 
ATOM   3105 O  OE1 . GLN A 1 394  ? 29.232 31.615  14.993  1.00 28.28 ? 394  GLN A OE1 1 
ATOM   3106 N  NE2 . GLN A 1 394  ? 28.014 33.285  14.127  1.00 25.02 ? 394  GLN A NE2 1 
ATOM   3107 N  N   . ALA A 1 395  ? 28.169 31.258  8.916   1.00 20.96 ? 395  ALA A N   1 
ATOM   3108 C  CA  . ALA A 1 395  ? 27.593 32.241  7.993   1.00 20.42 ? 395  ALA A CA  1 
ATOM   3109 C  C   . ALA A 1 395  ? 28.265 32.138  6.621   1.00 19.87 ? 395  ALA A C   1 
ATOM   3110 O  O   . ALA A 1 395  ? 29.405 31.696  6.514   1.00 19.88 ? 395  ALA A O   1 
ATOM   3111 C  CB  . ALA A 1 395  ? 27.817 33.676  8.576   1.00 21.49 ? 395  ALA A CB  1 
ATOM   3112 N  N   . GLU A 1 396  ? 27.543 32.506  5.574   1.00 19.72 ? 396  GLU A N   1 
ATOM   3113 C  CA  . GLU A 1 396  ? 28.105 32.563  4.226   1.00 20.30 ? 396  GLU A CA  1 
ATOM   3114 C  C   . GLU A 1 396  ? 27.698 33.987  3.816   1.00 18.80 ? 396  GLU A C   1 
ATOM   3115 O  O   . GLU A 1 396  ? 26.597 34.472  4.171   1.00 19.43 ? 396  GLU A O   1 
ATOM   3116 C  CB  . GLU A 1 396  ? 27.490 31.518  3.293   1.00 24.33 ? 396  GLU A CB  1 
ATOM   3117 C  CG  . GLU A 1 396  ? 26.014 31.708  3.087   1.00 30.12 ? 396  GLU A CG  1 
ATOM   3118 C  CD  . GLU A 1 396  ? 25.302 30.429  2.662   1.00 33.57 ? 396  GLU A CD  1 
ATOM   3119 O  OE1 . GLU A 1 396  ? 25.646 29.876  1.584   1.00 35.92 ? 396  GLU A OE1 1 
ATOM   3120 O  OE2 . GLU A 1 396  ? 24.393 29.979  3.414   1.00 36.80 ? 396  GLU A OE2 1 
ATOM   3121 N  N   . PHE A 1 397  ? 28.582 34.650  3.095   1.00 15.24 ? 397  PHE A N   1 
ATOM   3122 C  CA  . PHE A 1 397  ? 28.317 36.030  2.741   1.00 13.17 ? 397  PHE A CA  1 
ATOM   3123 C  C   . PHE A 1 397  ? 27.998 36.193  1.256   1.00 11.45 ? 397  PHE A C   1 
ATOM   3124 O  O   . PHE A 1 397  ? 28.558 35.481  0.423   1.00 13.61 ? 397  PHE A O   1 
ATOM   3125 C  CB  . PHE A 1 397  ? 29.555 36.844  3.104   1.00 12.61 ? 397  PHE A CB  1 
ATOM   3126 C  CG  . PHE A 1 397  ? 29.813 36.913  4.588   1.00 11.57 ? 397  PHE A CG  1 
ATOM   3127 C  CD1 . PHE A 1 397  ? 28.947 37.637  5.409   1.00 10.73 ? 397  PHE A CD1 1 
ATOM   3128 C  CD2 . PHE A 1 397  ? 30.888 36.230  5.146   1.00 13.04 ? 397  PHE A CD2 1 
ATOM   3129 C  CE1 . PHE A 1 397  ? 29.142 37.674  6.781   1.00 11.52 ? 397  PHE A CE1 1 
ATOM   3130 C  CE2 . PHE A 1 397  ? 31.089 36.261  6.560   1.00 13.61 ? 397  PHE A CE2 1 
ATOM   3131 C  CZ  . PHE A 1 397  ? 30.207 36.984  7.342   1.00 12.38 ? 397  PHE A CZ  1 
ATOM   3132 N  N   . PRO A 1 398  ? 27.083 37.102  0.952   1.00 10.55 ? 398  PRO A N   1 
ATOM   3133 C  CA  . PRO A 1 398  ? 26.698 37.353  -0.442  1.00 11.08 ? 398  PRO A CA  1 
ATOM   3134 C  C   . PRO A 1 398  ? 27.771 38.133  -1.198  1.00 10.05 ? 398  PRO A C   1 
ATOM   3135 O  O   . PRO A 1 398  ? 28.599 38.821  -0.579  1.00 10.10 ? 398  PRO A O   1 
ATOM   3136 C  CB  . PRO A 1 398  ? 25.417 38.167  -0.290  1.00 12.52 ? 398  PRO A CB  1 
ATOM   3137 C  CG  . PRO A 1 398  ? 25.724 39.024  0.982   1.00 11.72 ? 398  PRO A CG  1 
ATOM   3138 C  CD  . PRO A 1 398  ? 26.315 37.940  1.887   1.00 11.14 ? 398  PRO A CD  1 
ATOM   3139 N  N   . THR A 1 399  ? 27.747 38.005  -2.517  1.00 9.84  ? 399  THR A N   1 
ATOM   3140 C  CA  . THR A 1 399  ? 28.639 38.748  -3.399  1.00 9.32  ? 399  THR A CA  1 
ATOM   3141 C  C   . THR A 1 399  ? 27.837 39.971  -3.905  1.00 9.46  ? 399  THR A C   1 
ATOM   3142 O  O   . THR A 1 399  ? 26.615 39.962  -4.062  1.00 9.60  ? 399  THR A O   1 
ATOM   3143 C  CB  . THR A 1 399  ? 29.046 37.883  -4.597  1.00 9.37  ? 399  THR A CB  1 
ATOM   3144 O  OG1 . THR A 1 399  ? 27.858 37.438  -5.269  1.00 10.92 ? 399  THR A OG1 1 
ATOM   3145 C  CG2 . THR A 1 399  ? 29.836 36.669  -4.101  1.00 11.74 ? 399  THR A CG2 1 
ATOM   3146 N  N   . LEU A 1 400  ? 28.585 41.050  -4.156  1.00 8.31  ? 400  LEU A N   1 
ATOM   3147 C  CA  . LEU A 1 400  ? 27.991 42.290  -4.608  1.00 7.92  ? 400  LEU A CA  1 
ATOM   3148 C  C   . LEU A 1 400  ? 28.903 43.012  -5.568  1.00 7.56  ? 400  LEU A C   1 
ATOM   3149 O  O   . LEU A 1 400  ? 30.138 43.002  -5.454  1.00 8.26  ? 400  LEU A O   1 
ATOM   3150 C  CB  . LEU A 1 400  ? 27.751 43.199  -3.375  1.00 8.53  ? 400  LEU A CB  1 
ATOM   3151 C  CG  . LEU A 1 400  ? 27.038 44.561  -3.632  1.00 8.45  ? 400  LEU A CG  1 
ATOM   3152 C  CD1 . LEU A 1 400  ? 26.213 44.909  -2.357  1.00 10.10 ? 400  LEU A CD1 1 
ATOM   3153 C  CD2 . LEU A 1 400  ? 28.063 45.692  -3.911  1.00 9.44  ? 400  LEU A CD2 1 
ATOM   3154 N  N   . SER A 1 401  ? 28.283 43.648  -6.564  1.00 7.61  ? 401  SER A N   1 
ATOM   3155 C  CA  . SER A 1 401  ? 29.047 44.573  -7.422  1.00 7.92  ? 401  SER A CA  1 
ATOM   3156 C  C   . SER A 1 401  ? 28.183 45.822  -7.606  1.00 7.60  ? 401  SER A C   1 
ATOM   3157 O  O   . SER A 1 401  ? 26.946 45.814  -7.409  1.00 7.44  ? 401  SER A O   1 
ATOM   3158 C  CB  . SER A 1 401  ? 29.423 43.984  -8.787  1.00 8.16  ? 401  SER A CB  1 
ATOM   3159 O  OG  . SER A 1 401  ? 28.315 43.948  -9.686  1.00 8.67  ? 401  SER A OG  1 
ATOM   3160 N  N   . GLY A 1 402  ? 28.864 46.913  -7.965  1.00 7.29  ? 402  GLY A N   1 
ATOM   3161 C  CA  . GLY A 1 402  ? 28.207 48.194  -8.205  1.00 7.84  ? 402  GLY A CA  1 
ATOM   3162 C  C   . GLY A 1 402  ? 28.818 49.286  -7.334  1.00 7.01  ? 402  GLY A C   1 
ATOM   3163 O  O   . GLY A 1 402  ? 29.872 49.087  -6.715  1.00 8.72  ? 402  GLY A O   1 
ATOM   3164 N  N   . ASP A 1 403  ? 28.162 50.431  -7.304  1.00 7.25  ? 403  ASP A N   1 
ATOM   3165 C  CA  . ASP A 1 403  ? 28.647 51.571  -6.475  1.00 7.71  ? 403  ASP A CA  1 
ATOM   3166 C  C   . ASP A 1 403  ? 27.530 52.033  -5.564  1.00 7.07  ? 403  ASP A C   1 
ATOM   3167 O  O   . ASP A 1 403  ? 26.450 51.455  -5.530  1.00 8.18  ? 403  ASP A O   1 
ATOM   3168 C  CB  . ASP A 1 403  ? 29.166 52.723  -7.360  1.00 7.53  ? 403  ASP A CB  1 
ATOM   3169 C  CG  . ASP A 1 403  ? 28.059 53.505  -8.043  1.00 8.46  ? 403  ASP A CG  1 
ATOM   3170 O  OD1 . ASP A 1 403  ? 26.918 53.037  -8.096  1.00 11.45 ? 403  ASP A OD1 1 
ATOM   3171 O  OD2 . ASP A 1 403  ? 28.390 54.597  -8.516  1.00 10.96 ? 403  ASP A OD2 1 
ATOM   3172 N  N   . PHE A 1 404  ? 27.816 53.035  -4.756  1.00 6.63  ? 404  PHE A N   1 
ATOM   3173 C  CA  . PHE A 1 404  ? 26.876 53.605  -3.803  1.00 6.70  ? 404  PHE A CA  1 
ATOM   3174 C  C   . PHE A 1 404  ? 26.777 55.105  -3.966  1.00 6.85  ? 404  PHE A C   1 
ATOM   3175 O  O   . PHE A 1 404  ? 26.896 55.886  -3.006  1.00 7.80  ? 404  PHE A O   1 
ATOM   3176 C  CB  . PHE A 1 404  ? 27.234 53.211  -2.352  1.00 7.21  ? 404  PHE A CB  1 
ATOM   3177 C  CG  . PHE A 1 404  ? 27.213 51.726  -2.133  1.00 7.35  ? 404  PHE A CG  1 
ATOM   3178 C  CD1 . PHE A 1 404  ? 25.982 51.051  -1.996  1.00 8.06  ? 404  PHE A CD1 1 
ATOM   3179 C  CD2 . PHE A 1 404  ? 28.399 50.993  -2.125  1.00 6.99  ? 404  PHE A CD2 1 
ATOM   3180 C  CE1 . PHE A 1 404  ? 25.945 49.620  -1.858  1.00 7.87  ? 404  PHE A CE1 1 
ATOM   3181 C  CE2 . PHE A 1 404  ? 28.367 49.586  -1.988  1.00 7.97  ? 404  PHE A CE2 1 
ATOM   3182 C  CZ  . PHE A 1 404  ? 27.121 48.902  -1.863  1.00 7.99  ? 404  PHE A CZ  1 
ATOM   3183 N  N   . PHE A 1 405  ? 26.529 55.495  -5.206  1.00 7.76  ? 405  PHE A N   1 
ATOM   3184 C  CA  . PHE A 1 405  ? 26.210 56.887  -5.535  1.00 6.09  ? 405  PHE A CA  1 
ATOM   3185 C  C   . PHE A 1 405  ? 24.838 56.856  -6.225  1.00 8.12  ? 405  PHE A C   1 
ATOM   3186 O  O   . PHE A 1 405  ? 24.501 55.881  -6.911  1.00 8.94  ? 405  PHE A O   1 
ATOM   3187 C  CB  . PHE A 1 405  ? 27.230 57.474  -6.540  1.00 7.60  ? 405  PHE A CB  1 
ATOM   3188 C  CG  . PHE A 1 405  ? 28.600 57.598  -5.985  1.00 7.51  ? 405  PHE A CG  1 
ATOM   3189 C  CD1 . PHE A 1 405  ? 28.838 58.450  -4.894  1.00 7.75  ? 405  PHE A CD1 1 
ATOM   3190 C  CD2 . PHE A 1 405  ? 29.645 56.893  -6.557  1.00 7.89  ? 405  PHE A CD2 1 
ATOM   3191 C  CE1 . PHE A 1 405  ? 30.166 58.582  -4.354  1.00 7.73  ? 405  PHE A CE1 1 
ATOM   3192 C  CE2 . PHE A 1 405  ? 30.953 57.003  -6.036  1.00 8.09  ? 405  PHE A CE2 1 
ATOM   3193 C  CZ  . PHE A 1 405  ? 31.189 57.853  -4.920  1.00 7.30  ? 405  PHE A CZ  1 
ATOM   3194 N  N   . THR A 1 406  ? 24.019 57.893  -6.112  1.00 7.28  ? 406  THR A N   1 
ATOM   3195 C  CA  . THR A 1 406  ? 24.218 59.087  -5.315  1.00 7.22  ? 406  THR A CA  1 
ATOM   3196 C  C   . THR A 1 406  ? 23.562 58.966  -3.964  1.00 7.46  ? 406  THR A C   1 
ATOM   3197 O  O   . THR A 1 406  ? 22.376 58.587  -3.817  1.00 8.58  ? 406  THR A O   1 
ATOM   3198 C  CB  . THR A 1 406  ? 23.683 60.304  -6.120  1.00 7.32  ? 406  THR A CB  1 
ATOM   3199 O  OG1 . THR A 1 406  ? 24.624 60.528  -7.170  1.00 8.08  ? 406  THR A OG1 1 
ATOM   3200 C  CG2 . THR A 1 406  ? 23.568 61.586  -5.291  1.00 8.51  ? 406  THR A CG2 1 
ATOM   3201 N  N   . TYR A 1 407  ? 24.346 59.288  -2.950  1.00 7.66  ? 407  TYR A N   1 
ATOM   3202 C  CA  . TYR A 1 407  ? 23.916 59.219  -1.571  1.00 7.21  ? 407  TYR A CA  1 
ATOM   3203 C  C   . TYR A 1 407  ? 22.833 60.199  -1.196  1.00 7.77  ? 407  TYR A C   1 
ATOM   3204 O  O   . TYR A 1 407  ? 22.853 61.346  -1.617  1.00 8.05  ? 407  TYR A O   1 
ATOM   3205 C  CB  . TYR A 1 407  ? 25.162 59.530  -0.690  1.00 8.31  ? 407  TYR A CB  1 
ATOM   3206 C  CG  . TYR A 1 407  ? 24.919 59.662  0.784   1.00 7.22  ? 407  TYR A CG  1 
ATOM   3207 C  CD1 . TYR A 1 407  ? 24.438 58.575  1.555   1.00 8.40  ? 407  TYR A CD1 1 
ATOM   3208 C  CD2 . TYR A 1 407  ? 25.252 60.833  1.444   1.00 7.63  ? 407  TYR A CD2 1 
ATOM   3209 C  CE1 . TYR A 1 407  ? 24.330 58.689  2.937   1.00 7.94  ? 407  TYR A CE1 1 
ATOM   3210 C  CE2 . TYR A 1 407  ? 25.147 60.966  2.822   1.00 7.81  ? 407  TYR A CE2 1 
ATOM   3211 C  CZ  . TYR A 1 407  ? 24.697 59.884  3.574   1.00 8.41  ? 407  TYR A CZ  1 
ATOM   3212 O  OH  . TYR A 1 407  ? 24.705 59.990  4.951   1.00 8.56  ? 407  TYR A OH  1 
ATOM   3213 N  N   . ALA A 1 408  ? 21.864 59.708  -0.418  1.00 8.32  ? 408  ALA A N   1 
ATOM   3214 C  CA  . ALA A 1 408  ? 20.904 60.599  0.269   1.00 8.64  ? 408  ALA A CA  1 
ATOM   3215 C  C   . ALA A 1 408  ? 20.842 60.126  1.704   1.00 8.67  ? 408  ALA A C   1 
ATOM   3216 O  O   . ALA A 1 408  ? 20.707 58.898  1.972   1.00 8.87  ? 408  ALA A O   1 
ATOM   3217 C  CB  . ALA A 1 408  ? 19.475 60.550  -0.356  1.00 9.84  ? 408  ALA A CB  1 
ATOM   3218 N  N   . ASP A 1 409  ? 20.953 61.072  2.651   1.00 8.26  ? 409  ASP A N   1 
ATOM   3219 C  CA  . ASP A 1 409  ? 20.877 60.702  4.052   1.00 9.21  ? 409  ASP A CA  1 
ATOM   3220 C  C   . ASP A 1 409  ? 19.448 60.769  4.591   1.00 9.78  ? 409  ASP A C   1 
ATOM   3221 O  O   . ASP A 1 409  ? 19.181 60.163  5.634   1.00 10.81 ? 409  ASP A O   1 
ATOM   3222 C  CB  . ASP A 1 409  ? 21.832 61.562  4.934   1.00 9.19  ? 409  ASP A CB  1 
ATOM   3223 C  CG  . ASP A 1 409  ? 21.599 63.074  4.842   1.00 8.39  ? 409  ASP A CG  1 
ATOM   3224 O  OD1 . ASP A 1 409  ? 20.972 63.593  3.901   1.00 9.30  ? 409  ASP A OD1 1 
ATOM   3225 O  OD2 . ASP A 1 409  ? 22.142 63.758  5.735   1.00 9.93  ? 409  ASP A OD2 1 
ATOM   3226 N  N   . ARG A 1 410  ? 18.559 61.498  3.915   1.00 9.53  ? 410  ARG A N   1 
ATOM   3227 C  CA  . ARG A 1 410  ? 17.153 61.602  4.360   1.00 10.62 ? 410  ARG A CA  1 
ATOM   3228 C  C   . ARG A 1 410  ? 16.339 62.241  3.248   1.00 11.92 ? 410  ARG A C   1 
ATOM   3229 O  O   . ARG A 1 410  ? 16.892 62.979  2.398   1.00 12.03 ? 410  ARG A O   1 
ATOM   3230 C  CB  . ARG A 1 410  ? 17.048 62.433  5.646   1.00 11.73 ? 410  ARG A CB  1 
ATOM   3231 C  CG  . ARG A 1 410  ? 17.526 63.870  5.545   1.00 13.06 ? 410  ARG A CG  1 
ATOM   3232 C  CD  . ARG A 1 410  ? 17.472 64.424  6.953   1.00 13.80 ? 410  ARG A CD  1 
ATOM   3233 N  NE  . ARG A 1 410  ? 18.147 65.712  7.087   1.00 15.47 ? 410  ARG A NE  1 
ATOM   3234 C  CZ  . ARG A 1 410  ? 17.590 66.891  6.845   1.00 16.84 ? 410  ARG A CZ  1 
ATOM   3235 N  NH1 . ARG A 1 410  ? 16.310 66.953  6.431   1.00 17.62 ? 410  ARG A NH1 1 
ATOM   3236 N  NH2 . ARG A 1 410  ? 18.306 68.002  7.041   1.00 17.16 ? 410  ARG A NH2 1 
ATOM   3237 N  N   . SER A 1 411  ? 15.057 61.857  3.177   1.00 11.16 ? 411  SER A N   1 
ATOM   3238 C  CA  A SER A 1 411  ? 14.094 62.364  2.206   0.50 12.29 ? 411  SER A CA  1 
ATOM   3239 C  CA  B SER A 1 411  ? 14.104 62.619  2.334   0.50 12.28 ? 411  SER A CA  1 
ATOM   3240 C  C   . SER A 1 411  ? 14.629 62.543  0.787   1.00 11.56 ? 411  SER A C   1 
ATOM   3241 O  O   A SER A 1 411  ? 15.093 61.574  0.185   0.50 12.16 ? 411  SER A O   1 
ATOM   3242 O  O   B SER A 1 411  ? 15.107 61.577  0.444   0.50 12.18 ? 411  SER A O   1 
ATOM   3243 C  CB  A SER A 1 411  ? 13.425 63.644  2.763   0.50 13.53 ? 411  SER A CB  1 
ATOM   3244 C  CB  B SER A 1 411  ? 13.814 64.050  2.838   0.50 13.93 ? 411  SER A CB  1 
ATOM   3245 O  OG  A SER A 1 411  ? 14.340 64.697  2.983   0.50 15.51 ? 411  SER A OG  1 
ATOM   3246 O  OG  B SER A 1 411  ? 12.710 64.606  2.160   0.50 15.91 ? 411  SER A OG  1 
ATOM   3247 N  N   . ASP A 1 412  ? 14.562 63.756  0.228   1.00 11.34 ? 412  ASP A N   1 
ATOM   3248 C  CA  . ASP A 1 412  ? 15.065 63.962  -1.138  1.00 10.15 ? 412  ASP A CA  1 
ATOM   3249 C  C   . ASP A 1 412  ? 16.422 64.712  -1.097  1.00 9.63  ? 412  ASP A C   1 
ATOM   3250 O  O   . ASP A 1 412  ? 16.804 65.291  -2.095  1.00 9.52  ? 412  ASP A O   1 
ATOM   3251 C  CB  . ASP A 1 412  ? 14.068 64.813  -1.956  1.00 11.28 ? 412  ASP A CB  1 
ATOM   3252 C  CG  . ASP A 1 412  ? 13.896 66.236  -1.370  1.00 10.46 ? 412  ASP A CG  1 
ATOM   3253 O  OD1 . ASP A 1 412  ? 14.410 66.527  -0.275  1.00 12.04 ? 412  ASP A OD1 1 
ATOM   3254 O  OD2 . ASP A 1 412  ? 13.218 67.053  -2.045  1.00 13.75 ? 412  ASP A OD2 1 
ATOM   3255 N  N   . ASN A 1 413  ? 17.104 64.639  0.042   1.00 9.67  ? 413  ASN A N   1 
ATOM   3256 C  CA  . ASN A 1 413  ? 18.382 65.362  0.192   1.00 9.35  ? 413  ASN A CA  1 
ATOM   3257 C  C   . ASN A 1 413  ? 19.549 64.498  -0.365  1.00 8.51  ? 413  ASN A C   1 
ATOM   3258 O  O   . ASN A 1 413  ? 20.239 63.804  0.397   1.00 9.20  ? 413  ASN A O   1 
ATOM   3259 C  CB  . ASN A 1 413  ? 18.665 65.703  1.658   1.00 10.14 ? 413  ASN A CB  1 
ATOM   3260 C  CG  . ASN A 1 413  ? 17.727 66.799  2.275   1.00 9.37  ? 413  ASN A CG  1 
ATOM   3261 O  OD1 . ASN A 1 413  ? 18.025 67.300  3.360   1.00 11.60 ? 413  ASN A OD1 1 
ATOM   3262 N  ND2 . ASN A 1 413  ? 16.620 67.163  1.599   1.00 10.81 ? 413  ASN A ND2 1 
ATOM   3263 N  N   . TYR A 1 414  ? 19.724 64.574  -1.688  1.00 7.80  ? 414  TYR A N   1 
ATOM   3264 C  CA  . TYR A 1 414  ? 20.782 63.858  -2.401  1.00 8.47  ? 414  TYR A CA  1 
ATOM   3265 C  C   . TYR A 1 414  ? 22.016 64.757  -2.478  1.00 8.48  ? 414  TYR A C   1 
ATOM   3266 O  O   . TYR A 1 414  ? 21.924 65.965  -2.780  1.00 9.03  ? 414  TYR A O   1 
ATOM   3267 C  CB  . TYR A 1 414  ? 20.306 63.492  -3.818  1.00 9.41  ? 414  TYR A CB  1 
ATOM   3268 C  CG  . TYR A 1 414  ? 19.308 62.371  -3.857  1.00 8.37  ? 414  TYR A CG  1 
ATOM   3269 C  CD1 . TYR A 1 414  ? 17.966 62.617  -3.621  1.00 10.18 ? 414  TYR A CD1 1 
ATOM   3270 C  CD2 . TYR A 1 414  ? 19.736 61.064  -4.050  1.00 9.37  ? 414  TYR A CD2 1 
ATOM   3271 C  CE1 . TYR A 1 414  ? 17.051 61.530  -3.578  1.00 10.55 ? 414  TYR A CE1 1 
ATOM   3272 C  CE2 . TYR A 1 414  ? 18.823 59.968  -4.020  1.00 9.20  ? 414  TYR A CE2 1 
ATOM   3273 C  CZ  . TYR A 1 414  ? 17.511 60.246  -3.789  1.00 9.52  ? 414  TYR A CZ  1 
ATOM   3274 O  OH  . TYR A 1 414  ? 16.607 59.177  -3.804  1.00 10.14 ? 414  TYR A OH  1 
ATOM   3275 N  N   . TRP A 1 415  ? 23.162 64.121  -2.173  1.00 8.28  ? 415  TRP A N   1 
ATOM   3276 C  CA  . TRP A 1 415  ? 24.436 64.830  -2.082  1.00 7.93  ? 415  TRP A CA  1 
ATOM   3277 C  C   . TRP A 1 415  ? 25.141 64.895  -3.407  1.00 8.52  ? 415  TRP A C   1 
ATOM   3278 O  O   . TRP A 1 415  ? 26.275 64.409  -3.530  1.00 9.57  ? 415  TRP A O   1 
ATOM   3279 C  CB  . TRP A 1 415  ? 25.312 64.146  -1.040  1.00 7.60  ? 415  TRP A CB  1 
ATOM   3280 C  CG  . TRP A 1 415  ? 24.756 64.229  0.397   1.00 7.61  ? 415  TRP A CG  1 
ATOM   3281 C  CD1 . TRP A 1 415  ? 23.443 63.951  0.813   1.00 8.75  ? 415  TRP A CD1 1 
ATOM   3282 C  CD2 . TRP A 1 415  ? 25.492 64.505  1.588   1.00 7.97  ? 415  TRP A CD2 1 
ATOM   3283 N  NE1 . TRP A 1 415  ? 23.362 64.044  2.181   1.00 9.17  ? 415  TRP A NE1 1 
ATOM   3284 C  CE2 . TRP A 1 415  ? 24.603 64.376  2.691   1.00 8.00  ? 415  TRP A CE2 1 
ATOM   3285 C  CE3 . TRP A 1 415  ? 26.847 64.847  1.838   1.00 8.12  ? 415  TRP A CE3 1 
ATOM   3286 C  CZ2 . TRP A 1 415  ? 25.017 64.569  4.006   1.00 8.74  ? 415  TRP A CZ2 1 
ATOM   3287 C  CZ3 . TRP A 1 415  ? 27.257 65.030  3.082   1.00 8.32  ? 415  TRP A CZ3 1 
ATOM   3288 C  CH2 . TRP A 1 415  ? 26.367 64.894  4.207   1.00 8.36  ? 415  TRP A CH2 1 
ATOM   3289 N  N   . SER A 1 416  ? 24.485 65.466  -4.407  1.00 7.34  ? 416  SER A N   1 
ATOM   3290 C  CA  . SER A 1 416  ? 25.153 65.602  -5.713  1.00 7.88  ? 416  SER A CA  1 
ATOM   3291 C  C   . SER A 1 416  ? 25.707 67.008  -5.940  1.00 7.13  ? 416  SER A C   1 
ATOM   3292 O  O   . SER A 1 416  ? 26.349 67.240  -6.939  1.00 7.99  ? 416  SER A O   1 
ATOM   3293 C  CB  . SER A 1 416  ? 24.206 65.165  -6.831  1.00 7.24  ? 416  SER A CB  1 
ATOM   3294 O  OG  . SER A 1 416  ? 22.879 65.753  -6.677  1.00 8.56  ? 416  SER A OG  1 
ATOM   3295 N  N   . GLY A 1 417  ? 25.480 67.938  -5.013  1.00 6.93  ? 417  GLY A N   1 
ATOM   3296 C  CA  . GLY A 1 417  ? 26.044 69.269  -5.193  1.00 7.67  ? 417  GLY A CA  1 
ATOM   3297 C  C   . GLY A 1 417  ? 27.565 69.269  -5.109  1.00 6.71  ? 417  GLY A C   1 
ATOM   3298 O  O   . GLY A 1 417  ? 28.233 69.977  -5.869  1.00 7.35  ? 417  GLY A O   1 
ATOM   3299 N  N   . TYR A 1 418  ? 28.134 68.454  -4.213  1.00 6.56  ? 418  TYR A N   1 
ATOM   3300 C  CA  . TYR A 1 418  ? 29.608 68.477  -4.032  1.00 6.61  ? 418  TYR A CA  1 
ATOM   3301 C  C   . TYR A 1 418  ? 30.347 67.860  -5.212  1.00 6.19  ? 418  TYR A C   1 
ATOM   3302 O  O   . TYR A 1 418  ? 31.601 67.860  -5.257  1.00 6.86  ? 418  TYR A O   1 
ATOM   3303 C  CB  . TYR A 1 418  ? 30.012 67.818  -2.704  1.00 6.38  ? 418  TYR A CB  1 
ATOM   3304 C  CG  . TYR A 1 418  ? 30.109 66.304  -2.750  1.00 6.79  ? 418  TYR A CG  1 
ATOM   3305 C  CD1 . TYR A 1 418  ? 28.970 65.469  -2.565  1.00 7.72  ? 418  TYR A CD1 1 
ATOM   3306 C  CD2 . TYR A 1 418  ? 31.338 65.704  -2.953  1.00 6.88  ? 418  TYR A CD2 1 
ATOM   3307 C  CE1 . TYR A 1 418  ? 29.073 64.049  -2.581  1.00 6.35  ? 418  TYR A CE1 1 
ATOM   3308 C  CE2 . TYR A 1 418  ? 31.461 64.328  -2.987  1.00 6.38  ? 418  TYR A CE2 1 
ATOM   3309 C  CZ  . TYR A 1 418  ? 30.340 63.505  -2.790  1.00 6.17  ? 418  TYR A CZ  1 
ATOM   3310 O  OH  . TYR A 1 418  ? 30.532 62.134  -2.787  1.00 7.10  ? 418  TYR A OH  1 
ATOM   3311 N  N   . TYR A 1 419  ? 29.623 67.277  -6.169  1.00 6.23  ? 419  TYR A N   1 
ATOM   3312 C  CA  . TYR A 1 419  ? 30.279 66.834  -7.401  1.00 5.90  ? 419  TYR A CA  1 
ATOM   3313 C  C   . TYR A 1 419  ? 30.785 68.055  -8.207  1.00 6.53  ? 419  TYR A C   1 
ATOM   3314 O  O   . TYR A 1 419  ? 31.621 67.851  -9.102  1.00 6.90  ? 419  TYR A O   1 
ATOM   3315 C  CB  . TYR A 1 419  ? 29.341 66.030  -8.292  1.00 6.57  ? 419  TYR A CB  1 
ATOM   3316 C  CG  . TYR A 1 419  ? 28.709 64.826  -7.640  1.00 5.76  ? 419  TYR A CG  1 
ATOM   3317 C  CD1 . TYR A 1 419  ? 29.274 64.158  -6.545  1.00 6.61  ? 419  TYR A CD1 1 
ATOM   3318 C  CD2 . TYR A 1 419  ? 27.530 64.316  -8.211  1.00 7.05  ? 419  TYR A CD2 1 
ATOM   3319 C  CE1 . TYR A 1 419  ? 28.691 63.011  -6.018  1.00 6.61  ? 419  TYR A CE1 1 
ATOM   3320 C  CE2 . TYR A 1 419  ? 26.932 63.167  -7.694  1.00 7.07  ? 419  TYR A CE2 1 
ATOM   3321 C  CZ  . TYR A 1 419  ? 27.518 62.524  -6.601  1.00 6.46  ? 419  TYR A CZ  1 
ATOM   3322 O  OH  . TYR A 1 419  ? 26.929 61.382  -6.084  1.00 7.25  ? 419  TYR A OH  1 
ATOM   3323 N  N   . THR A 1 420  ? 30.310 69.267  -7.863  1.00 6.51  ? 420  THR A N   1 
ATOM   3324 C  CA  . THR A 1 420  ? 30.697 70.474  -8.586  1.00 7.13  ? 420  THR A CA  1 
ATOM   3325 C  C   . THR A 1 420  ? 31.234 71.582  -7.711  1.00 6.80  ? 420  THR A C   1 
ATOM   3326 O  O   . THR A 1 420  ? 32.008 72.429  -8.177  1.00 7.50  ? 420  THR A O   1 
ATOM   3327 C  CB  . THR A 1 420  ? 29.446 70.982  -9.369  1.00 7.22  ? 420  THR A CB  1 
ATOM   3328 O  OG1 . THR A 1 420  ? 28.998 69.950  -10.250 1.00 8.12  ? 420  THR A OG1 1 
ATOM   3329 C  CG2 . THR A 1 420  ? 29.717 72.234  -10.225 1.00 8.10  ? 420  THR A CG2 1 
ATOM   3330 N  N   . SER A 1 421  ? 30.890 71.606  -6.433  1.00 6.58  ? 421  SER A N   1 
ATOM   3331 C  CA  . SER A 1 421  ? 31.277 72.736  -5.565  1.00 7.36  ? 421  SER A CA  1 
ATOM   3332 C  C   . SER A 1 421  ? 32.743 73.069  -5.627  1.00 7.10  ? 421  SER A C   1 
ATOM   3333 O  O   . SER A 1 421  ? 33.601 72.171  -5.569  1.00 6.93  ? 421  SER A O   1 
ATOM   3334 C  CB  . SER A 1 421  ? 30.913 72.429  -4.098  1.00 7.00  ? 421  SER A CB  1 
ATOM   3335 O  OG  . SER A 1 421  ? 29.509 72.223  -4.033  1.00 7.73  ? 421  SER A OG  1 
ATOM   3336 N  N   . ARG A 1 422  ? 33.032 74.379  -5.663  1.00 6.25  ? 422  ARG A N   1 
ATOM   3337 C  CA  . ARG A 1 422  ? 34.443 74.864  -5.739  1.00 7.33  ? 422  ARG A CA  1 
ATOM   3338 C  C   . ARG A 1 422  ? 35.176 74.198  -6.910  1.00 6.85  ? 422  ARG A C   1 
ATOM   3339 O  O   . ARG A 1 422  ? 36.217 73.514  -6.774  1.00 7.33  ? 422  ARG A O   1 
ATOM   3340 C  CB  . ARG A 1 422  ? 35.201 74.639  -4.428  1.00 8.15  ? 422  ARG A CB  1 
ATOM   3341 C  CG  . ARG A 1 422  ? 34.943 75.724  -3.353  1.00 8.43  ? 422  ARG A CG  1 
ATOM   3342 C  CD  . ARG A 1 422  ? 33.494 75.832  -2.864  1.00 8.33  ? 422  ARG A CD  1 
ATOM   3343 N  NE  . ARG A 1 422  ? 33.452 76.831  -1.772  1.00 8.58  ? 422  ARG A NE  1 
ATOM   3344 C  CZ  . ARG A 1 422  ? 33.492 76.530  -0.482  1.00 8.72  ? 422  ARG A CZ  1 
ATOM   3345 N  NH1 . ARG A 1 422  ? 33.505 75.279  -0.059  1.00 8.48  ? 422  ARG A NH1 1 
ATOM   3346 N  NH2 . ARG A 1 422  ? 33.746 77.514  0.414   1.00 9.17  ? 422  ARG A NH2 1 
ATOM   3347 N  N   . PRO A 1 423  ? 34.682 74.420  -8.109  1.00 6.73  ? 423  PRO A N   1 
ATOM   3348 C  CA  . PRO A 1 423  ? 35.292 73.809  -9.285  1.00 6.71  ? 423  PRO A CA  1 
ATOM   3349 C  C   . PRO A 1 423  ? 36.678 74.285  -9.619  1.00 5.87  ? 423  PRO A C   1 
ATOM   3350 O  O   . PRO A 1 423  ? 37.402 73.555  -10.312 1.00 7.23  ? 423  PRO A O   1 
ATOM   3351 C  CB  . PRO A 1 423  ? 34.249 74.071  -10.409 1.00 6.58  ? 423  PRO A CB  1 
ATOM   3352 C  CG  . PRO A 1 423  ? 33.675 75.434  -9.990  1.00 7.06  ? 423  PRO A CG  1 
ATOM   3353 C  CD  . PRO A 1 423  ? 33.551 75.304  -8.468  1.00 7.12  ? 423  PRO A CD  1 
ATOM   3354 N  N   . TYR A 1 424  ? 37.072 75.474  -9.173  1.00 7.08  ? 424  TYR A N   1 
ATOM   3355 C  CA  . TYR A 1 424  ? 38.448 75.907  -9.446  1.00 7.16  ? 424  TYR A CA  1 
ATOM   3356 C  C   . TYR A 1 424  ? 39.422 74.895  -8.860  1.00 6.99  ? 424  TYR A C   1 
ATOM   3357 O  O   . TYR A 1 424  ? 40.412 74.485  -9.522  1.00 6.75  ? 424  TYR A O   1 
ATOM   3358 C  CB  . TYR A 1 424  ? 38.669 77.299  -8.797  1.00 7.85  ? 424  TYR A CB  1 
ATOM   3359 C  CG  . TYR A 1 424  ? 40.049 77.841  -9.050  1.00 7.54  ? 424  TYR A CG  1 
ATOM   3360 C  CD1 . TYR A 1 424  ? 41.121 77.554  -8.185  1.00 8.16  ? 424  TYR A CD1 1 
ATOM   3361 C  CD2 . TYR A 1 424  ? 40.278 78.633  -10.162 1.00 9.83  ? 424  TYR A CD2 1 
ATOM   3362 C  CE1 . TYR A 1 424  ? 42.405 78.069  -8.474  1.00 10.18 ? 424  TYR A CE1 1 
ATOM   3363 C  CE2 . TYR A 1 424  ? 41.505 79.145  -10.427 1.00 11.11 ? 424  TYR A CE2 1 
ATOM   3364 C  CZ  . TYR A 1 424  ? 42.563 78.869  -9.591  1.00 10.28 ? 424  TYR A CZ  1 
ATOM   3365 O  OH  . TYR A 1 424  ? 43.784 79.473  -9.934  1.00 14.31 ? 424  TYR A OH  1 
ATOM   3366 N  N   . HIS A 1 425  ? 39.134 74.478  -7.619  1.00 6.74  ? 425  HIS A N   1 
ATOM   3367 C  CA  . HIS A 1 425  ? 40.080 73.569  -6.945  1.00 5.92  ? 425  HIS A CA  1 
ATOM   3368 C  C   . HIS A 1 425  ? 39.964 72.153  -7.432  1.00 6.65  ? 425  HIS A C   1 
ATOM   3369 O  O   . HIS A 1 425  ? 40.936 71.365  -7.379  1.00 6.34  ? 425  HIS A O   1 
ATOM   3370 C  CB  . HIS A 1 425  ? 39.919 73.708  -5.415  1.00 7.46  ? 425  HIS A CB  1 
ATOM   3371 C  CG  . HIS A 1 425  ? 39.875 75.134  -4.995  1.00 8.07  ? 425  HIS A CG  1 
ATOM   3372 N  ND1 . HIS A 1 425  ? 40.997 75.901  -4.716  1.00 10.89 ? 425  HIS A ND1 1 
ATOM   3373 C  CD2 . HIS A 1 425  ? 38.820 75.970  -4.996  1.00 6.94  ? 425  HIS A CD2 1 
ATOM   3374 C  CE1 . HIS A 1 425  ? 40.606 77.165  -4.556  1.00 6.86  ? 425  HIS A CE1 1 
ATOM   3375 N  NE2 . HIS A 1 425  ? 39.297 77.223  -4.723  1.00 11.67 ? 425  HIS A NE2 1 
ATOM   3376 N  N   . LYS A 1 426  ? 38.768 71.759  -7.904  1.00 6.27  ? 426  LYS A N   1 
ATOM   3377 C  CA  . LYS A 1 426  ? 38.617 70.447  -8.557  1.00 6.45  ? 426  LYS A CA  1 
ATOM   3378 C  C   . LYS A 1 426  ? 39.495 70.395  -9.819  1.00 6.10  ? 426  LYS A C   1 
ATOM   3379 O  O   . LYS A 1 426  ? 40.156 69.371  -10.088 1.00 6.49  ? 426  LYS A O   1 
ATOM   3380 C  CB  . LYS A 1 426  ? 37.113 70.226  -8.949  1.00 6.94  ? 426  LYS A CB  1 
ATOM   3381 C  CG  . LYS A 1 426  ? 36.248 69.880  -7.737  1.00 6.46  ? 426  LYS A CG  1 
ATOM   3382 C  CD  . LYS A 1 426  ? 34.749 69.937  -8.119  1.00 6.84  ? 426  LYS A CD  1 
ATOM   3383 C  CE  . LYS A 1 426  ? 33.890 69.054  -7.208  1.00 6.77  ? 426  LYS A CE  1 
ATOM   3384 N  NZ  . LYS A 1 426  ? 33.853 69.430  -5.770  1.00 7.03  ? 426  LYS A NZ  1 
ATOM   3385 N  N   . ARG A 1 427  ? 39.564 71.496  -10.589 1.00 5.81  ? 427  ARG A N   1 
ATOM   3386 C  CA  . ARG A 1 427  ? 40.409 71.478  -11.751 1.00 6.62  ? 427  ARG A CA  1 
ATOM   3387 C  C   . ARG A 1 427  ? 41.879 71.504  -11.293 1.00 6.61  ? 427  ARG A C   1 
ATOM   3388 O  O   . ARG A 1 427  ? 42.725 70.810  -11.874 1.00 6.45  ? 427  ARG A O   1 
ATOM   3389 C  CB  . ARG A 1 427  ? 40.075 72.713  -12.608 1.00 7.50  ? 427  ARG A CB  1 
ATOM   3390 C  CG  . ARG A 1 427  ? 41.009 72.963  -13.783 1.00 8.79  ? 427  ARG A CG  1 
ATOM   3391 C  CD  . ARG A 1 427  ? 41.075 71.850  -14.806 1.00 9.69  ? 427  ARG A CD  1 
ATOM   3392 N  NE  . ARG A 1 427  ? 42.131 72.244  -15.754 1.00 10.39 ? 427  ARG A NE  1 
ATOM   3393 C  CZ  . ARG A 1 427  ? 42.943 71.416  -16.347 1.00 10.19 ? 427  ARG A CZ  1 
ATOM   3394 N  NH1 . ARG A 1 427  ? 42.885 70.115  -16.162 1.00 10.25 ? 427  ARG A NH1 1 
ATOM   3395 N  NH2 . ARG A 1 427  ? 43.926 71.943  -17.127 1.00 10.94 ? 427  ARG A NH2 1 
ATOM   3396 N  N   . MET A 1 428  ? 42.197 72.312  -10.261 1.00 6.58  ? 428  MET A N   1 
ATOM   3397 C  CA  . MET A 1 428  ? 43.581 72.359  -9.764  1.00 6.64  ? 428  MET A CA  1 
ATOM   3398 C  C   . MET A 1 428  ? 44.066 70.965  -9.350  1.00 6.64  ? 428  MET A C   1 
ATOM   3399 O  O   . MET A 1 428  ? 45.263 70.624  -9.554  1.00 6.73  ? 428  MET A O   1 
ATOM   3400 C  CB  . MET A 1 428  ? 43.651 73.309  -8.571  1.00 7.69  ? 428  MET A CB  1 
ATOM   3401 C  CG  . MET A 1 428  ? 45.113 73.715  -8.248  1.00 7.28  ? 428  MET A CG  1 
ATOM   3402 S  SD  . MET A 1 428  ? 44.999 75.010  -6.970  1.00 9.70  ? 428  MET A SD  1 
ATOM   3403 C  CE  . MET A 1 428  ? 46.726 75.545  -6.936  1.00 9.77  ? 428  MET A CE  1 
ATOM   3404 N  N   . ASP A 1 429  ? 43.190 70.151  -8.751  1.00 5.99  ? 429  ASP A N   1 
ATOM   3405 C  CA  . ASP A 1 429  ? 43.555 68.808  -8.354  1.00 5.86  ? 429  ASP A CA  1 
ATOM   3406 C  C   . ASP A 1 429  ? 44.108 67.997  -9.514  1.00 5.91  ? 429  ASP A C   1 
ATOM   3407 O  O   . ASP A 1 429  ? 45.093 67.274  -9.371  1.00 6.25  ? 429  ASP A O   1 
ATOM   3408 C  CB  . ASP A 1 429  ? 42.286 68.098  -7.835  1.00 7.11  ? 429  ASP A CB  1 
ATOM   3409 C  CG  . ASP A 1 429  ? 42.562 66.624  -7.518  1.00 6.14  ? 429  ASP A CG  1 
ATOM   3410 O  OD1 . ASP A 1 429  ? 43.076 66.379  -6.411  1.00 7.73  ? 429  ASP A OD1 1 
ATOM   3411 O  OD2 . ASP A 1 429  ? 42.252 65.729  -8.377  1.00 6.68  ? 429  ASP A OD2 1 
ATOM   3412 N  N   . ARG A 1 430  ? 43.463 68.113  -10.689 1.00 6.20  ? 430  ARG A N   1 
ATOM   3413 C  CA  . ARG A 1 430  ? 43.913 67.337  -11.824 1.00 5.45  ? 430  ARG A CA  1 
ATOM   3414 C  C   . ARG A 1 430  ? 45.215 67.856  -12.398 1.00 5.88  ? 430  ARG A C   1 
ATOM   3415 O  O   . ARG A 1 430  ? 46.068 67.052  -12.865 1.00 6.43  ? 430  ARG A O   1 
ATOM   3416 C  CB  . ARG A 1 430  ? 42.823 67.390  -12.906 1.00 6.47  ? 430  ARG A CB  1 
ATOM   3417 C  CG  . ARG A 1 430  ? 41.533 66.615  -12.506 1.00 6.88  ? 430  ARG A CG  1 
ATOM   3418 C  CD  . ARG A 1 430  ? 41.808 65.167  -12.077 1.00 6.45  ? 430  ARG A CD  1 
ATOM   3419 N  NE  . ARG A 1 430  ? 40.559 64.407  -12.094 1.00 6.12  ? 430  ARG A NE  1 
ATOM   3420 C  CZ  . ARG A 1 430  ? 39.880 64.070  -11.015 1.00 6.29  ? 430  ARG A CZ  1 
ATOM   3421 N  NH1 . ARG A 1 430  ? 40.278 64.402  -9.777  1.00 6.74  ? 430  ARG A NH1 1 
ATOM   3422 N  NH2 . ARG A 1 430  ? 38.744 63.355  -11.150 1.00 6.86  ? 430  ARG A NH2 1 
ATOM   3423 N  N   . VAL A 1 431  ? 45.410 69.174  -12.334 1.00 5.75  ? 431  VAL A N   1 
ATOM   3424 C  CA  . VAL A 1 431  ? 46.666 69.734  -12.818 1.00 6.86  ? 431  VAL A CA  1 
ATOM   3425 C  C   . VAL A 1 431  ? 47.804 69.250  -11.901 1.00 6.61  ? 431  VAL A C   1 
ATOM   3426 O  O   . VAL A 1 431  ? 48.851 68.766  -12.368 1.00 7.16  ? 431  VAL A O   1 
ATOM   3427 C  CB  . VAL A 1 431  ? 46.545 71.247  -12.794 1.00 6.32  ? 431  VAL A CB  1 
ATOM   3428 C  CG1 . VAL A 1 431  ? 47.932 71.865  -13.149 1.00 8.43  ? 431  VAL A CG1 1 
ATOM   3429 C  CG2 . VAL A 1 431  ? 45.510 71.702  -13.841 1.00 8.18  ? 431  VAL A CG2 1 
ATOM   3430 N  N   . LEU A 1 432  ? 47.621 69.366  -10.585 1.00 5.99  ? 432  LEU A N   1 
ATOM   3431 C  CA  . LEU A 1 432  ? 48.660 68.918  -9.651  1.00 6.36  ? 432  LEU A CA  1 
ATOM   3432 C  C   . LEU A 1 432  ? 48.852 67.414  -9.754  1.00 5.92  ? 432  LEU A C   1 
ATOM   3433 O  O   . LEU A 1 432  ? 49.984 66.940  -9.606  1.00 6.83  ? 432  LEU A O   1 
ATOM   3434 C  CB  . LEU A 1 432  ? 48.335 69.380  -8.230  1.00 7.26  ? 432  LEU A CB  1 
ATOM   3435 C  CG  . LEU A 1 432  ? 49.352 69.016  -7.158  1.00 7.24  ? 432  LEU A CG  1 
ATOM   3436 C  CD1 . LEU A 1 432  ? 50.807 69.524  -7.495  1.00 7.37  ? 432  LEU A CD1 1 
ATOM   3437 C  CD2 . LEU A 1 432  ? 48.868 69.637  -5.840  1.00 8.13  ? 432  LEU A CD2 1 
ATOM   3438 N  N   . MET A 1 433  ? 47.780 66.628  -9.993  1.00 5.66  ? 433  MET A N   1 
ATOM   3439 C  CA  . MET A 1 433  ? 47.936 65.179  -10.175 1.00 6.43  ? 433  MET A CA  1 
ATOM   3440 C  C   . MET A 1 433  ? 49.000 64.884  -11.209 1.00 5.70  ? 433  MET A C   1 
ATOM   3441 O  O   . MET A 1 433  ? 49.890 64.031  -11.002 1.00 6.03  ? 433  MET A O   1 
ATOM   3442 C  CB  . MET A 1 433  ? 46.602 64.592  -10.640 1.00 6.77  ? 433  MET A CB  1 
ATOM   3443 C  CG  . MET A 1 433  ? 46.714 63.114  -10.934 1.00 6.85  ? 433  MET A CG  1 
ATOM   3444 S  SD  . MET A 1 433  ? 45.152 62.435  -11.589 1.00 8.02  ? 433  MET A SD  1 
ATOM   3445 C  CE  . MET A 1 433  ? 45.142 63.114  -13.209 1.00 9.56  ? 433  MET A CE  1 
ATOM   3446 N  N   . HIS A 1 434  ? 48.892 65.571  -12.326 1.00 5.91  ? 434  HIS A N   1 
ATOM   3447 C  CA  . HIS A 1 434  ? 49.819 65.372  -13.430 1.00 5.67  ? 434  HIS A CA  1 
ATOM   3448 C  C   . HIS A 1 434  ? 51.229 65.884  -13.134 1.00 5.69  ? 434  HIS A C   1 
ATOM   3449 O  O   . HIS A 1 434  ? 52.225 65.224  -13.497 1.00 6.22  ? 434  HIS A O   1 
ATOM   3450 C  CB  . HIS A 1 434  ? 49.268 66.050  -14.694 1.00 6.73  ? 434  HIS A CB  1 
ATOM   3451 C  CG  . HIS A 1 434  ? 50.255 65.999  -15.826 1.00 6.12  ? 434  HIS A CG  1 
ATOM   3452 N  ND1 . HIS A 1 434  ? 51.056 67.073  -16.196 1.00 9.16  ? 434  HIS A ND1 1 
ATOM   3453 C  CD2 . HIS A 1 434  ? 50.688 64.925  -16.532 1.00 5.12  ? 434  HIS A CD2 1 
ATOM   3454 C  CE1 . HIS A 1 434  ? 51.942 66.640  -17.109 1.00 5.46  ? 434  HIS A CE1 1 
ATOM   3455 N  NE2 . HIS A 1 434  ? 51.738 65.354  -17.308 1.00 9.51  ? 434  HIS A NE2 1 
ATOM   3456 N  N   . TYR A 1 435  ? 51.325 67.042  -12.496 1.00 6.35  ? 435  TYR A N   1 
ATOM   3457 C  CA  . TYR A 1 435  ? 52.631 67.605  -12.160 1.00 7.02  ? 435  TYR A CA  1 
ATOM   3458 C  C   . TYR A 1 435  ? 53.367 66.691  -11.184 1.00 6.92  ? 435  TYR A C   1 
ATOM   3459 O  O   . TYR A 1 435  ? 54.580 66.502  -11.314 1.00 6.84  ? 435  TYR A O   1 
ATOM   3460 C  CB  A TYR A 1 435  ? 52.470 69.021  -11.531 0.50 7.92  ? 435  TYR A CB  1 
ATOM   3461 C  CB  B TYR A 1 435  ? 52.534 69.084  -11.820 0.50 7.71  ? 435  TYR A CB  1 
ATOM   3462 C  CG  A TYR A 1 435  ? 52.399 70.166  -12.526 0.50 9.65  ? 435  TYR A CG  1 
ATOM   3463 C  CG  B TYR A 1 435  ? 52.433 69.948  -13.065 0.50 8.36  ? 435  TYR A CG  1 
ATOM   3464 C  CD1 A TYR A 1 435  ? 51.445 70.191  -13.545 0.50 9.25  ? 435  TYR A CD1 1 
ATOM   3465 C  CD1 B TYR A 1 435  ? 53.498 70.036  -13.953 0.50 12.26 ? 435  TYR A CD1 1 
ATOM   3466 C  CD2 A TYR A 1 435  ? 53.240 71.263  -12.400 0.50 11.16 ? 435  TYR A CD2 1 
ATOM   3467 C  CD2 B TYR A 1 435  ? 51.294 70.684  -13.350 0.50 8.89  ? 435  TYR A CD2 1 
ATOM   3468 C  CE1 A TYR A 1 435  ? 51.321 71.284  -14.415 0.50 10.71 ? 435  TYR A CE1 1 
ATOM   3469 C  CE1 B TYR A 1 435  ? 53.432 70.854  -15.078 0.50 13.90 ? 435  TYR A CE1 1 
ATOM   3470 C  CE2 A TYR A 1 435  ? 53.134 72.354  -13.259 0.50 14.02 ? 435  TYR A CE2 1 
ATOM   3471 C  CE2 B TYR A 1 435  ? 51.207 71.490  -14.482 0.50 9.60  ? 435  TYR A CE2 1 
ATOM   3472 C  CZ  A TYR A 1 435  ? 52.176 72.361  -14.259 0.50 11.94 ? 435  TYR A CZ  1 
ATOM   3473 C  CZ  B TYR A 1 435  ? 52.283 71.578  -15.338 0.50 10.93 ? 435  TYR A CZ  1 
ATOM   3474 O  OH  A TYR A 1 435  ? 52.076 73.441  -15.102 0.50 15.47 ? 435  TYR A OH  1 
ATOM   3475 O  OH  B TYR A 1 435  ? 52.229 72.401  -16.469 0.50 12.89 ? 435  TYR A OH  1 
ATOM   3476 N  N   . VAL A 1 436  ? 52.658 66.105  -10.232 1.00 6.46  ? 436  VAL A N   1 
ATOM   3477 C  CA  . VAL A 1 436  ? 53.328 65.215  -9.293  1.00 6.48  ? 436  VAL A CA  1 
ATOM   3478 C  C   . VAL A 1 436  ? 53.850 64.004  -10.087 1.00 7.09  ? 436  VAL A C   1 
ATOM   3479 O  O   . VAL A 1 436  ? 55.005 63.564  -9.907  1.00 6.69  ? 436  VAL A O   1 
ATOM   3480 C  CB  . VAL A 1 436  ? 52.350 64.760  -8.194  1.00 6.40  ? 436  VAL A CB  1 
ATOM   3481 C  CG1 . VAL A 1 436  ? 52.894 63.525  -7.377  1.00 7.96  ? 436  VAL A CG1 1 
ATOM   3482 C  CG2 . VAL A 1 436  ? 52.194 65.961  -7.169  1.00 6.75  ? 436  VAL A CG2 1 
ATOM   3483 N  N   . ARG A 1 437  ? 53.025 63.399  -10.948 1.00 6.27  ? 437  ARG A N   1 
ATOM   3484 C  CA  . ARG A 1 437  ? 53.498 62.241  -11.735 1.00 6.88  ? 437  ARG A CA  1 
ATOM   3485 C  C   . ARG A 1 437  ? 54.730 62.640  -12.545 1.00 6.79  ? 437  ARG A C   1 
ATOM   3486 O  O   . ARG A 1 437  ? 55.731 61.893  -12.565 1.00 6.72  ? 437  ARG A O   1 
ATOM   3487 C  CB  . ARG A 1 437  ? 52.394 61.751  -12.679 1.00 6.60  ? 437  ARG A CB  1 
ATOM   3488 C  CG  . ARG A 1 437  ? 52.920 60.771  -13.715 1.00 7.54  ? 437  ARG A CG  1 
ATOM   3489 C  CD  . ARG A 1 437  ? 51.764 60.275  -14.573 1.00 8.27  ? 437  ARG A CD  1 
ATOM   3490 N  NE  . ARG A 1 437  ? 52.295 59.592  -15.755 1.00 7.79  ? 437  ARG A NE  1 
ATOM   3491 C  CZ  . ARG A 1 437  ? 51.565 58.757  -16.494 1.00 7.22  ? 437  ARG A CZ  1 
ATOM   3492 N  NH1 . ARG A 1 437  ? 50.284 58.457  -16.175 1.00 8.07  ? 437  ARG A NH1 1 
ATOM   3493 N  NH2 . ARG A 1 437  ? 52.094 58.228  -17.577 1.00 8.21  ? 437  ARG A NH2 1 
ATOM   3494 N  N   . ALA A 1 438  ? 54.634 63.782  -13.246 1.00 6.24  ? 438  ALA A N   1 
ATOM   3495 C  CA  . ALA A 1 438  ? 55.772 64.172  -14.097 1.00 6.87  ? 438  ALA A CA  1 
ATOM   3496 C  C   . ALA A 1 438  ? 57.037 64.483  -13.305 1.00 6.91  ? 438  ALA A C   1 
ATOM   3497 O  O   . ALA A 1 438  ? 58.130 64.118  -13.780 1.00 7.06  ? 438  ALA A O   1 
ATOM   3498 C  CB  . ALA A 1 438  ? 55.382 65.341  -14.992 1.00 7.71  ? 438  ALA A CB  1 
ATOM   3499 N  N   . ALA A 1 439  ? 56.909 65.122  -12.139 1.00 7.50  ? 439  ALA A N   1 
ATOM   3500 C  CA  . ALA A 1 439  ? 58.103 65.409  -11.325 1.00 7.03  ? 439  ALA A CA  1 
ATOM   3501 C  C   . ALA A 1 439  ? 58.704 64.130  -10.786 1.00 7.29  ? 439  ALA A C   1 
ATOM   3502 O  O   . ALA A 1 439  ? 59.954 63.981  -10.787 1.00 7.65  ? 439  ALA A O   1 
ATOM   3503 C  CB  . ALA A 1 439  ? 57.704 66.369  -10.202 1.00 7.29  ? 439  ALA A CB  1 
ATOM   3504 N  N   . GLU A 1 440  ? 57.876 63.202  -10.321 1.00 6.53  ? 440  GLU A N   1 
ATOM   3505 C  CA  . GLU A 1 440  ? 58.438 61.957  -9.793  1.00 6.94  ? 440  GLU A CA  1 
ATOM   3506 C  C   . GLU A 1 440  ? 59.069 61.150  -10.909 1.00 6.83  ? 440  GLU A C   1 
ATOM   3507 O  O   . GLU A 1 440  ? 60.147 60.585  -10.703 1.00 7.72  ? 440  GLU A O   1 
ATOM   3508 C  CB  . GLU A 1 440  ? 57.387 61.101  -9.078  1.00 7.31  ? 440  GLU A CB  1 
ATOM   3509 C  CG  . GLU A 1 440  ? 56.789 61.777  -7.818  1.00 8.26  ? 440  GLU A CG  1 
ATOM   3510 C  CD  . GLU A 1 440  ? 56.137 60.789  -6.904  1.00 10.03 ? 440  GLU A CD  1 
ATOM   3511 O  OE1 . GLU A 1 440  ? 55.033 60.287  -7.186  1.00 9.70  ? 440  GLU A OE1 1 
ATOM   3512 O  OE2 . GLU A 1 440  ? 56.766 60.431  -5.888  1.00 10.39 ? 440  GLU A OE2 1 
ATOM   3513 N  N   . MET A 1 441  ? 58.468 61.127  -12.093 1.00 6.40  ? 441  MET A N   1 
ATOM   3514 C  CA  . MET A 1 441  ? 59.046 60.358  -13.196 1.00 6.51  ? 441  MET A CA  1 
ATOM   3515 C  C   . MET A 1 441  ? 60.342 61.020  -13.734 1.00 7.38  ? 441  MET A C   1 
ATOM   3516 O  O   . MET A 1 441  ? 61.363 60.325  -13.845 1.00 7.66  ? 441  MET A O   1 
ATOM   3517 C  CB  . MET A 1 441  ? 58.008 60.265  -14.321 1.00 6.78  ? 441  MET A CB  1 
ATOM   3518 C  CG  . MET A 1 441  ? 58.530 59.489  -15.525 1.00 6.58  ? 441  MET A CG  1 
ATOM   3519 S  SD  . MET A 1 441  ? 57.247 59.257  -16.813 1.00 8.12  ? 441  MET A SD  1 
ATOM   3520 C  CE  . MET A 1 441  ? 56.149 58.086  -15.991 1.00 9.66  ? 441  MET A CE  1 
ATOM   3521 N  N   . LEU A 1 442  ? 60.316 62.304  -14.020 1.00 7.23  ? 442  LEU A N   1 
ATOM   3522 C  CA  . LEU A 1 442  ? 61.527 62.963  -14.557 1.00 7.64  ? 442  LEU A CA  1 
ATOM   3523 C  C   . LEU A 1 442  ? 62.718 62.860  -13.633 1.00 8.05  ? 442  LEU A C   1 
ATOM   3524 O  O   . LEU A 1 442  ? 63.852 62.675  -14.112 1.00 8.40  ? 442  LEU A O   1 
ATOM   3525 C  CB  . LEU A 1 442  ? 61.264 64.458  -14.850 1.00 7.28  ? 442  LEU A CB  1 
ATOM   3526 C  CG  . LEU A 1 442  ? 60.600 64.668  -16.208 1.00 6.85  ? 442  LEU A CG  1 
ATOM   3527 C  CD1 . LEU A 1 442  ? 60.001 66.043  -16.281 1.00 8.69  ? 442  LEU A CD1 1 
ATOM   3528 C  CD2 . LEU A 1 442  ? 61.677 64.512  -17.292 1.00 8.89  ? 442  LEU A CD2 1 
ATOM   3529 N  N   . SER A 1 443  ? 62.495 62.932  -12.315 1.00 7.28  ? 443  SER A N   1 
ATOM   3530 C  CA  . SER A 1 443  ? 63.604 62.867  -11.395 1.00 7.56  ? 443  SER A CA  1 
ATOM   3531 C  C   . SER A 1 443  ? 64.004 61.458  -11.034 1.00 8.37  ? 443  SER A C   1 
ATOM   3532 O  O   . SER A 1 443  ? 65.112 61.261  -10.497 1.00 9.30  ? 443  SER A O   1 
ATOM   3533 C  CB  . SER A 1 443  ? 63.330 63.655  -10.144 1.00 7.53  ? 443  SER A CB  1 
ATOM   3534 O  OG  . SER A 1 443  ? 62.207 63.160  -9.384  1.00 7.89  ? 443  SER A OG  1 
ATOM   3535 N  N   . ALA A 1 444  ? 63.188 60.475  -11.344 1.00 7.72  ? 444  ALA A N   1 
ATOM   3536 C  CA  . ALA A 1 444  ? 63.503 59.087  -11.019 1.00 8.51  ? 444  ALA A CA  1 
ATOM   3537 C  C   . ALA A 1 444  ? 64.656 58.537  -11.833 1.00 9.33  ? 444  ALA A C   1 
ATOM   3538 O  O   . ALA A 1 444  ? 65.263 57.559  -11.412 1.00 10.01 ? 444  ALA A O   1 
ATOM   3539 C  CB  . ALA A 1 444  ? 62.280 58.175  -11.228 1.00 9.10  ? 444  ALA A CB  1 
ATOM   3540 N  N   . TRP A 1 445  ? 64.915 59.107  -12.990 1.00 9.99  ? 445  TRP A N   1 
ATOM   3541 C  CA  . TRP A 1 445  ? 65.970 58.551  -13.863 1.00 9.83  ? 445  TRP A CA  1 
ATOM   3542 C  C   . TRP A 1 445  ? 67.358 58.626  -13.234 1.00 10.73 ? 445  TRP A C   1 
ATOM   3543 O  O   . TRP A 1 445  ? 68.226 57.851  -13.659 1.00 12.36 ? 445  TRP A O   1 
ATOM   3544 C  CB  . TRP A 1 445  ? 66.018 59.280  -15.220 1.00 9.68  ? 445  TRP A CB  1 
ATOM   3545 C  CG  . TRP A 1 445  ? 64.711 59.136  -16.001 1.00 8.21  ? 445  TRP A CG  1 
ATOM   3546 C  CD1 . TRP A 1 445  ? 63.723 60.085  -16.145 1.00 8.66  ? 445  TRP A CD1 1 
ATOM   3547 C  CD2 . TRP A 1 445  ? 64.246 57.958  -16.667 1.00 7.86  ? 445  TRP A CD2 1 
ATOM   3548 N  NE1 . TRP A 1 445  ? 62.684 59.561  -16.839 1.00 8.71  ? 445  TRP A NE1 1 
ATOM   3549 C  CE2 . TRP A 1 445  ? 62.964 58.253  -17.172 1.00 8.06  ? 445  TRP A CE2 1 
ATOM   3550 C  CE3 . TRP A 1 445  ? 64.797 56.671  -16.878 1.00 9.30  ? 445  TRP A CE3 1 
ATOM   3551 C  CZ2 . TRP A 1 445  ? 62.203 57.331  -17.865 1.00 8.79  ? 445  TRP A CZ2 1 
ATOM   3552 C  CZ3 . TRP A 1 445  ? 64.052 55.734  -17.567 1.00 9.98  ? 445  TRP A CZ3 1 
ATOM   3553 C  CH2 . TRP A 1 445  ? 62.741 56.066  -18.062 1.00 9.72  ? 445  TRP A CH2 1 
ATOM   3554 N  N   . HIS A 1 446  ? 67.556 59.547  -12.304 1.00 10.24 ? 446  HIS A N   1 
ATOM   3555 C  CA  . HIS A 1 446  ? 68.855 59.646  -11.663 1.00 11.72 ? 446  HIS A CA  1 
ATOM   3556 C  C   . HIS A 1 446  ? 68.736 59.619  -10.162 1.00 11.55 ? 446  HIS A C   1 
ATOM   3557 O  O   . HIS A 1 446  ? 67.657 59.831  -9.584  1.00 10.85 ? 446  HIS A O   1 
ATOM   3558 C  CB  . HIS A 1 446  ? 69.511 61.001  -11.935 1.00 12.87 ? 446  HIS A CB  1 
ATOM   3559 C  CG  . HIS A 1 446  ? 69.887 61.255  -13.356 1.00 14.66 ? 446  HIS A CG  1 
ATOM   3560 N  ND1 . HIS A 1 446  ? 69.098 61.995  -14.207 1.00 16.20 ? 446  HIS A ND1 1 
ATOM   3561 C  CD2 . HIS A 1 446  ? 71.016 60.956  -14.057 1.00 17.69 ? 446  HIS A CD2 1 
ATOM   3562 C  CE1 . HIS A 1 446  ? 69.703 62.141  -15.369 1.00 19.27 ? 446  HIS A CE1 1 
ATOM   3563 N  NE2 . HIS A 1 446  ? 70.866 61.520  -15.310 1.00 17.94 ? 446  HIS A NE2 1 
ATOM   3564 N  N   . SER A 1 447  ? 69.887 59.395  -9.529  1.00 12.10 ? 447  SER A N   1 
ATOM   3565 C  CA  . SER A 1 447  ? 70.036 59.471  -8.090  1.00 11.72 ? 447  SER A CA  1 
ATOM   3566 C  C   . SER A 1 447  ? 70.490 60.939  -7.869  1.00 12.24 ? 447  SER A C   1 
ATOM   3567 O  O   . SER A 1 447  ? 71.304 61.474  -8.653  1.00 13.73 ? 447  SER A O   1 
ATOM   3568 C  CB  A SER A 1 447  ? 71.123 58.491  -7.656  0.50 13.82 ? 447  SER A CB  1 
ATOM   3569 C  CB  B SER A 1 447  ? 70.966 58.491  -7.462  0.50 13.94 ? 447  SER A CB  1 
ATOM   3570 O  OG  A SER A 1 447  ? 71.128 58.353  -6.255  0.50 14.25 ? 447  SER A OG  1 
ATOM   3571 O  OG  B SER A 1 447  ? 70.338 57.265  -7.162  0.50 15.03 ? 447  SER A OG  1 
ATOM   3572 N  N   . TRP A 1 448  ? 69.957 61.616  -6.858  1.00 11.07 ? 448  TRP A N   1 
ATOM   3573 C  CA  . TRP A 1 448  ? 70.293 63.006  -6.621  1.00 12.49 ? 448  TRP A CA  1 
ATOM   3574 C  C   . TRP A 1 448  ? 70.946 63.212  -5.285  1.00 13.84 ? 448  TRP A C   1 
ATOM   3575 O  O   . TRP A 1 448  ? 70.613 62.576  -4.302  1.00 14.74 ? 448  TRP A O   1 
ATOM   3576 C  CB  . TRP A 1 448  ? 69.032 63.916  -6.678  1.00 10.97 ? 448  TRP A CB  1 
ATOM   3577 C  CG  . TRP A 1 448  ? 68.389 63.909  -8.031  1.00 10.14 ? 448  TRP A CG  1 
ATOM   3578 C  CD1 . TRP A 1 448  ? 67.530 62.962  -8.538  1.00 10.64 ? 448  TRP A CD1 1 
ATOM   3579 C  CD2 . TRP A 1 448  ? 68.540 64.908  -9.038  1.00 9.75  ? 448  TRP A CD2 1 
ATOM   3580 N  NE1 . TRP A 1 448  ? 67.134 63.319  -9.816  1.00 10.45 ? 448  TRP A NE1 1 
ATOM   3581 C  CE2 . TRP A 1 448  ? 67.736 64.509  -10.135 1.00 10.47 ? 448  TRP A CE2 1 
ATOM   3582 C  CE3 . TRP A 1 448  ? 69.259 66.099  -9.114  1.00 11.00 ? 448  TRP A CE3 1 
ATOM   3583 C  CZ2 . TRP A 1 448  ? 67.642 65.257  -11.279 1.00 11.31 ? 448  TRP A CZ2 1 
ATOM   3584 C  CZ3 . TRP A 1 448  ? 69.153 66.863  -10.285 1.00 10.98 ? 448  TRP A CZ3 1 
ATOM   3585 C  CH2 . TRP A 1 448  ? 68.344 66.420  -11.342 1.00 10.02 ? 448  TRP A CH2 1 
ATOM   3586 N  N   . ASP A 1 449  ? 71.920 64.104  -5.287  1.00 16.04 ? 449  ASP A N   1 
ATOM   3587 C  CA  . ASP A 1 449  ? 72.566 64.450  -4.052  1.00 17.73 ? 449  ASP A CA  1 
ATOM   3588 C  C   . ASP A 1 449  ? 71.548 65.106  -3.117  1.00 17.63 ? 449  ASP A C   1 
ATOM   3589 O  O   . ASP A 1 449  ? 70.672 65.835  -3.555  1.00 16.39 ? 449  ASP A O   1 
ATOM   3590 C  CB  . ASP A 1 449  ? 73.676 65.443  -4.371  1.00 21.12 ? 449  ASP A CB  1 
ATOM   3591 C  CG  . ASP A 1 449  ? 74.521 65.760  -3.163  1.00 23.70 ? 449  ASP A CG  1 
ATOM   3592 O  OD1 . ASP A 1 449  ? 75.442 64.962  -2.886  1.00 28.43 ? 449  ASP A OD1 1 
ATOM   3593 O  OD2 . ASP A 1 449  ? 74.261 66.766  -2.481  1.00 25.34 ? 449  ASP A OD2 1 
ATOM   3594 N  N   . GLY A 1 450  ? 71.695 64.901  -1.823  1.00 17.18 ? 450  GLY A N   1 
ATOM   3595 C  CA  . GLY A 1 450  ? 70.783 65.526  -0.890  1.00 17.89 ? 450  GLY A CA  1 
ATOM   3596 C  C   . GLY A 1 450  ? 70.669 67.024  -1.008  1.00 17.64 ? 450  GLY A C   1 
ATOM   3597 O  O   . GLY A 1 450  ? 69.607 67.592  -0.693  1.00 18.13 ? 450  GLY A O   1 
ATOM   3598 N  N   . MET A 1 451  ? 71.754 67.682  -1.450  1.00 17.08 ? 451  MET A N   1 
ATOM   3599 C  CA  . MET A 1 451  ? 71.754 69.118  -1.584  1.00 18.06 ? 451  MET A CA  1 
ATOM   3600 C  C   . MET A 1 451  ? 70.793 69.603  -2.652  1.00 15.53 ? 451  MET A C   1 
ATOM   3601 O  O   . MET A 1 451  ? 70.419 70.786  -2.682  1.00 16.61 ? 451  MET A O   1 
ATOM   3602 C  CB  . MET A 1 451  ? 73.174 69.612  -1.911  1.00 22.48 ? 451  MET A CB  1 
ATOM   3603 C  CG  . MET A 1 451  ? 74.172 69.516  -0.767  1.00 27.71 ? 451  MET A CG  1 
ATOM   3604 S  SD  . MET A 1 451  ? 73.681 70.472  0.719   1.00 36.08 ? 451  MET A SD  1 
ATOM   3605 C  CE  . MET A 1 451  ? 73.076 69.101  1.838   1.00 33.09 ? 451  MET A CE  1 
ATOM   3606 N  N   . ALA A 1 452  ? 70.370 68.685  -3.525  1.00 14.09 ? 452  ALA A N   1 
ATOM   3607 C  CA  . ALA A 1 452  ? 69.445 69.088  -4.583  1.00 13.72 ? 452  ALA A CA  1 
ATOM   3608 C  C   . ALA A 1 452  ? 68.026 69.221  -4.052  1.00 12.63 ? 452  ALA A C   1 
ATOM   3609 O  O   . ALA A 1 452  ? 67.178 69.814  -4.749  1.00 14.52 ? 452  ALA A O   1 
ATOM   3610 C  CB  . ALA A 1 452  ? 69.467 68.129  -5.722  1.00 13.00 ? 452  ALA A CB  1 
ATOM   3611 N  N   . ARG A 1 453  ? 67.775 68.701  -2.839  1.00 12.53 ? 453  ARG A N   1 
ATOM   3612 C  CA  . ARG A 1 453  ? 66.431 68.822  -2.224  1.00 13.11 ? 453  ARG A CA  1 
ATOM   3613 C  C   . ARG A 1 453  ? 65.331 68.224  -3.103  1.00 12.10 ? 453  ARG A C   1 
ATOM   3614 O  O   . ARG A 1 453  ? 64.188 68.689  -3.033  1.00 13.62 ? 453  ARG A O   1 
ATOM   3615 C  CB  . ARG A 1 453  ? 66.135 70.277  -1.940  1.00 13.76 ? 453  ARG A CB  1 
ATOM   3616 C  CG  . ARG A 1 453  ? 67.207 70.939  -1.030  1.00 16.23 ? 453  ARG A CG  1 
ATOM   3617 C  CD  . ARG A 1 453  ? 66.924 72.448  -0.827  1.00 19.20 ? 453  ARG A CD  1 
ATOM   3618 N  NE  . ARG A 1 453  ? 65.756 72.684  0.015   1.00 20.37 ? 453  ARG A NE  1 
ATOM   3619 C  CZ  . ARG A 1 453  ? 65.271 73.895  0.279   1.00 21.05 ? 453  ARG A CZ  1 
ATOM   3620 N  NH1 . ARG A 1 453  ? 65.861 74.989  -0.230  1.00 22.22 ? 453  ARG A NH1 1 
ATOM   3621 N  NH2 . ARG A 1 453  ? 64.183 74.013  1.023   1.00 22.90 ? 453  ARG A NH2 1 
ATOM   3622 N  N   . ILE A 1 454  ? 65.643 67.198  -3.871  1.00 10.98 ? 454  ILE A N   1 
ATOM   3623 C  CA  . ILE A 1 454  ? 64.637 66.587  -4.725  1.00 10.69 ? 454  ILE A CA  1 
ATOM   3624 C  C   . ILE A 1 454  ? 63.643 65.808  -3.862  1.00 11.13 ? 454  ILE A C   1 
ATOM   3625 O  O   . ILE A 1 454  ? 62.408 66.043  -3.981  1.00 10.06 ? 454  ILE A O   1 
ATOM   3626 C  CB  . ILE A 1 454  ? 65.320 65.652  -5.730  1.00 10.22 ? 454  ILE A CB  1 
ATOM   3627 C  CG1 . ILE A 1 454  ? 66.257 66.468  -6.647  1.00 12.32 ? 454  ILE A CG1 1 
ATOM   3628 C  CG2 . ILE A 1 454  ? 64.236 64.826  -6.473  1.00 11.13 ? 454  ILE A CG2 1 
ATOM   3629 C  CD1 . ILE A 1 454  ? 65.552 67.488  -7.549  1.00 12.39 ? 454  ILE A CD1 1 
ATOM   3630 N  N   . GLU A 1 455  ? 64.093 64.938  -2.970  1.00 11.02 ? 455  GLU A N   1 
ATOM   3631 C  CA  . GLU A 1 455  ? 63.151 64.166  -2.128  1.00 11.00 ? 455  GLU A CA  1 
ATOM   3632 C  C   . GLU A 1 455  ? 62.327 65.099  -1.271  1.00 10.40 ? 455  GLU A C   1 
ATOM   3633 O  O   . GLU A 1 455  ? 61.122 64.853  -1.085  1.00 10.57 ? 455  GLU A O   1 
ATOM   3634 C  CB  . GLU A 1 455  ? 63.916 63.176  -1.226  1.00 12.38 ? 455  GLU A CB  1 
ATOM   3635 C  CG  . GLU A 1 455  ? 64.525 61.979  -1.962  1.00 12.97 ? 455  GLU A CG  1 
ATOM   3636 C  CD  . GLU A 1 455  ? 65.937 62.264  -2.570  1.00 12.16 ? 455  GLU A CD  1 
ATOM   3637 O  OE1 . GLU A 1 455  ? 66.395 63.425  -2.481  1.00 13.46 ? 455  GLU A OE1 1 
ATOM   3638 O  OE2 . GLU A 1 455  ? 66.484 61.296  -3.103  1.00 12.62 ? 455  GLU A OE2 1 
ATOM   3639 N  N   . GLU A 1 456  ? 62.898 66.163  -0.749  1.00 11.16 ? 456  GLU A N   1 
ATOM   3640 C  CA  . GLU A 1 456  ? 62.185 67.117  0.072   1.00 10.47 ? 456  GLU A CA  1 
ATOM   3641 C  C   . GLU A 1 456  ? 61.029 67.754  -0.693  1.00 10.21 ? 456  GLU A C   1 
ATOM   3642 O  O   . GLU A 1 456  ? 59.879 67.828  -0.209  1.00 10.10 ? 456  GLU A O   1 
ATOM   3643 C  CB  . GLU A 1 456  ? 63.197 68.203  0.542   1.00 12.19 ? 456  GLU A CB  1 
ATOM   3644 C  CG  . GLU A 1 456  ? 62.584 69.331  1.322   1.00 15.41 ? 456  GLU A CG  1 
ATOM   3645 C  CD  . GLU A 1 456  ? 63.503 70.550  1.550   1.00 17.98 ? 456  GLU A CD  1 
ATOM   3646 O  OE1 . GLU A 1 456  ? 64.735 70.444  1.323   1.00 20.00 ? 456  GLU A OE1 1 
ATOM   3647 O  OE2 . GLU A 1 456  ? 62.987 71.623  1.973   1.00 20.33 ? 456  GLU A OE2 1 
ATOM   3648 N  N   . ARG A 1 457  ? 61.296 68.233  -1.906  1.00 9.53  ? 457  ARG A N   1 
ATOM   3649 C  CA  . ARG A 1 457  ? 60.232 68.889  -2.673  1.00 8.69  ? 457  ARG A CA  1 
ATOM   3650 C  C   . ARG A 1 457  ? 59.171 67.885  -3.127  1.00 8.34  ? 457  ARG A C   1 
ATOM   3651 O  O   . ARG A 1 457  ? 57.973 68.235  -3.118  1.00 8.79  ? 457  ARG A O   1 
ATOM   3652 C  CB  . ARG A 1 457  ? 60.847 69.642  -3.886  1.00 9.57  ? 457  ARG A CB  1 
ATOM   3653 C  CG  . ARG A 1 457  ? 61.140 71.099  -3.653  1.00 11.67 ? 457  ARG A CG  1 
ATOM   3654 C  CD  . ARG A 1 457  ? 62.179 71.329  -2.597  1.00 12.79 ? 457  ARG A CD  1 
ATOM   3655 N  NE  . ARG A 1 457  ? 62.352 72.763  -2.250  1.00 15.59 ? 457  ARG A NE  1 
ATOM   3656 C  CZ  . ARG A 1 457  ? 63.248 73.569  -2.830  1.00 17.87 ? 457  ARG A CZ  1 
ATOM   3657 N  NH1 . ARG A 1 457  ? 64.073 73.107  -3.793  1.00 16.88 ? 457  ARG A NH1 1 
ATOM   3658 N  NH2 . ARG A 1 457  ? 63.327 74.841  -2.443  1.00 18.85 ? 457  ARG A NH2 1 
ATOM   3659 N  N   . LEU A 1 458  ? 59.561 66.683  -3.487  1.00 7.89  ? 458  LEU A N   1 
ATOM   3660 C  CA  . LEU A 1 458  ? 58.556 65.675  -3.902  1.00 8.34  ? 458  LEU A CA  1 
ATOM   3661 C  C   . LEU A 1 458  ? 57.723 65.272  -2.716  1.00 8.97  ? 458  LEU A C   1 
ATOM   3662 O  O   . LEU A 1 458  ? 56.498 65.093  -2.878  1.00 8.80  ? 458  LEU A O   1 
ATOM   3663 C  CB  . LEU A 1 458  ? 59.228 64.468  -4.509  1.00 8.38  ? 458  LEU A CB  1 
ATOM   3664 C  CG  . LEU A 1 458  ? 59.944 64.785  -5.863  1.00 8.06  ? 458  LEU A CG  1 
ATOM   3665 C  CD1 . LEU A 1 458  ? 60.711 63.581  -6.274  1.00 10.68 ? 458  LEU A CD1 1 
ATOM   3666 C  CD2 . LEU A 1 458  ? 58.920 65.215  -6.996  1.00 10.00 ? 458  LEU A CD2 1 
ATOM   3667 N  N   . GLU A 1 459  ? 58.301 65.149  -1.511  1.00 8.64  ? 459  GLU A N   1 
ATOM   3668 C  CA  . GLU A 1 459  ? 57.468 64.758  -0.368  1.00 8.98  ? 459  GLU A CA  1 
ATOM   3669 C  C   . GLU A 1 459  ? 56.453 65.876  -0.080  1.00 9.15  ? 459  GLU A C   1 
ATOM   3670 O  O   . GLU A 1 459  ? 55.256 65.597  0.185   1.00 8.99  ? 459  GLU A O   1 
ATOM   3671 C  CB  . GLU A 1 459  ? 58.379 64.540  0.842   1.00 9.08  ? 459  GLU A CB  1 
ATOM   3672 C  CG  . GLU A 1 459  ? 57.574 64.197  2.116   1.00 13.09 ? 459  GLU A CG  1 
ATOM   3673 C  CD  . GLU A 1 459  ? 58.459 63.567  3.170   1.00 15.82 ? 459  GLU A CD  1 
ATOM   3674 O  OE1 . GLU A 1 459  ? 59.077 64.361  3.878   1.00 20.13 ? 459  GLU A OE1 1 
ATOM   3675 O  OE2 . GLU A 1 459  ? 58.561 62.332  3.250   1.00 18.35 ? 459  GLU A OE2 1 
ATOM   3676 N  N   . GLN A 1 460  ? 56.876 67.134  -0.156  1.00 8.33  ? 460  GLN A N   1 
ATOM   3677 C  CA  . GLN A 1 460  ? 55.937 68.224  0.063   1.00 9.33  ? 460  GLN A CA  1 
ATOM   3678 C  C   . GLN A 1 460  ? 54.806 68.141  -0.981  1.00 9.27  ? 460  GLN A C   1 
ATOM   3679 O  O   . GLN A 1 460  ? 53.615 68.243  -0.672  1.00 9.15  ? 460  GLN A O   1 
ATOM   3680 C  CB  . GLN A 1 460  ? 56.654 69.562  -0.087  1.00 11.26 ? 460  GLN A CB  1 
ATOM   3681 C  CG  . GLN A 1 460  ? 55.755 70.780  0.088   1.00 16.38 ? 460  GLN A CG  1 
ATOM   3682 C  CD  . GLN A 1 460  ? 56.551 72.093  -0.166  1.00 19.74 ? 460  GLN A CD  1 
ATOM   3683 O  OE1 . GLN A 1 460  ? 56.150 73.138  0.272   1.00 25.32 ? 460  GLN A OE1 1 
ATOM   3684 N  NE2 . GLN A 1 460  ? 57.641 72.003  -0.922  1.00 22.30 ? 460  GLN A NE2 1 
ATOM   3685 N  N   . ALA A 1 461  ? 55.172 67.984  -2.242  1.00 8.01  ? 461  ALA A N   1 
ATOM   3686 C  CA  . ALA A 1 461  ? 54.115 67.936  -3.259  1.00 8.13  ? 461  ALA A CA  1 
ATOM   3687 C  C   . ALA A 1 461  ? 53.137 66.776  -3.090  1.00 7.49  ? 461  ALA A C   1 
ATOM   3688 O  O   . ALA A 1 461  ? 51.915 66.983  -3.172  1.00 8.12  ? 461  ALA A O   1 
ATOM   3689 C  CB  . ALA A 1 461  ? 54.784 67.935  -4.661  1.00 8.77  ? 461  ALA A CB  1 
ATOM   3690 N  N   . ARG A 1 462  ? 53.658 65.588  -2.816  1.00 7.76  ? 462  ARG A N   1 
ATOM   3691 C  CA  . ARG A 1 462  ? 52.800 64.436  -2.600  1.00 7.49  ? 462  ARG A CA  1 
ATOM   3692 C  C   . ARG A 1 462  ? 51.893 64.685  -1.395  1.00 7.27  ? 462  ARG A C   1 
ATOM   3693 O  O   . ARG A 1 462  ? 50.686 64.309  -1.437  1.00 7.42  ? 462  ARG A O   1 
ATOM   3694 C  CB  . ARG A 1 462  ? 53.572 63.152  -2.325  1.00 8.12  ? 462  ARG A CB  1 
ATOM   3695 C  CG  . ARG A 1 462  ? 54.309 62.572  -3.564  1.00 7.05  ? 462  ARG A CG  1 
ATOM   3696 C  CD  . ARG A 1 462  ? 54.802 61.161  -3.304  1.00 8.11  ? 462  ARG A CD  1 
ATOM   3697 N  NE  . ARG A 1 462  ? 55.685 61.119  -2.123  1.00 7.94  ? 462  ARG A NE  1 
ATOM   3698 C  CZ  . ARG A 1 462  ? 57.001 61.264  -2.191  1.00 9.36  ? 462  ARG A CZ  1 
ATOM   3699 N  NH1 . ARG A 1 462  ? 57.605 61.424  -3.354  1.00 9.98  ? 462  ARG A NH1 1 
ATOM   3700 N  NH2 . ARG A 1 462  ? 57.723 61.273  -1.081  1.00 11.16 ? 462  ARG A NH2 1 
ATOM   3701 N  N   . ARG A 1 463  ? 52.421 65.305  -0.332  1.00 7.50  ? 463  ARG A N   1 
ATOM   3702 C  CA  . ARG A 1 463  ? 51.585 65.464  0.858   1.00 7.25  ? 463  ARG A CA  1 
ATOM   3703 C  C   . ARG A 1 463  ? 50.523 66.532  0.690   1.00 7.44  ? 463  ARG A C   1 
ATOM   3704 O  O   . ARG A 1 463  ? 49.389 66.356  1.213   1.00 8.26  ? 463  ARG A O   1 
ATOM   3705 C  CB  . ARG A 1 463  ? 52.485 65.725  2.089   1.00 7.76  ? 463  ARG A CB  1 
ATOM   3706 C  CG  . ARG A 1 463  ? 53.178 64.448  2.494   1.00 8.48  ? 463  ARG A CG  1 
ATOM   3707 C  CD  . ARG A 1 463  ? 54.224 64.709  3.606   1.00 11.00 ? 463  ARG A CD  1 
ATOM   3708 N  NE  . ARG A 1 463  ? 54.727 63.383  3.966   1.00 11.74 ? 463  ARG A NE  1 
ATOM   3709 C  CZ  . ARG A 1 463  ? 55.485 63.134  5.020   1.00 14.58 ? 463  ARG A CZ  1 
ATOM   3710 N  NH1 . ARG A 1 463  ? 55.850 64.131  5.793   1.00 15.08 ? 463  ARG A NH1 1 
ATOM   3711 N  NH2 . ARG A 1 463  ? 55.799 61.854  5.277   1.00 15.28 ? 463  ARG A NH2 1 
ATOM   3712 N  N   . GLU A 1 464  ? 50.767 67.626  -0.052  1.00 7.46  ? 464  GLU A N   1 
ATOM   3713 C  CA  . GLU A 1 464  ? 49.733 68.628  -0.178  1.00 7.66  ? 464  GLU A CA  1 
ATOM   3714 C  C   . GLU A 1 464  ? 48.649 68.097  -1.099  1.00 8.14  ? 464  GLU A C   1 
ATOM   3715 O  O   . GLU A 1 464  ? 47.460 68.346  -0.854  1.00 8.03  ? 464  GLU A O   1 
ATOM   3716 C  CB  . GLU A 1 464  ? 50.264 69.953  -0.768  1.00 9.72  ? 464  GLU A CB  1 
ATOM   3717 C  CG  . GLU A 1 464  ? 51.465 70.623  0.015   1.00 11.81 ? 464  GLU A CG  1 
ATOM   3718 C  CD  . GLU A 1 464  ? 51.194 71.009  1.473   1.00 16.04 ? 464  GLU A CD  1 
ATOM   3719 O  OE1 . GLU A 1 464  ? 50.232 70.551  2.072   1.00 15.35 ? 464  GLU A OE1 1 
ATOM   3720 O  OE2 . GLU A 1 464  ? 52.025 71.796  1.990   1.00 19.55 ? 464  GLU A OE2 1 
ATOM   3721 N  N   . LEU A 1 465  ? 49.035 67.374  -2.155  1.00 6.98  ? 465  LEU A N   1 
ATOM   3722 C  CA  . LEU A 1 465  ? 47.996 66.798  -3.049  1.00 6.73  ? 465  LEU A CA  1 
ATOM   3723 C  C   . LEU A 1 465  ? 47.227 65.727  -2.278  1.00 6.91  ? 465  LEU A C   1 
ATOM   3724 O  O   . LEU A 1 465  ? 45.962 65.638  -2.387  1.00 7.19  ? 465  LEU A O   1 
ATOM   3725 C  CB  . LEU A 1 465  ? 48.639 66.207  -4.317  1.00 7.09  ? 465  LEU A CB  1 
ATOM   3726 C  CG  . LEU A 1 465  ? 47.634 65.526  -5.289  1.00 7.40  ? 465  LEU A CG  1 
ATOM   3727 C  CD1 . LEU A 1 465  ? 46.565 66.552  -5.770  1.00 8.10  ? 465  LEU A CD1 1 
ATOM   3728 C  CD2 . LEU A 1 465  ? 48.412 64.986  -6.503  1.00 8.18  ? 465  LEU A CD2 1 
ATOM   3729 N  N   . SER A 1 466  ? 47.933 64.929  -1.452  1.00 6.42  ? 466  SER A N   1 
ATOM   3730 C  CA  . SER A 1 466  ? 47.235 63.893  -0.682  1.00 6.21  ? 466  SER A CA  1 
ATOM   3731 C  C   . SER A 1 466  ? 46.246 64.500  0.316   1.00 6.43  ? 466  SER A C   1 
ATOM   3732 O  O   . SER A 1 466  ? 45.117 63.984  0.455   1.00 6.72  ? 466  SER A O   1 
ATOM   3733 C  CB  . SER A 1 466  ? 48.255 63.055  0.069   1.00 6.51  ? 466  SER A CB  1 
ATOM   3734 O  OG  . SER A 1 466  ? 49.003 62.229  -0.831  1.00 7.26  ? 466  SER A OG  1 
ATOM   3735 N  N   . LEU A 1 467  ? 46.634 65.597  0.966   1.00 6.10  ? 467  LEU A N   1 
ATOM   3736 C  CA  . LEU A 1 467  ? 45.727 66.259  1.919   1.00 6.79  ? 467  LEU A CA  1 
ATOM   3737 C  C   . LEU A 1 467  ? 44.449 66.690  1.230   1.00 5.83  ? 467  LEU A C   1 
ATOM   3738 O  O   . LEU A 1 467  ? 43.363 66.537  1.800   1.00 6.38  ? 467  LEU A O   1 
ATOM   3739 C  CB  . LEU A 1 467  ? 46.484 67.452  2.523   1.00 7.92  ? 467  LEU A CB  1 
ATOM   3740 C  CG  . LEU A 1 467  ? 45.656 68.194  3.566   1.00 9.97  ? 467  LEU A CG  1 
ATOM   3741 C  CD1 . LEU A 1 467  ? 45.618 67.345  4.809   1.00 15.33 ? 467  LEU A CD1 1 
ATOM   3742 C  CD2 . LEU A 1 467  ? 46.317 69.545  3.861   1.00 11.02 ? 467  LEU A CD2 1 
ATOM   3743 N  N   . PHE A 1 468  ? 44.562 67.187  -0.003  1.00 6.01  ? 468  PHE A N   1 
ATOM   3744 C  CA  . PHE A 1 468  ? 43.389 67.697  -0.699  1.00 5.99  ? 468  PHE A CA  1 
ATOM   3745 C  C   . PHE A 1 468  ? 42.426 66.597  -1.074  1.00 6.07  ? 468  PHE A C   1 
ATOM   3746 O  O   . PHE A 1 468  ? 41.247 66.902  -1.373  1.00 6.94  ? 468  PHE A O   1 
ATOM   3747 C  CB  . PHE A 1 468  ? 43.821 68.488  -1.954  1.00 7.02  ? 468  PHE A CB  1 
ATOM   3748 C  CG  . PHE A 1 468  ? 42.699 69.328  -2.511  1.00 5.80  ? 468  PHE A CG  1 
ATOM   3749 C  CD1 . PHE A 1 468  ? 42.039 70.254  -1.733  1.00 7.11  ? 468  PHE A CD1 1 
ATOM   3750 C  CD2 . PHE A 1 468  ? 42.271 69.135  -3.815  1.00 7.04  ? 468  PHE A CD2 1 
ATOM   3751 C  CE1 . PHE A 1 468  ? 40.969 70.988  -2.211  1.00 7.03  ? 468  PHE A CE1 1 
ATOM   3752 C  CE2 . PHE A 1 468  ? 41.198 69.877  -4.308  1.00 6.57  ? 468  PHE A CE2 1 
ATOM   3753 C  CZ  . PHE A 1 468  ? 40.545 70.807  -3.506  1.00 7.04  ? 468  PHE A CZ  1 
ATOM   3754 N  N   . GLN A 1 469  ? 42.851 65.324  -1.061  1.00 5.56  ? 469  GLN A N   1 
ATOM   3755 C  CA  . GLN A 1 469  ? 41.884 64.258  -1.320  1.00 5.71  ? 469  GLN A CA  1 
ATOM   3756 C  C   . GLN A 1 469  ? 40.873 64.083  -0.206  1.00 6.11  ? 469  GLN A C   1 
ATOM   3757 O  O   . GLN A 1 469  ? 39.910 63.312  -0.380  1.00 6.51  ? 469  GLN A O   1 
ATOM   3758 C  CB  . GLN A 1 469  ? 42.618 62.910  -1.516  1.00 6.16  ? 469  GLN A CB  1 
ATOM   3759 C  CG  . GLN A 1 469  ? 43.741 62.977  -2.642  1.00 6.22  ? 469  GLN A CG  1 
ATOM   3760 C  CD  . GLN A 1 469  ? 43.257 63.676  -3.909  1.00 6.12  ? 469  GLN A CD  1 
ATOM   3761 O  OE1 . GLN A 1 469  ? 43.800 64.728  -4.357  1.00 8.71  ? 469  GLN A OE1 1 
ATOM   3762 N  NE2 . GLN A 1 469  ? 42.230 63.147  -4.456  1.00 4.65  ? 469  GLN A NE2 1 
ATOM   3763 N  N   . HIS A 1 470  ? 41.080 64.751  0.922   1.00 5.58  ? 470  HIS A N   1 
ATOM   3764 C  CA  . HIS A 1 470  ? 40.127 64.680  2.024   1.00 5.60  ? 470  HIS A CA  1 
ATOM   3765 C  C   . HIS A 1 470  ? 38.696 64.935  1.527   1.00 6.33  ? 470  HIS A C   1 
ATOM   3766 O  O   . HIS A 1 470  ? 38.483 65.684  0.567   1.00 6.45  ? 470  HIS A O   1 
ATOM   3767 C  CB  . HIS A 1 470  ? 40.529 65.726  3.074   1.00 6.44  ? 470  HIS A CB  1 
ATOM   3768 C  CG  . HIS A 1 470  ? 39.499 65.883  4.139   1.00 6.47  ? 470  HIS A CG  1 
ATOM   3769 N  ND1 . HIS A 1 470  ? 39.025 67.098  4.591   1.00 8.71  ? 470  HIS A ND1 1 
ATOM   3770 C  CD2 . HIS A 1 470  ? 38.854 64.923  4.849   1.00 4.79  ? 470  HIS A CD2 1 
ATOM   3771 C  CE1 . HIS A 1 470  ? 38.123 66.866  5.548   1.00 5.97  ? 470  HIS A CE1 1 
ATOM   3772 N  NE2 . HIS A 1 470  ? 38.015 65.559  5.704   1.00 10.00 ? 470  HIS A NE2 1 
ATOM   3773 N  N   . HIS A 1 471  ? 37.730 64.306  2.218   1.00 6.50  ? 471  HIS A N   1 
ATOM   3774 C  CA  . HIS A 1 471  ? 36.337 64.423  1.866   1.00 6.21  ? 471  HIS A CA  1 
ATOM   3775 C  C   . HIS A 1 471  ? 35.683 65.789  2.155   1.00 6.73  ? 471  HIS A C   1 
ATOM   3776 O  O   . HIS A 1 471  ? 34.487 65.920  1.924   1.00 7.69  ? 471  HIS A O   1 
ATOM   3777 C  CB  . HIS A 1 471  ? 35.559 63.254  2.464   1.00 5.83  ? 471  HIS A CB  1 
ATOM   3778 C  CG  . HIS A 1 471  ? 35.625 63.187  3.951   1.00 5.23  ? 471  HIS A CG  1 
ATOM   3779 N  ND1 . HIS A 1 471  ? 36.571 62.456  4.627   1.00 6.50  ? 471  HIS A ND1 1 
ATOM   3780 C  CD2 . HIS A 1 471  ? 34.875 63.808  4.883   1.00 6.23  ? 471  HIS A CD2 1 
ATOM   3781 C  CE1 . HIS A 1 471  ? 36.403 62.636  5.935   1.00 6.03  ? 471  HIS A CE1 1 
ATOM   3782 N  NE2 . HIS A 1 471  ? 35.372 63.445  6.128   1.00 6.63  ? 471  HIS A NE2 1 
ATOM   3783 N  N   . ASP A 1 472  ? 36.464 66.780  2.643   1.00 7.14  ? 472  ASP A N   1 
ATOM   3784 C  CA  . ASP A 1 472  ? 35.984 68.174  2.602   1.00 6.81  ? 472  ASP A CA  1 
ATOM   3785 C  C   . ASP A 1 472  ? 36.993 69.028  1.808   1.00 7.55  ? 472  ASP A C   1 
ATOM   3786 O  O   . ASP A 1 472  ? 36.846 70.269  1.809   1.00 8.02  ? 472  ASP A O   1 
ATOM   3787 C  CB  . ASP A 1 472  ? 35.741 68.817  3.965   1.00 7.64  ? 472  ASP A CB  1 
ATOM   3788 C  CG  . ASP A 1 472  ? 34.674 68.088  4.777   1.00 7.32  ? 472  ASP A CG  1 
ATOM   3789 O  OD1 . ASP A 1 472  ? 33.472 68.179  4.365   1.00 8.10  ? 472  ASP A OD1 1 
ATOM   3790 O  OD2 . ASP A 1 472  ? 35.097 67.430  5.747   1.00 7.91  ? 472  ASP A OD2 1 
ATOM   3791 N  N   . GLY A 1 473  ? 37.937 68.411  1.084   1.00 6.51  ? 473  GLY A N   1 
ATOM   3792 C  CA  . GLY A 1 473  ? 38.914 69.185  0.300   1.00 7.34  ? 473  GLY A CA  1 
ATOM   3793 C  C   . GLY A 1 473  ? 38.442 69.251  -1.153  1.00 5.91  ? 473  GLY A C   1 
ATOM   3794 O  O   . GLY A 1 473  ? 37.729 70.178  -1.528  1.00 7.28  ? 473  GLY A O   1 
ATOM   3795 N  N   . ILE A 1 474  ? 38.769 68.214  -1.929  1.00 6.33  ? 474  ILE A N   1 
ATOM   3796 C  CA  . ILE A 1 474  ? 38.331 68.210  -3.335  1.00 6.28  ? 474  ILE A CA  1 
ATOM   3797 C  C   . ILE A 1 474  ? 36.819 68.318  -3.515  1.00 6.16  ? 474  ILE A C   1 
ATOM   3798 O  O   . ILE A 1 474  ? 36.386 68.804  -4.548  1.00 7.01  ? 474  ILE A O   1 
ATOM   3799 C  CB  . ILE A 1 474  ? 38.949 66.939  -4.030  1.00 6.19  ? 474  ILE A CB  1 
ATOM   3800 C  CG1 . ILE A 1 474  ? 38.685 66.995  -5.536  1.00 7.19  ? 474  ILE A CG1 1 
ATOM   3801 C  CG2 . ILE A 1 474  ? 38.381 65.609  -3.383  1.00 7.56  ? 474  ILE A CG2 1 
ATOM   3802 C  CD1 . ILE A 1 474  ? 39.411 65.806  -6.293  1.00 8.72  ? 474  ILE A CD1 1 
ATOM   3803 N  N   . THR A 1 475  ? 36.078 67.867  -2.511  1.00 5.70  ? 475  THR A N   1 
ATOM   3804 C  CA  . THR A 1 475  ? 34.610 67.967  -2.549  1.00 7.11  ? 475  THR A CA  1 
ATOM   3805 C  C   . THR A 1 475  ? 34.088 69.419  -2.547  1.00 6.07  ? 475  THR A C   1 
ATOM   3806 O  O   . THR A 1 475  ? 32.917 69.647  -2.880  1.00 6.94  ? 475  THR A O   1 
ATOM   3807 C  CB  . THR A 1 475  ? 34.037 67.296  -1.293  1.00 7.09  ? 475  THR A CB  1 
ATOM   3808 O  OG1 . THR A 1 475  ? 34.566 68.032  -0.166  1.00 7.83  ? 475  THR A OG1 1 
ATOM   3809 C  CG2 . THR A 1 475  ? 34.431 65.828  -1.196  1.00 7.83  ? 475  THR A CG2 1 
ATOM   3810 N  N   . GLY A 1 476  ? 34.919 70.390  -2.193  1.00 6.85  ? 476  GLY A N   1 
ATOM   3811 C  CA  . GLY A 1 476  ? 34.420 71.773  -2.192  1.00 7.06  ? 476  GLY A CA  1 
ATOM   3812 C  C   . GLY A 1 476  ? 33.460 72.061  -1.032  1.00 7.14  ? 476  GLY A C   1 
ATOM   3813 O  O   . GLY A 1 476  ? 32.571 72.893  -1.176  1.00 7.73  ? 476  GLY A O   1 
ATOM   3814 N  N   . THR A 1 477  ? 33.633 71.342  0.072   1.00 7.05  ? 477  THR A N   1 
ATOM   3815 C  CA  . THR A 1 477  ? 32.749 71.501  1.192   1.00 7.74  ? 477  THR A CA  1 
ATOM   3816 C  C   . THR A 1 477  ? 33.361 72.072  2.465   1.00 6.94  ? 477  THR A C   1 
ATOM   3817 O  O   . THR A 1 477  ? 32.805 71.906  3.547   1.00 9.41  ? 477  THR A O   1 
ATOM   3818 C  CB  . THR A 1 477  ? 32.048 70.155  1.529   1.00 7.34  ? 477  THR A CB  1 
ATOM   3819 O  OG1 . THR A 1 477  ? 33.017 69.124  1.788   1.00 7.14  ? 477  THR A OG1 1 
ATOM   3820 C  CG2 . THR A 1 477  ? 31.200 69.698  0.322   1.00 7.83  ? 477  THR A CG2 1 
ATOM   3821 N  N   . ALA A 1 478  ? 34.458 72.820  2.342   1.00 6.94  ? 478  ALA A N   1 
ATOM   3822 C  CA  . ALA A 1 478  ? 35.099 73.430  3.529   1.00 7.41  ? 478  ALA A CA  1 
ATOM   3823 C  C   . ALA A 1 478  ? 34.819 74.938  3.581   1.00 7.43  ? 478  ALA A C   1 
ATOM   3824 O  O   . ALA A 1 478  ? 34.318 75.574  2.632   1.00 7.98  ? 478  ALA A O   1 
ATOM   3825 C  CB  . ALA A 1 478  ? 36.663 73.192  3.489   1.00 7.88  ? 478  ALA A CB  1 
ATOM   3826 N  N   . LYS A 1 479  ? 35.108 75.529  4.742   1.00 7.71  ? 479  LYS A N   1 
ATOM   3827 C  CA  . LYS A 1 479  ? 34.867 76.979  4.853   1.00 8.61  ? 479  LYS A CA  1 
ATOM   3828 C  C   . LYS A 1 479  ? 35.816 77.735  3.931   1.00 8.18  ? 479  LYS A C   1 
ATOM   3829 O  O   . LYS A 1 479  ? 36.887 77.229  3.556   1.00 7.77  ? 479  LYS A O   1 
ATOM   3830 C  CB  . LYS A 1 479  ? 35.074 77.427  6.309   1.00 9.39  ? 479  LYS A CB  1 
ATOM   3831 C  CG  . LYS A 1 479  ? 33.821 77.117  7.204   1.00 12.09 ? 479  LYS A CG  1 
ATOM   3832 C  CD  . LYS A 1 479  ? 33.931 77.853  8.514   1.00 13.27 ? 479  LYS A CD  1 
ATOM   3833 C  CE  . LYS A 1 479  ? 32.643 77.731  9.376   1.00 15.79 ? 479  LYS A CE  1 
ATOM   3834 N  NZ  . LYS A 1 479  ? 31.411 78.384  8.772   1.00 16.59 ? 479  LYS A NZ  1 
ATOM   3835 N  N   . THR A 1 480  ? 35.457 78.963  3.592   1.00 8.70  ? 480  THR A N   1 
ATOM   3836 C  CA  . THR A 1 480  ? 36.236 79.751  2.681   1.00 9.23  ? 480  THR A CA  1 
ATOM   3837 C  C   . THR A 1 480  ? 37.699 79.844  3.050   1.00 9.11  ? 480  THR A C   1 
ATOM   3838 O  O   . THR A 1 480  ? 38.566 79.662  2.155   1.00 9.27  ? 480  THR A O   1 
ATOM   3839 C  CB  . THR A 1 480  ? 35.646 81.154  2.621   1.00 10.54 ? 480  THR A CB  1 
ATOM   3840 O  OG1 . THR A 1 480  ? 34.311 81.049  2.120   1.00 13.17 ? 480  THR A OG1 1 
ATOM   3841 C  CG2 . THR A 1 480  ? 36.416 82.062  1.684   1.00 13.00 ? 480  THR A CG2 1 
ATOM   3842 N  N   . HIS A 1 481  ? 38.057 80.132  4.314   1.00 8.72  ? 481  HIS A N   1 
ATOM   3843 C  CA  . HIS A 1 481  ? 39.481 80.245  4.613   1.00 8.13  ? 481  HIS A CA  1 
ATOM   3844 C  C   . HIS A 1 481  ? 40.230 78.918  4.565   1.00 9.10  ? 481  HIS A C   1 
ATOM   3845 O  O   . HIS A 1 481  ? 41.448 78.876  4.427   1.00 9.67  ? 481  HIS A O   1 
ATOM   3846 C  CB  . HIS A 1 481  ? 39.687 80.957  5.997   1.00 9.93  ? 481  HIS A CB  1 
ATOM   3847 C  CG  . HIS A 1 481  ? 39.521 80.056  7.183   1.00 9.83  ? 481  HIS A CG  1 
ATOM   3848 N  ND1 . HIS A 1 481  ? 38.287 79.612  7.647   1.00 11.67 ? 481  HIS A ND1 1 
ATOM   3849 C  CD2 . HIS A 1 481  ? 40.455 79.538  8.015   1.00 10.56 ? 481  HIS A CD2 1 
ATOM   3850 C  CE1 . HIS A 1 481  ? 38.491 78.868  8.717   1.00 10.63 ? 481  HIS A CE1 1 
ATOM   3851 N  NE2 . HIS A 1 481  ? 39.788 78.811  8.961   1.00 11.86 ? 481  HIS A NE2 1 
ATOM   3852 N  N   . VAL A 1 482  ? 39.471 77.803  4.682   1.00 8.43  ? 482  VAL A N   1 
ATOM   3853 C  CA  . VAL A 1 482  ? 40.071 76.459  4.593   1.00 8.34  ? 482  VAL A CA  1 
ATOM   3854 C  C   . VAL A 1 482  ? 40.331 76.151  3.115   1.00 7.12  ? 482  VAL A C   1 
ATOM   3855 O  O   . VAL A 1 482  ? 41.400 75.609  2.800   1.00 7.42  ? 482  VAL A O   1 
ATOM   3856 C  CB  . VAL A 1 482  ? 39.122 75.428  5.244   1.00 7.17  ? 482  VAL A CB  1 
ATOM   3857 C  CG1 . VAL A 1 482  ? 39.775 74.030  5.219   1.00 8.81  ? 482  VAL A CG1 1 
ATOM   3858 C  CG2 . VAL A 1 482  ? 38.919 75.789  6.775   1.00 8.87  ? 482  VAL A CG2 1 
ATOM   3859 N  N   . VAL A 1 483  ? 39.395 76.493  2.236   1.00 7.28  ? 483  VAL A N   1 
ATOM   3860 C  CA  . VAL A 1 483  ? 39.649 76.357  0.801   1.00 7.56  ? 483  VAL A CA  1 
ATOM   3861 C  C   . VAL A 1 483  ? 40.903 77.159  0.409   1.00 7.55  ? 483  VAL A C   1 
ATOM   3862 O  O   . VAL A 1 483  ? 41.754 76.642  -0.348  1.00 8.08  ? 483  VAL A O   1 
ATOM   3863 C  CB  . VAL A 1 483  ? 38.449 76.865  0.006   1.00 7.21  ? 483  VAL A CB  1 
ATOM   3864 C  CG1 . VAL A 1 483  ? 38.735 76.850  -1.511  1.00 8.96  ? 483  VAL A CG1 1 
ATOM   3865 C  CG2 . VAL A 1 483  ? 37.218 75.972  0.326   1.00 8.46  ? 483  VAL A CG2 1 
ATOM   3866 N  N   . VAL A 1 484  ? 41.091 78.365  0.992   1.00 8.75  ? 484  VAL A N   1 
ATOM   3867 C  CA  . VAL A 1 484  ? 42.282 79.181  0.687   1.00 9.74  ? 484  VAL A CA  1 
ATOM   3868 C  C   . VAL A 1 484  ? 43.509 78.438  1.159   1.00 8.70  ? 484  VAL A C   1 
ATOM   3869 O  O   . VAL A 1 484  ? 44.514 78.418  0.430   1.00 8.87  ? 484  VAL A O   1 
ATOM   3870 C  CB  . VAL A 1 484  ? 42.171 80.533  1.367   1.00 10.77 ? 484  VAL A CB  1 
ATOM   3871 C  CG1 . VAL A 1 484  ? 43.548 81.276  1.292   1.00 11.61 ? 484  VAL A CG1 1 
ATOM   3872 C  CG2 . VAL A 1 484  ? 41.114 81.354  0.650   1.00 12.29 ? 484  VAL A CG2 1 
ATOM   3873 N  N   . ASP A 1 485  ? 43.468 77.798  2.334   1.00 8.78  ? 485  ASP A N   1 
ATOM   3874 C  CA  . ASP A 1 485  ? 44.628 77.038  2.794   1.00 8.22  ? 485  ASP A CA  1 
ATOM   3875 C  C   . ASP A 1 485  ? 44.969 75.900  1.838   1.00 8.57  ? 485  ASP A C   1 
ATOM   3876 O  O   . ASP A 1 485  ? 46.128 75.687  1.502   1.00 8.40  ? 485  ASP A O   1 
ATOM   3877 C  CB  . ASP A 1 485  ? 44.358 76.503  4.223   1.00 9.21  ? 485  ASP A CB  1 
ATOM   3878 C  CG  . ASP A 1 485  ? 45.593 75.869  4.832   1.00 9.83  ? 485  ASP A CG  1 
ATOM   3879 O  OD1 . ASP A 1 485  ? 46.616 76.581  4.950   1.00 14.31 ? 485  ASP A OD1 1 
ATOM   3880 O  OD2 . ASP A 1 485  ? 45.583 74.713  5.208   1.00 10.13 ? 485  ASP A OD2 1 
ATOM   3881 N  N   . TYR A 1 486  ? 43.966 75.142  1.402   1.00 7.32  ? 486  TYR A N   1 
ATOM   3882 C  CA  . TYR A 1 486  ? 44.244 74.063  0.464   1.00 7.87  ? 486  TYR A CA  1 
ATOM   3883 C  C   . TYR A 1 486  ? 44.828 74.610  -0.839  1.00 7.58  ? 486  TYR A C   1 
ATOM   3884 O  O   . TYR A 1 486  ? 45.751 73.978  -1.377  1.00 8.38  ? 486  TYR A O   1 
ATOM   3885 C  CB  . TYR A 1 486  ? 42.974 73.281  0.103   1.00 8.10  ? 486  TYR A CB  1 
ATOM   3886 C  CG  . TYR A 1 486  ? 42.365 72.445  1.234   1.00 7.76  ? 486  TYR A CG  1 
ATOM   3887 C  CD1 . TYR A 1 486  ? 43.156 71.590  2.015   1.00 9.15  ? 486  TYR A CD1 1 
ATOM   3888 C  CD2 . TYR A 1 486  ? 40.992 72.491  1.425   1.00 8.47  ? 486  TYR A CD2 1 
ATOM   3889 C  CE1 . TYR A 1 486  ? 42.536 70.746  3.016   1.00 9.56  ? 486  TYR A CE1 1 
ATOM   3890 C  CE2 . TYR A 1 486  ? 40.365 71.667  2.387   1.00 8.01  ? 486  TYR A CE2 1 
ATOM   3891 C  CZ  . TYR A 1 486  ? 41.151 70.822  3.152   1.00 8.76  ? 486  TYR A CZ  1 
ATOM   3892 O  OH  . TYR A 1 486  ? 40.527 69.999  4.087   1.00 10.09 ? 486  TYR A OH  1 
ATOM   3893 N  N   . GLU A 1 487  ? 44.297 75.723  -1.343  1.00 8.56  ? 487  GLU A N   1 
ATOM   3894 C  CA  . GLU A 1 487  ? 44.813 76.305  -2.574  1.00 8.49  ? 487  GLU A CA  1 
ATOM   3895 C  C   . GLU A 1 487  ? 46.266 76.746  -2.402  1.00 8.70  ? 487  GLU A C   1 
ATOM   3896 O  O   . GLU A 1 487  ? 47.120 76.466  -3.274  1.00 9.28  ? 487  GLU A O   1 
ATOM   3897 C  CB  . GLU A 1 487  ? 43.961 77.499  -2.971  1.00 9.17  ? 487  GLU A CB  1 
ATOM   3898 C  CG  . GLU A 1 487  ? 44.409 78.073  -4.317  1.00 12.04 ? 487  GLU A CG  1 
ATOM   3899 C  CD  . GLU A 1 487  ? 43.548 79.186  -4.820  1.00 15.04 ? 487  GLU A CD  1 
ATOM   3900 O  OE1 . GLU A 1 487  ? 42.395 79.362  -4.406  1.00 16.58 ? 487  GLU A OE1 1 
ATOM   3901 O  OE2 . GLU A 1 487  ? 44.090 79.907  -5.691  1.00 19.56 ? 487  GLU A OE2 1 
ATOM   3902 N  N   . GLN A 1 488  ? 46.565 77.392  -1.279  1.00 9.43  ? 488  GLN A N   1 
ATOM   3903 C  CA  . GLN A 1 488  ? 47.951 77.838  -1.027  1.00 10.31 ? 488  GLN A CA  1 
ATOM   3904 C  C   . GLN A 1 488  ? 48.875 76.655  -0.946  1.00 9.13  ? 488  GLN A C   1 
ATOM   3905 O  O   . GLN A 1 488  ? 49.998 76.683  -1.509  1.00 9.33  ? 488  GLN A O   1 
ATOM   3906 C  CB  . GLN A 1 488  ? 48.022 78.578  0.331   1.00 13.32 ? 488  GLN A CB  1 
ATOM   3907 C  CG  . GLN A 1 488  ? 47.349 79.907  0.244   1.00 18.57 ? 488  GLN A CG  1 
ATOM   3908 C  CD  . GLN A 1 488  ? 47.356 80.639  1.580   1.00 21.84 ? 488  GLN A CD  1 
ATOM   3909 O  OE1 . GLN A 1 488  ? 47.095 81.824  1.615   1.00 25.95 ? 488  GLN A OE1 1 
ATOM   3910 N  NE2 . GLN A 1 488  ? 47.628 79.930  2.680   1.00 22.99 ? 488  GLN A NE2 1 
ATOM   3911 N  N   . ARG A 1 489  ? 48.484 75.583  -0.254  1.00 8.52  ? 489  ARG A N   1 
ATOM   3912 C  CA  . ARG A 1 489  ? 49.303 74.384  -0.169  1.00 8.22  ? 489  ARG A CA  1 
ATOM   3913 C  C   . ARG A 1 489  ? 49.517 73.793  -1.561  1.00 8.25  ? 489  ARG A C   1 
ATOM   3914 O  O   . ARG A 1 489  ? 50.636 73.384  -1.900  1.00 8.10  ? 489  ARG A O   1 
ATOM   3915 C  CB  . ARG A 1 489  ? 48.624 73.372  0.765   1.00 8.20  ? 489  ARG A CB  1 
ATOM   3916 C  CG  . ARG A 1 489  ? 48.674 73.763  2.184   1.00 9.13  ? 489  ARG A CG  1 
ATOM   3917 C  CD  . ARG A 1 489  ? 47.730 72.790  2.953   1.00 10.49 ? 489  ARG A CD  1 
ATOM   3918 N  NE  . ARG A 1 489  ? 47.828 72.935  4.431   1.00 9.66  ? 489  ARG A NE  1 
ATOM   3919 C  CZ  . ARG A 1 489  ? 48.666 72.285  5.220   1.00 10.74 ? 489  ARG A CZ  1 
ATOM   3920 N  NH1 . ARG A 1 489  ? 49.516 71.399  4.734   1.00 12.09 ? 489  ARG A NH1 1 
ATOM   3921 N  NH2 . ARG A 1 489  ? 48.663 72.554  6.540   1.00 12.52 ? 489  ARG A NH2 1 
ATOM   3922 N  N   . MET A 1 490  ? 48.469 73.754  -2.389  1.00 7.38  ? 490  MET A N   1 
ATOM   3923 C  CA  . MET A 1 490  ? 48.650 73.189  -3.727  1.00 7.45  ? 490  MET A CA  1 
ATOM   3924 C  C   . MET A 1 490  ? 49.516 74.067  -4.606  1.00 7.54  ? 490  MET A C   1 
ATOM   3925 O  O   . MET A 1 490  ? 50.195 73.532  -5.472  1.00 7.94  ? 490  MET A O   1 
ATOM   3926 C  CB  . MET A 1 490  ? 47.308 72.912  -4.433  1.00 7.77  ? 490  MET A CB  1 
ATOM   3927 C  CG  . MET A 1 490  ? 46.578 71.677  -3.784  1.00 9.12  ? 490  MET A CG  1 
ATOM   3928 S  SD  . MET A 1 490  ? 45.228 70.986  -4.831  1.00 10.47 ? 490  MET A SD  1 
ATOM   3929 C  CE  . MET A 1 490  ? 43.950 72.222  -4.474  1.00 12.09 ? 490  MET A CE  1 
ATOM   3930 N  N   . GLN A 1 491  ? 49.445 75.390  -4.412  1.00 8.13  ? 491  GLN A N   1 
ATOM   3931 C  CA  . GLN A 1 491  ? 50.314 76.283  -5.191  1.00 9.60  ? 491  GLN A CA  1 
ATOM   3932 C  C   . GLN A 1 491  ? 51.763 76.026  -4.838  1.00 9.66  ? 491  GLN A C   1 
ATOM   3933 O  O   . GLN A 1 491  ? 52.632 75.964  -5.737  1.00 10.48 ? 491  GLN A O   1 
ATOM   3934 C  CB  . GLN A 1 491  ? 49.981 77.753  -4.919  1.00 11.02 ? 491  GLN A CB  1 
ATOM   3935 C  CG  . GLN A 1 491  ? 50.832 78.611  -5.848  1.00 17.72 ? 491  GLN A CG  1 
ATOM   3936 C  CD  . GLN A 1 491  ? 50.680 78.199  -7.306  1.00 21.61 ? 491  GLN A CD  1 
ATOM   3937 O  OE1 . GLN A 1 491  ? 51.671 78.014  -8.041  1.00 24.71 ? 491  GLN A OE1 1 
ATOM   3938 N  NE2 . GLN A 1 491  ? 49.452 78.036  -7.723  1.00 23.17 ? 491  GLN A NE2 1 
ATOM   3939 N  N   . GLU A 1 492  ? 52.051 75.818  -3.558  1.00 9.75  ? 492  GLU A N   1 
ATOM   3940 C  CA  . GLU A 1 492  ? 53.423 75.503  -3.155  1.00 10.51 ? 492  GLU A CA  1 
ATOM   3941 C  C   . GLU A 1 492  ? 53.826 74.161  -3.752  1.00 9.82  ? 492  GLU A C   1 
ATOM   3942 O  O   . GLU A 1 492  ? 54.969 73.998  -4.248  1.00 10.19 ? 492  GLU A O   1 
ATOM   3943 C  CB  . GLU A 1 492  ? 53.546 75.490  -1.630  1.00 12.86 ? 492  GLU A CB  1 
ATOM   3944 C  CG  . GLU A 1 492  ? 53.500 76.877  -1.009  1.00 20.08 ? 492  GLU A CG  1 
ATOM   3945 C  CD  . GLU A 1 492  ? 54.398 77.859  -1.743  1.00 23.63 ? 492  GLU A CD  1 
ATOM   3946 O  OE1 . GLU A 1 492  ? 55.620 77.565  -1.886  1.00 28.07 ? 492  GLU A OE1 1 
ATOM   3947 O  OE2 . GLU A 1 492  ? 53.881 78.908  -2.199  1.00 27.84 ? 492  GLU A OE2 1 
ATOM   3948 N  N   . ALA A 1 493  ? 52.912 73.187  -3.788  1.00 9.05  ? 493  ALA A N   1 
ATOM   3949 C  CA  . ALA A 1 493  ? 53.245 71.889  -4.375  1.00 7.21  ? 493  ALA A CA  1 
ATOM   3950 C  C   . ALA A 1 493  ? 53.538 72.030  -5.887  1.00 8.00  ? 493  ALA A C   1 
ATOM   3951 O  O   . ALA A 1 493  ? 54.422 71.318  -6.392  1.00 7.05  ? 493  ALA A O   1 
ATOM   3952 C  CB  . ALA A 1 493  ? 52.077 70.902  -4.171  1.00 8.23  ? 493  ALA A CB  1 
ATOM   3953 N  N   . LEU A 1 494  ? 52.756 72.850  -6.614  1.00 7.41  ? 494  LEU A N   1 
ATOM   3954 C  CA  . LEU A 1 494  ? 53.034 73.041  -8.045  1.00 7.66  ? 494  LEU A CA  1 
ATOM   3955 C  C   . LEU A 1 494  ? 54.437 73.651  -8.228  1.00 7.67  ? 494  LEU A C   1 
ATOM   3956 O  O   . LEU A 1 494  ? 55.156 73.212  -9.145  1.00 8.37  ? 494  LEU A O   1 
ATOM   3957 C  CB  . LEU A 1 494  ? 51.943 73.967  -8.637  1.00 8.71  ? 494  LEU A CB  1 
ATOM   3958 C  CG  . LEU A 1 494  ? 50.575 73.292  -8.892  1.00 8.73  ? 494  LEU A CG  1 
ATOM   3959 C  CD1 . LEU A 1 494  ? 49.554 74.377  -9.210  1.00 10.57 ? 494  LEU A CD1 1 
ATOM   3960 C  CD2 . LEU A 1 494  ? 50.662 72.267  -9.997  1.00 9.15  ? 494  LEU A CD2 1 
ATOM   3961 N  N   . LYS A 1 495  ? 54.820 74.613  -7.385  1.00 9.26  ? 495  LYS A N   1 
ATOM   3962 C  CA  . LYS A 1 495  ? 56.184 75.210  -7.496  1.00 9.15  ? 495  LYS A CA  1 
ATOM   3963 C  C   . LYS A 1 495  ? 57.238 74.161  -7.178  1.00 8.55  ? 495  LYS A C   1 
ATOM   3964 O  O   . LYS A 1 495  ? 58.268 74.099  -7.877  1.00 9.36  ? 495  LYS A O   1 
ATOM   3965 C  CB  . LYS A 1 495  ? 56.288 76.390  -6.571  1.00 11.42 ? 495  LYS A CB  1 
ATOM   3966 C  CG  . LYS A 1 495  ? 55.410 77.544  -7.020  1.00 16.35 ? 495  LYS A CG  1 
ATOM   3967 C  CD  . LYS A 1 495  ? 55.555 78.807  -6.150  1.00 21.55 ? 495  LYS A CD  1 
ATOM   3968 C  CE  . LYS A 1 495  ? 55.092 78.605  -4.727  1.00 24.74 ? 495  LYS A CE  1 
ATOM   3969 N  NZ  . LYS A 1 495  ? 55.197 79.908  -3.920  1.00 27.61 ? 495  LYS A NZ  1 
ATOM   3970 N  N   . ALA A 1 496  ? 57.000 73.280  -6.209  1.00 7.88  ? 496  ALA A N   1 
ATOM   3971 C  CA  . ALA A 1 496  ? 57.928 72.225  -5.921  1.00 7.82  ? 496  ALA A CA  1 
ATOM   3972 C  C   . ALA A 1 496  ? 58.104 71.285  -7.124  1.00 7.48  ? 496  ALA A C   1 
ATOM   3973 O  O   . ALA A 1 496  ? 59.216 70.856  -7.494  1.00 8.12  ? 496  ALA A O   1 
ATOM   3974 C  CB  . ALA A 1 496  ? 57.440 71.429  -4.664  1.00 8.44  ? 496  ALA A CB  1 
ATOM   3975 N  N   . CYS A 1 497  ? 56.985 70.912  -7.751  1.00 7.27  ? 497  CYS A N   1 
ATOM   3976 C  CA  . CYS A 1 497  ? 57.045 70.049  -8.939  1.00 7.73  ? 497  CYS A CA  1 
ATOM   3977 C  C   . CYS A 1 497  ? 57.804 70.723  -10.059 1.00 8.00  ? 497  CYS A C   1 
ATOM   3978 O  O   . CYS A 1 497  ? 58.627 70.084  -10.723 1.00 7.55  ? 497  CYS A O   1 
ATOM   3979 C  CB  . CYS A 1 497  ? 55.617 69.738  -9.435  1.00 7.62  ? 497  CYS A CB  1 
ATOM   3980 S  SG  . CYS A 1 497  ? 54.717 68.544  -8.347  1.00 8.20  ? 497  CYS A SG  1 
ATOM   3981 N  N   . GLN A 1 498  ? 57.512 71.988  -10.308 1.00 7.33  ? 498  GLN A N   1 
ATOM   3982 C  CA  . GLN A 1 498  ? 58.232 72.695  -11.394 1.00 8.41  ? 498  GLN A CA  1 
ATOM   3983 C  C   . GLN A 1 498  ? 59.726 72.680  -11.114 1.00 8.18  ? 498  GLN A C   1 
ATOM   3984 O  O   . GLN A 1 498  ? 60.523 72.406  -12.010 1.00 8.52  ? 498  GLN A O   1 
ATOM   3985 C  CB  . GLN A 1 498  ? 57.753 74.147  -11.504 1.00 8.01  ? 498  GLN A CB  1 
ATOM   3986 C  CG  A GLN A 1 498  ? 58.631 74.989  -12.446 0.50 9.86  ? 498  GLN A CG  1 
ATOM   3987 C  CG  B GLN A 1 498  ? 56.210 74.283  -11.881 0.50 13.57 ? 498  GLN A CG  1 
ATOM   3988 C  CD  A GLN A 1 498  ? 58.173 76.446  -12.554 0.50 10.70 ? 498  GLN A CD  1 
ATOM   3989 C  CD  B GLN A 1 498  ? 55.671 75.705  -11.787 0.50 16.00 ? 498  GLN A CD  1 
ATOM   3990 O  OE1 A GLN A 1 498  ? 58.040 77.152  -11.541 0.50 14.21 ? 498  GLN A OE1 1 
ATOM   3991 O  OE1 B GLN A 1 498  ? 56.163 76.607  -12.466 0.50 18.93 ? 498  GLN A OE1 1 
ATOM   3992 N  NE2 A GLN A 1 498  ? 57.963 76.909  -13.773 0.50 7.49  ? 498  GLN A NE2 1 
ATOM   3993 N  NE2 B GLN A 1 498  ? 54.674 75.915  -10.928 0.50 18.11 ? 498  GLN A NE2 1 
ATOM   3994 N  N   . MET A 1 499  ? 60.134 72.981  -9.883  1.00 7.86  ? 499  MET A N   1 
ATOM   3995 C  CA  . MET A 1 499  ? 61.559 72.988  -9.569  1.00 8.57  ? 499  MET A CA  1 
ATOM   3996 C  C   . MET A 1 499  ? 62.204 71.633  -9.863  1.00 8.15  ? 499  MET A C   1 
ATOM   3997 O  O   . MET A 1 499  ? 63.226 71.545  -10.545 1.00 8.70  ? 499  MET A O   1 
ATOM   3998 C  CB  . MET A 1 499  ? 61.716 73.383  -8.100  1.00 8.60  ? 499  MET A CB  1 
ATOM   3999 C  CG  . MET A 1 499  ? 63.136 73.258  -7.571  1.00 10.62 ? 499  MET A CG  1 
ATOM   4000 S  SD  . MET A 1 499  ? 64.457 74.197  -8.381  1.00 14.38 ? 499  MET A SD  1 
ATOM   4001 C  CE  . MET A 1 499  ? 63.964 75.857  -7.931  1.00 16.40 ? 499  MET A CE  1 
ATOM   4002 N  N   . VAL A 1 500  ? 61.568 70.546  -9.418  1.00 7.56  ? 500  VAL A N   1 
ATOM   4003 C  CA  . VAL A 1 500  ? 62.125 69.220  -9.645  1.00 7.44  ? 500  VAL A CA  1 
ATOM   4004 C  C   . VAL A 1 500  ? 62.141 68.907  -11.129 1.00 7.29  ? 500  VAL A C   1 
ATOM   4005 O  O   . VAL A 1 500  ? 63.144 68.374  -11.638 1.00 7.99  ? 500  VAL A O   1 
ATOM   4006 C  CB  . VAL A 1 500  ? 61.330 68.159  -8.832  1.00 7.82  ? 500  VAL A CB  1 
ATOM   4007 C  CG1 . VAL A 1 500  ? 61.729 66.773  -9.233  1.00 8.95  ? 500  VAL A CG1 1 
ATOM   4008 C  CG2 . VAL A 1 500  ? 61.605 68.424  -7.304  1.00 9.40  ? 500  VAL A CG2 1 
ATOM   4009 N  N   . MET A 1 501  ? 61.030 69.181  -11.815 1.00 7.05  ? 501  MET A N   1 
ATOM   4010 C  CA  . MET A 1 501  ? 60.975 68.911  -13.238 1.00 7.38  ? 501  MET A CA  1 
ATOM   4011 C  C   . MET A 1 501  ? 62.059 69.630  -14.007 1.00 6.69  ? 501  MET A C   1 
ATOM   4012 O  O   . MET A 1 501  ? 62.738 68.977  -14.851 1.00 7.88  ? 501  MET A O   1 
ATOM   4013 C  CB  . MET A 1 501  ? 59.600 69.289  -13.817 1.00 7.82  ? 501  MET A CB  1 
ATOM   4014 C  CG  . MET A 1 501  ? 58.483 68.292  -13.355 1.00 7.98  ? 501  MET A CG  1 
ATOM   4015 S  SD  . MET A 1 501  ? 56.822 68.999  -13.596 1.00 11.94 ? 501  MET A SD  1 
ATOM   4016 C  CE  . MET A 1 501  ? 56.695 68.787  -15.347 1.00 12.66 ? 501  MET A CE  1 
ATOM   4017 N  N   . GLN A 1 502  ? 62.219 70.931  -13.777 1.00 7.94  ? 502  GLN A N   1 
ATOM   4018 C  CA  . GLN A 1 502  ? 63.187 71.666  -14.618 1.00 7.60  ? 502  GLN A CA  1 
ATOM   4019 C  C   . GLN A 1 502  ? 64.624 71.285  -14.286 1.00 8.48  ? 502  GLN A C   1 
ATOM   4020 O  O   . GLN A 1 502  ? 65.450 71.206  -15.209 1.00 8.89  ? 502  GLN A O   1 
ATOM   4021 C  CB  . GLN A 1 502  ? 62.913 73.149  -14.522 1.00 8.43  ? 502  GLN A CB  1 
ATOM   4022 C  CG  . GLN A 1 502  ? 63.105 73.763  -13.138 1.00 9.36  ? 502  GLN A CG  1 
ATOM   4023 C  CD  . GLN A 1 502  ? 64.527 74.299  -12.928 1.00 10.49 ? 502  GLN A CD  1 
ATOM   4024 O  OE1 . GLN A 1 502  ? 65.286 74.462  -13.897 1.00 11.62 ? 502  GLN A OE1 1 
ATOM   4025 N  NE2 . GLN A 1 502  ? 64.876 74.632  -11.691 1.00 11.47 ? 502  GLN A NE2 1 
ATOM   4026 N  N   . GLN A 1 503  ? 64.909 71.004  -13.026 1.00 7.88  ? 503  GLN A N   1 
ATOM   4027 C  CA  . GLN A 1 503  ? 66.290 70.509  -12.727 1.00 8.30  ? 503  GLN A CA  1 
ATOM   4028 C  C   . GLN A 1 503  ? 66.500 69.171  -13.431 1.00 8.87  ? 503  GLN A C   1 
ATOM   4029 O  O   . GLN A 1 503  ? 67.614 68.869  -13.945 1.00 8.68  ? 503  GLN A O   1 
ATOM   4030 C  CB  . GLN A 1 503  ? 66.508 70.258  -11.226 1.00 9.65  ? 503  GLN A CB  1 
ATOM   4031 C  CG  . GLN A 1 503  ? 66.614 71.532  -10.388 1.00 10.44 ? 503  GLN A CG  1 
ATOM   4032 C  CD  . GLN A 1 503  ? 67.963 72.255  -10.545 1.00 11.46 ? 503  GLN A CD  1 
ATOM   4033 O  OE1 . GLN A 1 503  ? 68.958 71.605  -10.838 1.00 14.40 ? 503  GLN A OE1 1 
ATOM   4034 N  NE2 . GLN A 1 503  ? 67.993 73.570  -10.312 1.00 13.06 ? 503  GLN A NE2 1 
ATOM   4035 N  N   . SER A 1 504  ? 65.477 68.292  -13.485 1.00 7.68  ? 504  SER A N   1 
ATOM   4036 C  CA  . SER A 1 504  ? 65.618 66.993  -14.133 1.00 8.75  ? 504  SER A CA  1 
ATOM   4037 C  C   . SER A 1 504  ? 65.861 67.149  -15.637 1.00 8.79  ? 504  SER A C   1 
ATOM   4038 O  O   . SER A 1 504  ? 66.733 66.474  -16.214 1.00 8.82  ? 504  SER A O   1 
ATOM   4039 C  CB  . SER A 1 504  ? 64.346 66.138  -13.900 1.00 8.46  ? 504  SER A CB  1 
ATOM   4040 O  OG  . SER A 1 504  ? 64.256 65.852  -12.488 1.00 9.71  ? 504  SER A OG  1 
ATOM   4041 N  N   . VAL A 1 505  ? 65.090 68.029  -16.280 1.00 8.25  ? 505  VAL A N   1 
ATOM   4042 C  CA  . VAL A 1 505  ? 65.256 68.231  -17.732 1.00 8.46  ? 505  VAL A CA  1 
ATOM   4043 C  C   . VAL A 1 505  ? 66.699 68.762  -18.038 1.00 8.40  ? 505  VAL A C   1 
ATOM   4044 O  O   . VAL A 1 505  ? 67.372 68.279  -18.974 1.00 10.08 ? 505  VAL A O   1 
ATOM   4045 C  CB  . VAL A 1 505  ? 64.183 69.236  -18.238 1.00 8.95  ? 505  VAL A CB  1 
ATOM   4046 C  CG1 . VAL A 1 505  ? 64.511 69.712  -19.674 1.00 10.21 ? 505  VAL A CG1 1 
ATOM   4047 C  CG2 . VAL A 1 505  ? 62.771 68.576  -18.201 1.00 10.62 ? 505  VAL A CG2 1 
ATOM   4048 N  N   . TYR A 1 506  ? 67.199 69.654  -17.203 1.00 8.70  ? 506  TYR A N   1 
ATOM   4049 C  CA  . TYR A 1 506  ? 68.532 70.197  -17.456 1.00 9.48  ? 506  TYR A CA  1 
ATOM   4050 C  C   . TYR A 1 506  ? 69.560 69.069  -17.361 1.00 10.13 ? 506  TYR A C   1 
ATOM   4051 O  O   . TYR A 1 506  ? 70.477 68.949  -18.186 1.00 10.93 ? 506  TYR A O   1 
ATOM   4052 C  CB  . TYR A 1 506  ? 68.830 71.317  -16.458 1.00 10.60 ? 506  TYR A CB  1 
ATOM   4053 C  CG  . TYR A 1 506  ? 70.113 72.023  -16.721 1.00 13.58 ? 506  TYR A CG  1 
ATOM   4054 C  CD1 . TYR A 1 506  ? 70.275 72.673  -17.960 1.00 15.37 ? 506  TYR A CD1 1 
ATOM   4055 C  CD2 . TYR A 1 506  ? 71.128 72.018  -15.795 1.00 13.82 ? 506  TYR A CD2 1 
ATOM   4056 C  CE1 . TYR A 1 506  ? 71.424 73.312  -18.278 1.00 17.59 ? 506  TYR A CE1 1 
ATOM   4057 C  CE2 . TYR A 1 506  ? 72.383 72.673  -16.125 1.00 16.96 ? 506  TYR A CE2 1 
ATOM   4058 C  CZ  . TYR A 1 506  ? 72.460 73.308  -17.386 1.00 16.15 ? 506  TYR A CZ  1 
ATOM   4059 O  OH  . TYR A 1 506  ? 73.548 74.069  -17.793 1.00 18.21 ? 506  TYR A OH  1 
ATOM   4060 N  N   . ARG A 1 507  ? 69.401 68.200  -16.372 1.00 9.39  ? 507  ARG A N   1 
ATOM   4061 C  CA  . ARG A 1 507  ? 70.335 67.089  -16.231 1.00 9.22  ? 507  ARG A CA  1 
ATOM   4062 C  C   . ARG A 1 507  ? 70.215 66.058  -17.351 1.00 10.44 ? 507  ARG A C   1 
ATOM   4063 O  O   . ARG A 1 507  ? 71.210 65.524  -17.862 1.00 10.40 ? 507  ARG A O   1 
ATOM   4064 C  CB  . ARG A 1 507  ? 70.116 66.442  -14.882 1.00 10.19 ? 507  ARG A CB  1 
ATOM   4065 C  CG  . ARG A 1 507  ? 71.209 65.382  -14.568 1.00 11.30 ? 507  ARG A CG  1 
ATOM   4066 C  CD  . ARG A 1 507  ? 71.063 64.932  -13.093 1.00 12.98 ? 507  ARG A CD  1 
ATOM   4067 N  NE  . ARG A 1 507  ? 72.115 63.958  -12.702 1.00 15.08 ? 507  ARG A NE  1 
ATOM   4068 C  CZ  . ARG A 1 507  ? 72.135 63.353  -11.506 1.00 14.54 ? 507  ARG A CZ  1 
ATOM   4069 N  NH1 . ARG A 1 507  ? 71.214 63.620  -10.591 1.00 15.71 ? 507  ARG A NH1 1 
ATOM   4070 N  NH2 . ARG A 1 507  ? 73.031 62.405  -11.260 1.00 17.41 ? 507  ARG A NH2 1 
ATOM   4071 N  N   . LEU A 1 508  ? 68.990 65.752  -17.764 1.00 8.82  ? 508  LEU A N   1 
ATOM   4072 C  CA  . LEU A 1 508  ? 68.796 64.770  -18.782 1.00 8.65  ? 508  LEU A CA  1 
ATOM   4073 C  C   . LEU A 1 508  ? 69.225 65.181  -20.194 1.00 9.52  ? 508  LEU A C   1 
ATOM   4074 O  O   . LEU A 1 508  ? 69.429 64.307  -21.068 1.00 11.14 ? 508  LEU A O   1 
ATOM   4075 C  CB  . LEU A 1 508  ? 67.305 64.367  -18.846 1.00 8.71  ? 508  LEU A CB  1 
ATOM   4076 C  CG  . LEU A 1 508  ? 66.852 63.561  -17.615 1.00 9.06  ? 508  LEU A CG  1 
ATOM   4077 C  CD1 . LEU A 1 508  ? 65.290 63.632  -17.543 1.00 10.43 ? 508  LEU A CD1 1 
ATOM   4078 C  CD2 . LEU A 1 508  ? 67.312 62.115  -17.750 1.00 11.88 ? 508  LEU A CD2 1 
ATOM   4079 N  N   . LEU A 1 509  ? 69.271 66.498  -20.429 1.00 9.86  ? 509  LEU A N   1 
ATOM   4080 C  CA  . LEU A 1 509  ? 69.562 67.004  -21.779 1.00 10.01 ? 509  LEU A CA  1 
ATOM   4081 C  C   . LEU A 1 509  ? 70.835 67.843  -21.859 1.00 11.05 ? 509  LEU A C   1 
ATOM   4082 O  O   . LEU A 1 509  ? 70.979 68.617  -22.799 1.00 12.23 ? 509  LEU A O   1 
ATOM   4083 C  CB  . LEU A 1 509  ? 68.334 67.790  -22.298 1.00 9.49  ? 509  LEU A CB  1 
ATOM   4084 C  CG  . LEU A 1 509  ? 67.135 66.895  -22.636 1.00 9.75  ? 509  LEU A CG  1 
ATOM   4085 C  CD1 . LEU A 1 509  ? 66.021 67.873  -23.063 1.00 9.64  ? 509  LEU A CD1 1 
ATOM   4086 C  CD2 . LEU A 1 509  ? 67.389 65.881  -23.753 1.00 11.04 ? 509  LEU A CD2 1 
ATOM   4087 N  N   . THR A 1 510  ? 71.748 67.726  -20.902 1.00 10.21 ? 510  THR A N   1 
ATOM   4088 C  CA  . THR A 1 510  ? 73.005 68.476  -20.985 1.00 11.42 ? 510  THR A CA  1 
ATOM   4089 C  C   . THR A 1 510  ? 74.155 67.468  -21.015 1.00 12.00 ? 510  THR A C   1 
ATOM   4090 O  O   . THR A 1 510  ? 74.149 66.491  -20.271 1.00 11.59 ? 510  THR A O   1 
ATOM   4091 C  CB  . THR A 1 510  ? 73.155 69.408  -19.800 1.00 9.89  ? 510  THR A CB  1 
ATOM   4092 O  OG1 . THR A 1 510  ? 72.054 70.343  -19.832 1.00 11.56 ? 510  THR A OG1 1 
ATOM   4093 C  CG2 . THR A 1 510  ? 74.474 70.263  -19.862 1.00 10.94 ? 510  THR A CG2 1 
ATOM   4094 N  N   . LYS A 1 511  ? 75.119 67.716  -21.907 1.00 13.37 ? 511  LYS A N   1 
ATOM   4095 C  CA  . LYS A 1 511  ? 76.280 66.831  -21.988 1.00 14.08 ? 511  LYS A CA  1 
ATOM   4096 C  C   . LYS A 1 511  ? 76.796 66.639  -20.583 1.00 13.54 ? 511  LYS A C   1 
ATOM   4097 O  O   . LYS A 1 511  ? 77.076 67.578  -19.829 1.00 12.73 ? 511  LYS A O   1 
ATOM   4098 C  CB  . LYS A 1 511  ? 77.336 67.504  -22.852 1.00 15.71 ? 511  LYS A CB  1 
ATOM   4099 C  CG  . LYS A 1 511  ? 78.542 66.618  -22.988 1.00 19.93 ? 511  LYS A CG  1 
ATOM   4100 C  CD  . LYS A 1 511  ? 79.512 67.131  -24.016 1.00 23.86 ? 511  LYS A CD  1 
ATOM   4101 C  CE  . LYS A 1 511  ? 80.601 66.072  -24.195 1.00 26.22 ? 511  LYS A CE  1 
ATOM   4102 N  NZ  . LYS A 1 511  ? 81.629 66.477  -25.186 1.00 29.38 ? 511  LYS A NZ  1 
ATOM   4103 N  N   . PRO A 1 512  ? 77.012 65.381  -20.195 1.00 15.22 ? 512  PRO A N   1 
ATOM   4104 C  CA  . PRO A 1 512  ? 77.476 65.114  -18.847 1.00 15.79 ? 512  PRO A CA  1 
ATOM   4105 C  C   . PRO A 1 512  ? 78.717 65.838  -18.323 1.00 15.01 ? 512  PRO A C   1 
ATOM   4106 O  O   . PRO A 1 512  ? 78.748 66.305  -17.175 1.00 15.13 ? 512  PRO A O   1 
ATOM   4107 C  CB  . PRO A 1 512  ? 77.652 63.589  -18.844 1.00 17.86 ? 512  PRO A CB  1 
ATOM   4108 C  CG  . PRO A 1 512  ? 76.659 63.139  -19.834 1.00 18.86 ? 512  PRO A CG  1 
ATOM   4109 C  CD  . PRO A 1 512  ? 76.737 64.137  -20.940 1.00 16.99 ? 512  PRO A CD  1 
ATOM   4110 N  N   . SER A 1 513  ? 79.729 65.959  -19.177 1.00 14.60 ? 513  SER A N   1 
ATOM   4111 C  CA  . SER A 1 513  ? 80.936 66.616  -18.689 1.00 14.92 ? 513  SER A CA  1 
ATOM   4112 C  C   . SER A 1 513  ? 80.842 68.125  -18.645 1.00 14.28 ? 513  SER A C   1 
ATOM   4113 O  O   . SER A 1 513  ? 81.798 68.803  -18.220 1.00 15.20 ? 513  SER A O   1 
ATOM   4114 C  CB  . SER A 1 513  ? 82.106 66.218  -19.553 1.00 15.65 ? 513  SER A CB  1 
ATOM   4115 O  OG  . SER A 1 513  ? 81.869 66.552  -20.882 1.00 16.19 ? 513  SER A OG  1 
ATOM   4116 N  N   . ILE A 1 514  ? 79.693 68.679  -19.031 1.00 14.35 ? 514  ILE A N   1 
ATOM   4117 C  CA  . ILE A 1 514  ? 79.459 70.121  -19.011 1.00 15.10 ? 514  ILE A CA  1 
ATOM   4118 C  C   . ILE A 1 514  ? 78.451 70.463  -17.882 1.00 13.71 ? 514  ILE A C   1 
ATOM   4119 O  O   . ILE A 1 514  ? 78.463 71.550  -17.315 1.00 13.18 ? 514  ILE A O   1 
ATOM   4120 C  CB  . ILE A 1 514  ? 78.841 70.594  -20.398 1.00 16.69 ? 514  ILE A CB  1 
ATOM   4121 C  CG1 . ILE A 1 514  ? 79.913 70.508  -21.493 1.00 18.06 ? 514  ILE A CG1 1 
ATOM   4122 C  CG2 . ILE A 1 514  ? 78.180 71.993  -20.256 1.00 17.28 ? 514  ILE A CG2 1 
ATOM   4123 C  CD1 . ILE A 1 514  ? 79.434 70.841  -22.838 1.00 20.60 ? 514  ILE A CD1 1 
ATOM   4124 N  N   . TYR A 1 515  ? 77.590 69.496  -17.547 1.00 13.71 ? 515  TYR A N   1 
ATOM   4125 C  CA  . TYR A 1 515  ? 76.531 69.728  -16.547 1.00 12.72 ? 515  TYR A CA  1 
ATOM   4126 C  C   . TYR A 1 515  ? 77.080 70.300  -15.250 1.00 12.41 ? 515  TYR A C   1 
ATOM   4127 O  O   . TYR A 1 515  ? 77.947 69.659  -14.612 1.00 12.79 ? 515  TYR A O   1 
ATOM   4128 C  CB  . TYR A 1 515  ? 75.796 68.388  -16.361 1.00 12.79 ? 515  TYR A CB  1 
ATOM   4129 C  CG  . TYR A 1 515  ? 74.784 68.401  -15.271 1.00 11.92 ? 515  TYR A CG  1 
ATOM   4130 C  CD1 . TYR A 1 515  ? 73.612 69.155  -15.372 1.00 11.39 ? 515  TYR A CD1 1 
ATOM   4131 C  CD2 . TYR A 1 515  ? 74.976 67.586  -14.168 1.00 12.50 ? 515  TYR A CD2 1 
ATOM   4132 C  CE1 . TYR A 1 515  ? 72.639 69.076  -14.379 1.00 11.64 ? 515  TYR A CE1 1 
ATOM   4133 C  CE2 . TYR A 1 515  ? 74.013 67.491  -13.171 1.00 11.93 ? 515  TYR A CE2 1 
ATOM   4134 C  CZ  . TYR A 1 515  ? 72.844 68.241  -13.289 1.00 12.28 ? 515  TYR A CZ  1 
ATOM   4135 O  OH  . TYR A 1 515  ? 71.906 68.126  -12.313 1.00 12.68 ? 515  TYR A OH  1 
ATOM   4136 N  N   . SER A 1 516  ? 76.606 71.474  -14.807 1.00 12.91 ? 516  SER A N   1 
ATOM   4137 C  CA  . SER A 1 516  ? 77.140 72.126  -13.577 1.00 13.06 ? 516  SER A CA  1 
ATOM   4138 C  C   . SER A 1 516  ? 75.949 72.777  -12.880 1.00 13.52 ? 516  SER A C   1 
ATOM   4139 O  O   . SER A 1 516  ? 75.752 73.997  -12.923 1.00 14.47 ? 516  SER A O   1 
ATOM   4140 C  CB  . SER A 1 516  ? 78.144 73.192  -14.042 1.00 14.90 ? 516  SER A CB  1 
ATOM   4141 O  OG  . SER A 1 516  ? 78.860 73.657  -12.909 1.00 17.85 ? 516  SER A OG  1 
ATOM   4142 N  N   . PRO A 1 517  ? 75.177 71.953  -12.196 1.00 14.23 ? 517  PRO A N   1 
ATOM   4143 C  CA  . PRO A 1 517  ? 73.999 72.517  -11.566 1.00 14.98 ? 517  PRO A CA  1 
ATOM   4144 C  C   . PRO A 1 517  ? 74.058 73.376  -10.358 1.00 14.52 ? 517  PRO A C   1 
ATOM   4145 O  O   . PRO A 1 517  ? 74.832 73.115  -9.445  1.00 18.28 ? 517  PRO A O   1 
ATOM   4146 C  CB  . PRO A 1 517  ? 73.148 71.259  -11.314 1.00 15.70 ? 517  PRO A CB  1 
ATOM   4147 C  CG  . PRO A 1 517  ? 74.228 70.254  -10.912 1.00 14.69 ? 517  PRO A CG  1 
ATOM   4148 C  CD  . PRO A 1 517  ? 75.279 70.499  -12.004 1.00 14.84 ? 517  PRO A CD  1 
ATOM   4149 N  N   . ASP A 1 518  ? 73.215 74.399  -10.339 1.00 15.31 ? 518  ASP A N   1 
ATOM   4150 C  CA  . ASP A 1 518  ? 73.005 75.218  -9.141  1.00 15.28 ? 518  ASP A CA  1 
ATOM   4151 C  C   . ASP A 1 518  ? 71.568 74.730  -8.813  1.00 14.27 ? 518  ASP A C   1 
ATOM   4152 O  O   . ASP A 1 518  ? 70.630 75.002  -9.568  1.00 14.60 ? 518  ASP A O   1 
ATOM   4153 C  CB  . ASP A 1 518  ? 72.985 76.699  -9.493  1.00 17.40 ? 518  ASP A CB  1 
ATOM   4154 C  CG  . ASP A 1 518  ? 72.463 77.566  -8.366  1.00 18.74 ? 518  ASP A CG  1 
ATOM   4155 O  OD1 . ASP A 1 518  ? 71.884 77.046  -7.370  1.00 18.11 ? 518  ASP A OD1 1 
ATOM   4156 O  OD2 . ASP A 1 518  ? 72.614 78.799  -8.520  1.00 21.59 ? 518  ASP A OD2 1 
ATOM   4157 N  N   . PHE A 1 519  ? 71.432 74.019  -7.701  1.00 14.29 ? 519  PHE A N   1 
ATOM   4158 C  CA  . PHE A 1 519  ? 70.144 73.415  -7.371  1.00 14.29 ? 519  PHE A CA  1 
ATOM   4159 C  C   . PHE A 1 519  ? 69.070 74.389  -6.970  1.00 15.30 ? 519  PHE A C   1 
ATOM   4160 O  O   . PHE A 1 519  ? 67.910 73.985  -6.820  1.00 16.77 ? 519  PHE A O   1 
ATOM   4161 C  CB  . PHE A 1 519  ? 70.343 72.334  -6.327  1.00 13.86 ? 519  PHE A CB  1 
ATOM   4162 C  CG  . PHE A 1 519  ? 71.225 71.196  -6.796  1.00 15.08 ? 519  PHE A CG  1 
ATOM   4163 C  CD1 . PHE A 1 519  ? 70.944 70.481  -7.983  1.00 14.56 ? 519  PHE A CD1 1 
ATOM   4164 C  CD2 . PHE A 1 519  ? 72.316 70.808  -6.023  1.00 15.78 ? 519  PHE A CD2 1 
ATOM   4165 C  CE1 . PHE A 1 519  ? 71.727 69.402  -8.395  1.00 14.27 ? 519  PHE A CE1 1 
ATOM   4166 C  CE2 . PHE A 1 519  ? 73.104 69.733  -6.423  1.00 15.53 ? 519  PHE A CE2 1 
ATOM   4167 C  CZ  . PHE A 1 519  ? 72.817 69.017  -7.616  1.00 15.43 ? 519  PHE A CZ  1 
ATOM   4168 N  N   . SER A 1 520  ? 69.392 75.666  -6.838  1.00 15.20 ? 520  SER A N   1 
ATOM   4169 C  CA  . SER A 1 520  ? 68.380 76.666  -6.504  1.00 16.17 ? 520  SER A CA  1 
ATOM   4170 C  C   . SER A 1 520  ? 68.012 77.479  -7.775  1.00 15.65 ? 520  SER A C   1 
ATOM   4171 O  O   . SER A 1 520  ? 67.106 78.328  -7.733  1.00 16.89 ? 520  SER A O   1 
ATOM   4172 C  CB  . SER A 1 520  ? 68.943 77.643  -5.457  1.00 17.99 ? 520  SER A CB  1 
ATOM   4173 O  OG  . SER A 1 520  ? 69.932 78.486  -6.047  1.00 21.25 ? 520  SER A OG  1 
ATOM   4174 N  N   . PHE A 1 521  ? 68.682 77.185  -8.910  1.00 14.23 ? 521  PHE A N   1 
ATOM   4175 C  CA  . PHE A 1 521  ? 68.472 77.984  -10.109 1.00 14.46 ? 521  PHE A CA  1 
ATOM   4176 C  C   . PHE A 1 521  ? 67.362 77.472  -11.019 1.00 13.45 ? 521  PHE A C   1 
ATOM   4177 O  O   . PHE A 1 521  ? 67.161 76.273  -11.086 1.00 13.74 ? 521  PHE A O   1 
ATOM   4178 C  CB  . PHE A 1 521  ? 69.810 78.017  -10.891 1.00 15.06 ? 521  PHE A CB  1 
ATOM   4179 C  CG  . PHE A 1 521  ? 69.814 78.981  -12.069 1.00 16.70 ? 521  PHE A CG  1 
ATOM   4180 C  CD1 . PHE A 1 521  ? 69.924 80.350  -11.834 1.00 18.69 ? 521  PHE A CD1 1 
ATOM   4181 C  CD2 . PHE A 1 521  ? 69.668 78.524  -13.398 1.00 16.96 ? 521  PHE A CD2 1 
ATOM   4182 C  CE1 . PHE A 1 521  ? 69.885 81.252  -12.893 1.00 19.73 ? 521  PHE A CE1 1 
ATOM   4183 C  CE2 . PHE A 1 521  ? 69.628 79.426  -14.455 1.00 18.61 ? 521  PHE A CE2 1 
ATOM   4184 C  CZ  . PHE A 1 521  ? 69.736 80.786  -14.210 1.00 18.78 ? 521  PHE A CZ  1 
ATOM   4185 N  N   . SER A 1 522  ? 66.741 78.386  -11.748 1.00 14.07 ? 522  SER A N   1 
ATOM   4186 C  CA  . SER A 1 522  ? 65.686 78.035  -12.689 1.00 14.71 ? 522  SER A CA  1 
ATOM   4187 C  C   . SER A 1 522  ? 66.245 77.977  -14.103 1.00 12.92 ? 522  SER A C   1 
ATOM   4188 O  O   . SER A 1 522  ? 66.380 78.999  -14.782 1.00 14.90 ? 522  SER A O   1 
ATOM   4189 C  CB  . SER A 1 522  ? 64.538 79.050  -12.626 1.00 18.24 ? 522  SER A CB  1 
ATOM   4190 O  OG  . SER A 1 522  ? 63.688 78.633  -11.565 1.00 22.50 ? 522  SER A OG  1 
ATOM   4191 N  N   . TYR A 1 523  ? 66.611 76.788  -14.537 1.00 10.20 ? 523  TYR A N   1 
ATOM   4192 C  CA  . TYR A 1 523  ? 67.133 76.597  -15.902 1.00 9.70  ? 523  TYR A CA  1 
ATOM   4193 C  C   . TYR A 1 523  ? 66.022 76.657  -16.918 1.00 9.89  ? 523  TYR A C   1 
ATOM   4194 O  O   . TYR A 1 523  ? 66.250 77.037  -18.061 1.00 9.76  ? 523  TYR A O   1 
ATOM   4195 C  CB  . TYR A 1 523  ? 67.843 75.241  -16.021 1.00 9.69  ? 523  TYR A CB  1 
ATOM   4196 C  CG  . TYR A 1 523  ? 69.100 75.197  -15.216 1.00 11.04 ? 523  TYR A CG  1 
ATOM   4197 C  CD1 . TYR A 1 523  ? 70.268 75.784  -15.729 1.00 13.11 ? 523  TYR A CD1 1 
ATOM   4198 C  CD2 . TYR A 1 523  ? 69.134 74.634  -13.941 1.00 10.96 ? 523  TYR A CD2 1 
ATOM   4199 C  CE1 . TYR A 1 523  ? 71.420 75.812  -14.995 1.00 13.71 ? 523  TYR A CE1 1 
ATOM   4200 C  CE2 . TYR A 1 523  ? 70.295 74.675  -13.199 1.00 12.67 ? 523  TYR A CE2 1 
ATOM   4201 C  CZ  . TYR A 1 523  ? 71.413 75.275  -13.737 1.00 13.95 ? 523  TYR A CZ  1 
ATOM   4202 O  OH  . TYR A 1 523  ? 72.584 75.420  -12.961 1.00 15.60 ? 523  TYR A OH  1 
ATOM   4203 N  N   . PHE A 1 524  ? 64.815 76.245  -16.518 1.00 9.79  ? 524  PHE A N   1 
ATOM   4204 C  CA  . PHE A 1 524  ? 63.654 76.318  -17.381 1.00 8.95  ? 524  PHE A CA  1 
ATOM   4205 C  C   . PHE A 1 524  ? 62.462 76.774  -16.571 1.00 10.61 ? 524  PHE A C   1 
ATOM   4206 O  O   . PHE A 1 524  ? 62.398 76.577  -15.367 1.00 11.07 ? 524  PHE A O   1 
ATOM   4207 C  CB  . PHE A 1 524  ? 63.222 74.933  -17.928 1.00 8.97  ? 524  PHE A CB  1 
ATOM   4208 C  CG  . PHE A 1 524  ? 64.277 74.247  -18.799 1.00 8.81  ? 524  PHE A CG  1 
ATOM   4209 C  CD1 . PHE A 1 524  ? 65.279 73.492  -18.201 1.00 9.98  ? 524  PHE A CD1 1 
ATOM   4210 C  CD2 . PHE A 1 524  ? 64.274 74.374  -20.213 1.00 8.34  ? 524  PHE A CD2 1 
ATOM   4211 C  CE1 . PHE A 1 524  ? 66.242 72.900  -18.966 1.00 10.96 ? 524  PHE A CE1 1 
ATOM   4212 C  CE2 . PHE A 1 524  ? 65.239 73.784  -20.987 1.00 9.47  ? 524  PHE A CE2 1 
ATOM   4213 C  CZ  . PHE A 1 524  ? 66.239 73.038  -20.358 1.00 10.56 ? 524  PHE A CZ  1 
ATOM   4214 N  N   . THR A 1 525  ? 61.556 77.419  -17.263 1.00 10.96 ? 525  THR A N   1 
ATOM   4215 C  CA  . THR A 1 525  ? 60.266 77.680  -16.644 1.00 12.95 ? 525  THR A CA  1 
ATOM   4216 C  C   . THR A 1 525  ? 59.223 76.885  -17.387 1.00 11.83 ? 525  THR A C   1 
ATOM   4217 O  O   . THR A 1 525  ? 59.288 76.685  -18.625 1.00 12.79 ? 525  THR A O   1 
ATOM   4218 C  CB  . THR A 1 525  ? 59.861 79.097  -16.657 1.00 15.32 ? 525  THR A CB  1 
ATOM   4219 O  OG1 . THR A 1 525  ? 59.812 79.562  -17.977 1.00 17.56 ? 525  THR A OG1 1 
ATOM   4220 C  CG2 . THR A 1 525  ? 60.863 79.961  -15.904 1.00 19.01 ? 525  THR A CG2 1 
ATOM   4221 N  N   . LEU A 1 526  ? 58.270 76.383  -16.639 1.00 11.50 ? 526  LEU A N   1 
ATOM   4222 C  CA  . LEU A 1 526  ? 57.183 75.653  -17.260 1.00 12.15 ? 526  LEU A CA  1 
ATOM   4223 C  C   . LEU A 1 526  ? 56.211 76.610  -17.931 1.00 12.46 ? 526  LEU A C   1 
ATOM   4224 O  O   . LEU A 1 526  ? 55.986 77.732  -17.465 1.00 15.30 ? 526  LEU A O   1 
ATOM   4225 C  CB  . LEU A 1 526  ? 56.412 74.813  -16.211 1.00 15.48 ? 526  LEU A CB  1 
ATOM   4226 C  CG  . LEU A 1 526  ? 56.961 73.472  -15.782 1.00 16.97 ? 526  LEU A CG  1 
ATOM   4227 C  CD1 . LEU A 1 526  ? 56.120 72.934  -14.607 1.00 19.85 ? 526  LEU A CD1 1 
ATOM   4228 C  CD2 . LEU A 1 526  ? 56.884 72.502  -16.973 1.00 17.67 ? 526  LEU A CD2 1 
ATOM   4229 N  N   . ASP A 1 527  ? 55.677 76.178  -19.046 1.00 9.93  ? 527  ASP A N   1 
ATOM   4230 C  CA  . ASP A 1 527  ? 54.658 76.954  -19.756 1.00 11.03 ? 527  ASP A CA  1 
ATOM   4231 C  C   . ASP A 1 527  ? 53.418 76.090  -19.780 1.00 10.98 ? 527  ASP A C   1 
ATOM   4232 O  O   . ASP A 1 527  ? 53.464 74.988  -20.278 1.00 13.11 ? 527  ASP A O   1 
ATOM   4233 C  CB  . ASP A 1 527  ? 55.110 77.322  -21.203 1.00 11.59 ? 527  ASP A CB  1 
ATOM   4234 C  CG  . ASP A 1 527  ? 54.066 78.192  -21.920 1.00 13.58 ? 527  ASP A CG  1 
ATOM   4235 O  OD1 . ASP A 1 527  ? 53.833 79.321  -21.495 1.00 14.58 ? 527  ASP A OD1 1 
ATOM   4236 O  OD2 . ASP A 1 527  ? 53.475 77.710  -22.890 1.00 15.07 ? 527  ASP A OD2 1 
ATOM   4237 N  N   . ASP A 1 528  ? 52.317 76.569  -19.215 1.00 10.40 ? 528  ASP A N   1 
ATOM   4238 C  CA  . ASP A 1 528  ? 51.094 75.762  -19.200 1.00 10.33 ? 528  ASP A CA  1 
ATOM   4239 C  C   . ASP A 1 528  ? 49.988 76.600  -19.811 1.00 11.02 ? 528  ASP A C   1 
ATOM   4240 O  O   . ASP A 1 528  ? 49.664 77.672  -19.299 1.00 11.67 ? 528  ASP A O   1 
ATOM   4241 C  CB  . ASP A 1 528  ? 50.773 75.359  -17.759 1.00 10.74 ? 528  ASP A CB  1 
ATOM   4242 C  CG  . ASP A 1 528  ? 49.689 74.292  -17.677 1.00 12.08 ? 528  ASP A CG  1 
ATOM   4243 O  OD1 . ASP A 1 528  ? 48.662 74.386  -18.379 1.00 12.39 ? 528  ASP A OD1 1 
ATOM   4244 O  OD2 . ASP A 1 528  ? 49.899 73.322  -16.902 1.00 12.62 ? 528  ASP A OD2 1 
ATOM   4245 N  N   . SER A 1 529  ? 49.470 76.107  -20.943 1.00 12.05 ? 529  SER A N   1 
ATOM   4246 C  CA  . SER A 1 529  ? 48.385 76.776  -21.676 1.00 13.14 ? 529  SER A CA  1 
ATOM   4247 C  C   . SER A 1 529  ? 46.994 76.658  -21.103 1.00 13.75 ? 529  SER A C   1 
ATOM   4248 O  O   . SER A 1 529  ? 46.125 77.395  -21.496 1.00 15.23 ? 529  SER A O   1 
ATOM   4249 C  CB  . SER A 1 529  ? 48.258 76.218  -23.107 1.00 17.03 ? 529  SER A CB  1 
ATOM   4250 O  OG  . SER A 1 529  ? 49.469 76.382  -23.776 1.00 20.39 ? 529  SER A OG  1 
ATOM   4251 N  N   . ARG A 1 530  ? 46.803 75.759  -20.146 1.00 11.42 ? 530  ARG A N   1 
ATOM   4252 C  CA  . ARG A 1 530  ? 45.450 75.555  -19.620 1.00 11.99 ? 530  ARG A CA  1 
ATOM   4253 C  C   . ARG A 1 530  ? 45.337 75.673  -18.137 1.00 13.11 ? 530  ARG A C   1 
ATOM   4254 O  O   . ARG A 1 530  ? 44.313 75.245  -17.569 1.00 16.57 ? 530  ARG A O   1 
ATOM   4255 C  CB  . ARG A 1 530  ? 44.908 74.183  -20.064 1.00 12.39 ? 530  ARG A CB  1 
ATOM   4256 C  CG  . ARG A 1 530  ? 44.949 74.089  -21.601 1.00 14.53 ? 530  ARG A CG  1 
ATOM   4257 C  CD  . ARG A 1 530  ? 44.304 72.841  -22.182 1.00 14.93 ? 530  ARG A CD  1 
ATOM   4258 N  NE  . ARG A 1 530  ? 45.001 71.642  -21.718 1.00 13.80 ? 530  ARG A NE  1 
ATOM   4259 C  CZ  . ARG A 1 530  ? 44.796 70.454  -22.267 1.00 15.30 ? 530  ARG A CZ  1 
ATOM   4260 N  NH1 . ARG A 1 530  ? 43.932 70.314  -23.278 1.00 15.89 ? 530  ARG A NH1 1 
ATOM   4261 N  NH2 . ARG A 1 530  ? 45.433 69.415  -21.816 1.00 14.98 ? 530  ARG A NH2 1 
ATOM   4262 N  N   . TRP A 1 531  ? 46.382 76.123  -17.455 1.00 11.04 ? 531  TRP A N   1 
ATOM   4263 C  CA  . TRP A 1 531  ? 46.200 76.317  -15.996 1.00 10.70 ? 531  TRP A CA  1 
ATOM   4264 C  C   . TRP A 1 531  ? 47.150 77.444  -15.581 1.00 11.70 ? 531  TRP A C   1 
ATOM   4265 O  O   . TRP A 1 531  ? 48.345 77.348  -15.828 1.00 12.54 ? 531  TRP A O   1 
ATOM   4266 C  CB  . TRP A 1 531  ? 46.586 75.077  -15.166 1.00 11.29 ? 531  TRP A CB  1 
ATOM   4267 C  CG  . TRP A 1 531  ? 46.481 75.428  -13.717 1.00 13.43 ? 531  TRP A CG  1 
ATOM   4268 C  CD1 . TRP A 1 531  ? 47.505 75.856  -12.894 1.00 14.24 ? 531  TRP A CD1 1 
ATOM   4269 C  CD2 . TRP A 1 531  ? 45.294 75.512  -12.968 1.00 14.89 ? 531  TRP A CD2 1 
ATOM   4270 N  NE1 . TRP A 1 531  ? 46.997 76.209  -11.681 1.00 16.78 ? 531  TRP A NE1 1 
ATOM   4271 C  CE2 . TRP A 1 531  ? 45.644 76.015  -11.697 1.00 13.40 ? 531  TRP A CE2 1 
ATOM   4272 C  CE3 . TRP A 1 531  ? 43.980 75.223  -13.243 1.00 15.03 ? 531  TRP A CE3 1 
ATOM   4273 C  CZ2 . TRP A 1 531  ? 44.687 76.241  -10.676 1.00 15.40 ? 531  TRP A CZ2 1 
ATOM   4274 C  CZ3 . TRP A 1 531  ? 43.024 75.439  -12.256 1.00 15.25 ? 531  TRP A CZ3 1 
ATOM   4275 C  CH2 . TRP A 1 531  ? 43.391 75.950  -10.980 1.00 15.56 ? 531  TRP A CH2 1 
ATOM   4276 N  N   . PRO A 1 532  ? 46.656 78.485  -14.904 1.00 11.49 ? 532  PRO A N   1 
ATOM   4277 C  CA  . PRO A 1 532  ? 45.258 78.678  -14.503 1.00 13.00 ? 532  PRO A CA  1 
ATOM   4278 C  C   . PRO A 1 532  ? 44.375 78.932  -15.687 1.00 14.00 ? 532  PRO A C   1 
ATOM   4279 O  O   . PRO A 1 532  ? 43.143 78.790  -15.610 1.00 14.87 ? 532  PRO A O   1 
ATOM   4280 C  CB  . PRO A 1 532  ? 45.307 79.902  -13.559 1.00 13.00 ? 532  PRO A CB  1 
ATOM   4281 C  CG  . PRO A 1 532  ? 46.680 79.810  -12.956 1.00 14.79 ? 532  PRO A CG  1 
ATOM   4282 C  CD  . PRO A 1 532  ? 47.556 79.412  -14.176 1.00 12.80 ? 532  PRO A CD  1 
ATOM   4283 N  N   . GLY A 1 533  ? 44.994 79.304  -16.798 1.00 14.55 ? 533  GLY A N   1 
ATOM   4284 C  CA  . GLY A 1 533  ? 44.216 79.561  -17.995 1.00 17.06 ? 533  GLY A CA  1 
ATOM   4285 C  C   . GLY A 1 533  ? 44.094 80.994  -18.418 1.00 20.54 ? 533  GLY A C   1 
ATOM   4286 O  O   . GLY A 1 533  ? 44.207 81.934  -17.593 1.00 19.45 ? 533  GLY A O   1 
ATOM   4287 N  N   . SER A 1 534  ? 43.868 81.138  -19.729 1.00 23.35 ? 534  SER A N   1 
ATOM   4288 C  CA  . SER A 1 534  ? 43.695 82.446  -20.361 1.00 26.10 ? 534  SER A CA  1 
ATOM   4289 C  C   . SER A 1 534  ? 42.436 83.002  -19.770 1.00 26.35 ? 534  SER A C   1 
ATOM   4290 O  O   . SER A 1 534  ? 41.378 82.336  -19.775 1.00 27.56 ? 534  SER A O   1 
ATOM   4291 C  CB  . SER A 1 534  ? 43.503 82.341  -21.888 1.00 28.43 ? 534  SER A CB  1 
ATOM   4292 O  OG  . SER A 1 534  ? 43.431 83.641  -22.466 1.00 32.20 ? 534  SER A OG  1 
ATOM   4293 N  N   . GLY A 1 535  ? 42.527 84.227  -19.287 1.00 26.18 ? 535  GLY A N   1 
ATOM   4294 C  CA  . GLY A 1 535  ? 41.347 84.832  -18.702 1.00 25.09 ? 535  GLY A CA  1 
ATOM   4295 C  C   . GLY A 1 535  ? 41.220 84.520  -17.226 1.00 24.74 ? 535  GLY A C   1 
ATOM   4296 O  O   . GLY A 1 535  ? 40.328 85.052  -16.549 1.00 25.11 ? 535  GLY A O   1 
ATOM   4297 N  N   . VAL A 1 536  ? 42.071 83.635  -16.700 1.00 24.09 ? 536  VAL A N   1 
ATOM   4298 C  CA  . VAL A 1 536  ? 42.004 83.344  -15.272 1.00 23.92 ? 536  VAL A CA  1 
ATOM   4299 C  C   . VAL A 1 536  ? 43.172 84.088  -14.601 1.00 25.74 ? 536  VAL A C   1 
ATOM   4300 O  O   . VAL A 1 536  ? 42.975 84.850  -13.644 1.00 24.71 ? 536  VAL A O   1 
ATOM   4301 C  CB  . VAL A 1 536  ? 42.063 81.803  -14.995 1.00 22.57 ? 536  VAL A CB  1 
ATOM   4302 C  CG1 . VAL A 1 536  ? 41.936 81.507  -13.478 1.00 22.98 ? 536  VAL A CG1 1 
ATOM   4303 C  CG2 . VAL A 1 536  ? 40.864 81.105  -15.694 1.00 22.78 ? 536  VAL A CG2 1 
ATOM   4304 N  N   . GLU A 1 537  ? 44.381 83.885  -15.113 1.00 27.46 ? 537  GLU A N   1 
ATOM   4305 C  CA  . GLU A 1 537  ? 45.566 84.564  -14.577 1.00 29.77 ? 537  GLU A CA  1 
ATOM   4306 C  C   . GLU A 1 537  ? 46.493 84.835  -15.772 1.00 30.37 ? 537  GLU A C   1 
ATOM   4307 O  O   . GLU A 1 537  ? 46.705 83.938  -16.600 1.00 29.91 ? 537  GLU A O   1 
ATOM   4308 C  CB  . GLU A 1 537  ? 46.264 83.652  -13.562 1.00 31.39 ? 537  GLU A CB  1 
ATOM   4309 C  CG  . GLU A 1 537  ? 47.496 84.225  -12.882 1.00 35.05 ? 537  GLU A CG  1 
ATOM   4310 C  CD  . GLU A 1 537  ? 48.041 83.293  -11.789 1.00 37.08 ? 537  GLU A CD  1 
ATOM   4311 O  OE1 . GLU A 1 537  ? 47.318 83.052  -10.782 1.00 38.32 ? 537  GLU A OE1 1 
ATOM   4312 O  OE2 . GLU A 1 537  ? 49.183 82.787  -11.936 1.00 38.26 ? 537  GLU A OE2 1 
ATOM   4313 N  N   . ASP A 1 538  ? 47.012 86.056  -15.902 1.00 31.37 ? 538  ASP A N   1 
ATOM   4314 C  CA  . ASP A 1 538  ? 47.944 86.345  -17.022 1.00 32.72 ? 538  ASP A CA  1 
ATOM   4315 C  C   . ASP A 1 538  ? 49.274 85.900  -16.406 1.00 31.91 ? 538  ASP A C   1 
ATOM   4316 O  O   . ASP A 1 538  ? 49.970 86.685  -15.745 1.00 32.85 ? 538  ASP A O   1 
ATOM   4317 C  CB  . ASP A 1 538  ? 47.971 87.858  -17.340 1.00 35.10 ? 538  ASP A CB  1 
ATOM   4318 C  CG  . ASP A 1 538  ? 48.690 88.180  -18.669 1.00 37.32 ? 538  ASP A CG  1 
ATOM   4319 O  OD1 . ASP A 1 538  ? 49.800 87.632  -18.890 1.00 38.59 ? 538  ASP A OD1 1 
ATOM   4320 O  OD2 . ASP A 1 538  ? 48.155 88.984  -19.496 1.00 38.41 ? 538  ASP A OD2 1 
ATOM   4321 N  N   . SER A 1 539  ? 49.641 84.642  -16.579 1.00 29.92 ? 539  SER A N   1 
ATOM   4322 C  CA  . SER A 1 539  ? 50.866 84.204  -15.918 1.00 28.41 ? 539  SER A CA  1 
ATOM   4323 C  C   . SER A 1 539  ? 51.928 83.568  -16.803 1.00 26.18 ? 539  SER A C   1 
ATOM   4324 O  O   . SER A 1 539  ? 53.040 83.291  -16.335 1.00 26.47 ? 539  SER A O   1 
ATOM   4325 C  CB  . SER A 1 539  ? 50.520 83.228  -14.787 1.00 29.31 ? 539  SER A CB  1 
ATOM   4326 O  OG  . SER A 1 539  ? 50.109 81.971  -15.301 1.00 30.77 ? 539  SER A OG  1 
ATOM   4327 N  N   . ARG A 1 540  ? 51.574 83.328  -18.059 1.00 23.22 ? 540  ARG A N   1 
ATOM   4328 C  CA  . ARG A 1 540  ? 52.505 82.705  -18.992 1.00 20.85 ? 540  ARG A CA  1 
ATOM   4329 C  C   . ARG A 1 540  ? 53.589 83.676  -19.389 1.00 20.00 ? 540  ARG A C   1 
ATOM   4330 O  O   . ARG A 1 540  ? 53.331 84.849  -19.557 1.00 21.27 ? 540  ARG A O   1 
ATOM   4331 C  CB  . ARG A 1 540  ? 51.761 82.270  -20.249 1.00 20.54 ? 540  ARG A CB  1 
ATOM   4332 C  CG  . ARG A 1 540  ? 50.928 80.975  -20.010 1.00 18.10 ? 540  ARG A CG  1 
ATOM   4333 C  CD  . ARG A 1 540  ? 50.149 80.612  -21.221 1.00 16.80 ? 540  ARG A CD  1 
ATOM   4334 N  NE  . ARG A 1 540  ? 51.014 79.989  -22.210 1.00 14.76 ? 540  ARG A NE  1 
ATOM   4335 C  CZ  . ARG A 1 540  ? 50.582 79.599  -23.404 1.00 15.48 ? 540  ARG A CZ  1 
ATOM   4336 N  NH1 . ARG A 1 540  ? 49.303 79.762  -23.766 1.00 16.62 ? 540  ARG A NH1 1 
ATOM   4337 N  NH2 . ARG A 1 540  ? 51.419 79.037  -24.242 1.00 15.05 ? 540  ARG A NH2 1 
ATOM   4338 N  N   . THR A 1 541  ? 54.802 83.169  -19.564 1.00 18.76 ? 541  THR A N   1 
ATOM   4339 C  CA  . THR A 1 541  ? 55.864 84.055  -19.985 1.00 18.71 ? 541  THR A CA  1 
ATOM   4340 C  C   . THR A 1 541  ? 55.949 84.084  -21.512 1.00 16.77 ? 541  THR A C   1 
ATOM   4341 O  O   . THR A 1 541  ? 55.746 83.086  -22.195 1.00 19.79 ? 541  THR A O   1 
ATOM   4342 C  CB  . THR A 1 541  ? 57.213 83.621  -19.445 1.00 20.89 ? 541  THR A CB  1 
ATOM   4343 O  OG1 . THR A 1 541  ? 57.718 82.572  -20.248 1.00 24.29 ? 541  THR A OG1 1 
ATOM   4344 C  CG2 . THR A 1 541  ? 57.107 83.141  -18.027 1.00 20.16 ? 541  THR A CG2 1 
ATOM   4345 N  N   . THR A 1 542  ? 56.238 85.259  -22.027 1.00 14.91 ? 542  THR A N   1 
ATOM   4346 C  CA  . THR A 1 542  ? 56.426 85.441  -23.443 1.00 13.36 ? 542  THR A CA  1 
ATOM   4347 C  C   . THR A 1 542  ? 57.899 85.194  -23.744 1.00 12.16 ? 542  THR A C   1 
ATOM   4348 O  O   . THR A 1 542  ? 58.791 85.679  -23.010 1.00 13.34 ? 542  THR A O   1 
ATOM   4349 C  CB  . THR A 1 542  ? 56.063 86.884  -23.846 1.00 14.81 ? 542  THR A CB  1 
ATOM   4350 O  OG1 . THR A 1 542  ? 54.705 87.123  -23.484 1.00 16.33 ? 542  THR A OG1 1 
ATOM   4351 C  CG2 . THR A 1 542  ? 56.225 87.112  -25.355 1.00 14.36 ? 542  THR A CG2 1 
ATOM   4352 N  N   . ILE A 1 543  ? 58.148 84.434  -24.812 1.00 11.79 ? 543  ILE A N   1 
ATOM   4353 C  CA  . ILE A 1 543  ? 59.521 84.228  -25.248 1.00 11.60 ? 543  ILE A CA  1 
ATOM   4354 C  C   . ILE A 1 543  ? 59.875 85.521  -26.031 1.00 11.47 ? 543  ILE A C   1 
ATOM   4355 O  O   . ILE A 1 543  ? 59.252 85.840  -27.059 1.00 11.66 ? 543  ILE A O   1 
ATOM   4356 C  CB  . ILE A 1 543  ? 59.591 83.007  -26.124 1.00 11.43 ? 543  ILE A CB  1 
ATOM   4357 C  CG1 . ILE A 1 543  ? 59.243 81.751  -25.252 1.00 11.86 ? 543  ILE A CG1 1 
ATOM   4358 C  CG2 . ILE A 1 543  ? 60.968 82.978  -26.834 1.00 11.63 ? 543  ILE A CG2 1 
ATOM   4359 C  CD1 . ILE A 1 543  ? 59.199 80.464  -26.067 1.00 11.33 ? 543  ILE A CD1 1 
ATOM   4360 N  N   . ILE A 1 544  ? 60.835 86.271  -25.498 1.00 11.29 ? 544  ILE A N   1 
ATOM   4361 C  CA  . ILE A 1 544  ? 61.203 87.562  -26.081 1.00 11.96 ? 544  ILE A CA  1 
ATOM   4362 C  C   . ILE A 1 544  ? 62.407 87.405  -26.982 1.00 11.89 ? 544  ILE A C   1 
ATOM   4363 O  O   . ILE A 1 544  ? 63.499 87.078  -26.520 1.00 12.19 ? 544  ILE A O   1 
ATOM   4364 C  CB  . ILE A 1 544  ? 61.444 88.548  -24.944 1.00 14.26 ? 544  ILE A CB  1 
ATOM   4365 C  CG1 . ILE A 1 544  ? 60.104 88.795  -24.221 1.00 16.99 ? 544  ILE A CG1 1 
ATOM   4366 C  CG2 . ILE A 1 544  ? 61.964 89.872  -25.514 1.00 15.41 ? 544  ILE A CG2 1 
ATOM   4367 C  CD1 . ILE A 1 544  ? 60.160 89.692  -23.003 1.00 19.12 ? 544  ILE A CD1 1 
ATOM   4368 N  N   . LEU A 1 545  ? 62.170 87.617  -28.268 1.00 11.65 ? 545  LEU A N   1 
ATOM   4369 C  CA  . LEU A 1 545  ? 63.191 87.495  -29.293 1.00 11.88 ? 545  LEU A CA  1 
ATOM   4370 C  C   . LEU A 1 545  ? 63.303 88.843  -29.996 1.00 12.77 ? 545  LEU A C   1 
ATOM   4371 O  O   . LEU A 1 545  ? 62.341 89.613  -30.033 1.00 14.07 ? 545  LEU A O   1 
ATOM   4372 C  CB  . LEU A 1 545  ? 62.797 86.424  -30.317 1.00 12.04 ? 545  LEU A CB  1 
ATOM   4373 C  CG  . LEU A 1 545  ? 62.596 85.034  -29.730 1.00 11.86 ? 545  LEU A CG  1 
ATOM   4374 C  CD1 . LEU A 1 545  ? 62.126 84.103  -30.856 1.00 13.87 ? 545  LEU A CD1 1 
ATOM   4375 C  CD2 . LEU A 1 545  ? 63.895 84.490  -29.109 1.00 12.79 ? 545  LEU A CD2 1 
ATOM   4376 N  N   . GLY A 1 546  ? 64.475 89.108  -30.552 1.00 13.00 ? 546  GLY A N   1 
ATOM   4377 C  CA  . GLY A 1 546  ? 64.656 90.374  -31.271 1.00 13.96 ? 546  GLY A CA  1 
ATOM   4378 C  C   . GLY A 1 546  ? 66.096 90.467  -31.708 1.00 14.35 ? 546  GLY A C   1 
ATOM   4379 O  O   . GLY A 1 546  ? 67.012 89.980  -31.022 1.00 13.56 ? 546  GLY A O   1 
ATOM   4380 N  N   . GLU A 1 547  ? 66.323 91.143  -32.829 1.00 15.94 ? 547  GLU A N   1 
ATOM   4381 C  CA  . GLU A 1 547  ? 67.686 91.254  -33.350 1.00 18.53 ? 547  GLU A CA  1 
ATOM   4382 C  C   . GLU A 1 547  ? 68.654 91.920  -32.402 1.00 17.65 ? 547  GLU A C   1 
ATOM   4383 O  O   . GLU A 1 547  ? 69.836 91.608  -32.388 1.00 20.32 ? 547  GLU A O   1 
ATOM   4384 C  CB  . GLU A 1 547  ? 67.697 92.031  -34.671 1.00 22.01 ? 547  GLU A CB  1 
ATOM   4385 C  CG  . GLU A 1 547  ? 69.037 91.877  -35.405 1.00 28.20 ? 547  GLU A CG  1 
ATOM   4386 C  CD  . GLU A 1 547  ? 69.138 92.752  -36.653 1.00 31.26 ? 547  GLU A CD  1 
ATOM   4387 O  OE1 . GLU A 1 547  ? 68.103 92.929  -37.357 1.00 33.80 ? 547  GLU A OE1 1 
ATOM   4388 O  OE2 . GLU A 1 547  ? 70.258 93.259  -36.936 1.00 34.31 ? 547  GLU A OE2 1 
ATOM   4389 N  N   . ASP A 1 548  ? 68.125 92.823  -31.595 1.00 16.17 ? 548  ASP A N   1 
ATOM   4390 C  CA  . ASP A 1 548  ? 68.962 93.535  -30.660 1.00 16.62 ? 548  ASP A CA  1 
ATOM   4391 C  C   . ASP A 1 548  ? 68.892 92.945  -29.265 1.00 16.72 ? 548  ASP A C   1 
ATOM   4392 O  O   . ASP A 1 548  ? 69.278 93.609  -28.287 1.00 18.40 ? 548  ASP A O   1 
ATOM   4393 C  CB  . ASP A 1 548  ? 68.547 95.010  -30.612 1.00 17.77 ? 548  ASP A CB  1 
ATOM   4394 C  CG  . ASP A 1 548  ? 68.776 95.722  -31.929 1.00 19.27 ? 548  ASP A CG  1 
ATOM   4395 O  OD1 . ASP A 1 548  ? 69.939 95.724  -32.383 1.00 22.02 ? 548  ASP A OD1 1 
ATOM   4396 O  OD2 . ASP A 1 548  ? 67.808 96.258  -32.502 1.00 21.88 ? 548  ASP A OD2 1 
ATOM   4397 N  N   . ILE A 1 549  ? 68.411 91.702  -29.131 1.00 15.00 ? 549  ILE A N   1 
ATOM   4398 C  CA  . ILE A 1 549  ? 68.402 91.114  -27.796 1.00 14.96 ? 549  ILE A CA  1 
ATOM   4399 C  C   . ILE A 1 549  ? 68.678 89.611  -27.777 1.00 13.87 ? 549  ILE A C   1 
ATOM   4400 O  O   . ILE A 1 549  ? 69.535 89.181  -27.009 1.00 14.39 ? 549  ILE A O   1 
ATOM   4401 C  CB  . ILE A 1 549  ? 67.067 91.417  -26.986 1.00 14.66 ? 549  ILE A CB  1 
ATOM   4402 C  CG1 . ILE A 1 549  ? 67.209 90.862  -25.545 1.00 15.65 ? 549  ILE A CG1 1 
ATOM   4403 C  CG2 . ILE A 1 549  ? 65.800 90.938  -27.735 1.00 13.58 ? 549  ILE A CG2 1 
ATOM   4404 C  CD1 . ILE A 1 549  ? 66.017 91.200  -24.602 1.00 18.47 ? 549  ILE A CD1 1 
ATOM   4405 N  N   . LEU A 1 550  ? 67.995 88.847  -28.641 1.00 12.51 ? 550  LEU A N   1 
ATOM   4406 C  CA  . LEU A 1 550  ? 68.128 87.380  -28.571 1.00 12.45 ? 550  LEU A CA  1 
ATOM   4407 C  C   . LEU A 1 550  ? 67.500 86.810  -29.828 1.00 12.34 ? 550  LEU A C   1 
ATOM   4408 O  O   . LEU A 1 550  ? 66.284 86.946  -30.063 1.00 12.93 ? 550  LEU A O   1 
ATOM   4409 C  CB  . LEU A 1 550  ? 67.356 86.856  -27.349 1.00 13.19 ? 550  LEU A CB  1 
ATOM   4410 C  CG  . LEU A 1 550  ? 67.469 85.346  -27.145 1.00 13.85 ? 550  LEU A CG  1 
ATOM   4411 C  CD1 . LEU A 1 550  ? 68.930 84.937  -26.884 1.00 15.32 ? 550  LEU A CD1 1 
ATOM   4412 C  CD2 . LEU A 1 550  ? 66.569 84.982  -25.953 1.00 15.13 ? 550  LEU A CD2 1 
ATOM   4413 N  N   . PRO A 1 551  ? 68.286 86.123  -30.640 1.00 12.30 ? 551  PRO A N   1 
ATOM   4414 C  CA  . PRO A 1 551  ? 67.728 85.578  -31.863 1.00 13.16 ? 551  PRO A CA  1 
ATOM   4415 C  C   . PRO A 1 551  ? 66.833 84.333  -31.755 1.00 12.30 ? 551  PRO A C   1 
ATOM   4416 O  O   . PRO A 1 551  ? 65.978 84.111  -32.637 1.00 13.33 ? 551  PRO A O   1 
ATOM   4417 C  CB  . PRO A 1 551  ? 68.970 85.207  -32.701 1.00 14.02 ? 551  PRO A CB  1 
ATOM   4418 C  CG  . PRO A 1 551  ? 70.044 85.950  -32.138 1.00 17.36 ? 551  PRO A CG  1 
ATOM   4419 C  CD  . PRO A 1 551  ? 69.759 86.133  -30.671 1.00 14.23 ? 551  PRO A CD  1 
ATOM   4420 N  N   . SER A 1 552  ? 67.099 83.502  -30.741 1.00 10.92 ? 552  SER A N   1 
ATOM   4421 C  CA  . SER A 1 552  ? 66.385 82.223  -30.717 1.00 11.37 ? 552  SER A CA  1 
ATOM   4422 C  C   . SER A 1 552  ? 66.285 81.736  -29.294 1.00 10.31 ? 552  SER A C   1 
ATOM   4423 O  O   . SER A 1 552  ? 66.946 82.227  -28.394 1.00 10.78 ? 552  SER A O   1 
ATOM   4424 C  CB  . SER A 1 552  ? 67.158 81.194  -31.565 1.00 12.71 ? 552  SER A CB  1 
ATOM   4425 O  OG  . SER A 1 552  ? 68.414 80.870  -31.013 1.00 14.05 ? 552  SER A OG  1 
ATOM   4426 N  N   . LYS A 1 553  ? 65.437 80.724  -29.111 1.00 10.30 ? 553  LYS A N   1 
ATOM   4427 C  CA  . LYS A 1 553  ? 65.181 80.158  -27.782 1.00 9.50  ? 553  LYS A CA  1 
ATOM   4428 C  C   . LYS A 1 553  ? 64.894 78.665  -27.894 1.00 8.90  ? 553  LYS A C   1 
ATOM   4429 O  O   . LYS A 1 553  ? 64.083 78.217  -28.728 1.00 9.64  ? 553  LYS A O   1 
ATOM   4430 C  CB  . LYS A 1 553  ? 63.896 80.853  -27.234 1.00 10.56 ? 553  LYS A CB  1 
ATOM   4431 C  CG  . LYS A 1 553  ? 63.387 80.222  -25.898 1.00 11.92 ? 553  LYS A CG  1 
ATOM   4432 C  CD  . LYS A 1 553  ? 64.431 80.371  -24.777 1.00 11.86 ? 553  LYS A CD  1 
ATOM   4433 C  CE  . LYS A 1 553  ? 64.655 81.838  -24.310 1.00 12.84 ? 553  LYS A CE  1 
ATOM   4434 N  NZ  . LYS A 1 553  ? 65.860 81.949  -23.459 1.00 11.94 ? 553  LYS A NZ  1 
ATOM   4435 N  N   . HIS A 1 554  ? 65.523 77.901  -27.002 1.00 9.09  ? 554  HIS A N   1 
ATOM   4436 C  CA  . HIS A 1 554  ? 65.228 76.463  -26.931 1.00 8.85  ? 554  HIS A CA  1 
ATOM   4437 C  C   . HIS A 1 554  ? 64.051 76.214  -25.999 1.00 8.33  ? 554  HIS A C   1 
ATOM   4438 O  O   . HIS A 1 554  ? 63.896 76.852  -24.945 1.00 9.27  ? 554  HIS A O   1 
ATOM   4439 C  CB  . HIS A 1 554  ? 66.424 75.689  -26.344 1.00 11.38 ? 554  HIS A CB  1 
ATOM   4440 C  CG  . HIS A 1 554  ? 67.560 75.573  -27.299 1.00 13.41 ? 554  HIS A CG  1 
ATOM   4441 N  ND1 . HIS A 1 554  ? 68.223 74.400  -27.562 1.00 18.14 ? 554  HIS A ND1 1 
ATOM   4442 C  CD2 . HIS A 1 554  ? 68.175 76.533  -28.043 1.00 15.73 ? 554  HIS A CD2 1 
ATOM   4443 C  CE1 . HIS A 1 554  ? 69.227 74.643  -28.391 1.00 15.32 ? 554  HIS A CE1 1 
ATOM   4444 N  NE2 . HIS A 1 554  ? 69.218 75.927  -28.696 1.00 20.33 ? 554  HIS A NE2 1 
ATOM   4445 N  N   . VAL A 1 555  ? 63.212 75.298  -26.432 1.00 7.77  ? 555  VAL A N   1 
ATOM   4446 C  CA  . VAL A 1 555  ? 62.049 74.812  -25.667 1.00 8.80  ? 555  VAL A CA  1 
ATOM   4447 C  C   . VAL A 1 555  ? 62.142 73.293  -25.664 1.00 8.33  ? 555  VAL A C   1 
ATOM   4448 O  O   . VAL A 1 555  ? 62.685 72.685  -26.584 1.00 8.95  ? 555  VAL A O   1 
ATOM   4449 C  CB  . VAL A 1 555  ? 60.685 75.279  -26.216 1.00 8.44  ? 555  VAL A CB  1 
ATOM   4450 C  CG1 . VAL A 1 555  ? 60.598 76.810  -26.183 1.00 8.85  ? 555  VAL A CG1 1 
ATOM   4451 C  CG2 . VAL A 1 555  ? 60.455 74.776  -27.607 1.00 9.81  ? 555  VAL A CG2 1 
ATOM   4452 N  N   . VAL A 1 556  ? 61.655 72.666  -24.590 1.00 7.65  ? 556  VAL A N   1 
ATOM   4453 C  CA  . VAL A 1 556  ? 61.701 71.209  -24.435 1.00 7.81  ? 556  VAL A CA  1 
ATOM   4454 C  C   . VAL A 1 556  ? 60.327 70.707  -24.017 1.00 6.88  ? 556  VAL A C   1 
ATOM   4455 O  O   . VAL A 1 556  ? 59.665 71.295  -23.138 1.00 7.85  ? 556  VAL A O   1 
ATOM   4456 C  CB  . VAL A 1 556  ? 62.707 70.821  -23.319 1.00 7.78  ? 556  VAL A CB  1 
ATOM   4457 C  CG1 . VAL A 1 556  ? 62.627 69.319  -23.025 1.00 8.60  ? 556  VAL A CG1 1 
ATOM   4458 C  CG2 . VAL A 1 556  ? 64.097 71.233  -23.714 1.00 9.43  ? 556  VAL A CG2 1 
ATOM   4459 N  N   . MET A 1 557  ? 59.898 69.625  -24.632 1.00 7.25  ? 557  MET A N   1 
ATOM   4460 C  CA  . MET A 1 557  ? 58.651 68.946  -24.274 1.00 7.18  ? 557  MET A CA  1 
ATOM   4461 C  C   . MET A 1 557  ? 58.939 67.626  -23.604 1.00 7.12  ? 557  MET A C   1 
ATOM   4462 O  O   . MET A 1 557  ? 59.836 66.877  -24.003 1.00 7.97  ? 557  MET A O   1 
ATOM   4463 C  CB  . MET A 1 557  ? 57.763 68.660  -25.521 1.00 7.38  ? 557  MET A CB  1 
ATOM   4464 C  CG  . MET A 1 557  ? 56.749 69.805  -25.827 1.00 8.91  ? 557  MET A CG  1 
ATOM   4465 S  SD  . MET A 1 557  ? 57.399 71.457  -26.026 1.00 9.85  ? 557  MET A SD  1 
ATOM   4466 C  CE  . MET A 1 557  ? 57.629 72.041  -24.429 1.00 19.51 ? 557  MET A CE  1 
ATOM   4467 N  N   . HIS A 1 558  ? 58.148 67.330  -22.565 1.00 7.09  ? 558  HIS A N   1 
ATOM   4468 C  CA  . HIS A 1 558  ? 58.224 66.043  -21.879 1.00 6.00  ? 558  HIS A CA  1 
ATOM   4469 C  C   . HIS A 1 558  ? 56.916 65.296  -22.115 1.00 7.32  ? 558  HIS A C   1 
ATOM   4470 O  O   . HIS A 1 558  ? 55.806 65.872  -22.104 1.00 7.10  ? 558  HIS A O   1 
ATOM   4471 C  CB  . HIS A 1 558  ? 58.371 66.236  -20.356 1.00 7.29  ? 558  HIS A CB  1 
ATOM   4472 C  CG  . HIS A 1 558  ? 58.246 64.967  -19.568 1.00 7.19  ? 558  HIS A CG  1 
ATOM   4473 N  ND1 . HIS A 1 558  ? 57.305 64.793  -18.565 1.00 7.44  ? 558  HIS A ND1 1 
ATOM   4474 C  CD2 . HIS A 1 558  ? 58.995 63.837  -19.586 1.00 7.39  ? 558  HIS A CD2 1 
ATOM   4475 C  CE1 . HIS A 1 558  ? 57.500 63.601  -18.001 1.00 7.65  ? 558  HIS A CE1 1 
ATOM   4476 N  NE2 . HIS A 1 558  ? 58.515 63.003  -18.599 1.00 7.53  ? 558  HIS A NE2 1 
ATOM   4477 N  N   . ASN A 1 559  ? 57.041 63.989  -22.306 1.00 7.03  ? 559  ASN A N   1 
ATOM   4478 C  CA  . ASN A 1 559  ? 55.899 63.110  -22.507 1.00 6.38  ? 559  ASN A CA  1 
ATOM   4479 C  C   . ASN A 1 559  ? 55.902 62.019  -21.445 1.00 6.75  ? 559  ASN A C   1 
ATOM   4480 O  O   . ASN A 1 559  ? 56.654 61.071  -21.544 1.00 8.15  ? 559  ASN A O   1 
ATOM   4481 C  CB  . ASN A 1 559  ? 55.995 62.451  -23.903 1.00 7.19  ? 559  ASN A CB  1 
ATOM   4482 C  CG  . ASN A 1 559  ? 54.972 61.369  -24.099 1.00 7.97  ? 559  ASN A CG  1 
ATOM   4483 O  OD1 . ASN A 1 559  ? 53.884 61.352  -23.519 1.00 7.75  ? 559  ASN A OD1 1 
ATOM   4484 N  ND2 . ASN A 1 559  ? 55.285 60.455  -25.007 1.00 9.20  ? 559  ASN A ND2 1 
ATOM   4485 N  N   . THR A 1 560  ? 55.030 62.152  -20.445 1.00 6.47  ? 560  THR A N   1 
ATOM   4486 C  CA  . THR A 1 560  ? 55.033 61.167  -19.346 1.00 7.17  ? 560  THR A CA  1 
ATOM   4487 C  C   . THR A 1 560  ? 54.427 59.821  -19.735 1.00 6.95  ? 560  THR A C   1 
ATOM   4488 O  O   . THR A 1 560  ? 54.615 58.856  -19.021 1.00 7.54  ? 560  THR A O   1 
ATOM   4489 C  CB  . THR A 1 560  ? 54.263 61.800  -18.162 1.00 6.26  ? 560  THR A CB  1 
ATOM   4490 O  OG1 . THR A 1 560  ? 54.540 61.043  -16.956 1.00 7.74  ? 560  THR A OG1 1 
ATOM   4491 C  CG2 . THR A 1 560  ? 52.762 61.767  -18.366 1.00 8.13  ? 560  THR A CG2 1 
ATOM   4492 N  N   . LEU A 1 561  ? 53.683 59.755  -20.854 1.00 7.50  ? 561  LEU A N   1 
ATOM   4493 C  CA  . LEU A 1 561  ? 53.067 58.488  -21.260 1.00 8.17  ? 561  LEU A CA  1 
ATOM   4494 C  C   . LEU A 1 561  ? 54.091 57.561  -21.942 1.00 7.58  ? 561  LEU A C   1 
ATOM   4495 O  O   . LEU A 1 561  ? 54.970 58.033  -22.676 1.00 8.25  ? 561  LEU A O   1 
ATOM   4496 C  CB  . LEU A 1 561  ? 51.905 58.734  -22.271 1.00 8.53  ? 561  LEU A CB  1 
ATOM   4497 C  CG  . LEU A 1 561  ? 50.823 59.663  -21.723 1.00 8.52  ? 561  LEU A CG  1 
ATOM   4498 C  CD1 . LEU A 1 561  ? 49.728 59.772  -22.778 1.00 9.72  ? 561  LEU A CD1 1 
ATOM   4499 C  CD2 . LEU A 1 561  ? 50.176 59.078  -20.480 1.00 10.12 ? 561  LEU A CD2 1 
ATOM   4500 N  N   . PRO A 1 562  ? 53.920 56.248  -21.797 1.00 7.64  ? 562  PRO A N   1 
ATOM   4501 C  CA  . PRO A 1 562  ? 54.873 55.285  -22.382 1.00 9.06  ? 562  PRO A CA  1 
ATOM   4502 C  C   . PRO A 1 562  ? 54.676 54.921  -23.823 1.00 9.13  ? 562  PRO A C   1 
ATOM   4503 O  O   . PRO A 1 562  ? 54.804 53.767  -24.202 1.00 10.23 ? 562  PRO A O   1 
ATOM   4504 C  CB  . PRO A 1 562  ? 54.767 54.087  -21.424 1.00 8.66  ? 562  PRO A CB  1 
ATOM   4505 C  CG  . PRO A 1 562  ? 53.229 54.067  -21.130 1.00 8.08  ? 562  PRO A CG  1 
ATOM   4506 C  CD  . PRO A 1 562  ? 52.977 55.569  -20.894 1.00 8.34  ? 562  PRO A CD  1 
ATOM   4507 N  N   . HIS A 1 563  ? 54.312 55.906  -24.641 1.00 9.45  ? 563  HIS A N   1 
ATOM   4508 C  CA  . HIS A 1 563  ? 54.247 55.676  -26.096 1.00 9.50  ? 563  HIS A CA  1 
ATOM   4509 C  C   . HIS A 1 563  ? 54.616 56.980  -26.762 1.00 10.29 ? 563  HIS A C   1 
ATOM   4510 O  O   . HIS A 1 563  ? 54.490 58.061  -26.163 1.00 10.29 ? 563  HIS A O   1 
ATOM   4511 C  CB  . HIS A 1 563  ? 52.843 55.180  -26.546 1.00 9.67  ? 563  HIS A CB  1 
ATOM   4512 C  CG  . HIS A 1 563  ? 51.712 56.052  -26.104 1.00 10.11 ? 563  HIS A CG  1 
ATOM   4513 N  ND1 . HIS A 1 563  ? 50.889 55.688  -25.059 1.00 10.61 ? 563  HIS A ND1 1 
ATOM   4514 C  CD2 . HIS A 1 563  ? 51.199 57.204  -26.613 1.00 10.12 ? 563  HIS A CD2 1 
ATOM   4515 C  CE1 . HIS A 1 563  ? 49.906 56.584  -24.947 1.00 11.47 ? 563  HIS A CE1 1 
ATOM   4516 N  NE2 . HIS A 1 563  ? 50.081 57.519  -25.874 1.00 11.89 ? 563  HIS A NE2 1 
ATOM   4517 N  N   . TRP A 1 564  ? 55.152 56.898  -27.985 1.00 10.33 ? 564  TRP A N   1 
ATOM   4518 C  CA  . TRP A 1 564  ? 55.476 58.119  -28.735 1.00 9.98  ? 564  TRP A CA  1 
ATOM   4519 C  C   . TRP A 1 564  ? 54.224 58.938  -28.864 1.00 10.83 ? 564  TRP A C   1 
ATOM   4520 O  O   . TRP A 1 564  ? 53.114 58.427  -29.075 1.00 11.26 ? 564  TRP A O   1 
ATOM   4521 C  CB  . TRP A 1 564  ? 55.937 57.751  -30.160 1.00 11.74 ? 564  TRP A CB  1 
ATOM   4522 C  CG  . TRP A 1 564  ? 57.321 57.291  -30.246 1.00 11.02 ? 564  TRP A CG  1 
ATOM   4523 C  CD1 . TRP A 1 564  ? 57.780 55.985  -30.126 1.00 13.09 ? 564  TRP A CD1 1 
ATOM   4524 C  CD2 . TRP A 1 564  ? 58.488 58.110  -30.407 1.00 11.89 ? 564  TRP A CD2 1 
ATOM   4525 N  NE1 . TRP A 1 564  ? 59.140 55.968  -30.197 1.00 14.25 ? 564  TRP A NE1 1 
ATOM   4526 C  CE2 . TRP A 1 564  ? 59.611 57.245  -30.367 1.00 12.84 ? 564  TRP A CE2 1 
ATOM   4527 C  CE3 . TRP A 1 564  ? 58.699 59.493  -30.577 1.00 12.77 ? 564  TRP A CE3 1 
ATOM   4528 C  CZ2 . TRP A 1 564  ? 60.931 57.718  -30.481 1.00 13.47 ? 564  TRP A CZ2 1 
ATOM   4529 C  CZ3 . TRP A 1 564  ? 60.019 59.956  -30.694 1.00 13.18 ? 564  TRP A CZ3 1 
ATOM   4530 C  CH2 . TRP A 1 564  ? 61.107 59.072  -30.643 1.00 14.37 ? 564  TRP A CH2 1 
ATOM   4531 N  N   . ARG A 1 565  ? 54.391 60.250  -28.749 1.00 11.29 ? 565  ARG A N   1 
ATOM   4532 C  CA  . ARG A 1 565  ? 53.239 61.084  -28.899 1.00 12.17 ? 565  ARG A CA  1 
ATOM   4533 C  C   . ARG A 1 565  ? 53.595 62.296  -29.740 1.00 11.87 ? 565  ARG A C   1 
ATOM   4534 O  O   . ARG A 1 565  ? 54.688 62.875  -29.618 1.00 13.17 ? 565  ARG A O   1 
ATOM   4535 C  CB  . ARG A 1 565  ? 52.779 61.532  -27.500 1.00 15.10 ? 565  ARG A CB  1 
ATOM   4536 C  CG  . ARG A 1 565  ? 51.463 62.208  -27.425 1.00 18.06 ? 565  ARG A CG  1 
ATOM   4537 C  CD  . ARG A 1 565  ? 50.662 61.828  -26.109 1.00 15.04 ? 565  ARG A CD  1 
ATOM   4538 N  NE  . ARG A 1 565  ? 51.414 62.138  -24.905 1.00 14.26 ? 565  ARG A NE  1 
ATOM   4539 C  CZ  . ARG A 1 565  ? 50.859 62.777  -23.869 1.00 11.23 ? 565  ARG A CZ  1 
ATOM   4540 N  NH1 . ARG A 1 565  ? 49.557 63.176  -23.865 1.00 11.19 ? 565  ARG A NH1 1 
ATOM   4541 N  NH2 . ARG A 1 565  ? 51.658 63.067  -22.837 1.00 10.77 ? 565  ARG A NH2 1 
ATOM   4542 N  N   . GLU A 1 566  ? 52.693 62.639  -30.641 1.00 13.32 ? 566  GLU A N   1 
ATOM   4543 C  CA  . GLU A 1 566  ? 52.794 63.882  -31.372 1.00 15.96 ? 566  GLU A CA  1 
ATOM   4544 C  C   . GLU A 1 566  ? 51.621 64.692  -30.760 1.00 17.56 ? 566  GLU A C   1 
ATOM   4545 O  O   . GLU A 1 566  ? 50.562 64.129  -30.378 1.00 19.88 ? 566  GLU A O   1 
ATOM   4546 C  CB  . GLU A 1 566  ? 52.582 63.649  -32.823 1.00 19.46 ? 566  GLU A CB  1 
ATOM   4547 C  CG  . GLU A 1 566  ? 53.717 63.106  -33.461 1.00 20.93 ? 566  GLU A CG  1 
ATOM   4548 C  CD  . GLU A 1 566  ? 53.452 63.016  -34.944 1.00 25.08 ? 566  GLU A CD  1 
ATOM   4549 O  OE1 . GLU A 1 566  ? 52.312 62.611  -35.304 1.00 27.42 ? 566  GLU A OE1 1 
ATOM   4550 O  OE2 . GLU A 1 566  ? 54.375 63.381  -35.713 1.00 25.86 ? 566  GLU A OE2 1 
ATOM   4551 N  N   . GLN A 1 567  ? 51.778 66.003  -30.628 1.00 14.61 ? 567  GLN A N   1 
ATOM   4552 C  CA  . GLN A 1 567  ? 50.678 66.793  -30.039 1.00 14.34 ? 567  GLN A CA  1 
ATOM   4553 C  C   . GLN A 1 567  ? 51.054 68.230  -30.401 1.00 13.39 ? 567  GLN A C   1 
ATOM   4554 O  O   . GLN A 1 567  ? 52.241 68.576  -30.401 1.00 11.52 ? 567  GLN A O   1 
ATOM   4555 C  CB  . GLN A 1 567  ? 50.605 66.645  -28.473 1.00 15.24 ? 567  GLN A CB  1 
ATOM   4556 C  CG  . GLN A 1 567  ? 49.468 67.521  -27.712 1.00 16.43 ? 567  GLN A CG  1 
ATOM   4557 C  CD  . GLN A 1 567  ? 49.860 68.045  -26.278 1.00 17.86 ? 567  GLN A CD  1 
ATOM   4558 O  OE1 . GLN A 1 567  ? 49.854 67.258  -25.267 1.00 13.06 ? 567  GLN A OE1 1 
ATOM   4559 N  NE2 . GLN A 1 567  ? 50.181 69.396  -26.185 1.00 17.24 ? 567  GLN A NE2 1 
ATOM   4560 N  N   . LEU A 1 568  ? 50.077 69.038  -30.763 1.00 11.24 ? 568  LEU A N   1 
ATOM   4561 C  CA  . LEU A 1 568  ? 50.382 70.469  -30.999 1.00 10.93 ? 568  LEU A CA  1 
ATOM   4562 C  C   . LEU A 1 568  ? 50.666 71.091  -29.641 1.00 10.13 ? 568  LEU A C   1 
ATOM   4563 O  O   . LEU A 1 568  ? 50.001 70.769  -28.597 1.00 11.08 ? 568  LEU A O   1 
ATOM   4564 C  CB  . LEU A 1 568  ? 49.170 71.194  -31.608 1.00 12.23 ? 568  LEU A CB  1 
ATOM   4565 C  CG  . LEU A 1 568  ? 48.794 70.847  -33.049 1.00 13.81 ? 568  LEU A CG  1 
ATOM   4566 C  CD1 . LEU A 1 568  ? 47.713 71.861  -33.511 1.00 15.40 ? 568  LEU A CD1 1 
ATOM   4567 C  CD2 . LEU A 1 568  ? 49.964 70.984  -33.978 1.00 15.14 ? 568  LEU A CD2 1 
ATOM   4568 N  N   . VAL A 1 569  ? 51.668 71.953  -29.644 1.00 8.46  ? 569  VAL A N   1 
ATOM   4569 C  CA  . VAL A 1 569  ? 52.036 72.720  -28.466 1.00 9.46  ? 569  VAL A CA  1 
ATOM   4570 C  C   . VAL A 1 569  ? 52.088 74.185  -28.862 1.00 10.20 ? 569  VAL A C   1 
ATOM   4571 O  O   . VAL A 1 569  ? 52.302 74.506  -30.039 1.00 11.33 ? 569  VAL A O   1 
ATOM   4572 C  CB  . VAL A 1 569  ? 53.432 72.331  -27.872 1.00 8.76  ? 569  VAL A CB  1 
ATOM   4573 C  CG1 . VAL A 1 569  ? 53.328 70.915  -27.231 1.00 10.46 ? 569  VAL A CG1 1 
ATOM   4574 C  CG2 . VAL A 1 569  ? 54.561 72.382  -28.933 1.00 9.48  ? 569  VAL A CG2 1 
ATOM   4575 N  N   . ASP A 1 570  ? 51.867 75.077  -27.919 1.00 9.99  ? 570  ASP A N   1 
ATOM   4576 C  CA  . ASP A 1 570  ? 51.912 76.498  -28.236 1.00 10.99 ? 570  ASP A CA  1 
ATOM   4577 C  C   . ASP A 1 570  ? 52.684 77.278  -27.197 1.00 10.44 ? 570  ASP A C   1 
ATOM   4578 O  O   . ASP A 1 570  ? 52.769 76.887  -26.009 1.00 11.77 ? 570  ASP A O   1 
ATOM   4579 C  CB  . ASP A 1 570  ? 50.478 77.075  -28.376 1.00 13.78 ? 570  ASP A CB  1 
ATOM   4580 C  CG  . ASP A 1 570  ? 49.747 77.184  -27.023 1.00 17.46 ? 570  ASP A CG  1 
ATOM   4581 O  OD1 . ASP A 1 570  ? 49.539 76.163  -26.366 1.00 23.94 ? 570  ASP A OD1 1 
ATOM   4582 O  OD2 . ASP A 1 570  ? 49.381 78.290  -26.604 1.00 21.88 ? 570  ASP A OD2 1 
ATOM   4583 N  N   . PHE A 1 571  ? 53.300 78.358  -27.664 1.00 9.35  ? 571  PHE A N   1 
ATOM   4584 C  CA  . PHE A 1 571  ? 54.049 79.275  -26.820 1.00 9.71  ? 571  PHE A CA  1 
ATOM   4585 C  C   . PHE A 1 571  ? 53.717 80.702  -27.198 1.00 9.66  ? 571  PHE A C   1 
ATOM   4586 O  O   . PHE A 1 571  ? 53.306 80.957  -28.322 1.00 10.91 ? 571  PHE A O   1 
ATOM   4587 C  CB  . PHE A 1 571  ? 55.563 79.104  -27.042 1.00 9.49  ? 571  PHE A CB  1 
ATOM   4588 C  CG  . PHE A 1 571  ? 56.073 77.763  -26.643 1.00 8.65  ? 571  PHE A CG  1 
ATOM   4589 C  CD1 . PHE A 1 571  ? 56.071 76.675  -27.499 1.00 9.42  ? 571  PHE A CD1 1 
ATOM   4590 C  CD2 . PHE A 1 571  ? 56.531 77.592  -25.353 1.00 9.20  ? 571  PHE A CD2 1 
ATOM   4591 C  CE1 . PHE A 1 571  ? 56.519 75.434  -27.074 1.00 8.95  ? 571  PHE A CE1 1 
ATOM   4592 C  CE2 . PHE A 1 571  ? 56.982 76.334  -24.914 1.00 9.30  ? 571  PHE A CE2 1 
ATOM   4593 C  CZ  . PHE A 1 571  ? 56.972 75.251  -25.786 1.00 10.05 ? 571  PHE A CZ  1 
ATOM   4594 N  N   . TYR A 1 572  ? 53.850 81.601  -26.252 1.00 9.01  ? 572  TYR A N   1 
ATOM   4595 C  CA  . TYR A 1 572  ? 53.731 83.029  -26.534 1.00 9.57  ? 572  TYR A CA  1 
ATOM   4596 C  C   . TYR A 1 572  ? 55.101 83.535  -26.947 1.00 10.13 ? 572  TYR A C   1 
ATOM   4597 O  O   . TYR A 1 572  ? 56.123 83.199  -26.310 1.00 10.30 ? 572  TYR A O   1 
ATOM   4598 C  CB  . TYR A 1 572  ? 53.275 83.805  -25.294 1.00 11.21 ? 572  TYR A CB  1 
ATOM   4599 C  CG  . TYR A 1 572  ? 51.823 83.672  -24.909 1.00 12.50 ? 572  TYR A CG  1 
ATOM   4600 C  CD1 . TYR A 1 572  ? 50.923 82.981  -25.699 1.00 14.56 ? 572  TYR A CD1 1 
ATOM   4601 C  CD2 . TYR A 1 572  ? 51.375 84.277  -23.729 1.00 16.20 ? 572  TYR A CD2 1 
ATOM   4602 C  CE1 . TYR A 1 572  ? 49.578 82.880  -25.329 1.00 16.41 ? 572  TYR A CE1 1 
ATOM   4603 C  CE2 . TYR A 1 572  ? 50.023 84.179  -23.349 1.00 17.20 ? 572  TYR A CE2 1 
ATOM   4604 C  CZ  . TYR A 1 572  ? 49.162 83.477  -24.163 1.00 16.76 ? 572  TYR A CZ  1 
ATOM   4605 O  OH  . TYR A 1 572  ? 47.807 83.324  -23.789 1.00 20.80 ? 572  TYR A OH  1 
ATOM   4606 N  N   . VAL A 1 573  ? 55.130 84.348  -28.014 1.00 10.47 ? 573  VAL A N   1 
ATOM   4607 C  CA  . VAL A 1 573  ? 56.370 84.936  -28.545 1.00 10.62 ? 573  VAL A CA  1 
ATOM   4608 C  C   . VAL A 1 573  ? 56.132 86.412  -28.823 1.00 9.49  ? 573  VAL A C   1 
ATOM   4609 O  O   . VAL A 1 573  ? 55.025 86.849  -29.074 1.00 10.53 ? 573  VAL A O   1 
ATOM   4610 C  CB  . VAL A 1 573  ? 56.822 84.209  -29.861 1.00 11.05 ? 573  VAL A CB  1 
ATOM   4611 C  CG1 . VAL A 1 573  ? 57.391 82.848  -29.529 1.00 13.21 ? 573  VAL A CG1 1 
ATOM   4612 C  CG2 . VAL A 1 573  ? 55.658 84.076  -30.832 1.00 11.30 ? 573  VAL A CG2 1 
ATOM   4613 N  N   . SER A 1 574  ? 57.212 87.167  -28.821 1.00 10.75 ? 574  SER A N   1 
ATOM   4614 C  CA  . SER A 1 574  ? 57.114 88.629  -29.000 1.00 11.78 ? 574  SER A CA  1 
ATOM   4615 C  C   . SER A 1 574  ? 57.102 89.130  -30.409 1.00 12.12 ? 574  SER A C   1 
ATOM   4616 O  O   . SER A 1 574  ? 57.086 90.361  -30.632 1.00 14.68 ? 574  SER A O   1 
ATOM   4617 C  CB  . SER A 1 574  ? 58.227 89.271  -28.212 1.00 11.60 ? 574  SER A CB  1 
ATOM   4618 O  OG  . SER A 1 574  ? 59.491 88.951  -28.765 1.00 12.51 ? 574  SER A OG  1 
ATOM   4619 N  N   . SER A 1 575  ? 57.101 88.228  -31.377 1.00 12.79 ? 575  SER A N   1 
ATOM   4620 C  CA  . SER A 1 575  ? 57.049 88.582  -32.787 1.00 13.77 ? 575  SER A CA  1 
ATOM   4621 C  C   . SER A 1 575  ? 56.285 87.513  -33.544 1.00 14.45 ? 575  SER A C   1 
ATOM   4622 O  O   . SER A 1 575  ? 56.292 86.324  -33.165 1.00 13.14 ? 575  SER A O   1 
ATOM   4623 C  CB  . SER A 1 575  ? 58.455 88.605  -33.369 1.00 14.08 ? 575  SER A CB  1 
ATOM   4624 O  OG  . SER A 1 575  ? 58.451 88.716  -34.801 1.00 15.34 ? 575  SER A OG  1 
ATOM   4625 N  N   . PRO A 1 576  ? 55.576 87.898  -34.600 1.00 14.04 ? 576  PRO A N   1 
ATOM   4626 C  CA  . PRO A 1 576  ? 54.861 86.882  -35.367 1.00 14.12 ? 576  PRO A CA  1 
ATOM   4627 C  C   . PRO A 1 576  ? 55.798 86.178  -36.362 1.00 12.79 ? 576  PRO A C   1 
ATOM   4628 O  O   . PRO A 1 576  ? 55.432 85.147  -36.943 1.00 14.18 ? 576  PRO A O   1 
ATOM   4629 C  CB  . PRO A 1 576  ? 53.769 87.668  -36.063 1.00 15.41 ? 576  PRO A CB  1 
ATOM   4630 C  CG  . PRO A 1 576  ? 54.367 89.058  -36.236 1.00 16.50 ? 576  PRO A CG  1 
ATOM   4631 C  CD  . PRO A 1 576  ? 55.290 89.277  -35.068 1.00 14.45 ? 576  PRO A CD  1 
ATOM   4632 N  N   . PHE A 1 577  ? 57.032 86.688  -36.524 1.00 12.55 ? 577  PHE A N   1 
ATOM   4633 C  CA  . PHE A 1 577  ? 57.934 86.137  -37.563 1.00 12.81 ? 577  PHE A CA  1 
ATOM   4634 C  C   . PHE A 1 577  ? 58.912 85.203  -36.893 1.00 13.16 ? 577  PHE A C   1 
ATOM   4635 O  O   . PHE A 1 577  ? 60.083 85.508  -36.665 1.00 13.75 ? 577  PHE A O   1 
ATOM   4636 C  CB  . PHE A 1 577  ? 58.658 87.314  -38.277 1.00 14.18 ? 577  PHE A CB  1 
ATOM   4637 C  CG  . PHE A 1 577  ? 57.696 88.330  -38.872 1.00 17.22 ? 577  PHE A CG  1 
ATOM   4638 C  CD1 . PHE A 1 577  ? 56.652 87.925  -39.671 1.00 16.68 ? 577  PHE A CD1 1 
ATOM   4639 C  CD2 . PHE A 1 577  ? 57.906 89.706  -38.669 1.00 19.70 ? 577  PHE A CD2 1 
ATOM   4640 C  CE1 . PHE A 1 577  ? 55.802 88.879  -40.303 1.00 18.46 ? 577  PHE A CE1 1 
ATOM   4641 C  CE2 . PHE A 1 577  ? 57.071 90.660  -39.290 1.00 20.73 ? 577  PHE A CE2 1 
ATOM   4642 C  CZ  . PHE A 1 577  ? 56.034 90.234  -40.101 1.00 20.24 ? 577  PHE A CZ  1 
ATOM   4643 N  N   . VAL A 1 578  ? 58.371 84.045  -36.522 1.00 12.41 ? 578  VAL A N   1 
ATOM   4644 C  CA  . VAL A 1 578  ? 59.137 83.017  -35.812 1.00 12.29 ? 578  VAL A CA  1 
ATOM   4645 C  C   . VAL A 1 578  ? 58.991 81.681  -36.513 1.00 11.99 ? 578  VAL A C   1 
ATOM   4646 O  O   . VAL A 1 578  ? 57.912 81.338  -36.997 1.00 13.38 ? 578  VAL A O   1 
ATOM   4647 C  CB  . VAL A 1 578  ? 58.611 82.912  -34.327 1.00 12.02 ? 578  VAL A CB  1 
ATOM   4648 C  CG1 . VAL A 1 578  ? 59.368 81.773  -33.578 1.00 12.45 ? 578  VAL A CG1 1 
ATOM   4649 C  CG2 . VAL A 1 578  ? 58.861 84.197  -33.615 1.00 12.49 ? 578  VAL A CG2 1 
ATOM   4650 N  N   . SER A 1 579  ? 60.086 80.956  -36.584 1.00 12.97 ? 579  SER A N   1 
ATOM   4651 C  CA  . SER A 1 579  ? 60.007 79.644  -37.186 1.00 14.58 ? 579  SER A CA  1 
ATOM   4652 C  C   . SER A 1 579  ? 60.581 78.630  -36.232 1.00 12.55 ? 579  SER A C   1 
ATOM   4653 O  O   . SER A 1 579  ? 61.352 78.963  -35.324 1.00 12.96 ? 579  SER A O   1 
ATOM   4654 C  CB  . SER A 1 579  ? 60.609 79.618  -38.583 1.00 18.41 ? 579  SER A CB  1 
ATOM   4655 O  OG  . SER A 1 579  ? 61.910 80.057  -38.519 1.00 20.19 ? 579  SER A OG  1 
ATOM   4656 N  N   . VAL A 1 580  ? 60.191 77.393  -36.440 1.00 10.95 ? 580  VAL A N   1 
ATOM   4657 C  CA  . VAL A 1 580  ? 60.580 76.309  -35.548 1.00 10.72 ? 580  VAL A CA  1 
ATOM   4658 C  C   . VAL A 1 580  ? 61.442 75.272  -36.239 1.00 11.03 ? 580  VAL A C   1 
ATOM   4659 O  O   . VAL A 1 580  ? 61.186 74.933  -37.422 1.00 12.09 ? 580  VAL A O   1 
ATOM   4660 C  CB  . VAL A 1 580  ? 59.287 75.611  -35.033 1.00 10.83 ? 580  VAL A CB  1 
ATOM   4661 C  CG1 . VAL A 1 580  ? 59.642 74.563  -33.987 1.00 12.12 ? 580  VAL A CG1 1 
ATOM   4662 C  CG2 . VAL A 1 580  ? 58.314 76.644  -34.390 1.00 11.76 ? 580  VAL A CG2 1 
ATOM   4663 N  N   . THR A 1 581  ? 62.423 74.771  -35.503 1.00 11.03 ? 581  THR A N   1 
ATOM   4664 C  CA  . THR A 1 581  ? 63.277 73.701  -35.996 1.00 11.24 ? 581  THR A CA  1 
ATOM   4665 C  C   . THR A 1 581  ? 63.450 72.676  -34.883 1.00 10.71 ? 581  THR A C   1 
ATOM   4666 O  O   . THR A 1 581  ? 63.216 72.988  -33.688 1.00 11.19 ? 581  THR A O   1 
ATOM   4667 C  CB  . THR A 1 581  ? 64.714 74.185  -36.377 1.00 12.38 ? 581  THR A CB  1 
ATOM   4668 O  OG1 . THR A 1 581  ? 65.211 75.108  -35.384 1.00 14.72 ? 581  THR A OG1 1 
ATOM   4669 C  CG2 . THR A 1 581  ? 64.688 74.926  -37.732 1.00 12.99 ? 581  THR A CG2 1 
ATOM   4670 N  N   . ASP A 1 582  ? 63.782 71.450  -35.240 1.00 12.81 ? 582  ASP A N   1 
ATOM   4671 C  CA  . ASP A 1 582  ? 64.076 70.404  -34.238 1.00 14.00 ? 582  ASP A CA  1 
ATOM   4672 C  C   . ASP A 1 582  ? 65.588 70.500  -33.939 1.00 16.08 ? 582  ASP A C   1 
ATOM   4673 O  O   . ASP A 1 582  ? 66.236 71.406  -34.469 1.00 15.66 ? 582  ASP A O   1 
ATOM   4674 C  CB  . ASP A 1 582  ? 63.591 69.032  -34.697 1.00 16.39 ? 582  ASP A CB  1 
ATOM   4675 C  CG  . ASP A 1 582  ? 64.341 68.492  -35.908 1.00 15.64 ? 582  ASP A CG  1 
ATOM   4676 O  OD1 . ASP A 1 582  ? 65.417 69.029  -36.272 1.00 14.79 ? 582  ASP A OD1 1 
ATOM   4677 O  OD2 . ASP A 1 582  ? 63.796 67.494  -36.438 1.00 17.35 ? 582  ASP A OD2 1 
ATOM   4678 N  N   . LEU A 1 583  ? 66.186 69.646  -33.089 1.00 19.99 ? 583  LEU A N   1 
ATOM   4679 C  CA  . LEU A 1 583  ? 67.610 69.961  -32.887 1.00 21.48 ? 583  LEU A CA  1 
ATOM   4680 C  C   . LEU A 1 583  ? 68.525 69.458  -33.995 1.00 21.88 ? 583  LEU A C   1 
ATOM   4681 O  O   . LEU A 1 583  ? 69.747 69.681  -33.924 1.00 24.59 ? 583  LEU A O   1 
ATOM   4682 C  CB  . LEU A 1 583  ? 68.176 69.589  -31.478 1.00 21.76 ? 583  LEU A CB  1 
ATOM   4683 C  CG  . LEU A 1 583  ? 69.132 70.620  -30.765 1.00 20.90 ? 583  LEU A CG  1 
ATOM   4684 C  CD1 . LEU A 1 583  ? 68.521 72.011  -30.749 1.00 23.86 ? 583  LEU A CD1 1 
ATOM   4685 C  CD2 . LEU A 1 583  ? 69.402 70.236  -29.317 1.00 22.99 ? 583  LEU A CD2 1 
ATOM   4686 N  N   . ALA A 1 584  ? 67.963 68.805  -35.025 1.00 18.89 ? 584  ALA A N   1 
ATOM   4687 C  CA  . ALA A 1 584  ? 68.827 68.501  -36.185 1.00 16.61 ? 584  ALA A CA  1 
ATOM   4688 C  C   . ALA A 1 584  ? 68.624 69.646  -37.178 1.00 15.53 ? 584  ALA A C   1 
ATOM   4689 O  O   . ALA A 1 584  ? 69.036 69.542  -38.347 1.00 14.38 ? 584  ALA A O   1 
ATOM   4690 C  CB  . ALA A 1 584  ? 68.463 67.213  -36.844 1.00 15.80 ? 584  ALA A CB  1 
ATOM   4691 N  N   . ASN A 1 585  ? 67.976 70.727  -36.752 1.00 15.10 ? 585  ASN A N   1 
ATOM   4692 C  CA  . ASN A 1 585  ? 67.750 71.898  -37.615 1.00 15.85 ? 585  ASN A CA  1 
ATOM   4693 C  C   . ASN A 1 585  ? 66.726 71.663  -38.735 1.00 15.61 ? 585  ASN A C   1 
ATOM   4694 O  O   A ASN A 1 585  ? 66.605 72.432  -39.708 0.50 16.20 ? 585  ASN A O   1 
ATOM   4695 O  O   B ASN A 1 585  ? 66.917 72.278  -39.766 0.50 15.82 ? 585  ASN A O   1 
ATOM   4696 C  CB  . ASN A 1 585  ? 69.074 72.379  -38.224 1.00 18.18 ? 585  ASN A CB  1 
ATOM   4697 C  CG  A ASN A 1 585  ? 69.307 73.830  -37.993 0.50 20.22 ? 585  ASN A CG  1 
ATOM   4698 C  CG  B ASN A 1 585  ? 68.999 73.889  -38.494 0.50 17.58 ? 585  ASN A CG  1 
ATOM   4699 O  OD1 A ASN A 1 585  ? 68.383 74.643  -38.080 0.50 21.74 ? 585  ASN A OD1 1 
ATOM   4700 O  OD1 B ASN A 1 585  ? 68.450 74.728  -37.769 0.50 19.54 ? 585  ASN A OD1 1 
ATOM   4701 N  ND2 A ASN A 1 585  ? 70.550 74.182  -37.691 0.50 22.19 ? 585  ASN A ND2 1 
ATOM   4702 N  ND2 B ASN A 1 585  ? 69.543 74.201  -39.667 0.50 17.78 ? 585  ASN A ND2 1 
ATOM   4703 N  N   . ASN A 1 586  ? 65.957 70.606  -38.598 1.00 13.99 ? 586  ASN A N   1 
ATOM   4704 C  CA  . ASN A 1 586  ? 64.942 70.312  -39.621 1.00 14.93 ? 586  ASN A CA  1 
ATOM   4705 C  C   . ASN A 1 586  ? 63.778 71.288  -39.371 1.00 14.93 ? 586  ASN A C   1 
ATOM   4706 O  O   . ASN A 1 586  ? 63.316 71.455  -38.243 1.00 13.56 ? 586  ASN A O   1 
ATOM   4707 C  CB  . ASN A 1 586  ? 64.357 68.904  -39.495 1.00 16.32 ? 586  ASN A CB  1 
ATOM   4708 C  CG  . ASN A 1 586  ? 65.397 67.823  -39.610 1.00 16.18 ? 586  ASN A CG  1 
ATOM   4709 O  OD1 . ASN A 1 586  ? 66.282 67.891  -40.479 1.00 16.30 ? 586  ASN A OD1 1 
ATOM   4710 N  ND2 . ASN A 1 586  ? 65.317 66.810  -38.728 1.00 15.78 ? 586  ASN A ND2 1 
ATOM   4711 N  N   . PRO A 1 587  ? 63.282 71.966  -40.397 1.00 14.51 ? 587  PRO A N   1 
ATOM   4712 C  CA  . PRO A 1 587  ? 62.161 72.882  -40.167 1.00 14.62 ? 587  PRO A CA  1 
ATOM   4713 C  C   . PRO A 1 587  ? 60.924 72.112  -39.743 1.00 13.64 ? 587  PRO A C   1 
ATOM   4714 O  O   . PRO A 1 587  ? 60.694 70.968  -40.146 1.00 15.58 ? 587  PRO A O   1 
ATOM   4715 C  CB  . PRO A 1 587  ? 61.959 73.579  -41.511 1.00 15.93 ? 587  PRO A CB  1 
ATOM   4716 C  CG  . PRO A 1 587  ? 62.544 72.652  -42.485 1.00 18.90 ? 587  PRO A CG  1 
ATOM   4717 C  CD  . PRO A 1 587  ? 63.729 71.979  -41.807 1.00 16.07 ? 587  PRO A CD  1 
ATOM   4718 N  N   . VAL A 1 588  ? 60.102 72.740  -38.900 1.00 12.47 ? 588  VAL A N   1 
ATOM   4719 C  CA  . VAL A 1 588  ? 58.892 72.127  -38.413 1.00 12.04 ? 588  VAL A CA  1 
ATOM   4720 C  C   . VAL A 1 588  ? 57.779 73.125  -38.769 1.00 11.98 ? 588  VAL A C   1 
ATOM   4721 O  O   . VAL A 1 588  ? 57.904 74.335  -38.496 1.00 12.69 ? 588  VAL A O   1 
ATOM   4722 C  CB  . VAL A 1 588  ? 58.956 71.979  -36.855 1.00 11.98 ? 588  VAL A CB  1 
ATOM   4723 C  CG1 . VAL A 1 588  ? 57.651 71.498  -36.320 1.00 13.99 ? 588  VAL A CG1 1 
ATOM   4724 C  CG2 . VAL A 1 588  ? 60.136 71.042  -36.449 1.00 12.40 ? 588  VAL A CG2 1 
ATOM   4725 N  N   . GLU A 1 589  ? 56.703 72.631  -39.367 1.00 12.28 ? 589  GLU A N   1 
ATOM   4726 C  CA  . GLU A 1 589  ? 55.609 73.483  -39.769 1.00 12.83 ? 589  GLU A CA  1 
ATOM   4727 C  C   . GLU A 1 589  ? 54.972 74.128  -38.552 1.00 12.51 ? 589  GLU A C   1 
ATOM   4728 O  O   . GLU A 1 589  ? 54.742 73.436  -37.538 1.00 12.67 ? 589  GLU A O   1 
ATOM   4729 C  CB  . GLU A 1 589  ? 54.559 72.657  -40.489 1.00 16.05 ? 589  GLU A CB  1 
ATOM   4730 C  CG  . GLU A 1 589  ? 53.504 73.534  -41.043 1.00 22.34 ? 589  GLU A CG  1 
ATOM   4731 C  CD  . GLU A 1 589  ? 52.370 72.806  -41.715 1.00 25.09 ? 589  GLU A CD  1 
ATOM   4732 O  OE1 . GLU A 1 589  ? 52.469 71.560  -41.883 1.00 27.50 ? 589  GLU A OE1 1 
ATOM   4733 O  OE2 . GLU A 1 589  ? 51.367 73.503  -42.081 1.00 27.61 ? 589  GLU A OE2 1 
ATOM   4734 N  N   . ALA A 1 590  ? 54.664 75.417  -38.638 1.00 11.31 ? 590  ALA A N   1 
ATOM   4735 C  CA  . ALA A 1 590  ? 54.080 76.103  -37.493 1.00 10.84 ? 590  ALA A CA  1 
ATOM   4736 C  C   . ALA A 1 590  ? 52.991 77.045  -37.935 1.00 11.04 ? 590  ALA A C   1 
ATOM   4737 O  O   . ALA A 1 590  ? 52.922 77.417  -39.111 1.00 12.07 ? 590  ALA A O   1 
ATOM   4738 C  CB  . ALA A 1 590  ? 55.137 76.868  -36.768 1.00 11.46 ? 590  ALA A CB  1 
ATOM   4739 N  N   . GLN A 1 591  ? 52.169 77.438  -36.995 1.00 10.08 ? 591  GLN A N   1 
ATOM   4740 C  CA  . GLN A 1 591  ? 51.085 78.388  -37.235 1.00 9.96  ? 591  GLN A CA  1 
ATOM   4741 C  C   . GLN A 1 591  ? 51.156 79.469  -36.170 1.00 10.74 ? 591  GLN A C   1 
ATOM   4742 O  O   . GLN A 1 591  ? 51.392 79.180  -34.988 1.00 11.72 ? 591  GLN A O   1 
ATOM   4743 C  CB  . GLN A 1 591  ? 49.702 77.689  -37.162 1.00 10.74 ? 591  GLN A CB  1 
ATOM   4744 C  CG  . GLN A 1 591  ? 48.547 78.687  -37.142 1.00 11.80 ? 591  GLN A CG  1 
ATOM   4745 C  CD  . GLN A 1 591  ? 47.220 77.978  -36.898 1.00 11.16 ? 591  GLN A CD  1 
ATOM   4746 O  OE1 . GLN A 1 591  ? 46.993 76.912  -37.464 1.00 12.15 ? 591  GLN A OE1 1 
ATOM   4747 N  NE2 . GLN A 1 591  ? 46.366 78.545  -36.092 1.00 11.75 ? 591  GLN A NE2 1 
ATOM   4748 N  N   . VAL A 1 592  ? 50.978 80.726  -36.567 1.00 10.29 ? 592  VAL A N   1 
ATOM   4749 C  CA  . VAL A 1 592  ? 50.962 81.812  -35.616 1.00 10.48 ? 592  VAL A CA  1 
ATOM   4750 C  C   . VAL A 1 592  ? 49.560 82.376  -35.613 1.00 10.62 ? 592  VAL A C   1 
ATOM   4751 O  O   . VAL A 1 592  ? 48.927 82.527  -36.671 1.00 10.84 ? 592  VAL A O   1 
ATOM   4752 C  CB  . VAL A 1 592  ? 51.995 82.895  -35.980 1.00 11.43 ? 592  VAL A CB  1 
ATOM   4753 C  CG1 . VAL A 1 592  ? 51.771 84.171  -35.163 1.00 12.51 ? 592  VAL A CG1 1 
ATOM   4754 C  CG2 . VAL A 1 592  ? 53.402 82.369  -35.673 1.00 10.96 ? 592  VAL A CG2 1 
ATOM   4755 N  N   . SER A 1 593  ? 49.042 82.664  -34.430 1.00 11.61 ? 593  SER A N   1 
ATOM   4756 C  CA  . SER A 1 593  ? 47.708 83.241  -34.239 1.00 12.05 ? 593  SER A CA  1 
ATOM   4757 C  C   . SER A 1 593  ? 47.863 84.357  -33.252 1.00 12.55 ? 593  SER A C   1 
ATOM   4758 O  O   . SER A 1 593  ? 48.868 84.442  -32.510 1.00 13.76 ? 593  SER A O   1 
ATOM   4759 C  CB  . SER A 1 593  ? 46.739 82.215  -33.583 1.00 13.04 ? 593  SER A CB  1 
ATOM   4760 O  OG  . SER A 1 593  ? 46.535 81.057  -34.397 1.00 13.71 ? 593  SER A OG  1 
ATOM   4761 N  N   . PRO A 1 594  ? 46.878 85.234  -33.164 1.00 12.00 ? 594  PRO A N   1 
ATOM   4762 C  CA  . PRO A 1 594  ? 46.969 86.330  -32.188 1.00 11.32 ? 594  PRO A CA  1 
ATOM   4763 C  C   . PRO A 1 594  ? 46.726 85.796  -30.764 1.00 11.80 ? 594  PRO A C   1 
ATOM   4764 O  O   . PRO A 1 594  ? 46.298 84.635  -30.563 1.00 12.33 ? 594  PRO A O   1 
ATOM   4765 C  CB  . PRO A 1 594  ? 45.801 87.268  -32.566 1.00 12.24 ? 594  PRO A CB  1 
ATOM   4766 C  CG  . PRO A 1 594  ? 45.441 86.830  -34.014 1.00 12.15 ? 594  PRO A CG  1 
ATOM   4767 C  CD  . PRO A 1 594  ? 45.677 85.363  -34.023 1.00 11.37 ? 594  PRO A CD  1 
ATOM   4768 N  N   . VAL A 1 595  ? 47.000 86.650  -29.774 1.00 11.65 ? 595  VAL A N   1 
ATOM   4769 C  CA  . VAL A 1 595  ? 46.673 86.331  -28.400 1.00 11.75 ? 595  VAL A CA  1 
ATOM   4770 C  C   . VAL A 1 595  ? 45.408 87.140  -28.142 1.00 12.10 ? 595  VAL A C   1 
ATOM   4771 O  O   . VAL A 1 595  ? 45.433 88.381  -28.131 1.00 13.00 ? 595  VAL A O   1 
ATOM   4772 C  CB  . VAL A 1 595  ? 47.771 86.723  -27.407 1.00 12.34 ? 595  VAL A CB  1 
ATOM   4773 C  CG1 . VAL A 1 595  ? 47.261 86.464  -25.979 1.00 13.93 ? 595  VAL A CG1 1 
ATOM   4774 C  CG2 . VAL A 1 595  ? 49.004 85.846  -27.680 1.00 13.63 ? 595  VAL A CG2 1 
ATOM   4775 N  N   . TRP A 1 596  ? 44.294 86.436  -27.969 1.00 11.94 ? 596  TRP A N   1 
ATOM   4776 C  CA  . TRP A 1 596  ? 43.003 87.036  -27.732 1.00 12.93 ? 596  TRP A CA  1 
ATOM   4777 C  C   . TRP A 1 596  ? 42.570 86.935  -26.286 1.00 14.27 ? 596  TRP A C   1 
ATOM   4778 O  O   . TRP A 1 596  ? 42.667 85.858  -25.696 1.00 15.63 ? 596  TRP A O   1 
ATOM   4779 C  CB  . TRP A 1 596  ? 41.929 86.328  -28.585 1.00 13.01 ? 596  TRP A CB  1 
ATOM   4780 C  CG  . TRP A 1 596  ? 42.068 86.518  -30.056 1.00 12.14 ? 596  TRP A CG  1 
ATOM   4781 C  CD1 . TRP A 1 596  ? 42.470 85.585  -30.995 1.00 12.30 ? 596  TRP A CD1 1 
ATOM   4782 C  CD2 . TRP A 1 596  ? 41.760 87.703  -30.789 1.00 11.78 ? 596  TRP A CD2 1 
ATOM   4783 N  NE1 . TRP A 1 596  ? 42.417 86.133  -32.266 1.00 12.32 ? 596  TRP A NE1 1 
ATOM   4784 C  CE2 . TRP A 1 596  ? 41.994 87.427  -32.158 1.00 12.15 ? 596  TRP A CE2 1 
ATOM   4785 C  CE3 . TRP A 1 596  ? 41.309 88.991  -30.419 1.00 12.66 ? 596  TRP A CE3 1 
ATOM   4786 C  CZ2 . TRP A 1 596  ? 41.801 88.375  -33.148 1.00 13.43 ? 596  TRP A CZ2 1 
ATOM   4787 C  CZ3 . TRP A 1 596  ? 41.120 89.940  -31.437 1.00 14.11 ? 596  TRP A CZ3 1 
ATOM   4788 C  CH2 . TRP A 1 596  ? 41.364 89.619  -32.763 1.00 14.71 ? 596  TRP A CH2 1 
ATOM   4789 N  N   . SER A 1 597  ? 42.121 88.032  -25.700 1.00 14.72 ? 597  SER A N   1 
ATOM   4790 C  CA  . SER A 1 597  ? 41.603 87.985  -24.349 1.00 15.93 ? 597  SER A CA  1 
ATOM   4791 C  C   . SER A 1 597  ? 40.203 88.591  -24.416 1.00 15.95 ? 597  SER A C   1 
ATOM   4792 O  O   . SER A 1 597  ? 39.928 89.486  -25.230 1.00 18.16 ? 597  SER A O   1 
ATOM   4793 C  CB  A SER A 1 597  ? 42.481 88.785  -23.391 0.50 15.72 ? 597  SER A CB  1 
ATOM   4794 C  CB  B SER A 1 597  ? 42.515 89.171  -23.596 0.50 15.42 ? 597  SER A CB  1 
ATOM   4795 O  OG  A SER A 1 597  ? 42.630 90.104  -23.857 0.50 15.98 ? 597  SER A OG  1 
ATOM   4796 O  OG  B SER A 1 597  ? 43.892 88.840  -23.705 0.50 16.70 ? 597  SER A OG  1 
ATOM   4797 N  N   . TRP A 1 598  ? 39.332 88.108  -23.556 1.00 15.78 ? 598  TRP A N   1 
ATOM   4798 C  CA  . TRP A 1 598  ? 37.942 88.555  -23.528 1.00 15.69 ? 598  TRP A CA  1 
ATOM   4799 C  C   . TRP A 1 598  ? 37.708 89.501  -22.362 1.00 18.49 ? 598  TRP A C   1 
ATOM   4800 O  O   . TRP A 1 598  ? 38.180 89.263  -21.270 1.00 19.20 ? 598  TRP A O   1 
ATOM   4801 C  CB  . TRP A 1 598  ? 37.008 87.337  -23.424 1.00 15.59 ? 598  TRP A CB  1 
ATOM   4802 C  CG  . TRP A 1 598  ? 36.960 86.587  -24.709 1.00 13.03 ? 598  TRP A CG  1 
ATOM   4803 C  CD1 . TRP A 1 598  ? 37.866 85.684  -25.172 1.00 12.12 ? 598  TRP A CD1 1 
ATOM   4804 C  CD2 . TRP A 1 598  ? 35.952 86.694  -25.702 1.00 12.62 ? 598  TRP A CD2 1 
ATOM   4805 N  NE1 . TRP A 1 598  ? 37.500 85.224  -26.398 1.00 12.13 ? 598  TRP A NE1 1 
ATOM   4806 C  CE2 . TRP A 1 598  ? 36.314 85.808  -26.753 1.00 11.43 ? 598  TRP A CE2 1 
ATOM   4807 C  CE3 . TRP A 1 598  ? 34.768 87.439  -25.811 1.00 12.41 ? 598  TRP A CE3 1 
ATOM   4808 C  CZ2 . TRP A 1 598  ? 35.522 85.644  -27.903 1.00 12.04 ? 598  TRP A CZ2 1 
ATOM   4809 C  CZ3 . TRP A 1 598  ? 33.977 87.274  -26.959 1.00 12.17 ? 598  TRP A CZ3 1 
ATOM   4810 C  CH2 . TRP A 1 598  ? 34.365 86.374  -27.992 1.00 12.62 ? 598  TRP A CH2 1 
ATOM   4811 N  N   . HIS A 1 599  ? 36.969 90.558  -22.614 1.00 21.03 ? 599  HIS A N   1 
ATOM   4812 C  CA  . HIS A 1 599  ? 36.752 91.547  -21.589 1.00 24.77 ? 599  HIS A CA  1 
ATOM   4813 C  C   . HIS A 1 599  ? 35.297 91.879  -21.479 1.00 26.14 ? 599  HIS A C   1 
ATOM   4814 O  O   . HIS A 1 599  ? 34.597 91.954  -22.498 1.00 24.70 ? 599  HIS A O   1 
ATOM   4815 C  CB  . HIS A 1 599  ? 37.525 92.816  -21.936 1.00 27.44 ? 599  HIS A CB  1 
ATOM   4816 C  CG  . HIS A 1 599  ? 39.009 92.609  -22.000 1.00 30.37 ? 599  HIS A CG  1 
ATOM   4817 N  ND1 . HIS A 1 599  ? 39.760 92.241  -20.903 1.00 31.53 ? 599  HIS A ND1 1 
ATOM   4818 C  CD2 . HIS A 1 599  ? 39.863 92.613  -23.053 1.00 31.74 ? 599  HIS A CD2 1 
ATOM   4819 C  CE1 . HIS A 1 599  ? 41.006 92.015  -21.280 1.00 31.97 ? 599  HIS A CE1 1 
ATOM   4820 N  NE2 . HIS A 1 599  ? 41.095 92.232  -22.579 1.00 32.30 ? 599  HIS A NE2 1 
ATOM   4821 N  N   . HIS A 1 600  ? 34.822 92.049  -20.248 1.00 29.26 ? 600  HIS A N   1 
ATOM   4822 C  CA  . HIS A 1 600  ? 33.438 92.453  -20.095 1.00 32.61 ? 600  HIS A CA  1 
ATOM   4823 C  C   . HIS A 1 600  ? 33.553 93.955  -20.071 1.00 33.25 ? 600  HIS A C   1 
ATOM   4824 O  O   . HIS A 1 600  ? 34.003 94.524  -19.077 1.00 33.89 ? 600  HIS A O   1 
ATOM   4825 C  CB  . HIS A 1 600  ? 32.781 92.003  -18.788 1.00 35.43 ? 600  HIS A CB  1 
ATOM   4826 C  CG  . HIS A 1 600  ? 31.437 92.643  -18.579 1.00 38.55 ? 600  HIS A CG  1 
ATOM   4827 N  ND1 . HIS A 1 600  ? 30.442 92.599  -19.538 1.00 39.95 ? 600  HIS A ND1 1 
ATOM   4828 C  CD2 . HIS A 1 600  ? 30.962 93.436  -17.586 1.00 39.87 ? 600  HIS A CD2 1 
ATOM   4829 C  CE1 . HIS A 1 600  ? 29.418 93.338  -19.149 1.00 40.54 ? 600  HIS A CE1 1 
ATOM   4830 N  NE2 . HIS A 1 600  ? 29.707 93.859  -17.968 1.00 40.58 ? 600  HIS A NE2 1 
ATOM   4831 N  N   . ASP A 1 601  ? 33.169 94.575  -21.179 1.00 34.01 ? 601  ASP A N   1 
ATOM   4832 C  CA  . ASP A 1 601  ? 33.229 96.014  -21.359 1.00 35.29 ? 601  ASP A CA  1 
ATOM   4833 C  C   . ASP A 1 601  ? 32.073 96.661  -20.578 1.00 36.02 ? 601  ASP A C   1 
ATOM   4834 O  O   . ASP A 1 601  ? 30.923 96.525  -20.967 1.00 35.50 ? 601  ASP A O   1 
ATOM   4835 C  CB  . ASP A 1 601  ? 33.088 96.314  -22.848 1.00 35.64 ? 601  ASP A CB  1 
ATOM   4836 C  CG  . ASP A 1 601  ? 33.433 97.746  -23.200 1.00 36.61 ? 601  ASP A CG  1 
ATOM   4837 O  OD1 . ASP A 1 601  ? 33.235 98.647  -22.353 1.00 36.29 ? 601  ASP A OD1 1 
ATOM   4838 O  OD2 . ASP A 1 601  ? 33.884 97.979  -24.350 1.00 36.99 ? 601  ASP A OD2 1 
ATOM   4839 N  N   . THR A 1 602  ? 32.365 97.347  -19.479 1.00 37.25 ? 602  THR A N   1 
ATOM   4840 C  CA  . THR A 1 602  ? 31.287 97.987  -18.717 1.00 38.56 ? 602  THR A CA  1 
ATOM   4841 C  C   . THR A 1 602  ? 30.749 99.204  -19.449 1.00 38.21 ? 602  THR A C   1 
ATOM   4842 O  O   . THR A 1 602  ? 29.589 99.603  -19.243 1.00 39.17 ? 602  THR A O   1 
ATOM   4843 C  CB  . THR A 1 602  ? 31.746 98.419  -17.324 1.00 39.65 ? 602  THR A CB  1 
ATOM   4844 O  OG1 . THR A 1 602  ? 32.926 99.231  -17.441 1.00 40.91 ? 602  THR A OG1 1 
ATOM   4845 C  CG2 . THR A 1 602  ? 32.013 97.190  -16.453 1.00 40.58 ? 602  THR A CG2 1 
ATOM   4846 N  N   . LEU A 1 603  ? 31.561 99.792  -20.319 1.00 37.19 ? 603  LEU A N   1 
ATOM   4847 C  CA  . LEU A 1 603  ? 31.086 100.944 -21.063 1.00 36.19 ? 603  LEU A CA  1 
ATOM   4848 C  C   . LEU A 1 603  ? 30.000 100.559 -22.053 1.00 34.34 ? 603  LEU A C   1 
ATOM   4849 O  O   . LEU A 1 603  ? 28.913 101.136 -22.049 1.00 35.02 ? 603  LEU A O   1 
ATOM   4850 C  CB  . LEU A 1 603  ? 32.233 101.660 -21.800 1.00 37.78 ? 603  LEU A CB  1 
ATOM   4851 C  CG  . LEU A 1 603  ? 33.220 102.458 -20.928 1.00 38.88 ? 603  LEU A CG  1 
ATOM   4852 C  CD1 . LEU A 1 603  ? 32.449 103.199 -19.811 1.00 39.69 ? 603  LEU A CD1 1 
ATOM   4853 C  CD2 . LEU A 1 603  ? 34.248 101.521 -20.312 1.00 39.81 ? 603  LEU A CD2 1 
ATOM   4854 N  N   . THR A 1 604  ? 30.271 99.561  -22.883 1.00 31.04 ? 604  THR A N   1 
ATOM   4855 C  CA  . THR A 1 604  ? 29.313 99.112  -23.886 1.00 27.90 ? 604  THR A CA  1 
ATOM   4856 C  C   . THR A 1 604  ? 28.376 97.995  -23.397 1.00 25.02 ? 604  THR A C   1 
ATOM   4857 O  O   . THR A 1 604  ? 27.409 97.670  -24.083 1.00 23.46 ? 604  THR A O   1 
ATOM   4858 C  CB  . THR A 1 604  ? 30.045 98.593  -25.123 1.00 28.24 ? 604  THR A CB  1 
ATOM   4859 O  OG1 . THR A 1 604  ? 30.935 97.527  -24.723 1.00 28.57 ? 604  THR A OG1 1 
ATOM   4860 C  CG2 . THR A 1 604  ? 30.860 99.726  -25.773 1.00 28.98 ? 604  THR A CG2 1 
ATOM   4861 N  N   . LYS A 1 605  ? 28.656 97.442  -22.221 1.00 23.25 ? 605  LYS A N   1 
ATOM   4862 C  CA  . LYS A 1 605  ? 27.854 96.337  -21.660 1.00 22.27 ? 605  LYS A CA  1 
ATOM   4863 C  C   . LYS A 1 605  ? 27.873 95.147  -22.609 1.00 21.91 ? 605  LYS A C   1 
ATOM   4864 O  O   . LYS A 1 605  ? 26.841 94.579  -22.919 1.00 22.58 ? 605  LYS A O   1 
ATOM   4865 C  CB  . LYS A 1 605  ? 26.387 96.743  -21.415 1.00 22.60 ? 605  LYS A CB  1 
ATOM   4866 C  CG  . LYS A 1 605  ? 26.222 97.849  -20.419 1.00 23.88 ? 605  LYS A CG  1 
ATOM   4867 C  CD  . LYS A 1 605  ? 26.777 97.446  -19.067 1.00 24.78 ? 605  LYS A CD  1 
ATOM   4868 C  CE  . LYS A 1 605  ? 26.677 98.612  -18.066 1.00 26.06 ? 605  LYS A CE  1 
ATOM   4869 N  NZ  . LYS A 1 605  ? 27.091 98.145  -16.725 1.00 28.55 ? 605  LYS A NZ  1 
ATOM   4870 N  N   . THR A 1 606  ? 29.049 94.815  -23.121 1.00 20.19 ? 606  THR A N   1 
ATOM   4871 C  CA  . THR A 1 606  ? 29.190 93.649  -24.015 1.00 19.60 ? 606  THR A CA  1 
ATOM   4872 C  C   . THR A 1 606  ? 30.438 92.920  -23.590 1.00 19.13 ? 606  THR A C   1 
ATOM   4873 O  O   . THR A 1 606  ? 31.313 93.482  -22.940 1.00 19.69 ? 606  THR A O   1 
ATOM   4874 C  CB  . THR A 1 606  ? 29.428 94.046  -25.479 1.00 20.61 ? 606  THR A CB  1 
ATOM   4875 O  OG1 . THR A 1 606  ? 30.600 94.882  -25.552 1.00 23.02 ? 606  THR A OG1 1 
ATOM   4876 C  CG2 . THR A 1 606  ? 28.204 94.722  -26.060 1.00 21.28 ? 606  THR A CG2 1 
ATOM   4877 N  N   . ILE A 1 607  ? 30.508 91.643  -23.955 1.00 17.65 ? 607  ILE A N   1 
ATOM   4878 C  CA  . ILE A 1 607  ? 31.682 90.809  -23.696 1.00 16.51 ? 607  ILE A CA  1 
ATOM   4879 C  C   . ILE A 1 607  ? 32.356 90.612  -25.070 1.00 15.85 ? 607  ILE A C   1 
ATOM   4880 O  O   . ILE A 1 607  ? 31.782 90.030  -25.990 1.00 15.98 ? 607  ILE A O   1 
ATOM   4881 C  CB  . ILE A 1 607  ? 31.237 89.497  -23.134 1.00 15.96 ? 607  ILE A CB  1 
ATOM   4882 C  CG1 . ILE A 1 607  ? 30.422 89.769  -21.863 1.00 17.53 ? 607  ILE A CG1 1 
ATOM   4883 C  CG2 . ILE A 1 607  ? 32.462 88.633  -22.814 1.00 17.34 ? 607  ILE A CG2 1 
ATOM   4884 C  CD1 . ILE A 1 607  ? 29.758 88.573  -21.275 1.00 19.66 ? 607  ILE A CD1 1 
ATOM   4885 N  N   . HIS A 1 608  ? 33.594 91.088  -25.223 1.00 15.99 ? 608  HIS A N   1 
ATOM   4886 C  CA  . HIS A 1 608  ? 34.204 90.998  -26.534 1.00 16.29 ? 608  HIS A CA  1 
ATOM   4887 C  C   . HIS A 1 608  ? 35.701 90.795  -26.413 1.00 15.22 ? 608  HIS A C   1 
ATOM   4888 O  O   . HIS A 1 608  ? 36.286 91.081  -25.373 1.00 16.96 ? 608  HIS A O   1 
ATOM   4889 C  CB  . HIS A 1 608  ? 33.842 92.247  -27.366 1.00 20.07 ? 608  HIS A CB  1 
ATOM   4890 C  CG  . HIS A 1 608  ? 34.427 93.515  -26.847 1.00 23.28 ? 608  HIS A CG  1 
ATOM   4891 N  ND1 . HIS A 1 608  ? 34.153 94.023  -25.594 1.00 26.33 ? 608  HIS A ND1 1 
ATOM   4892 C  CD2 . HIS A 1 608  ? 35.299 94.379  -27.419 1.00 26.06 ? 608  HIS A CD2 1 
ATOM   4893 C  CE1 . HIS A 1 608  ? 34.832 95.145  -25.413 1.00 26.61 ? 608  HIS A CE1 1 
ATOM   4894 N  NE2 . HIS A 1 608  ? 35.537 95.383  -26.506 1.00 27.02 ? 608  HIS A NE2 1 
ATOM   4895 N  N   . PRO A 1 609  ? 36.338 90.346  -27.493 1.00 14.51 ? 609  PRO A N   1 
ATOM   4896 C  CA  . PRO A 1 609  ? 37.771 90.069  -27.482 1.00 14.95 ? 609  PRO A CA  1 
ATOM   4897 C  C   . PRO A 1 609  ? 38.662 91.213  -27.912 1.00 15.84 ? 609  PRO A C   1 
ATOM   4898 O  O   . PRO A 1 609  ? 38.274 91.987  -28.791 1.00 17.86 ? 609  PRO A O   1 
ATOM   4899 C  CB  . PRO A 1 609  ? 37.867 88.879  -28.453 1.00 14.86 ? 609  PRO A CB  1 
ATOM   4900 C  CG  . PRO A 1 609  ? 36.865 89.267  -29.531 1.00 15.24 ? 609  PRO A CG  1 
ATOM   4901 C  CD  . PRO A 1 609  ? 35.724 89.942  -28.777 1.00 14.20 ? 609  PRO A CD  1 
ATOM   4902 N  N   . GLN A 1 610  ? 39.836 91.287  -27.286 1.00 16.04 ? 610  GLN A N   1 
ATOM   4903 C  CA  . GLN A 1 610  ? 40.871 92.262  -27.605 1.00 17.28 ? 610  GLN A CA  1 
ATOM   4904 C  C   . GLN A 1 610  ? 42.109 91.452  -27.971 1.00 15.24 ? 610  GLN A C   1 
ATOM   4905 O  O   . GLN A 1 610  ? 42.388 90.446  -27.334 1.00 15.75 ? 610  GLN A O   1 
ATOM   4906 C  CB  . GLN A 1 610  ? 41.165 93.143  -26.389 1.00 20.90 ? 610  GLN A CB  1 
ATOM   4907 C  CG  . GLN A 1 610  ? 39.905 93.917  -25.947 1.00 27.10 ? 610  GLN A CG  1 
ATOM   4908 C  CD  . GLN A 1 610  ? 39.568 95.128  -26.824 1.00 30.85 ? 610  GLN A CD  1 
ATOM   4909 O  OE1 . GLN A 1 610  ? 39.151 95.004  -28.003 1.00 32.69 ? 610  GLN A OE1 1 
ATOM   4910 N  NE2 . GLN A 1 610  ? 39.743 96.327  -26.236 1.00 32.93 ? 610  GLN A NE2 1 
ATOM   4911 N  N   . GLY A 1 611  ? 42.796 91.868  -29.012 1.00 14.65 ? 611  GLY A N   1 
ATOM   4912 C  CA  . GLY A 1 611  ? 43.995 91.153  -29.414 1.00 14.94 ? 611  GLY A CA  1 
ATOM   4913 C  C   . GLY A 1 611  ? 45.224 91.895  -28.970 1.00 15.46 ? 611  GLY A C   1 
ATOM   4914 O  O   . GLY A 1 611  ? 45.242 93.132  -28.905 1.00 15.75 ? 611  GLY A O   1 
ATOM   4915 N  N   . SER A 1 612  ? 46.260 91.124  -28.657 1.00 15.02 ? 612  SER A N   1 
ATOM   4916 C  CA  . SER A 1 612  ? 47.520 91.748  -28.257 1.00 15.54 ? 612  SER A CA  1 
ATOM   4917 C  C   . SER A 1 612  ? 48.231 92.344  -29.441 1.00 15.64 ? 612  SER A C   1 
ATOM   4918 O  O   . SER A 1 612  ? 48.189 91.815  -30.535 1.00 16.05 ? 612  SER A O   1 
ATOM   4919 C  CB  . SER A 1 612  ? 48.445 90.703  -27.630 1.00 14.71 ? 612  SER A CB  1 
ATOM   4920 O  OG  . SER A 1 612  ? 49.671 91.312  -27.294 1.00 16.72 ? 612  SER A OG  1 
ATOM   4921 N  N   . THR A 1 613  ? 48.930 93.461  -29.219 1.00 18.67 ? 613  THR A N   1 
ATOM   4922 C  CA  . THR A 1 613  ? 49.691 94.023  -30.310 1.00 18.86 ? 613  THR A CA  1 
ATOM   4923 C  C   . THR A 1 613  ? 51.189 93.792  -30.048 1.00 19.68 ? 613  THR A C   1 
ATOM   4924 O  O   . THR A 1 613  ? 52.028 94.261  -30.827 1.00 21.59 ? 613  THR A O   1 
ATOM   4925 C  CB  . THR A 1 613  ? 49.450 95.511  -30.484 1.00 21.08 ? 613  THR A CB  1 
ATOM   4926 O  OG1 . THR A 1 613  ? 49.832 96.177  -29.283 1.00 21.29 ? 613  THR A OG1 1 
ATOM   4927 C  CG2 . THR A 1 613  ? 47.967 95.785  -30.741 1.00 20.16 ? 613  THR A CG2 1 
ATOM   4928 N  N   . THR A 1 614  ? 51.510 93.063  -28.978 1.00 19.45 ? 614  THR A N   1 
ATOM   4929 C  CA  . THR A 1 614  ? 52.920 92.791  -28.668 1.00 20.36 ? 614  THR A CA  1 
ATOM   4930 C  C   . THR A 1 614  ? 53.320 91.316  -28.466 1.00 19.70 ? 614  THR A C   1 
ATOM   4931 O  O   . THR A 1 614  ? 54.517 91.004  -28.338 1.00 19.69 ? 614  THR A O   1 
ATOM   4932 C  CB  . THR A 1 614  ? 53.334 93.532  -27.430 1.00 21.49 ? 614  THR A CB  1 
ATOM   4933 O  OG1 . THR A 1 614  ? 52.474 93.182  -26.355 1.00 23.91 ? 614  THR A OG1 1 
ATOM   4934 C  CG2 . THR A 1 614  ? 53.351 95.057  -27.692 1.00 23.47 ? 614  THR A CG2 1 
ATOM   4935 N  N   . LYS A 1 615  ? 52.350 90.411  -28.373 1.00 17.38 ? 615  LYS A N   1 
ATOM   4936 C  CA  . LYS A 1 615  ? 52.680 89.004  -28.242 1.00 15.94 ? 615  LYS A CA  1 
ATOM   4937 C  C   . LYS A 1 615  ? 51.725 88.210  -29.101 1.00 14.38 ? 615  LYS A C   1 
ATOM   4938 O  O   . LYS A 1 615  ? 50.613 88.639  -29.383 1.00 14.27 ? 615  LYS A O   1 
ATOM   4939 C  CB  . LYS A 1 615  ? 52.711 88.520  -26.793 1.00 18.16 ? 615  LYS A CB  1 
ATOM   4940 C  CG  . LYS A 1 615  ? 51.408 88.504  -26.070 1.00 20.13 ? 615  LYS A CG  1 
ATOM   4941 C  CD  . LYS A 1 615  ? 51.640 88.140  -24.577 1.00 23.00 ? 615  LYS A CD  1 
ATOM   4942 C  CE  . LYS A 1 615  ? 50.340 87.898  -23.872 1.00 23.08 ? 615  LYS A CE  1 
ATOM   4943 N  NZ  . LYS A 1 615  ? 50.542 88.046  -22.399 1.00 26.58 ? 615  LYS A NZ  1 
ATOM   4944 N  N   . TYR A 1 616  ? 52.202 87.041  -29.523 1.00 11.88 ? 616  TYR A N   1 
ATOM   4945 C  CA  . TYR A 1 616  ? 51.510 86.165  -30.440 1.00 12.09 ? 616  TYR A CA  1 
ATOM   4946 C  C   . TYR A 1 616  ? 51.678 84.733  -30.021 1.00 11.35 ? 616  TYR A C   1 
ATOM   4947 O  O   . TYR A 1 616  ? 52.584 84.413  -29.255 1.00 12.27 ? 616  TYR A O   1 
ATOM   4948 C  CB  . TYR A 1 616  ? 52.146 86.381  -31.847 1.00 12.42 ? 616  TYR A CB  1 
ATOM   4949 C  CG  . TYR A 1 616  ? 52.185 87.840  -32.216 1.00 14.99 ? 616  TYR A CG  1 
ATOM   4950 C  CD1 . TYR A 1 616  ? 51.043 88.438  -32.780 1.00 14.72 ? 616  TYR A CD1 1 
ATOM   4951 C  CD2 . TYR A 1 616  ? 53.285 88.640  -31.888 1.00 15.37 ? 616  TYR A CD2 1 
ATOM   4952 C  CE1 . TYR A 1 616  ? 50.985 89.776  -32.981 1.00 18.68 ? 616  TYR A CE1 1 
ATOM   4953 C  CE2 . TYR A 1 616  ? 53.247 90.023  -32.108 1.00 17.56 ? 616  TYR A CE2 1 
ATOM   4954 C  CZ  . TYR A 1 616  ? 52.093 90.564  -32.642 1.00 18.10 ? 616  TYR A CZ  1 
ATOM   4955 O  OH  . TYR A 1 616  ? 51.997 91.935  -32.861 1.00 23.08 ? 616  TYR A OH  1 
ATOM   4956 N  N   . ARG A 1 617  ? 50.799 83.867  -30.499 1.00 11.29 ? 617  ARG A N   1 
ATOM   4957 C  CA  . ARG A 1 617  ? 50.895 82.461  -30.172 1.00 12.10 ? 617  ARG A CA  1 
ATOM   4958 C  C   . ARG A 1 617  ? 51.518 81.695  -31.330 1.00 12.12 ? 617  ARG A C   1 
ATOM   4959 O  O   . ARG A 1 617  ? 51.021 81.841  -32.450 1.00 13.41 ? 617  ARG A O   1 
ATOM   4960 C  CB  . ARG A 1 617  ? 49.509 81.862  -29.961 1.00 14.69 ? 617  ARG A CB  1 
ATOM   4961 C  CG  . ARG A 1 617  ? 48.813 82.263  -28.707 1.00 17.94 ? 617  ARG A CG  1 
ATOM   4962 C  CD  . ARG A 1 617  ? 47.416 81.555  -28.579 1.00 18.73 ? 617  ARG A CD  1 
ATOM   4963 N  NE  . ARG A 1 617  ? 47.482 80.096  -28.631 1.00 18.46 ? 617  ARG A NE  1 
ATOM   4964 C  CZ  . ARG A 1 617  ? 46.821 79.336  -29.510 1.00 19.94 ? 617  ARG A CZ  1 
ATOM   4965 N  NH1 . ARG A 1 617  ? 46.023 79.901  -30.428 1.00 18.60 ? 617  ARG A NH1 1 
ATOM   4966 N  NH2 . ARG A 1 617  ? 46.960 78.025  -29.501 1.00 19.54 ? 617  ARG A NH2 1 
ATOM   4967 N  N   . ILE A 1 618  ? 52.555 80.883  -31.095 1.00 11.10 ? 618  ILE A N   1 
ATOM   4968 C  CA  . ILE A 1 618  ? 53.107 80.018  -32.123 1.00 11.85 ? 618  ILE A CA  1 
ATOM   4969 C  C   . ILE A 1 618  ? 52.737 78.608  -31.744 1.00 10.88 ? 618  ILE A C   1 
ATOM   4970 O  O   . ILE A 1 618  ? 52.878 78.221  -30.596 1.00 11.37 ? 618  ILE A O   1 
ATOM   4971 C  CB  . ILE A 1 618  ? 54.607 80.212  -32.369 1.00 11.86 ? 618  ILE A CB  1 
ATOM   4972 C  CG1 . ILE A 1 618  ? 54.978 79.407  -33.622 1.00 13.53 ? 618  ILE A CG1 1 
ATOM   4973 C  CG2 . ILE A 1 618  ? 55.455 79.878  -31.124 1.00 12.68 ? 618  ILE A CG2 1 
ATOM   4974 C  CD1 . ILE A 1 618  ? 56.231 79.836  -34.308 1.00 13.34 ? 618  ILE A CD1 1 
ATOM   4975 N  N   . ILE A 1 619  ? 52.299 77.825  -32.710 1.00 10.96 ? 619  ILE A N   1 
ATOM   4976 C  CA  . ILE A 1 619  ? 51.777 76.468  -32.501 1.00 10.46 ? 619  ILE A CA  1 
ATOM   4977 C  C   . ILE A 1 619  ? 52.473 75.536  -33.466 1.00 10.03 ? 619  ILE A C   1 
ATOM   4978 O  O   . ILE A 1 619  ? 52.663 75.863  -34.648 1.00 10.76 ? 619  ILE A O   1 
ATOM   4979 C  CB  . ILE A 1 619  ? 50.268 76.463  -32.865 1.00 13.42 ? 619  ILE A CB  1 
ATOM   4980 C  CG1 . ILE A 1 619  ? 49.548 77.488  -32.003 1.00 15.14 ? 619  ILE A CG1 1 
ATOM   4981 C  CG2 . ILE A 1 619  ? 49.642 75.104  -32.795 1.00 16.03 ? 619  ILE A CG2 1 
ATOM   4982 C  CD1 . ILE A 1 619  ? 48.472 78.285  -32.849 1.00 15.94 ? 619  ILE A CD1 1 
ATOM   4983 N  N   . PHE A 1 620  ? 52.872 74.372  -33.012 1.00 9.60  ? 620  PHE A N   1 
ATOM   4984 C  CA  . PHE A 1 620  ? 53.533 73.401  -33.888 1.00 9.86  ? 620  PHE A CA  1 
ATOM   4985 C  C   . PHE A 1 620  ? 53.412 72.029  -33.278 1.00 9.36  ? 620  PHE A C   1 
ATOM   4986 O  O   . PHE A 1 620  ? 53.135 71.886  -32.080 1.00 9.96  ? 620  PHE A O   1 
ATOM   4987 C  CB  . PHE A 1 620  ? 55.033 73.745  -34.109 1.00 9.33  ? 620  PHE A CB  1 
ATOM   4988 C  CG  . PHE A 1 620  ? 55.877 73.685  -32.854 1.00 9.23  ? 620  PHE A CG  1 
ATOM   4989 C  CD1 . PHE A 1 620  ? 56.017 74.813  -32.044 1.00 10.16 ? 620  PHE A CD1 1 
ATOM   4990 C  CD2 . PHE A 1 620  ? 56.569 72.491  -32.526 1.00 10.58 ? 620  PHE A CD2 1 
ATOM   4991 C  CE1 . PHE A 1 620  ? 56.872 74.751  -30.889 1.00 10.71 ? 620  PHE A CE1 1 
ATOM   4992 C  CE2 . PHE A 1 620  ? 57.417 72.455  -31.369 1.00 9.81  ? 620  PHE A CE2 1 
ATOM   4993 C  CZ  . PHE A 1 620  ? 57.544 73.585  -30.595 1.00 11.11 ? 620  PHE A CZ  1 
ATOM   4994 N  N   . LYS A 1 621  ? 53.629 71.015  -34.090 1.00 9.87  ? 621  LYS A N   1 
ATOM   4995 C  CA  . LYS A 1 621  ? 53.564 69.655  -33.583 1.00 11.47 ? 621  LYS A CA  1 
ATOM   4996 C  C   . LYS A 1 621  ? 54.878 69.185  -32.989 1.00 11.14 ? 621  LYS A C   1 
ATOM   4997 O  O   . LYS A 1 621  ? 55.916 69.207  -33.642 1.00 12.84 ? 621  LYS A O   1 
ATOM   4998 C  CB  . LYS A 1 621  ? 53.140 68.718  -34.752 1.00 13.14 ? 621  LYS A CB  1 
ATOM   4999 C  CG  . LYS A 1 621  ? 52.762 67.339  -34.276 1.00 17.66 ? 621  LYS A CG  1 
ATOM   5000 C  CD  . LYS A 1 621  ? 51.802 66.641  -35.226 1.00 22.47 ? 621  LYS A CD  1 
ATOM   5001 C  CE  . LYS A 1 621  ? 52.397 66.568  -36.608 1.00 24.15 ? 621  LYS A CE  1 
ATOM   5002 N  NZ  . LYS A 1 621  ? 51.545 65.688  -37.519 1.00 26.72 ? 621  LYS A NZ  1 
ATOM   5003 N  N   . ALA A 1 622  ? 54.829 68.801  -31.705 1.00 10.84 ? 622  ALA A N   1 
ATOM   5004 C  CA  . ALA A 1 622  ? 55.985 68.230  -31.055 1.00 10.23 ? 622  ALA A CA  1 
ATOM   5005 C  C   . ALA A 1 622  ? 55.885 66.701  -31.046 1.00 10.64 ? 622  ALA A C   1 
ATOM   5006 O  O   . ALA A 1 622  ? 54.835 66.166  -30.754 1.00 12.67 ? 622  ALA A O   1 
ATOM   5007 C  CB  . ALA A 1 622  ? 56.084 68.722  -29.585 1.00 11.09 ? 622  ALA A CB  1 
ATOM   5008 N  N   . ARG A 1 623  ? 56.969 66.031  -31.416 1.00 9.54  ? 623  ARG A N   1 
ATOM   5009 C  CA  . ARG A 1 623  ? 57.025 64.554  -31.399 1.00 10.24 ? 623  ARG A CA  1 
ATOM   5010 C  C   . ARG A 1 623  ? 58.003 64.167  -30.309 1.00 8.88  ? 623  ARG A C   1 
ATOM   5011 O  O   . ARG A 1 623  ? 59.171 64.551  -30.320 1.00 11.46 ? 623  ARG A O   1 
ATOM   5012 C  CB  . ARG A 1 623  ? 57.464 64.068  -32.775 1.00 12.19 ? 623  ARG A CB  1 
ATOM   5013 C  CG  . ARG A 1 623  ? 57.632 62.571  -32.848 1.00 13.62 ? 623  ARG A CG  1 
ATOM   5014 C  CD  . ARG A 1 623  ? 57.887 62.084  -34.316 1.00 16.51 ? 623  ARG A CD  1 
ATOM   5015 N  NE  . ARG A 1 623  ? 57.951 60.621  -34.292 1.00 21.02 ? 623  ARG A NE  1 
ATOM   5016 C  CZ  . ARG A 1 623  ? 59.099 59.961  -34.161 1.00 21.75 ? 623  ARG A CZ  1 
ATOM   5017 N  NH1 . ARG A 1 623  ? 60.251 60.621  -34.075 1.00 24.55 ? 623  ARG A NH1 1 
ATOM   5018 N  NH2 . ARG A 1 623  ? 59.092 58.640  -34.026 1.00 23.96 ? 623  ARG A NH2 1 
ATOM   5019 N  N   . VAL A 1 624  ? 57.476 63.452  -29.306 1.00 9.23  ? 624  VAL A N   1 
ATOM   5020 C  CA  . VAL A 1 624  ? 58.228 63.175  -28.085 1.00 8.66  ? 624  VAL A CA  1 
ATOM   5021 C  C   . VAL A 1 624  ? 58.261 61.687  -27.793 1.00 8.36  ? 624  VAL A C   1 
ATOM   5022 O  O   . VAL A 1 624  ? 57.234 61.013  -27.869 1.00 8.99  ? 624  VAL A O   1 
ATOM   5023 C  CB  . VAL A 1 624  ? 57.550 63.935  -26.914 1.00 9.48  ? 624  VAL A CB  1 
ATOM   5024 C  CG1 . VAL A 1 624  ? 58.467 63.963  -25.684 1.00 9.70  ? 624  VAL A CG1 1 
ATOM   5025 C  CG2 . VAL A 1 624  ? 57.210 65.390  -27.348 1.00 10.62 ? 624  VAL A CG2 1 
ATOM   5026 N  N   . PRO A 1 625  ? 59.457 61.179  -27.424 1.00 8.70  ? 625  PRO A N   1 
ATOM   5027 C  CA  . PRO A 1 625  ? 59.564 59.736  -27.142 1.00 9.41  ? 625  PRO A CA  1 
ATOM   5028 C  C   . PRO A 1 625  ? 58.741 59.287  -25.925 1.00 9.05  ? 625  PRO A C   1 
ATOM   5029 O  O   . PRO A 1 625  ? 58.333 60.105  -25.086 1.00 8.96  ? 625  PRO A O   1 
ATOM   5030 C  CB  . PRO A 1 625  ? 61.063 59.501  -26.847 1.00 10.13 ? 625  PRO A CB  1 
ATOM   5031 C  CG  . PRO A 1 625  ? 61.791 60.709  -27.423 1.00 10.53 ? 625  PRO A CG  1 
ATOM   5032 C  CD  . PRO A 1 625  ? 60.754 61.861  -27.319 1.00 8.94  ? 625  PRO A CD  1 
ATOM   5033 N  N   . PRO A 1 626  ? 58.522 57.990  -25.816 1.00 9.24  ? 626  PRO A N   1 
ATOM   5034 C  CA  . PRO A 1 626  ? 57.780 57.435  -24.659 1.00 8.53  ? 626  PRO A CA  1 
ATOM   5035 C  C   . PRO A 1 626  ? 58.575 57.854  -23.401 1.00 8.54  ? 626  PRO A C   1 
ATOM   5036 O  O   . PRO A 1 626  ? 59.820 57.661  -23.328 1.00 8.70  ? 626  PRO A O   1 
ATOM   5037 C  CB  . PRO A 1 626  ? 57.937 55.918  -24.839 1.00 8.41  ? 626  PRO A CB  1 
ATOM   5038 C  CG  . PRO A 1 626  ? 58.189 55.742  -26.359 1.00 9.65  ? 626  PRO A CG  1 
ATOM   5039 C  CD  . PRO A 1 626  ? 59.052 56.908  -26.707 1.00 10.78 ? 626  PRO A CD  1 
ATOM   5040 N  N   . MET A 1 627  ? 57.899 58.412  -22.389 1.00 7.45  ? 627  MET A N   1 
ATOM   5041 C  CA  . MET A 1 627  ? 58.537 58.825  -21.109 1.00 6.93  ? 627  MET A CA  1 
ATOM   5042 C  C   . MET A 1 627  ? 59.828 59.604  -21.370 1.00 7.84  ? 627  MET A C   1 
ATOM   5043 O  O   . MET A 1 627  ? 60.838 59.447  -20.704 1.00 8.54  ? 627  MET A O   1 
ATOM   5044 C  CB  . MET A 1 627  ? 58.829 57.566  -20.258 1.00 7.88  ? 627  MET A CB  1 
ATOM   5045 C  CG  . MET A 1 627  ? 57.550 56.883  -19.892 1.00 8.63  ? 627  MET A CG  1 
ATOM   5046 S  SD  . MET A 1 627  ? 57.713 55.195  -19.179 1.00 10.79 ? 627  MET A SD  1 
ATOM   5047 C  CE  . MET A 1 627  ? 58.583 55.572  -17.715 1.00 10.52 ? 627  MET A CE  1 
ATOM   5048 N  N   . GLY A 1 628  ? 59.744 60.487  -22.372 1.00 7.90  ? 628  GLY A N   1 
ATOM   5049 C  CA  . GLY A 1 628  ? 60.942 61.164  -22.812 1.00 8.47  ? 628  GLY A CA  1 
ATOM   5050 C  C   . GLY A 1 628  ? 60.823 62.654  -23.051 1.00 7.70  ? 628  GLY A C   1 
ATOM   5051 O  O   . GLY A 1 628  ? 59.848 63.304  -22.643 1.00 7.86  ? 628  GLY A O   1 
ATOM   5052 N  N   . LEU A 1 629  ? 61.875 63.183  -23.688 1.00 8.28  ? 629  LEU A N   1 
ATOM   5053 C  CA  . LEU A 1 629  ? 62.006 64.616  -23.930 1.00 8.57  ? 629  LEU A CA  1 
ATOM   5054 C  C   . LEU A 1 629  ? 62.445 64.915  -25.336 1.00 8.74  ? 629  LEU A C   1 
ATOM   5055 O  O   . LEU A 1 629  ? 63.204 64.142  -25.956 1.00 9.48  ? 629  LEU A O   1 
ATOM   5056 C  CB  . LEU A 1 629  ? 63.078 65.217  -23.031 1.00 8.67  ? 629  LEU A CB  1 
ATOM   5057 C  CG  . LEU A 1 629  ? 62.853 65.052  -21.526 1.00 8.51  ? 629  LEU A CG  1 
ATOM   5058 C  CD1 . LEU A 1 629  ? 64.146 65.343  -20.749 1.00 8.86  ? 629  LEU A CD1 1 
ATOM   5059 C  CD2 . LEU A 1 629  ? 61.755 66.052  -21.075 1.00 9.30  ? 629  LEU A CD2 1 
ATOM   5060 N  N   . ALA A 1 630  ? 61.950 66.029  -25.847 1.00 7.82  ? 630  ALA A N   1 
ATOM   5061 C  CA  . ALA A 1 630  ? 62.354 66.471  -27.205 1.00 9.39  ? 630  ALA A CA  1 
ATOM   5062 C  C   . ALA A 1 630  ? 62.581 67.960  -27.188 1.00 9.10  ? 630  ALA A C   1 
ATOM   5063 O  O   . ALA A 1 630  ? 61.748 68.736  -26.663 1.00 9.66  ? 630  ALA A O   1 
ATOM   5064 C  CB  . ALA A 1 630  ? 61.284 66.119  -28.237 1.00 10.65 ? 630  ALA A CB  1 
ATOM   5065 N  N   . THR A 1 631  ? 63.668 68.389  -27.849 1.00 9.04  ? 631  THR A N   1 
ATOM   5066 C  CA  . THR A 1 631  ? 64.052 69.812  -27.888 1.00 10.15 ? 631  THR A CA  1 
ATOM   5067 C  C   . THR A 1 631  ? 63.766 70.455  -29.222 1.00 9.96  ? 631  THR A C   1 
ATOM   5068 O  O   . THR A 1 631  ? 64.014 69.843  -30.279 1.00 10.37 ? 631  THR A O   1 
ATOM   5069 C  CB  . THR A 1 631  ? 65.553 69.918  -27.626 1.00 9.69  ? 631  THR A CB  1 
ATOM   5070 O  OG1 . THR A 1 631  ? 65.841 69.257  -26.363 1.00 10.67 ? 631  THR A OG1 1 
ATOM   5071 C  CG2 . THR A 1 631  ? 66.011 71.387  -27.501 1.00 11.39 ? 631  THR A CG2 1 
ATOM   5072 N  N   . TYR A 1 632  ? 63.250 71.675  -29.182 1.00 9.19  ? 632  TYR A N   1 
ATOM   5073 C  CA  . TYR A 1 632  ? 63.012 72.474  -30.381 1.00 9.09  ? 632  TYR A CA  1 
ATOM   5074 C  C   . TYR A 1 632  ? 63.595 73.853  -30.192 1.00 9.35  ? 632  TYR A C   1 
ATOM   5075 O  O   . TYR A 1 632  ? 63.886 74.294  -29.083 1.00 10.37 ? 632  TYR A O   1 
ATOM   5076 C  CB  . TYR A 1 632  ? 61.512 72.561  -30.700 1.00 9.95  ? 632  TYR A CB  1 
ATOM   5077 C  CG  . TYR A 1 632  ? 60.904 71.248  -31.108 1.00 9.33  ? 632  TYR A CG  1 
ATOM   5078 C  CD1 . TYR A 1 632  ? 60.547 70.317  -30.148 1.00 10.85 ? 632  TYR A CD1 1 
ATOM   5079 C  CD2 . TYR A 1 632  ? 60.705 70.938  -32.463 1.00 11.42 ? 632  TYR A CD2 1 
ATOM   5080 C  CE1 . TYR A 1 632  ? 59.997 69.080  -30.532 1.00 11.62 ? 632  TYR A CE1 1 
ATOM   5081 C  CE2 . TYR A 1 632  ? 60.161 69.714  -32.866 1.00 12.41 ? 632  TYR A CE2 1 
ATOM   5082 C  CZ  . TYR A 1 632  ? 59.816 68.799  -31.886 1.00 11.11 ? 632  TYR A CZ  1 
ATOM   5083 O  OH  . TYR A 1 632  ? 59.314 67.577  -32.256 1.00 13.82 ? 632  TYR A OH  1 
ATOM   5084 N  N   . VAL A 1 633  ? 63.761 74.569  -31.313 1.00 9.68  ? 633  VAL A N   1 
ATOM   5085 C  CA  . VAL A 1 633  ? 64.307 75.913  -31.292 1.00 10.61 ? 633  VAL A CA  1 
ATOM   5086 C  C   . VAL A 1 633  ? 63.362 76.871  -32.021 1.00 9.93  ? 633  VAL A C   1 
ATOM   5087 O  O   . VAL A 1 633  ? 62.860 76.548  -33.096 1.00 10.21 ? 633  VAL A O   1 
ATOM   5088 C  CB  . VAL A 1 633  ? 65.685 75.972  -31.998 1.00 11.14 ? 633  VAL A CB  1 
ATOM   5089 C  CG1 . VAL A 1 633  ? 66.269 77.420  -31.946 1.00 13.32 ? 633  VAL A CG1 1 
ATOM   5090 C  CG2 . VAL A 1 633  ? 66.624 74.957  -31.348 1.00 14.01 ? 633  VAL A CG2 1 
ATOM   5091 N  N   . LEU A 1 634  ? 63.087 78.023  -31.402 1.00 9.72  ? 634  LEU A N   1 
ATOM   5092 C  CA  . LEU A 1 634  ? 62.232 79.071  -31.997 1.00 10.45 ? 634  LEU A CA  1 
ATOM   5093 C  C   . LEU A 1 634  ? 63.184 80.195  -32.401 1.00 10.82 ? 634  LEU A C   1 
ATOM   5094 O  O   . LEU A 1 634  ? 63.959 80.681  -31.574 1.00 10.48 ? 634  LEU A O   1 
ATOM   5095 C  CB  . LEU A 1 634  ? 61.207 79.617  -30.985 1.00 11.43 ? 634  LEU A CB  1 
ATOM   5096 C  CG  . LEU A 1 634  ? 60.300 78.587  -30.272 1.00 17.26 ? 634  LEU A CG  1 
ATOM   5097 C  CD1 . LEU A 1 634  ? 59.048 79.317  -29.739 1.00 16.60 ? 634  LEU A CD1 1 
ATOM   5098 C  CD2 . LEU A 1 634  ? 59.968 77.400  -31.067 1.00 19.05 ? 634  LEU A CD2 1 
ATOM   5099 N  N   . THR A 1 635  ? 63.117 80.619  -33.682 1.00 10.28 ? 635  THR A N   1 
ATOM   5100 C  CA  . THR A 1 635  ? 64.038 81.643  -34.174 1.00 10.47 ? 635  THR A CA  1 
ATOM   5101 C  C   . THR A 1 635  ? 63.256 82.783  -34.842 1.00 11.27 ? 635  THR A C   1 
ATOM   5102 O  O   . THR A 1 635  ? 62.347 82.561  -35.635 1.00 11.77 ? 635  THR A O   1 
ATOM   5103 C  CB  . THR A 1 635  ? 64.965 80.986  -35.222 1.00 12.33 ? 635  THR A CB  1 
ATOM   5104 O  OG1 . THR A 1 635  ? 65.683 79.880  -34.620 1.00 12.25 ? 635  THR A OG1 1 
ATOM   5105 C  CG2 . THR A 1 635  ? 66.029 82.022  -35.718 1.00 12.35 ? 635  THR A CG2 1 
ATOM   5106 N  N   . ILE A 1 636  ? 63.677 84.015  -34.559 1.00 11.81 ? 636  ILE A N   1 
ATOM   5107 C  CA  . ILE A 1 636  ? 62.976 85.167  -35.159 1.00 12.27 ? 636  ILE A CA  1 
ATOM   5108 C  C   . ILE A 1 636  ? 63.598 85.497  -36.518 1.00 13.86 ? 636  ILE A C   1 
ATOM   5109 O  O   . ILE A 1 636  ? 64.777 85.195  -36.769 1.00 14.81 ? 636  ILE A O   1 
ATOM   5110 C  CB  . ILE A 1 636  ? 63.070 86.416  -34.223 1.00 12.18 ? 636  ILE A CB  1 
ATOM   5111 C  CG1 . ILE A 1 636  ? 62.109 87.500  -34.699 1.00 13.39 ? 636  ILE A CG1 1 
ATOM   5112 C  CG2 . ILE A 1 636  ? 64.508 86.956  -34.149 1.00 14.61 ? 636  ILE A CG2 1 
ATOM   5113 C  CD1 . ILE A 1 636  ? 62.048 88.677  -33.733 1.00 15.43 ? 636  ILE A CD1 1 
ATOM   5114 N  N   . SER A 1 637  ? 62.783 86.067  -37.395 1.00 15.66 ? 637  SER A N   1 
ATOM   5115 C  CA  . SER A 1 637  ? 63.311 86.528  -38.687 1.00 18.97 ? 637  SER A CA  1 
ATOM   5116 C  C   . SER A 1 637  ? 62.670 87.891  -38.961 1.00 20.31 ? 637  SER A C   1 
ATOM   5117 O  O   . SER A 1 637  ? 61.770 88.313  -38.252 1.00 19.30 ? 637  SER A O   1 
ATOM   5118 C  CB  . SER A 1 637  ? 63.042 85.506  -39.814 1.00 21.27 ? 637  SER A CB  1 
ATOM   5119 O  OG  . SER A 1 637  ? 61.663 85.304  -39.960 1.00 24.47 ? 637  SER A OG  1 
ATOM   5120 N  N   . ASP A 1 638  ? 63.172 88.616  -39.964 1.00 23.23 ? 638  ASP A N   1 
ATOM   5121 C  CA  . ASP A 1 638  ? 62.623 89.954  -40.232 1.00 26.07 ? 638  ASP A CA  1 
ATOM   5122 C  C   . ASP A 1 638  ? 61.225 89.931  -40.871 1.00 25.76 ? 638  ASP A C   1 
ATOM   5123 O  O   . ASP A 1 638  ? 60.416 90.872  -40.693 1.00 27.37 ? 638  ASP A O   1 
ATOM   5124 C  CB  . ASP A 1 638  ? 63.573 90.740  -41.138 1.00 29.32 ? 638  ASP A CB  1 
ATOM   5125 C  CG  . ASP A 1 638  ? 63.546 90.228  -42.564 1.00 32.74 ? 638  ASP A CG  1 
ATOM   5126 O  OD1 . ASP A 1 638  ? 63.972 89.063  -42.801 1.00 35.54 ? 638  ASP A OD1 1 
ATOM   5127 O  OD2 . ASP A 1 638  ? 63.068 90.983  -43.457 1.00 36.94 ? 638  ASP A OD2 1 
ATOM   5128 N  N   . SER A 1 639  ? 60.930 88.841  -41.571 1.00 24.74 ? 639  SER A N   1 
ATOM   5129 C  CA  . SER A 1 639  ? 59.667 88.691  -42.272 1.00 24.14 ? 639  SER A CA  1 
ATOM   5130 C  C   . SER A 1 639  ? 59.107 87.284  -42.192 1.00 22.96 ? 639  SER A C   1 
ATOM   5131 O  O   . SER A 1 639  ? 59.714 86.399  -41.586 1.00 20.66 ? 639  SER A O   1 
ATOM   5132 C  CB  . SER A 1 639  ? 59.848 89.069  -43.753 1.00 24.29 ? 639  SER A CB  1 
ATOM   5133 O  OG  . SER A 1 639  ? 60.841 88.252  -44.333 1.00 26.31 ? 639  SER A OG  1 
ATOM   5134 N  N   . LYS A 1 640  ? 57.952 87.083  -42.814 1.00 22.05 ? 640  LYS A N   1 
ATOM   5135 C  CA  . LYS A 1 640  ? 57.303 85.775  -42.785 1.00 22.39 ? 640  LYS A CA  1 
ATOM   5136 C  C   . LYS A 1 640  ? 58.241 84.647  -43.180 1.00 21.64 ? 640  LYS A C   1 
ATOM   5137 O  O   . LYS A 1 640  ? 58.800 84.646  -44.278 1.00 22.28 ? 640  LYS A O   1 
ATOM   5138 C  CB  . LYS A 1 640  ? 56.075 85.759  -43.703 1.00 23.80 ? 640  LYS A CB  1 
ATOM   5139 C  CG  . LYS A 1 640  ? 54.965 86.765  -43.353 1.00 28.09 ? 640  LYS A CG  1 
ATOM   5140 C  CD  . LYS A 1 640  ? 53.639 86.475  -44.114 1.00 30.30 ? 640  LYS A CD  1 
ATOM   5141 C  CE  . LYS A 1 640  ? 53.787 86.413  -45.636 1.00 32.83 ? 640  LYS A CE  1 
ATOM   5142 N  NZ  . LYS A 1 640  ? 54.030 87.736  -46.301 1.00 34.34 ? 640  LYS A NZ  1 
ATOM   5143 N  N   . PRO A 1 641  ? 58.476 83.684  -42.273 1.00 19.52 ? 641  PRO A N   1 
ATOM   5144 C  CA  . PRO A 1 641  ? 59.355 82.562  -42.598 1.00 18.99 ? 641  PRO A CA  1 
ATOM   5145 C  C   . PRO A 1 641  ? 58.610 81.540  -43.452 1.00 18.15 ? 641  PRO A C   1 
ATOM   5146 O  O   . PRO A 1 641  ? 57.374 81.439  -43.428 1.00 17.50 ? 641  PRO A O   1 
ATOM   5147 C  CB  . PRO A 1 641  ? 59.740 81.980  -41.243 1.00 20.56 ? 641  PRO A CB  1 
ATOM   5148 C  CG  . PRO A 1 641  ? 58.687 82.404  -40.375 1.00 19.66 ? 641  PRO A CG  1 
ATOM   5149 C  CD  . PRO A 1 641  ? 58.210 83.748  -40.823 1.00 19.69 ? 641  PRO A CD  1 
ATOM   5150 N  N   . GLU A 1 642  ? 59.384 80.753  -44.177 1.00 18.61 ? 642  GLU A N   1 
ATOM   5151 C  CA  . GLU A 1 642  ? 58.823 79.777  -45.090 1.00 19.51 ? 642  GLU A CA  1 
ATOM   5152 C  C   . GLU A 1 642  ? 57.897 78.719  -44.521 1.00 19.04 ? 642  GLU A C   1 
ATOM   5153 O  O   . GLU A 1 642  ? 56.899 78.347  -45.124 1.00 20.08 ? 642  GLU A O   1 
ATOM   5154 C  CB  . GLU A 1 642  ? 59.983 79.088  -45.845 1.00 21.64 ? 642  GLU A CB  1 
ATOM   5155 C  CG  . GLU A 1 642  ? 59.559 77.942  -46.737 1.00 25.98 ? 642  GLU A CG  1 
ATOM   5156 C  CD  . GLU A 1 642  ? 60.736 77.270  -47.474 1.00 28.46 ? 642  GLU A CD  1 
ATOM   5157 O  OE1 . GLU A 1 642  ? 61.893 77.776  -47.390 1.00 30.84 ? 642  GLU A OE1 1 
ATOM   5158 O  OE2 . GLU A 1 642  ? 60.482 76.228  -48.129 1.00 30.59 ? 642  GLU A OE2 1 
ATOM   5159 N  N   . HIS A 1 643  ? 58.192 78.274  -43.308 1.00 17.32 ? 643  HIS A N   1 
ATOM   5160 C  CA  . HIS A 1 643  ? 57.419 77.175  -42.730 1.00 16.01 ? 643  HIS A CA  1 
ATOM   5161 C  C   . HIS A 1 643  ? 56.420 77.577  -41.649 1.00 14.72 ? 643  HIS A C   1 
ATOM   5162 O  O   . HIS A 1 643  ? 55.974 76.709  -40.884 1.00 14.73 ? 643  HIS A O   1 
ATOM   5163 C  CB  . HIS A 1 643  ? 58.384 76.142  -42.187 1.00 16.78 ? 643  HIS A CB  1 
ATOM   5164 C  CG  . HIS A 1 643  ? 59.255 75.560  -43.255 1.00 18.04 ? 643  HIS A CG  1 
ATOM   5165 N  ND1 . HIS A 1 643  ? 58.824 74.554  -44.080 1.00 20.93 ? 643  HIS A ND1 1 
ATOM   5166 C  CD2 . HIS A 1 643  ? 60.508 75.875  -43.657 1.00 18.18 ? 643  HIS A CD2 1 
ATOM   5167 C  CE1 . HIS A 1 643  ? 59.780 74.261  -44.951 1.00 19.13 ? 643  HIS A CE1 1 
ATOM   5168 N  NE2 . HIS A 1 643  ? 60.812 75.048  -44.712 1.00 19.84 ? 643  HIS A NE2 1 
ATOM   5169 N  N   . THR A 1 644  ? 56.105 78.861  -41.589 1.00 13.24 ? 644  THR A N   1 
ATOM   5170 C  CA  . THR A 1 644  ? 55.132 79.359  -40.634 1.00 12.77 ? 644  THR A CA  1 
ATOM   5171 C  C   . THR A 1 644  ? 53.986 80.019  -41.389 1.00 13.30 ? 644  THR A C   1 
ATOM   5172 O  O   . THR A 1 644  ? 54.253 80.836  -42.292 1.00 14.21 ? 644  THR A O   1 
ATOM   5173 C  CB  . THR A 1 644  ? 55.785 80.387  -39.693 1.00 12.77 ? 644  THR A CB  1 
ATOM   5174 O  OG1 . THR A 1 644  ? 56.821 79.707  -38.961 1.00 12.97 ? 644  THR A OG1 1 
ATOM   5175 C  CG2 . THR A 1 644  ? 54.743 80.976  -38.643 1.00 13.26 ? 644  THR A CG2 1 
ATOM   5176 N  N   . SER A 1 645  ? 52.755 79.641  -41.047 1.00 12.39 ? 645  SER A N   1 
ATOM   5177 C  CA  . SER A 1 645  ? 51.551 80.209  -41.657 1.00 12.88 ? 645  SER A CA  1 
ATOM   5178 C  C   . SER A 1 645  ? 50.851 81.024  -40.597 1.00 12.09 ? 645  SER A C   1 
ATOM   5179 O  O   . SER A 1 645  ? 51.186 80.944  -39.407 1.00 12.26 ? 645  SER A O   1 
ATOM   5180 C  CB  . SER A 1 645  ? 50.605 79.113  -42.163 1.00 13.50 ? 645  SER A CB  1 
ATOM   5181 O  OG  . SER A 1 645  ? 50.145 78.300  -41.057 1.00 15.21 ? 645  SER A OG  1 
ATOM   5182 N  N   . TYR A 1 646  ? 49.887 81.836  -41.007 1.00 11.56 ? 646  TYR A N   1 
ATOM   5183 C  CA  . TYR A 1 646  ? 49.164 82.743  -40.127 1.00 11.86 ? 646  TYR A CA  1 
ATOM   5184 C  C   . TYR A 1 646  ? 47.669 82.538  -40.208 1.00 11.96 ? 646  TYR A C   1 
ATOM   5185 O  O   . TYR A 1 646  ? 47.110 82.428  -41.285 1.00 13.39 ? 646  TYR A O   1 
ATOM   5186 C  CB  . TYR A 1 646  ? 49.506 84.191  -40.518 1.00 13.40 ? 646  TYR A CB  1 
ATOM   5187 C  CG  . TYR A 1 646  ? 50.961 84.459  -40.320 1.00 12.01 ? 646  TYR A CG  1 
ATOM   5188 C  CD1 . TYR A 1 646  ? 51.423 84.854  -39.068 1.00 12.04 ? 646  TYR A CD1 1 
ATOM   5189 C  CD2 . TYR A 1 646  ? 51.899 84.165  -41.328 1.00 13.18 ? 646  TYR A CD2 1 
ATOM   5190 C  CE1 . TYR A 1 646  ? 52.769 84.944  -38.825 1.00 13.10 ? 646  TYR A CE1 1 
ATOM   5191 C  CE2 . TYR A 1 646  ? 53.282 84.255  -41.073 1.00 15.11 ? 646  TYR A CE2 1 
ATOM   5192 C  CZ  . TYR A 1 646  ? 53.687 84.644  -39.811 1.00 13.23 ? 646  TYR A CZ  1 
ATOM   5193 O  OH  . TYR A 1 646  ? 55.041 84.711  -39.512 1.00 15.35 ? 646  TYR A OH  1 
ATOM   5194 N  N   . ALA A 1 647  ? 47.013 82.407  -39.057 1.00 10.95 ? 647  ALA A N   1 
ATOM   5195 C  CA  . ALA A 1 647  ? 45.596 82.210  -39.034 1.00 10.37 ? 647  ALA A CA  1 
ATOM   5196 C  C   . ALA A 1 647  ? 44.820 83.436  -39.469 1.00 11.25 ? 647  ALA A C   1 
ATOM   5197 O  O   . ALA A 1 647  ? 45.256 84.588  -39.323 1.00 11.77 ? 647  ALA A O   1 
ATOM   5198 C  CB  . ALA A 1 647  ? 45.152 81.837  -37.614 1.00 12.21 ? 647  ALA A CB  1 
ATOM   5199 N  N   . SER A 1 648  ? 43.677 83.181  -40.068 1.00 11.02 ? 648  SER A N   1 
ATOM   5200 C  CA  . SER A 1 648  ? 42.795 84.296  -40.353 1.00 11.68 ? 648  SER A CA  1 
ATOM   5201 C  C   . SER A 1 648  ? 41.908 84.488  -39.102 1.00 11.17 ? 648  SER A C   1 
ATOM   5202 O  O   . SER A 1 648  ? 41.723 83.551  -38.274 1.00 11.23 ? 648  SER A O   1 
ATOM   5203 C  CB  . SER A 1 648  ? 41.920 83.986  -41.572 1.00 12.88 ? 648  SER A CB  1 
ATOM   5204 O  OG  . SER A 1 648  ? 41.105 82.857  -41.369 1.00 17.94 ? 648  SER A OG  1 
ATOM   5205 N  N   . ASN A 1 649  ? 41.280 85.648  -38.953 1.00 10.21 ? 649  ASN A N   1 
ATOM   5206 C  CA  . ASN A 1 649  ? 40.445 85.929  -37.789 1.00 10.81 ? 649  ASN A CA  1 
ATOM   5207 C  C   . ASN A 1 649  ? 39.227 86.678  -38.260 1.00 10.85 ? 649  ASN A C   1 
ATOM   5208 O  O   . ASN A 1 649  ? 39.369 87.647  -39.035 1.00 12.49 ? 649  ASN A O   1 
ATOM   5209 C  CB  . ASN A 1 649  ? 41.219 86.753  -36.744 1.00 10.62 ? 649  ASN A CB  1 
ATOM   5210 C  CG  . ASN A 1 649  ? 42.395 85.980  -36.166 1.00 11.41 ? 649  ASN A CG  1 
ATOM   5211 O  OD1 . ASN A 1 649  ? 42.240 85.196  -35.187 1.00 11.33 ? 649  ASN A OD1 1 
ATOM   5212 N  ND2 . ASN A 1 649  ? 43.568 86.137  -36.765 1.00 11.50 ? 649  ASN A ND2 1 
ATOM   5213 N  N   . LEU A 1 650  ? 38.065 86.233  -37.817 1.00 11.01 ? 650  LEU A N   1 
ATOM   5214 C  CA  . LEU A 1 650  ? 36.785 86.840  -38.229 1.00 10.94 ? 650  LEU A CA  1 
ATOM   5215 C  C   . LEU A 1 650  ? 35.967 87.108  -36.974 1.00 11.03 ? 650  LEU A C   1 
ATOM   5216 O  O   . LEU A 1 650  ? 35.667 86.173  -36.190 1.00 12.25 ? 650  LEU A O   1 
ATOM   5217 C  CB  . LEU A 1 650  ? 36.044 85.877  -39.144 1.00 12.44 ? 650  LEU A CB  1 
ATOM   5218 C  CG  . LEU A 1 650  ? 34.571 86.202  -39.434 1.00 12.32 ? 650  LEU A CG  1 
ATOM   5219 C  CD1 . LEU A 1 650  ? 34.531 87.515  -40.321 1.00 14.40 ? 650  LEU A CD1 1 
ATOM   5220 C  CD2 . LEU A 1 650  ? 33.966 85.055  -40.255 1.00 14.88 ? 650  LEU A CD2 1 
ATOM   5221 N  N   . LEU A 1 651  ? 35.615 88.356  -36.731 1.00 12.31 ? 651  LEU A N   1 
ATOM   5222 C  CA  . LEU A 1 651  ? 34.837 88.786  -35.580 1.00 13.18 ? 651  LEU A CA  1 
ATOM   5223 C  C   . LEU A 1 651  ? 33.402 89.015  -36.037 1.00 14.15 ? 651  LEU A C   1 
ATOM   5224 O  O   . LEU A 1 651  ? 33.155 89.845  -36.912 1.00 14.50 ? 651  LEU A O   1 
ATOM   5225 C  CB  . LEU A 1 651  ? 35.441 90.059  -35.006 1.00 16.07 ? 651  LEU A CB  1 
ATOM   5226 C  CG  . LEU A 1 651  ? 35.097 90.492  -33.570 1.00 19.82 ? 651  LEU A CG  1 
ATOM   5227 C  CD1 . LEU A 1 651  ? 33.838 91.249  -33.550 1.00 23.27 ? 651  LEU A CD1 1 
ATOM   5228 C  CD2 . LEU A 1 651  ? 35.099 89.309  -32.638 1.00 19.52 ? 651  LEU A CD2 1 
ATOM   5229 N  N   . LEU A 1 652  ? 32.454 88.266  -35.494 1.00 14.65 ? 652  LEU A N   1 
ATOM   5230 C  CA  . LEU A 1 652  ? 31.082 88.358  -35.894 1.00 14.84 ? 652  LEU A CA  1 
ATOM   5231 C  C   . LEU A 1 652  ? 30.278 89.055  -34.824 1.00 16.66 ? 652  LEU A C   1 
ATOM   5232 O  O   . LEU A 1 652  ? 30.123 88.552  -33.687 1.00 16.02 ? 652  LEU A O   1 
ATOM   5233 C  CB  . LEU A 1 652  ? 30.505 86.958  -36.159 1.00 14.72 ? 652  LEU A CB  1 
ATOM   5234 C  CG  . LEU A 1 652  ? 31.223 86.183  -37.253 1.00 14.65 ? 652  LEU A CG  1 
ATOM   5235 C  CD1 . LEU A 1 652  ? 30.686 84.745  -37.366 1.00 16.30 ? 652  LEU A CD1 1 
ATOM   5236 C  CD2 . LEU A 1 652  ? 31.057 86.945  -38.625 1.00 16.45 ? 652  LEU A CD2 1 
ATOM   5237 N  N   . ARG A 1 653  ? 29.772 90.240  -35.171 1.00 17.56 ? 653  ARG A N   1 
ATOM   5238 C  CA  . ARG A 1 653  ? 28.953 91.043  -34.307 1.00 20.22 ? 653  ARG A CA  1 
ATOM   5239 C  C   . ARG A 1 653  ? 28.478 92.252  -35.139 1.00 20.45 ? 653  ARG A C   1 
ATOM   5240 O  O   . ARG A 1 653  ? 29.124 92.648  -36.109 1.00 20.93 ? 653  ARG A O   1 
ATOM   5241 C  CB  . ARG A 1 653  ? 29.746 91.533  -33.117 1.00 22.06 ? 653  ARG A CB  1 
ATOM   5242 C  CG  . ARG A 1 653  ? 30.860 92.423  -33.491 1.00 24.50 ? 653  ARG A CG  1 
ATOM   5243 C  CD  . ARG A 1 653  ? 30.637 93.665  -32.700 1.00 28.84 ? 653  ARG A CD  1 
ATOM   5244 N  NE  . ARG A 1 653  ? 31.310 93.660  -31.420 1.00 29.45 ? 653  ARG A NE  1 
ATOM   5245 C  CZ  . ARG A 1 653  ? 31.004 94.463  -30.401 1.00 31.09 ? 653  ARG A CZ  1 
ATOM   5246 N  NH1 . ARG A 1 653  ? 30.010 95.337  -30.491 1.00 33.29 ? 653  ARG A NH1 1 
ATOM   5247 N  NH2 . ARG A 1 653  ? 31.749 94.460  -29.312 1.00 32.71 ? 653  ARG A NH2 1 
ATOM   5248 N  N   . LYS A 1 654  ? 27.323 92.780  -34.775 1.00 22.78 ? 654  LYS A N   1 
ATOM   5249 C  CA  . LYS A 1 654  ? 26.845 93.970  -35.469 1.00 24.98 ? 654  LYS A CA  1 
ATOM   5250 C  C   . LYS A 1 654  ? 27.618 95.145  -34.833 1.00 25.55 ? 654  LYS A C   1 
ATOM   5251 O  O   . LYS A 1 654  ? 28.087 95.033  -33.709 1.00 25.92 ? 654  LYS A O   1 
ATOM   5252 C  CB  . LYS A 1 654  ? 25.335 94.087  -35.277 1.00 27.06 ? 654  LYS A CB  1 
ATOM   5253 C  CG  . LYS A 1 654  ? 24.577 92.990  -36.035 1.00 30.56 ? 654  LYS A CG  1 
ATOM   5254 C  CD  . LYS A 1 654  ? 23.101 93.322  -36.245 1.00 34.32 ? 654  LYS A CD  1 
ATOM   5255 C  CE  . LYS A 1 654  ? 22.939 94.502  -37.208 1.00 36.02 ? 654  LYS A CE  1 
ATOM   5256 N  NZ  . LYS A 1 654  ? 21.549 95.088  -37.193 1.00 38.13 ? 654  LYS A NZ  1 
ATOM   5257 N  N   . ASN A 1 655  ? 27.789 96.255  -35.530 1.00 27.16 ? 655  ASN A N   1 
ATOM   5258 C  CA  . ASN A 1 655  ? 28.482 97.381  -34.890 1.00 27.11 ? 655  ASN A CA  1 
ATOM   5259 C  C   . ASN A 1 655  ? 29.889 97.022  -34.400 1.00 25.44 ? 655  ASN A C   1 
ATOM   5260 O  O   . ASN A 1 655  ? 30.219 97.218  -33.227 1.00 25.72 ? 655  ASN A O   1 
ATOM   5261 C  CB  . ASN A 1 655  ? 27.678 97.877  -33.680 1.00 30.21 ? 655  ASN A CB  1 
ATOM   5262 C  CG  . ASN A 1 655  ? 28.103 99.277  -33.217 1.00 33.09 ? 655  ASN A CG  1 
ATOM   5263 O  OD1 . ASN A 1 655  ? 28.520 99.474  -32.053 1.00 34.71 ? 655  ASN A OD1 1 
ATOM   5264 N  ND2 . ASN A 1 655  ? 27.980 100.268 -34.121 1.00 34.88 ? 655  ASN A ND2 1 
ATOM   5265 N  N   . PRO A 1 656  ? 30.740 96.497  -35.292 1.00 22.42 ? 656  PRO A N   1 
ATOM   5266 C  CA  . PRO A 1 656  ? 32.101 96.134  -34.884 1.00 20.78 ? 656  PRO A CA  1 
ATOM   5267 C  C   . PRO A 1 656  ? 32.977 97.375  -34.865 1.00 19.45 ? 656  PRO A C   1 
ATOM   5268 O  O   . PRO A 1 656  ? 32.629 98.406  -35.469 1.00 18.69 ? 656  PRO A O   1 
ATOM   5269 C  CB  . PRO A 1 656  ? 32.553 95.190  -35.987 1.00 20.35 ? 656  PRO A CB  1 
ATOM   5270 C  CG  . PRO A 1 656  ? 31.849 95.738  -37.193 1.00 19.95 ? 656  PRO A CG  1 
ATOM   5271 C  CD  . PRO A 1 656  ? 30.459 96.070  -36.675 1.00 21.78 ? 656  PRO A CD  1 
ATOM   5272 N  N   . THR A 1 657  ? 34.088 97.278  -34.151 1.00 19.12 ? 657  THR A N   1 
ATOM   5273 C  CA  . THR A 1 657  ? 35.079 98.333  -34.142 1.00 18.91 ? 657  THR A CA  1 
ATOM   5274 C  C   . THR A 1 657  ? 36.358 97.595  -34.492 1.00 18.08 ? 657  THR A C   1 
ATOM   5275 O  O   . THR A 1 657  ? 36.431 96.341  -34.385 1.00 18.16 ? 657  THR A O   1 
ATOM   5276 C  CB  . THR A 1 657  ? 35.188 99.042  -32.804 1.00 19.46 ? 657  THR A CB  1 
ATOM   5277 O  OG1 . THR A 1 657  ? 35.303 98.072  -31.753 1.00 22.43 ? 657  THR A OG1 1 
ATOM   5278 C  CG2 . THR A 1 657  ? 33.944 99.916  -32.582 1.00 20.46 ? 657  THR A CG2 1 
ATOM   5279 N  N   . SER A 1 658  ? 37.364 98.354  -34.889 1.00 17.03 ? 658  SER A N   1 
ATOM   5280 C  CA  . SER A 1 658  ? 38.632 97.828  -35.376 1.00 17.31 ? 658  SER A CA  1 
ATOM   5281 C  C   . SER A 1 658  ? 39.378 96.999  -34.314 1.00 17.65 ? 658  SER A C   1 
ATOM   5282 O  O   . SER A 1 658  ? 39.168 97.184  -33.105 1.00 18.41 ? 658  SER A O   1 
ATOM   5283 C  CB  . SER A 1 658  ? 39.498 98.991  -35.823 1.00 18.41 ? 658  SER A CB  1 
ATOM   5284 O  OG  . SER A 1 658  ? 39.927 99.702  -34.671 1.00 19.40 ? 658  SER A OG  1 
ATOM   5285 N  N   . LEU A 1 659  ? 40.227 96.085  -34.775 1.00 16.78 ? 659  LEU A N   1 
ATOM   5286 C  CA  . LEU A 1 659  ? 41.000 95.208  -33.848 1.00 17.38 ? 659  LEU A CA  1 
ATOM   5287 C  C   . LEU A 1 659  ? 42.412 95.131  -34.412 1.00 17.77 ? 659  LEU A C   1 
ATOM   5288 O  O   . LEU A 1 659  ? 42.755 94.225  -35.175 1.00 17.27 ? 659  LEU A O   1 
ATOM   5289 C  CB  . LEU A 1 659  ? 40.371 93.781  -33.794 1.00 18.33 ? 659  LEU A CB  1 
ATOM   5290 C  CG  . LEU A 1 659  ? 39.010 93.677  -33.112 1.00 19.41 ? 659  LEU A CG  1 
ATOM   5291 C  CD1 . LEU A 1 659  ? 38.457 92.249  -33.299 1.00 20.41 ? 659  LEU A CD1 1 
ATOM   5292 C  CD2 . LEU A 1 659  ? 39.116 94.039  -31.644 1.00 19.95 ? 659  LEU A CD2 1 
ATOM   5293 N  N   . PRO A 1 660  ? 43.236 96.141  -34.112 1.00 18.71 ? 660  PRO A N   1 
ATOM   5294 C  CA  . PRO A 1 660  ? 44.599 96.125  -34.624 1.00 18.44 ? 660  PRO A CA  1 
ATOM   5295 C  C   . PRO A 1 660  ? 45.391 95.024  -33.891 1.00 17.42 ? 660  PRO A C   1 
ATOM   5296 O  O   . PRO A 1 660  ? 45.127 94.723  -32.733 1.00 17.56 ? 660  PRO A O   1 
ATOM   5297 C  CB  . PRO A 1 660  ? 45.104 97.539  -34.312 1.00 19.69 ? 660  PRO A CB  1 
ATOM   5298 C  CG  . PRO A 1 660  ? 44.396 97.900  -33.100 1.00 20.67 ? 660  PRO A CG  1 
ATOM   5299 C  CD  . PRO A 1 660  ? 42.964 97.356  -33.331 1.00 19.13 ? 660  PRO A CD  1 
ATOM   5300 N  N   . LEU A 1 661  ? 46.376 94.475  -34.583 1.00 18.18 ? 661  LEU A N   1 
ATOM   5301 C  CA  . LEU A 1 661  ? 47.165 93.359  -34.007 1.00 17.91 ? 661  LEU A CA  1 
ATOM   5302 C  C   . LEU A 1 661  ? 48.698 93.544  -34.133 1.00 19.04 ? 661  LEU A C   1 
ATOM   5303 O  O   . LEU A 1 661  ? 49.444 92.566  -34.304 1.00 17.24 ? 661  LEU A O   1 
ATOM   5304 C  CB  . LEU A 1 661  ? 46.749 92.076  -34.715 1.00 17.68 ? 661  LEU A CB  1 
ATOM   5305 C  CG  . LEU A 1 661  ? 45.315 91.615  -34.497 1.00 16.27 ? 661  LEU A CG  1 
ATOM   5306 C  CD1 . LEU A 1 661  ? 45.059 90.311  -35.339 1.00 16.56 ? 661  LEU A CD1 1 
ATOM   5307 C  CD2 . LEU A 1 661  ? 45.132 91.351  -33.009 1.00 16.95 ? 661  LEU A CD2 1 
ATOM   5308 N  N   . GLY A 1 662  ? 49.171 94.789  -34.087 1.00 20.41 ? 662  GLY A N   1 
ATOM   5309 C  CA  . GLY A 1 662  ? 50.622 95.031  -34.193 1.00 20.46 ? 662  GLY A CA  1 
ATOM   5310 C  C   . GLY A 1 662  ? 51.212 94.513  -35.494 1.00 20.93 ? 662  GLY A C   1 
ATOM   5311 O  O   . GLY A 1 662  ? 50.694 94.762  -36.565 1.00 22.14 ? 662  GLY A O   1 
ATOM   5312 N  N   . GLN A 1 663  ? 52.277 93.709  -35.411 1.00 20.68 ? 663  GLN A N   1 
ATOM   5313 C  CA  . GLN A 1 663  ? 52.878 93.199  -36.622 1.00 20.95 ? 663  GLN A CA  1 
ATOM   5314 C  C   . GLN A 1 663  ? 52.177 91.977  -37.228 1.00 19.14 ? 663  GLN A C   1 
ATOM   5315 O  O   . GLN A 1 663  ? 52.578 91.519  -38.274 1.00 20.13 ? 663  GLN A O   1 
ATOM   5316 C  CB  . GLN A 1 663  ? 54.333 92.785  -36.391 1.00 22.86 ? 663  GLN A CB  1 
ATOM   5317 C  CG  . GLN A 1 663  ? 55.191 93.714  -35.521 1.00 26.10 ? 663  GLN A CG  1 
ATOM   5318 C  CD  . GLN A 1 663  ? 56.480 92.995  -35.130 1.00 26.76 ? 663  GLN A CD  1 
ATOM   5319 O  OE1 . GLN A 1 663  ? 57.361 92.814  -35.996 1.00 27.35 ? 663  GLN A OE1 1 
ATOM   5320 N  NE2 . GLN A 1 663  ? 56.583 92.529  -33.852 1.00 27.51 ? 663  GLN A NE2 1 
ATOM   5321 N  N   . TYR A 1 664  ? 51.123 91.464  -36.583 1.00 18.61 ? 664  TYR A N   1 
ATOM   5322 C  CA  . TYR A 1 664  ? 50.464 90.275  -37.156 1.00 17.48 ? 664  TYR A CA  1 
ATOM   5323 C  C   . TYR A 1 664  ? 50.158 90.565  -38.628 1.00 17.08 ? 664  TYR A C   1 
ATOM   5324 O  O   . TYR A 1 664  ? 49.499 91.561  -38.929 1.00 18.18 ? 664  TYR A O   1 
ATOM   5325 C  CB  . TYR A 1 664  ? 49.217 90.015  -36.340 1.00 15.27 ? 664  TYR A CB  1 
ATOM   5326 C  CG  . TYR A 1 664  ? 48.625 88.669  -36.642 1.00 14.19 ? 664  TYR A CG  1 
ATOM   5327 C  CD1 . TYR A 1 664  ? 49.175 87.513  -36.068 1.00 12.54 ? 664  TYR A CD1 1 
ATOM   5328 C  CD2 . TYR A 1 664  ? 47.512 88.541  -37.474 1.00 12.52 ? 664  TYR A CD2 1 
ATOM   5329 C  CE1 . TYR A 1 664  ? 48.626 86.285  -36.301 1.00 13.82 ? 664  TYR A CE1 1 
ATOM   5330 C  CE2 . TYR A 1 664  ? 46.957 87.302  -37.739 1.00 13.57 ? 664  TYR A CE2 1 
ATOM   5331 C  CZ  . TYR A 1 664  ? 47.527 86.181  -37.124 1.00 12.02 ? 664  TYR A CZ  1 
ATOM   5332 O  OH  . TYR A 1 664  ? 46.922 84.992  -37.337 1.00 13.09 ? 664  TYR A OH  1 
ATOM   5333 N  N   . PRO A 1 665  ? 50.544 89.684  -39.544 1.00 17.87 ? 665  PRO A N   1 
ATOM   5334 C  CA  . PRO A 1 665  ? 50.307 89.985  -40.972 1.00 18.52 ? 665  PRO A CA  1 
ATOM   5335 C  C   . PRO A 1 665  ? 48.991 89.938  -41.665 1.00 19.88 ? 665  PRO A C   1 
ATOM   5336 O  O   . PRO A 1 665  ? 48.904 90.398  -42.807 1.00 22.32 ? 665  PRO A O   1 
ATOM   5337 C  CB  . PRO A 1 665  ? 51.116 88.905  -41.690 1.00 18.75 ? 665  PRO A CB  1 
ATOM   5338 C  CG  . PRO A 1 665  ? 51.117 87.750  -40.747 1.00 19.02 ? 665  PRO A CG  1 
ATOM   5339 C  CD  . PRO A 1 665  ? 51.013 88.338  -39.368 1.00 18.17 ? 665  PRO A CD  1 
ATOM   5340 N  N   . GLU A 1 666  ? 47.973 89.381  -41.024 1.00 19.34 ? 666  GLU A N   1 
ATOM   5341 C  CA  . GLU A 1 666  ? 46.655 89.307  -41.651 1.00 19.20 ? 666  GLU A CA  1 
ATOM   5342 C  C   . GLU A 1 666  ? 45.718 90.201  -40.872 1.00 18.16 ? 666  GLU A C   1 
ATOM   5343 O  O   A GLU A 1 666  ? 45.654 90.136  -39.642 0.50 16.85 ? 666  GLU A O   1 
ATOM   5344 O  O   B GLU A 1 666  ? 45.475 89.991  -39.668 0.50 17.19 ? 666  GLU A O   1 
ATOM   5345 C  CB  . GLU A 1 666  ? 46.114 87.870  -41.628 1.00 21.13 ? 666  GLU A CB  1 
ATOM   5346 C  CG  A GLU A 1 666  ? 44.655 87.798  -42.008 0.50 23.73 ? 666  GLU A CG  1 
ATOM   5347 C  CG  B GLU A 1 666  ? 47.070 86.901  -42.347 0.50 23.58 ? 666  GLU A CG  1 
ATOM   5348 C  CD  A GLU A 1 666  ? 44.373 86.876  -43.172 0.50 24.49 ? 666  GLU A CD  1 
ATOM   5349 C  CD  B GLU A 1 666  ? 46.984 87.225  -43.821 0.50 24.88 ? 666  GLU A CD  1 
ATOM   5350 O  OE1 A GLU A 1 666  ? 45.301 86.619  -43.966 0.50 25.85 ? 666  GLU A OE1 1 
ATOM   5351 O  OE1 B GLU A 1 666  ? 45.924 86.964  -44.412 0.50 25.84 ? 666  GLU A OE1 1 
ATOM   5352 O  OE2 A GLU A 1 666  ? 43.218 86.430  -43.303 0.50 23.30 ? 666  GLU A OE2 1 
ATOM   5353 O  OE2 B GLU A 1 666  ? 47.962 87.759  -44.387 0.50 26.94 ? 666  GLU A OE2 1 
ATOM   5354 N  N   . ASP A 1 667  ? 44.999 91.062  -41.586 1.00 17.19 ? 667  ASP A N   1 
ATOM   5355 C  CA  . ASP A 1 667  ? 44.045 91.951  -40.939 1.00 16.93 ? 667  ASP A CA  1 
ATOM   5356 C  C   . ASP A 1 667  ? 42.784 91.175  -40.485 1.00 14.63 ? 667  ASP A C   1 
ATOM   5357 O  O   . ASP A 1 667  ? 42.300 90.320  -41.202 1.00 13.73 ? 667  ASP A O   1 
ATOM   5358 C  CB  . ASP A 1 667  ? 43.543 93.039  -41.934 1.00 18.94 ? 667  ASP A CB  1 
ATOM   5359 C  CG  . ASP A 1 667  ? 44.626 94.025  -42.338 1.00 21.79 ? 667  ASP A CG  1 
ATOM   5360 O  OD1 . ASP A 1 667  ? 45.632 94.184  -41.587 1.00 24.91 ? 667  ASP A OD1 1 
ATOM   5361 O  OD2 . ASP A 1 667  ? 44.467 94.685  -43.406 1.00 24.30 ? 667  ASP A OD2 1 
ATOM   5362 N  N   . VAL A 1 668  ? 42.275 91.498  -39.310 1.00 13.91 ? 668  VAL A N   1 
ATOM   5363 C  CA  . VAL A 1 668  ? 41.031 90.894  -38.813 1.00 14.15 ? 668  VAL A CA  1 
ATOM   5364 C  C   . VAL A 1 668  ? 39.876 91.294  -39.765 1.00 14.26 ? 668  VAL A C   1 
ATOM   5365 O  O   . VAL A 1 668  ? 39.817 92.458  -40.264 1.00 14.77 ? 668  VAL A O   1 
ATOM   5366 C  CB  . VAL A 1 668  ? 40.668 91.393  -37.388 1.00 15.30 ? 668  VAL A CB  1 
ATOM   5367 C  CG1 . VAL A 1 668  ? 39.329 90.769  -36.932 1.00 14.80 ? 668  VAL A CG1 1 
ATOM   5368 C  CG2 . VAL A 1 668  ? 41.776 90.975  -36.395 1.00 15.47 ? 668  VAL A CG2 1 
ATOM   5369 N  N   . LYS A 1 669  ? 38.977 90.348  -40.014 1.00 12.72 ? 669  LYS A N   1 
ATOM   5370 C  CA  . LYS A 1 669  ? 37.782 90.505  -40.877 1.00 13.40 ? 669  LYS A CA  1 
ATOM   5371 C  C   . LYS A 1 669  ? 36.557 90.614  -39.955 1.00 12.40 ? 669  LYS A C   1 
ATOM   5372 O  O   . LYS A 1 669  ? 36.553 90.055  -38.831 1.00 12.84 ? 669  LYS A O   1 
ATOM   5373 C  CB  . LYS A 1 669  ? 37.636 89.301  -41.789 1.00 16.68 ? 669  LYS A CB  1 
ATOM   5374 C  CG  . LYS A 1 669  ? 38.597 89.264  -42.976 1.00 22.86 ? 669  LYS A CG  1 
ATOM   5375 C  CD  . LYS A 1 669  ? 40.097 89.106  -42.656 1.00 27.01 ? 669  LYS A CD  1 
ATOM   5376 C  CE  . LYS A 1 669  ? 40.994 89.794  -43.769 1.00 28.79 ? 669  LYS A CE  1 
ATOM   5377 N  NZ  . LYS A 1 669  ? 40.469 89.542  -45.166 1.00 31.86 ? 669  LYS A NZ  1 
ATOM   5378 N  N   . PHE A 1 670  ? 35.513 91.300  -40.396 1.00 12.90 ? 670  PHE A N   1 
ATOM   5379 C  CA  . PHE A 1 670  ? 34.314 91.506  -39.603 1.00 13.40 ? 670  PHE A CA  1 
ATOM   5380 C  C   . PHE A 1 670  ? 33.087 91.090  -40.374 1.00 14.11 ? 670  PHE A C   1 
ATOM   5381 O  O   . PHE A 1 670  ? 33.094 91.047  -41.585 1.00 15.38 ? 670  PHE A O   1 
ATOM   5382 C  CB  . PHE A 1 670  ? 34.175 92.969  -39.184 1.00 14.41 ? 670  PHE A CB  1 
ATOM   5383 C  CG  . PHE A 1 670  ? 35.339 93.464  -38.406 1.00 15.16 ? 670  PHE A CG  1 
ATOM   5384 C  CD1 . PHE A 1 670  ? 36.478 93.916  -39.071 1.00 15.99 ? 670  PHE A CD1 1 
ATOM   5385 C  CD2 . PHE A 1 670  ? 35.330 93.399  -37.015 1.00 16.37 ? 670  PHE A CD2 1 
ATOM   5386 C  CE1 . PHE A 1 670  ? 37.613 94.300  -38.328 1.00 15.83 ? 670  PHE A CE1 1 
ATOM   5387 C  CE2 . PHE A 1 670  ? 36.453 93.775  -36.271 1.00 16.99 ? 670  PHE A CE2 1 
ATOM   5388 C  CZ  . PHE A 1 670  ? 37.593 94.228  -36.944 1.00 16.07 ? 670  PHE A CZ  1 
ATOM   5389 N  N   . GLY A 1 671  ? 32.020 90.741  -39.660 1.00 14.35 ? 671  GLY A N   1 
ATOM   5390 C  CA  . GLY A 1 671  ? 30.773 90.377  -40.333 1.00 14.65 ? 671  GLY A CA  1 
ATOM   5391 C  C   . GLY A 1 671  ? 29.628 90.314  -39.337 1.00 15.53 ? 671  GLY A C   1 
ATOM   5392 O  O   . GLY A 1 671  ? 29.826 90.296  -38.115 1.00 14.80 ? 671  GLY A O   1 
ATOM   5393 N  N   . ASP A 1 672  ? 28.398 90.301  -39.829 1.00 16.04 ? 672  ASP A N   1 
ATOM   5394 C  CA  . ASP A 1 672  ? 27.273 90.164  -38.921 1.00 16.82 ? 672  ASP A CA  1 
ATOM   5395 C  C   . ASP A 1 672  ? 27.218 88.688  -38.469 1.00 15.89 ? 672  ASP A C   1 
ATOM   5396 O  O   . ASP A 1 672  ? 27.703 87.814  -39.183 1.00 15.26 ? 672  ASP A O   1 
ATOM   5397 C  CB  . ASP A 1 672  ? 25.963 90.439  -39.665 1.00 19.79 ? 672  ASP A CB  1 
ATOM   5398 C  CG  . ASP A 1 672  ? 25.667 91.911  -39.836 1.00 22.05 ? 672  ASP A CG  1 
ATOM   5399 O  OD1 . ASP A 1 672  ? 26.362 92.772  -39.266 1.00 23.00 ? 672  ASP A OD1 1 
ATOM   5400 O  OD2 . ASP A 1 672  ? 24.680 92.194  -40.552 1.00 25.81 ? 672  ASP A OD2 1 
ATOM   5401 N  N   . PRO A 1 673  ? 26.645 88.425  -37.279 1.00 16.89 ? 673  PRO A N   1 
ATOM   5402 C  CA  . PRO A 1 673  ? 26.539 87.026  -36.805 1.00 17.18 ? 673  PRO A CA  1 
ATOM   5403 C  C   . PRO A 1 673  ? 25.943 86.158  -37.910 1.00 16.88 ? 673  PRO A C   1 
ATOM   5404 O  O   . PRO A 1 673  ? 24.991 86.559  -38.625 1.00 17.86 ? 673  PRO A O   1 
ATOM   5405 C  CB  . PRO A 1 673  ? 25.625 87.153  -35.596 1.00 18.08 ? 673  PRO A CB  1 
ATOM   5406 C  CG  . PRO A 1 673  ? 25.956 88.491  -35.028 1.00 18.85 ? 673  PRO A CG  1 
ATOM   5407 C  CD  . PRO A 1 673  ? 26.120 89.370  -36.275 1.00 18.12 ? 673  PRO A CD  1 
ATOM   5408 N  N   . ARG A 1 674  ? 26.470 84.954  -38.052 1.00 16.15 ? 674  ARG A N   1 
ATOM   5409 C  CA  . ARG A 1 674  ? 26.001 84.027  -39.078 1.00 16.24 ? 674  ARG A CA  1 
ATOM   5410 C  C   . ARG A 1 674  ? 26.423 82.606  -38.740 1.00 17.10 ? 674  ARG A C   1 
ATOM   5411 O  O   . ARG A 1 674  ? 27.356 82.411  -37.951 1.00 16.80 ? 674  ARG A O   1 
ATOM   5412 C  CB  . ARG A 1 674  ? 26.588 84.395  -40.452 1.00 17.44 ? 674  ARG A CB  1 
ATOM   5413 C  CG  . ARG A 1 674  ? 28.106 84.309  -40.597 1.00 19.56 ? 674  ARG A CG  1 
ATOM   5414 C  CD  . ARG A 1 674  ? 28.418 84.342  -42.096 1.00 21.78 ? 674  ARG A CD  1 
ATOM   5415 N  NE  . ARG A 1 674  ? 29.792 84.016  -42.448 1.00 24.42 ? 674  ARG A NE  1 
ATOM   5416 C  CZ  . ARG A 1 674  ? 30.768 84.910  -42.592 1.00 24.60 ? 674  ARG A CZ  1 
ATOM   5417 N  NH1 . ARG A 1 674  ? 30.555 86.221  -42.402 1.00 26.11 ? 674  ARG A NH1 1 
ATOM   5418 N  NH2 . ARG A 1 674  ? 31.955 84.488  -42.983 1.00 26.13 ? 674  ARG A NH2 1 
ATOM   5419 N  N   . GLU A 1 675  ? 25.738 81.608  -39.282 1.00 17.15 ? 675  GLU A N   1 
ATOM   5420 C  CA  . GLU A 1 675  ? 26.193 80.261  -39.043 1.00 17.42 ? 675  GLU A CA  1 
ATOM   5421 C  C   . GLU A 1 675  ? 27.516 80.033  -39.760 1.00 18.53 ? 675  GLU A C   1 
ATOM   5422 O  O   . GLU A 1 675  ? 27.803 80.638  -40.820 1.00 19.43 ? 675  GLU A O   1 
ATOM   5423 C  CB  . GLU A 1 675  ? 25.131 79.247  -39.519 1.00 19.61 ? 675  GLU A CB  1 
ATOM   5424 C  CG  . GLU A 1 675  ? 23.856 79.470  -38.798 1.00 22.92 ? 675  GLU A CG  1 
ATOM   5425 C  CD  . GLU A 1 675  ? 22.953 78.252  -38.774 1.00 26.26 ? 675  GLU A CD  1 
ATOM   5426 O  OE1 . GLU A 1 675  ? 23.034 77.464  -39.749 1.00 28.07 ? 675  GLU A OE1 1 
ATOM   5427 O  OE2 . GLU A 1 675  ? 22.163 78.090  -37.782 1.00 28.00 ? 675  GLU A OE2 1 
ATOM   5428 N  N   . ILE A 1 676  ? 28.379 79.191  -39.202 1.00 18.01 ? 676  ILE A N   1 
ATOM   5429 C  CA  . ILE A 1 676  ? 29.608 78.917  -39.896 1.00 19.36 ? 676  ILE A CA  1 
ATOM   5430 C  C   . ILE A 1 676  ? 30.027 77.480  -39.721 1.00 17.18 ? 676  ILE A C   1 
ATOM   5431 O  O   . ILE A 1 676  ? 29.577 76.809  -38.789 1.00 17.53 ? 676  ILE A O   1 
ATOM   5432 C  CB  . ILE A 1 676  ? 30.743 79.792  -39.464 1.00 21.67 ? 676  ILE A CB  1 
ATOM   5433 C  CG1 . ILE A 1 676  ? 31.074 79.521  -38.031 1.00 21.58 ? 676  ILE A CG1 1 
ATOM   5434 C  CG2 . ILE A 1 676  ? 30.426 81.250  -39.649 1.00 24.25 ? 676  ILE A CG2 1 
ATOM   5435 C  CD1 . ILE A 1 676  ? 32.520 79.191  -37.908 1.00 24.78 ? 676  ILE A CD1 1 
ATOM   5436 N  N   . SER A 1 677  ? 30.885 77.036  -40.627 1.00 16.97 ? 677  SER A N   1 
ATOM   5437 C  CA  . SER A 1 677  ? 31.398 75.670  -40.667 1.00 17.08 ? 677  SER A CA  1 
ATOM   5438 C  C   . SER A 1 677  ? 32.920 75.670  -40.746 1.00 17.20 ? 677  SER A C   1 
ATOM   5439 O  O   . SER A 1 677  ? 33.516 76.493  -41.438 1.00 17.95 ? 677  SER A O   1 
ATOM   5440 C  CB  A SER A 1 677  ? 30.826 74.970  -41.908 0.50 18.65 ? 677  SER A CB  1 
ATOM   5441 C  CB  B SER A 1 677  ? 30.752 74.763  -41.669 0.50 17.51 ? 677  SER A CB  1 
ATOM   5442 O  OG  A SER A 1 677  ? 31.350 73.674  -42.048 0.50 19.95 ? 677  SER A OG  1 
ATOM   5443 O  OG  B SER A 1 677  ? 29.402 74.488  -41.366 0.50 17.21 ? 677  SER A OG  1 
ATOM   5444 N  N   . LEU A 1 678  ? 33.570 74.742  -40.042 1.00 15.91 ? 678  LEU A N   1 
ATOM   5445 C  CA  . LEU A 1 678  ? 35.008 74.665  -40.073 1.00 15.30 ? 678  LEU A CA  1 
ATOM   5446 C  C   . LEU A 1 678  ? 35.474 73.228  -40.133 1.00 15.16 ? 678  LEU A C   1 
ATOM   5447 O  O   . LEU A 1 678  ? 34.804 72.325  -39.579 1.00 14.83 ? 678  LEU A O   1 
ATOM   5448 C  CB  . LEU A 1 678  ? 35.622 75.225  -38.783 1.00 17.30 ? 678  LEU A CB  1 
ATOM   5449 C  CG  . LEU A 1 678  ? 35.696 76.715  -38.514 1.00 17.38 ? 678  LEU A CG  1 
ATOM   5450 C  CD1 . LEU A 1 678  ? 36.048 76.897  -37.029 1.00 18.93 ? 678  LEU A CD1 1 
ATOM   5451 C  CD2 . LEU A 1 678  ? 36.766 77.352  -39.351 1.00 19.98 ? 678  LEU A CD2 1 
ATOM   5452 N  N   . ARG A 1 679  ? 36.613 73.026  -40.768 1.00 14.19 ? 679  ARG A N   1 
ATOM   5453 C  CA  . ARG A 1 679  ? 37.215 71.700  -40.828 1.00 16.43 ? 679  ARG A CA  1 
ATOM   5454 C  C   . ARG A 1 679  ? 38.727 71.870  -40.825 1.00 16.60 ? 679  ARG A C   1 
ATOM   5455 O  O   . ARG A 1 679  ? 39.301 72.648  -41.633 1.00 18.73 ? 679  ARG A O   1 
ATOM   5456 C  CB  . ARG A 1 679  ? 36.758 70.955  -42.096 1.00 19.13 ? 679  ARG A CB  1 
ATOM   5457 C  CG  . ARG A 1 679  ? 37.330 69.538  -42.171 1.00 20.80 ? 679  ARG A CG  1 
ATOM   5458 C  CD  . ARG A 1 679  ? 37.153 68.972  -43.572 1.00 24.44 ? 679  ARG A CD  1 
ATOM   5459 N  NE  . ARG A 1 679  ? 37.449 67.556  -43.533 1.00 28.62 ? 679  ARG A NE  1 
ATOM   5460 C  CZ  . ARG A 1 679  ? 37.587 66.799  -44.609 1.00 30.54 ? 679  ARG A CZ  1 
ATOM   5461 N  NH1 . ARG A 1 679  ? 37.460 67.338  -45.820 1.00 32.56 ? 679  ARG A NH1 1 
ATOM   5462 N  NH2 . ARG A 1 679  ? 37.822 65.502  -44.468 1.00 32.60 ? 679  ARG A NH2 1 
ATOM   5463 N  N   . VAL A 1 680  ? 39.391 71.203  -39.887 1.00 15.56 ? 680  VAL A N   1 
ATOM   5464 C  CA  . VAL A 1 680  ? 40.822 71.205  -39.835 1.00 15.47 ? 680  VAL A CA  1 
ATOM   5465 C  C   . VAL A 1 680  ? 41.345 69.850  -40.315 1.00 18.21 ? 680  VAL A C   1 
ATOM   5466 O  O   . VAL A 1 680  ? 40.854 68.782  -39.892 1.00 17.86 ? 680  VAL A O   1 
ATOM   5467 C  CB  . VAL A 1 680  ? 41.325 71.457  -38.392 1.00 14.59 ? 680  VAL A CB  1 
ATOM   5468 C  CG1 . VAL A 1 680  ? 42.806 71.263  -38.335 1.00 15.08 ? 680  VAL A CG1 1 
ATOM   5469 C  CG2 . VAL A 1 680  ? 40.906 72.931  -37.959 1.00 13.74 ? 680  VAL A CG2 1 
ATOM   5470 N  N   . GLY A 1 681  ? 42.334 69.924  -41.208 1.00 18.88 ? 681  GLY A N   1 
ATOM   5471 C  CA  . GLY A 1 681  ? 42.919 68.722  -41.779 1.00 22.55 ? 681  GLY A CA  1 
ATOM   5472 C  C   . GLY A 1 681  ? 41.842 67.878  -42.471 1.00 23.99 ? 681  GLY A C   1 
ATOM   5473 O  O   . GLY A 1 681  ? 40.964 68.386  -43.191 1.00 24.81 ? 681  GLY A O   1 
ATOM   5474 N  N   . ASN A 1 682  ? 41.905 66.572  -42.212 1.00 27.45 ? 682  ASN A N   1 
ATOM   5475 C  CA  . ASN A 1 682  ? 40.953 65.616  -42.781 1.00 28.96 ? 682  ASN A CA  1 
ATOM   5476 C  C   . ASN A 1 682  ? 39.962 65.209  -41.712 1.00 28.82 ? 682  ASN A C   1 
ATOM   5477 O  O   . ASN A 1 682  ? 39.174 64.271  -41.901 1.00 30.18 ? 682  ASN A O   1 
ATOM   5478 C  CB  . ASN A 1 682  ? 41.676 64.363  -43.249 1.00 31.95 ? 682  ASN A CB  1 
ATOM   5479 C  CG  . ASN A 1 682  ? 42.556 64.628  -44.421 1.00 34.22 ? 682  ASN A CG  1 
ATOM   5480 O  OD1 . ASN A 1 682  ? 42.100 65.156  -45.440 1.00 36.87 ? 682  ASN A OD1 1 
ATOM   5481 N  ND2 . ASN A 1 682  ? 43.836 64.274  -44.295 1.00 35.94 ? 682  ASN A ND2 1 
ATOM   5482 N  N   . GLY A 1 683  ? 39.993 65.930  -40.595 1.00 27.11 ? 683  GLY A N   1 
ATOM   5483 C  CA  . GLY A 1 683  ? 39.144 65.612  -39.474 1.00 24.71 ? 683  GLY A CA  1 
ATOM   5484 C  C   . GLY A 1 683  ? 37.695 65.935  -39.688 1.00 22.30 ? 683  GLY A C   1 
ATOM   5485 O  O   . GLY A 1 683  ? 37.285 66.165  -40.829 1.00 23.11 ? 683  GLY A O   1 
ATOM   5486 N  N   . PRO A 1 684  ? 36.896 66.009  -38.601 1.00 20.34 ? 684  PRO A N   1 
ATOM   5487 C  CA  . PRO A 1 684  ? 35.473 66.313  -38.765 1.00 18.85 ? 684  PRO A CA  1 
ATOM   5488 C  C   . PRO A 1 684  ? 35.173 67.746  -39.179 1.00 17.15 ? 684  PRO A C   1 
ATOM   5489 O  O   . PRO A 1 684  ? 35.994 68.626  -39.009 1.00 16.76 ? 684  PRO A O   1 
ATOM   5490 C  CB  . PRO A 1 684  ? 34.871 65.991  -37.391 1.00 18.31 ? 684  PRO A CB  1 
ATOM   5491 C  CG  . PRO A 1 684  ? 36.033 66.266  -36.416 1.00 20.56 ? 684  PRO A CG  1 
ATOM   5492 C  CD  . PRO A 1 684  ? 37.260 65.815  -37.181 1.00 20.72 ? 684  PRO A CD  1 
ATOM   5493 N  N   . THR A 1 685  ? 33.990 67.956  -39.723 1.00 16.21 ? 685  THR A N   1 
ATOM   5494 C  CA  . THR A 1 685  ? 33.543 69.293  -40.089 1.00 15.87 ? 685  THR A CA  1 
ATOM   5495 C  C   . THR A 1 685  ? 32.497 69.627  -39.045 1.00 16.31 ? 685  THR A C   1 
ATOM   5496 O  O   . THR A 1 685  ? 31.563 68.861  -38.820 1.00 15.32 ? 685  THR A O   1 
ATOM   5497 C  CB  . THR A 1 685  ? 32.942 69.326  -41.508 1.00 17.82 ? 685  THR A CB  1 
ATOM   5498 O  OG1 . THR A 1 685  ? 33.966 69.000  -42.439 1.00 18.85 ? 685  THR A OG1 1 
ATOM   5499 C  CG2 . THR A 1 685  ? 32.382 70.696  -41.804 1.00 18.31 ? 685  THR A CG2 1 
ATOM   5500 N  N   . LEU A 1 686  ? 32.651 70.786  -38.387 1.00 14.38 ? 686  LEU A N   1 
ATOM   5501 C  CA  . LEU A 1 686  ? 31.760 71.217  -37.339 1.00 14.43 ? 686  LEU A CA  1 
ATOM   5502 C  C   . LEU A 1 686  ? 30.989 72.436  -37.808 1.00 13.30 ? 686  LEU A C   1 
ATOM   5503 O  O   . LEU A 1 686  ? 31.588 73.377  -38.354 1.00 13.65 ? 686  LEU A O   1 
ATOM   5504 C  CB  . LEU A 1 686  ? 32.552 71.614  -36.056 1.00 13.36 ? 686  LEU A CB  1 
ATOM   5505 C  CG  . LEU A 1 686  ? 33.499 70.614  -35.374 1.00 18.44 ? 686  LEU A CG  1 
ATOM   5506 C  CD1 . LEU A 1 686  ? 33.562 70.980  -33.917 1.00 17.72 ? 686  LEU A CD1 1 
ATOM   5507 C  CD2 . LEU A 1 686  ? 33.190 69.203  -35.590 1.00 17.32 ? 686  LEU A CD2 1 
ATOM   5508 N  N   . ALA A 1 687  ? 29.705 72.431  -37.543 1.00 12.63 ? 687  ALA A N   1 
ATOM   5509 C  CA  . ALA A 1 687  ? 28.836 73.565  -37.839 1.00 12.72 ? 687  ALA A CA  1 
ATOM   5510 C  C   . ALA A 1 687  ? 28.420 74.243  -36.558 1.00 13.70 ? 687  ALA A C   1 
ATOM   5511 O  O   . ALA A 1 687  ? 28.073 73.597  -35.572 1.00 13.97 ? 687  ALA A O   1 
ATOM   5512 C  CB  . ALA A 1 687  ? 27.567 73.103  -38.609 1.00 13.51 ? 687  ALA A CB  1 
ATOM   5513 N  N   . PHE A 1 688  ? 28.354 75.560  -36.603 1.00 12.05 ? 688  PHE A N   1 
ATOM   5514 C  CA  . PHE A 1 688  ? 28.030 76.374  -35.465 1.00 12.14 ? 688  PHE A CA  1 
ATOM   5515 C  C   . PHE A 1 688  ? 26.862 77.299  -35.714 1.00 12.08 ? 688  PHE A C   1 
ATOM   5516 O  O   . PHE A 1 688  ? 26.686 77.795  -36.857 1.00 14.70 ? 688  PHE A O   1 
ATOM   5517 C  CB  . PHE A 1 688  ? 29.238 77.258  -35.052 1.00 11.94 ? 688  PHE A CB  1 
ATOM   5518 C  CG  . PHE A 1 688  ? 30.439 76.457  -34.673 1.00 11.26 ? 688  PHE A CG  1 
ATOM   5519 C  CD1 . PHE A 1 688  ? 31.290 75.988  -35.641 1.00 11.28 ? 688  PHE A CD1 1 
ATOM   5520 C  CD2 . PHE A 1 688  ? 30.698 76.174  -33.343 1.00 10.43 ? 688  PHE A CD2 1 
ATOM   5521 C  CE1 . PHE A 1 688  ? 32.434 75.233  -35.364 1.00 11.42 ? 688  PHE A CE1 1 
ATOM   5522 C  CE2 . PHE A 1 688  ? 31.825 75.428  -33.009 1.00 11.49 ? 688  PHE A CE2 1 
ATOM   5523 C  CZ  . PHE A 1 688  ? 32.710 74.946  -34.012 1.00 10.80 ? 688  PHE A CZ  1 
ATOM   5524 N  N   . SER A 1 689  ? 26.083 77.546  -34.703 1.00 12.81 ? 689  SER A N   1 
ATOM   5525 C  CA  . SER A 1 689  ? 24.963 78.515  -34.768 1.00 14.24 ? 689  SER A CA  1 
ATOM   5526 C  C   . SER A 1 689  ? 25.513 79.940  -34.833 1.00 14.58 ? 689  SER A C   1 
ATOM   5527 O  O   . SER A 1 689  ? 26.722 80.178  -34.613 1.00 13.53 ? 689  SER A O   1 
ATOM   5528 C  CB  . SER A 1 689  ? 24.118 78.414  -33.512 1.00 15.13 ? 689  SER A CB  1 
ATOM   5529 O  OG  . SER A 1 689  ? 24.756 78.987  -32.390 1.00 14.81 ? 689  SER A OG  1 
ATOM   5530 N  N   . GLU A 1 690  ? 24.631 80.896  -35.116 1.00 14.94 ? 690  GLU A N   1 
ATOM   5531 C  CA  . GLU A 1 690  ? 25.037 82.292  -35.134 1.00 15.61 ? 690  GLU A CA  1 
ATOM   5532 C  C   . GLU A 1 690  ? 25.426 82.778  -33.737 1.00 15.85 ? 690  GLU A C   1 
ATOM   5533 O  O   . GLU A 1 690  ? 25.994 83.861  -33.596 1.00 14.71 ? 690  GLU A O   1 
ATOM   5534 C  CB  . GLU A 1 690  ? 23.910 83.149  -35.757 1.00 18.33 ? 690  GLU A CB  1 
ATOM   5535 C  CG  . GLU A 1 690  ? 22.811 83.553  -34.879 1.00 21.98 ? 690  GLU A CG  1 
ATOM   5536 C  CD  . GLU A 1 690  ? 21.943 84.632  -35.578 1.00 24.44 ? 690  GLU A CD  1 
ATOM   5537 O  OE1 . GLU A 1 690  ? 21.435 84.326  -36.680 1.00 27.19 ? 690  GLU A OE1 1 
ATOM   5538 O  OE2 . GLU A 1 690  ? 21.797 85.765  -35.042 1.00 27.45 ? 690  GLU A OE2 1 
ATOM   5539 N  N   . GLN A 1 691  ? 25.097 82.011  -32.684 1.00 15.19 ? 691  GLN A N   1 
ATOM   5540 C  CA  . GLN A 1 691  ? 25.551 82.382  -31.342 1.00 15.88 ? 691  GLN A CA  1 
ATOM   5541 C  C   . GLN A 1 691  ? 26.871 81.696  -30.970 1.00 13.88 ? 691  GLN A C   1 
ATOM   5542 O  O   . GLN A 1 691  ? 27.266 81.765  -29.830 1.00 15.26 ? 691  GLN A O   1 
ATOM   5543 C  CB  . GLN A 1 691  ? 24.550 82.067  -30.245 1.00 17.03 ? 691  GLN A CB  1 
ATOM   5544 C  CG  . GLN A 1 691  ? 23.270 82.817  -30.370 1.00 21.15 ? 691  GLN A CG  1 
ATOM   5545 C  CD  . GLN A 1 691  ? 22.249 81.807  -30.590 1.00 26.02 ? 691  GLN A CD  1 
ATOM   5546 O  OE1 . GLN A 1 691  ? 21.727 81.205  -29.613 1.00 28.11 ? 691  GLN A OE1 1 
ATOM   5547 N  NE2 . GLN A 1 691  ? 21.995 81.505  -31.856 1.00 25.87 ? 691  GLN A NE2 1 
ATOM   5548 N  N   . GLY A 1 692  ? 27.515 81.058  -31.924 1.00 12.98 ? 692  GLY A N   1 
ATOM   5549 C  CA  . GLY A 1 692  ? 28.847 80.463  -31.698 1.00 12.98 ? 692  GLY A CA  1 
ATOM   5550 C  C   . GLY A 1 692  ? 28.868 79.114  -31.018 1.00 12.91 ? 692  GLY A C   1 
ATOM   5551 O  O   . GLY A 1 692  ? 29.918 78.693  -30.566 1.00 13.41 ? 692  GLY A O   1 
ATOM   5552 N  N   . LEU A 1 693  ? 27.736 78.421  -30.993 1.00 12.32 ? 693  LEU A N   1 
ATOM   5553 C  CA  . LEU A 1 693  ? 27.618 77.106  -30.324 1.00 11.96 ? 693  LEU A CA  1 
ATOM   5554 C  C   . LEU A 1 693  ? 27.463 76.009  -31.348 1.00 12.52 ? 693  LEU A C   1 
ATOM   5555 O  O   . LEU A 1 693  ? 26.759 76.148  -32.377 1.00 12.65 ? 693  LEU A O   1 
ATOM   5556 C  CB  . LEU A 1 693  ? 26.423 77.118  -29.379 1.00 14.91 ? 693  LEU A CB  1 
ATOM   5557 C  CG  . LEU A 1 693  ? 26.605 78.083  -28.197 1.00 16.50 ? 693  LEU A CG  1 
ATOM   5558 C  CD1 . LEU A 1 693  ? 25.292 78.807  -27.958 1.00 20.43 ? 693  LEU A CD1 1 
ATOM   5559 C  CD2 . LEU A 1 693  ? 27.006 77.353  -26.925 1.00 18.22 ? 693  LEU A CD2 1 
ATOM   5560 N  N   . LEU A 1 694  ? 28.108 74.877  -31.095 1.00 11.67 ? 694  LEU A N   1 
ATOM   5561 C  CA  . LEU A 1 694  ? 28.043 73.732  -31.971 1.00 11.39 ? 694  LEU A CA  1 
ATOM   5562 C  C   . LEU A 1 694  ? 26.599 73.316  -32.233 1.00 10.69 ? 694  LEU A C   1 
ATOM   5563 O  O   . LEU A 1 694  ? 25.756 73.346  -31.331 1.00 11.89 ? 694  LEU A O   1 
ATOM   5564 C  CB  . LEU A 1 694  ? 28.784 72.565  -31.277 1.00 11.71 ? 694  LEU A CB  1 
ATOM   5565 C  CG  . LEU A 1 694  ? 28.923 71.332  -32.165 1.00 12.20 ? 694  LEU A CG  1 
ATOM   5566 C  CD1 . LEU A 1 694  ? 29.847 71.575  -33.317 1.00 13.11 ? 694  LEU A CD1 1 
ATOM   5567 C  CD2 . LEU A 1 694  ? 29.498 70.173  -31.297 1.00 12.61 ? 694  LEU A CD2 1 
ATOM   5568 N  N   . LYS A 1 695  ? 26.348 72.996  -33.492 1.00 12.23 ? 695  LYS A N   1 
ATOM   5569 C  CA  . LYS A 1 695  ? 25.051 72.531  -33.945 1.00 14.46 ? 695  LYS A CA  1 
ATOM   5570 C  C   . LYS A 1 695  ? 25.159 71.153  -34.551 1.00 12.76 ? 695  LYS A C   1 
ATOM   5571 O  O   . LYS A 1 695  ? 24.170 70.407  -34.427 1.00 14.36 ? 695  LYS A O   1 
ATOM   5572 C  CB  . LYS A 1 695  ? 24.521 73.496  -35.019 1.00 19.41 ? 695  LYS A CB  1 
ATOM   5573 C  CG  . LYS A 1 695  ? 23.081 73.508  -35.255 1.00 25.07 ? 695  LYS A CG  1 
ATOM   5574 C  CD  . LYS A 1 695  ? 22.854 74.711  -36.216 1.00 28.66 ? 695  LYS A CD  1 
ATOM   5575 C  CE  . LYS A 1 695  ? 21.468 74.744  -36.766 1.00 30.59 ? 695  LYS A CE  1 
ATOM   5576 N  NZ  . LYS A 1 695  ? 21.510 75.235  -38.174 1.00 32.04 ? 695  LYS A NZ  1 
ATOM   5577 N  N   . SER A 1 696  ? 26.248 70.793  -35.200 1.00 12.86 ? 696  SER A N   1 
ATOM   5578 C  CA  . SER A 1 696  ? 26.372 69.486  -35.843 1.00 13.53 ? 696  SER A CA  1 
ATOM   5579 C  C   . SER A 1 696  ? 27.781 69.101  -36.094 1.00 13.91 ? 696  SER A C   1 
ATOM   5580 O  O   . SER A 1 696  ? 28.698 69.977  -36.150 1.00 13.04 ? 696  SER A O   1 
ATOM   5581 C  CB  . SER A 1 696  ? 25.576 69.468  -37.182 1.00 16.77 ? 696  SER A CB  1 
ATOM   5582 O  OG  . SER A 1 696  ? 26.265 70.206  -38.202 1.00 18.13 ? 696  SER A OG  1 
ATOM   5583 N  N   . ILE A 1 697  ? 28.018 67.794  -36.249 1.00 14.74 ? 697  ILE A N   1 
ATOM   5584 C  CA  . ILE A 1 697  ? 29.323 67.260  -36.547 1.00 14.61 ? 697  ILE A CA  1 
ATOM   5585 C  C   . ILE A 1 697  ? 29.173 66.300  -37.714 1.00 16.59 ? 697  ILE A C   1 
ATOM   5586 O  O   . ILE A 1 697  ? 28.257 65.459  -37.676 1.00 16.91 ? 697  ILE A O   1 
ATOM   5587 C  CB  . ILE A 1 697  ? 29.967 66.445  -35.337 1.00 14.87 ? 697  ILE A CB  1 
ATOM   5588 C  CG1 . ILE A 1 697  ? 30.155 67.344  -34.131 1.00 14.81 ? 697  ILE A CG1 1 
ATOM   5589 C  CG2 . ILE A 1 697  ? 31.284 65.870  -35.716 1.00 15.26 ? 697  ILE A CG2 1 
ATOM   5590 C  CD1 . ILE A 1 697  ? 30.611 66.512  -32.892 1.00 14.63 ? 697  ILE A CD1 1 
ATOM   5591 N  N   . GLN A 1 698  ? 30.010 66.465  -38.733 1.00 15.84 ? 698  GLN A N   1 
ATOM   5592 C  CA  . GLN A 1 698  ? 30.005 65.591  -39.913 1.00 17.47 ? 698  GLN A CA  1 
ATOM   5593 C  C   . GLN A 1 698  ? 31.357 64.907  -39.861 1.00 17.57 ? 698  GLN A C   1 
ATOM   5594 O  O   . GLN A 1 698  ? 32.414 65.516  -40.015 1.00 17.23 ? 698  GLN A O   1 
ATOM   5595 C  CB  . GLN A 1 698  ? 29.868 66.414  -41.204 1.00 18.08 ? 698  GLN A CB  1 
ATOM   5596 C  CG  . GLN A 1 698  ? 29.804 65.477  -42.417 1.00 20.24 ? 698  GLN A CG  1 
ATOM   5597 C  CD  . GLN A 1 698  ? 29.921 66.247  -43.701 1.00 22.17 ? 698  GLN A CD  1 
ATOM   5598 O  OE1 . GLN A 1 698  ? 29.074 66.119  -44.585 1.00 25.08 ? 698  GLN A OE1 1 
ATOM   5599 N  NE2 . GLN A 1 698  ? 30.958 67.055  -43.812 1.00 22.50 ? 698  GLN A NE2 1 
ATOM   5600 N  N   . LEU A 1 699  ? 31.376 63.594  -39.632 1.00 19.99 ? 699  LEU A N   1 
ATOM   5601 C  CA  . LEU A 1 699  ? 32.639 62.912  -39.482 1.00 21.80 ? 699  LEU A CA  1 
ATOM   5602 C  C   . LEU A 1 699  ? 33.558 62.814  -40.676 1.00 25.03 ? 699  LEU A C   1 
ATOM   5603 O  O   . LEU A 1 699  ? 34.773 62.931  -40.530 1.00 24.73 ? 699  LEU A O   1 
ATOM   5604 C  CB  . LEU A 1 699  ? 32.425 61.496  -38.905 1.00 22.43 ? 699  LEU A CB  1 
ATOM   5605 C  CG  . LEU A 1 699  ? 31.771 61.439  -37.512 1.00 21.47 ? 699  LEU A CG  1 
ATOM   5606 C  CD1 . LEU A 1 699  ? 31.582 59.950  -37.096 1.00 22.37 ? 699  LEU A CD1 1 
ATOM   5607 C  CD2 . LEU A 1 699  ? 32.627 62.163  -36.526 1.00 22.09 ? 699  LEU A CD2 1 
ATOM   5608 N  N   . THR A 1 700  ? 32.981 62.613  -41.857 1.00 28.18 ? 700  THR A N   1 
ATOM   5609 C  CA  . THR A 1 700  ? 33.772 62.456  -43.076 1.00 31.97 ? 700  THR A CA  1 
ATOM   5610 C  C   . THR A 1 700  ? 33.070 63.188  -44.208 1.00 33.83 ? 700  THR A C   1 
ATOM   5611 O  O   . THR A 1 700  ? 31.912 63.556  -44.070 1.00 33.75 ? 700  THR A O   1 
ATOM   5612 C  CB  . THR A 1 700  ? 33.917 60.952  -43.465 1.00 31.81 ? 700  THR A CB  1 
ATOM   5613 O  OG1 . THR A 1 700  ? 32.616 60.388  -43.723 1.00 32.68 ? 700  THR A OG1 1 
ATOM   5614 C  CG2 . THR A 1 700  ? 34.578 60.164  -42.328 1.00 32.48 ? 700  THR A CG2 1 
ATOM   5615 N  N   . GLN A 1 701  ? 33.785 63.398  -45.317 1.00 37.08 ? 701  GLN A N   1 
ATOM   5616 C  CA  . GLN A 1 701  ? 33.249 64.098  -46.494 1.00 40.17 ? 701  GLN A CA  1 
ATOM   5617 C  C   . GLN A 1 701  ? 31.836 63.700  -46.906 1.00 40.70 ? 701  GLN A C   1 
ATOM   5618 O  O   . GLN A 1 701  ? 30.998 64.557  -47.210 1.00 41.39 ? 701  GLN A O   1 
ATOM   5619 C  CB  . GLN A 1 701  ? 34.175 63.901  -47.706 1.00 42.19 ? 701  GLN A CB  1 
ATOM   5620 C  CG  . GLN A 1 701  ? 35.411 64.808  -47.732 1.00 45.19 ? 701  GLN A CG  1 
ATOM   5621 C  CD  . GLN A 1 701  ? 35.056 66.291  -47.863 1.00 46.99 ? 701  GLN A CD  1 
ATOM   5622 O  OE1 . GLN A 1 701  ? 35.943 67.149  -48.022 1.00 47.72 ? 701  GLN A OE1 1 
ATOM   5623 N  NE2 . GLN A 1 701  ? 33.756 66.604  -47.787 1.00 48.16 ? 701  GLN A NE2 1 
ATOM   5624 N  N   . ASP A 1 702  ? 31.574 62.403  -46.901 1.00 41.22 ? 702  ASP A N   1 
ATOM   5625 C  CA  . ASP A 1 702  ? 30.273 61.872  -47.287 1.00 41.65 ? 702  ASP A CA  1 
ATOM   5626 C  C   . ASP A 1 702  ? 29.156 61.859  -46.229 1.00 40.74 ? 702  ASP A C   1 
ATOM   5627 O  O   . ASP A 1 702  ? 28.000 62.230  -46.513 1.00 41.00 ? 702  ASP A O   1 
ATOM   5628 C  CB  . ASP A 1 702  ? 30.468 60.443  -47.810 1.00 43.56 ? 702  ASP A CB  1 
ATOM   5629 C  CG  . ASP A 1 702  ? 31.289 59.566  -46.847 1.00 45.20 ? 702  ASP A CG  1 
ATOM   5630 O  OD1 . ASP A 1 702  ? 32.395 60.001  -46.434 1.00 45.63 ? 702  ASP A OD1 1 
ATOM   5631 O  OD2 . ASP A 1 702  ? 30.832 58.440  -46.521 1.00 45.88 ? 702  ASP A OD2 1 
ATOM   5632 N  N   . SER A 1 703  ? 29.521 61.440  -45.017 1.00 38.80 ? 703  SER A N   1 
ATOM   5633 C  CA  . SER A 1 703  ? 28.593 61.275  -43.907 1.00 36.49 ? 703  SER A CA  1 
ATOM   5634 C  C   . SER A 1 703  ? 27.610 62.390  -43.574 1.00 34.61 ? 703  SER A C   1 
ATOM   5635 O  O   . SER A 1 703  ? 27.758 63.527  -44.008 1.00 34.71 ? 703  SER A O   1 
ATOM   5636 C  CB  . SER A 1 703  ? 29.385 60.873  -42.659 1.00 36.98 ? 703  SER A CB  1 
ATOM   5637 O  OG  . SER A 1 703  ? 30.217 61.926  -42.206 1.00 35.95 ? 703  SER A OG  1 
ATOM   5638 N  N   . PRO A 1 704  ? 26.576 62.070  -42.782 1.00 32.73 ? 704  PRO A N   1 
ATOM   5639 C  CA  . PRO A 1 704  ? 25.610 63.104  -42.435 1.00 30.91 ? 704  PRO A CA  1 
ATOM   5640 C  C   . PRO A 1 704  ? 26.097 64.094  -41.387 1.00 28.88 ? 704  PRO A C   1 
ATOM   5641 O  O   . PRO A 1 704  ? 27.060 63.842  -40.642 1.00 27.49 ? 704  PRO A O   1 
ATOM   5642 C  CB  . PRO A 1 704  ? 24.397 62.312  -41.956 1.00 31.89 ? 704  PRO A CB  1 
ATOM   5643 C  CG  . PRO A 1 704  ? 24.984 61.070  -41.437 1.00 32.64 ? 704  PRO A CG  1 
ATOM   5644 C  CD  . PRO A 1 704  ? 26.101 60.737  -42.374 1.00 32.60 ? 704  PRO A CD  1 
ATOM   5645 N  N   . HIS A 1 705  ? 25.430 65.240  -41.370 1.00 27.05 ? 705  HIS A N   1 
ATOM   5646 C  CA  . HIS A 1 705  ? 25.736 66.281  -40.386 1.00 24.86 ? 705  HIS A CA  1 
ATOM   5647 C  C   . HIS A 1 705  ? 24.863 65.868  -39.192 1.00 22.87 ? 705  HIS A C   1 
ATOM   5648 O  O   . HIS A 1 705  ? 23.679 66.159  -39.121 1.00 23.28 ? 705  HIS A O   1 
ATOM   5649 C  CB  . HIS A 1 705  ? 25.354 67.674  -40.963 1.00 26.94 ? 705  HIS A CB  1 
ATOM   5650 C  CG  . HIS A 1 705  ? 26.244 68.127  -42.095 1.00 28.71 ? 705  HIS A CG  1 
ATOM   5651 N  ND1 . HIS A 1 705  ? 27.478 68.716  -41.889 1.00 28.86 ? 705  HIS A ND1 1 
ATOM   5652 C  CD2 . HIS A 1 705  ? 26.136 67.960  -43.438 1.00 29.27 ? 705  HIS A CD2 1 
ATOM   5653 C  CE1 . HIS A 1 705  ? 28.097 68.872  -43.047 1.00 30.11 ? 705  HIS A CE1 1 
ATOM   5654 N  NE2 . HIS A 1 705  ? 27.302 68.420  -44.007 1.00 30.21 ? 705  HIS A NE2 1 
ATOM   5655 N  N   . VAL A 1 706  ? 25.500 65.204  -38.220 1.00 19.57 ? 706  VAL A N   1 
ATOM   5656 C  CA  . VAL A 1 706  ? 24.817 64.700  -37.036 1.00 17.19 ? 706  VAL A CA  1 
ATOM   5657 C  C   . VAL A 1 706  ? 24.483 65.804  -36.043 1.00 15.56 ? 706  VAL A C   1 
ATOM   5658 O  O   . VAL A 1 706  ? 25.396 66.508  -35.590 1.00 14.92 ? 706  VAL A O   1 
ATOM   5659 C  CB  . VAL A 1 706  ? 25.750 63.632  -36.345 1.00 17.27 ? 706  VAL A CB  1 
ATOM   5660 C  CG1 . VAL A 1 706  ? 25.059 63.034  -35.152 1.00 16.98 ? 706  VAL A CG1 1 
ATOM   5661 C  CG2 . VAL A 1 706  ? 26.189 62.581  -37.339 1.00 18.32 ? 706  VAL A CG2 1 
ATOM   5662 N  N   . PRO A 1 707  ? 23.222 65.996  -35.661 1.00 15.27 ? 707  PRO A N   1 
ATOM   5663 C  CA  . PRO A 1 707  ? 22.892 67.055  -34.712 1.00 15.86 ? 707  PRO A CA  1 
ATOM   5664 C  C   . PRO A 1 707  ? 23.609 66.813  -33.372 1.00 15.56 ? 707  PRO A C   1 
ATOM   5665 O  O   . PRO A 1 707  ? 23.455 65.728  -32.767 1.00 15.93 ? 707  PRO A O   1 
ATOM   5666 C  CB  . PRO A 1 707  ? 21.366 66.947  -34.564 1.00 16.55 ? 707  PRO A CB  1 
ATOM   5667 C  CG  . PRO A 1 707  ? 20.924 66.306  -35.843 1.00 17.92 ? 707  PRO A CG  1 
ATOM   5668 C  CD  . PRO A 1 707  ? 21.994 65.301  -36.124 1.00 15.15 ? 707  PRO A CD  1 
ATOM   5669 N  N   . VAL A 1 708  ? 24.414 67.795  -32.922 1.00 15.10 ? 708  VAL A N   1 
ATOM   5670 C  CA  . VAL A 1 708  ? 25.107 67.749  -31.609 1.00 13.12 ? 708  VAL A CA  1 
ATOM   5671 C  C   . VAL A 1 708  ? 25.042 69.225  -31.241 1.00 13.13 ? 708  VAL A C   1 
ATOM   5672 O  O   . VAL A 1 708  ? 25.801 70.045  -31.790 1.00 14.30 ? 708  VAL A O   1 
ATOM   5673 C  CB  . VAL A 1 708  ? 26.545 67.242  -31.728 1.00 13.75 ? 708  VAL A CB  1 
ATOM   5674 C  CG1 . VAL A 1 708  ? 27.191 67.209  -30.311 1.00 12.72 ? 708  VAL A CG1 1 
ATOM   5675 C  CG2 . VAL A 1 708  ? 26.565 65.817  -32.323 1.00 14.64 ? 708  VAL A CG2 1 
ATOM   5676 N  N   . HIS A 1 709  ? 24.135 69.573  -30.358 1.00 12.68 ? 709  HIS A N   1 
ATOM   5677 C  CA  . HIS A 1 709  ? 23.939 70.974  -30.004 1.00 13.54 ? 709  HIS A CA  1 
ATOM   5678 C  C   . HIS A 1 709  ? 24.378 71.305  -28.577 1.00 13.12 ? 709  HIS A C   1 
ATOM   5679 O  O   A HIS A 1 709  ? 23.948 70.631  -27.645 0.50 13.32 ? 709  HIS A O   1 
ATOM   5680 O  O   B HIS A 1 709  ? 23.792 70.763  -27.606 0.50 13.12 ? 709  HIS A O   1 
ATOM   5681 C  CB  A HIS A 1 709  ? 22.437 71.327  -30.122 0.50 15.86 ? 709  HIS A CB  1 
ATOM   5682 C  CB  B HIS A 1 709  ? 22.552 71.403  -30.288 0.50 15.26 ? 709  HIS A CB  1 
ATOM   5683 C  CG  A HIS A 1 709  ? 21.916 71.465  -31.526 0.50 18.67 ? 709  HIS A CG  1 
ATOM   5684 C  CG  B HIS A 1 709  ? 22.258 72.840  -29.979 0.50 17.43 ? 709  HIS A CG  1 
ATOM   5685 N  ND1 A HIS A 1 709  ? 21.961 70.449  -32.458 0.50 20.73 ? 709  HIS A ND1 1 
ATOM   5686 N  ND1 B HIS A 1 709  ? 23.070 73.873  -30.399 0.50 18.40 ? 709  HIS A ND1 1 
ATOM   5687 C  CD2 A HIS A 1 709  ? 21.256 72.487  -32.122 0.50 20.49 ? 709  HIS A CD2 1 
ATOM   5688 C  CD2 B HIS A 1 709  ? 21.213 73.417  -29.339 0.50 18.30 ? 709  HIS A CD2 1 
ATOM   5689 C  CE1 A HIS A 1 709  ? 21.348 70.835  -33.562 0.50 18.48 ? 709  HIS A CE1 1 
ATOM   5690 C  CE1 B HIS A 1 709  ? 22.536 75.026  -30.030 0.50 18.86 ? 709  HIS A CE1 1 
ATOM   5691 N  NE2 A HIS A 1 709  ? 20.909 72.068  -33.384 0.50 21.11 ? 709  HIS A NE2 1 
ATOM   5692 N  NE2 B HIS A 1 709  ? 21.408 74.776  -29.389 0.50 19.21 ? 709  HIS A NE2 1 
ATOM   5693 N  N   . PHE A 1 710  ? 25.262 72.300  -28.393 1.00 12.08 ? 710  PHE A N   1 
ATOM   5694 C  CA  . PHE A 1 710  ? 25.629 72.739  -27.081 1.00 11.36 ? 710  PHE A CA  1 
ATOM   5695 C  C   . PHE A 1 710  ? 24.634 73.834  -26.629 1.00 11.29 ? 710  PHE A C   1 
ATOM   5696 O  O   . PHE A 1 710  ? 24.186 74.701  -27.445 1.00 12.06 ? 710  PHE A O   1 
ATOM   5697 C  CB  . PHE A 1 710  ? 27.059 73.333  -27.053 1.00 12.02 ? 710  PHE A CB  1 
ATOM   5698 C  CG  . PHE A 1 710  ? 28.153 72.361  -26.644 1.00 13.29 ? 710  PHE A CG  1 
ATOM   5699 C  CD1 . PHE A 1 710  ? 28.078 71.687  -25.442 1.00 15.17 ? 710  PHE A CD1 1 
ATOM   5700 C  CD2 . PHE A 1 710  ? 29.270 72.163  -27.442 1.00 14.74 ? 710  PHE A CD2 1 
ATOM   5701 C  CE1 . PHE A 1 710  ? 29.105 70.807  -25.025 1.00 15.31 ? 710  PHE A CE1 1 
ATOM   5702 C  CE2 . PHE A 1 710  ? 30.296 71.282  -27.008 1.00 13.75 ? 710  PHE A CE2 1 
ATOM   5703 C  CZ  . PHE A 1 710  ? 30.193 70.627  -25.823 1.00 14.90 ? 710  PHE A CZ  1 
ATOM   5704 N  N   . LYS A 1 711  ? 24.273 73.826  -25.359 1.00 11.09 ? 711  LYS A N   1 
ATOM   5705 C  CA  . LYS A 1 711  ? 23.368 74.798  -24.785 1.00 13.03 ? 711  LYS A CA  1 
ATOM   5706 C  C   . LYS A 1 711  ? 23.761 75.020  -23.349 1.00 12.95 ? 711  LYS A C   1 
ATOM   5707 O  O   . LYS A 1 711  ? 24.185 74.056  -22.686 1.00 14.14 ? 711  LYS A O   1 
ATOM   5708 C  CB  . LYS A 1 711  ? 21.912 74.270  -24.856 1.00 15.55 ? 711  LYS A CB  1 
ATOM   5709 C  CG  . LYS A 1 711  ? 20.876 75.234  -24.366 1.00 18.65 ? 711  LYS A CG  1 
ATOM   5710 C  CD  . LYS A 1 711  ? 19.434 74.657  -24.523 1.00 21.04 ? 711  LYS A CD  1 
ATOM   5711 C  CE  . LYS A 1 711  ? 19.074 74.600  -26.016 1.00 22.43 ? 711  LYS A CE  1 
ATOM   5712 N  NZ  . LYS A 1 711  ? 17.753 73.862  -26.168 1.00 23.70 ? 711  LYS A NZ  1 
ATOM   5713 N  N   . PHE A 1 712  ? 23.619 76.232  -22.842 1.00 10.88 ? 712  PHE A N   1 
ATOM   5714 C  CA  . PHE A 1 712  ? 23.860 76.563  -21.466 1.00 11.18 ? 712  PHE A CA  1 
ATOM   5715 C  C   . PHE A 1 712  ? 22.537 76.899  -20.788 1.00 10.14 ? 712  PHE A C   1 
ATOM   5716 O  O   . PHE A 1 712  ? 21.721 77.652  -21.337 1.00 11.44 ? 712  PHE A O   1 
ATOM   5717 C  CB  . PHE A 1 712  ? 24.884 77.731  -21.328 1.00 10.70 ? 712  PHE A CB  1 
ATOM   5718 C  CG  . PHE A 1 712  ? 26.298 77.322  -21.640 1.00 10.66 ? 712  PHE A CG  1 
ATOM   5719 C  CD1 . PHE A 1 712  ? 26.770 77.392  -22.943 1.00 11.01 ? 712  PHE A CD1 1 
ATOM   5720 C  CD2 . PHE A 1 712  ? 27.140 76.822  -20.637 1.00 9.91  ? 712  PHE A CD2 1 
ATOM   5721 C  CE1 . PHE A 1 712  ? 28.065 76.970  -23.261 1.00 10.18 ? 712  PHE A CE1 1 
ATOM   5722 C  CE2 . PHE A 1 712  ? 28.401 76.415  -20.944 1.00 10.01 ? 712  PHE A CE2 1 
ATOM   5723 C  CZ  . PHE A 1 712  ? 28.868 76.480  -22.226 1.00 10.74 ? 712  PHE A CZ  1 
ATOM   5724 N  N   . LEU A 1 713  ? 22.330 76.340  -19.608 1.00 9.93  ? 713  LEU A N   1 
ATOM   5725 C  CA  . LEU A 1 713  ? 21.079 76.545  -18.856 1.00 9.87  ? 713  LEU A CA  1 
ATOM   5726 C  C   . LEU A 1 713  ? 21.401 76.814  -17.412 1.00 10.22 ? 713  LEU A C   1 
ATOM   5727 O  O   . LEU A 1 713  ? 22.586 76.709  -16.977 1.00 11.39 ? 713  LEU A O   1 
ATOM   5728 C  CB  . LEU A 1 713  ? 20.144 75.316  -18.963 1.00 10.97 ? 713  LEU A CB  1 
ATOM   5729 C  CG  . LEU A 1 713  ? 19.832 74.883  -20.396 1.00 11.07 ? 713  LEU A CG  1 
ATOM   5730 C  CD1 . LEU A 1 713  ? 20.702 73.678  -20.821 1.00 12.34 ? 713  LEU A CD1 1 
ATOM   5731 C  CD2 . LEU A 1 713  ? 18.334 74.368  -20.494 1.00 12.21 ? 713  LEU A CD2 1 
ATOM   5732 N  N   . LYS A 1 714  ? 20.401 77.181  -16.632 1.00 11.23 ? 714  LYS A N   1 
ATOM   5733 C  CA  . LYS A 1 714  ? 20.597 77.470  -15.245 1.00 12.52 ? 714  LYS A CA  1 
ATOM   5734 C  C   . LYS A 1 714  ? 19.583 76.822  -14.354 1.00 12.05 ? 714  LYS A C   1 
ATOM   5735 O  O   . LYS A 1 714  ? 18.375 76.743  -14.689 1.00 13.02 ? 714  LYS A O   1 
ATOM   5736 C  CB  . LYS A 1 714  ? 20.575 78.972  -14.982 1.00 17.03 ? 714  LYS A CB  1 
ATOM   5737 C  CG  . LYS A 1 714  ? 19.457 79.695  -15.629 1.00 22.02 ? 714  LYS A CG  1 
ATOM   5738 C  CD  . LYS A 1 714  ? 19.486 81.188  -15.201 1.00 25.36 ? 714  LYS A CD  1 
ATOM   5739 C  CE  . LYS A 1 714  ? 20.830 81.855  -15.501 1.00 26.61 ? 714  LYS A CE  1 
ATOM   5740 N  NZ  . LYS A 1 714  ? 20.888 83.356  -15.251 1.00 29.36 ? 714  LYS A NZ  1 
ATOM   5741 N  N   . TYR A 1 715  ? 20.078 76.279  -13.248 1.00 9.81  ? 715  TYR A N   1 
ATOM   5742 C  CA  . TYR A 1 715  ? 19.219 75.765  -12.206 1.00 10.12 ? 715  TYR A CA  1 
ATOM   5743 C  C   . TYR A 1 715  ? 19.181 76.786  -11.069 1.00 11.39 ? 715  TYR A C   1 
ATOM   5744 O  O   . TYR A 1 715  ? 20.154 77.534  -10.819 1.00 12.25 ? 715  TYR A O   1 
ATOM   5745 C  CB  . TYR A 1 715  ? 19.758 74.450  -11.598 1.00 10.48 ? 715  TYR A CB  1 
ATOM   5746 C  CG  . TYR A 1 715  ? 19.685 73.245  -12.459 1.00 9.29  ? 715  TYR A CG  1 
ATOM   5747 C  CD1 . TYR A 1 715  ? 18.513 72.498  -12.522 1.00 9.63  ? 715  TYR A CD1 1 
ATOM   5748 C  CD2 . TYR A 1 715  ? 20.806 72.788  -13.231 1.00 9.47  ? 715  TYR A CD2 1 
ATOM   5749 C  CE1 . TYR A 1 715  ? 18.458 71.358  -13.295 1.00 10.55 ? 715  TYR A CE1 1 
ATOM   5750 C  CE2 . TYR A 1 715  ? 20.724 71.644  -14.013 1.00 9.61  ? 715  TYR A CE2 1 
ATOM   5751 C  CZ  . TYR A 1 715  ? 19.538 70.913  -14.039 1.00 9.42  ? 715  TYR A CZ  1 
ATOM   5752 O  OH  . TYR A 1 715  ? 19.398 69.787  -14.751 1.00 10.47 ? 715  TYR A OH  1 
ATOM   5753 N  N   . GLY A 1 716  ? 18.068 76.833  -10.357 1.00 11.64 ? 716  GLY A N   1 
ATOM   5754 C  CA  . GLY A 1 716  ? 17.916 77.726  -9.236  1.00 11.83 ? 716  GLY A CA  1 
ATOM   5755 C  C   . GLY A 1 716  ? 17.794 76.952  -7.931  1.00 11.97 ? 716  GLY A C   1 
ATOM   5756 O  O   . GLY A 1 716  ? 18.112 75.731  -7.850  1.00 12.69 ? 716  GLY A O   1 
ATOM   5757 N  N   . VAL A 1 717  ? 17.317 77.640  -6.915  1.00 12.29 ? 717  VAL A N   1 
ATOM   5758 C  CA  . VAL A 1 717  ? 17.199 77.118  -5.579  1.00 13.82 ? 717  VAL A CA  1 
ATOM   5759 C  C   . VAL A 1 717  ? 15.743 77.295  -5.142  1.00 13.25 ? 717  VAL A C   1 
ATOM   5760 O  O   . VAL A 1 717  ? 15.090 78.263  -5.556  1.00 15.66 ? 717  VAL A O   1 
ATOM   5761 C  CB  . VAL A 1 717  ? 18.170 77.915  -4.657  1.00 13.86 ? 717  VAL A CB  1 
ATOM   5762 C  CG1 . VAL A 1 717  ? 18.001 77.513  -3.199  1.00 16.53 ? 717  VAL A CG1 1 
ATOM   5763 C  CG2 . VAL A 1 717  ? 19.637 77.698  -5.156  1.00 13.84 ? 717  VAL A CG2 1 
ATOM   5764 N  N   . ARG A 1 718  ? 15.278 76.408  -4.273  1.00 13.76 ? 718  ARG A N   1 
ATOM   5765 C  CA  . ARG A 1 718  ? 13.890 76.456  -3.808  1.00 14.30 ? 718  ARG A CA  1 
ATOM   5766 C  C   . ARG A 1 718  ? 13.670 77.611  -2.871  1.00 16.69 ? 718  ARG A C   1 
ATOM   5767 O  O   . ARG A 1 718  ? 14.513 77.950  -2.050  1.00 19.22 ? 718  ARG A O   1 
ATOM   5768 C  CB  . ARG A 1 718  ? 13.512 75.146  -3.100  1.00 13.46 ? 718  ARG A CB  1 
ATOM   5769 C  CG  . ARG A 1 718  ? 13.540 73.957  -4.046  1.00 13.37 ? 718  ARG A CG  1 
ATOM   5770 C  CD  . ARG A 1 718  ? 13.541 72.621  -3.334  1.00 13.52 ? 718  ARG A CD  1 
ATOM   5771 N  NE  . ARG A 1 718  ? 13.828 71.605  -4.328  1.00 13.95 ? 718  ARG A NE  1 
ATOM   5772 C  CZ  . ARG A 1 718  ? 13.780 70.288  -4.104  1.00 13.22 ? 718  ARG A CZ  1 
ATOM   5773 N  NH1 . ARG A 1 718  ? 13.449 69.843  -2.899  1.00 13.16 ? 718  ARG A NH1 1 
ATOM   5774 N  NH2 . ARG A 1 718  ? 14.088 69.464  -5.106  1.00 13.86 ? 718  ARG A NH2 1 
ATOM   5775 N  N   . SER A 1 719  ? 12.488 78.205  -2.997  1.00 17.71 ? 719  SER A N   1 
ATOM   5776 C  CA  . SER A 1 719  ? 12.151 79.325  -2.137  1.00 20.77 ? 719  SER A CA  1 
ATOM   5777 C  C   . SER A 1 719  ? 11.394 78.827  -0.903  1.00 22.11 ? 719  SER A C   1 
ATOM   5778 O  O   . SER A 1 719  ? 11.133 79.597  0.002   1.00 23.82 ? 719  SER A O   1 
ATOM   5779 C  CB  . SER A 1 719  ? 11.307 80.343  -2.919  1.00 21.67 ? 719  SER A CB  1 
ATOM   5780 O  OG  . SER A 1 719  ? 10.142 79.724  -3.391  1.00 24.24 ? 719  SER A OG  1 
ATOM   5781 N  N   . HIS A 1 720  ? 10.990 77.562  -0.907  1.00 23.61 ? 720  HIS A N   1 
ATOM   5782 C  CA  . HIS A 1 720  ? 10.351 76.952  0.237   1.00 24.32 ? 720  HIS A CA  1 
ATOM   5783 C  C   . HIS A 1 720  ? 10.978 75.548  0.364   1.00 23.16 ? 720  HIS A C   1 
ATOM   5784 O  O   . HIS A 1 720  ? 11.306 74.905  -0.642  1.00 23.07 ? 720  HIS A O   1 
ATOM   5785 C  CB  . HIS A 1 720  ? 8.807  76.911  0.081   1.00 28.56 ? 720  HIS A CB  1 
ATOM   5786 C  CG  . HIS A 1 720  ? 8.313  76.157  -1.115  1.00 32.77 ? 720  HIS A CG  1 
ATOM   5787 N  ND1 . HIS A 1 720  ? 7.767  74.890  -1.022  1.00 34.94 ? 720  HIS A ND1 1 
ATOM   5788 C  CD2 . HIS A 1 720  ? 8.240  76.503  -2.427  1.00 34.81 ? 720  HIS A CD2 1 
ATOM   5789 C  CE1 . HIS A 1 720  ? 7.380  74.490  -2.226  1.00 35.27 ? 720  HIS A CE1 1 
ATOM   5790 N  NE2 . HIS A 1 720  ? 7.655  75.450  -3.095  1.00 35.71 ? 720  HIS A NE2 1 
ATOM   5791 N  N   . GLY A 1 721  ? 11.159 75.101  1.594   1.00 21.90 ? 721  GLY A N   1 
ATOM   5792 C  CA  . GLY A 1 721  ? 11.751 73.784  1.800   1.00 21.16 ? 721  GLY A CA  1 
ATOM   5793 C  C   . GLY A 1 721  ? 13.263 73.844  1.948   1.00 20.30 ? 721  GLY A C   1 
ATOM   5794 O  O   . GLY A 1 721  ? 13.857 74.853  2.327   1.00 20.43 ? 721  GLY A O   1 
ATOM   5795 N  N   . ASP A 1 722  ? 13.903 72.744  1.601   1.00 17.76 ? 722  ASP A N   1 
ATOM   5796 C  CA  . ASP A 1 722  ? 15.350 72.660  1.794   1.00 16.28 ? 722  ASP A CA  1 
ATOM   5797 C  C   . ASP A 1 722  ? 16.126 73.339  0.689   1.00 14.98 ? 722  ASP A C   1 
ATOM   5798 O  O   . ASP A 1 722  ? 15.771 73.271  -0.478  1.00 14.90 ? 722  ASP A O   1 
ATOM   5799 C  CB  . ASP A 1 722  ? 15.767 71.202  1.899   1.00 15.57 ? 722  ASP A CB  1 
ATOM   5800 C  CG  . ASP A 1 722  ? 15.173 70.480  3.135   1.00 15.78 ? 722  ASP A CG  1 
ATOM   5801 O  OD1 . ASP A 1 722  ? 14.977 71.087  4.223   1.00 18.09 ? 722  ASP A OD1 1 
ATOM   5802 O  OD2 . ASP A 1 722  ? 14.929 69.266  3.007   1.00 16.77 ? 722  ASP A OD2 1 
ATOM   5803 N  N   . ARG A 1 723  ? 17.196 74.011  1.101   1.00 13.98 ? 723  ARG A N   1 
ATOM   5804 C  CA  . ARG A 1 723  ? 18.028 74.734  0.154   1.00 14.06 ? 723  ARG A CA  1 
ATOM   5805 C  C   . ARG A 1 723  ? 19.308 74.010  -0.237  1.00 11.82 ? 723  ARG A C   1 
ATOM   5806 O  O   . ARG A 1 723  ? 19.954 73.398  0.607   1.00 12.33 ? 723  ARG A O   1 
ATOM   5807 C  CB  . ARG A 1 723  ? 18.461 76.082  0.769   1.00 16.34 ? 723  ARG A CB  1 
ATOM   5808 C  CG  . ARG A 1 723  ? 17.365 77.206  0.765   1.00 23.04 ? 723  ARG A CG  1 
ATOM   5809 C  CD  . ARG A 1 723  ? 16.168 76.830  1.620   1.00 28.87 ? 723  ARG A CD  1 
ATOM   5810 N  NE  . ARG A 1 723  ? 15.019 77.755  1.539   1.00 34.24 ? 723  ARG A NE  1 
ATOM   5811 C  CZ  . ARG A 1 723  ? 15.105 79.081  1.590   1.00 36.25 ? 723  ARG A CZ  1 
ATOM   5812 N  NH1 . ARG A 1 723  ? 16.291 79.684  1.700   1.00 38.01 ? 723  ARG A NH1 1 
ATOM   5813 N  NH2 . ARG A 1 723  ? 13.995 79.810  1.598   1.00 37.32 ? 723  ARG A NH2 1 
ATOM   5814 N  N   . SER A 1 724  ? 19.621 74.117  -1.537  1.00 10.90 ? 724  SER A N   1 
ATOM   5815 C  CA  . SER A 1 724  ? 20.910 73.642  -2.014  1.00 10.68 ? 724  SER A CA  1 
ATOM   5816 C  C   . SER A 1 724  ? 22.027 74.369  -1.279  1.00 11.18 ? 724  SER A C   1 
ATOM   5817 O  O   . SER A 1 724  ? 21.917 75.552  -0.911  1.00 12.84 ? 724  SER A O   1 
ATOM   5818 C  CB  . SER A 1 724  ? 21.101 73.971  -3.470  1.00 11.20 ? 724  SER A CB  1 
ATOM   5819 O  OG  . SER A 1 724  ? 20.040 73.398  -4.204  1.00 10.58 ? 724  SER A OG  1 
ATOM   5820 N  N   . GLY A 1 725  ? 23.147 73.654  -1.087  1.00 10.24 ? 725  GLY A N   1 
ATOM   5821 C  CA  . GLY A 1 725  ? 24.333 74.227  -0.435  1.00 9.70  ? 725  GLY A CA  1 
ATOM   5822 C  C   . GLY A 1 725  ? 25.552 73.496  -1.008  1.00 9.12  ? 725  GLY A C   1 
ATOM   5823 O  O   . GLY A 1 725  ? 25.455 72.827  -2.035  1.00 9.34  ? 725  GLY A O   1 
ATOM   5824 N  N   . ALA A 1 726  ? 26.683 73.574  -0.327  1.00 8.68  ? 726  ALA A N   1 
ATOM   5825 C  CA  . ALA A 1 726  ? 27.910 72.934  -0.837  1.00 8.29  ? 726  ALA A CA  1 
ATOM   5826 C  C   . ALA A 1 726  ? 27.758 71.432  -1.044  1.00 8.54  ? 726  ALA A C   1 
ATOM   5827 O  O   . ALA A 1 726  ? 28.416 70.867  -1.916  1.00 8.09  ? 726  ALA A O   1 
ATOM   5828 C  CB  . ALA A 1 726  ? 29.071 73.185  0.146   1.00 9.46  ? 726  ALA A CB  1 
ATOM   5829 N  N   . TYR A 1 727  ? 26.951 70.780  -0.194  1.00 8.44  ? 727  TYR A N   1 
ATOM   5830 C  CA  . TYR A 1 727  ? 26.759 69.323  -0.327  1.00 7.65  ? 727  TYR A CA  1 
ATOM   5831 C  C   . TYR A 1 727  ? 25.581 68.927  -1.186  1.00 7.45  ? 727  TYR A C   1 
ATOM   5832 O  O   . TYR A 1 727  ? 25.715 68.090  -2.095  1.00 8.37  ? 727  TYR A O   1 
ATOM   5833 C  CB  . TYR A 1 727  ? 26.551 68.661  1.044   1.00 8.84  ? 727  TYR A CB  1 
ATOM   5834 C  CG  . TYR A 1 727  ? 27.674 68.880  2.060   1.00 8.70  ? 727  TYR A CG  1 
ATOM   5835 C  CD1 . TYR A 1 727  ? 27.683 69.993  2.898   1.00 8.92  ? 727  TYR A CD1 1 
ATOM   5836 C  CD2 . TYR A 1 727  ? 28.715 67.970  2.183   1.00 8.28  ? 727  TYR A CD2 1 
ATOM   5837 C  CE1 . TYR A 1 727  ? 28.710 70.199  3.852   1.00 9.07  ? 727  TYR A CE1 1 
ATOM   5838 C  CE2 . TYR A 1 727  ? 29.744 68.148  3.126   1.00 8.85  ? 727  TYR A CE2 1 
ATOM   5839 C  CZ  . TYR A 1 727  ? 29.740 69.247  3.950   1.00 8.84  ? 727  TYR A CZ  1 
ATOM   5840 O  OH  . TYR A 1 727  ? 30.756 69.393  4.884   1.00 10.05 ? 727  TYR A OH  1 
ATOM   5841 N  N   . LEU A 1 728  ? 24.430 69.542  -0.913  1.00 8.36  ? 728  LEU A N   1 
ATOM   5842 C  CA  . LEU A 1 728  ? 23.184 69.140  -1.565  1.00 7.83  ? 728  LEU A CA  1 
ATOM   5843 C  C   . LEU A 1 728  ? 22.800 69.884  -2.824  1.00 8.40  ? 728  LEU A C   1 
ATOM   5844 O  O   . LEU A 1 728  ? 23.001 71.099  -2.920  1.00 9.16  ? 728  LEU A O   1 
ATOM   5845 C  CB  . LEU A 1 728  ? 22.019 69.352  -0.570  1.00 10.35 ? 728  LEU A CB  1 
ATOM   5846 C  CG  . LEU A 1 728  ? 22.199 68.755  0.813   1.00 8.41  ? 728  LEU A CG  1 
ATOM   5847 C  CD1 . LEU A 1 728  ? 20.844 68.999  1.593   1.00 11.51 ? 728  LEU A CD1 1 
ATOM   5848 C  CD2 . LEU A 1 728  ? 22.514 67.297  0.734   1.00 10.38 ? 728  LEU A CD2 1 
ATOM   5849 N  N   . PHE A 1 729  ? 22.236 69.162  -3.784  1.00 9.44  ? 729  PHE A N   1 
ATOM   5850 C  CA  . PHE A 1 729  ? 21.688 69.751  -4.990  1.00 9.16  ? 729  PHE A CA  1 
ATOM   5851 C  C   . PHE A 1 729  ? 20.153 69.553  -4.866  1.00 9.75  ? 729  PHE A C   1 
ATOM   5852 O  O   . PHE A 1 729  ? 19.647 68.416  -4.944  1.00 10.28 ? 729  PHE A O   1 
ATOM   5853 C  CB  . PHE A 1 729  ? 22.223 69.034  -6.216  1.00 8.58  ? 729  PHE A CB  1 
ATOM   5854 C  CG  . PHE A 1 729  ? 21.701 69.532  -7.552  1.00 8.03  ? 729  PHE A CG  1 
ATOM   5855 C  CD1 . PHE A 1 729  ? 21.375 70.882  -7.773  1.00 8.88  ? 729  PHE A CD1 1 
ATOM   5856 C  CD2 . PHE A 1 729  ? 21.614 68.632  -8.602  1.00 8.48  ? 729  PHE A CD2 1 
ATOM   5857 C  CE1 . PHE A 1 729  ? 20.968 71.278  -9.073  1.00 8.92  ? 729  PHE A CE1 1 
ATOM   5858 C  CE2 . PHE A 1 729  ? 21.203 69.033  -9.886  1.00 8.46  ? 729  PHE A CE2 1 
ATOM   5859 C  CZ  . PHE A 1 729  ? 20.888 70.355  -10.103 1.00 8.99  ? 729  PHE A CZ  1 
ATOM   5860 N  N   . LEU A 1 730  ? 19.452 70.683  -4.680  1.00 9.57  ? 730  LEU A N   1 
ATOM   5861 C  CA  . LEU A 1 730  ? 17.966 70.658  -4.528  1.00 10.19 ? 730  LEU A CA  1 
ATOM   5862 C  C   . LEU A 1 730  ? 17.374 71.679  -5.501  1.00 9.66  ? 730  LEU A C   1 
ATOM   5863 O  O   . LEU A 1 730  ? 16.937 72.768  -5.087  1.00 10.53 ? 730  LEU A O   1 
ATOM   5864 C  CB  . LEU A 1 730  ? 17.656 71.001  -3.076  1.00 10.08 ? 730  LEU A CB  1 
ATOM   5865 C  CG  . LEU A 1 730  ? 18.047 69.918  -2.072  1.00 10.54 ? 730  LEU A CG  1 
ATOM   5866 C  CD1 . LEU A 1 730  ? 18.034 70.488  -0.684  1.00 12.92 ? 730  LEU A CD1 1 
ATOM   5867 C  CD2 . LEU A 1 730  ? 17.040 68.751  -2.224  1.00 13.49 ? 730  LEU A CD2 1 
ATOM   5868 N  N   . PRO A 1 731  ? 17.411 71.368  -6.781  1.00 9.80  ? 731  PRO A N   1 
ATOM   5869 C  CA  . PRO A 1 731  ? 16.887 72.326  -7.780  1.00 11.26 ? 731  PRO A CA  1 
ATOM   5870 C  C   . PRO A 1 731  ? 15.442 72.668  -7.678  1.00 11.47 ? 731  PRO A C   1 
ATOM   5871 O  O   . PRO A 1 731  ? 14.661 71.860  -7.189  1.00 12.20 ? 731  PRO A O   1 
ATOM   5872 C  CB  . PRO A 1 731  ? 17.214 71.681  -9.118  1.00 11.29 ? 731  PRO A CB  1 
ATOM   5873 C  CG  . PRO A 1 731  ? 17.192 70.151  -8.779  1.00 11.52 ? 731  PRO A CG  1 
ATOM   5874 C  CD  . PRO A 1 731  ? 17.803 70.083  -7.399  1.00 10.90 ? 731  PRO A CD  1 
ATOM   5875 N  N   . ASN A 1 732  ? 15.095 73.861  -8.142  1.00 12.34 ? 732  ASN A N   1 
ATOM   5876 C  CA  . ASN A 1 732  ? 13.656 74.249  -8.121  1.00 13.62 ? 732  ASN A CA  1 
ATOM   5877 C  C   . ASN A 1 732  ? 13.111 73.956  -9.518  1.00 13.51 ? 732  ASN A C   1 
ATOM   5878 O  O   . ASN A 1 732  ? 12.586 74.844  -10.241 1.00 16.14 ? 732  ASN A O   1 
ATOM   5879 C  CB  . ASN A 1 732  ? 13.522 75.735  -7.775  1.00 16.28 ? 732  ASN A CB  1 
ATOM   5880 C  CG  . ASN A 1 732  ? 14.187 76.627  -8.789  1.00 18.15 ? 732  ASN A CG  1 
ATOM   5881 O  OD1 . ASN A 1 732  ? 15.187 76.265  -9.391  1.00 18.63 ? 732  ASN A OD1 1 
ATOM   5882 N  ND2 . ASN A 1 732  ? 13.612 77.832  -9.009  1.00 20.39 ? 732  ASN A ND2 1 
ATOM   5883 N  N   . GLY A 1 733  ? 13.241 72.703  -9.936  1.00 13.05 ? 733  GLY A N   1 
ATOM   5884 C  CA  . GLY A 1 733  ? 12.771 72.217  -11.222 1.00 14.17 ? 733  GLY A CA  1 
ATOM   5885 C  C   . GLY A 1 733  ? 13.865 72.103  -12.279 1.00 12.68 ? 733  GLY A C   1 
ATOM   5886 O  O   . GLY A 1 733  ? 15.046 72.440  -12.004 1.00 13.00 ? 733  GLY A O   1 
ATOM   5887 N  N   . PRO A 1 734  ? 13.531 71.666  -13.488 1.00 11.83 ? 734  PRO A N   1 
ATOM   5888 C  CA  . PRO A 1 734  ? 14.455 71.519  -14.619 1.00 13.14 ? 734  PRO A CA  1 
ATOM   5889 C  C   . PRO A 1 734  ? 15.074 72.889  -14.909 1.00 12.27 ? 734  PRO A C   1 
ATOM   5890 O  O   . PRO A 1 734  ? 14.503 73.965  -14.642 1.00 13.15 ? 734  PRO A O   1 
ATOM   5891 C  CB  . PRO A 1 734  ? 13.561 71.072  -15.784 1.00 14.09 ? 734  PRO A CB  1 
ATOM   5892 C  CG  . PRO A 1 734  ? 12.412 70.413  -15.075 1.00 16.82 ? 734  PRO A CG  1 
ATOM   5893 C  CD  . PRO A 1 734  ? 12.184 71.150  -13.822 1.00 14.12 ? 734  PRO A CD  1 
ATOM   5894 N  N   . ALA A 1 735  ? 16.259 72.839  -15.509 1.00 11.62 ? 735  ALA A N   1 
ATOM   5895 C  CA  . ALA A 1 735  ? 16.983 74.058  -15.795 1.00 12.85 ? 735  ALA A CA  1 
ATOM   5896 C  C   . ALA A 1 735  ? 16.279 74.893  -16.879 1.00 13.09 ? 735  ALA A C   1 
ATOM   5897 O  O   . ALA A 1 735  ? 15.585 74.355  -17.723 1.00 14.06 ? 735  ALA A O   1 
ATOM   5898 C  CB  . ALA A 1 735  ? 18.435 73.659  -16.227 1.00 12.15 ? 735  ALA A CB  1 
ATOM   5899 N  N   . SER A 1 736  ? 16.544 76.202  -16.869 1.00 13.53 ? 736  SER A N   1 
ATOM   5900 C  CA  . SER A 1 736  ? 15.957 77.145  -17.846 1.00 15.20 ? 736  SER A CA  1 
ATOM   5901 C  C   . SER A 1 736  ? 17.107 77.657  -18.686 1.00 15.15 ? 736  SER A C   1 
ATOM   5902 O  O   . SER A 1 736  ? 18.175 77.858  -18.164 1.00 13.99 ? 736  SER A O   1 
ATOM   5903 C  CB  . SER A 1 736  ? 15.346 78.321  -17.099 1.00 17.53 ? 736  SER A CB  1 
ATOM   5904 O  OG  . SER A 1 736  ? 14.444 77.858  -16.121 1.00 22.82 ? 736  SER A OG  1 
ATOM   5905 N  N   . PRO A 1 737  ? 16.915 77.900  -19.977 1.00 15.77 ? 737  PRO A N   1 
ATOM   5906 C  CA  . PRO A 1 737  ? 18.036 78.391  -20.818 1.00 17.33 ? 737  PRO A CA  1 
ATOM   5907 C  C   . PRO A 1 737  ? 18.614 79.715  -20.397 1.00 16.63 ? 737  PRO A C   1 
ATOM   5908 O  O   . PRO A 1 737  ? 17.890 80.582  -19.904 1.00 17.96 ? 737  PRO A O   1 
ATOM   5909 C  CB  . PRO A 1 737  ? 17.442 78.500  -22.223 1.00 18.02 ? 737  PRO A CB  1 
ATOM   5910 C  CG  . PRO A 1 737  ? 16.216 77.602  -22.178 1.00 18.81 ? 737  PRO A CG  1 
ATOM   5911 C  CD  . PRO A 1 737  ? 15.683 77.672  -20.760 1.00 17.68 ? 737  PRO A CD  1 
ATOM   5912 N  N   . VAL A 1 738  ? 19.948 79.851  -20.501 1.00 16.46 ? 738  VAL A N   1 
ATOM   5913 C  CA  . VAL A 1 738  ? 20.552 81.148  -20.185 1.00 16.36 ? 738  VAL A CA  1 
ATOM   5914 C  C   . VAL A 1 738  ? 20.145 82.076  -21.358 1.00 16.97 ? 738  VAL A C   1 
ATOM   5915 O  O   . VAL A 1 738  ? 20.203 81.663  -22.508 1.00 16.41 ? 738  VAL A O   1 
ATOM   5916 C  CB  . VAL A 1 738  ? 22.064 81.008  -20.144 1.00 15.09 ? 738  VAL A CB  1 
ATOM   5917 C  CG1 . VAL A 1 738  ? 22.720 82.429  -20.052 1.00 16.23 ? 738  VAL A CG1 1 
ATOM   5918 C  CG2 . VAL A 1 738  ? 22.481 80.165  -18.910 1.00 14.96 ? 738  VAL A CG2 1 
ATOM   5919 N  N   . GLU A 1 739  ? 19.719 83.317  -21.085 1.00 18.18 ? 739  GLU A N   1 
ATOM   5920 C  CA  . GLU A 1 739  ? 19.349 84.236  -22.191 1.00 19.42 ? 739  GLU A CA  1 
ATOM   5921 C  C   . GLU A 1 739  ? 20.660 84.752  -22.727 1.00 18.03 ? 739  GLU A C   1 
ATOM   5922 O  O   . GLU A 1 739  ? 21.441 85.386  -22.003 1.00 19.36 ? 739  GLU A O   1 
ATOM   5923 C  CB  . GLU A 1 739  ? 18.496 85.397  -21.688 1.00 22.09 ? 739  GLU A CB  1 
ATOM   5924 C  CG  . GLU A 1 739  ? 17.024 85.031  -21.536 1.00 28.54 ? 739  GLU A CG  1 
ATOM   5925 C  CD  . GLU A 1 739  ? 16.145 86.228  -21.136 1.00 32.01 ? 739  GLU A CD  1 
ATOM   5926 O  OE1 . GLU A 1 739  ? 16.612 87.389  -21.204 1.00 34.13 ? 739  GLU A OE1 1 
ATOM   5927 O  OE2 . GLU A 1 739  ? 14.970 85.986  -20.763 1.00 34.65 ? 739  GLU A OE2 1 
ATOM   5928 N  N   . LEU A 1 740  ? 20.894 84.461  -23.996 1.00 17.91 ? 740  LEU A N   1 
ATOM   5929 C  CA  . LEU A 1 740  ? 22.175 84.794  -24.615 1.00 18.34 ? 740  LEU A CA  1 
ATOM   5930 C  C   . LEU A 1 740  ? 22.361 86.155  -25.213 1.00 19.39 ? 740  LEU A C   1 
ATOM   5931 O  O   . LEU A 1 740  ? 23.490 86.561  -25.378 1.00 19.38 ? 740  LEU A O   1 
ATOM   5932 C  CB  . LEU A 1 740  ? 22.522 83.750  -25.673 1.00 18.56 ? 740  LEU A CB  1 
ATOM   5933 C  CG  . LEU A 1 740  ? 22.487 82.282  -25.217 1.00 18.38 ? 740  LEU A CG  1 
ATOM   5934 C  CD1 . LEU A 1 740  ? 22.967 81.442  -26.347 1.00 19.29 ? 740  LEU A CD1 1 
ATOM   5935 C  CD2 . LEU A 1 740  ? 23.409 82.042  -23.990 1.00 17.85 ? 740  LEU A CD2 1 
ATOM   5936 N  N   . GLY A 1 741  ? 21.268 86.850  -25.526 1.00 19.80 ? 741  GLY A N   1 
ATOM   5937 C  CA  . GLY A 1 741  ? 21.407 88.160  -26.158 1.00 20.11 ? 741  GLY A CA  1 
ATOM   5938 C  C   . GLY A 1 741  ? 21.965 87.931  -27.564 1.00 19.67 ? 741  GLY A C   1 
ATOM   5939 O  O   . GLY A 1 741  ? 21.622 86.953  -28.210 1.00 19.93 ? 741  GLY A O   1 
ATOM   5940 N  N   . GLN A 1 742  ? 22.793 88.847  -28.079 1.00 19.92 ? 742  GLN A N   1 
ATOM   5941 C  CA  . GLN A 1 742  ? 23.405 88.646  -29.401 1.00 19.74 ? 742  GLN A CA  1 
ATOM   5942 C  C   . GLN A 1 742  ? 24.910 88.644  -29.051 1.00 18.21 ? 742  GLN A C   1 
ATOM   5943 O  O   . GLN A 1 742  ? 25.593 89.662  -29.109 1.00 19.46 ? 742  GLN A O   1 
ATOM   5944 C  CB  . GLN A 1 742  ? 23.081 89.810  -30.333 1.00 22.59 ? 742  GLN A CB  1 
ATOM   5945 C  CG  . GLN A 1 742  ? 23.506 89.518  -31.751 1.00 28.06 ? 742  GLN A CG  1 
ATOM   5946 C  CD  . GLN A 1 742  ? 22.824 90.410  -32.777 1.00 30.55 ? 742  GLN A CD  1 
ATOM   5947 O  OE1 . GLN A 1 742  ? 23.069 90.267  -33.975 1.00 31.64 ? 742  GLN A OE1 1 
ATOM   5948 N  NE2 . GLN A 1 742  ? 21.948 91.331  -32.311 1.00 32.47 ? 742  GLN A NE2 1 
ATOM   5949 N  N   . PRO A 1 743  ? 25.440 87.480  -28.679 1.00 16.66 ? 743  PRO A N   1 
ATOM   5950 C  CA  . PRO A 1 743  ? 26.858 87.457  -28.300 1.00 15.68 ? 743  PRO A CA  1 
ATOM   5951 C  C   . PRO A 1 743  ? 27.890 87.661  -29.397 1.00 14.72 ? 743  PRO A C   1 
ATOM   5952 O  O   . PRO A 1 743  ? 27.658 87.399  -30.588 1.00 16.59 ? 743  PRO A O   1 
ATOM   5953 C  CB  . PRO A 1 743  ? 27.000 86.102  -27.613 1.00 15.75 ? 743  PRO A CB  1 
ATOM   5954 C  CG  . PRO A 1 743  ? 26.010 85.240  -28.331 1.00 15.58 ? 743  PRO A CG  1 
ATOM   5955 C  CD  . PRO A 1 743  ? 24.820 86.146  -28.650 1.00 15.34 ? 743  PRO A CD  1 
ATOM   5956 N  N   . VAL A 1 744  ? 29.068 88.135  -28.987 1.00 12.54 ? 744  VAL A N   1 
ATOM   5957 C  CA  . VAL A 1 744  ? 30.163 88.327  -29.945 1.00 12.05 ? 744  VAL A CA  1 
ATOM   5958 C  C   . VAL A 1 744  ? 30.850 86.980  -30.168 1.00 11.38 ? 744  VAL A C   1 
ATOM   5959 O  O   . VAL A 1 744  ? 31.183 86.270  -29.185 1.00 12.26 ? 744  VAL A O   1 
ATOM   5960 C  CB  . VAL A 1 744  ? 31.182 89.335  -29.404 1.00 12.06 ? 744  VAL A CB  1 
ATOM   5961 C  CG1 . VAL A 1 744  ? 32.312 89.551  -30.380 1.00 12.70 ? 744  VAL A CG1 1 
ATOM   5962 C  CG2 . VAL A 1 744  ? 30.442 90.679  -29.105 1.00 14.37 ? 744  VAL A CG2 1 
ATOM   5963 N  N   . VAL A 1 745  ? 31.060 86.621  -31.417 1.00 11.01 ? 745  VAL A N   1 
ATOM   5964 C  CA  . VAL A 1 745  ? 31.696 85.382  -31.821 1.00 10.22 ? 745  VAL A CA  1 
ATOM   5965 C  C   . VAL A 1 745  ? 32.987 85.631  -32.565 1.00 10.83 ? 745  VAL A C   1 
ATOM   5966 O  O   . VAL A 1 745  ? 33.039 86.457  -33.499 1.00 11.83 ? 745  VAL A O   1 
ATOM   5967 C  CB  . VAL A 1 745  ? 30.720 84.521  -32.721 1.00 10.92 ? 745  VAL A CB  1 
ATOM   5968 C  CG1 . VAL A 1 745  ? 31.411 83.203  -33.135 1.00 11.53 ? 745  VAL A CG1 1 
ATOM   5969 C  CG2 . VAL A 1 745  ? 29.429 84.227  -31.968 1.00 11.94 ? 745  VAL A CG2 1 
ATOM   5970 N  N   . LEU A 1 746  ? 34.061 84.935  -32.214 1.00 9.71  ? 746  LEU A N   1 
ATOM   5971 C  CA  . LEU A 1 746  ? 35.379 85.059  -32.828 1.00 9.40  ? 746  LEU A CA  1 
ATOM   5972 C  C   . LEU A 1 746  ? 35.788 83.762  -33.476 1.00 10.07 ? 746  LEU A C   1 
ATOM   5973 O  O   . LEU A 1 746  ? 35.880 82.709  -32.787 1.00 10.29 ? 746  LEU A O   1 
ATOM   5974 C  CB  . LEU A 1 746  ? 36.412 85.467  -31.774 1.00 11.08 ? 746  LEU A CB  1 
ATOM   5975 C  CG  . LEU A 1 746  ? 37.868 85.480  -32.253 1.00 11.75 ? 746  LEU A CG  1 
ATOM   5976 C  CD1 . LEU A 1 746  ? 38.112 86.546  -33.283 1.00 13.02 ? 746  LEU A CD1 1 
ATOM   5977 C  CD2 . LEU A 1 746  ? 38.741 85.760  -31.035 1.00 14.37 ? 746  LEU A CD2 1 
ATOM   5978 N  N   . VAL A 1 747  ? 36.063 83.789  -34.762 1.00 9.90  ? 747  VAL A N   1 
ATOM   5979 C  CA  . VAL A 1 747  ? 36.471 82.606  -35.509 1.00 10.05 ? 747  VAL A CA  1 
ATOM   5980 C  C   . VAL A 1 747  ? 37.890 82.753  -35.930 1.00 10.73 ? 747  VAL A C   1 
ATOM   5981 O  O   . VAL A 1 747  ? 38.264 83.727  -36.628 1.00 12.20 ? 747  VAL A O   1 
ATOM   5982 C  CB  . VAL A 1 747  ? 35.590 82.400  -36.754 1.00 10.62 ? 747  VAL A CB  1 
ATOM   5983 C  CG1 . VAL A 1 747  ? 35.948 81.136  -37.459 1.00 12.06 ? 747  VAL A CG1 1 
ATOM   5984 C  CG2 . VAL A 1 747  ? 34.135 82.352  -36.368 1.00 11.09 ? 747  VAL A CG2 1 
ATOM   5985 N  N   . THR A 1 748  ? 38.764 81.841  -35.531 1.00 10.51 ? 748  THR A N   1 
ATOM   5986 C  CA  . THR A 1 748  ? 40.153 81.880  -35.945 1.00 11.13 ? 748  THR A CA  1 
ATOM   5987 C  C   . THR A 1 748  ? 40.356 80.649  -36.765 1.00 10.96 ? 748  THR A C   1 
ATOM   5988 O  O   . THR A 1 748  ? 40.039 79.543  -36.290 1.00 12.82 ? 748  THR A O   1 
ATOM   5989 C  CB  . THR A 1 748  ? 41.079 81.902  -34.703 1.00 12.13 ? 748  THR A CB  1 
ATOM   5990 O  OG1 . THR A 1 748  ? 40.820 83.111  -33.966 1.00 13.28 ? 748  THR A OG1 1 
ATOM   5991 C  CG2 . THR A 1 748  ? 42.579 81.794  -35.122 1.00 12.65 ? 748  THR A CG2 1 
ATOM   5992 N  N   . LYS A 1 749  ? 40.831 80.791  -38.002 1.00 12.04 ? 749  LYS A N   1 
ATOM   5993 C  CA  . LYS A 1 749  ? 40.985 79.646  -38.900 1.00 12.15 ? 749  LYS A CA  1 
ATOM   5994 C  C   . LYS A 1 749  ? 42.423 79.499  -39.323 1.00 11.70 ? 749  LYS A C   1 
ATOM   5995 O  O   . LYS A 1 749  ? 43.054 80.426  -39.882 1.00 11.81 ? 749  LYS A O   1 
ATOM   5996 C  CB  . LYS A 1 749  ? 40.109 79.834  -40.131 1.00 14.04 ? 749  LYS A CB  1 
ATOM   5997 C  CG  . LYS A 1 749  ? 40.296 78.712  -41.138 1.00 16.82 ? 749  LYS A CG  1 
ATOM   5998 C  CD  . LYS A 1 749  ? 39.307 78.912  -42.317 1.00 21.24 ? 749  LYS A CD  1 
ATOM   5999 C  CE  . LYS A 1 749  ? 39.653 77.970  -43.458 1.00 23.46 ? 749  LYS A CE  1 
ATOM   6000 N  NZ  . LYS A 1 749  ? 39.291 78.578  -44.775 1.00 27.12 ? 749  LYS A NZ  1 
ATOM   6001 N  N   . GLY A 1 750  ? 42.986 78.362  -38.982 1.00 11.79 ? 750  GLY A N   1 
ATOM   6002 C  CA  . GLY A 1 750  ? 44.366 78.096  -39.311 1.00 12.22 ? 750  GLY A CA  1 
ATOM   6003 C  C   . GLY A 1 750  ? 44.558 76.727  -39.895 1.00 12.37 ? 750  GLY A C   1 
ATOM   6004 O  O   . GLY A 1 750  ? 43.651 75.870  -39.796 1.00 13.70 ? 750  GLY A O   1 
ATOM   6005 N  N   . LYS A 1 751  ? 45.736 76.509  -40.450 1.00 12.42 ? 751  LYS A N   1 
ATOM   6006 C  CA  . LYS A 1 751  ? 46.021 75.214  -41.046 1.00 13.74 ? 751  LYS A CA  1 
ATOM   6007 C  C   . LYS A 1 751  ? 46.186 74.108  -40.012 1.00 13.43 ? 751  LYS A C   1 
ATOM   6008 O  O   . LYS A 1 751  ? 45.841 72.942  -40.282 1.00 13.24 ? 751  LYS A O   1 
ATOM   6009 C  CB  . LYS A 1 751  ? 47.292 75.301  -41.876 1.00 17.00 ? 751  LYS A CB  1 
ATOM   6010 C  CG  . LYS A 1 751  ? 47.658 73.992  -42.535 1.00 23.91 ? 751  LYS A CG  1 
ATOM   6011 C  CD  . LYS A 1 751  ? 48.740 74.161  -43.621 1.00 28.72 ? 751  LYS A CD  1 
ATOM   6012 C  CE  . LYS A 1 751  ? 49.065 72.795  -44.206 1.00 31.20 ? 751  LYS A CE  1 
ATOM   6013 N  NZ  . LYS A 1 751  ? 47.786 72.046  -44.493 1.00 34.25 ? 751  LYS A NZ  1 
ATOM   6014 N  N   . LEU A 1 752  ? 46.729 74.460  -38.854 1.00 12.29 ? 752  LEU A N   1 
ATOM   6015 C  CA  . LEU A 1 752  ? 46.948 73.468  -37.791 1.00 11.19 ? 752  LEU A CA  1 
ATOM   6016 C  C   . LEU A 1 752  ? 45.901 73.507  -36.690 1.00 11.42 ? 752  LEU A C   1 
ATOM   6017 O  O   . LEU A 1 752  ? 45.603 72.480  -36.064 1.00 10.91 ? 752  LEU A O   1 
ATOM   6018 C  CB  . LEU A 1 752  ? 48.319 73.688  -37.122 1.00 12.33 ? 752  LEU A CB  1 
ATOM   6019 C  CG  . LEU A 1 752  ? 49.560 73.668  -38.029 1.00 13.54 ? 752  LEU A CG  1 
ATOM   6020 C  CD1 . LEU A 1 752  ? 50.842 73.797  -37.200 1.00 15.09 ? 752  LEU A CD1 1 
ATOM   6021 C  CD2 . LEU A 1 752  ? 49.560 72.412  -38.882 1.00 17.17 ? 752  LEU A CD2 1 
ATOM   6022 N  N   . GLU A 1 753  ? 45.300 74.676  -36.462 1.00 11.65 ? 753  GLU A N   1 
ATOM   6023 C  CA  . GLU A 1 753  ? 44.366 74.805  -35.371 1.00 11.43 ? 753  GLU A CA  1 
ATOM   6024 C  C   . GLU A 1 753  ? 43.365 75.918  -35.697 1.00 10.87 ? 753  GLU A C   1 
ATOM   6025 O  O   . GLU A 1 753  ? 43.823 77.025  -36.124 1.00 12.37 ? 753  GLU A O   1 
ATOM   6026 C  CB  . GLU A 1 753  ? 45.128 75.198  -34.074 1.00 11.75 ? 753  GLU A CB  1 
ATOM   6027 C  CG  . GLU A 1 753  ? 44.207 75.387  -32.858 1.00 14.53 ? 753  GLU A CG  1 
ATOM   6028 C  CD  . GLU A 1 753  ? 44.946 75.986  -31.644 1.00 16.59 ? 753  GLU A CD  1 
ATOM   6029 O  OE1 . GLU A 1 753  ? 45.251 77.203  -31.648 1.00 22.37 ? 753  GLU A OE1 1 
ATOM   6030 O  OE2 . GLU A 1 753  ? 45.225 75.182  -30.751 1.00 20.36 ? 753  GLU A OE2 1 
ATOM   6031 N  N   . SER A 1 754  ? 42.086 75.638  -35.500 1.00 10.18 ? 754  SER A N   1 
ATOM   6032 C  CA  . SER A 1 754  ? 41.016 76.614  -35.687 1.00 9.86  ? 754  SER A CA  1 
ATOM   6033 C  C   . SER A 1 754  ? 40.140 76.632  -34.459 1.00 9.62  ? 754  SER A C   1 
ATOM   6034 O  O   . SER A 1 754  ? 40.134 75.661  -33.646 1.00 10.20 ? 754  SER A O   1 
ATOM   6035 C  CB  . SER A 1 754  ? 40.167 76.229  -36.885 1.00 10.83 ? 754  SER A CB  1 
ATOM   6036 O  OG  . SER A 1 754  ? 40.925 76.369  -38.086 1.00 11.88 ? 754  SER A OG  1 
ATOM   6037 N  N   . SER A 1 755  ? 39.364 77.689  -34.297 1.00 9.82  ? 755  SER A N   1 
ATOM   6038 C  CA  . SER A 1 755  ? 38.497 77.766  -33.155 1.00 10.16 ? 755  SER A CA  1 
ATOM   6039 C  C   . SER A 1 755  ? 37.329 78.686  -33.346 1.00 9.17  ? 755  SER A C   1 
ATOM   6040 O  O   A SER A 1 755  ? 37.373 79.574  -34.200 0.50 10.24 ? 755  SER A O   1 
ATOM   6041 O  O   B SER A 1 755  ? 37.500 79.724  -33.998 0.50 10.31 ? 755  SER A O   1 
ATOM   6042 C  CB  A SER A 1 755  ? 39.304 78.245  -31.935 0.50 11.12 ? 755  SER A CB  1 
ATOM   6043 C  CB  B SER A 1 755  ? 39.262 78.021  -31.810 0.50 12.51 ? 755  SER A CB  1 
ATOM   6044 O  OG  A SER A 1 755  ? 39.955 79.468  -32.192 0.50 12.09 ? 755  SER A OG  1 
ATOM   6045 O  OG  B SER A 1 755  ? 39.659 79.357  -31.716 0.50 13.12 ? 755  SER A OG  1 
ATOM   6046 N  N   . VAL A 1 756  ? 36.298 78.497  -32.548 1.00 9.13  ? 756  VAL A N   1 
ATOM   6047 C  CA  . VAL A 1 756  ? 35.149 79.362  -32.490 1.00 9.66  ? 756  VAL A CA  1 
ATOM   6048 C  C   . VAL A 1 756  ? 35.018 79.701  -31.008 1.00 9.80  ? 756  VAL A C   1 
ATOM   6049 O  O   . VAL A 1 756  ? 34.867 78.769  -30.151 1.00 10.15 ? 756  VAL A O   1 
ATOM   6050 C  CB  . VAL A 1 756  ? 33.865 78.728  -32.995 1.00 10.33 ? 756  VAL A CB  1 
ATOM   6051 C  CG1 . VAL A 1 756  ? 32.674 79.723  -32.776 1.00 12.08 ? 756  VAL A CG1 1 
ATOM   6052 C  CG2 . VAL A 1 756  ? 34.051 78.343  -34.484 1.00 12.49 ? 756  VAL A CG2 1 
ATOM   6053 N  N   . SER A 1 757  ? 35.041 80.974  -30.642 1.00 9.29  ? 757  SER A N   1 
ATOM   6054 C  CA  . SER A 1 757  ? 34.919 81.405  -29.233 1.00 9.77  ? 757  SER A CA  1 
ATOM   6055 C  C   . SER A 1 757  ? 33.776 82.374  -29.106 1.00 10.02 ? 757  SER A C   1 
ATOM   6056 O  O   . SER A 1 757  ? 33.608 83.235  -30.015 1.00 11.34 ? 757  SER A O   1 
ATOM   6057 C  CB  . SER A 1 757  ? 36.219 82.117  -28.777 1.00 10.72 ? 757  SER A CB  1 
ATOM   6058 O  OG  . SER A 1 757  ? 37.294 81.222  -28.948 1.00 12.95 ? 757  SER A OG  1 
ATOM   6059 N  N   . VAL A 1 758  ? 32.984 82.308  -28.061 1.00 9.83  ? 758  VAL A N   1 
ATOM   6060 C  CA  . VAL A 1 758  ? 31.858 83.220  -27.892 1.00 10.45 ? 758  VAL A CA  1 
ATOM   6061 C  C   . VAL A 1 758  ? 31.738 83.670  -26.470 1.00 9.95  ? 758  VAL A C   1 
ATOM   6062 O  O   . VAL A 1 758  ? 31.914 82.876  -25.521 1.00 9.98  ? 758  VAL A O   1 
ATOM   6063 C  CB  . VAL A 1 758  ? 30.542 82.568  -28.416 1.00 10.43 ? 758  VAL A CB  1 
ATOM   6064 C  CG1 . VAL A 1 758  ? 30.288 81.216  -27.700 1.00 11.06 ? 758  VAL A CG1 1 
ATOM   6065 C  CG2 . VAL A 1 758  ? 29.381 83.522  -28.205 1.00 11.31 ? 758  VAL A CG2 1 
ATOM   6066 N  N   . GLY A 1 759  ? 31.483 84.951  -26.287 1.00 10.56 ? 759  GLY A N   1 
ATOM   6067 C  CA  . GLY A 1 759  ? 31.357 85.505  -24.953 1.00 11.97 ? 759  GLY A CA  1 
ATOM   6068 C  C   . GLY A 1 759  ? 29.914 85.491  -24.496 1.00 11.71 ? 759  GLY A C   1 
ATOM   6069 O  O   . GLY A 1 759  ? 29.113 86.390  -24.819 1.00 12.19 ? 759  GLY A O   1 
ATOM   6070 N  N   . LEU A 1 760  ? 29.539 84.471  -23.750 1.00 12.12 ? 760  LEU A N   1 
ATOM   6071 C  CA  . LEU A 1 760  ? 28.171 84.338  -23.250 1.00 12.89 ? 760  LEU A CA  1 
ATOM   6072 C  C   . LEU A 1 760  ? 28.086 84.822  -21.826 1.00 12.92 ? 760  LEU A C   1 
ATOM   6073 O  O   . LEU A 1 760  ? 29.094 84.984  -21.143 1.00 14.03 ? 760  LEU A O   1 
ATOM   6074 C  CB  . LEU A 1 760  ? 27.811 82.838  -23.248 1.00 13.02 ? 760  LEU A CB  1 
ATOM   6075 C  CG  . LEU A 1 760  ? 28.001 82.136  -24.591 1.00 12.96 ? 760  LEU A CG  1 
ATOM   6076 C  CD1 . LEU A 1 760  ? 27.783 80.632  -24.489 1.00 14.34 ? 760  LEU A CD1 1 
ATOM   6077 C  CD2 . LEU A 1 760  ? 26.987 82.745  -25.619 1.00 15.89 ? 760  LEU A CD2 1 
ATOM   6078 N  N   . PRO A 1 761  ? 26.876 85.034  -21.302 1.00 14.45 ? 761  PRO A N   1 
ATOM   6079 C  CA  . PRO A 1 761  ? 26.832 85.485  -19.904 1.00 14.16 ? 761  PRO A CA  1 
ATOM   6080 C  C   . PRO A 1 761  ? 27.402 84.362  -19.031 1.00 14.28 ? 761  PRO A C   1 
ATOM   6081 O  O   . PRO A 1 761  ? 26.923 83.209  -19.099 1.00 14.58 ? 761  PRO A O   1 
ATOM   6082 C  CB  . PRO A 1 761  ? 25.315 85.692  -19.650 1.00 15.29 ? 761  PRO A CB  1 
ATOM   6083 C  CG  . PRO A 1 761  ? 24.823 86.035  -21.042 1.00 16.25 ? 761  PRO A CG  1 
ATOM   6084 C  CD  . PRO A 1 761  ? 25.546 85.072  -21.938 1.00 14.97 ? 761  PRO A CD  1 
ATOM   6085 N  N   . SER A 1 762  ? 28.410 84.751  -18.243 1.00 13.36 ? 762  SER A N   1 
ATOM   6086 C  CA  . SER A 1 762  ? 29.120 83.899  -17.298 1.00 12.53 ? 762  SER A CA  1 
ATOM   6087 C  C   . SER A 1 762  ? 30.050 82.880  -17.910 1.00 10.75 ? 762  SER A C   1 
ATOM   6088 O  O   . SER A 1 762  ? 30.727 82.183  -17.163 1.00 10.94 ? 762  SER A O   1 
ATOM   6089 C  CB  . SER A 1 762  ? 28.165 83.114  -16.419 1.00 13.19 ? 762  SER A CB  1 
ATOM   6090 O  OG  . SER A 1 762  ? 27.258 83.922  -15.661 1.00 16.95 ? 762  SER A OG  1 
ATOM   6091 N  N   . VAL A 1 763  ? 30.138 82.798  -19.222 1.00 10.49 ? 763  VAL A N   1 
ATOM   6092 C  CA  . VAL A 1 763  ? 30.990 81.791  -19.846 1.00 10.88 ? 763  VAL A CA  1 
ATOM   6093 C  C   . VAL A 1 763  ? 31.591 82.204  -21.159 1.00 10.41 ? 763  VAL A C   1 
ATOM   6094 O  O   . VAL A 1 763  ? 30.857 82.573  -22.043 1.00 11.76 ? 763  VAL A O   1 
ATOM   6095 C  CB  . VAL A 1 763  ? 30.218 80.464  -20.164 1.00 12.01 ? 763  VAL A CB  1 
ATOM   6096 C  CG1 . VAL A 1 763  ? 31.182 79.388  -20.698 1.00 11.97 ? 763  VAL A CG1 1 
ATOM   6097 C  CG2 . VAL A 1 763  ? 29.515 79.909  -18.921 1.00 14.96 ? 763  VAL A CG2 1 
ATOM   6098 N  N   . VAL A 1 764  ? 32.912 82.231  -21.267 1.00 9.12  ? 764  VAL A N   1 
ATOM   6099 C  CA  . VAL A 1 764  ? 33.507 82.402  -22.586 1.00 8.84  ? 764  VAL A CA  1 
ATOM   6100 C  C   . VAL A 1 764  ? 33.675 80.925  -23.042 1.00 8.77  ? 764  VAL A C   1 
ATOM   6101 O  O   . VAL A 1 764  ? 34.454 80.146  -22.463 1.00 9.29  ? 764  VAL A O   1 
ATOM   6102 C  CB  . VAL A 1 764  ? 34.885 83.112  -22.578 1.00 9.54  ? 764  VAL A CB  1 
ATOM   6103 C  CG1 . VAL A 1 764  ? 35.439 83.169  -24.038 1.00 11.11 ? 764  VAL A CG1 1 
ATOM   6104 C  CG2 . VAL A 1 764  ? 34.727 84.543  -21.985 1.00 11.75 ? 764  VAL A CG2 1 
ATOM   6105 N  N   . HIS A 1 765  ? 32.922 80.526  -24.069 1.00 9.39  ? 765  HIS A N   1 
ATOM   6106 C  CA  . HIS A 1 765  ? 32.869 79.147  -24.565 1.00 8.34  ? 765  HIS A CA  1 
ATOM   6107 C  C   . HIS A 1 765  ? 33.699 79.031  -25.805 1.00 8.87  ? 765  HIS A C   1 
ATOM   6108 O  O   . HIS A 1 765  ? 33.517 79.843  -26.722 1.00 10.26 ? 765  HIS A O   1 
ATOM   6109 C  CB  . HIS A 1 765  ? 31.388 78.823  -24.859 1.00 9.67  ? 765  HIS A CB  1 
ATOM   6110 C  CG  . HIS A 1 765  ? 31.147 77.464  -25.398 1.00 8.69  ? 765  HIS A CG  1 
ATOM   6111 N  ND1 . HIS A 1 765  ? 30.596 77.199  -26.641 1.00 12.62 ? 765  HIS A ND1 1 
ATOM   6112 C  CD2 . HIS A 1 765  ? 31.347 76.262  -24.813 1.00 7.28  ? 765  HIS A CD2 1 
ATOM   6113 C  CE1 . HIS A 1 765  ? 30.470 75.889  -26.803 1.00 9.36  ? 765  HIS A CE1 1 
ATOM   6114 N  NE2 . HIS A 1 765  ? 30.925 75.295  -25.699 1.00 12.81 ? 765  HIS A NE2 1 
ATOM   6115 N  N   . GLN A 1 766  ? 34.570 78.040  -25.888 1.00 8.66  ? 766  GLN A N   1 
ATOM   6116 C  CA  . GLN A 1 766  ? 35.447 77.909  -27.020 1.00 8.78  ? 766  GLN A CA  1 
ATOM   6117 C  C   . GLN A 1 766  ? 35.397 76.478  -27.505 1.00 8.34  ? 766  GLN A C   1 
ATOM   6118 O  O   A GLN A 1 766  ? 35.329 75.537  -26.682 0.50 7.33  ? 766  GLN A O   1 
ATOM   6119 O  O   B GLN A 1 766  ? 35.850 75.492  -26.792 0.50 8.64  ? 766  GLN A O   1 
ATOM   6120 C  CB  . GLN A 1 766  ? 36.901 78.270  -26.596 1.00 10.53 ? 766  GLN A CB  1 
ATOM   6121 C  CG  A GLN A 1 766  ? 37.047 79.604  -25.807 0.50 12.76 ? 766  GLN A CG  1 
ATOM   6122 C  CG  B GLN A 1 766  ? 37.866 78.268  -27.850 0.50 10.32 ? 766  GLN A CG  1 
ATOM   6123 C  CD  A GLN A 1 766  ? 38.083 79.564  -24.647 0.50 15.98 ? 766  GLN A CD  1 
ATOM   6124 C  CD  B GLN A 1 766  ? 39.278 78.752  -27.527 0.50 11.61 ? 766  GLN A CD  1 
ATOM   6125 O  OE1 A GLN A 1 766  ? 39.259 79.277  -24.875 0.50 15.39 ? 766  GLN A OE1 1 
ATOM   6126 O  OE1 B GLN A 1 766  ? 40.047 79.171  -28.424 0.50 13.30 ? 766  GLN A OE1 1 
ATOM   6127 N  NE2 A GLN A 1 766  ? 37.635 79.863  -23.395 0.50 14.10 ? 766  GLN A NE2 1 
ATOM   6128 N  NE2 B GLN A 1 766  ? 39.632 78.698  -26.247 0.50 12.54 ? 766  GLN A NE2 1 
ATOM   6129 N  N   . THR A 1 767  ? 35.385 76.311  -28.831 1.00 8.23  ? 767  THR A N   1 
ATOM   6130 C  CA  . THR A 1 767  ? 35.490 75.019  -29.481 1.00 8.62  ? 767  THR A CA  1 
ATOM   6131 C  C   . THR A 1 767  ? 36.755 75.072  -30.296 1.00 8.91  ? 767  THR A C   1 
ATOM   6132 O  O   . THR A 1 767  ? 36.884 75.928  -31.201 1.00 10.21 ? 767  THR A O   1 
ATOM   6133 C  CB  . THR A 1 767  ? 34.297 74.755  -30.367 1.00 9.50  ? 767  THR A CB  1 
ATOM   6134 O  OG1 . THR A 1 767  ? 33.117 74.847  -29.568 1.00 11.01 ? 767  THR A OG1 1 
ATOM   6135 C  CG2 . THR A 1 767  ? 34.396 73.319  -30.982 1.00 10.16 ? 767  THR A CG2 1 
ATOM   6136 N  N   . ILE A 1 768  ? 37.715 74.196  -30.034 1.00 9.88  ? 768  ILE A N   1 
ATOM   6137 C  CA  . ILE A 1 768  ? 39.009 74.178  -30.725 1.00 9.06  ? 768  ILE A CA  1 
ATOM   6138 C  C   . ILE A 1 768  ? 39.171 72.914  -31.546 1.00 9.81  ? 768  ILE A C   1 
ATOM   6139 O  O   . ILE A 1 768  ? 38.849 71.804  -31.074 1.00 11.20 ? 768  ILE A O   1 
ATOM   6140 C  CB  . ILE A 1 768  ? 40.147 74.271  -29.717 1.00 9.77  ? 768  ILE A CB  1 
ATOM   6141 C  CG1 . ILE A 1 768  ? 39.939 75.523  -28.892 1.00 11.03 ? 768  ILE A CG1 1 
ATOM   6142 C  CG2 . ILE A 1 768  ? 41.512 74.350  -30.392 1.00 11.07 ? 768  ILE A CG2 1 
ATOM   6143 C  CD1 . ILE A 1 768  ? 40.769 75.487  -27.585 1.00 13.60 ? 768  ILE A CD1 1 
ATOM   6144 N  N   . MET A 1 769  ? 39.632 73.051  -32.766 1.00 9.64  ? 769  MET A N   1 
ATOM   6145 C  CA  . MET A 1 769  ? 39.797 71.919  -33.689 1.00 9.57  ? 769  MET A CA  1 
ATOM   6146 C  C   . MET A 1 769  ? 41.228 71.809  -34.129 1.00 10.76 ? 769  MET A C   1 
ATOM   6147 O  O   . MET A 1 769  ? 41.849 72.792  -34.595 1.00 10.92 ? 769  MET A O   1 
ATOM   6148 C  CB  . MET A 1 769  ? 38.938 72.181  -34.926 1.00 11.83 ? 769  MET A CB  1 
ATOM   6149 C  CG  . MET A 1 769  ? 37.490 72.314  -34.547 1.00 12.19 ? 769  MET A CG  1 
ATOM   6150 S  SD  . MET A 1 769  ? 36.454 72.922  -35.879 1.00 15.84 ? 769  MET A SD  1 
ATOM   6151 C  CE  . MET A 1 769  ? 36.774 71.556  -37.026 1.00 18.30 ? 769  MET A CE  1 
ATOM   6152 N  N   . ARG A 1 770  ? 41.809 70.632  -33.941 1.00 11.27 ? 770  ARG A N   1 
ATOM   6153 C  CA  . ARG A 1 770  ? 43.167 70.419  -34.356 1.00 13.06 ? 770  ARG A CA  1 
ATOM   6154 C  C   . ARG A 1 770  ? 43.270 69.233  -35.317 1.00 15.03 ? 770  ARG A C   1 
ATOM   6155 O  O   . ARG A 1 770  ? 44.371 68.730  -35.538 1.00 16.34 ? 770  ARG A O   1 
ATOM   6156 C  CB  . ARG A 1 770  ? 44.067 70.231  -33.126 1.00 13.52 ? 770  ARG A CB  1 
ATOM   6157 C  CG  A ARG A 1 770  ? 43.851 71.298  -32.037 0.50 14.11 ? 770  ARG A CG  1 
ATOM   6158 C  CG  B ARG A 1 770  ? 44.360 71.274  -32.386 0.50 13.15 ? 770  ARG A CG  1 
ATOM   6159 C  CD  A ARG A 1 770  ? 45.001 71.355  -31.001 0.50 14.48 ? 770  ARG A CD  1 
ATOM   6160 C  CD  B ARG A 1 770  ? 45.211 70.802  -31.230 0.50 14.37 ? 770  ARG A CD  1 
ATOM   6161 N  NE  A ARG A 1 770  ? 44.813 72.355  -29.949 0.50 16.43 ? 770  ARG A NE  1 
ATOM   6162 N  NE  B ARG A 1 770  ? 44.537 69.697  -30.559 0.50 16.06 ? 770  ARG A NE  1 
ATOM   6163 C  CZ  A ARG A 1 770  ? 44.031 72.187  -28.886 0.50 15.62 ? 770  ARG A CZ  1 
ATOM   6164 C  CZ  B ARG A 1 770  ? 43.764 69.839  -29.490 0.50 16.80 ? 770  ARG A CZ  1 
ATOM   6165 N  NH1 A ARG A 1 770  ? 43.353 71.059  -28.741 0.50 17.22 ? 770  ARG A NH1 1 
ATOM   6166 N  NH1 B ARG A 1 770  ? 43.563 71.039  -28.953 0.50 18.11 ? 770  ARG A NH1 1 
ATOM   6167 N  NH2 A ARG A 1 770  ? 43.956 73.122  -27.946 0.50 15.81 ? 770  ARG A NH2 1 
ATOM   6168 N  NH2 B ARG A 1 770  ? 43.196 68.774  -28.952 0.50 15.96 ? 770  ARG A NH2 1 
ATOM   6169 N  N   . GLY A 1 771  ? 42.128 68.792  -35.852 1.00 15.39 ? 771  GLY A N   1 
ATOM   6170 C  CA  . GLY A 1 771  ? 42.139 67.705  -36.809 1.00 17.55 ? 771  GLY A CA  1 
ATOM   6171 C  C   . GLY A 1 771  ? 41.449 66.431  -36.429 1.00 19.01 ? 771  GLY A C   1 
ATOM   6172 O  O   . GLY A 1 771  ? 41.193 65.573  -37.303 1.00 20.05 ? 771  GLY A O   1 
ATOM   6173 N  N   . GLY A 1 772  ? 41.180 66.279  -35.134 1.00 18.05 ? 772  GLY A N   1 
ATOM   6174 C  CA  . GLY A 1 772  ? 40.480 65.102  -34.596 1.00 16.71 ? 772  GLY A CA  1 
ATOM   6175 C  C   . GLY A 1 772  ? 39.325 65.565  -33.698 1.00 15.96 ? 772  GLY A C   1 
ATOM   6176 O  O   . GLY A 1 772  ? 38.651 66.550  -34.018 1.00 14.77 ? 772  GLY A O   1 
ATOM   6177 N  N   . ALA A 1 773  ? 39.078 64.892  -32.570 1.00 13.80 ? 773  ALA A N   1 
ATOM   6178 C  CA  . ALA A 1 773  ? 37.971 65.285  -31.702 1.00 12.95 ? 773  ALA A CA  1 
ATOM   6179 C  C   . ALA A 1 773  ? 38.197 66.710  -31.216 1.00 10.53 ? 773  ALA A C   1 
ATOM   6180 O  O   . ALA A 1 773  ? 39.302 67.052  -30.803 1.00 10.83 ? 773  ALA A O   1 
ATOM   6181 C  CB  . ALA A 1 773  ? 37.886 64.372  -30.508 1.00 14.68 ? 773  ALA A CB  1 
ATOM   6182 N  N   . PRO A 1 774  ? 37.158 67.520  -31.218 1.00 10.08 ? 774  PRO A N   1 
ATOM   6183 C  CA  . PRO A 1 774  ? 37.369 68.895  -30.751 1.00 10.35 ? 774  PRO A CA  1 
ATOM   6184 C  C   . PRO A 1 774  ? 37.650 68.946  -29.265 1.00 9.83  ? 774  PRO A C   1 
ATOM   6185 O  O   . PRO A 1 774  ? 37.362 68.010  -28.518 1.00 9.31  ? 774  PRO A O   1 
ATOM   6186 C  CB  . PRO A 1 774  ? 36.046 69.624  -31.074 1.00 12.11 ? 774  PRO A CB  1 
ATOM   6187 C  CG  . PRO A 1 774  ? 35.077 68.569  -31.235 1.00 14.90 ? 774  PRO A CG  1 
ATOM   6188 C  CD  . PRO A 1 774  ? 35.825 67.364  -31.813 1.00 11.29 ? 774  PRO A CD  1 
ATOM   6189 N  N   . GLU A 1 775  ? 38.212 70.058  -28.869 1.00 9.33  ? 775  GLU A N   1 
ATOM   6190 C  CA  . GLU A 1 775  ? 38.457 70.395  -27.478 1.00 8.62  ? 775  GLU A CA  1 
ATOM   6191 C  C   . GLU A 1 775  ? 37.533 71.533  -27.124 1.00 7.79  ? 775  GLU A C   1 
ATOM   6192 O  O   . GLU A 1 775  ? 37.381 72.484  -27.940 1.00 10.63 ? 775  GLU A O   1 
ATOM   6193 C  CB  . GLU A 1 775  ? 39.896 70.839  -27.269 1.00 9.27  ? 775  GLU A CB  1 
ATOM   6194 C  CG  . GLU A 1 775  ? 40.216 71.260  -25.796 1.00 10.61 ? 775  GLU A CG  1 
ATOM   6195 C  CD  . GLU A 1 775  ? 41.677 71.493  -25.565 1.00 15.82 ? 775  GLU A CD  1 
ATOM   6196 O  OE1 . GLU A 1 775  ? 42.499 70.710  -26.064 1.00 19.27 ? 775  GLU A OE1 1 
ATOM   6197 O  OE2 . GLU A 1 775  ? 42.004 72.433  -24.852 1.00 18.77 ? 775  GLU A OE2 1 
ATOM   6198 N  N   . ILE A 1 776  ? 36.870 71.486  -25.993 1.00 7.79  ? 776  ILE A N   1 
ATOM   6199 C  CA  . ILE A 1 776  ? 36.024 72.565  -25.548 1.00 8.34  ? 776  ILE A CA  1 
ATOM   6200 C  C   . ILE A 1 776  ? 36.667 73.178  -24.319 1.00 7.61  ? 776  ILE A C   1 
ATOM   6201 O  O   . ILE A 1 776  ? 37.118 72.445  -23.425 1.00 8.13  ? 776  ILE A O   1 
ATOM   6202 C  CB  . ILE A 1 776  ? 34.625 72.051  -25.139 1.00 9.10  ? 776  ILE A CB  1 
ATOM   6203 C  CG1 . ILE A 1 776  ? 34.072 71.103  -26.218 1.00 12.76 ? 776  ILE A CG1 1 
ATOM   6204 C  CG2 . ILE A 1 776  ? 33.738 73.239  -24.701 1.00 10.01 ? 776  ILE A CG2 1 
ATOM   6205 C  CD1 . ILE A 1 776  ? 33.922 71.667  -27.628 1.00 14.76 ? 776  ILE A CD1 1 
ATOM   6206 N  N   . ARG A 1 777  ? 36.718 74.498  -24.258 1.00 8.27  ? 777  ARG A N   1 
ATOM   6207 C  CA  . ARG A 1 777  ? 37.196 75.210  -23.054 1.00 7.84  ? 777  ARG A CA  1 
ATOM   6208 C  C   . ARG A 1 777  ? 36.138 76.202  -22.650 1.00 8.99  ? 777  ARG A C   1 
ATOM   6209 O  O   . ARG A 1 777  ? 35.615 77.007  -23.489 1.00 10.11 ? 777  ARG A O   1 
ATOM   6210 C  CB  . ARG A 1 777  ? 38.499 75.984  -23.321 1.00 9.94  ? 777  ARG A CB  1 
ATOM   6211 C  CG  . ARG A 1 777  ? 39.658 75.088  -23.692 1.00 9.51  ? 777  ARG A CG  1 
ATOM   6212 C  CD  . ARG A 1 777  ? 40.945 75.901  -23.812 1.00 11.21 ? 777  ARG A CD  1 
ATOM   6213 N  NE  . ARG A 1 777  ? 42.024 75.042  -24.259 1.00 12.63 ? 777  ARG A NE  1 
ATOM   6214 C  CZ  . ARG A 1 777  ? 43.227 75.501  -24.588 1.00 17.05 ? 777  ARG A CZ  1 
ATOM   6215 N  NH1 . ARG A 1 777  ? 43.474 76.808  -24.476 1.00 18.99 ? 777  ARG A NH1 1 
ATOM   6216 N  NH2 . ARG A 1 777  ? 44.150 74.675  -25.105 1.00 19.05 ? 777  ARG A NH2 1 
ATOM   6217 N  N   . ASN A 1 778  ? 35.789 76.213  -21.395 1.00 7.97  ? 778  ASN A N   1 
ATOM   6218 C  CA  . ASN A 1 778  ? 34.852 77.176  -20.837 1.00 8.00  ? 778  ASN A CA  1 
ATOM   6219 C  C   . ASN A 1 778  ? 35.551 77.994  -19.760 1.00 8.03  ? 778  ASN A C   1 
ATOM   6220 O  O   . ASN A 1 778  ? 36.001 77.415  -18.725 1.00 7.69  ? 778  ASN A O   1 
ATOM   6221 C  CB  . ASN A 1 778  ? 33.627 76.516  -20.163 1.00 8.64  ? 778  ASN A CB  1 
ATOM   6222 C  CG  . ASN A 1 778  ? 32.679 75.836  -21.144 1.00 8.58  ? 778  ASN A CG  1 
ATOM   6223 O  OD1 . ASN A 1 778  ? 32.615 76.171  -22.327 1.00 9.67  ? 778  ASN A OD1 1 
ATOM   6224 N  ND2 . ASN A 1 778  ? 31.904 74.877  -20.635 1.00 9.52  ? 778  ASN A ND2 1 
ATOM   6225 N  N   . LEU A 1 779  ? 35.618 79.317  -19.942 1.00 8.07  ? 779  LEU A N   1 
ATOM   6226 C  CA  . LEU A 1 779  ? 36.138 80.187  -18.870 1.00 8.37  ? 779  LEU A CA  1 
ATOM   6227 C  C   . LEU A 1 779  ? 34.863 80.596  -18.145 1.00 8.54  ? 779  LEU A C   1 
ATOM   6228 O  O   . LEU A 1 779  ? 34.044 81.380  -18.658 1.00 9.51  ? 779  LEU A O   1 
ATOM   6229 C  CB  . LEU A 1 779  ? 36.902 81.381  -19.487 1.00 10.72 ? 779  LEU A CB  1 
ATOM   6230 C  CG  . LEU A 1 779  ? 37.458 82.334  -18.413 1.00 13.40 ? 779  LEU A CG  1 
ATOM   6231 C  CD1 . LEU A 1 779  ? 38.453 81.671  -17.530 1.00 15.11 ? 779  LEU A CD1 1 
ATOM   6232 C  CD2 . LEU A 1 779  ? 38.057 83.540  -19.182 1.00 17.34 ? 779  LEU A CD2 1 
ATOM   6233 N  N   . VAL A 1 780  ? 34.651 80.001  -16.982 1.00 8.21  ? 780  VAL A N   1 
ATOM   6234 C  CA  . VAL A 1 780  ? 33.400 80.170  -16.244 1.00 9.30  ? 780  VAL A CA  1 
ATOM   6235 C  C   . VAL A 1 780  ? 33.545 81.171  -15.091 1.00 9.73  ? 780  VAL A C   1 
ATOM   6236 O  O   . VAL A 1 780  ? 34.344 80.971  -14.180 1.00 9.80  ? 780  VAL A O   1 
ATOM   6237 C  CB  . VAL A 1 780  ? 32.917 78.800  -15.687 1.00 8.77  ? 780  VAL A CB  1 
ATOM   6238 C  CG1 . VAL A 1 780  ? 31.609 78.976  -14.926 1.00 10.14 ? 780  VAL A CG1 1 
ATOM   6239 C  CG2 . VAL A 1 780  ? 32.818 77.772  -16.804 1.00 9.81  ? 780  VAL A CG2 1 
ATOM   6240 N  N   . ASP A 1 781  ? 32.785 82.271  -15.157 1.00 9.86  ? 781  ASP A N   1 
ATOM   6241 C  CA  . ASP A 1 781  ? 32.761 83.304  -14.103 1.00 10.20 ? 781  ASP A CA  1 
ATOM   6242 C  C   . ASP A 1 781  ? 31.339 83.615  -13.757 1.00 10.83 ? 781  ASP A C   1 
ATOM   6243 O  O   . ASP A 1 781  ? 30.678 84.444  -14.410 1.00 11.27 ? 781  ASP A O   1 
ATOM   6244 C  CB  . ASP A 1 781  ? 33.452 84.551  -14.602 1.00 11.87 ? 781  ASP A CB  1 
ATOM   6245 C  CG  . ASP A 1 781  ? 33.531 85.597  -13.528 1.00 12.96 ? 781  ASP A CG  1 
ATOM   6246 O  OD1 . ASP A 1 781  ? 33.086 85.341  -12.396 1.00 12.24 ? 781  ASP A OD1 1 
ATOM   6247 O  OD2 . ASP A 1 781  ? 34.080 86.680  -13.860 1.00 17.35 ? 781  ASP A OD2 1 
ATOM   6248 N  N   . ILE A 1 782  ? 30.830 82.906  -12.765 1.00 10.84 ? 782  ILE A N   1 
ATOM   6249 C  CA  . ILE A 1 782  ? 29.423 83.034  -12.338 1.00 12.28 ? 782  ILE A CA  1 
ATOM   6250 C  C   . ILE A 1 782  ? 29.172 84.392  -11.718 1.00 14.36 ? 782  ILE A C   1 
ATOM   6251 O  O   . ILE A 1 782  ? 28.013 84.750  -11.418 1.00 16.07 ? 782  ILE A O   1 
ATOM   6252 C  CB  . ILE A 1 782  ? 29.073 81.810  -11.435 1.00 13.46 ? 782  ILE A CB  1 
ATOM   6253 C  CG1 . ILE A 1 782  ? 27.576 81.654  -11.217 1.00 14.07 ? 782  ILE A CG1 1 
ATOM   6254 C  CG2 . ILE A 1 782  ? 29.749 81.962  -10.091 1.00 13.82 ? 782  ILE A CG2 1 
ATOM   6255 C  CD1 . ILE A 1 782  ? 27.261 80.266  -10.724 1.00 15.11 ? 782  ILE A CD1 1 
ATOM   6256 N  N   . GLY A 1 783  ? 30.244 85.159  -11.498 1.00 14.27 ? 783  GLY A N   1 
ATOM   6257 C  CA  . GLY A 1 783  ? 30.065 86.536  -11.041 1.00 15.41 ? 783  GLY A CA  1 
ATOM   6258 C  C   . GLY A 1 783  ? 29.239 86.637  -9.777  1.00 15.75 ? 783  GLY A C   1 
ATOM   6259 O  O   . GLY A 1 783  ? 29.491 85.901  -8.816  1.00 17.53 ? 783  GLY A O   1 
ATOM   6260 N  N   . SER A 1 784  ? 28.243 87.526  -9.766  1.00 18.43 ? 784  SER A N   1 
ATOM   6261 C  CA  . SER A 1 784  ? 27.448 87.645  -8.545  1.00 19.45 ? 784  SER A CA  1 
ATOM   6262 C  C   . SER A 1 784  ? 26.043 87.054  -8.674  1.00 19.55 ? 784  SER A C   1 
ATOM   6263 O  O   . SER A 1 784  ? 25.108 87.460  -7.949  1.00 19.99 ? 784  SER A O   1 
ATOM   6264 C  CB  . SER A 1 784  ? 27.357 89.105  -8.107  1.00 21.12 ? 784  SER A CB  1 
ATOM   6265 O  OG  . SER A 1 784  ? 26.760 89.889  -9.131  1.00 24.74 ? 784  SER A OG  1 
ATOM   6266 N  N   . LEU A 1 785  ? 25.889 86.087  -9.576  1.00 18.63 ? 785  LEU A N   1 
ATOM   6267 C  CA  . LEU A 1 785  ? 24.588 85.451  -9.766  1.00 18.75 ? 785  LEU A CA  1 
ATOM   6268 C  C   . LEU A 1 785  ? 24.258 84.547  -8.602  1.00 19.74 ? 785  LEU A C   1 
ATOM   6269 O  O   . LEU A 1 785  ? 24.590 83.342  -8.613  1.00 21.58 ? 785  LEU A O   1 
ATOM   6270 C  CB  . LEU A 1 785  ? 24.571 84.611  -11.038 1.00 18.89 ? 785  LEU A CB  1 
ATOM   6271 C  CG  . LEU A 1 785  ? 24.806 85.366  -12.342 1.00 19.06 ? 785  LEU A CG  1 
ATOM   6272 C  CD1 . LEU A 1 785  ? 24.791 84.409  -13.487 1.00 22.00 ? 785  LEU A CD1 1 
ATOM   6273 C  CD2 . LEU A 1 785  ? 23.772 86.475  -12.473 1.00 19.82 ? 785  LEU A CD2 1 
ATOM   6274 N  N   . ASP A 1 786  ? 23.511 85.030  -7.631  1.00 19.14 ? 786  ASP A N   1 
ATOM   6275 C  CA  . ASP A 1 786  ? 23.269 84.158  -6.500  1.00 18.76 ? 786  ASP A CA  1 
ATOM   6276 C  C   . ASP A 1 786  ? 22.215 83.104  -6.797  1.00 15.51 ? 786  ASP A C   1 
ATOM   6277 O  O   . ASP A 1 786  ? 21.394 83.242  -7.700  1.00 15.64 ? 786  ASP A O   1 
ATOM   6278 C  CB  . ASP A 1 786  ? 22.879 84.920  -5.224  1.00 21.35 ? 786  ASP A CB  1 
ATOM   6279 C  CG  . ASP A 1 786  ? 23.886 85.997  -4.857  1.00 24.35 ? 786  ASP A CG  1 
ATOM   6280 O  OD1 . ASP A 1 786  ? 25.143 85.775  -4.811  1.00 22.49 ? 786  ASP A OD1 1 
ATOM   6281 O  OD2 . ASP A 1 786  ? 23.397 87.113  -4.627  1.00 26.96 ? 786  ASP A OD2 1 
ATOM   6282 N  N   . ASN A 1 787  ? 22.345 82.024  -6.039  1.00 14.31 ? 787  ASN A N   1 
ATOM   6283 C  CA  . ASN A 1 787  ? 21.442 80.892  -6.121  1.00 13.05 ? 787  ASN A CA  1 
ATOM   6284 C  C   . ASN A 1 787  ? 21.255 80.421  -7.526  1.00 12.47 ? 787  ASN A C   1 
ATOM   6285 O  O   . ASN A 1 787  ? 20.141 80.209  -8.012  1.00 13.76 ? 787  ASN A O   1 
ATOM   6286 C  CB  . ASN A 1 787  ? 20.131 81.253  -5.403  1.00 14.47 ? 787  ASN A CB  1 
ATOM   6287 C  CG  . ASN A 1 787  ? 20.382 81.529  -3.969  1.00 17.96 ? 787  ASN A CG  1 
ATOM   6288 O  OD1 . ASN A 1 787  ? 21.052 80.716  -3.302  1.00 18.16 ? 787  ASN A OD1 1 
ATOM   6289 N  ND2 . ASN A 1 787  ? 19.900 82.704  -3.462  1.00 22.34 ? 787  ASN A ND2 1 
ATOM   6290 N  N   . THR A 1 788  ? 22.387 80.211  -8.199  1.00 11.28 ? 788  THR A N   1 
ATOM   6291 C  CA  . THR A 1 788  ? 22.384 79.800  -9.589  1.00 11.06 ? 788  THR A CA  1 
ATOM   6292 C  C   . THR A 1 788  ? 23.424 78.688  -9.819  1.00 10.10 ? 788  THR A C   1 
ATOM   6293 O  O   . THR A 1 788  ? 24.522 78.756  -9.256  1.00 10.84 ? 788  THR A O   1 
ATOM   6294 C  CB  . THR A 1 788  ? 22.805 80.995  -10.464 1.00 12.50 ? 788  THR A CB  1 
ATOM   6295 O  OG1 . THR A 1 788  ? 21.803 82.034  -10.324 1.00 14.19 ? 788  THR A OG1 1 
ATOM   6296 C  CG2 . THR A 1 788  ? 22.862 80.615  -11.917 1.00 14.04 ? 788  THR A CG2 1 
ATOM   6297 N  N   . GLU A 1 789  ? 23.036 77.676  -10.597 1.00 9.15  ? 789  GLU A N   1 
ATOM   6298 C  CA  . GLU A 1 789  ? 23.993 76.631  -11.003 1.00 9.47  ? 789  GLU A CA  1 
ATOM   6299 C  C   . GLU A 1 789  ? 23.977 76.660  -12.521 1.00 9.68  ? 789  GLU A C   1 
ATOM   6300 O  O   . GLU A 1 789  ? 22.900 76.572  -13.131 1.00 11.16 ? 789  GLU A O   1 
ATOM   6301 C  CB  . GLU A 1 789  ? 23.619 75.226  -10.420 1.00 9.85  ? 789  GLU A CB  1 
ATOM   6302 C  CG  . GLU A 1 789  ? 23.233 75.279  -8.957  1.00 10.50 ? 789  GLU A CG  1 
ATOM   6303 C  CD  . GLU A 1 789  ? 23.457 73.956  -8.209  1.00 9.26  ? 789  GLU A CD  1 
ATOM   6304 O  OE1 . GLU A 1 789  ? 24.290 73.139  -8.708  1.00 9.66  ? 789  GLU A OE1 1 
ATOM   6305 O  OE2 . GLU A 1 789  ? 22.809 73.810  -7.153  1.00 9.76  ? 789  GLU A OE2 1 
ATOM   6306 N  N   . ILE A 1 790  ? 25.123 76.823  -13.172 1.00 8.85  ? 790  ILE A N   1 
ATOM   6307 C  CA  . ILE A 1 790  ? 25.208 76.866  -14.612 1.00 9.93  ? 790  ILE A CA  1 
ATOM   6308 C  C   . ILE A 1 790  ? 25.569 75.495  -15.145 1.00 9.08  ? 790  ILE A C   1 
ATOM   6309 O  O   . ILE A 1 790  ? 26.572 74.888  -14.677 1.00 9.63  ? 790  ILE A O   1 
ATOM   6310 C  CB  . ILE A 1 790  ? 26.311 77.854  -15.082 1.00 10.82 ? 790  ILE A CB  1 
ATOM   6311 C  CG1 . ILE A 1 790  ? 25.961 79.287  -14.604 1.00 14.61 ? 790  ILE A CG1 1 
ATOM   6312 C  CG2 . ILE A 1 790  ? 26.440 77.782  -16.634 1.00 11.82 ? 790  ILE A CG2 1 
ATOM   6313 C  CD1 . ILE A 1 790  ? 27.203 80.247  -14.691 1.00 17.97 ? 790  ILE A CD1 1 
ATOM   6314 N  N   . VAL A 1 791  ? 24.767 74.995  -16.070 1.00 8.86  ? 791  VAL A N   1 
ATOM   6315 C  CA  . VAL A 1 791  ? 24.995 73.681  -16.661 1.00 8.48  ? 791  VAL A CA  1 
ATOM   6316 C  C   . VAL A 1 791  ? 25.245 73.777  -18.152 1.00 8.72  ? 791  VAL A C   1 
ATOM   6317 O  O   . VAL A 1 791  ? 24.659 74.688  -18.854 1.00 9.14  ? 791  VAL A O   1 
ATOM   6318 C  CB  . VAL A 1 791  ? 23.776 72.740  -16.351 1.00 8.33  ? 791  VAL A CB  1 
ATOM   6319 C  CG1 . VAL A 1 791  ? 22.465 73.208  -17.115 1.00 10.60 ? 791  VAL A CG1 1 
ATOM   6320 C  CG2 . VAL A 1 791  ? 24.104 71.304  -16.753 1.00 9.67  ? 791  VAL A CG2 1 
ATOM   6321 N  N   . MET A 1 792  ? 26.128 72.937  -18.653 1.00 8.13  ? 792  MET A N   1 
ATOM   6322 C  CA  . MET A 1 792  ? 26.396 72.830  -20.078 1.00 8.31  ? 792  MET A CA  1 
ATOM   6323 C  C   . MET A 1 792  ? 25.731 71.515  -20.537 1.00 7.83  ? 792  MET A C   1 
ATOM   6324 O  O   . MET A 1 792  ? 26.048 70.426  -20.023 1.00 9.54  ? 792  MET A O   1 
ATOM   6325 C  CB  . MET A 1 792  ? 27.921 72.794  -20.382 1.00 9.05  ? 792  MET A CB  1 
ATOM   6326 C  CG  . MET A 1 792  ? 28.192 72.601  -21.893 1.00 10.02 ? 792  MET A CG  1 
ATOM   6327 S  SD  . MET A 1 792  ? 29.948 72.719  -22.254 1.00 10.01 ? 792  MET A SD  1 
ATOM   6328 C  CE  . MET A 1 792  ? 30.544 71.200  -21.464 1.00 11.64 ? 792  MET A CE  1 
ATOM   6329 N  N   . ARG A 1 793  ? 24.798 71.609  -21.479 1.00 9.16  ? 793  ARG A N   1 
ATOM   6330 C  CA  . ARG A 1 793  ? 24.090 70.439  -22.002 1.00 9.28  ? 793  ARG A CA  1 
ATOM   6331 C  C   . ARG A 1 793  ? 24.388 70.234  -23.469 1.00 9.33  ? 793  ARG A C   1 
ATOM   6332 O  O   . ARG A 1 793  ? 24.619 71.200  -24.230 1.00 10.20 ? 793  ARG A O   1 
ATOM   6333 C  CB  . ARG A 1 793  ? 22.581 70.678  -21.797 1.00 9.84  ? 793  ARG A CB  1 
ATOM   6334 C  CG  . ARG A 1 793  ? 21.750 69.441  -22.236 1.00 9.81  ? 793  ARG A CG  1 
ATOM   6335 C  CD  . ARG A 1 793  ? 20.250 69.690  -21.965 1.00 10.19 ? 793  ARG A CD  1 
ATOM   6336 N  NE  . ARG A 1 793  ? 19.985 69.723  -20.536 1.00 10.78 ? 793  ARG A NE  1 
ATOM   6337 C  CZ  . ARG A 1 793  ? 18.929 70.297  -19.974 1.00 10.66 ? 793  ARG A CZ  1 
ATOM   6338 N  NH1 . ARG A 1 793  ? 17.995 70.912  -20.758 1.00 11.97 ? 793  ARG A NH1 1 
ATOM   6339 N  NH2 . ARG A 1 793  ? 18.836 70.354  -18.653 1.00 12.14 ? 793  ARG A NH2 1 
ATOM   6340 N  N   . LEU A 1 794  ? 24.427 68.977  -23.877 1.00 9.36  ? 794  LEU A N   1 
ATOM   6341 C  CA  . LEU A 1 794  ? 24.580 68.531  -25.245 1.00 9.78  ? 794  LEU A CA  1 
ATOM   6342 C  C   . LEU A 1 794  ? 23.242 67.845  -25.608 1.00 10.37 ? 794  LEU A C   1 
ATOM   6343 O  O   . LEU A 1 794  ? 22.758 66.980  -24.883 1.00 10.74 ? 794  LEU A O   1 
ATOM   6344 C  CB  . LEU A 1 794  ? 25.720 67.534  -25.373 1.00 12.09 ? 794  LEU A CB  1 
ATOM   6345 C  CG  . LEU A 1 794  ? 27.075 68.202  -25.478 1.00 10.84 ? 794  LEU A CG  1 
ATOM   6346 C  CD1 . LEU A 1 794  ? 28.171 67.191  -25.102 1.00 12.75 ? 794  LEU A CD1 1 
ATOM   6347 C  CD2 . LEU A 1 794  ? 27.270 68.631  -26.948 1.00 14.44 ? 794  LEU A CD2 1 
ATOM   6348 N  N   . GLU A 1 795  ? 22.644 68.271  -26.723 1.00 10.48 ? 795  GLU A N   1 
ATOM   6349 C  CA  . GLU A 1 795  ? 21.392 67.663  -27.217 1.00 11.91 ? 795  GLU A CA  1 
ATOM   6350 C  C   . GLU A 1 795  ? 21.686 66.961  -28.520 1.00 11.78 ? 795  GLU A C   1 
ATOM   6351 O  O   . GLU A 1 795  ? 22.210 67.542  -29.451 1.00 13.25 ? 795  GLU A O   1 
ATOM   6352 C  CB  . GLU A 1 795  ? 20.312 68.736  -27.447 1.00 13.32 ? 795  GLU A CB  1 
ATOM   6353 C  CG  . GLU A 1 795  ? 19.921 69.452  -26.170 1.00 17.20 ? 795  GLU A CG  1 
ATOM   6354 C  CD  . GLU A 1 795  ? 19.015 70.693  -26.387 1.00 17.79 ? 795  GLU A CD  1 
ATOM   6355 O  OE1 . GLU A 1 795  ? 19.009 71.236  -27.517 1.00 21.90 ? 795  GLU A OE1 1 
ATOM   6356 O  OE2 . GLU A 1 795  ? 18.343 71.144  -25.430 1.00 18.80 ? 795  GLU A OE2 1 
ATOM   6357 N  N   . THR A 1 796  ? 21.310 65.687  -28.616 1.00 11.77 ? 796  THR A N   1 
ATOM   6358 C  CA  . THR A 1 796  ? 21.528 64.920  -29.783 1.00 11.83 ? 796  THR A CA  1 
ATOM   6359 C  C   . THR A 1 796  ? 20.282 64.078  -30.087 1.00 12.44 ? 796  THR A C   1 
ATOM   6360 O  O   . THR A 1 796  ? 19.305 64.105  -29.305 1.00 14.61 ? 796  THR A O   1 
ATOM   6361 C  CB  . THR A 1 796  ? 22.690 63.896  -29.662 1.00 12.03 ? 796  THR A CB  1 
ATOM   6362 O  OG1 . THR A 1 796  ? 22.273 62.749  -28.878 1.00 11.11 ? 796  THR A OG1 1 
ATOM   6363 C  CG2 . THR A 1 796  ? 23.925 64.541  -28.938 1.00 12.38 ? 796  THR A CG2 1 
ATOM   6364 N  N   . HIS A 1 797  ? 20.348 63.345  -31.189 1.00 13.40 ? 797  HIS A N   1 
ATOM   6365 C  CA  . HIS A 1 797  ? 19.230 62.458  -31.523 1.00 14.09 ? 797  HIS A CA  1 
ATOM   6366 C  C   A HIS A 1 797  ? 19.690 60.971  -31.390 0.50 14.75 ? 797  HIS A C   1 
ATOM   6367 C  C   B HIS A 1 797  ? 19.537 61.024  -31.167 0.50 14.31 ? 797  HIS A C   1 
ATOM   6368 O  O   A HIS A 1 797  ? 19.198 60.041  -32.039 0.50 14.78 ? 797  HIS A O   1 
ATOM   6369 O  O   B HIS A 1 797  ? 18.615 60.227  -31.365 0.50 11.81 ? 797  HIS A O   1 
ATOM   6370 C  CB  A HIS A 1 797  ? 18.637 62.856  -32.897 0.50 13.48 ? 797  HIS A CB  1 
ATOM   6371 C  CB  B HIS A 1 797  ? 19.331 62.376  -33.132 0.50 14.17 ? 797  HIS A CB  1 
ATOM   6372 C  CG  A HIS A 1 797  ? 18.046 64.242  -32.924 0.50 12.69 ? 797  HIS A CG  1 
ATOM   6373 C  CG  B HIS A 1 797  ? 18.551 63.499  -33.697 0.50 12.96 ? 797  HIS A CG  1 
ATOM   6374 N  ND1 A HIS A 1 797  ? 17.720 64.907  -34.093 0.50 12.68 ? 797  HIS A ND1 1 
ATOM   6375 N  ND1 B HIS A 1 797  ? 18.680 63.924  -34.996 0.50 14.17 ? 797  HIS A ND1 1 
ATOM   6376 C  CD2 A HIS A 1 797  ? 17.753 65.097  -31.916 0.50 12.77 ? 797  HIS A CD2 1 
ATOM   6377 C  CD2 B HIS A 1 797  ? 17.704 64.360  -33.094 0.50 14.51 ? 797  HIS A CD2 1 
ATOM   6378 C  CE1 A HIS A 1 797  ? 17.253 66.107  -33.798 0.50 12.26 ? 797  HIS A CE1 1 
ATOM   6379 C  CE1 B HIS A 1 797  ? 17.946 65.006  -35.168 0.50 13.86 ? 797  HIS A CE1 1 
ATOM   6380 N  NE2 A HIS A 1 797  ? 17.263 66.250  -32.486 0.50 14.74 ? 797  HIS A NE2 1 
ATOM   6381 N  NE2 B HIS A 1 797  ? 17.346 65.294  -34.030 0.50 13.98 ? 797  HIS A NE2 1 
ATOM   6382 N  N   . ILE A 1 798  ? 20.686 60.751  -30.531 1.00 13.93 ? 798  ILE A N   1 
ATOM   6383 C  CA  . ILE A 1 798  ? 21.105 59.398  -30.156 1.00 12.79 ? 798  ILE A CA  1 
ATOM   6384 C  C   . ILE A 1 798  ? 19.990 58.827  -29.270 1.00 11.72 ? 798  ILE A C   1 
ATOM   6385 O  O   . ILE A 1 798  ? 19.469 59.469  -28.363 1.00 12.76 ? 798  ILE A O   1 
ATOM   6386 C  CB  . ILE A 1 798  ? 22.445 59.434  -29.407 1.00 11.76 ? 798  ILE A CB  1 
ATOM   6387 C  CG1 . ILE A 1 798  ? 23.558 59.915  -30.323 1.00 13.02 ? 798  ILE A CG1 1 
ATOM   6388 C  CG2 . ILE A 1 798  ? 22.772 58.042  -28.861 1.00 14.05 ? 798  ILE A CG2 1 
ATOM   6389 C  CD1 . ILE A 1 798  ? 24.942 60.207  -29.609 1.00 13.66 ? 798  ILE A CD1 1 
ATOM   6390 N  N   . ASP A 1 799  ? 19.572 57.586  -29.630 1.00 13.49 ? 799  ASP A N   1 
ATOM   6391 C  CA  . ASP A 1 799  ? 18.476 56.927  -28.975 1.00 12.35 ? 799  ASP A CA  1 
ATOM   6392 C  C   . ASP A 1 799  ? 18.988 56.140  -27.789 1.00 12.07 ? 799  ASP A C   1 
ATOM   6393 O  O   . ASP A 1 799  ? 18.946 54.934  -27.730 1.00 11.34 ? 799  ASP A O   1 
ATOM   6394 C  CB  . ASP A 1 799  ? 17.731 55.976  -29.961 1.00 15.79 ? 799  ASP A CB  1 
ATOM   6395 C  CG  . ASP A 1 799  ? 16.388 55.495  -29.399 1.00 16.52 ? 799  ASP A CG  1 
ATOM   6396 O  OD1 . ASP A 1 799  ? 15.908 55.952  -28.334 1.00 21.64 ? 799  ASP A OD1 1 
ATOM   6397 O  OD2 . ASP A 1 799  ? 15.839 54.563  -30.000 1.00 23.25 ? 799  ASP A OD2 1 
ATOM   6398 N  N   . SER A 1 800  ? 19.410 56.914  -26.798 1.00 11.17 ? 800  SER A N   1 
ATOM   6399 C  CA  . SER A 1 800  ? 19.978 56.327  -25.597 1.00 10.72 ? 800  SER A CA  1 
ATOM   6400 C  C   . SER A 1 800  ? 18.928 55.945  -24.574 1.00 10.54 ? 800  SER A C   1 
ATOM   6401 O  O   . SER A 1 800  ? 19.213 55.166  -23.663 1.00 11.29 ? 800  SER A O   1 
ATOM   6402 C  CB  . SER A 1 800  ? 21.005 57.331  -24.980 1.00 11.01 ? 800  SER A CB  1 
ATOM   6403 O  OG  . SER A 1 800  ? 20.356 58.530  -24.628 1.00 11.17 ? 800  SER A OG  1 
ATOM   6404 N  N   . GLY A 1 801  ? 17.697 56.448  -24.689 1.00 10.85 ? 801  GLY A N   1 
ATOM   6405 C  CA  . GLY A 1 801  ? 16.678 56.074  -23.744 1.00 11.69 ? 801  GLY A CA  1 
ATOM   6406 C  C   . GLY A 1 801  ? 16.931 56.612  -22.382 1.00 12.19 ? 801  GLY A C   1 
ATOM   6407 O  O   . GLY A 1 801  ? 16.956 57.811  -22.193 1.00 13.65 ? 801  GLY A O   1 
ATOM   6408 N  N   . ASP A 1 802  ? 17.070 55.715  -21.418 1.00 11.59 ? 802  ASP A N   1 
ATOM   6409 C  CA  . ASP A 1 802  ? 17.341 56.083  -20.038 1.00 11.47 ? 802  ASP A CA  1 
ATOM   6410 C  C   . ASP A 1 802  ? 18.716 55.648  -19.587 1.00 10.59 ? 802  ASP A C   1 
ATOM   6411 O  O   . ASP A 1 802  ? 18.990 55.674  -18.373 1.00 11.41 ? 802  ASP A O   1 
ATOM   6412 C  CB  . ASP A 1 802  ? 16.276 55.494  -19.083 1.00 12.43 ? 802  ASP A CB  1 
ATOM   6413 C  CG  . ASP A 1 802  ? 16.110 53.979  -19.199 1.00 12.87 ? 802  ASP A CG  1 
ATOM   6414 O  OD1 . ASP A 1 802  ? 16.907 53.275  -19.884 1.00 15.88 ? 802  ASP A OD1 1 
ATOM   6415 O  OD2 . ASP A 1 802  ? 15.126 53.506  -18.552 1.00 16.13 ? 802  ASP A OD2 1 
ATOM   6416 N  N   . ILE A 1 803  ? 19.536 55.243  -20.520 1.00 8.87  ? 803  ILE A N   1 
ATOM   6417 C  CA  . ILE A 1 803  ? 20.887 54.770  -20.192 1.00 9.46  ? 803  ILE A CA  1 
ATOM   6418 C  C   . ILE A 1 803  ? 21.981 55.753  -20.501 1.00 9.14  ? 803  ILE A C   1 
ATOM   6419 O  O   . ILE A 1 803  ? 21.933 56.439  -21.531 1.00 9.46  ? 803  ILE A O   1 
ATOM   6420 C  CB  . ILE A 1 803  ? 21.213 53.467  -20.983 1.00 9.37  ? 803  ILE A CB  1 
ATOM   6421 C  CG1 . ILE A 1 803  ? 20.156 52.358  -20.645 1.00 10.80 ? 803  ILE A CG1 1 
ATOM   6422 C  CG2 . ILE A 1 803  ? 22.653 52.973  -20.709 1.00 9.75  ? 803  ILE A CG2 1 
ATOM   6423 C  CD1 . ILE A 1 803  ? 20.069 52.028  -19.149 1.00 12.81 ? 803  ILE A CD1 1 
ATOM   6424 N  N   . PHE A 1 804  ? 22.980 55.831  -19.595 1.00 9.13  ? 804  PHE A N   1 
ATOM   6425 C  CA  . PHE A 1 804  ? 24.169 56.647  -19.860 1.00 7.74  ? 804  PHE A CA  1 
ATOM   6426 C  C   . PHE A 1 804  ? 25.274 56.033  -19.030 1.00 8.33  ? 804  PHE A C   1 
ATOM   6427 O  O   . PHE A 1 804  ? 25.032 55.159  -18.213 1.00 9.29  ? 804  PHE A O   1 
ATOM   6428 C  CB  . PHE A 1 804  ? 23.965 58.162  -19.541 1.00 8.40  ? 804  PHE A CB  1 
ATOM   6429 C  CG  . PHE A 1 804  ? 23.544 58.480  -18.163 1.00 7.37  ? 804  PHE A CG  1 
ATOM   6430 C  CD1 . PHE A 1 804  ? 22.252 58.266  -17.707 1.00 8.89  ? 804  PHE A CD1 1 
ATOM   6431 C  CD2 . PHE A 1 804  ? 24.460 59.098  -17.287 1.00 8.12  ? 804  PHE A CD2 1 
ATOM   6432 C  CE1 . PHE A 1 804  ? 21.849 58.653  -16.411 1.00 8.28  ? 804  PHE A CE1 1 
ATOM   6433 C  CE2 . PHE A 1 804  ? 24.096 59.503  -16.004 1.00 8.52  ? 804  PHE A CE2 1 
ATOM   6434 C  CZ  . PHE A 1 804  ? 22.797 59.297  -15.536 1.00 8.24  ? 804  PHE A CZ  1 
ATOM   6435 N  N   . TYR A 1 805  ? 26.487 56.491  -19.265 1.00 7.85  ? 805  TYR A N   1 
ATOM   6436 C  CA  . TYR A 1 805  ? 27.674 55.937  -18.601 1.00 8.61  ? 805  TYR A CA  1 
ATOM   6437 C  C   . TYR A 1 805  ? 28.490 57.045  -18.053 1.00 7.94  ? 805  TYR A C   1 
ATOM   6438 O  O   . TYR A 1 805  ? 28.665 58.077  -18.707 1.00 8.22  ? 805  TYR A O   1 
ATOM   6439 C  CB  . TYR A 1 805  ? 28.520 55.129  -19.625 1.00 8.36  ? 805  TYR A CB  1 
ATOM   6440 C  CG  . TYR A 1 805  ? 27.814 53.901  -20.160 1.00 7.95  ? 805  TYR A CG  1 
ATOM   6441 C  CD1 . TYR A 1 805  ? 26.871 54.023  -21.148 1.00 9.19  ? 805  TYR A CD1 1 
ATOM   6442 C  CD2 . TYR A 1 805  ? 28.109 52.655  -19.642 1.00 9.10  ? 805  TYR A CD2 1 
ATOM   6443 C  CE1 . TYR A 1 805  ? 26.216 52.891  -21.600 1.00 9.89  ? 805  TYR A CE1 1 
ATOM   6444 C  CE2 . TYR A 1 805  ? 27.451 51.479  -20.118 1.00 9.65  ? 805  TYR A CE2 1 
ATOM   6445 C  CZ  . TYR A 1 805  ? 26.515 51.665  -21.101 1.00 9.62  ? 805  TYR A CZ  1 
ATOM   6446 O  OH  . TYR A 1 805  ? 25.906 50.532  -21.655 1.00 11.08 ? 805  TYR A OH  1 
ATOM   6447 N  N   . THR A 1 806  ? 28.998 56.828  -16.832 1.00 7.77  ? 806  THR A N   1 
ATOM   6448 C  CA  . THR A 1 806  ? 29.888 57.846  -16.193 1.00 7.00  ? 806  THR A CA  1 
ATOM   6449 C  C   . THR A 1 806  ? 31.047 57.058  -15.593 1.00 8.01  ? 806  THR A C   1 
ATOM   6450 O  O   . THR A 1 806  ? 30.948 55.828  -15.349 1.00 7.86  ? 806  THR A O   1 
ATOM   6451 C  CB  . THR A 1 806  ? 29.156 58.630  -15.087 1.00 7.17  ? 806  THR A CB  1 
ATOM   6452 O  OG1 . THR A 1 806  ? 28.772 57.731  -14.041 1.00 8.04  ? 806  THR A OG1 1 
ATOM   6453 C  CG2 . THR A 1 806  ? 27.868 59.300  -15.614 1.00 7.97  ? 806  THR A CG2 1 
ATOM   6454 N  N   . ASP A 1 807  ? 32.159 57.721  -15.369 1.00 6.91  ? 807  ASP A N   1 
ATOM   6455 C  CA  . ASP A 1 807  ? 33.289 56.986  -14.794 1.00 8.06  ? 807  ASP A CA  1 
ATOM   6456 C  C   . ASP A 1 807  ? 33.379 57.100  -13.275 1.00 6.25  ? 807  ASP A C   1 
ATOM   6457 O  O   . ASP A 1 807  ? 32.710 57.928  -12.637 1.00 7.00  ? 807  ASP A O   1 
ATOM   6458 C  CB  . ASP A 1 807  ? 34.616 57.437  -15.432 1.00 9.13  ? 807  ASP A CB  1 
ATOM   6459 C  CG  . ASP A 1 807  ? 35.054 58.776  -14.952 1.00 8.27  ? 807  ASP A CG  1 
ATOM   6460 O  OD1 . ASP A 1 807  ? 34.315 59.770  -15.033 1.00 9.00  ? 807  ASP A OD1 1 
ATOM   6461 O  OD2 . ASP A 1 807  ? 36.207 58.856  -14.436 1.00 9.78  ? 807  ASP A OD2 1 
ATOM   6462 N  N   . LEU A 1 808  ? 34.120 56.141  -12.755 1.00 6.80  ? 808  LEU A N   1 
ATOM   6463 C  CA  . LEU A 1 808  ? 34.405 56.110  -11.316 1.00 6.16  ? 808  LEU A CA  1 
ATOM   6464 C  C   . LEU A 1 808  ? 35.902 56.325  -11.156 1.00 5.49  ? 808  LEU A C   1 
ATOM   6465 O  O   . LEU A 1 808  ? 36.722 55.524  -11.607 1.00 6.66  ? 808  LEU A O   1 
ATOM   6466 C  CB  . LEU A 1 808  ? 33.981 54.792  -10.666 1.00 7.54  ? 808  LEU A CB  1 
ATOM   6467 C  CG  . LEU A 1 808  ? 32.442 54.679  -10.621 1.00 7.67  ? 808  LEU A CG  1 
ATOM   6468 C  CD1 . LEU A 1 808  ? 32.076 53.191  -10.388 1.00 9.14  ? 808  LEU A CD1 1 
ATOM   6469 C  CD2 . LEU A 1 808  ? 31.920 55.485  -9.433  1.00 10.24 ? 808  LEU A CD2 1 
ATOM   6470 N  N   . ASN A 1 809  ? 36.246 57.502  -10.587 1.00 6.01  ? 809  ASN A N   1 
ATOM   6471 C  CA  . ASN A 1 809  ? 37.646 57.853  -10.262 1.00 5.86  ? 809  ASN A CA  1 
ATOM   6472 C  C   . ASN A 1 809  ? 38.625 57.754  -11.404 1.00 6.05  ? 809  ASN A C   1 
ATOM   6473 O  O   . ASN A 1 809  ? 39.798 57.482  -11.216 1.00 6.74  ? 809  ASN A O   1 
ATOM   6474 C  CB  . ASN A 1 809  ? 38.137 56.958  -9.087  1.00 5.91  ? 809  ASN A CB  1 
ATOM   6475 C  CG  . ASN A 1 809  ? 37.087 56.856  -8.003  1.00 6.01  ? 809  ASN A CG  1 
ATOM   6476 O  OD1 . ASN A 1 809  ? 36.232 55.938  -8.015  1.00 6.55  ? 809  ASN A OD1 1 
ATOM   6477 N  ND2 . ASN A 1 809  ? 37.110 57.809  -7.070  1.00 7.04  ? 809  ASN A ND2 1 
ATOM   6478 N  N   . GLY A 1 810  ? 38.141 57.964  -12.636 1.00 6.14  ? 810  GLY A N   1 
ATOM   6479 C  CA  . GLY A 1 810  ? 39.064 57.880  -13.793 1.00 7.43  ? 810  GLY A CA  1 
ATOM   6480 C  C   . GLY A 1 810  ? 39.553 56.452  -14.071 1.00 8.23  ? 810  GLY A C   1 
ATOM   6481 O  O   . GLY A 1 810  ? 40.490 56.282  -14.869 1.00 9.52  ? 810  GLY A O   1 
ATOM   6482 N  N   . LEU A 1 811  ? 38.925 55.449  -13.443 1.00 6.89  ? 811  LEU A N   1 
ATOM   6483 C  CA  . LEU A 1 811  ? 39.372 54.059  -13.527 1.00 8.06  ? 811  LEU A CA  1 
ATOM   6484 C  C   . LEU A 1 811  ? 38.489 53.164  -14.377 1.00 8.86  ? 811  LEU A C   1 
ATOM   6485 O  O   . LEU A 1 811  ? 38.995 52.282  -15.083 1.00 10.43 ? 811  LEU A O   1 
ATOM   6486 C  CB  . LEU A 1 811  ? 39.439 53.479  -12.092 1.00 8.88  ? 811  LEU A CB  1 
ATOM   6487 C  CG  . LEU A 1 811  ? 39.839 51.999  -11.987 1.00 9.98  ? 811  LEU A CG  1 
ATOM   6488 C  CD1 . LEU A 1 811  ? 41.276 51.831  -12.473 1.00 11.29 ? 811  LEU A CD1 1 
ATOM   6489 C  CD2 . LEU A 1 811  ? 39.709 51.545  -10.537 1.00 10.56 ? 811  LEU A CD2 1 
ATOM   6490 N  N   . GLN A 1 812  ? 37.182 53.394  -14.327 1.00 7.29  ? 812  GLN A N   1 
ATOM   6491 C  CA  . GLN A 1 812  ? 36.249 52.479  -14.992 1.00 7.48  ? 812  GLN A CA  1 
ATOM   6492 C  C   . GLN A 1 812  ? 34.957 53.213  -15.330 1.00 7.59  ? 812  GLN A C   1 
ATOM   6493 O  O   . GLN A 1 812  ? 34.636 54.231  -14.668 1.00 8.87  ? 812  GLN A O   1 
ATOM   6494 C  CB  . GLN A 1 812  ? 35.915 51.310  -14.041 1.00 8.98  ? 812  GLN A CB  1 
ATOM   6495 C  CG  . GLN A 1 812  ? 35.295 51.815  -12.728 1.00 11.03 ? 812  GLN A CG  1 
ATOM   6496 C  CD  . GLN A 1 812  ? 35.022 50.687  -11.735 1.00 11.92 ? 812  GLN A CD  1 
ATOM   6497 O  OE1 . GLN A 1 812  ? 34.058 49.931  -11.882 1.00 12.14 ? 812  GLN A OE1 1 
ATOM   6498 N  NE2 . GLN A 1 812  ? 35.824 50.617  -10.678 1.00 13.40 ? 812  GLN A NE2 1 
ATOM   6499 N  N   . PHE A 1 813  ? 34.216 52.752  -16.335 1.00 7.93  ? 813  PHE A N   1 
ATOM   6500 C  CA  . PHE A 1 813  ? 32.924 53.364  -16.657 1.00 7.49  ? 813  PHE A CA  1 
ATOM   6501 C  C   . PHE A 1 813  ? 31.809 52.440  -16.211 1.00 7.58  ? 813  PHE A C   1 
ATOM   6502 O  O   . PHE A 1 813  ? 31.828 51.195  -16.498 1.00 9.52  ? 813  PHE A O   1 
ATOM   6503 C  CB  . PHE A 1 813  ? 32.856 53.653  -18.161 1.00 7.74  ? 813  PHE A CB  1 
ATOM   6504 C  CG  . PHE A 1 813  ? 33.620 54.878  -18.558 1.00 8.19  ? 813  PHE A CG  1 
ATOM   6505 C  CD1 . PHE A 1 813  ? 35.000 54.839  -18.633 1.00 8.55  ? 813  PHE A CD1 1 
ATOM   6506 C  CD2 . PHE A 1 813  ? 32.940 56.109  -18.771 1.00 8.35  ? 813  PHE A CD2 1 
ATOM   6507 C  CE1 . PHE A 1 813  ? 35.720 56.029  -18.892 1.00 10.36 ? 813  PHE A CE1 1 
ATOM   6508 C  CE2 . PHE A 1 813  ? 33.678 57.267  -19.039 1.00 9.61  ? 813  PHE A CE2 1 
ATOM   6509 C  CZ  . PHE A 1 813  ? 35.044 57.204  -19.090 1.00 9.89  ? 813  PHE A CZ  1 
ATOM   6510 N  N   . ILE A 1 814  ? 30.840 53.017  -15.534 1.00 6.62  ? 814  ILE A N   1 
ATOM   6511 C  CA  . ILE A 1 814  ? 29.745 52.226  -15.003 1.00 8.04  ? 814  ILE A CA  1 
ATOM   6512 C  C   . ILE A 1 814  ? 28.438 52.665  -15.695 1.00 7.86  ? 814  ILE A C   1 
ATOM   6513 O  O   . ILE A 1 814  ? 28.212 53.855  -15.954 1.00 7.85  ? 814  ILE A O   1 
ATOM   6514 C  CB  . ILE A 1 814  ? 29.693 52.421  -13.448 1.00 7.65  ? 814  ILE A CB  1 
ATOM   6515 C  CG1 . ILE A 1 814  ? 28.627 51.504  -12.856 1.00 8.10  ? 814  ILE A CG1 1 
ATOM   6516 C  CG2 . ILE A 1 814  ? 29.429 53.883  -13.044 1.00 8.17  ? 814  ILE A CG2 1 
ATOM   6517 C  CD1 . ILE A 1 814  ? 28.773 51.337  -11.292 1.00 8.96  ? 814  ILE A CD1 1 
ATOM   6518 N  N   . LYS A 1 815  ? 27.597 51.670  -16.011 1.00 8.00  ? 815  LYS A N   1 
ATOM   6519 C  CA  . LYS A 1 815  ? 26.289 51.980  -16.593 1.00 8.31  ? 815  LYS A CA  1 
ATOM   6520 C  C   . LYS A 1 815  ? 25.372 52.595  -15.551 1.00 7.66  ? 815  LYS A C   1 
ATOM   6521 O  O   . LYS A 1 815  ? 25.233 52.124  -14.423 1.00 8.17  ? 815  LYS A O   1 
ATOM   6522 C  CB  . LYS A 1 815  ? 25.672 50.658  -17.118 1.00 9.34  ? 815  LYS A CB  1 
ATOM   6523 C  CG  . LYS A 1 815  ? 24.371 50.826  -17.887 1.00 10.45 ? 815  LYS A CG  1 
ATOM   6524 C  CD  . LYS A 1 815  ? 23.998 49.417  -18.442 1.00 13.49 ? 815  LYS A CD  1 
ATOM   6525 C  CE  . LYS A 1 815  ? 22.866 49.426  -19.429 1.00 17.49 ? 815  LYS A CE  1 
ATOM   6526 N  NZ  . LYS A 1 815  ? 22.541 48.007  -19.806 1.00 19.16 ? 815  LYS A NZ  1 
ATOM   6527 N  N   . ARG A 1 816  ? 24.724 53.680  -15.952 1.00 7.73  ? 816  ARG A N   1 
ATOM   6528 C  CA  . ARG A 1 816  ? 23.724 54.360  -15.183 1.00 7.82  ? 816  ARG A CA  1 
ATOM   6529 C  C   . ARG A 1 816  ? 22.349 54.252  -15.855 1.00 8.47  ? 816  ARG A C   1 
ATOM   6530 O  O   . ARG A 1 816  ? 22.284 54.205  -17.104 1.00 8.38  ? 816  ARG A O   1 
ATOM   6531 C  CB  . ARG A 1 816  ? 23.984 55.890  -15.059 1.00 8.13  ? 816  ARG A CB  1 
ATOM   6532 C  CG  . ARG A 1 816  ? 25.426 56.218  -14.546 1.00 7.87  ? 816  ARG A CG  1 
ATOM   6533 C  CD  . ARG A 1 816  ? 25.626 55.637  -13.163 1.00 8.02  ? 816  ARG A CD  1 
ATOM   6534 N  NE  . ARG A 1 816  ? 26.842 56.196  -12.538 1.00 7.36  ? 816  ARG A NE  1 
ATOM   6535 C  CZ  . ARG A 1 816  ? 27.224 55.792  -11.327 1.00 7.96  ? 816  ARG A CZ  1 
ATOM   6536 N  NH1 . ARG A 1 816  ? 26.509 54.876  -10.699 1.00 7.69  ? 816  ARG A NH1 1 
ATOM   6537 N  NH2 . ARG A 1 816  ? 28.275 56.372  -10.713 1.00 8.39  ? 816  ARG A NH2 1 
ATOM   6538 N  N   . ARG A 1 817  ? 21.297 54.196  -15.028 1.00 8.16  ? 817  ARG A N   1 
ATOM   6539 C  CA  . ARG A 1 817  ? 19.941 54.252  -15.621 1.00 8.12  ? 817  ARG A CA  1 
ATOM   6540 C  C   . ARG A 1 817  ? 19.222 55.385  -14.933 1.00 8.67  ? 817  ARG A C   1 
ATOM   6541 O  O   . ARG A 1 817  ? 19.107 55.429  -13.694 1.00 9.23  ? 817  ARG A O   1 
ATOM   6542 C  CB  . ARG A 1 817  ? 19.230 52.917  -15.386 1.00 9.61  ? 817  ARG A CB  1 
ATOM   6543 C  CG  . ARG A 1 817  ? 17.747 52.933  -15.788 1.00 10.97 ? 817  ARG A CG  1 
ATOM   6544 C  CD  . ARG A 1 817  ? 17.069 51.530  -15.654 1.00 12.20 ? 817  ARG A CD  1 
ATOM   6545 N  NE  . ARG A 1 817  ? 17.626 50.508  -16.540 1.00 12.19 ? 817  ARG A NE  1 
ATOM   6546 C  CZ  . ARG A 1 817  ? 18.398 49.510  -16.138 1.00 12.74 ? 817  ARG A CZ  1 
ATOM   6547 N  NH1 . ARG A 1 817  ? 18.726 49.386  -14.837 1.00 12.99 ? 817  ARG A NH1 1 
ATOM   6548 N  NH2 . ARG A 1 817  ? 18.843 48.621  -17.021 1.00 15.88 ? 817  ARG A NH2 1 
ATOM   6549 N  N   . ARG A 1 818  ? 18.757 56.340  -15.750 1.00 8.66  ? 818  ARG A N   1 
ATOM   6550 C  CA  . ARG A 1 818  ? 17.983 57.469  -15.251 1.00 9.46  ? 818  ARG A CA  1 
ATOM   6551 C  C   . ARG A 1 818  ? 16.669 56.885  -14.726 1.00 9.72  ? 818  ARG A C   1 
ATOM   6552 O  O   A ARG A 1 818  ? 16.009 56.133  -15.452 0.50 11.51 ? 818  ARG A O   1 
ATOM   6553 O  O   B ARG A 1 818  ? 16.124 55.930  -15.320 0.50 11.07 ? 818  ARG A O   1 
ATOM   6554 C  CB  . ARG A 1 818  ? 17.699 58.428  -16.413 1.00 9.97  ? 818  ARG A CB  1 
ATOM   6555 C  CG  A ARG A 1 818  ? 17.072 59.737  -15.963 0.50 10.07 ? 818  ARG A CG  1 
ATOM   6556 C  CG  B ARG A 1 818  ? 16.721 59.587  -15.929 0.50 11.56 ? 818  ARG A CG  1 
ATOM   6557 C  CD  . ARG A 1 818  ? 16.335 60.433  -17.105 1.00 10.03 ? 818  ARG A CD  1 
ATOM   6558 N  NE  A ARG A 1 818  ? 15.037 59.798  -17.366 0.50 10.04 ? 818  ARG A NE  1 
ATOM   6559 N  NE  B ARG A 1 818  ? 17.161 60.373  -18.192 0.50 14.85 ? 818  ARG A NE  1 
ATOM   6560 C  CZ  A ARG A 1 818  ? 14.679 59.242  -18.516 0.50 10.21 ? 818  ARG A CZ  1 
ATOM   6561 C  CZ  B ARG A 1 818  ? 16.999 59.792  -19.384 0.50 13.61 ? 818  ARG A CZ  1 
ATOM   6562 N  NH1 A ARG A 1 818  ? 15.483 59.220  -19.552 0.50 11.06 ? 818  ARG A NH1 1 
ATOM   6563 N  NH1 B ARG A 1 818  ? 15.845 59.188  -19.726 0.50 15.56 ? 818  ARG A NH1 1 
ATOM   6564 N  NH2 A ARG A 1 818  ? 13.493 58.656  -18.609 0.50 10.63 ? 818  ARG A NH2 1 
ATOM   6565 N  NH2 B ARG A 1 818  ? 18.066 59.706  -20.180 0.50 10.31 ? 818  ARG A NH2 1 
ATOM   6566 N  N   . LEU A 1 819  ? 16.306 57.241  -13.503 1.00 9.86  ? 819  LEU A N   1 
ATOM   6567 C  CA  . LEU A 1 819  ? 15.086 56.702  -12.844 1.00 11.99 ? 819  LEU A CA  1 
ATOM   6568 C  C   . LEU A 1 819  ? 14.140 57.863  -12.575 1.00 11.47 ? 819  LEU A C   1 
ATOM   6569 O  O   . LEU A 1 819  ? 14.387 58.747  -11.731 1.00 12.00 ? 819  LEU A O   1 
ATOM   6570 C  CB  . LEU A 1 819  ? 15.466 55.991  -11.527 1.00 12.58 ? 819  LEU A CB  1 
ATOM   6571 C  CG  . LEU A 1 819  ? 16.408 54.768  -11.679 1.00 12.81 ? 819  LEU A CG  1 
ATOM   6572 C  CD1 . LEU A 1 819  ? 16.816 54.262  -10.314 1.00 15.34 ? 819  LEU A CD1 1 
ATOM   6573 C  CD2 . LEU A 1 819  ? 15.745 53.698  -12.514 1.00 14.86 ? 819  LEU A CD2 1 
ATOM   6574 N  N   . ASP A 1 820  ? 13.019 57.843  -13.315 1.00 12.59 ? 820  ASP A N   1 
ATOM   6575 C  CA  . ASP A 1 820  ? 12.067 58.904  -13.120 1.00 13.86 ? 820  ASP A CA  1 
ATOM   6576 C  C   . ASP A 1 820  ? 11.348 58.780  -11.777 1.00 12.74 ? 820  ASP A C   1 
ATOM   6577 O  O   . ASP A 1 820  ? 10.722 59.738  -11.312 1.00 13.69 ? 820  ASP A O   1 
ATOM   6578 C  CB  . ASP A 1 820  ? 11.099 58.945  -14.289 1.00 16.16 ? 820  ASP A CB  1 
ATOM   6579 C  CG  . ASP A 1 820  ? 11.794 59.305  -15.600 1.00 16.99 ? 820  ASP A CG  1 
ATOM   6580 O  OD1 . ASP A 1 820  ? 12.908 59.912  -15.604 1.00 17.87 ? 820  ASP A OD1 1 
ATOM   6581 O  OD2 . ASP A 1 820  ? 11.232 58.994  -16.677 1.00 20.10 ? 820  ASP A OD2 1 
ATOM   6582 N  N   . LYS A 1 821  ? 11.470 57.627  -11.110 1.00 11.37 ? 821  LYS A N   1 
ATOM   6583 C  CA  . LYS A 1 821  ? 10.879 57.509  -9.783  1.00 12.95 ? 821  LYS A CA  1 
ATOM   6584 C  C   . LYS A 1 821  ? 11.699 58.238  -8.706  1.00 13.42 ? 821  LYS A C   1 
ATOM   6585 O  O   . LYS A 1 821  ? 11.274 58.380  -7.569  1.00 15.26 ? 821  LYS A O   1 
ATOM   6586 C  CB  . LYS A 1 821  ? 10.703 56.039  -9.364  1.00 13.19 ? 821  LYS A CB  1 
ATOM   6587 C  CG  . LYS A 1 821  ? 12.052 55.315  -9.107  1.00 12.34 ? 821  LYS A CG  1 
ATOM   6588 C  CD  . LYS A 1 821  ? 11.867 53.812  -9.083  1.00 13.38 ? 821  LYS A CD  1 
ATOM   6589 C  CE  . LYS A 1 821  ? 13.225 53.143  -8.918  1.00 12.36 ? 821  LYS A CE  1 
ATOM   6590 N  NZ  . LYS A 1 821  ? 13.197 51.688  -9.180  1.00 12.90 ? 821  LYS A NZ  1 
ATOM   6591 N  N   . LEU A 1 822  ? 12.889 58.714  -9.089  1.00 11.75 ? 822  LEU A N   1 
ATOM   6592 C  CA  . LEU A 1 822  ? 13.717 59.479  -8.146  1.00 12.29 ? 822  LEU A CA  1 
ATOM   6593 C  C   . LEU A 1 822  ? 13.743 60.922  -8.656  1.00 12.18 ? 822  LEU A C   1 
ATOM   6594 O  O   . LEU A 1 822  ? 13.571 61.162  -9.847  1.00 12.21 ? 822  LEU A O   1 
ATOM   6595 C  CB  . LEU A 1 822  ? 15.158 58.935  -8.144  1.00 13.03 ? 822  LEU A CB  1 
ATOM   6596 C  CG  . LEU A 1 822  ? 15.295 57.465  -7.683  1.00 13.62 ? 822  LEU A CG  1 
ATOM   6597 C  CD1 . LEU A 1 822  ? 16.780 57.094  -7.704  1.00 14.73 ? 822  LEU A CD1 1 
ATOM   6598 C  CD2 . LEU A 1 822  ? 14.645 57.207  -6.314  1.00 14.35 ? 822  LEU A CD2 1 
ATOM   6599 N  N   . PRO A 1 823  ? 14.008 61.881  -7.754  1.00 11.51 ? 823  PRO A N   1 
ATOM   6600 C  CA  . PRO A 1 823  ? 14.067 63.296  -8.173  1.00 11.16 ? 823  PRO A CA  1 
ATOM   6601 C  C   . PRO A 1 823  ? 15.286 63.587  -9.040  1.00 10.88 ? 823  PRO A C   1 
ATOM   6602 O  O   . PRO A 1 823  ? 16.267 62.802  -9.082  1.00 11.44 ? 823  PRO A O   1 
ATOM   6603 C  CB  . PRO A 1 823  ? 14.087 64.084  -6.868  1.00 12.75 ? 823  PRO A CB  1 
ATOM   6604 C  CG  . PRO A 1 823  ? 14.668 63.138  -5.857  1.00 13.88 ? 823  PRO A CG  1 
ATOM   6605 C  CD  . PRO A 1 823  ? 14.221 61.710  -6.310  1.00 12.19 ? 823  PRO A CD  1 
ATOM   6606 N  N   . LEU A 1 824  ? 15.220 64.703  -9.769  1.00 10.63 ? 824  LEU A N   1 
ATOM   6607 C  CA  . LEU A 1 824  ? 16.275 65.094  -10.670 1.00 9.76  ? 824  LEU A CA  1 
ATOM   6608 C  C   . LEU A 1 824  ? 17.702 64.978  -10.059 1.00 9.16  ? 824  LEU A C   1 
ATOM   6609 O  O   . LEU A 1 824  ? 18.575 64.369  -10.698 1.00 9.33  ? 824  LEU A O   1 
ATOM   6610 C  CB  . LEU A 1 824  ? 15.947 66.536  -11.162 1.00 11.13 ? 824  LEU A CB  1 
ATOM   6611 C  CG  . LEU A 1 824  ? 16.747 67.143  -12.306 1.00 10.07 ? 824  LEU A CG  1 
ATOM   6612 C  CD1 . LEU A 1 824  ? 15.980 68.426  -12.801 1.00 12.26 ? 824  LEU A CD1 1 
ATOM   6613 C  CD2 . LEU A 1 824  ? 18.250 67.546  -11.907 1.00 10.46 ? 824  LEU A CD2 1 
ATOM   6614 N  N   . GLN A 1 825  ? 17.876 65.541  -8.865  1.00 9.05  ? 825  GLN A N   1 
ATOM   6615 C  CA  . GLN A 1 825  ? 19.199 65.532  -8.227  1.00 9.10  ? 825  GLN A CA  1 
ATOM   6616 C  C   . GLN A 1 825  ? 19.698 64.124  -7.939  1.00 9.26  ? 825  GLN A C   1 
ATOM   6617 O  O   . GLN A 1 825  ? 20.948 63.950  -7.808  1.00 9.09  ? 825  GLN A O   1 
ATOM   6618 C  CB  . GLN A 1 825  ? 19.185 66.413  -6.968  1.00 9.95  ? 825  GLN A CB  1 
ATOM   6619 C  CG  . GLN A 1 825  ? 18.261 65.890  -5.842  1.00 9.63  ? 825  GLN A CG  1 
ATOM   6620 C  CD  . GLN A 1 825  ? 16.802 66.371  -5.952  1.00 9.38  ? 825  GLN A CD  1 
ATOM   6621 O  OE1 . GLN A 1 825  ? 16.351 66.828  -6.976  1.00 10.92 ? 825  GLN A OE1 1 
ATOM   6622 N  NE2 . GLN A 1 825  ? 16.105 66.263  -4.866  1.00 10.90 ? 825  GLN A NE2 1 
ATOM   6623 N  N   . ALA A 1 826  ? 18.814 63.116  -7.833  1.00 9.02  ? 826  ALA A N   1 
ATOM   6624 C  CA  . ALA A 1 826  ? 19.282 61.739  -7.588  1.00 8.23  ? 826  ALA A CA  1 
ATOM   6625 C  C   . ALA A 1 826  ? 19.863 61.154  -8.864  1.00 8.76  ? 826  ALA A C   1 
ATOM   6626 O  O   . ALA A 1 826  ? 20.619 60.182  -8.823  1.00 9.32  ? 826  ALA A O   1 
ATOM   6627 C  CB  . ALA A 1 826  ? 18.089 60.867  -7.121  1.00 9.02  ? 826  ALA A CB  1 
ATOM   6628 N  N   . ASN A 1 827  ? 19.515 61.715  -10.026 1.00 8.26  ? 827  ASN A N   1 
ATOM   6629 C  CA  . ASN A 1 827  ? 20.004 61.235  -11.331 1.00 9.11  ? 827  ASN A CA  1 
ATOM   6630 C  C   . ASN A 1 827  ? 21.314 61.880  -11.772 1.00 8.51  ? 827  ASN A C   1 
ATOM   6631 O  O   . ASN A 1 827  ? 21.839 61.607  -12.830 1.00 8.97  ? 827  ASN A O   1 
ATOM   6632 C  CB  . ASN A 1 827  ? 18.885 61.382  -12.380 1.00 9.79  ? 827  ASN A CB  1 
ATOM   6633 C  CG  . ASN A 1 827  ? 17.770 60.368  -12.140 1.00 10.75 ? 827  ASN A CG  1 
ATOM   6634 O  OD1 . ASN A 1 827  ? 18.001 59.155  -12.183 1.00 11.06 ? 827  ASN A OD1 1 
ATOM   6635 N  ND2 . ASN A 1 827  ? 16.582 60.862  -11.841 1.00 12.25 ? 827  ASN A ND2 1 
ATOM   6636 N  N   . TYR A 1 828  ? 21.801 62.741  -10.886 1.00 8.29  ? 828  TYR A N   1 
ATOM   6637 C  CA  . TYR A 1 828  ? 23.147 63.361  -11.053 1.00 7.77  ? 828  TYR A CA  1 
ATOM   6638 C  C   . TYR A 1 828  ? 24.174 62.424  -10.421 1.00 7.04  ? 828  TYR A C   1 
ATOM   6639 O  O   . TYR A 1 828  ? 23.951 61.901  -9.330  1.00 8.30  ? 828  TYR A O   1 
ATOM   6640 C  CB  . TYR A 1 828  ? 23.195 64.738  -10.348 1.00 8.80  ? 828  TYR A CB  1 
ATOM   6641 C  CG  . TYR A 1 828  ? 23.227 65.883  -11.328 1.00 7.54  ? 828  TYR A CG  1 
ATOM   6642 C  CD1 . TYR A 1 828  ? 22.187 66.084  -12.248 1.00 8.71  ? 828  TYR A CD1 1 
ATOM   6643 C  CD2 . TYR A 1 828  ? 24.316 66.739  -11.392 1.00 8.92  ? 828  TYR A CD2 1 
ATOM   6644 C  CE1 . TYR A 1 828  ? 22.241 67.094  -13.208 1.00 9.32  ? 828  TYR A CE1 1 
ATOM   6645 C  CE2 . TYR A 1 828  ? 24.368 67.725  -12.353 1.00 9.81  ? 828  TYR A CE2 1 
ATOM   6646 C  CZ  . TYR A 1 828  ? 23.341 67.896  -13.248 1.00 8.41  ? 828  TYR A CZ  1 
ATOM   6647 O  OH  . TYR A 1 828  ? 23.466 68.917  -14.184 1.00 9.94  ? 828  TYR A OH  1 
ATOM   6648 N  N   . TYR A 1 829  ? 25.274 62.252  -11.151 1.00 7.29  ? 829  TYR A N   1 
ATOM   6649 C  CA  . TYR A 1 829  ? 26.369 61.375  -10.749 1.00 7.87  ? 829  TYR A CA  1 
ATOM   6650 C  C   . TYR A 1 829  ? 27.696 62.078  -10.898 1.00 8.45  ? 829  TYR A C   1 
ATOM   6651 O  O   . TYR A 1 829  ? 27.792 63.089  -11.558 1.00 8.16  ? 829  TYR A O   1 
ATOM   6652 C  CB  . TYR A 1 829  ? 26.403 60.125  -11.647 1.00 7.92  ? 829  TYR A CB  1 
ATOM   6653 C  CG  . TYR A 1 829  ? 25.262 59.204  -11.356 1.00 7.71  ? 829  TYR A CG  1 
ATOM   6654 C  CD1 . TYR A 1 829  ? 25.321 58.310  -10.297 1.00 7.45  ? 829  TYR A CD1 1 
ATOM   6655 C  CD2 . TYR A 1 829  ? 24.078 59.261  -12.119 1.00 7.94  ? 829  TYR A CD2 1 
ATOM   6656 C  CE1 . TYR A 1 829  ? 24.202 57.485  -9.961  1.00 7.92  ? 829  TYR A CE1 1 
ATOM   6657 C  CE2 . TYR A 1 829  ? 22.998 58.428  -11.814 1.00 9.10  ? 829  TYR A CE2 1 
ATOM   6658 C  CZ  . TYR A 1 829  ? 23.072 57.556  -10.735 1.00 8.29  ? 829  TYR A CZ  1 
ATOM   6659 O  OH  . TYR A 1 829  ? 22.016 56.731  -10.419 1.00 9.38  ? 829  TYR A OH  1 
ATOM   6660 N  N   . PRO A 1 830  ? 28.729 61.586  -10.211 1.00 8.09  ? 830  PRO A N   1 
ATOM   6661 C  CA  . PRO A 1 830  ? 30.040 62.223  -10.381 1.00 7.50  ? 830  PRO A CA  1 
ATOM   6662 C  C   . PRO A 1 830  ? 30.507 61.997  -11.833 1.00 7.18  ? 830  PRO A C   1 
ATOM   6663 O  O   . PRO A 1 830  ? 30.300 60.906  -12.393 1.00 7.61  ? 830  PRO A O   1 
ATOM   6664 C  CB  . PRO A 1 830  ? 30.951 61.398  -9.439  1.00 10.98 ? 830  PRO A CB  1 
ATOM   6665 C  CG  . PRO A 1 830  ? 30.039 60.663  -8.508  1.00 9.77  ? 830  PRO A CG  1 
ATOM   6666 C  CD  . PRO A 1 830  ? 28.723 60.478  -9.235  1.00 7.80  ? 830  PRO A CD  1 
ATOM   6667 N  N   . ILE A 1 831  ? 31.114 63.002  -12.463 1.00 7.00  ? 831  ILE A N   1 
ATOM   6668 C  CA  . ILE A 1 831  ? 31.768 62.847  -13.764 1.00 7.40  ? 831  ILE A CA  1 
ATOM   6669 C  C   . ILE A 1 831  ? 33.252 63.155  -13.475 1.00 7.45  ? 831  ILE A C   1 
ATOM   6670 O  O   . ILE A 1 831  ? 33.791 64.241  -13.801 1.00 7.65  ? 831  ILE A O   1 
ATOM   6671 C  CB  . ILE A 1 831  ? 31.204 63.837  -14.823 1.00 6.79  ? 831  ILE A CB  1 
ATOM   6672 C  CG1 . ILE A 1 831  ? 29.673 63.873  -14.832 1.00 7.95  ? 831  ILE A CG1 1 
ATOM   6673 C  CG2 . ILE A 1 831  ? 31.709 63.394  -16.218 1.00 8.10  ? 831  ILE A CG2 1 
ATOM   6674 C  CD1 . ILE A 1 831  ? 28.961 62.576  -15.162 1.00 8.31  ? 831  ILE A CD1 1 
ATOM   6675 N  N   . PRO A 1 832  ? 33.978 62.194  -12.894 1.00 6.92  ? 832  PRO A N   1 
ATOM   6676 C  CA  . PRO A 1 832  ? 35.390 62.508  -12.579 1.00 7.26  ? 832  PRO A CA  1 
ATOM   6677 C  C   . PRO A 1 832  ? 36.288 62.615  -13.772 1.00 8.01  ? 832  PRO A C   1 
ATOM   6678 O  O   . PRO A 1 832  ? 37.242 63.380  -13.674 1.00 9.70  ? 832  PRO A O   1 
ATOM   6679 C  CB  . PRO A 1 832  ? 35.786 61.427  -11.544 1.00 7.25  ? 832  PRO A CB  1 
ATOM   6680 C  CG  . PRO A 1 832  ? 34.788 60.333  -11.775 1.00 8.40  ? 832  PRO A CG  1 
ATOM   6681 C  CD  . PRO A 1 832  ? 33.500 61.012  -12.160 1.00 7.62  ? 832  PRO A CD  1 
ATOM   6682 N  N   . SER A 1 833  ? 35.968 61.965  -14.890 1.00 7.15  ? 833  SER A N   1 
ATOM   6683 C  CA  . SER A 1 833  ? 36.787 62.113  -16.069 1.00 7.39  ? 833  SER A CA  1 
ATOM   6684 C  C   . SER A 1 833  ? 36.013 61.924  -17.387 1.00 7.28  ? 833  SER A C   1 
ATOM   6685 O  O   . SER A 1 833  ? 36.549 62.262  -18.444 1.00 6.87  ? 833  SER A O   1 
ATOM   6686 C  CB  . SER A 1 833  ? 38.006 61.178  -16.048 1.00 8.93  ? 833  SER A CB  1 
ATOM   6687 O  OG  . SER A 1 833  ? 37.721 59.864  -16.326 1.00 10.49 ? 833  SER A OG  1 
ATOM   6688 N  N   . GLY A 1 834  ? 34.791 61.376  -17.329 1.00 7.01  ? 834  GLY A N   1 
ATOM   6689 C  CA  . GLY A 1 834  ? 34.088 61.272  -18.630 1.00 7.37  ? 834  GLY A CA  1 
ATOM   6690 C  C   . GLY A 1 834  ? 32.725 60.668  -18.498 1.00 6.61  ? 834  GLY A C   1 
ATOM   6691 O  O   . GLY A 1 834  ? 32.341 60.090  -17.485 1.00 7.28  ? 834  GLY A O   1 
ATOM   6692 N  N   . MET A 1 835  ? 31.948 60.835  -19.560 1.00 6.97  ? 835  MET A N   1 
ATOM   6693 C  CA  . MET A 1 835  ? 30.575 60.288  -19.598 1.00 7.70  ? 835  MET A CA  1 
ATOM   6694 C  C   . MET A 1 835  ? 30.220 60.066  -21.057 1.00 7.60  ? 835  MET A C   1 
ATOM   6695 O  O   . MET A 1 835  ? 30.813 60.701  -21.960 1.00 8.48  ? 835  MET A O   1 
ATOM   6696 C  CB  . MET A 1 835  ? 29.593 61.287  -18.986 1.00 8.05  ? 835  MET A CB  1 
ATOM   6697 C  CG  . MET A 1 835  ? 29.479 62.627  -19.752 1.00 9.64  ? 835  MET A CG  1 
ATOM   6698 S  SD  . MET A 1 835  ? 28.620 63.916  -18.847 1.00 11.05 ? 835  MET A SD  1 
ATOM   6699 C  CE  . MET A 1 835  ? 27.175 63.179  -18.390 1.00 12.41 ? 835  MET A CE  1 
ATOM   6700 N  N   . PHE A 1 836  ? 29.285 59.147  -21.297 1.00 7.08  ? 836  PHE A N   1 
ATOM   6701 C  CA  . PHE A 1 836  ? 28.858 58.930  -22.694 1.00 8.06  ? 836  PHE A CA  1 
ATOM   6702 C  C   . PHE A 1 836  ? 27.466 58.367  -22.761 1.00 8.30  ? 836  PHE A C   1 
ATOM   6703 O  O   . PHE A 1 836  ? 26.908 57.835  -21.788 1.00 8.17  ? 836  PHE A O   1 
ATOM   6704 C  CB  . PHE A 1 836  ? 29.882 58.071  -23.488 1.00 8.61  ? 836  PHE A CB  1 
ATOM   6705 C  CG  . PHE A 1 836  ? 30.052 56.612  -23.039 1.00 9.00  ? 836  PHE A CG  1 
ATOM   6706 C  CD1 . PHE A 1 836  ? 29.170 55.627  -23.503 1.00 9.39  ? 836  PHE A CD1 1 
ATOM   6707 C  CD2 . PHE A 1 836  ? 31.138 56.239  -22.245 1.00 8.45  ? 836  PHE A CD2 1 
ATOM   6708 C  CE1 . PHE A 1 836  ? 29.392 54.278  -23.172 1.00 10.22 ? 836  PHE A CE1 1 
ATOM   6709 C  CE2 . PHE A 1 836  ? 31.360 54.893  -21.933 1.00 9.87  ? 836  PHE A CE2 1 
ATOM   6710 C  CZ  . PHE A 1 836  ? 30.499 53.911  -22.399 1.00 9.66  ? 836  PHE A CZ  1 
ATOM   6711 N  N   . ILE A 1 837  ? 26.880 58.592  -23.956 1.00 8.64  ? 837  ILE A N   1 
ATOM   6712 C  CA  . ILE A 1 837  ? 25.559 57.994  -24.295 1.00 9.61  ? 837  ILE A CA  1 
ATOM   6713 C  C   . ILE A 1 837  ? 25.738 57.325  -25.635 1.00 9.13  ? 837  ILE A C   1 
ATOM   6714 O  O   . ILE A 1 837  ? 26.578 57.708  -26.431 1.00 9.22  ? 837  ILE A O   1 
ATOM   6715 C  CB  . ILE A 1 837  ? 24.389 59.024  -24.399 1.00 10.41 ? 837  ILE A CB  1 
ATOM   6716 C  CG1 . ILE A 1 837  ? 24.847 60.253  -25.211 1.00 9.65  ? 837  ILE A CG1 1 
ATOM   6717 C  CG2 . ILE A 1 837  ? 23.862 59.337  -23.045 1.00 11.02 ? 837  ILE A CG2 1 
ATOM   6718 C  CD1 . ILE A 1 837  ? 23.601 61.108  -25.662 1.00 11.73 ? 837  ILE A CD1 1 
ATOM   6719 N  N   . GLU A 1 838  ? 24.944 56.284  -25.861 1.00 9.74  ? 838  GLU A N   1 
ATOM   6720 C  CA  . GLU A 1 838  ? 25.041 55.593  -27.159 1.00 10.23 ? 838  GLU A CA  1 
ATOM   6721 C  C   . GLU A 1 838  ? 23.752 54.855  -27.471 1.00 10.24 ? 838  GLU A C   1 
ATOM   6722 O  O   . GLU A 1 838  ? 22.888 54.649  -26.648 1.00 11.08 ? 838  GLU A O   1 
ATOM   6723 C  CB  . GLU A 1 838  ? 26.165 54.560  -27.156 1.00 10.84 ? 838  GLU A CB  1 
ATOM   6724 C  CG  . GLU A 1 838  ? 25.947 53.416  -26.114 1.00 11.28 ? 838  GLU A CG  1 
ATOM   6725 C  CD  . GLU A 1 838  ? 27.055 52.363  -26.106 1.00 11.95 ? 838  GLU A CD  1 
ATOM   6726 O  OE1 . GLU A 1 838  ? 28.079 52.507  -26.794 1.00 14.36 ? 838  GLU A OE1 1 
ATOM   6727 O  OE2 . GLU A 1 838  ? 26.914 51.314  -25.417 1.00 14.09 ? 838  GLU A OE2 1 
ATOM   6728 N  N   . ASP A 1 839  ? 23.633 54.559  -28.765 1.00 10.27 ? 839  ASP A N   1 
ATOM   6729 C  CA  . ASP A 1 839  ? 22.517 53.678  -29.220 1.00 11.34 ? 839  ASP A CA  1 
ATOM   6730 C  C   . ASP A 1 839  ? 23.221 52.598  -30.026 1.00 12.28 ? 839  ASP A C   1 
ATOM   6731 O  O   . ASP A 1 839  ? 24.441 52.376  -29.932 1.00 13.00 ? 839  ASP A O   1 
ATOM   6732 C  CB  . ASP A 1 839  ? 21.418 54.423  -30.006 1.00 11.56 ? 839  ASP A CB  1 
ATOM   6733 C  CG  . ASP A 1 839  ? 21.917 55.144  -31.276 1.00 11.55 ? 839  ASP A CG  1 
ATOM   6734 O  OD1 . ASP A 1 839  ? 22.922 54.738  -31.872 1.00 11.92 ? 839  ASP A OD1 1 
ATOM   6735 O  OD2 . ASP A 1 839  ? 21.197 56.142  -31.584 1.00 15.02 ? 839  ASP A OD2 1 
ATOM   6736 N  N   . ALA A 1 840  ? 22.461 51.864  -30.859 1.00 13.25 ? 840  ALA A N   1 
ATOM   6737 C  CA  . ALA A 1 840  ? 23.091 50.819  -31.594 1.00 14.13 ? 840  ALA A CA  1 
ATOM   6738 C  C   . ALA A 1 840  ? 24.208 51.258  -32.534 1.00 13.53 ? 840  ALA A C   1 
ATOM   6739 O  O   . ALA A 1 840  ? 25.181 50.547  -32.777 1.00 15.27 ? 840  ALA A O   1 
ATOM   6740 C  CB  . ALA A 1 840  ? 22.018 50.052  -32.405 1.00 15.57 ? 840  ALA A CB  1 
ATOM   6741 N  N   . ASN A 1 841  ? 24.086 52.481  -33.056 1.00 12.78 ? 841  ASN A N   1 
ATOM   6742 C  CA  . ASN A 1 841  ? 25.047 52.927  -34.044 1.00 12.73 ? 841  ASN A CA  1 
ATOM   6743 C  C   . ASN A 1 841  ? 26.004 54.069  -33.700 1.00 11.18 ? 841  ASN A C   1 
ATOM   6744 O  O   . ASN A 1 841  ? 27.079 54.155  -34.293 1.00 11.90 ? 841  ASN A O   1 
ATOM   6745 C  CB  . ASN A 1 841  ? 24.295 53.385  -35.311 1.00 13.58 ? 841  ASN A CB  1 
ATOM   6746 C  CG  . ASN A 1 841  ? 23.539 52.246  -35.985 1.00 14.92 ? 841  ASN A CG  1 
ATOM   6747 O  OD1 . ASN A 1 841  ? 24.033 51.141  -36.094 1.00 18.37 ? 841  ASN A OD1 1 
ATOM   6748 N  ND2 . ASN A 1 841  ? 22.327 52.552  -36.445 1.00 19.22 ? 841  ASN A ND2 1 
ATOM   6749 N  N   . THR A 1 842  ? 25.590 54.908  -32.767 1.00 10.97 ? 842  THR A N   1 
ATOM   6750 C  CA  . THR A 1 842  ? 26.332 56.141  -32.504 1.00 10.88 ? 842  THR A CA  1 
ATOM   6751 C  C   . THR A 1 842  ? 26.583 56.308  -31.015 1.00 10.21 ? 842  THR A C   1 
ATOM   6752 O  O   . THR A 1 842  ? 25.724 56.001  -30.203 1.00 11.20 ? 842  THR A O   1 
ATOM   6753 C  CB  . THR A 1 842  ? 25.460 57.342  -32.969 1.00 9.97  ? 842  THR A CB  1 
ATOM   6754 O  OG1 . THR A 1 842  ? 25.069 57.116  -34.339 1.00 12.76 ? 842  THR A OG1 1 
ATOM   6755 C  CG2 . THR A 1 842  ? 26.239 58.668  -32.962 1.00 12.54 ? 842  THR A CG2 1 
ATOM   6756 N  N   . ARG A 1 843  ? 27.763 56.867  -30.738 1.00 10.01 ? 843  ARG A N   1 
ATOM   6757 C  CA  . ARG A 1 843  ? 28.125 57.189  -29.336 1.00 9.93  ? 843  ARG A CA  1 
ATOM   6758 C  C   . ARG A 1 843  ? 28.667 58.633  -29.291 1.00 8.91  ? 843  ARG A C   1 
ATOM   6759 O  O   . ARG A 1 843  ? 29.361 59.078  -30.221 1.00 9.83  ? 843  ARG A O   1 
ATOM   6760 C  CB  . ARG A 1 843  ? 29.238 56.268  -28.844 1.00 10.70 ? 843  ARG A CB  1 
ATOM   6761 C  CG  . ARG A 1 843  ? 29.587 56.545  -27.318 1.00 9.69  ? 843  ARG A CG  1 
ATOM   6762 C  CD  . ARG A 1 843  ? 30.777 55.693  -26.928 1.00 10.07 ? 843  ARG A CD  1 
ATOM   6763 N  NE  . ARG A 1 843  ? 30.413 54.295  -26.655 1.00 9.67  ? 843  ARG A NE  1 
ATOM   6764 C  CZ  . ARG A 1 843  ? 31.236 53.469  -26.050 1.00 10.06 ? 843  ARG A CZ  1 
ATOM   6765 N  NH1 . ARG A 1 843  ? 32.459 53.843  -25.695 1.00 9.66  ? 843  ARG A NH1 1 
ATOM   6766 N  NH2 . ARG A 1 843  ? 30.740 52.287  -25.667 1.00 11.03 ? 843  ARG A NH2 1 
ATOM   6767 N  N   . LEU A 1 844  ? 28.293 59.316  -28.227 1.00 8.68  ? 844  LEU A N   1 
ATOM   6768 C  CA  . LEU A 1 844  ? 28.881 60.671  -27.968 1.00 8.63  ? 844  LEU A CA  1 
ATOM   6769 C  C   . LEU A 1 844  ? 29.536 60.540  -26.580 1.00 8.35  ? 844  LEU A C   1 
ATOM   6770 O  O   . LEU A 1 844  ? 28.830 60.249  -25.590 1.00 8.66  ? 844  LEU A O   1 
ATOM   6771 C  CB  . LEU A 1 844  ? 27.813 61.767  -27.932 1.00 9.72  ? 844  LEU A CB  1 
ATOM   6772 C  CG  . LEU A 1 844  ? 28.477 63.167  -27.802 1.00 10.51 ? 844  LEU A CG  1 
ATOM   6773 C  CD1 . LEU A 1 844  ? 29.350 63.519  -28.984 1.00 12.09 ? 844  LEU A CD1 1 
ATOM   6774 C  CD2 . LEU A 1 844  ? 27.361 64.193  -27.654 1.00 13.09 ? 844  LEU A CD2 1 
ATOM   6775 N  N   . THR A 1 845  ? 30.844 60.830  -26.559 1.00 8.54  ? 845  THR A N   1 
ATOM   6776 C  CA  . THR A 1 845  ? 31.602 60.791  -25.271 1.00 8.10  ? 845  THR A CA  1 
ATOM   6777 C  C   . THR A 1 845  ? 32.151 62.204  -24.994 1.00 8.03  ? 845  THR A C   1 
ATOM   6778 O  O   . THR A 1 845  ? 32.749 62.834  -25.873 1.00 8.71  ? 845  THR A O   1 
ATOM   6779 C  CB  . THR A 1 845  ? 32.819 59.867  -25.344 1.00 7.88  ? 845  THR A CB  1 
ATOM   6780 O  OG1 . THR A 1 845  ? 32.365 58.549  -25.755 1.00 9.28  ? 845  THR A OG1 1 
ATOM   6781 C  CG2 . THR A 1 845  ? 33.467 59.671  -23.962 1.00 9.20  ? 845  THR A CG2 1 
ATOM   6782 N  N   . LEU A 1 846  ? 31.972 62.642  -23.756 1.00 8.47  ? 846  LEU A N   1 
ATOM   6783 C  CA  . LEU A 1 846  ? 32.482 63.928  -23.280 1.00 8.28  ? 846  LEU A CA  1 
ATOM   6784 C  C   . LEU A 1 846  ? 33.529 63.605  -22.222 1.00 7.09  ? 846  LEU A C   1 
ATOM   6785 O  O   . LEU A 1 846  ? 33.177 63.024  -21.178 1.00 7.43  ? 846  LEU A O   1 
ATOM   6786 C  CB  . LEU A 1 846  ? 31.356 64.794  -22.689 1.00 9.58  ? 846  LEU A CB  1 
ATOM   6787 C  CG  . LEU A 1 846  ? 31.795 66.191  -22.195 1.00 10.58 ? 846  LEU A CG  1 
ATOM   6788 C  CD1 . LEU A 1 846  ? 32.237 67.061  -23.418 1.00 10.14 ? 846  LEU A CD1 1 
ATOM   6789 C  CD2 . LEU A 1 846  ? 30.687 66.896  -21.410 1.00 13.20 ? 846  LEU A CD2 1 
ATOM   6790 N  N   . LEU A 1 847  ? 34.795 63.906  -22.507 1.00 7.81  ? 847  LEU A N   1 
ATOM   6791 C  CA  . LEU A 1 847  ? 35.890 63.681  -21.520 1.00 6.36  ? 847  LEU A CA  1 
ATOM   6792 C  C   . LEU A 1 847  ? 36.140 65.006  -20.809 1.00 7.29  ? 847  LEU A C   1 
ATOM   6793 O  O   . LEU A 1 847  ? 36.004 66.098  -21.410 1.00 7.55  ? 847  LEU A O   1 
ATOM   6794 C  CB  . LEU A 1 847  ? 37.144 63.223  -22.223 1.00 7.44  ? 847  LEU A CB  1 
ATOM   6795 C  CG  . LEU A 1 847  ? 37.169 61.859  -22.926 1.00 6.97  ? 847  LEU A CG  1 
ATOM   6796 C  CD1 . LEU A 1 847  ? 36.510 60.768  -22.037 1.00 8.50  ? 847  LEU A CD1 1 
ATOM   6797 C  CD2 . LEU A 1 847  ? 36.455 61.980  -24.272 1.00 8.31  ? 847  LEU A CD2 1 
ATOM   6798 N  N   . THR A 1 848  ? 36.516 64.911  -19.539 1.00 6.51  ? 848  THR A N   1 
ATOM   6799 C  CA  . THR A 1 848  ? 36.795 66.126  -18.755 1.00 6.80  ? 848  THR A CA  1 
ATOM   6800 C  C   . THR A 1 848  ? 38.220 66.220  -18.194 1.00 7.22  ? 848  THR A C   1 
ATOM   6801 O  O   A THR A 1 848  ? 38.955 65.217  -18.002 0.50 6.51  ? 848  THR A O   1 
ATOM   6802 O  O   B THR A 1 848  ? 38.676 65.210  -17.679 0.50 8.80  ? 848  THR A O   1 
ATOM   6803 C  CB  A THR A 1 848  ? 35.895 66.313  -17.523 0.50 7.10  ? 848  THR A CB  1 
ATOM   6804 C  CB  B THR A 1 848  ? 35.647 66.173  -17.627 0.50 8.97  ? 848  THR A CB  1 
ATOM   6805 O  OG1 A THR A 1 848  ? 36.227 65.322  -16.539 0.50 4.25  ? 848  THR A OG1 1 
ATOM   6806 O  OG1 B THR A 1 848  ? 34.379 65.765  -18.128 0.50 13.05 ? 848  THR A OG1 1 
ATOM   6807 C  CG2 A THR A 1 848  ? 34.476 66.196  -17.818 0.50 8.59  ? 848  THR A CG2 1 
ATOM   6808 C  CG2 B THR A 1 848  ? 35.573 67.529  -17.049 0.50 9.02  ? 848  THR A CG2 1 
ATOM   6809 N  N   . GLY A 1 849  ? 38.588 67.465  -17.942 1.00 6.71  ? 849  GLY A N   1 
ATOM   6810 C  CA  . GLY A 1 849  ? 39.864 67.710  -17.287 1.00 6.77  ? 849  GLY A CA  1 
ATOM   6811 C  C   . GLY A 1 849  ? 39.680 68.071  -15.846 1.00 5.71  ? 849  GLY A C   1 
ATOM   6812 O  O   . GLY A 1 849  ? 40.635 68.515  -15.208 1.00 6.75  ? 849  GLY A O   1 
ATOM   6813 N  N   . GLN A 1 850  ? 38.497 67.855  -15.285 1.00 5.94  ? 850  GLN A N   1 
ATOM   6814 C  CA  . GLN A 1 850  ? 38.212 68.196  -13.898 1.00 5.53  ? 850  GLN A CA  1 
ATOM   6815 C  C   . GLN A 1 850  ? 36.950 67.448  -13.523 1.00 6.42  ? 850  GLN A C   1 
ATOM   6816 O  O   . GLN A 1 850  ? 36.053 67.216  -14.369 1.00 6.74  ? 850  GLN A O   1 
ATOM   6817 C  CB  . GLN A 1 850  ? 37.986 69.742  -13.775 1.00 7.03  ? 850  GLN A CB  1 
ATOM   6818 C  CG  . GLN A 1 850  ? 36.830 70.301  -14.687 1.00 7.11  ? 850  GLN A CG  1 
ATOM   6819 C  CD  . GLN A 1 850  ? 37.190 70.401  -16.144 1.00 6.96  ? 850  GLN A CD  1 
ATOM   6820 O  OE1 . GLN A 1 850  ? 38.300 70.802  -16.520 1.00 7.77  ? 850  GLN A OE1 1 
ATOM   6821 N  NE2 . GLN A 1 850  ? 36.232 70.072  -17.016 1.00 7.42  ? 850  GLN A NE2 1 
ATOM   6822 N  N   . PRO A 1 851  ? 36.813 67.047  -12.260 1.00 5.52  ? 851  PRO A N   1 
ATOM   6823 C  CA  . PRO A 1 851  ? 35.577 66.336  -11.867 1.00 6.22  ? 851  PRO A CA  1 
ATOM   6824 C  C   . PRO A 1 851  ? 34.468 67.338  -11.682 1.00 6.12  ? 851  PRO A C   1 
ATOM   6825 O  O   . PRO A 1 851  ? 34.658 68.375  -11.023 1.00 6.69  ? 851  PRO A O   1 
ATOM   6826 C  CB  . PRO A 1 851  ? 35.948 65.659  -10.508 1.00 6.15  ? 851  PRO A CB  1 
ATOM   6827 C  CG  . PRO A 1 851  ? 37.108 66.611  -9.954  1.00 6.14  ? 851  PRO A CG  1 
ATOM   6828 C  CD  . PRO A 1 851  ? 37.861 67.048  -11.207 1.00 5.25  ? 851  PRO A CD  1 
ATOM   6829 N  N   . LEU A 1 852  ? 33.279 67.007  -12.249 1.00 6.74  ? 852  LEU A N   1 
ATOM   6830 C  CA  . LEU A 1 852  ? 32.088 67.866  -12.123 1.00 7.24  ? 852  LEU A CA  1 
ATOM   6831 C  C   . LEU A 1 852  ? 30.885 66.940  -12.020 1.00 8.19  ? 852  LEU A C   1 
ATOM   6832 O  O   . LEU A 1 852  ? 31.019 65.766  -12.294 1.00 11.02 ? 852  LEU A O   1 
ATOM   6833 C  CB  . LEU A 1 852  ? 31.956 68.748  -13.362 1.00 8.01  ? 852  LEU A CB  1 
ATOM   6834 C  CG  . LEU A 1 852  ? 33.119 69.779  -13.502 1.00 6.92  ? 852  LEU A CG  1 
ATOM   6835 C  CD1 . LEU A 1 852  ? 33.043 70.350  -14.974 1.00 9.26  ? 852  LEU A CD1 1 
ATOM   6836 C  CD2 . LEU A 1 852  ? 33.035 70.923  -12.506 1.00 8.00  ? 852  LEU A CD2 1 
ATOM   6837 N  N   . GLY A 1 853  ? 29.728 67.472  -11.684 1.00 6.82  ? 853  GLY A N   1 
ATOM   6838 C  CA  . GLY A 1 853  ? 28.539 66.616  -11.638 1.00 7.78  ? 853  GLY A CA  1 
ATOM   6839 C  C   . GLY A 1 853  ? 27.799 66.608  -12.967 1.00 6.81  ? 853  GLY A C   1 
ATOM   6840 O  O   . GLY A 1 853  ? 27.833 67.594  -13.725 1.00 7.32  ? 853  GLY A O   1 
ATOM   6841 N  N   . GLY A 1 854  ? 27.092 65.523  -13.262 1.00 6.71  ? 854  GLY A N   1 
ATOM   6842 C  CA  . GLY A 1 854  ? 26.385 65.493  -14.533 1.00 8.05  ? 854  GLY A CA  1 
ATOM   6843 C  C   . GLY A 1 854  ? 25.354 64.385  -14.627 1.00 7.11  ? 854  GLY A C   1 
ATOM   6844 O  O   . GLY A 1 854  ? 25.163 63.573  -13.703 1.00 7.69  ? 854  GLY A O   1 
ATOM   6845 N  N   . SER A 1 855  ? 24.669 64.367  -15.775 1.00 7.50  ? 855  SER A N   1 
ATOM   6846 C  CA  . SER A 1 855  ? 23.600 63.372  -15.938 1.00 8.34  ? 855  SER A CA  1 
ATOM   6847 C  C   . SER A 1 855  ? 23.222 63.330  -17.390 1.00 8.14  ? 855  SER A C   1 
ATOM   6848 O  O   . SER A 1 855  ? 23.788 64.019  -18.233 1.00 8.99  ? 855  SER A O   1 
ATOM   6849 C  CB  . SER A 1 855  ? 22.364 63.865  -15.180 1.00 9.16  ? 855  SER A CB  1 
ATOM   6850 O  OG  . SER A 1 855  ? 21.376 62.827  -15.128 1.00 9.70  ? 855  SER A OG  1 
ATOM   6851 N  N   . SER A 1 856  ? 22.230 62.467  -17.670 1.00 8.35  ? 856  SER A N   1 
ATOM   6852 C  CA  . SER A 1 856  ? 21.538 62.436  -18.991 1.00 8.59  ? 856  SER A CA  1 
ATOM   6853 C  C   . SER A 1 856  ? 20.075 62.442  -18.546 1.00 9.33  ? 856  SER A C   1 
ATOM   6854 O  O   . SER A 1 856  ? 19.541 61.387  -18.158 1.00 10.09 ? 856  SER A O   1 
ATOM   6855 C  CB  . SER A 1 856  ? 21.864 61.161  -19.707 1.00 8.39  ? 856  SER A CB  1 
ATOM   6856 O  OG  . SER A 1 856  ? 21.057 61.092  -20.910 1.00 10.26 ? 856  SER A OG  1 
ATOM   6857 N  N   . LEU A 1 857  ? 19.402 63.603  -18.598 1.00 9.58  ? 857  LEU A N   1 
ATOM   6858 C  CA  . LEU A 1 857  ? 18.027 63.732  -18.078 1.00 10.07 ? 857  LEU A CA  1 
ATOM   6859 C  C   . LEU A 1 857  ? 16.944 63.393  -19.093 1.00 10.21 ? 857  LEU A C   1 
ATOM   6860 O  O   . LEU A 1 857  ? 15.769 63.329  -18.735 1.00 11.52 ? 857  LEU A O   1 
ATOM   6861 C  CB  . LEU A 1 857  ? 17.831 65.148  -17.467 1.00 10.68 ? 857  LEU A CB  1 
ATOM   6862 C  CG  . LEU A 1 857  ? 18.682 65.343  -16.222 1.00 10.70 ? 857  LEU A CG  1 
ATOM   6863 C  CD1 . LEU A 1 857  ? 18.511 66.799  -15.728 1.00 12.67 ? 857  LEU A CD1 1 
ATOM   6864 C  CD2 . LEU A 1 857  ? 18.283 64.347  -15.117 1.00 11.57 ? 857  LEU A CD2 1 
ATOM   6865 N  N   . ALA A 1 858  ? 17.371 63.195  -20.295 1.00 9.52  ? 858  ALA A N   1 
ATOM   6866 C  CA  . ALA A 1 858  ? 16.478 62.745  -21.396 1.00 10.07 ? 858  ALA A CA  1 
ATOM   6867 C  C   . ALA A 1 858  ? 17.297 62.039  -22.463 1.00 10.89 ? 858  ALA A C   1 
ATOM   6868 O  O   . ALA A 1 858  ? 18.505 62.284  -22.622 1.00 10.52 ? 858  ALA A O   1 
ATOM   6869 C  CB  . ALA A 1 858  ? 15.714 63.957  -22.020 1.00 11.89 ? 858  ALA A CB  1 
ATOM   6870 N  N   . SER A 1 859  ? 16.674 61.143  -23.227 1.00 11.19 ? 859  SER A N   1 
ATOM   6871 C  CA  . SER A 1 859  ? 17.330 60.408  -24.272 1.00 10.38 ? 859  SER A CA  1 
ATOM   6872 C  C   . SER A 1 859  ? 18.055 61.370  -25.202 1.00 9.52  ? 859  SER A C   1 
ATOM   6873 O  O   . SER A 1 859  ? 17.498 62.418  -25.574 1.00 12.27 ? 859  SER A O   1 
ATOM   6874 C  CB  . SER A 1 859  ? 16.233 59.586  -25.044 1.00 12.20 ? 859  SER A CB  1 
ATOM   6875 O  OG  . SER A 1 859  ? 16.794 58.823  -26.024 1.00 12.64 ? 859  SER A OG  1 
ATOM   6876 N  N   . GLY A 1 860  ? 19.270 61.026  -25.581 1.00 10.51 ? 860  GLY A N   1 
ATOM   6877 C  CA  . GLY A 1 860  ? 20.044 61.867  -26.480 1.00 10.79 ? 860  GLY A CA  1 
ATOM   6878 C  C   . GLY A 1 860  ? 20.795 63.013  -25.774 1.00 9.58  ? 860  GLY A C   1 
ATOM   6879 O  O   . GLY A 1 860  ? 21.565 63.674  -26.481 1.00 10.09 ? 860  GLY A O   1 
ATOM   6880 N  N   . GLU A 1 861  ? 20.624 63.207  -24.466 1.00 9.85  ? 861  GLU A N   1 
ATOM   6881 C  CA  . GLU A 1 861  ? 21.286 64.314  -23.791 1.00 9.81  ? 861  GLU A CA  1 
ATOM   6882 C  C   . GLU A 1 861  ? 22.433 63.915  -22.883 1.00 9.70  ? 861  GLU A C   1 
ATOM   6883 O  O   . GLU A 1 861  ? 22.491 62.806  -22.341 1.00 10.93 ? 861  GLU A O   1 
ATOM   6884 C  CB  . GLU A 1 861  ? 20.339 65.085  -22.886 1.00 11.09 ? 861  GLU A CB  1 
ATOM   6885 C  CG  . GLU A 1 861  ? 19.171 65.735  -23.608 1.00 12.82 ? 861  GLU A CG  1 
ATOM   6886 C  CD  . GLU A 1 861  ? 18.289 66.568  -22.701 1.00 13.60 ? 861  GLU A CD  1 
ATOM   6887 O  OE1 . GLU A 1 861  ? 18.445 66.628  -21.467 1.00 13.68 ? 861  GLU A OE1 1 
ATOM   6888 O  OE2 . GLU A 1 861  ? 17.312 67.196  -23.261 1.00 16.31 ? 861  GLU A OE2 1 
ATOM   6889 N  N   . LEU A 1 862  ? 23.356 64.845  -22.784 1.00 9.48  ? 862  LEU A N   1 
ATOM   6890 C  CA  . LEU A 1 862  ? 24.422 64.774  -21.744 1.00 9.22  ? 862  LEU A CA  1 
ATOM   6891 C  C   . LEU A 1 862  ? 24.445 66.138  -21.101 1.00 8.16  ? 862  LEU A C   1 
ATOM   6892 O  O   . LEU A 1 862  ? 24.258 67.152  -21.793 1.00 8.81  ? 862  LEU A O   1 
ATOM   6893 C  CB  . LEU A 1 862  ? 25.836 64.510  -22.374 1.00 9.57  ? 862  LEU A CB  1 
ATOM   6894 C  CG  . LEU A 1 862  ? 26.220 63.139  -23.024 1.00 10.18 ? 862  LEU A CG  1 
ATOM   6895 C  CD1 . LEU A 1 862  ? 27.515 63.164  -23.773 1.00 10.20 ? 862  LEU A CD1 1 
ATOM   6896 C  CD2 . LEU A 1 862  ? 26.173 62.064  -21.907 1.00 11.05 ? 862  LEU A CD2 1 
ATOM   6897 N  N   . GLU A 1 863  ? 24.698 66.220  -19.804 1.00 7.95  ? 863  GLU A N   1 
ATOM   6898 C  CA  . GLU A 1 863  ? 24.871 67.552  -19.218 1.00 8.51  ? 863  GLU A CA  1 
ATOM   6899 C  C   . GLU A 1 863  ? 25.854 67.482  -18.078 1.00 8.02  ? 863  GLU A C   1 
ATOM   6900 O  O   . GLU A 1 863  ? 25.978 66.452  -17.412 1.00 8.15  ? 863  GLU A O   1 
ATOM   6901 C  CB  . GLU A 1 863  ? 23.558 68.226  -18.790 1.00 9.00  ? 863  GLU A CB  1 
ATOM   6902 C  CG  . GLU A 1 863  ? 22.958 67.644  -17.545 1.00 9.95  ? 863  GLU A CG  1 
ATOM   6903 C  CD  . GLU A 1 863  ? 21.690 68.372  -17.127 1.00 8.63  ? 863  GLU A CD  1 
ATOM   6904 O  OE1 . GLU A 1 863  ? 20.789 68.385  -18.018 1.00 11.19 ? 863  GLU A OE1 1 
ATOM   6905 O  OE2 . GLU A 1 863  ? 21.558 68.879  -16.004 1.00 10.01 ? 863  GLU A OE2 1 
ATOM   6906 N  N   . ILE A 1 864  ? 26.603 68.570  -17.917 1.00 8.20  ? 864  ILE A N   1 
ATOM   6907 C  CA  . ILE A 1 864  ? 27.638 68.637  -16.859 1.00 7.74  ? 864  ILE A CA  1 
ATOM   6908 C  C   . ILE A 1 864  ? 27.625 70.029  -16.235 1.00 7.38  ? 864  ILE A C   1 
ATOM   6909 O  O   . ILE A 1 864  ? 27.644 71.049  -16.975 1.00 7.94  ? 864  ILE A O   1 
ATOM   6910 C  CB  . ILE A 1 864  ? 28.985 68.225  -17.484 1.00 9.44  ? 864  ILE A CB  1 
ATOM   6911 C  CG1 . ILE A 1 864  ? 30.056 68.182  -16.384 1.00 10.85 ? 864  ILE A CG1 1 
ATOM   6912 C  CG2 . ILE A 1 864  ? 29.368 69.096  -18.664 1.00 10.69 ? 864  ILE A CG2 1 
ATOM   6913 C  CD1 . ILE A 1 864  ? 31.172 67.134  -16.850 1.00 11.80 ? 864  ILE A CD1 1 
ATOM   6914 N  N   . MET A 1 865  ? 27.567 70.070  -14.917 1.00 7.08  ? 865  MET A N   1 
ATOM   6915 C  CA  . MET A 1 865  ? 27.528 71.345  -14.203 1.00 7.31  ? 865  MET A CA  1 
ATOM   6916 C  C   . MET A 1 865  ? 28.894 72.049  -14.247 1.00 8.04  ? 865  MET A C   1 
ATOM   6917 O  O   . MET A 1 865  ? 29.935 71.435  -14.080 1.00 8.52  ? 865  MET A O   1 
ATOM   6918 C  CB  . MET A 1 865  ? 27.079 71.117  -12.748 1.00 7.38  ? 865  MET A CB  1 
ATOM   6919 C  CG  . MET A 1 865  ? 26.476 72.381  -12.081 1.00 7.60  ? 865  MET A CG  1 
ATOM   6920 S  SD  . MET A 1 865  ? 24.830 72.788  -12.813 1.00 9.85  ? 865  MET A SD  1 
ATOM   6921 C  CE  . MET A 1 865  ? 23.848 71.539  -11.893 1.00 9.81  ? 865  MET A CE  1 
ATOM   6922 N  N   . GLN A 1 866  ? 28.860 73.367  -14.453 1.00 8.28  ? 866  GLN A N   1 
ATOM   6923 C  CA  . GLN A 1 866  ? 30.074 74.192  -14.574 1.00 7.75  ? 866  GLN A CA  1 
ATOM   6924 C  C   . GLN A 1 866  ? 30.460 74.895  -13.268 1.00 8.21  ? 866  GLN A C   1 
ATOM   6925 O  O   . GLN A 1 866  ? 31.655 74.918  -12.916 1.00 8.99  ? 866  GLN A O   1 
ATOM   6926 C  CB  . GLN A 1 866  ? 29.891 75.236  -15.679 1.00 8.41  ? 866  GLN A CB  1 
ATOM   6927 C  CG  . GLN A 1 866  ? 29.551 74.618  -17.029 1.00 9.00  ? 866  GLN A CG  1 
ATOM   6928 C  CD  . GLN A 1 866  ? 30.589 73.651  -17.466 1.00 9.07  ? 866  GLN A CD  1 
ATOM   6929 O  OE1 . GLN A 1 866  ? 31.735 74.007  -17.806 1.00 8.98  ? 866  GLN A OE1 1 
ATOM   6930 N  NE2 . GLN A 1 866  ? 30.219 72.394  -17.457 1.00 9.32  ? 866  GLN A NE2 1 
ATOM   6931 N  N   . ASP A 1 867  ? 29.492 75.503  -12.575 1.00 8.15  ? 867  ASP A N   1 
ATOM   6932 C  CA  . ASP A 1 867  ? 29.746 76.140  -11.268 1.00 8.53  ? 867  ASP A CA  1 
ATOM   6933 C  C   . ASP A 1 867  ? 28.417 76.367  -10.607 1.00 7.81  ? 867  ASP A C   1 
ATOM   6934 O  O   . ASP A 1 867  ? 27.352 76.230  -11.286 1.00 8.43  ? 867  ASP A O   1 
ATOM   6935 C  CB  . ASP A 1 867  ? 30.556 77.452  -11.416 1.00 8.69  ? 867  ASP A CB  1 
ATOM   6936 C  CG  . ASP A 1 867  ? 31.270 77.849  -10.121 1.00 8.42  ? 867  ASP A CG  1 
ATOM   6937 O  OD1 . ASP A 1 867  ? 31.120 77.186  -9.091  1.00 8.77  ? 867  ASP A OD1 1 
ATOM   6938 O  OD2 . ASP A 1 867  ? 31.972 78.875  -10.169 1.00 9.25  ? 867  ASP A OD2 1 
ATOM   6939 N  N   . ARG A 1 868  ? 28.458 76.619  -9.321  1.00 8.23  ? 868  ARG A N   1 
ATOM   6940 C  CA  . ARG A 1 868  ? 27.242 76.855  -8.551  1.00 8.22  ? 868  ARG A CA  1 
ATOM   6941 C  C   . ARG A 1 868  ? 27.570 77.893  -7.477  1.00 8.50  ? 868  ARG A C   1 
ATOM   6942 O  O   . ARG A 1 868  ? 28.628 77.830  -6.827  1.00 8.72  ? 868  ARG A O   1 
ATOM   6943 C  CB  . ARG A 1 868  ? 26.700 75.527  -7.951  1.00 8.64  ? 868  ARG A CB  1 
ATOM   6944 C  CG  . ARG A 1 868  ? 27.743 74.783  -7.095  1.00 9.24  ? 868  ARG A CG  1 
ATOM   6945 C  CD  . ARG A 1 868  ? 27.498 73.266  -7.097  1.00 8.05  ? 868  ARG A CD  1 
ATOM   6946 N  NE  . ARG A 1 868  ? 26.114 72.932  -6.690  1.00 7.85  ? 868  ARG A NE  1 
ATOM   6947 C  CZ  . ARG A 1 868  ? 25.768 72.623  -5.455  1.00 7.82  ? 868  ARG A CZ  1 
ATOM   6948 N  NH1 . ARG A 1 868  ? 26.672 72.524  -4.460  1.00 8.52  ? 868  ARG A NH1 1 
ATOM   6949 N  NH2 . ARG A 1 868  ? 24.450 72.497  -5.195  1.00 9.18  ? 868  ARG A NH2 1 
ATOM   6950 N  N   . ARG A 1 869  ? 26.644 78.838  -7.305  1.00 9.35  ? 869  ARG A N   1 
ATOM   6951 C  CA  . ARG A 1 869  ? 26.841 79.929  -6.308  1.00 10.06 ? 869  ARG A CA  1 
ATOM   6952 C  C   . ARG A 1 869  ? 25.563 79.909  -5.507  1.00 9.81  ? 869  ARG A C   1 
ATOM   6953 O  O   . ARG A 1 869  ? 24.495 80.098  -6.059  1.00 10.57 ? 869  ARG A O   1 
ATOM   6954 C  CB  . ARG A 1 869  ? 27.042 81.281  -7.021  1.00 10.95 ? 869  ARG A CB  1 
ATOM   6955 C  CG  . ARG A 1 869  ? 27.223 82.409  -6.033  1.00 11.27 ? 869  ARG A CG  1 
ATOM   6956 C  CD  . ARG A 1 869  ? 27.524 83.697  -6.820  1.00 14.53 ? 869  ARG A CD  1 
ATOM   6957 N  NE  . ARG A 1 869  ? 27.719 84.860  -5.930  1.00 16.33 ? 869  ARG A NE  1 
ATOM   6958 C  CZ  . ARG A 1 869  ? 28.862 85.185  -5.361  1.00 15.63 ? 869  ARG A CZ  1 
ATOM   6959 N  NH1 . ARG A 1 869  ? 29.958 84.477  -5.548  1.00 16.03 ? 869  ARG A NH1 1 
ATOM   6960 N  NH2 . ARG A 1 869  ? 28.899 86.276  -4.578  1.00 17.71 ? 869  ARG A NH2 1 
ATOM   6961 N  N   . LEU A 1 870  ? 25.709 79.631  -4.229  1.00 11.44 ? 870  LEU A N   1 
ATOM   6962 C  CA  . LEU A 1 870  ? 24.568 79.369  -3.304  1.00 11.48 ? 870  LEU A CA  1 
ATOM   6963 C  C   . LEU A 1 870  ? 24.636 80.205  -2.058  1.00 12.08 ? 870  LEU A C   1 
ATOM   6964 O  O   . LEU A 1 870  ? 25.615 80.196  -1.327  1.00 11.67 ? 870  LEU A O   1 
ATOM   6965 C  CB  . LEU A 1 870  ? 24.629 77.882  -2.943  1.00 12.60 ? 870  LEU A CB  1 
ATOM   6966 C  CG  . LEU A 1 870  ? 24.621 77.027  -4.210  1.00 14.49 ? 870  LEU A CG  1 
ATOM   6967 C  CD1 . LEU A 1 870  ? 25.076 75.681  -3.882  1.00 16.72 ? 870  LEU A CD1 1 
ATOM   6968 C  CD2 . LEU A 1 870  ? 23.287 77.006  -4.908  1.00 13.78 ? 870  LEU A CD2 1 
ATOM   6969 N  N   . ALA A 1 871  ? 23.528 80.898  -1.773  1.00 12.77 ? 871  ALA A N   1 
ATOM   6970 C  CA  . ALA A 1 871  ? 23.537 81.770  -0.623  1.00 14.24 ? 871  ALA A CA  1 
ATOM   6971 C  C   . ALA A 1 871  ? 23.347 81.070  0.735   1.00 15.28 ? 871  ALA A C   1 
ATOM   6972 O  O   . ALA A 1 871  ? 23.765 81.568  1.785   1.00 17.06 ? 871  ALA A O   1 
ATOM   6973 C  CB  . ALA A 1 871  ? 22.408 82.824  -0.808  1.00 15.81 ? 871  ALA A CB  1 
ATOM   6974 N  N   . SER A 1 872  ? 22.754 79.889  0.691   1.00 14.70 ? 872  SER A N   1 
ATOM   6975 C  CA  . SER A 1 872  ? 22.413 79.208  1.919   1.00 15.42 ? 872  SER A CA  1 
ATOM   6976 C  C   . SER A 1 872  ? 23.271 78.061  2.323   1.00 14.20 ? 872  SER A C   1 
ATOM   6977 O  O   . SER A 1 872  ? 23.908 77.447  1.466   1.00 14.16 ? 872  SER A O   1 
ATOM   6978 C  CB  . SER A 1 872  ? 20.977 78.690  1.793   1.00 18.03 ? 872  SER A CB  1 
ATOM   6979 O  OG  . SER A 1 872  ? 20.099 79.780  1.519   1.00 21.42 ? 872  SER A OG  1 
ATOM   6980 N  N   . ASP A 1 873  ? 23.340 77.839  3.630   1.00 13.89 ? 873  ASP A N   1 
ATOM   6981 C  CA  . ASP A 1 873  ? 23.964 76.654  4.243   1.00 13.49 ? 873  ASP A CA  1 
ATOM   6982 C  C   . ASP A 1 873  ? 22.945 75.508  4.069   1.00 13.81 ? 873  ASP A C   1 
ATOM   6983 O  O   . ASP A 1 873  ? 21.740 75.729  4.117   1.00 14.25 ? 873  ASP A O   1 
ATOM   6984 C  CB  . ASP A 1 873  ? 24.200 76.868  5.727   1.00 13.30 ? 873  ASP A CB  1 
ATOM   6985 C  CG  . ASP A 1 873  ? 24.668 75.610  6.401   1.00 13.11 ? 873  ASP A CG  1 
ATOM   6986 O  OD1 . ASP A 1 873  ? 25.774 75.133  6.015   1.00 14.56 ? 873  ASP A OD1 1 
ATOM   6987 O  OD2 . ASP A 1 873  ? 23.978 75.068  7.291   1.00 15.28 ? 873  ASP A OD2 1 
ATOM   6988 N  N   . ASP A 1 874  ? 23.438 74.281  3.876   1.00 12.13 ? 874  ASP A N   1 
ATOM   6989 C  CA  . ASP A 1 874  ? 22.546 73.149  3.675   1.00 10.71 ? 874  ASP A CA  1 
ATOM   6990 C  C   . ASP A 1 874  ? 22.488 72.170  4.839   1.00 10.56 ? 874  ASP A C   1 
ATOM   6991 O  O   . ASP A 1 874  ? 22.275 70.965  4.663   1.00 11.70 ? 874  ASP A O   1 
ATOM   6992 C  CB  . ASP A 1 874  ? 22.866 72.436  2.347   1.00 10.92 ? 874  ASP A CB  1 
ATOM   6993 C  CG  . ASP A 1 874  ? 24.352 72.047  2.206   1.00 9.26  ? 874  ASP A CG  1 
ATOM   6994 O  OD1 . ASP A 1 874  ? 25.157 72.296  3.124   1.00 11.46 ? 874  ASP A OD1 1 
ATOM   6995 O  OD2 . ASP A 1 874  ? 24.622 71.482  1.142   1.00 10.04 ? 874  ASP A OD2 1 
ATOM   6996 N  N   . GLU A 1 875  ? 22.755 72.686  6.026   1.00 11.52 ? 875  GLU A N   1 
ATOM   6997 C  CA  . GLU A 1 875  ? 22.503 71.898  7.252   1.00 12.74 ? 875  GLU A CA  1 
ATOM   6998 C  C   . GLU A 1 875  ? 23.292 70.644  7.479   1.00 12.83 ? 875  GLU A C   1 
ATOM   6999 O  O   . GLU A 1 875  ? 22.882 69.732  8.191   1.00 13.10 ? 875  GLU A O   1 
ATOM   7000 C  CB  . GLU A 1 875  ? 20.986 71.573  7.372   1.00 16.29 ? 875  GLU A CB  1 
ATOM   7001 C  CG  . GLU A 1 875  ? 20.112 72.858  7.282   1.00 21.86 ? 875  GLU A CG  1 
ATOM   7002 C  CD  . GLU A 1 875  ? 18.684 72.702  7.844   1.00 25.97 ? 875  GLU A CD  1 
ATOM   7003 O  OE1 . GLU A 1 875  ? 18.528 72.312  9.014   1.00 30.94 ? 875  GLU A OE1 1 
ATOM   7004 O  OE2 . GLU A 1 875  ? 17.716 72.979  7.125   1.00 29.26 ? 875  GLU A OE2 1 
ATOM   7005 N  N   . ARG A 1 876  ? 24.479 70.610  6.883   1.00 11.42 ? 876  ARG A N   1 
ATOM   7006 C  CA  . ARG A 1 876  ? 25.389 69.463  7.053   1.00 11.35 ? 876  ARG A CA  1 
ATOM   7007 C  C   . ARG A 1 876  ? 26.656 69.839  7.841   1.00 11.69 ? 876  ARG A C   1 
ATOM   7008 O  O   . ARG A 1 876  ? 27.632 69.080  7.877   1.00 11.96 ? 876  ARG A O   1 
ATOM   7009 C  CB  . ARG A 1 876  ? 25.718 68.835  5.672   1.00 10.39 ? 876  ARG A CB  1 
ATOM   7010 C  CG  . ARG A 1 876  ? 24.468 68.286  4.920   1.00 10.23 ? 876  ARG A CG  1 
ATOM   7011 C  CD  . ARG A 1 876  ? 23.685 67.335  5.818   1.00 10.73 ? 876  ARG A CD  1 
ATOM   7012 N  NE  . ARG A 1 876  ? 22.591 66.617  5.147   1.00 9.91  ? 876  ARG A NE  1 
ATOM   7013 C  CZ  . ARG A 1 876  ? 21.397 67.156  4.877   1.00 9.79  ? 876  ARG A CZ  1 
ATOM   7014 N  NH1 . ARG A 1 876  ? 21.159 68.453  5.146   1.00 10.31 ? 876  ARG A NH1 1 
ATOM   7015 N  NH2 . ARG A 1 876  ? 20.415 66.356  4.436   1.00 10.29 ? 876  ARG A NH2 1 
ATOM   7016 N  N   . GLY A 1 877  ? 26.652 71.030  8.441   1.00 11.78 ? 877  GLY A N   1 
ATOM   7017 C  CA  . GLY A 1 877  ? 27.756 71.454  9.299   1.00 11.33 ? 877  GLY A CA  1 
ATOM   7018 C  C   . GLY A 1 877  ? 28.700 72.516  8.787   1.00 11.23 ? 877  GLY A C   1 
ATOM   7019 O  O   . GLY A 1 877  ? 29.505 73.023  9.562   1.00 12.83 ? 877  GLY A O   1 
ATOM   7020 N  N   . LEU A 1 878  ? 28.627 72.815  7.500   1.00 10.32 ? 878  LEU A N   1 
ATOM   7021 C  CA  . LEU A 1 878  ? 29.567 73.808  6.919   1.00 11.80 ? 878  LEU A CA  1 
ATOM   7022 C  C   . LEU A 1 878  ? 29.330 75.217  7.461   1.00 12.34 ? 878  LEU A C   1 
ATOM   7023 O  O   . LEU A 1 878  ? 30.269 75.949  7.726   1.00 12.07 ? 878  LEU A O   1 
ATOM   7024 C  CB  . LEU A 1 878  ? 29.498 73.781  5.374   1.00 11.42 ? 878  LEU A CB  1 
ATOM   7025 C  CG  . LEU A 1 878  ? 30.243 74.886  4.617   1.00 10.76 ? 878  LEU A CG  1 
ATOM   7026 C  CD1 . LEU A 1 878  ? 31.737 74.860  5.018   1.00 11.34 ? 878  LEU A CD1 1 
ATOM   7027 C  CD2 . LEU A 1 878  ? 30.066 74.681  3.100   1.00 11.40 ? 878  LEU A CD2 1 
ATOM   7028 N  N   . GLY A 1 879  ? 28.060 75.572  7.644   1.00 11.35 ? 879  GLY A N   1 
ATOM   7029 C  CA  . GLY A 1 879  ? 27.796 76.877  8.231   1.00 13.05 ? 879  GLY A CA  1 
ATOM   7030 C  C   . GLY A 1 879  ? 28.000 78.078  7.337   1.00 13.50 ? 879  GLY A C   1 
ATOM   7031 O  O   . GLY A 1 879  ? 28.216 79.177  7.837   1.00 15.85 ? 879  GLY A O   1 
ATOM   7032 N  N   . GLN A 1 880  ? 27.954 77.880  6.038   1.00 12.30 ? 880  GLN A N   1 
ATOM   7033 C  CA  . GLN A 1 880  ? 28.013 79.009  5.113   1.00 12.35 ? 880  GLN A CA  1 
ATOM   7034 C  C   . GLN A 1 880  ? 27.489 78.524  3.762   1.00 12.75 ? 880  GLN A C   1 
ATOM   7035 O  O   . GLN A 1 880  ? 27.406 77.318  3.553   1.00 13.32 ? 880  GLN A O   1 
ATOM   7036 C  CB  . GLN A 1 880  ? 29.455 79.547  4.947   1.00 11.46 ? 880  GLN A CB  1 
ATOM   7037 C  CG  . GLN A 1 880  ? 30.499 78.510  4.436   1.00 12.70 ? 880  GLN A CG  1 
ATOM   7038 C  CD  . GLN A 1 880  ? 31.745 79.169  3.848   1.00 10.91 ? 880  GLN A CD  1 
ATOM   7039 O  OE1 . GLN A 1 880  ? 31.801 79.442  2.634   1.00 15.43 ? 880  GLN A OE1 1 
ATOM   7040 N  NE2 . GLN A 1 880  ? 32.697 79.437  4.659   1.00 10.51 ? 880  GLN A NE2 1 
ATOM   7041 N  N   . GLY A 1 881  ? 27.183 79.472  2.877   1.00 13.42 ? 881  GLY A N   1 
ATOM   7042 C  CA  . GLY A 1 881  ? 26.823 79.137  1.497   1.00 14.40 ? 881  GLY A CA  1 
ATOM   7043 C  C   . GLY A 1 881  ? 28.136 79.015  0.692   1.00 13.31 ? 881  GLY A C   1 
ATOM   7044 O  O   . GLY A 1 881  ? 29.239 78.881  1.241   1.00 14.85 ? 881  GLY A O   1 
ATOM   7045 N  N   . VAL A 1 882  ? 27.999 79.008  -0.628  1.00 12.47 ? 882  VAL A N   1 
ATOM   7046 C  CA  . VAL A 1 882  ? 29.162 78.939  -1.518  1.00 10.55 ? 882  VAL A CA  1 
ATOM   7047 C  C   . VAL A 1 882  ? 29.089 80.230  -2.316  1.00 10.60 ? 882  VAL A C   1 
ATOM   7048 O  O   . VAL A 1 882  ? 28.345 80.370  -3.275  1.00 10.93 ? 882  VAL A O   1 
ATOM   7049 C  CB  . VAL A 1 882  ? 29.053 77.708  -2.439  1.00 11.09 ? 882  VAL A CB  1 
ATOM   7050 C  CG1 . VAL A 1 882  ? 30.194 77.701  -3.469  1.00 11.80 ? 882  VAL A CG1 1 
ATOM   7051 C  CG2 . VAL A 1 882  ? 29.125 76.427  -1.578  1.00 13.06 ? 882  VAL A CG2 1 
ATOM   7052 N  N   . LEU A 1 883  ? 29.841 81.211  -1.806  1.00 11.80 ? 883  LEU A N   1 
ATOM   7053 C  CA  . LEU A 1 883  ? 29.841 82.559  -2.421  1.00 12.82 ? 883  LEU A CA  1 
ATOM   7054 C  C   . LEU A 1 883  ? 31.245 83.044  -2.734  1.00 13.36 ? 883  LEU A C   1 
ATOM   7055 O  O   . LEU A 1 883  ? 31.464 84.256  -2.923  1.00 16.04 ? 883  LEU A O   1 
ATOM   7056 C  CB  . LEU A 1 883  ? 29.140 83.571  -1.487  1.00 14.15 ? 883  LEU A CB  1 
ATOM   7057 C  CG  . LEU A 1 883  ? 27.674 83.221  -1.150  1.00 13.68 ? 883  LEU A CG  1 
ATOM   7058 C  CD1 . LEU A 1 883  ? 27.086 84.208  -0.058  1.00 15.19 ? 883  LEU A CD1 1 
ATOM   7059 C  CD2 . LEU A 1 883  ? 26.834 83.365  -2.419  1.00 15.09 ? 883  LEU A CD2 1 
ATOM   7060 N  N   . ASP A 1 884  ? 32.182 82.126  -2.800  1.00 11.43 ? 884  ASP A N   1 
ATOM   7061 C  CA  . ASP A 1 884  ? 33.581 82.431  -3.043  1.00 11.11 ? 884  ASP A CA  1 
ATOM   7062 C  C   . ASP A 1 884  ? 34.070 81.979  -4.407  1.00 11.24 ? 884  ASP A C   1 
ATOM   7063 O  O   . ASP A 1 884  ? 35.251 81.720  -4.595  1.00 11.56 ? 884  ASP A O   1 
ATOM   7064 C  CB  . ASP A 1 884  ? 34.463 81.819  -1.956  1.00 12.65 ? 884  ASP A CB  1 
ATOM   7065 C  CG  . ASP A 1 884  ? 34.262 80.302  -1.743  1.00 12.82 ? 884  ASP A CG  1 
ATOM   7066 O  OD1 . ASP A 1 884  ? 33.456 79.668  -2.453  1.00 12.00 ? 884  ASP A OD1 1 
ATOM   7067 O  OD2 . ASP A 1 884  ? 34.940 79.801  -0.803  1.00 15.83 ? 884  ASP A OD2 1 
ATOM   7068 N  N   . ASN A 1 885  ? 33.155 81.925  -5.359  1.00 10.00 ? 885  ASN A N   1 
ATOM   7069 C  CA  . ASN A 1 885  ? 33.463 81.530  -6.717  1.00 10.84 ? 885  ASN A CA  1 
ATOM   7070 C  C   . ASN A 1 885  ? 34.529 82.398  -7.348  1.00 11.49 ? 885  ASN A C   1 
ATOM   7071 O  O   . ASN A 1 885  ? 34.636 83.589  -7.027  1.00 12.05 ? 885  ASN A O   1 
ATOM   7072 C  CB  . ASN A 1 885  ? 32.228 81.654  -7.587  1.00 10.93 ? 885  ASN A CB  1 
ATOM   7073 C  CG  . ASN A 1 885  ? 31.039 80.913  -7.019  1.00 10.60 ? 885  ASN A CG  1 
ATOM   7074 O  OD1 . ASN A 1 885  ? 30.710 79.786  -7.464  1.00 12.71 ? 885  ASN A OD1 1 
ATOM   7075 N  ND2 . ASN A 1 885  ? 30.377 81.510  -6.055  1.00 10.38 ? 885  ASN A ND2 1 
ATOM   7076 N  N   . LYS A 1 886  ? 35.312 81.802  -8.231  1.00 10.23 ? 886  LYS A N   1 
ATOM   7077 C  CA  . LYS A 1 886  ? 36.325 82.530  -8.944  1.00 12.55 ? 886  LYS A CA  1 
ATOM   7078 C  C   . LYS A 1 886  ? 36.406 81.943  -10.348 1.00 11.80 ? 886  LYS A C   1 
ATOM   7079 O  O   . LYS A 1 886  ? 36.025 80.799  -10.588 1.00 11.13 ? 886  LYS A O   1 
ATOM   7080 C  CB  . LYS A 1 886  ? 37.659 82.450  -8.207  1.00 15.34 ? 886  LYS A CB  1 
ATOM   7081 C  CG  . LYS A 1 886  ? 38.193 81.033  -8.014  1.00 17.10 ? 886  LYS A CG  1 
ATOM   7082 C  CD  . LYS A 1 886  ? 39.303 80.923  -6.921  1.00 19.51 ? 886  LYS A CD  1 
ATOM   7083 C  CE  . LYS A 1 886  ? 40.585 81.459  -7.469  1.00 20.13 ? 886  LYS A CE  1 
ATOM   7084 N  NZ  . LYS A 1 886  ? 41.747 81.560  -6.506  1.00 20.97 ? 886  LYS A NZ  1 
ATOM   7085 N  N   . PRO A 1 887  ? 36.871 82.718  -11.317 1.00 9.74  ? 887  PRO A N   1 
ATOM   7086 C  CA  . PRO A 1 887  ? 36.966 82.237  -12.688 1.00 9.38  ? 887  PRO A CA  1 
ATOM   7087 C  C   . PRO A 1 887  ? 37.749 80.971  -12.784 1.00 8.50  ? 887  PRO A C   1 
ATOM   7088 O  O   . PRO A 1 887  ? 38.808 80.830  -12.179 1.00 9.48  ? 887  PRO A O   1 
ATOM   7089 C  CB  . PRO A 1 887  ? 37.640 83.404  -13.433 1.00 10.18 ? 887  PRO A CB  1 
ATOM   7090 C  CG  . PRO A 1 887  ? 37.160 84.611  -12.635 1.00 11.70 ? 887  PRO A CG  1 
ATOM   7091 C  CD  . PRO A 1 887  ? 37.187 84.156  -11.208 1.00 10.40 ? 887  PRO A CD  1 
ATOM   7092 N  N   . VAL A 1 888  ? 37.248 80.019  -13.559 1.00 8.40  ? 888  VAL A N   1 
ATOM   7093 C  CA  . VAL A 1 888  ? 37.930 78.743  -13.744 1.00 8.19  ? 888  VAL A CA  1 
ATOM   7094 C  C   . VAL A 1 888  ? 37.837 78.361  -15.200 1.00 7.86  ? 888  VAL A C   1 
ATOM   7095 O  O   . VAL A 1 888  ? 36.795 78.619  -15.884 1.00 8.90  ? 888  VAL A O   1 
ATOM   7096 C  CB  . VAL A 1 888  ? 37.265 77.613  -12.832 1.00 8.28  ? 888  VAL A CB  1 
ATOM   7097 C  CG1 . VAL A 1 888  ? 35.731 77.496  -13.085 1.00 10.02 ? 888  VAL A CG1 1 
ATOM   7098 C  CG2 . VAL A 1 888  ? 37.935 76.301  -13.085 1.00 8.76  ? 888  VAL A CG2 1 
ATOM   7099 N  N   . LEU A 1 889  ? 38.913 77.802  -15.730 1.00 7.68  ? 889  LEU A N   1 
ATOM   7100 C  CA  . LEU A 1 889  ? 38.944 77.312  -17.101 1.00 7.79  ? 889  LEU A CA  1 
ATOM   7101 C  C   . LEU A 1 889  ? 38.730 75.780  -17.131 1.00 8.04  ? 889  LEU A C   1 
ATOM   7102 O  O   . LEU A 1 889  ? 39.626 74.986  -16.818 1.00 8.97  ? 889  LEU A O   1 
ATOM   7103 C  CB  . LEU A 1 889  ? 40.266 77.659  -17.789 1.00 9.43  ? 889  LEU A CB  1 
ATOM   7104 C  CG  . LEU A 1 889  ? 40.345 77.269  -19.286 1.00 9.72  ? 889  LEU A CG  1 
ATOM   7105 C  CD1 . LEU A 1 889  ? 39.412 78.187  -20.096 1.00 12.07 ? 889  LEU A CD1 1 
ATOM   7106 C  CD2 . LEU A 1 889  ? 41.791 77.340  -19.779 1.00 13.50 ? 889  LEU A CD2 1 
ATOM   7107 N  N   . HIS A 1 890  ? 37.508 75.385  -17.472 1.00 6.95  ? 890  HIS A N   1 
ATOM   7108 C  CA  . HIS A 1 890  ? 37.213 73.960  -17.596 1.00 7.13  ? 890  HIS A CA  1 
ATOM   7109 C  C   . HIS A 1 890  ? 37.556 73.474  -18.994 1.00 7.34  ? 890  HIS A C   1 
ATOM   7110 O  O   . HIS A 1 890  ? 37.335 74.214  -19.993 1.00 7.74  ? 890  HIS A O   1 
ATOM   7111 C  CB  . HIS A 1 890  ? 35.723 73.696  -17.380 1.00 7.50  ? 890  HIS A CB  1 
ATOM   7112 C  CG  . HIS A 1 890  ? 35.271 73.899  -15.969 1.00 7.66  ? 890  HIS A CG  1 
ATOM   7113 N  ND1 . HIS A 1 890  ? 36.065 73.520  -14.903 1.00 9.15  ? 890  HIS A ND1 1 
ATOM   7114 C  CD2 . HIS A 1 890  ? 34.097 74.314  -15.441 1.00 9.30  ? 890  HIS A CD2 1 
ATOM   7115 C  CE1 . HIS A 1 890  ? 35.386 73.680  -13.778 1.00 9.58  ? 890  HIS A CE1 1 
ATOM   7116 N  NE2 . HIS A 1 890  ? 34.184 74.162  -14.079 1.00 8.50  ? 890  HIS A NE2 1 
ATOM   7117 N  N   . ILE A 1 891  ? 38.098 72.266  -19.105 1.00 6.48  ? 891  ILE A N   1 
ATOM   7118 C  CA  . ILE A 1 891  ? 38.492 71.711  -20.387 1.00 7.09  ? 891  ILE A CA  1 
ATOM   7119 C  C   . ILE A 1 891  ? 37.841 70.352  -20.621 1.00 6.42  ? 891  ILE A C   1 
ATOM   7120 O  O   . ILE A 1 891  ? 37.564 69.587  -19.690 1.00 6.62  ? 891  ILE A O   1 
ATOM   7121 C  CB  . ILE A 1 891  ? 40.034 71.660  -20.519 1.00 7.02  ? 891  ILE A CB  1 
ATOM   7122 C  CG1 . ILE A 1 891  ? 40.648 70.659  -19.541 1.00 9.50  ? 891  ILE A CG1 1 
ATOM   7123 C  CG2 . ILE A 1 891  ? 40.625 73.047  -20.279 1.00 9.95  ? 891  ILE A CG2 1 
ATOM   7124 C  CD1 . ILE A 1 891  ? 42.202 70.496  -19.775 1.00 10.40 ? 891  ILE A CD1 1 
ATOM   7125 N  N   . TYR A 1 892  ? 37.585 70.089  -21.904 1.00 6.39  ? 892  TYR A N   1 
ATOM   7126 C  CA  . TYR A 1 892  ? 36.924 68.857  -22.346 1.00 6.18  ? 892  TYR A CA  1 
ATOM   7127 C  C   . TYR A 1 892  ? 37.342 68.428  -23.714 1.00 6.14  ? 892  TYR A C   1 
ATOM   7128 O  O   . TYR A 1 892  ? 37.923 69.218  -24.479 1.00 6.90  ? 892  TYR A O   1 
ATOM   7129 C  CB  . TYR A 1 892  ? 35.389 69.077  -22.468 1.00 6.89  ? 892  TYR A CB  1 
ATOM   7130 C  CG  . TYR A 1 892  ? 34.723 69.766  -21.296 1.00 6.10  ? 892  TYR A CG  1 
ATOM   7131 C  CD1 . TYR A 1 892  ? 34.714 71.161  -21.188 1.00 6.70  ? 892  TYR A CD1 1 
ATOM   7132 C  CD2 . TYR A 1 892  ? 34.130 68.998  -20.267 1.00 6.73  ? 892  TYR A CD2 1 
ATOM   7133 C  CE1 . TYR A 1 892  ? 34.126 71.774  -20.082 1.00 7.15  ? 892  TYR A CE1 1 
ATOM   7134 C  CE2 . TYR A 1 892  ? 33.552 69.582  -19.184 1.00 6.85  ? 892  TYR A CE2 1 
ATOM   7135 C  CZ  . TYR A 1 892  ? 33.542 70.974  -19.082 1.00 7.08  ? 892  TYR A CZ  1 
ATOM   7136 O  OH  . TYR A 1 892  ? 32.933 71.533  -17.977 1.00 8.16  ? 892  TYR A OH  1 
ATOM   7137 N  N   . ARG A 1 893  ? 37.056 67.166  -24.026 1.00 6.53  ? 893  ARG A N   1 
ATOM   7138 C  CA  . ARG A 1 893  ? 37.168 66.687  -25.438 1.00 7.41  ? 893  ARG A CA  1 
ATOM   7139 C  C   . ARG A 1 893  ? 35.800 66.079  -25.761 1.00 7.30  ? 893  ARG A C   1 
ATOM   7140 O  O   . ARG A 1 893  ? 35.172 65.444  -24.924 1.00 8.27  ? 893  ARG A O   1 
ATOM   7141 C  CB  . ARG A 1 893  ? 38.221 65.635  -25.678 1.00 6.95  ? 893  ARG A CB  1 
ATOM   7142 C  CG  . ARG A 1 893  ? 39.633 66.174  -25.400 1.00 8.13  ? 893  ARG A CG  1 
ATOM   7143 C  CD  . ARG A 1 893  ? 40.064 67.296  -26.417 1.00 8.82  ? 893  ARG A CD  1 
ATOM   7144 N  NE  . ARG A 1 893  ? 40.242 66.763  -27.764 1.00 9.32  ? 893  ARG A NE  1 
ATOM   7145 C  CZ  . ARG A 1 893  ? 41.316 66.104  -28.206 1.00 9.13  ? 893  ARG A CZ  1 
ATOM   7146 N  NH1 . ARG A 1 893  ? 42.372 65.891  -27.406 1.00 11.12 ? 893  ARG A NH1 1 
ATOM   7147 N  NH2 . ARG A 1 893  ? 41.354 65.645  -29.470 1.00 11.73 ? 893  ARG A NH2 1 
ATOM   7148 N  N   . LEU A 1 894  ? 35.350 66.271  -27.002 1.00 8.33  ? 894  LEU A N   1 
ATOM   7149 C  CA  . LEU A 1 894  ? 34.028 65.785  -27.438 1.00 9.66  ? 894  LEU A CA  1 
ATOM   7150 C  C   . LEU A 1 894  ? 34.251 64.807  -28.593 1.00 9.16  ? 894  LEU A C   1 
ATOM   7151 O  O   . LEU A 1 894  ? 34.760 65.176  -29.634 1.00 10.29 ? 894  LEU A O   1 
ATOM   7152 C  CB  . LEU A 1 894  ? 33.204 66.976  -27.903 1.00 10.42 ? 894  LEU A CB  1 
ATOM   7153 C  CG  . LEU A 1 894  ? 31.773 66.583  -28.298 1.00 11.87 ? 894  LEU A CG  1 
ATOM   7154 C  CD1 . LEU A 1 894  ? 30.984 66.084  -27.107 1.00 14.71 ? 894  LEU A CD1 1 
ATOM   7155 C  CD2 . LEU A 1 894  ? 31.090 67.834  -28.876 1.00 15.22 ? 894  LEU A CD2 1 
ATOM   7156 N  N   . VAL A 1 895  ? 33.900 63.547  -28.363 1.00 9.41  ? 895  VAL A N   1 
ATOM   7157 C  CA  . VAL A 1 895  ? 34.126 62.491  -29.353 1.00 10.16 ? 895  VAL A CA  1 
ATOM   7158 C  C   . VAL A 1 895  ? 32.816 61.848  -29.826 1.00 10.39 ? 895  VAL A C   1 
ATOM   7159 O  O   . VAL A 1 895  ? 32.112 61.157  -29.075 1.00 10.17 ? 895  VAL A O   1 
ATOM   7160 C  CB  . VAL A 1 895  ? 34.984 61.384  -28.720 1.00 10.39 ? 895  VAL A CB  1 
ATOM   7161 C  CG1 . VAL A 1 895  ? 35.352 60.378  -29.801 1.00 13.54 ? 895  VAL A CG1 1 
ATOM   7162 C  CG2 . VAL A 1 895  ? 36.267 61.982  -28.047 1.00 13.12 ? 895  VAL A CG2 1 
ATOM   7163 N  N   . LEU A 1 896  ? 32.458 62.149  -31.075 1.00 10.77 ? 896  LEU A N   1 
ATOM   7164 C  CA  . LEU A 1 896  ? 31.279 61.539  -31.723 1.00 11.15 ? 896  LEU A CA  1 
ATOM   7165 C  C   . LEU A 1 896  ? 31.846 60.404  -32.555 1.00 10.74 ? 896  LEU A C   1 
ATOM   7166 O  O   . LEU A 1 896  ? 32.768 60.587  -33.321 1.00 12.02 ? 896  LEU A O   1 
ATOM   7167 C  CB  . LEU A 1 896  ? 30.606 62.561  -32.648 1.00 11.11 ? 896  LEU A CB  1 
ATOM   7168 C  CG  . LEU A 1 896  ? 29.429 61.913  -33.422 1.00 12.32 ? 896  LEU A CG  1 
ATOM   7169 C  CD1 . LEU A 1 896  ? 28.301 61.649  -32.524 1.00 13.39 ? 896  LEU A CD1 1 
ATOM   7170 C  CD2 . LEU A 1 896  ? 28.946 62.890  -34.488 1.00 13.76 ? 896  LEU A CD2 1 
ATOM   7171 N  N   . GLU A 1 897  ? 31.285 59.192  -32.390 1.00 10.59 ? 897  GLU A N   1 
ATOM   7172 C  CA  . GLU A 1 897  ? 31.798 58.044  -33.129 1.00 12.00 ? 897  GLU A CA  1 
ATOM   7173 C  C   . GLU A 1 897  ? 30.718 57.057  -33.540 1.00 11.71 ? 897  GLU A C   1 
ATOM   7174 O  O   . GLU A 1 897  ? 29.677 56.951  -32.896 1.00 12.12 ? 897  GLU A O   1 
ATOM   7175 C  CB  . GLU A 1 897  ? 32.763 57.240  -32.233 1.00 14.38 ? 897  GLU A CB  1 
ATOM   7176 C  CG  . GLU A 1 897  ? 33.847 58.011  -31.507 1.00 17.01 ? 897  GLU A CG  1 
ATOM   7177 C  CD  . GLU A 1 897  ? 34.506 57.103  -30.400 1.00 16.48 ? 897  GLU A CD  1 
ATOM   7178 O  OE1 . GLU A 1 897  ? 33.899 56.893  -29.311 1.00 18.62 ? 897  GLU A OE1 1 
ATOM   7179 O  OE2 . GLU A 1 897  ? 35.631 56.678  -30.690 1.00 22.15 ? 897  GLU A OE2 1 
ATOM   7180 N  N   . LYS A 1 898  ? 31.016 56.309  -34.608 1.00 12.95 ? 898  LYS A N   1 
ATOM   7181 C  CA  . LYS A 1 898  ? 30.126 55.219  -34.999 1.00 14.11 ? 898  LYS A CA  1 
ATOM   7182 C  C   . LYS A 1 898  ? 30.589 54.006  -34.187 1.00 14.51 ? 898  LYS A C   1 
ATOM   7183 O  O   . LYS A 1 898  ? 31.794 53.700  -34.102 1.00 17.68 ? 898  LYS A O   1 
ATOM   7184 C  CB  . LYS A 1 898  ? 30.276 54.937  -36.493 1.00 16.68 ? 898  LYS A CB  1 
ATOM   7185 C  CG  . LYS A 1 898  ? 29.890 56.072  -37.427 1.00 19.95 ? 898  LYS A CG  1 
ATOM   7186 C  CD  . LYS A 1 898  ? 28.630 56.918  -37.034 1.00 23.86 ? 898  LYS A CD  1 
ATOM   7187 C  CE  . LYS A 1 898  ? 27.297 56.123  -36.829 1.00 24.95 ? 898  LYS A CE  1 
ATOM   7188 N  NZ  . LYS A 1 898  ? 27.115 54.912  -37.694 1.00 27.86 ? 898  LYS A NZ  1 
ATOM   7189 N  N   . VAL A 1 899  ? 29.658 53.308  -33.581 1.00 14.48 ? 899  VAL A N   1 
ATOM   7190 C  CA  . VAL A 1 899  ? 30.027 52.158  -32.769 1.00 14.80 ? 899  VAL A CA  1 
ATOM   7191 C  C   . VAL A 1 899  ? 29.281 50.868  -33.147 1.00 15.31 ? 899  VAL A C   1 
ATOM   7192 O  O   . VAL A 1 899  ? 29.369 49.888  -32.445 1.00 14.75 ? 899  VAL A O   1 
ATOM   7193 C  CB  . VAL A 1 899  ? 29.796 52.453  -31.264 1.00 14.67 ? 899  VAL A CB  1 
ATOM   7194 C  CG1 . VAL A 1 899  ? 30.801 53.546  -30.790 1.00 15.70 ? 899  VAL A CG1 1 
ATOM   7195 C  CG2 . VAL A 1 899  ? 28.391 52.947  -31.030 1.00 14.55 ? 899  VAL A CG2 1 
ATOM   7196 N  N   . ASN A 1 900  ? 28.574 50.856  -34.280 1.00 15.70 ? 900  ASN A N   1 
ATOM   7197 C  CA  . ASN A 1 900  ? 27.854 49.637  -34.626 1.00 17.08 ? 900  ASN A CA  1 
ATOM   7198 C  C   . ASN A 1 900  ? 28.798 48.473  -34.917 1.00 16.20 ? 900  ASN A C   1 
ATOM   7199 O  O   . ASN A 1 900  ? 28.336 47.319  -34.851 1.00 18.34 ? 900  ASN A O   1 
ATOM   7200 C  CB  . ASN A 1 900  ? 26.948 49.853  -35.841 1.00 19.02 ? 900  ASN A CB  1 
ATOM   7201 C  CG  . ASN A 1 900  ? 27.684 50.388  -37.011 1.00 20.64 ? 900  ASN A CG  1 
ATOM   7202 O  OD1 . ASN A 1 900  ? 28.288 51.456  -36.964 1.00 22.45 ? 900  ASN A OD1 1 
ATOM   7203 N  ND2 . ASN A 1 900  ? 27.636 49.633  -38.130 1.00 24.12 ? 900  ASN A ND2 1 
ATOM   7204 N  N   . ASN A 1 901  ? 30.071 48.718  -35.216 1.00 14.90 ? 901  ASN A N   1 
ATOM   7205 C  CA  . ASN A 1 901  ? 30.987 47.610  -35.475 1.00 15.76 ? 901  ASN A CA  1 
ATOM   7206 C  C   . ASN A 1 901  ? 31.797 47.218  -34.237 1.00 14.51 ? 901  ASN A C   1 
ATOM   7207 O  O   . ASN A 1 901  ? 32.578 46.281  -34.277 1.00 15.01 ? 901  ASN A O   1 
ATOM   7208 C  CB  . ASN A 1 901  ? 31.971 47.979  -36.567 1.00 18.64 ? 901  ASN A CB  1 
ATOM   7209 C  CG  . ASN A 1 901  ? 31.336 48.032  -37.914 1.00 21.38 ? 901  ASN A CG  1 
ATOM   7210 O  OD1 . ASN A 1 901  ? 31.588 48.967  -38.686 1.00 26.12 ? 901  ASN A OD1 1 
ATOM   7211 N  ND2 . ASN A 1 901  ? 30.533 47.044  -38.227 1.00 22.68 ? 901  ASN A ND2 1 
ATOM   7212 N  N   . CYS A 1 902  ? 31.571 47.901  -33.125 1.00 13.42 ? 902  CYS A N   1 
ATOM   7213 C  CA  . CYS A 1 902  ? 32.344 47.588  -31.917 1.00 13.49 ? 902  CYS A CA  1 
ATOM   7214 C  C   . CYS A 1 902  ? 31.794 46.398  -31.164 1.00 13.58 ? 902  CYS A C   1 
ATOM   7215 O  O   . CYS A 1 902  ? 30.573 46.221  -31.086 1.00 14.70 ? 902  CYS A O   1 
ATOM   7216 C  CB  . CYS A 1 902  ? 32.309 48.774  -30.951 1.00 14.25 ? 902  CYS A CB  1 
ATOM   7217 S  SG  . CYS A 1 902  ? 33.061 50.316  -31.533 1.00 16.03 ? 902  CYS A SG  1 
ATOM   7218 N  N   . VAL A 1 903  ? 32.674 45.593  -30.585 1.00 12.39 ? 903  VAL A N   1 
ATOM   7219 C  CA  . VAL A 1 903  ? 32.248 44.465  -29.749 1.00 13.14 ? 903  VAL A CA  1 
ATOM   7220 C  C   . VAL A 1 903  ? 31.965 45.050  -28.355 1.00 12.70 ? 903  VAL A C   1 
ATOM   7221 O  O   . VAL A 1 903  ? 32.894 45.393  -27.586 1.00 14.46 ? 903  VAL A O   1 
ATOM   7222 C  CB  . VAL A 1 903  ? 33.371 43.397  -29.706 1.00 13.08 ? 903  VAL A CB  1 
ATOM   7223 C  CG1 . VAL A 1 903  ? 32.955 42.243  -28.781 1.00 13.88 ? 903  VAL A CG1 1 
ATOM   7224 C  CG2 . VAL A 1 903  ? 33.595 42.808  -31.109 1.00 14.32 ? 903  VAL A CG2 1 
ATOM   7225 N  N   . ARG A 1 904  ? 30.703 45.192  -28.033 1.00 12.63 ? 904  ARG A N   1 
ATOM   7226 C  CA  . ARG A 1 904  ? 30.306 45.777  -26.750 1.00 12.27 ? 904  ARG A CA  1 
ATOM   7227 C  C   . ARG A 1 904  ? 29.779 44.721  -25.807 1.00 12.74 ? 904  ARG A C   1 
ATOM   7228 O  O   . ARG A 1 904  ? 29.421 43.597  -26.217 1.00 13.38 ? 904  ARG A O   1 
ATOM   7229 C  CB  . ARG A 1 904  ? 29.190 46.811  -26.978 1.00 13.41 ? 904  ARG A CB  1 
ATOM   7230 C  CG  . ARG A 1 904  ? 29.772 48.081  -27.637 1.00 15.30 ? 904  ARG A CG  1 
ATOM   7231 C  CD  . ARG A 1 904  ? 28.751 49.186  -27.907 1.00 17.59 ? 904  ARG A CD  1 
ATOM   7232 N  NE  . ARG A 1 904  ? 28.007 48.856  -29.095 1.00 17.98 ? 904  ARG A NE  1 
ATOM   7233 C  CZ  . ARG A 1 904  ? 27.008 49.601  -29.578 1.00 19.07 ? 904  ARG A CZ  1 
ATOM   7234 N  NH1 . ARG A 1 904  ? 26.623 50.721  -28.972 1.00 19.48 ? 904  ARG A NH1 1 
ATOM   7235 N  NH2 . ARG A 1 904  ? 26.399 49.187  -30.685 1.00 19.75 ? 904  ARG A NH2 1 
ATOM   7236 N  N   . PRO A 1 905  ? 29.741 45.053  -24.512 1.00 11.36 ? 905  PRO A N   1 
ATOM   7237 C  CA  . PRO A 1 905  ? 29.199 44.121  -23.526 1.00 12.35 ? 905  PRO A CA  1 
ATOM   7238 C  C   . PRO A 1 905  ? 27.713 43.913  -23.862 1.00 12.85 ? 905  PRO A C   1 
ATOM   7239 O  O   . PRO A 1 905  ? 27.071 44.733  -24.527 1.00 12.80 ? 905  PRO A O   1 
ATOM   7240 C  CB  . PRO A 1 905  ? 29.307 44.892  -22.206 1.00 11.02 ? 905  PRO A CB  1 
ATOM   7241 C  CG  . PRO A 1 905  ? 30.458 45.875  -22.470 1.00 10.66 ? 905  PRO A CG  1 
ATOM   7242 C  CD  . PRO A 1 905  ? 30.195 46.321  -23.889 1.00 11.38 ? 905  PRO A CD  1 
ATOM   7243 N  N   . SER A 1 906  ? 27.176 42.787  -23.403 1.00 12.24 ? 906  SER A N   1 
ATOM   7244 C  CA  . SER A 1 906  ? 25.763 42.493  -23.576 1.00 15.47 ? 906  SER A CA  1 
ATOM   7245 C  C   . SER A 1 906  ? 24.905 43.486  -22.770 1.00 15.71 ? 906  SER A C   1 
ATOM   7246 O  O   . SER A 1 906  ? 25.407 44.204  -21.866 1.00 15.64 ? 906  SER A O   1 
ATOM   7247 C  CB  . SER A 1 906  ? 25.515 41.103  -23.040 1.00 17.81 ? 906  SER A CB  1 
ATOM   7248 O  OG  . SER A 1 906  ? 25.182 41.225  -21.666 1.00 22.90 ? 906  SER A OG  1 
ATOM   7249 N  N   . LYS A 1 907  ? 23.615 43.542  -23.060 1.00 16.43 ? 907  LYS A N   1 
ATOM   7250 C  CA  . LYS A 1 907  ? 22.682 44.441  -22.387 1.00 18.19 ? 907  LYS A CA  1 
ATOM   7251 C  C   . LYS A 1 907  ? 22.660 44.253  -20.883 1.00 17.79 ? 907  LYS A C   1 
ATOM   7252 O  O   . LYS A 1 907  ? 22.371 45.205  -20.171 1.00 19.05 ? 907  LYS A O   1 
ATOM   7253 C  CB  . LYS A 1 907  ? 21.266 44.241  -22.959 1.00 21.06 ? 907  LYS A CB  1 
ATOM   7254 C  CG  . LYS A 1 907  ? 21.216 44.540  -24.445 1.00 26.34 ? 907  LYS A CG  1 
ATOM   7255 C  CD  . LYS A 1 907  ? 19.813 44.338  -25.014 1.00 29.85 ? 907  LYS A CD  1 
ATOM   7256 C  CE  . LYS A 1 907  ? 19.688 44.857  -26.437 1.00 32.39 ? 907  LYS A CE  1 
ATOM   7257 N  NZ  . LYS A 1 907  ? 18.265 44.677  -26.910 1.00 34.60 ? 907  LYS A NZ  1 
ATOM   7258 N  N   . LEU A 1 908  ? 22.976 43.070  -20.371 1.00 16.21 ? 908  LEU A N   1 
ATOM   7259 C  CA  . LEU A 1 908  ? 22.947 42.901  -18.907 1.00 16.26 ? 908  LEU A CA  1 
ATOM   7260 C  C   . LEU A 1 908  ? 24.268 43.247  -18.196 1.00 14.17 ? 908  LEU A C   1 
ATOM   7261 O  O   . LEU A 1 908  ? 24.326 43.224  -16.957 1.00 14.87 ? 908  LEU A O   1 
ATOM   7262 C  CB  . LEU A 1 908  ? 22.526 41.458  -18.528 1.00 18.64 ? 908  LEU A CB  1 
ATOM   7263 C  CG  . LEU A 1 908  ? 21.071 41.134  -18.915 1.00 20.22 ? 908  LEU A CG  1 
ATOM   7264 C  CD1 . LEU A 1 908  ? 20.838 39.632  -18.754 1.00 21.10 ? 908  LEU A CD1 1 
ATOM   7265 C  CD2 . LEU A 1 908  ? 20.115 41.920  -18.040 1.00 22.12 ? 908  LEU A CD2 1 
ATOM   7266 N  N   . HIS A 1 909  ? 25.323 43.570  -18.941 1.00 12.18 ? 909  HIS A N   1 
ATOM   7267 C  CA  . HIS A 1 909  ? 26.603 43.868  -18.309 1.00 11.74 ? 909  HIS A CA  1 
ATOM   7268 C  C   . HIS A 1 909  ? 26.546 45.257  -17.661 1.00 10.97 ? 909  HIS A C   1 
ATOM   7269 O  O   . HIS A 1 909  ? 26.038 46.203  -18.259 1.00 11.01 ? 909  HIS A O   1 
ATOM   7270 C  CB  . HIS A 1 909  ? 27.684 43.842  -19.352 1.00 11.72 ? 909  HIS A CB  1 
ATOM   7271 C  CG  . HIS A 1 909  ? 29.033 43.614  -18.796 1.00 11.00 ? 909  HIS A CG  1 
ATOM   7272 N  ND1 . HIS A 1 909  ? 29.702 44.575  -18.060 1.00 11.39 ? 909  HIS A ND1 1 
ATOM   7273 C  CD2 . HIS A 1 909  ? 29.859 42.539  -18.859 1.00 11.81 ? 909  HIS A CD2 1 
ATOM   7274 C  CE1 . HIS A 1 909  ? 30.883 44.101  -17.718 1.00 11.25 ? 909  HIS A CE1 1 
ATOM   7275 N  NE2 . HIS A 1 909  ? 31.016 42.868  -18.202 1.00 12.03 ? 909  HIS A NE2 1 
ATOM   7276 N  N   . PRO A 1 910  ? 27.032 45.381  -16.425 1.00 10.51 ? 910  PRO A N   1 
ATOM   7277 C  CA  . PRO A 1 910  ? 26.972 46.713  -15.780 1.00 9.55  ? 910  PRO A CA  1 
ATOM   7278 C  C   . PRO A 1 910  ? 28.074 47.719  -16.147 1.00 7.98  ? 910  PRO A C   1 
ATOM   7279 O  O   . PRO A 1 910  ? 28.012 48.828  -15.605 1.00 9.06  ? 910  PRO A O   1 
ATOM   7280 C  CB  . PRO A 1 910  ? 27.009 46.419  -14.279 1.00 10.09 ? 910  PRO A CB  1 
ATOM   7281 C  CG  . PRO A 1 910  ? 27.107 44.906  -14.136 1.00 12.62 ? 910  PRO A CG  1 
ATOM   7282 C  CD  . PRO A 1 910  ? 27.422 44.302  -15.479 1.00 10.36 ? 910  PRO A CD  1 
ATOM   7283 N  N   . ALA A 1 911  ? 29.034 47.327  -16.970 1.00 8.49  ? 911  ALA A N   1 
ATOM   7284 C  CA  . ALA A 1 911  ? 30.141 48.232  -17.337 1.00 8.75  ? 911  ALA A CA  1 
ATOM   7285 C  C   . ALA A 1 911  ? 30.024 48.715  -18.759 1.00 8.78  ? 911  ALA A C   1 
ATOM   7286 O  O   . ALA A 1 911  ? 29.286 48.118  -19.609 1.00 10.12 ? 911  ALA A O   1 
ATOM   7287 C  CB  . ALA A 1 911  ? 31.474 47.518  -17.223 1.00 9.34  ? 911  ALA A CB  1 
ATOM   7288 N  N   . GLY A 1 912  ? 30.781 49.775  -19.041 1.00 8.71  ? 912  GLY A N   1 
ATOM   7289 C  CA  . GLY A 1 912  ? 30.976 50.198  -20.419 1.00 9.17  ? 912  GLY A CA  1 
ATOM   7290 C  C   . GLY A 1 912  ? 32.471 50.478  -20.569 1.00 8.61  ? 912  GLY A C   1 
ATOM   7291 O  O   . GLY A 1 912  ? 33.199 50.574  -19.568 1.00 9.30  ? 912  GLY A O   1 
ATOM   7292 N  N   . TYR A 1 913  ? 32.932 50.653  -21.799 1.00 8.64  ? 913  TYR A N   1 
ATOM   7293 C  CA  . TYR A 1 913  ? 34.335 50.860  -22.096 1.00 8.65  ? 913  TYR A CA  1 
ATOM   7294 C  C   . TYR A 1 913  ? 34.488 51.883  -23.199 1.00 9.24  ? 913  TYR A C   1 
ATOM   7295 O  O   . TYR A 1 913  ? 33.677 51.910  -24.150 1.00 9.76  ? 913  TYR A O   1 
ATOM   7296 C  CB  . TYR A 1 913  ? 34.995 49.523  -22.568 1.00 9.75  ? 913  TYR A CB  1 
ATOM   7297 C  CG  . TYR A 1 913  ? 34.972 48.461  -21.472 1.00 8.75  ? 913  TYR A CG  1 
ATOM   7298 C  CD1 . TYR A 1 913  ? 35.863 48.504  -20.431 1.00 8.72  ? 913  TYR A CD1 1 
ATOM   7299 C  CD2 . TYR A 1 913  ? 33.976 47.475  -21.462 1.00 9.76  ? 913  TYR A CD2 1 
ATOM   7300 C  CE1 . TYR A 1 913  ? 35.797 47.645  -19.393 1.00 9.27  ? 913  TYR A CE1 1 
ATOM   7301 C  CE2 . TYR A 1 913  ? 33.868 46.558  -20.408 1.00 9.88  ? 913  TYR A CE2 1 
ATOM   7302 C  CZ  . TYR A 1 913  ? 34.806 46.670  -19.361 1.00 8.63  ? 913  TYR A CZ  1 
ATOM   7303 O  OH  . TYR A 1 913  ? 34.727 45.802  -18.304 1.00 10.75 ? 913  TYR A OH  1 
ATOM   7304 N  N   . LEU A 1 914  ? 35.574 52.634  -23.095 1.00 9.33  ? 914  LEU A N   1 
ATOM   7305 C  CA  . LEU A 1 914  ? 35.893 53.651  -24.083 1.00 9.78  ? 914  LEU A CA  1 
ATOM   7306 C  C   . LEU A 1 914  ? 36.454 53.026  -25.335 1.00 10.10 ? 914  LEU A C   1 
ATOM   7307 O  O   . LEU A 1 914  ? 36.969 51.890  -25.347 1.00 10.68 ? 914  LEU A O   1 
ATOM   7308 C  CB  . LEU A 1 914  ? 36.978 54.624  -23.523 1.00 9.01  ? 914  LEU A CB  1 
ATOM   7309 C  CG  . LEU A 1 914  ? 36.498 55.483  -22.359 1.00 8.47  ? 914  LEU A CG  1 
ATOM   7310 C  CD1 . LEU A 1 914  ? 37.564 56.520  -22.120 1.00 10.42 ? 914  LEU A CD1 1 
ATOM   7311 C  CD2 . LEU A 1 914  ? 35.178 56.207  -22.635 1.00 9.49  ? 914  LEU A CD2 1 
ATOM   7312 N  N   . THR A 1 915  ? 36.353 53.801  -26.413 1.00 9.91  ? 915  THR A N   1 
ATOM   7313 C  CA  . THR A 1 915  ? 37.080 53.455  -27.628 1.00 9.46  ? 915  THR A CA  1 
ATOM   7314 C  C   . THR A 1 915  ? 38.506 54.034  -27.506 1.00 10.24 ? 915  THR A C   1 
ATOM   7315 O  O   . THR A 1 915  ? 38.845 54.858  -26.596 1.00 10.38 ? 915  THR A O   1 
ATOM   7316 C  CB  . THR A 1 915  ? 36.473 54.137  -28.844 1.00 11.05 ? 915  THR A CB  1 
ATOM   7317 O  OG1 . THR A 1 915  ? 36.465 55.555  -28.543 1.00 12.26 ? 915  THR A OG1 1 
ATOM   7318 C  CG2 . THR A 1 915  ? 35.023 53.652  -29.128 1.00 12.13 ? 915  THR A CG2 1 
ATOM   7319 N  N   . SER A 1 916  ? 39.366 53.632  -28.405 1.00 10.42 ? 916  SER A N   1 
ATOM   7320 C  CA  . SER A 1 916  ? 40.715 54.128  -28.470 1.00 11.02 ? 916  SER A CA  1 
ATOM   7321 C  C   . SER A 1 916  ? 40.746 55.670  -28.566 1.00 10.57 ? 916  SER A C   1 
ATOM   7322 O  O   . SER A 1 916  ? 41.471 56.333  -27.812 1.00 10.31 ? 916  SER A O   1 
ATOM   7323 C  CB  . SER A 1 916  ? 41.413 53.576  -29.704 1.00 12.85 ? 916  SER A CB  1 
ATOM   7324 O  OG  . SER A 1 916  ? 42.623 54.263  -29.859 1.00 19.79 ? 916  SER A OG  1 
ATOM   7325 N  N   . ALA A 1 917  ? 39.956 56.256  -29.448 1.00 9.59  ? 917  ALA A N   1 
ATOM   7326 C  CA  . ALA A 1 917  ? 39.978 57.701  -29.568 1.00 9.86  ? 917  ALA A CA  1 
ATOM   7327 C  C   . ALA A 1 917  ? 39.518 58.418  -28.331 1.00 9.67  ? 917  ALA A C   1 
ATOM   7328 O  O   . ALA A 1 917  ? 40.069 59.464  -28.006 1.00 9.32  ? 917  ALA A O   1 
ATOM   7329 C  CB  . ALA A 1 917  ? 39.078 58.139  -30.741 1.00 11.78 ? 917  ALA A CB  1 
ATOM   7330 N  N   . ALA A 1 918  ? 38.503 57.888  -27.628 1.00 9.07  ? 918  ALA A N   1 
ATOM   7331 C  CA  . ALA A 1 918  ? 38.048 58.600  -26.430 1.00 8.98  ? 918  ALA A CA  1 
ATOM   7332 C  C   . ALA A 1 918  ? 39.082 58.450  -25.324 1.00 8.53  ? 918  ALA A C   1 
ATOM   7333 O  O   . ALA A 1 918  ? 39.292 59.409  -24.528 1.00 8.63  ? 918  ALA A O   1 
ATOM   7334 C  CB  . ALA A 1 918  ? 36.706 58.067  -26.022 1.00 9.13  ? 918  ALA A CB  1 
ATOM   7335 N  N   . HIS A 1 919  ? 39.689 57.273  -25.195 1.00 7.55  ? 919  HIS A N   1 
ATOM   7336 C  CA  . HIS A 1 919  ? 40.739 57.104  -24.184 1.00 8.53  ? 919  HIS A CA  1 
ATOM   7337 C  C   . HIS A 1 919  ? 41.912 58.049  -24.472 1.00 8.18  ? 919  HIS A C   1 
ATOM   7338 O  O   . HIS A 1 919  ? 42.424 58.714  -23.530 1.00 8.67  ? 919  HIS A O   1 
ATOM   7339 C  CB  . HIS A 1 919  ? 41.200 55.645  -24.182 1.00 9.77  ? 919  HIS A CB  1 
ATOM   7340 C  CG  . HIS A 1 919  ? 42.353 55.399  -23.260 1.00 10.38 ? 919  HIS A CG  1 
ATOM   7341 N  ND1 . HIS A 1 919  ? 43.606 55.051  -23.710 1.00 13.68 ? 919  HIS A ND1 1 
ATOM   7342 C  CD2 . HIS A 1 919  ? 42.436 55.490  -21.911 1.00 11.12 ? 919  HIS A CD2 1 
ATOM   7343 C  CE1 . HIS A 1 919  ? 44.423 54.922  -22.673 1.00 12.99 ? 919  HIS A CE1 1 
ATOM   7344 N  NE2 . HIS A 1 919  ? 43.747 55.195  -21.581 1.00 12.75 ? 919  HIS A NE2 1 
ATOM   7345 N  N   . LYS A 1 920  ? 42.364 58.131  -25.727 1.00 8.62  ? 920  LYS A N   1 
ATOM   7346 C  CA  . LYS A 1 920  ? 43.462 59.046  -26.030 1.00 9.53  ? 920  LYS A CA  1 
ATOM   7347 C  C   . LYS A 1 920  ? 43.049 60.493  -25.747 1.00 8.41  ? 920  LYS A C   1 
ATOM   7348 O  O   . LYS A 1 920  ? 43.881 61.280  -25.277 1.00 8.57  ? 920  LYS A O   1 
ATOM   7349 C  CB  . LYS A 1 920  ? 43.914 58.871  -27.470 1.00 11.54 ? 920  LYS A CB  1 
ATOM   7350 C  CG  . LYS A 1 920  ? 44.754 57.615  -27.604 1.00 14.42 ? 920  LYS A CG  1 
ATOM   7351 C  CD  . LYS A 1 920  ? 45.601 57.631  -28.915 1.00 17.82 ? 920  LYS A CD  1 
ATOM   7352 C  CE  . LYS A 1 920  ? 46.517 56.418  -29.039 1.00 19.58 ? 920  LYS A CE  1 
ATOM   7353 N  NZ  . LYS A 1 920  ? 47.705 56.487  -28.152 1.00 17.58 ? 920  LYS A NZ  1 
ATOM   7354 N  N   . ALA A 1 921  ? 41.798 60.848  -26.038 1.00 8.04  ? 921  ALA A N   1 
ATOM   7355 C  CA  . ALA A 1 921  ? 41.334 62.224  -25.768 1.00 8.43  ? 921  ALA A CA  1 
ATOM   7356 C  C   . ALA A 1 921  ? 41.407 62.494  -24.248 1.00 7.80  ? 921  ALA A C   1 
ATOM   7357 O  O   . ALA A 1 921  ? 41.776 63.597  -23.820 1.00 8.34  ? 921  ALA A O   1 
ATOM   7358 C  CB  . ALA A 1 921  ? 39.886 62.403  -26.338 1.00 7.77  ? 921  ALA A CB  1 
ATOM   7359 N  N   . SER A 1 922  ? 41.035 61.504  -23.435 1.00 7.52  ? 922  SER A N   1 
ATOM   7360 C  CA  . SER A 1 922  ? 41.115 61.688  -21.979 1.00 7.25  ? 922  SER A CA  1 
ATOM   7361 C  C   . SER A 1 922  ? 42.572 61.888  -21.556 1.00 8.03  ? 922  SER A C   1 
ATOM   7362 O  O   . SER A 1 922  ? 42.843 62.772  -20.724 1.00 8.78  ? 922  SER A O   1 
ATOM   7363 C  CB  . SER A 1 922  ? 40.518 60.444  -21.291 1.00 7.35  ? 922  SER A CB  1 
ATOM   7364 O  OG  . SER A 1 922  ? 40.655 60.616  -19.864 1.00 7.69  ? 922  SER A OG  1 
ATOM   7365 N  N   . GLN A 1 923  ? 43.478 61.080  -22.095 1.00 7.75  ? 923  GLN A N   1 
ATOM   7366 C  CA  . GLN A 1 923  ? 44.918 61.235  -21.796 1.00 7.64  ? 923  GLN A CA  1 
ATOM   7367 C  C   . GLN A 1 923  ? 45.418 62.626  -22.215 1.00 8.07  ? 923  GLN A C   1 
ATOM   7368 O  O   . GLN A 1 923  ? 46.250 63.201  -21.542 1.00 8.53  ? 923  GLN A O   1 
ATOM   7369 C  CB  . GLN A 1 923  ? 45.734 60.149  -22.513 1.00 8.10  ? 923  GLN A CB  1 
ATOM   7370 C  CG  . GLN A 1 923  ? 45.481 58.763  -21.961 1.00 9.07  ? 923  GLN A CG  1 
ATOM   7371 C  CD  . GLN A 1 923  ? 46.413 57.760  -22.567 1.00 9.45  ? 923  GLN A CD  1 
ATOM   7372 O  OE1 . GLN A 1 923  ? 46.564 57.706  -23.796 1.00 10.93 ? 923  GLN A OE1 1 
ATOM   7373 N  NE2 . GLN A 1 923  ? 47.055 56.949  -21.703 1.00 9.62  ? 923  GLN A NE2 1 
ATOM   7374 N  N   . SER A 1 924  ? 44.895 63.165  -23.314 1.00 8.33  ? 924  SER A N   1 
ATOM   7375 C  CA  . SER A 1 924  ? 45.294 64.480  -23.788 1.00 8.45  ? 924  SER A CA  1 
ATOM   7376 C  C   . SER A 1 924  ? 44.931 65.537  -22.738 1.00 9.20  ? 924  SER A C   1 
ATOM   7377 O  O   A SER A 1 924  ? 45.668 66.496  -22.538 0.50 10.46 ? 924  SER A O   1 
ATOM   7378 O  O   B SER A 1 924  ? 45.488 66.673  -22.692 0.50 8.24  ? 924  SER A O   1 
ATOM   7379 C  CB  A SER A 1 924  ? 44.588 64.808  -25.113 0.50 8.50  ? 924  SER A CB  1 
ATOM   7380 C  CB  B SER A 1 924  ? 44.812 64.817  -25.121 0.50 7.78  ? 924  SER A CB  1 
ATOM   7381 O  OG  A SER A 1 924  ? 43.269 65.314  -24.961 0.50 10.93 ? 924  SER A OG  1 
ATOM   7382 O  OG  B SER A 1 924  ? 45.396 63.974  -26.099 0.50 7.60  ? 924  SER A OG  1 
ATOM   7383 N  N   . LEU A 1 925  ? 43.823 65.340  -22.037 1.00 8.41  ? 925  LEU A N   1 
ATOM   7384 C  CA  . LEU A 1 925  ? 43.373 66.302  -21.039 1.00 8.25  ? 925  LEU A CA  1 
ATOM   7385 C  C   . LEU A 1 925  ? 44.123 66.142  -19.698 1.00 9.13  ? 925  LEU A C   1 
ATOM   7386 O  O   . LEU A 1 925  ? 44.504 67.146  -19.057 1.00 10.40 ? 925  LEU A O   1 
ATOM   7387 C  CB  . LEU A 1 925  ? 41.872 66.106  -20.740 1.00 8.12  ? 925  LEU A CB  1 
ATOM   7388 C  CG  . LEU A 1 925  ? 40.961 66.421  -21.927 1.00 6.70  ? 925  LEU A CG  1 
ATOM   7389 C  CD1 . LEU A 1 925  ? 39.517 66.148  -21.482 1.00 8.52  ? 925  LEU A CD1 1 
ATOM   7390 C  CD2 . LEU A 1 925  ? 41.111 67.897  -22.361 1.00 9.34  ? 925  LEU A CD2 1 
ATOM   7391 N  N   . LEU A 1 926  ? 44.325 64.881  -19.300 1.00 7.67  ? 926  LEU A N   1 
ATOM   7392 C  CA  . LEU A 1 926  ? 44.899 64.637  -17.969 1.00 7.45  ? 926  LEU A CA  1 
ATOM   7393 C  C   . LEU A 1 926  ? 46.381 64.610  -17.928 1.00 7.87  ? 926  LEU A C   1 
ATOM   7394 O  O   . LEU A 1 926  ? 46.950 65.014  -16.890 1.00 8.34  ? 926  LEU A O   1 
ATOM   7395 C  CB  . LEU A 1 926  ? 44.325 63.347  -17.340 1.00 8.58  ? 926  LEU A CB  1 
ATOM   7396 C  CG  . LEU A 1 926  ? 42.776 63.415  -17.135 1.00 11.05 ? 926  LEU A CG  1 
ATOM   7397 C  CD1 . LEU A 1 926  ? 42.326 62.041  -16.561 1.00 11.32 ? 926  LEU A CD1 1 
ATOM   7398 C  CD2 . LEU A 1 926  ? 42.407 64.594  -16.183 1.00 13.55 ? 926  LEU A CD2 1 
ATOM   7399 N  N   . ASP A 1 927  ? 47.005 64.139  -18.988 1.00 7.00  ? 927  ASP A N   1 
ATOM   7400 C  CA  . ASP A 1 927  ? 48.476 64.056  -19.023 1.00 7.33  ? 927  ASP A CA  1 
ATOM   7401 C  C   . ASP A 1 927  ? 49.052 64.596  -20.322 1.00 7.13  ? 927  ASP A C   1 
ATOM   7402 O  O   . ASP A 1 927  ? 49.619 63.861  -21.121 1.00 7.74  ? 927  ASP A O   1 
ATOM   7403 C  CB  . ASP A 1 927  ? 48.947 62.608  -18.730 1.00 7.99  ? 927  ASP A CB  1 
ATOM   7404 C  CG  . ASP A 1 927  ? 48.606 62.184  -17.299 1.00 7.95  ? 927  ASP A CG  1 
ATOM   7405 O  OD1 . ASP A 1 927  ? 49.341 62.576  -16.346 1.00 7.92  ? 927  ASP A OD1 1 
ATOM   7406 O  OD2 . ASP A 1 927  ? 47.575 61.508  -17.154 1.00 9.72  ? 927  ASP A OD2 1 
ATOM   7407 N  N   . PRO A 1 928  ? 48.879 65.893  -20.529 1.00 7.49  ? 928  PRO A N   1 
ATOM   7408 C  CA  . PRO A 1 928  ? 49.395 66.547  -21.749 1.00 8.01  ? 928  PRO A CA  1 
ATOM   7409 C  C   . PRO A 1 928  ? 50.921 66.568  -21.741 1.00 8.24  ? 928  PRO A C   1 
ATOM   7410 O  O   . PRO A 1 928  ? 51.573 66.293  -20.734 1.00 8.29  ? 928  PRO A O   1 
ATOM   7411 C  CB  . PRO A 1 928  ? 48.863 67.977  -21.626 1.00 9.53  ? 928  PRO A CB  1 
ATOM   7412 C  CG  . PRO A 1 928  ? 48.853 68.229  -20.129 1.00 10.62 ? 928  PRO A CG  1 
ATOM   7413 C  CD  . PRO A 1 928  ? 48.331 66.874  -19.569 1.00 9.50  ? 928  PRO A CD  1 
ATOM   7414 N  N   . LEU A 1 929  ? 51.504 66.863  -22.875 1.00 7.67  ? 929  LEU A N   1 
ATOM   7415 C  CA  . LEU A 1 929  ? 52.934 67.143  -22.888 1.00 7.68  ? 929  LEU A CA  1 
ATOM   7416 C  C   . LEU A 1 929  ? 53.232 68.341  -21.981 1.00 7.80  ? 929  LEU A C   1 
ATOM   7417 O  O   . LEU A 1 929  ? 52.476 69.299  -21.911 1.00 9.42  ? 929  LEU A O   1 
ATOM   7418 C  CB  . LEU A 1 929  ? 53.410 67.499  -24.327 1.00 8.43  ? 929  LEU A CB  1 
ATOM   7419 C  CG  . LEU A 1 929  ? 53.188 66.441  -25.375 1.00 8.43  ? 929  LEU A CG  1 
ATOM   7420 C  CD1 . LEU A 1 929  ? 53.739 67.049  -26.687 1.00 10.36 ? 929  LEU A CD1 1 
ATOM   7421 C  CD2 . LEU A 1 929  ? 54.005 65.156  -25.060 1.00 8.33  ? 929  LEU A CD2 1 
ATOM   7422 N  N   . ASP A 1 930  ? 54.340 68.271  -21.263 1.00 7.54  ? 930  ASP A N   1 
ATOM   7423 C  CA  . ASP A 1 930  ? 54.808 69.399  -20.449 1.00 7.10  ? 930  ASP A CA  1 
ATOM   7424 C  C   . ASP A 1 930  ? 55.763 70.221  -21.307 1.00 7.55  ? 930  ASP A C   1 
ATOM   7425 O  O   . ASP A 1 930  ? 56.522 69.682  -22.134 1.00 9.29  ? 930  ASP A O   1 
ATOM   7426 C  CB  . ASP A 1 930  ? 55.538 68.878  -19.204 1.00 8.24  ? 930  ASP A CB  1 
ATOM   7427 C  CG  . ASP A 1 930  ? 54.745 67.844  -18.488 1.00 8.54  ? 930  ASP A CG  1 
ATOM   7428 O  OD1 . ASP A 1 930  ? 53.650 68.249  -18.009 1.00 11.20 ? 930  ASP A OD1 1 
ATOM   7429 O  OD2 . ASP A 1 930  ? 55.164 66.663  -18.436 1.00 8.91  ? 930  ASP A OD2 1 
ATOM   7430 N  N   . LYS A 1 931  ? 55.745 71.528  -21.126 1.00 7.57  ? 931  LYS A N   1 
ATOM   7431 C  CA  . LYS A 1 931  ? 56.559 72.455  -21.931 1.00 7.30  ? 931  LYS A CA  1 
ATOM   7432 C  C   . LYS A 1 931  ? 57.471 73.239  -21.061 1.00 8.03  ? 931  LYS A C   1 
ATOM   7433 O  O   . LYS A 1 931  ? 57.030 73.841  -20.068 1.00 9.98  ? 931  LYS A O   1 
ATOM   7434 C  CB  . LYS A 1 931  ? 55.607 73.413  -22.676 1.00 8.66  ? 931  LYS A CB  1 
ATOM   7435 C  CG  . LYS A 1 931  ? 54.643 72.747  -23.703 1.00 11.23 ? 931  LYS A CG  1 
ATOM   7436 C  CD  . LYS A 1 931  ? 53.706 73.789  -24.336 1.00 13.92 ? 931  LYS A CD  1 
ATOM   7437 C  CE  . LYS A 1 931  ? 52.743 74.386  -23.326 1.00 15.65 ? 931  LYS A CE  1 
ATOM   7438 N  NZ  . LYS A 1 931  ? 52.051 75.465  -23.937 1.00 16.11 ? 931  LYS A NZ  1 
ATOM   7439 N  N   . PHE A 1 932  ? 58.740 73.316  -21.456 1.00 7.47  ? 932  PHE A N   1 
ATOM   7440 C  CA  . PHE A 1 932  ? 59.777 74.026  -20.712 1.00 7.29  ? 932  PHE A CA  1 
ATOM   7441 C  C   . PHE A 1 932  ? 60.445 75.075  -21.593 1.00 6.89  ? 932  PHE A C   1 
ATOM   7442 O  O   . PHE A 1 932  ? 60.788 74.754  -22.719 1.00 8.79  ? 932  PHE A O   1 
ATOM   7443 C  CB  . PHE A 1 932  ? 60.838 73.037  -20.230 1.00 8.57  ? 932  PHE A CB  1 
ATOM   7444 C  CG  . PHE A 1 932  ? 60.326 71.959  -19.333 1.00 8.64  ? 932  PHE A CG  1 
ATOM   7445 C  CD1 . PHE A 1 932  ? 59.724 70.806  -19.844 1.00 8.95  ? 932  PHE A CD1 1 
ATOM   7446 C  CD2 . PHE A 1 932  ? 60.505 72.091  -17.955 1.00 10.16 ? 932  PHE A CD2 1 
ATOM   7447 C  CE1 . PHE A 1 932  ? 59.294 69.756  -19.006 1.00 8.01  ? 932  PHE A CE1 1 
ATOM   7448 C  CE2 . PHE A 1 932  ? 60.090 71.053  -17.080 1.00 9.96  ? 932  PHE A CE2 1 
ATOM   7449 C  CZ  . PHE A 1 932  ? 59.487 69.892  -17.607 1.00 9.89  ? 932  PHE A CZ  1 
ATOM   7450 N  N   . ILE A 1 933  ? 60.633 76.288  -21.106 1.00 8.19  ? 933  ILE A N   1 
ATOM   7451 C  CA  . ILE A 1 933  ? 61.305 77.358  -21.877 1.00 8.27  ? 933  ILE A CA  1 
ATOM   7452 C  C   . ILE A 1 933  ? 62.655 77.566  -21.198 1.00 8.35  ? 933  ILE A C   1 
ATOM   7453 O  O   . ILE A 1 933  ? 62.719 77.855  -19.982 1.00 8.48  ? 933  ILE A O   1 
ATOM   7454 C  CB  . ILE A 1 933  ? 60.491 78.659  -21.798 1.00 8.82  ? 933  ILE A CB  1 
ATOM   7455 C  CG1 . ILE A 1 933  ? 59.070 78.415  -22.343 1.00 8.75  ? 933  ILE A CG1 1 
ATOM   7456 C  CG2 . ILE A 1 933  ? 61.227 79.765  -22.572 1.00 8.79  ? 933  ILE A CG2 1 
ATOM   7457 C  CD1 . ILE A 1 933  ? 58.158 79.636  -22.146 1.00 10.09 ? 933  ILE A CD1 1 
ATOM   7458 N  N   . PHE A 1 934  ? 63.758 77.413  -21.939 1.00 7.74  ? 934  PHE A N   1 
ATOM   7459 C  CA  . PHE A 1 934  ? 65.074 77.618  -21.327 1.00 9.01  ? 934  PHE A CA  1 
ATOM   7460 C  C   . PHE A 1 934  ? 65.162 79.091  -20.862 1.00 9.00  ? 934  PHE A C   1 
ATOM   7461 O  O   . PHE A 1 934  ? 64.850 80.023  -21.610 1.00 10.54 ? 934  PHE A O   1 
ATOM   7462 C  CB  . PHE A 1 934  ? 66.194 77.280  -22.338 1.00 10.31 ? 934  PHE A CB  1 
ATOM   7463 C  CG  . PHE A 1 934  ? 67.569 77.291  -21.741 1.00 10.41 ? 934  PHE A CG  1 
ATOM   7464 C  CD1 . PHE A 1 934  ? 67.967 76.289  -20.895 1.00 10.79 ? 934  PHE A CD1 1 
ATOM   7465 C  CD2 . PHE A 1 934  ? 68.442 78.360  -21.989 1.00 11.85 ? 934  PHE A CD2 1 
ATOM   7466 C  CE1 . PHE A 1 934  ? 69.224 76.318  -20.278 1.00 13.40 ? 934  PHE A CE1 1 
ATOM   7467 C  CE2 . PHE A 1 934  ? 69.697 78.412  -21.391 1.00 12.85 ? 934  PHE A CE2 1 
ATOM   7468 C  CZ  . PHE A 1 934  ? 70.097 77.396  -20.534 1.00 14.12 ? 934  PHE A CZ  1 
ATOM   7469 N  N   . ALA A 1 935  ? 65.582 79.311  -19.611 1.00 9.74  ? 935  ALA A N   1 
ATOM   7470 C  CA  . ALA A 1 935  ? 65.536 80.666  -19.075 1.00 11.62 ? 935  ALA A CA  1 
ATOM   7471 C  C   . ALA A 1 935  ? 66.676 81.611  -19.503 1.00 13.80 ? 935  ALA A C   1 
ATOM   7472 O  O   . ALA A 1 935  ? 66.428 82.829  -19.798 1.00 17.46 ? 935  ALA A O   1 
ATOM   7473 C  CB  . ALA A 1 935  ? 65.463 80.572  -17.537 1.00 14.10 ? 935  ALA A CB  1 
ATOM   7474 N  N   . GLU A 1 936  ? 67.883 81.098  -19.605 1.00 13.13 ? 936  GLU A N   1 
ATOM   7475 C  CA  . GLU A 1 936  ? 69.057 81.918  -19.946 1.00 13.74 ? 936  GLU A CA  1 
ATOM   7476 C  C   . GLU A 1 936  ? 69.162 82.119  -21.461 1.00 13.04 ? 936  GLU A C   1 
ATOM   7477 O  O   . GLU A 1 936  ? 68.380 81.541  -22.248 1.00 13.73 ? 936  GLU A O   1 
ATOM   7478 C  CB  . GLU A 1 936  ? 70.339 81.246  -19.445 1.00 16.35 ? 936  GLU A CB  1 
ATOM   7479 C  CG  . GLU A 1 936  ? 70.480 80.958  -17.912 1.00 21.13 ? 936  GLU A CG  1 
ATOM   7480 C  CD  . GLU A 1 936  ? 71.609 79.870  -17.612 1.00 23.20 ? 936  GLU A CD  1 
ATOM   7481 O  OE1 . GLU A 1 936  ? 71.432 78.635  -17.860 1.00 22.25 ? 936  GLU A OE1 1 
ATOM   7482 O  OE2 . GLU A 1 936  ? 72.720 80.244  -17.150 1.00 25.89 ? 936  GLU A OE2 1 
ATOM   7483 N  N   . ASN A 1 937  ? 70.160 82.879  -21.890 1.00 13.19 ? 937  ASN A N   1 
ATOM   7484 C  CA  . ASN A 1 937  ? 70.265 83.122  -23.306 1.00 12.65 ? 937  ASN A CA  1 
ATOM   7485 C  C   . ASN A 1 937  ? 70.854 81.976  -24.101 1.00 12.46 ? 937  ASN A C   1 
ATOM   7486 O  O   . ASN A 1 937  ? 70.465 81.768  -25.260 1.00 12.91 ? 937  ASN A O   1 
ATOM   7487 C  CB  . ASN A 1 937  ? 71.097 84.386  -23.559 1.00 14.76 ? 937  ASN A CB  1 
ATOM   7488 C  CG  . ASN A 1 937  ? 70.370 85.654  -23.170 1.00 17.50 ? 937  ASN A CG  1 
ATOM   7489 O  OD1 . ASN A 1 937  ? 69.130 85.688  -23.020 1.00 15.99 ? 937  ASN A OD1 1 
ATOM   7490 N  ND2 . ASN A 1 937  ? 71.149 86.730  -23.021 1.00 20.25 ? 937  ASN A ND2 1 
ATOM   7491 N  N   . GLU A 1 938  ? 71.809 81.251  -23.508 1.00 13.07 ? 938  GLU A N   1 
ATOM   7492 C  CA  . GLU A 1 938  ? 72.409 80.154  -24.246 1.00 15.15 ? 938  GLU A CA  1 
ATOM   7493 C  C   . GLU A 1 938  ? 72.505 78.913  -23.380 1.00 13.56 ? 938  GLU A C   1 
ATOM   7494 O  O   . GLU A 1 938  ? 72.940 78.978  -22.255 1.00 14.13 ? 938  GLU A O   1 
ATOM   7495 C  CB  . GLU A 1 938  ? 73.819 80.516  -24.741 1.00 17.82 ? 938  GLU A CB  1 
ATOM   7496 C  CG  . GLU A 1 938  ? 74.454 79.345  -25.457 1.00 23.34 ? 938  GLU A CG  1 
ATOM   7497 C  CD  . GLU A 1 938  ? 75.695 79.696  -26.255 1.00 25.78 ? 938  GLU A CD  1 
ATOM   7498 O  OE1 . GLU A 1 938  ? 76.394 80.674  -25.906 1.00 29.47 ? 938  GLU A OE1 1 
ATOM   7499 O  OE2 . GLU A 1 938  ? 75.969 78.947  -27.229 1.00 28.82 ? 938  GLU A OE2 1 
ATOM   7500 N  N   . TRP A 1 939  ? 72.103 77.778  -23.946 1.00 14.64 ? 939  TRP A N   1 
ATOM   7501 C  CA  . TRP A 1 939  ? 72.181 76.512  -23.221 1.00 14.58 ? 939  TRP A CA  1 
ATOM   7502 C  C   . TRP A 1 939  ? 73.406 75.736  -23.735 1.00 15.34 ? 939  TRP A C   1 
ATOM   7503 O  O   . TRP A 1 939  ? 73.331 75.097  -24.773 1.00 17.08 ? 939  TRP A O   1 
ATOM   7504 C  CB  . TRP A 1 939  ? 70.865 75.762  -23.477 1.00 13.90 ? 939  TRP A CB  1 
ATOM   7505 C  CG  . TRP A 1 939  ? 70.756 74.377  -22.832 1.00 11.56 ? 939  TRP A CG  1 
ATOM   7506 C  CD1 . TRP A 1 939  ? 71.643 73.745  -21.975 1.00 11.79 ? 939  TRP A CD1 1 
ATOM   7507 C  CD2 . TRP A 1 939  ? 69.679 73.478  -23.035 1.00 11.43 ? 939  TRP A CD2 1 
ATOM   7508 N  NE1 . TRP A 1 939  ? 71.154 72.494  -21.643 1.00 10.94 ? 939  TRP A NE1 1 
ATOM   7509 C  CE2 . TRP A 1 939  ? 69.952 72.308  -22.290 1.00 11.35 ? 939  TRP A CE2 1 
ATOM   7510 C  CE3 . TRP A 1 939  ? 68.495 73.548  -23.788 1.00 10.89 ? 939  TRP A CE3 1 
ATOM   7511 C  CZ2 . TRP A 1 939  ? 69.089 71.217  -22.281 1.00 11.84 ? 939  TRP A CZ2 1 
ATOM   7512 C  CZ3 . TRP A 1 939  ? 67.626 72.476  -23.786 1.00 11.87 ? 939  TRP A CZ3 1 
ATOM   7513 C  CH2 . TRP A 1 939  ? 67.929 71.309  -23.036 1.00 11.23 ? 939  TRP A CH2 1 
ATOM   7514 N  N   . ILE A 1 940  ? 74.506 75.806  -22.986 1.00 17.24 ? 940  ILE A N   1 
ATOM   7515 C  CA  . ILE A 1 940  ? 75.713 75.101  -23.449 1.00 18.83 ? 940  ILE A CA  1 
ATOM   7516 C  C   . ILE A 1 940  ? 75.595 73.579  -23.192 1.00 17.96 ? 940  ILE A C   1 
ATOM   7517 O  O   . ILE A 1 940  ? 75.162 73.152  -22.130 1.00 18.58 ? 940  ILE A O   1 
ATOM   7518 C  CB  . ILE A 1 940  ? 76.966 75.695  -22.780 1.00 20.37 ? 940  ILE A CB  1 
ATOM   7519 C  CG1 . ILE A 1 940  ? 77.165 77.142  -23.268 1.00 22.38 ? 940  ILE A CG1 1 
ATOM   7520 C  CG2 . ILE A 1 940  ? 78.200 74.832  -23.120 1.00 21.28 ? 940  ILE A CG2 1 
ATOM   7521 C  CD1 . ILE A 1 940  ? 77.926 78.000  -22.288 1.00 25.72 ? 940  ILE A CD1 1 
ATOM   7522 N  N   . GLY A 1 941  ? 75.930 72.790  -24.195 1.00 17.88 ? 941  GLY A N   1 
ATOM   7523 C  CA  . GLY A 1 941  ? 75.840 71.339  -24.030 1.00 16.78 ? 941  GLY A CA  1 
ATOM   7524 C  C   . GLY A 1 941  ? 74.444 70.746  -24.262 1.00 16.68 ? 941  GLY A C   1 
ATOM   7525 O  O   . GLY A 1 941  ? 74.217 69.551  -23.982 1.00 15.63 ? 941  GLY A O   1 
ATOM   7526 N  N   . ALA A 1 942  ? 73.519 71.542  -24.799 1.00 15.66 ? 942  ALA A N   1 
ATOM   7527 C  CA  . ALA A 1 942  ? 72.158 71.060  -25.054 1.00 16.30 ? 942  ALA A CA  1 
ATOM   7528 C  C   . ALA A 1 942  ? 72.084 69.846  -25.954 1.00 15.91 ? 942  ALA A C   1 
ATOM   7529 O  O   . ALA A 1 942  ? 72.794 69.756  -26.961 1.00 17.44 ? 942  ALA A O   1 
ATOM   7530 C  CB  . ALA A 1 942  ? 71.311 72.176  -25.675 1.00 16.48 ? 942  ALA A CB  1 
ATOM   7531 N  N   . GLN A 1 943  ? 71.213 68.902  -25.604 1.00 15.35 ? 943  GLN A N   1 
ATOM   7532 C  CA  . GLN A 1 943  ? 70.984 67.711  -26.391 1.00 14.47 ? 943  GLN A CA  1 
ATOM   7533 C  C   . GLN A 1 943  ? 69.561 67.737  -26.927 1.00 13.36 ? 943  GLN A C   1 
ATOM   7534 O  O   . GLN A 1 943  ? 68.675 68.408  -26.332 1.00 14.77 ? 943  GLN A O   1 
ATOM   7535 C  CB  . GLN A 1 943  ? 71.185 66.446  -25.553 1.00 17.14 ? 943  GLN A CB  1 
ATOM   7536 C  CG  . GLN A 1 943  ? 72.576 66.471  -24.929 1.00 20.50 ? 943  GLN A CG  1 
ATOM   7537 C  CD  . GLN A 1 943  ? 72.850 65.226  -24.129 1.00 22.52 ? 943  GLN A CD  1 
ATOM   7538 O  OE1 . GLN A 1 943  ? 71.966 64.752  -23.401 1.00 25.82 ? 943  GLN A OE1 1 
ATOM   7539 N  NE2 . GLN A 1 943  ? 74.083 64.687  -24.238 1.00 25.10 ? 943  GLN A NE2 1 
ATOM   7540 N  N   . GLY A 1 944  ? 69.303 67.026  -28.013 1.00 13.27 ? 944  GLY A N   1 
ATOM   7541 C  CA  . GLY A 1 944  ? 68.029 67.091  -28.669 1.00 13.65 ? 944  GLY A CA  1 
ATOM   7542 C  C   . GLY A 1 944  ? 66.930 66.159  -28.253 1.00 13.05 ? 944  GLY A C   1 
ATOM   7543 O  O   . GLY A 1 944  ? 65.741 66.390  -28.542 1.00 13.58 ? 944  GLY A O   1 
ATOM   7544 N  N   . GLN A 1 945  ? 67.297 65.097  -27.546 1.00 12.76 ? 945  GLN A N   1 
ATOM   7545 C  CA  . GLN A 1 945  ? 66.283 64.112  -27.199 1.00 13.12 ? 945  GLN A CA  1 
ATOM   7546 C  C   . GLN A 1 945  ? 66.715 63.223  -26.063 1.00 13.07 ? 945  GLN A C   1 
ATOM   7547 O  O   . GLN A 1 945  ? 67.911 63.015  -25.820 1.00 13.90 ? 945  GLN A O   1 
ATOM   7548 C  CB  . GLN A 1 945  ? 65.988 63.265  -28.440 1.00 13.80 ? 945  GLN A CB  1 
ATOM   7549 C  CG  . GLN A 1 945  ? 64.738 62.355  -28.399 1.00 16.30 ? 945  GLN A CG  1 
ATOM   7550 C  CD  . GLN A 1 945  ? 64.686 61.395  -29.628 1.00 17.19 ? 945  GLN A CD  1 
ATOM   7551 O  OE1 . GLN A 1 945  ? 63.876 61.559  -30.542 1.00 20.49 ? 945  GLN A OE1 1 
ATOM   7552 N  NE2 . GLN A 1 945  ? 65.537 60.407  -29.623 1.00 18.70 ? 945  GLN A NE2 1 
ATOM   7553 N  N   . PHE A 1 946  ? 65.724 62.747  -25.306 1.00 10.94 ? 946  PHE A N   1 
ATOM   7554 C  CA  . PHE A 1 946  ? 65.979 61.747  -24.243 1.00 10.46 ? 946  PHE A CA  1 
ATOM   7555 C  C   . PHE A 1 946  ? 64.854 60.748  -24.362 1.00 10.35 ? 946  PHE A C   1 
ATOM   7556 O  O   . PHE A 1 946  ? 63.707 61.094  -24.574 1.00 10.07 ? 946  PHE A O   1 
ATOM   7557 C  CB  . PHE A 1 946  ? 65.949 62.398  -22.850 1.00 10.91 ? 946  PHE A CB  1 
ATOM   7558 C  CG  . PHE A 1 946  ? 65.830 61.392  -21.732 1.00 10.94 ? 946  PHE A CG  1 
ATOM   7559 C  CD1 . PHE A 1 946  ? 66.891 60.560  -21.403 1.00 11.82 ? 946  PHE A CD1 1 
ATOM   7560 C  CD2 . PHE A 1 946  ? 64.604 61.231  -21.069 1.00 11.35 ? 946  PHE A CD2 1 
ATOM   7561 C  CE1 . PHE A 1 946  ? 66.739 59.545  -20.408 1.00 12.68 ? 946  PHE A CE1 1 
ATOM   7562 C  CE2 . PHE A 1 946  ? 64.436 60.247  -20.101 1.00 12.48 ? 946  PHE A CE2 1 
ATOM   7563 C  CZ  . PHE A 1 946  ? 65.466 59.409  -19.762 1.00 12.45 ? 946  PHE A CZ  1 
ATOM   7564 N  N   . GLY A 1 947  ? 65.188 59.469  -24.207 1.00 10.94 ? 947  GLY A N   1 
ATOM   7565 C  CA  . GLY A 1 947  ? 64.212 58.404  -24.256 1.00 12.27 ? 947  GLY A CA  1 
ATOM   7566 C  C   . GLY A 1 947  ? 63.872 57.820  -25.600 1.00 11.88 ? 947  GLY A C   1 
ATOM   7567 O  O   . GLY A 1 947  ? 62.936 57.043  -25.684 1.00 13.00 ? 947  GLY A O   1 
ATOM   7568 N  N   . GLY A 1 948  ? 64.672 58.126  -26.641 1.00 13.45 ? 948  GLY A N   1 
ATOM   7569 C  CA  . GLY A 1 948  ? 64.394 57.590  -27.960 1.00 15.25 ? 948  GLY A CA  1 
ATOM   7570 C  C   . GLY A 1 948  ? 64.391 56.063  -28.003 1.00 16.17 ? 948  GLY A C   1 
ATOM   7571 O  O   . GLY A 1 948  ? 63.750 55.476  -28.897 1.00 18.92 ? 948  GLY A O   1 
ATOM   7572 N  N   . ASP A 1 949  ? 65.089 55.436  -27.048 1.00 17.12 ? 949  ASP A N   1 
ATOM   7573 C  CA  . ASP A 1 949  ? 65.167 53.974  -26.952 1.00 18.72 ? 949  ASP A CA  1 
ATOM   7574 C  C   . ASP A 1 949  ? 64.161 53.361  -25.972 1.00 18.22 ? 949  ASP A C   1 
ATOM   7575 O  O   . ASP A 1 949  ? 64.160 52.131  -25.714 1.00 18.35 ? 949  ASP A O   1 
ATOM   7576 C  CB  . ASP A 1 949  ? 66.614 53.541  -26.580 1.00 21.81 ? 949  ASP A CB  1 
ATOM   7577 C  CG  . ASP A 1 949  ? 67.090 54.061  -25.202 1.00 25.38 ? 949  ASP A CG  1 
ATOM   7578 O  OD1 . ASP A 1 949  ? 66.579 55.082  -24.631 1.00 26.86 ? 949  ASP A OD1 1 
ATOM   7579 O  OD2 . ASP A 1 949  ? 68.048 53.427  -24.663 1.00 28.96 ? 949  ASP A OD2 1 
ATOM   7580 N  N   . HIS A 1 950  ? 63.306 54.200  -25.380 1.00 16.50 ? 950  HIS A N   1 
ATOM   7581 C  CA  . HIS A 1 950  ? 62.295 53.653  -24.478 1.00 14.15 ? 950  HIS A CA  1 
ATOM   7582 C  C   . HIS A 1 950  ? 61.208 52.923  -25.305 1.00 14.17 ? 950  HIS A C   1 
ATOM   7583 O  O   . HIS A 1 950  ? 60.814 53.378  -26.376 1.00 14.60 ? 950  HIS A O   1 
ATOM   7584 C  CB  . HIS A 1 950  ? 61.589 54.779  -23.751 1.00 12.16 ? 950  HIS A CB  1 
ATOM   7585 C  CG  . HIS A 1 950  ? 62.414 55.554  -22.786 1.00 11.48 ? 950  HIS A CG  1 
ATOM   7586 N  ND1 . HIS A 1 950  ? 63.663 55.213  -22.290 1.00 13.65 ? 950  HIS A ND1 1 
ATOM   7587 C  CD2 . HIS A 1 950  ? 62.070 56.702  -22.165 1.00 8.80  ? 950  HIS A CD2 1 
ATOM   7588 C  CE1 . HIS A 1 950  ? 64.039 56.129  -21.406 1.00 10.70 ? 950  HIS A CE1 1 
ATOM   7589 N  NE2 . HIS A 1 950  ? 63.080 57.041  -21.321 1.00 13.74 ? 950  HIS A NE2 1 
ATOM   7590 N  N   . PRO A 1 951  ? 60.723 51.762  -24.839 1.00 13.91 ? 951  PRO A N   1 
ATOM   7591 C  CA  . PRO A 1 951  ? 59.689 51.031  -25.588 1.00 13.93 ? 951  PRO A CA  1 
ATOM   7592 C  C   . PRO A 1 951  ? 58.411 51.830  -25.701 1.00 13.93 ? 951  PRO A C   1 
ATOM   7593 O  O   . PRO A 1 951  ? 57.996 52.483  -24.719 1.00 13.58 ? 951  PRO A O   1 
ATOM   7594 C  CB  . PRO A 1 951  ? 59.443 49.749  -24.746 1.00 15.35 ? 951  PRO A CB  1 
ATOM   7595 C  CG  . PRO A 1 951  ? 60.706 49.577  -24.019 1.00 16.24 ? 951  PRO A CG  1 
ATOM   7596 C  CD  . PRO A 1 951  ? 61.191 50.998  -23.671 1.00 16.11 ? 951  PRO A CD  1 
ATOM   7597 N  N   . SER A 1 952  ? 57.761 51.765  -26.849 1.00 12.73 ? 952  SER A N   1 
ATOM   7598 C  CA  . SER A 1 952  ? 56.526 52.478  -27.068 1.00 12.62 ? 952  SER A CA  1 
ATOM   7599 C  C   . SER A 1 952  ? 55.444 51.415  -26.886 1.00 12.83 ? 952  SER A C   1 
ATOM   7600 O  O   . SER A 1 952  ? 55.154 50.595  -27.808 1.00 13.20 ? 952  SER A O   1 
ATOM   7601 C  CB  . SER A 1 952  ? 56.508 53.114  -28.474 1.00 12.53 ? 952  SER A CB  1 
ATOM   7602 O  OG  . SER A 1 952  ? 55.408 53.999  -28.624 1.00 14.15 ? 952  SER A OG  1 
ATOM   7603 N  N   . ALA A 1 953  ? 54.842 51.398  -25.694 1.00 12.17 ? 953  ALA A N   1 
ATOM   7604 C  CA  . ALA A 1 953  ? 53.875 50.375  -25.319 1.00 11.48 ? 953  ALA A CA  1 
ATOM   7605 C  C   . ALA A 1 953  ? 52.516 50.502  -25.937 1.00 11.44 ? 953  ALA A C   1 
ATOM   7606 O  O   . ALA A 1 953  ? 52.117 51.549  -26.406 1.00 12.02 ? 953  ALA A O   1 
ATOM   7607 C  CB  . ALA A 1 953  ? 53.737 50.344  -23.766 1.00 12.64 ? 953  ALA A CB  1 
ATOM   7608 N  N   . ARG A 1 954  ? 51.789 49.391  -25.937 1.00 11.53 ? 954  ARG A N   1 
ATOM   7609 C  CA  . ARG A 1 954  ? 50.447 49.318  -26.444 1.00 12.30 ? 954  ARG A CA  1 
ATOM   7610 C  C   . ARG A 1 954  ? 49.619 50.463  -25.818 1.00 11.26 ? 954  ARG A C   1 
ATOM   7611 O  O   . ARG A 1 954  ? 49.758 50.778  -24.626 1.00 10.57 ? 954  ARG A O   1 
ATOM   7612 C  CB  . ARG A 1 954  ? 49.898 47.918  -26.114 1.00 14.66 ? 954  ARG A CB  1 
ATOM   7613 C  CG  . ARG A 1 954  ? 49.906 47.610  -24.621 1.00 18.88 ? 954  ARG A CG  1 
ATOM   7614 C  CD  . ARG A 1 954  ? 49.319 46.218  -24.285 1.00 22.87 ? 954  ARG A CD  1 
ATOM   7615 N  NE  . ARG A 1 954  ? 50.194 45.097  -24.643 1.00 27.37 ? 954  ARG A NE  1 
ATOM   7616 C  CZ  . ARG A 1 954  ? 49.853 44.158  -25.519 1.00 29.85 ? 954  ARG A CZ  1 
ATOM   7617 N  NH1 . ARG A 1 954  ? 48.661 44.231  -26.130 1.00 30.98 ? 954  ARG A NH1 1 
ATOM   7618 N  NH2 . ARG A 1 954  ? 50.673 43.131  -25.759 1.00 31.57 ? 954  ARG A NH2 1 
ATOM   7619 N  N   . GLU A 1 955  ? 48.698 50.996  -26.607 1.00 10.80 ? 955  GLU A N   1 
ATOM   7620 C  CA  . GLU A 1 955  ? 47.933 52.175  -26.234 1.00 11.66 ? 955  GLU A CA  1 
ATOM   7621 C  C   . GLU A 1 955  ? 47.106 52.054  -24.971 1.00 10.42 ? 955  GLU A C   1 
ATOM   7622 O  O   . GLU A 1 955  ? 46.819 53.086  -24.326 1.00 11.70 ? 955  GLU A O   1 
ATOM   7623 C  CB  . GLU A 1 955  ? 47.041 52.628  -27.422 1.00 13.37 ? 955  GLU A CB  1 
ATOM   7624 C  CG  . GLU A 1 955  ? 45.951 51.629  -27.779 1.00 15.64 ? 955  GLU A CG  1 
ATOM   7625 C  CD  . GLU A 1 955  ? 45.073 52.093  -28.898 1.00 17.76 ? 955  GLU A CD  1 
ATOM   7626 O  OE1 . GLU A 1 955  ? 44.938 53.311  -29.113 1.00 22.20 ? 955  GLU A OE1 1 
ATOM   7627 O  OE2 . GLU A 1 955  ? 44.488 51.209  -29.556 1.00 21.28 ? 955  GLU A OE2 1 
ATOM   7628 N  N   . ASP A 1 956  ? 46.704 50.841  -24.627 1.00 9.53  ? 956  ASP A N   1 
ATOM   7629 C  CA  . ASP A 1 956  ? 45.902 50.673  -23.419 1.00 10.03 ? 956  ASP A CA  1 
ATOM   7630 C  C   . ASP A 1 956  ? 46.738 50.560  -22.152 1.00 8.67  ? 956  ASP A C   1 
ATOM   7631 O  O   . ASP A 1 956  ? 46.156 50.479  -21.085 1.00 11.19 ? 956  ASP A O   1 
ATOM   7632 C  CB  . ASP A 1 956  ? 44.910 49.500  -23.552 1.00 11.20 ? 956  ASP A CB  1 
ATOM   7633 C  CG  . ASP A 1 956  ? 45.563 48.191  -23.891 1.00 12.72 ? 956  ASP A CG  1 
ATOM   7634 O  OD1 . ASP A 1 956  ? 46.794 48.137  -24.097 1.00 16.31 ? 956  ASP A OD1 1 
ATOM   7635 O  OD2 . ASP A 1 956  ? 44.792 47.191  -23.948 1.00 14.07 ? 956  ASP A OD2 1 
ATOM   7636 N  N   . LEU A 1 957  ? 48.051 50.570  -22.245 1.00 9.23  ? 957  LEU A N   1 
ATOM   7637 C  CA  . LEU A 1 957  ? 48.904 50.433  -21.064 1.00 9.00  ? 957  LEU A CA  1 
ATOM   7638 C  C   . LEU A 1 957  ? 49.489 51.781  -20.671 1.00 8.74  ? 957  LEU A C   1 
ATOM   7639 O  O   . LEU A 1 957  ? 49.921 52.562  -21.521 1.00 9.93  ? 957  LEU A O   1 
ATOM   7640 C  CB  . LEU A 1 957  ? 50.064 49.473  -21.422 1.00 10.48 ? 957  LEU A CB  1 
ATOM   7641 C  CG  . LEU A 1 957  ? 50.934 49.012  -20.250 1.00 12.82 ? 957  LEU A CG  1 
ATOM   7642 C  CD1 . LEU A 1 957  ? 50.102 48.276  -19.208 1.00 16.05 ? 957  LEU A CD1 1 
ATOM   7643 C  CD2 . LEU A 1 957  ? 52.020 48.077  -20.789 1.00 14.01 ? 957  LEU A CD2 1 
ATOM   7644 N  N   . ASP A 1 958  ? 49.518 52.059  -19.368 1.00 8.53  ? 958  ASP A N   1 
ATOM   7645 C  CA  . ASP A 1 958  ? 50.171 53.278  -18.863 1.00 7.53  ? 958  ASP A CA  1 
ATOM   7646 C  C   . ASP A 1 958  ? 51.081 52.952  -17.699 1.00 7.10  ? 958  ASP A C   1 
ATOM   7647 O  O   . ASP A 1 958  ? 50.835 51.983  -16.945 1.00 8.15  ? 958  ASP A O   1 
ATOM   7648 C  CB  . ASP A 1 958  ? 49.079 54.295  -18.393 1.00 8.53  ? 958  ASP A CB  1 
ATOM   7649 C  CG  . ASP A 1 958  ? 49.634 55.694  -18.205 1.00 8.95  ? 958  ASP A CG  1 
ATOM   7650 O  OD1 . ASP A 1 958  ? 50.742 55.995  -18.673 1.00 8.91  ? 958  ASP A OD1 1 
ATOM   7651 O  OD2 . ASP A 1 958  ? 48.906 56.484  -17.562 1.00 9.12  ? 958  ASP A OD2 1 
ATOM   7652 N  N   . VAL A 1 959  ? 52.159 53.753  -17.588 1.00 7.42  ? 959  VAL A N   1 
ATOM   7653 C  CA  . VAL A 1 959  ? 53.034 53.717  -16.418 1.00 7.99  ? 959  VAL A CA  1 
ATOM   7654 C  C   . VAL A 1 959  ? 52.434 54.866  -15.581 1.00 6.83  ? 959  VAL A C   1 
ATOM   7655 O  O   . VAL A 1 959  ? 52.846 56.040  -15.694 1.00 8.31  ? 959  VAL A O   1 
ATOM   7656 C  CB  . VAL A 1 959  ? 54.485 53.966  -16.781 1.00 8.43  ? 959  VAL A CB  1 
ATOM   7657 C  CG1 . VAL A 1 959  ? 55.333 54.098  -15.462 1.00 8.38  ? 959  VAL A CG1 1 
ATOM   7658 C  CG2 . VAL A 1 959  ? 55.020 52.729  -17.611 1.00 10.04 ? 959  VAL A CG2 1 
ATOM   7659 N  N   . SER A 1 960  ? 51.473 54.526  -14.722 1.00 7.67  ? 960  SER A N   1 
ATOM   7660 C  CA  . SER A 1 960  ? 50.772 55.528  -13.907 1.00 7.58  ? 960  SER A CA  1 
ATOM   7661 C  C   . SER A 1 960  ? 51.666 56.223  -12.924 1.00 7.64  ? 960  SER A C   1 
ATOM   7662 O  O   . SER A 1 960  ? 51.501 57.442  -12.668 1.00 8.79  ? 960  SER A O   1 
ATOM   7663 C  CB  . SER A 1 960  ? 49.650 54.868  -13.126 1.00 8.33  ? 960  SER A CB  1 
ATOM   7664 O  OG  . SER A 1 960  ? 48.826 54.052  -13.978 1.00 10.14 ? 960  SER A OG  1 
ATOM   7665 N  N   . VAL A 1 961  ? 52.638 55.452  -12.411 1.00 7.72  ? 961  VAL A N   1 
ATOM   7666 C  CA  . VAL A 1 961  ? 53.620 55.987  -11.436 1.00 7.98  ? 961  VAL A CA  1 
ATOM   7667 C  C   . VAL A 1 961  ? 55.006 55.425  -11.759 1.00 7.13  ? 961  VAL A C   1 
ATOM   7668 O  O   . VAL A 1 961  ? 55.154 54.207  -12.015 1.00 7.15  ? 961  VAL A O   1 
ATOM   7669 C  CB  . VAL A 1 961  ? 53.293 55.511  -9.986  1.00 8.11  ? 961  VAL A CB  1 
ATOM   7670 C  CG1 . VAL A 1 961  ? 54.416 55.954  -9.005  1.00 10.04 ? 961  VAL A CG1 1 
ATOM   7671 C  CG2 . VAL A 1 961  ? 51.934 56.130  -9.560  1.00 10.18 ? 961  VAL A CG2 1 
ATOM   7672 N  N   . MET A 1 962  ? 56.007 56.310  -11.745 1.00 7.89  ? 962  MET A N   1 
ATOM   7673 C  CA  . MET A 1 962  ? 57.411 55.897  -11.738 1.00 7.64  ? 962  MET A CA  1 
ATOM   7674 C  C   . MET A 1 962  ? 57.977 56.713  -10.588 1.00 7.38  ? 962  MET A C   1 
ATOM   7675 O  O   . MET A 1 962  ? 57.907 57.955  -10.560 1.00 7.90  ? 962  MET A O   1 
ATOM   7676 C  CB  . MET A 1 962  ? 58.132 56.246  -13.044 1.00 8.17  ? 962  MET A CB  1 
ATOM   7677 C  CG  . MET A 1 962  ? 59.648 55.872  -12.950 1.00 7.75  ? 962  MET A CG  1 
ATOM   7678 S  SD  . MET A 1 962  ? 60.378 56.187  -14.581 1.00 9.77  ? 962  MET A SD  1 
ATOM   7679 C  CE  . MET A 1 962  ? 62.123 55.714  -14.288 1.00 9.72  ? 962  MET A CE  1 
ATOM   7680 N  N   . ARG A 1 963  ? 58.544 56.012  -9.588  1.00 8.04  ? 963  ARG A N   1 
ATOM   7681 C  CA  . ARG A 1 963  ? 59.061 56.663  -8.396  1.00 8.07  ? 963  ARG A CA  1 
ATOM   7682 C  C   . ARG A 1 963  ? 60.313 55.999  -7.858  1.00 8.04  ? 963  ARG A C   1 
ATOM   7683 O  O   . ARG A 1 963  ? 60.252 54.817  -7.539  1.00 8.30  ? 963  ARG A O   1 
ATOM   7684 C  CB  . ARG A 1 963  ? 57.988 56.594  -7.292  1.00 8.30  ? 963  ARG A CB  1 
ATOM   7685 C  CG  . ARG A 1 963  ? 58.443 57.262  -5.954  1.00 8.40  ? 963  ARG A CG  1 
ATOM   7686 C  CD  . ARG A 1 963  ? 57.381 57.088  -4.820  1.00 8.88  ? 963  ARG A CD  1 
ATOM   7687 N  NE  . ARG A 1 963  ? 56.166 57.817  -5.226  1.00 8.62  ? 963  ARG A NE  1 
ATOM   7688 C  CZ  . ARG A 1 963  ? 54.940 57.298  -5.161  1.00 8.45  ? 963  ARG A CZ  1 
ATOM   7689 N  NH1 . ARG A 1 963  ? 54.665 56.077  -4.646  1.00 8.81  ? 963  ARG A NH1 1 
ATOM   7690 N  NH2 . ARG A 1 963  ? 53.986 57.949  -5.804  1.00 8.81  ? 963  ARG A NH2 1 
ATOM   7691 N  N   . ARG A 1 964  ? 61.425 56.722  -7.802  1.00 8.63  ? 964  ARG A N   1 
ATOM   7692 C  CA  . ARG A 1 964  ? 62.619 56.132  -7.157  1.00 8.69  ? 964  ARG A CA  1 
ATOM   7693 C  C   . ARG A 1 964  ? 62.297 56.084  -5.650  1.00 9.06  ? 964  ARG A C   1 
ATOM   7694 O  O   . ARG A 1 964  ? 61.866 57.055  -5.055  1.00 9.10  ? 964  ARG A O   1 
ATOM   7695 C  CB  . ARG A 1 964  ? 63.813 57.050  -7.445  1.00 8.17  ? 964  ARG A CB  1 
ATOM   7696 C  CG  . ARG A 1 964  ? 65.097 56.421  -6.843  1.00 8.81  ? 964  ARG A CG  1 
ATOM   7697 C  CD  . ARG A 1 964  ? 66.410 57.053  -7.341  1.00 9.76  ? 964  ARG A CD  1 
ATOM   7698 N  NE  . ARG A 1 964  ? 66.588 56.870  -8.785  1.00 10.62 ? 964  ARG A NE  1 
ATOM   7699 C  CZ  . ARG A 1 964  ? 67.471 56.062  -9.355  1.00 11.43 ? 964  ARG A CZ  1 
ATOM   7700 N  NH1 . ARG A 1 964  ? 68.286 55.318  -8.585  1.00 14.38 ? 964  ARG A NH1 1 
ATOM   7701 N  NH2 . ARG A 1 964  ? 67.585 56.016  -10.695 1.00 12.39 ? 964  ARG A NH2 1 
ATOM   7702 N  N   . LEU A 1 965  ? 62.592 54.920  -5.068  1.00 9.41  ? 965  LEU A N   1 
ATOM   7703 C  CA  . LEU A 1 965  ? 62.216 54.651  -3.681  1.00 9.54  ? 965  LEU A CA  1 
ATOM   7704 C  C   . LEU A 1 965  ? 63.374 54.770  -2.695  1.00 10.20 ? 965  LEU A C   1 
ATOM   7705 O  O   . LEU A 1 965  ? 63.157 54.699  -1.483  1.00 11.91 ? 965  LEU A O   1 
ATOM   7706 C  CB  . LEU A 1 965  ? 61.653 53.237  -3.578  1.00 10.96 ? 965  LEU A CB  1 
ATOM   7707 C  CG  . LEU A 1 965  ? 60.412 52.950  -4.458  1.00 9.72  ? 965  LEU A CG  1 
ATOM   7708 C  CD1 . LEU A 1 965  ? 60.013 51.455  -4.434  1.00 11.47 ? 965  LEU A CD1 1 
ATOM   7709 C  CD2 . LEU A 1 965  ? 59.197 53.806  -3.990  1.00 11.31 ? 965  LEU A CD2 1 
ATOM   7710 N  N   . THR A 1 966  ? 64.578 54.941  -3.234  1.00 9.93  ? 966  THR A N   1 
ATOM   7711 C  CA  . THR A 1 966  ? 65.792 55.041  -2.400  1.00 10.54 ? 966  THR A CA  1 
ATOM   7712 C  C   . THR A 1 966  ? 66.492 56.355  -2.573  1.00 10.06 ? 966  THR A C   1 
ATOM   7713 O  O   . THR A 1 966  ? 66.460 56.921  -3.686  1.00 10.52 ? 966  THR A O   1 
ATOM   7714 C  CB  . THR A 1 966  ? 66.793 53.939  -2.817  1.00 10.96 ? 966  THR A CB  1 
ATOM   7715 O  OG1 . THR A 1 966  ? 66.837 53.861  -4.234  1.00 11.35 ? 966  THR A OG1 1 
ATOM   7716 C  CG2 . THR A 1 966  ? 66.371 52.568  -2.258  1.00 12.28 ? 966  THR A CG2 1 
ATOM   7717 N  N   . LYS A 1 967  ? 67.143 56.832  -1.508  1.00 11.63 ? 967  LYS A N   1 
ATOM   7718 C  CA  . LYS A 1 967  ? 67.988 58.028  -1.536  1.00 12.03 ? 967  LYS A CA  1 
ATOM   7719 C  C   . LYS A 1 967  ? 69.380 57.584  -2.032  1.00 11.87 ? 967  LYS A C   1 
ATOM   7720 O  O   . LYS A 1 967  ? 69.644 56.404  -2.202  1.00 11.54 ? 967  LYS A O   1 
ATOM   7721 C  CB  . LYS A 1 967  ? 68.052 58.668  -0.152  1.00 13.69 ? 967  LYS A CB  1 
ATOM   7722 C  CG  . LYS A 1 967  ? 66.663 59.243  0.302   1.00 16.62 ? 967  LYS A CG  1 
ATOM   7723 C  CD  . LYS A 1 967  ? 66.812 59.989  1.605   1.00 19.58 ? 967  LYS A CD  1 
ATOM   7724 C  CE  . LYS A 1 967  ? 65.457 60.639  2.012   1.00 23.89 ? 967  LYS A CE  1 
ATOM   7725 N  NZ  . LYS A 1 967  ? 65.745 61.605  3.146   1.00 28.36 ? 967  LYS A NZ  1 
ATOM   7726 N  N   . SER A 1 968  ? 70.197 58.594  -2.344  1.00 13.25 ? 968  SER A N   1 
ATOM   7727 C  CA  . SER A 1 968  ? 71.495 58.330  -2.979  1.00 15.36 ? 968  SER A CA  1 
ATOM   7728 C  C   . SER A 1 968  ? 72.469 57.477  -2.199  1.00 16.55 ? 968  SER A C   1 
ATOM   7729 O  O   . SER A 1 968  ? 73.273 56.777  -2.832  1.00 18.74 ? 968  SER A O   1 
ATOM   7730 C  CB  . SER A 1 968  ? 72.168 59.644  -3.400  1.00 16.55 ? 968  SER A CB  1 
ATOM   7731 O  OG  . SER A 1 968  ? 72.413 60.482  -2.304  1.00 21.42 ? 968  SER A OG  1 
ATOM   7732 N  N   . SER A 1 969  ? 72.330 57.473  -0.881  1.00 17.14 ? 969  SER A N   1 
ATOM   7733 C  CA  . SER A 1 969  ? 73.257 56.666  -0.059  1.00 18.57 ? 969  SER A CA  1 
ATOM   7734 C  C   . SER A 1 969  ? 72.998 55.159  -0.107  1.00 18.05 ? 969  SER A C   1 
ATOM   7735 O  O   . SER A 1 969  ? 73.829 54.370  0.340   1.00 18.60 ? 969  SER A O   1 
ATOM   7736 C  CB  . SER A 1 969  ? 73.246 57.149  1.376   1.00 21.45 ? 969  SER A CB  1 
ATOM   7737 O  OG  . SER A 1 969  ? 71.964 56.939  1.951   1.00 26.26 ? 969  SER A OG  1 
ATOM   7738 N  N   . ALA A 1 970  ? 71.852 54.708  -0.617  1.00 15.71 ? 970  ALA A N   1 
ATOM   7739 C  CA  . ALA A 1 970  ? 71.602 53.282  -0.749  1.00 14.87 ? 970  ALA A CA  1 
ATOM   7740 C  C   . ALA A 1 970  ? 72.457 52.580  -1.786  1.00 16.12 ? 970  ALA A C   1 
ATOM   7741 O  O   . ALA A 1 970  ? 72.449 52.921  -2.972  1.00 16.18 ? 970  ALA A O   1 
ATOM   7742 C  CB  . ALA A 1 970  ? 70.103 52.987  -1.082  1.00 14.68 ? 970  ALA A CB  1 
ATOM   7743 N  N   . LYS A 1 971  ? 73.181 51.546  -1.360  1.00 17.65 ? 971  LYS A N   1 
ATOM   7744 C  CA  . LYS A 1 971  ? 74.005 50.773  -2.273  1.00 19.68 ? 971  LYS A CA  1 
ATOM   7745 C  C   . LYS A 1 971  ? 73.121 50.150  -3.364  1.00 18.63 ? 971  LYS A C   1 
ATOM   7746 O  O   . LYS A 1 971  ? 73.508 50.138  -4.509  1.00 20.38 ? 971  LYS A O   1 
ATOM   7747 C  CB  . LYS A 1 971  ? 74.731 49.655  -1.495  1.00 21.69 ? 971  LYS A CB  1 
ATOM   7748 C  CG  . LYS A 1 971  ? 75.767 48.883  -2.315  1.00 26.65 ? 971  LYS A CG  1 
ATOM   7749 C  CD  . LYS A 1 971  ? 76.581 47.940  -1.409  1.00 29.16 ? 971  LYS A CD  1 
ATOM   7750 C  CE  . LYS A 1 971  ? 76.621 48.443  0.035   1.00 31.51 ? 971  LYS A CE  1 
ATOM   7751 N  NZ  . LYS A 1 971  ? 77.150 49.823  0.193   1.00 33.05 ? 971  LYS A NZ  1 
ATOM   7752 N  N   . THR A 1 972  ? 71.938 49.635  -3.008  1.00 17.56 ? 972  THR A N   1 
ATOM   7753 C  CA  . THR A 1 972  ? 71.058 49.039  -4.013  1.00 16.92 ? 972  THR A CA  1 
ATOM   7754 C  C   . THR A 1 972  ? 69.902 50.012  -4.246  1.00 15.66 ? 972  THR A C   1 
ATOM   7755 O  O   . THR A 1 972  ? 69.073 50.252  -3.368  1.00 15.74 ? 972  THR A O   1 
ATOM   7756 C  CB  . THR A 1 972  ? 70.498 47.664  -3.567  1.00 17.57 ? 972  THR A CB  1 
ATOM   7757 O  OG1 . THR A 1 972  ? 71.608 46.767  -3.368  1.00 18.94 ? 972  THR A OG1 1 
ATOM   7758 C  CG2 . THR A 1 972  ? 69.612 47.032  -4.665  1.00 19.05 ? 972  THR A CG2 1 
ATOM   7759 N  N   . GLN A 1 973  ? 69.889 50.615  -5.422  1.00 13.77 ? 973  GLN A N   1 
ATOM   7760 C  CA  . GLN A 1 973  ? 68.813 51.583  -5.719  1.00 12.93 ? 973  GLN A CA  1 
ATOM   7761 C  C   . GLN A 1 973  ? 67.552 50.825  -6.092  1.00 12.78 ? 973  GLN A C   1 
ATOM   7762 O  O   . GLN A 1 973  ? 67.585 49.760  -6.689  1.00 13.35 ? 973  GLN A O   1 
ATOM   7763 C  CB  . GLN A 1 973  ? 69.279 52.444  -6.866  1.00 12.12 ? 973  GLN A CB  1 
ATOM   7764 C  CG  . GLN A 1 973  ? 70.369 53.460  -6.443  1.00 12.92 ? 973  GLN A CG  1 
ATOM   7765 C  CD  . GLN A 1 973  ? 69.923 54.450  -5.411  1.00 13.26 ? 973  GLN A CD  1 
ATOM   7766 O  OE1 . GLN A 1 973  ? 70.533 54.636  -4.334  1.00 14.54 ? 973  GLN A OE1 1 
ATOM   7767 N  NE2 . GLN A 1 973  ? 68.813 55.138  -5.722  1.00 10.98 ? 973  GLN A NE2 1 
ATOM   7768 N  N   . ARG A 1 974  ? 66.396 51.421  -5.758  1.00 11.85 ? 974  ARG A N   1 
ATOM   7769 C  CA  . ARG A 1 974  ? 65.127 50.777  -6.087  1.00 11.95 ? 974  ARG A CA  1 
ATOM   7770 C  C   . ARG A 1 974  ? 64.176 51.765  -6.742  1.00 10.07 ? 974  ARG A C   1 
ATOM   7771 O  O   . ARG A 1 974  ? 64.053 52.896  -6.280  1.00 10.83 ? 974  ARG A O   1 
ATOM   7772 C  CB  . ARG A 1 974  ? 64.460 50.238  -4.842  1.00 12.02 ? 974  ARG A CB  1 
ATOM   7773 C  CG  . ARG A 1 974  ? 65.321 49.168  -4.067  1.00 13.16 ? 974  ARG A CG  1 
ATOM   7774 C  CD  . ARG A 1 974  ? 64.749 48.948  -2.619  1.00 16.16 ? 974  ARG A CD  1 
ATOM   7775 N  NE  . ARG A 1 974  ? 63.494 48.202  -2.660  1.00 20.13 ? 974  ARG A NE  1 
ATOM   7776 C  CZ  . ARG A 1 974  ? 62.331 48.608  -2.167  1.00 19.67 ? 974  ARG A CZ  1 
ATOM   7777 N  NH1 . ARG A 1 974  ? 62.195 49.788  -1.554  1.00 20.17 ? 974  ARG A NH1 1 
ATOM   7778 N  NH2 . ARG A 1 974  ? 61.287 47.819  -2.332  1.00 18.89 ? 974  ARG A NH2 1 
ATOM   7779 N  N   . VAL A 1 975  ? 63.537 51.311  -7.798  1.00 10.00 ? 975  VAL A N   1 
ATOM   7780 C  CA  . VAL A 1 975  ? 62.594 52.200  -8.496  1.00 10.43 ? 975  VAL A CA  1 
ATOM   7781 C  C   . VAL A 1 975  ? 61.283 51.435  -8.606  1.00 10.38 ? 975  VAL A C   1 
ATOM   7782 O  O   . VAL A 1 975  ? 61.223 50.271  -9.092  1.00 10.27 ? 975  VAL A O   1 
ATOM   7783 C  CB  . VAL A 1 975  ? 63.090 52.520  -9.912  1.00 10.15 ? 975  VAL A CB  1 
ATOM   7784 C  CG1 . VAL A 1 975  ? 62.060 53.438  -10.633 1.00 11.57 ? 975  VAL A CG1 1 
ATOM   7785 C  CG2 . VAL A 1 975  ? 64.475 53.275  -9.803  1.00 13.81 ? 975  VAL A CG2 1 
ATOM   7786 N  N   . GLY A 1 976  ? 60.193 52.119  -8.212  1.00 9.39  ? 976  GLY A N   1 
ATOM   7787 C  CA  . GLY A 1 976  ? 58.851 51.539  -8.263  1.00 9.57  ? 976  GLY A CA  1 
ATOM   7788 C  C   . GLY A 1 976  ? 58.041 52.024  -9.447  1.00 8.51  ? 976  GLY A C   1 
ATOM   7789 O  O   . GLY A 1 976  ? 58.128 53.200  -9.815  1.00 8.52  ? 976  GLY A O   1 
ATOM   7790 N  N   . TYR A 1 977  ? 57.267 51.126  -10.012 1.00 8.46  ? 977  TYR A N   1 
ATOM   7791 C  CA  . TYR A 1 977  ? 56.390 51.431  -11.129 1.00 7.94  ? 977  TYR A CA  1 
ATOM   7792 C  C   . TYR A 1 977  ? 54.988 50.935  -10.847 1.00 8.48  ? 977  TYR A C   1 
ATOM   7793 O  O   . TYR A 1 977  ? 54.819 49.823  -10.316 1.00 9.01  ? 977  TYR A O   1 
ATOM   7794 C  CB  . TYR A 1 977  ? 56.860 50.718  -12.405 1.00 9.23  ? 977  TYR A CB  1 
ATOM   7795 C  CG  . TYR A 1 977  ? 58.251 51.072  -12.807 1.00 8.98  ? 977  TYR A CG  1 
ATOM   7796 C  CD1 . TYR A 1 977  ? 59.334 50.343  -12.324 1.00 9.02  ? 977  TYR A CD1 1 
ATOM   7797 C  CD2 . TYR A 1 977  ? 58.471 52.134  -13.665 1.00 8.80  ? 977  TYR A CD2 1 
ATOM   7798 C  CE1 . TYR A 1 977  ? 60.626 50.682  -12.712 1.00 10.18 ? 977  TYR A CE1 1 
ATOM   7799 C  CE2 . TYR A 1 977  ? 59.739 52.514  -14.057 1.00 9.58  ? 977  TYR A CE2 1 
ATOM   7800 C  CZ  . TYR A 1 977  ? 60.811 51.776  -13.578 1.00 9.17  ? 977  TYR A CZ  1 
ATOM   7801 O  OH  . TYR A 1 977  ? 62.066 52.168  -14.017 1.00 10.95 ? 977  TYR A OH  1 
ATOM   7802 N  N   . VAL A 1 978  ? 53.955 51.755  -11.136 1.00 7.28  ? 978  VAL A N   1 
ATOM   7803 C  CA  . VAL A 1 978  ? 52.596 51.225  -11.088 1.00 8.13  ? 978  VAL A CA  1 
ATOM   7804 C  C   . VAL A 1 978  ? 52.156 51.176  -12.560 1.00 7.90  ? 978  VAL A C   1 
ATOM   7805 O  O   . VAL A 1 978  ? 52.235 52.224  -13.235 1.00 8.70  ? 978  VAL A O   1 
ATOM   7806 C  CB  . VAL A 1 978  ? 51.615 52.125  -10.281 1.00 7.54  ? 978  VAL A CB  1 
ATOM   7807 C  CG1 . VAL A 1 978  ? 50.161 51.612  -10.436 1.00 8.25  ? 978  VAL A CG1 1 
ATOM   7808 C  CG2 . VAL A 1 978  ? 52.027 52.140  -8.793  1.00 8.76  ? 978  VAL A CG2 1 
ATOM   7809 N  N   . LEU A 1 979  ? 51.741 50.005  -13.034 1.00 8.31  ? 979  LEU A N   1 
ATOM   7810 C  CA  . LEU A 1 979  ? 51.295 49.787  -14.411 1.00 9.57  ? 979  LEU A CA  1 
ATOM   7811 C  C   . LEU A 1 979  ? 49.813 49.555  -14.437 1.00 9.33  ? 979  LEU A C   1 
ATOM   7812 O  O   . LEU A 1 979  ? 49.297 48.680  -13.743 1.00 11.60 ? 979  LEU A O   1 
ATOM   7813 C  CB  . LEU A 1 979  ? 51.970 48.553  -15.010 1.00 12.03 ? 979  LEU A CB  1 
ATOM   7814 C  CG  A LEU A 1 979  ? 53.438 48.706  -15.373 0.50 12.52 ? 979  LEU A CG  1 
ATOM   7815 C  CG  B LEU A 1 979  ? 52.999 48.470  -16.134 0.50 16.05 ? 979  LEU A CG  1 
ATOM   7816 C  CD1 A LEU A 1 979  ? 53.942 47.389  -15.978 0.50 14.86 ? 979  LEU A CD1 1 
ATOM   7817 C  CD1 B LEU A 1 979  ? 52.886 47.090  -16.770 0.50 15.95 ? 979  LEU A CD1 1 
ATOM   7818 C  CD2 A LEU A 1 979  ? 53.569 49.818  -16.382 0.50 13.89 ? 979  LEU A CD2 1 
ATOM   7819 C  CD2 B LEU A 1 979  ? 52.848 49.520  -17.184 0.50 15.72 ? 979  LEU A CD2 1 
ATOM   7820 N  N   . HIS A 1 980  ? 49.118 50.329  -15.246 1.00 9.24  ? 980  HIS A N   1 
ATOM   7821 C  CA  . HIS A 1 980  ? 47.672 50.172  -15.361 1.00 9.42  ? 980  HIS A CA  1 
ATOM   7822 C  C   . HIS A 1 980  ? 47.280 49.873  -16.822 1.00 9.07  ? 980  HIS A C   1 
ATOM   7823 O  O   . HIS A 1 980  ? 47.714 50.604  -17.693 1.00 10.37 ? 980  HIS A O   1 
ATOM   7824 C  CB  . HIS A 1 980  ? 46.886 51.437  -14.929 1.00 9.84  ? 980  HIS A CB  1 
ATOM   7825 C  CG  . HIS A 1 980  ? 45.414 51.217  -15.029 1.00 10.51 ? 980  HIS A CG  1 
ATOM   7826 N  ND1 . HIS A 1 980  ? 44.585 51.804  -15.967 1.00 11.69 ? 980  HIS A ND1 1 
ATOM   7827 C  CD2 . HIS A 1 980  ? 44.646 50.323  -14.365 1.00 7.46  ? 980  HIS A CD2 1 
ATOM   7828 C  CE1 . HIS A 1 980  ? 43.370 51.274  -15.877 1.00 8.40  ? 980  HIS A CE1 1 
ATOM   7829 N  NE2 . HIS A 1 980  ? 43.383 50.374  -14.912 1.00 13.41 ? 980  HIS A NE2 1 
ATOM   7830 N  N   . ARG A 1 981  ? 46.483 48.832  -17.060 1.00 8.69  ? 981  ARG A N   1 
ATOM   7831 C  CA  . ARG A 1 981  ? 46.020 48.591  -18.410 1.00 9.43  ? 981  ARG A CA  1 
ATOM   7832 C  C   . ARG A 1 981  ? 44.531 48.779  -18.355 1.00 9.26  ? 981  ARG A C   1 
ATOM   7833 O  O   . ARG A 1 981  ? 43.843 48.156  -17.564 1.00 9.22  ? 981  ARG A O   1 
ATOM   7834 C  CB  . ARG A 1 981  ? 46.336 47.187  -18.851 1.00 12.19 ? 981  ARG A CB  1 
ATOM   7835 C  CG  . ARG A 1 981  ? 46.087 47.033  -20.336 1.00 16.11 ? 981  ARG A CG  1 
ATOM   7836 C  CD  . ARG A 1 981  ? 46.683 45.700  -20.767 1.00 20.43 ? 981  ARG A CD  1 
ATOM   7837 N  NE  . ARG A 1 981  ? 46.167 45.396  -22.078 1.00 23.23 ? 981  ARG A NE  1 
ATOM   7838 C  CZ  . ARG A 1 981  ? 46.243 44.188  -22.615 1.00 23.93 ? 981  ARG A CZ  1 
ATOM   7839 N  NH1 . ARG A 1 981  ? 46.826 43.215  -21.920 1.00 24.71 ? 981  ARG A NH1 1 
ATOM   7840 N  NH2 . ARG A 1 981  ? 45.719 43.947  -23.819 1.00 24.78 ? 981  ARG A NH2 1 
ATOM   7841 N  N   . THR A 1 982  ? 44.030 49.675  -19.189 1.00 9.55  ? 982  THR A N   1 
ATOM   7842 C  CA  . THR A 1 982  ? 42.566 49.870  -19.283 1.00 9.31  ? 982  THR A CA  1 
ATOM   7843 C  C   . THR A 1 982  ? 42.023 48.828  -20.299 1.00 10.05 ? 982  THR A C   1 
ATOM   7844 O  O   . THR A 1 982  ? 42.723 47.885  -20.645 1.00 11.32 ? 982  THR A O   1 
ATOM   7845 C  CB  . THR A 1 982  ? 42.260 51.334  -19.737 1.00 8.85  ? 982  THR A CB  1 
ATOM   7846 O  OG1 . THR A 1 982  ? 40.862 51.603  -19.614 1.00 9.79  ? 982  THR A OG1 1 
ATOM   7847 C  CG2 . THR A 1 982  ? 42.697 51.610  -21.189 1.00 11.13 ? 982  THR A CG2 1 
ATOM   7848 N  N   . ASN A 1 983  ? 40.745 48.908  -20.618 1.00 9.80  ? 983  ASN A N   1 
ATOM   7849 C  CA  . ASN A 1 983  ? 40.182 48.012  -21.651 1.00 9.10  ? 983  ASN A CA  1 
ATOM   7850 C  C   . ASN A 1 983  ? 39.452 48.884  -22.682 1.00 9.90  ? 983  ASN A C   1 
ATOM   7851 O  O   . ASN A 1 983  ? 38.578 49.664  -22.319 1.00 11.19 ? 983  ASN A O   1 
ATOM   7852 C  CB  . ASN A 1 983  ? 39.211 47.007  -21.055 1.00 9.16  ? 983  ASN A CB  1 
ATOM   7853 C  CG  . ASN A 1 983  ? 38.708 46.054  -22.100 1.00 9.77  ? 983  ASN A CG  1 
ATOM   7854 O  OD1 . ASN A 1 983  ? 39.461 45.166  -22.483 1.00 11.94 ? 983  ASN A OD1 1 
ATOM   7855 N  ND2 . ASN A 1 983  ? 37.504 46.254  -22.585 1.00 10.80 ? 983  ASN A ND2 1 
ATOM   7856 N  N   . LEU A 1 984  ? 39.920 48.811  -23.917 1.00 9.67  ? 984  LEU A N   1 
ATOM   7857 C  CA  . LEU A 1 984  ? 39.345 49.588  -25.028 1.00 10.83 ? 984  LEU A CA  1 
ATOM   7858 C  C   . LEU A 1 984  ? 38.528 48.687  -25.922 1.00 12.33 ? 984  LEU A C   1 
ATOM   7859 O  O   . LEU A 1 984  ? 38.854 47.523  -26.095 1.00 12.84 ? 984  LEU A O   1 
ATOM   7860 C  CB  . LEU A 1 984  ? 40.453 50.223  -25.862 1.00 11.98 ? 984  LEU A CB  1 
ATOM   7861 C  CG  . LEU A 1 984  ? 41.421 51.054  -25.001 1.00 12.46 ? 984  LEU A CG  1 
ATOM   7862 C  CD1 . LEU A 1 984  ? 42.611 51.509  -25.905 1.00 14.34 ? 984  LEU A CD1 1 
ATOM   7863 C  CD2 . LEU A 1 984  ? 40.708 52.204  -24.372 1.00 12.21 ? 984  LEU A CD2 1 
ATOM   7864 N  N   . MET A 1 985  ? 37.440 49.222  -26.449 1.00 12.37 ? 985  MET A N   1 
ATOM   7865 C  CA  . MET A 1 985  ? 36.621 48.382  -27.326 1.00 14.70 ? 985  MET A CA  1 
ATOM   7866 C  C   . MET A 1 985  ? 37.280 48.016  -28.623 1.00 15.28 ? 985  MET A C   1 
ATOM   7867 O  O   . MET A 1 985  ? 38.062 48.798  -29.216 1.00 15.44 ? 985  MET A O   1 
ATOM   7868 C  CB  . MET A 1 985  ? 35.318 49.078  -27.674 1.00 15.89 ? 985  MET A CB  1 
ATOM   7869 C  CG  . MET A 1 985  ? 34.444 49.201  -26.477 1.00 17.89 ? 985  MET A CG  1 
ATOM   7870 S  SD  . MET A 1 985  ? 32.730 49.386  -26.988 1.00 19.65 ? 985  MET A SD  1 
ATOM   7871 C  CE  . MET A 1 985  ? 32.851 50.931  -27.816 1.00 20.67 ? 985  MET A CE  1 
ATOM   7872 N  N   . GLN A 1 986  ? 36.995 46.786  -29.047 1.00 15.47 ? 986  GLN A N   1 
ATOM   7873 C  CA  . GLN A 1 986  ? 37.471 46.263  -30.343 1.00 16.71 ? 986  GLN A CA  1 
ATOM   7874 C  C   . GLN A 1 986  ? 36.446 46.772  -31.370 1.00 16.08 ? 986  GLN A C   1 
ATOM   7875 O  O   . GLN A 1 986  ? 35.250 46.427  -31.287 1.00 16.06 ? 986  GLN A O   1 
ATOM   7876 C  CB  . GLN A 1 986  ? 37.453 44.711  -30.341 1.00 18.75 ? 986  GLN A CB  1 
ATOM   7877 C  CG  . GLN A 1 986  ? 38.476 44.075  -29.439 1.00 22.14 ? 986  GLN A CG  1 
ATOM   7878 C  CD  . GLN A 1 986  ? 39.888 44.405  -29.865 1.00 24.95 ? 986  GLN A CD  1 
ATOM   7879 O  OE1 . GLN A 1 986  ? 40.766 44.617  -29.019 1.00 28.38 ? 986  GLN A OE1 1 
ATOM   7880 N  NE2 . GLN A 1 986  ? 40.128 44.450  -31.192 1.00 25.75 ? 986  GLN A NE2 1 
ATOM   7881 N  N   . CYS A 1 987  ? 36.887 47.604  -32.313 1.00 16.80 ? 987  CYS A N   1 
ATOM   7882 C  CA  . CYS A 1 987  ? 35.976 48.133  -33.324 1.00 18.18 ? 987  CYS A CA  1 
ATOM   7883 C  C   . CYS A 1 987  ? 36.502 47.940  -34.736 1.00 19.81 ? 987  CYS A C   1 
ATOM   7884 O  O   . CYS A 1 987  ? 36.013 48.607  -35.663 1.00 20.38 ? 987  CYS A O   1 
ATOM   7885 C  CB  . CYS A 1 987  ? 35.676 49.613  -33.097 1.00 18.21 ? 987  CYS A CB  1 
ATOM   7886 S  SG  . CYS A 1 987  ? 35.088 49.996  -31.412 1.00 19.33 ? 987  CYS A SG  1 
ATOM   7887 N  N   . GLY A 1 988  ? 37.464 47.034  -34.892 1.00 21.29 ? 988  GLY A N   1 
ATOM   7888 C  CA  . GLY A 1 988  ? 38.009 46.711  -36.204 1.00 27.42 ? 988  GLY A CA  1 
ATOM   7889 C  C   . GLY A 1 988  ? 39.138 47.568  -36.677 1.00 31.91 ? 988  GLY A C   1 
ATOM   7890 O  O   . GLY A 1 988  ? 39.477 47.553  -37.881 1.00 31.69 ? 988  GLY A O   1 
ATOM   7891 N  N   . THR A 1 989  ? 39.734 48.313  -35.747 1.00 35.98 ? 989  THR A N   1 
ATOM   7892 C  CA  . THR A 1 989  ? 40.862 49.173  -36.079 1.00 40.85 ? 989  THR A CA  1 
ATOM   7893 C  C   . THR A 1 989  ? 42.095 48.424  -35.612 1.00 44.20 ? 989  THR A C   1 
ATOM   7894 O  O   . THR A 1 989  ? 42.471 48.505  -34.448 1.00 44.56 ? 989  THR A O   1 
ATOM   7895 C  CB  . THR A 1 989  ? 40.811 50.499  -35.339 1.00 40.78 ? 989  THR A CB  1 
ATOM   7896 O  OG1 . THR A 1 989  ? 39.595 51.182  -35.649 1.00 41.06 ? 989  THR A OG1 1 
ATOM   7897 C  CG2 . THR A 1 989  ? 41.992 51.360  -35.752 1.00 41.72 ? 989  THR A CG2 1 
ATOM   7898 N  N   . PRO A 1 990  ? 42.741 47.681  -36.528 1.00 47.67 ? 990  PRO A N   1 
ATOM   7899 C  CA  . PRO A 1 990  ? 43.940 46.914  -36.181 1.00 50.16 ? 990  PRO A CA  1 
ATOM   7900 C  C   . PRO A 1 990  ? 44.819 47.615  -35.143 1.00 52.46 ? 990  PRO A C   1 
ATOM   7901 O  O   . PRO A 1 990  ? 44.808 47.240  -33.967 1.00 53.08 ? 990  PRO A O   1 
ATOM   7902 C  CB  . PRO A 1 990  ? 44.646 46.748  -37.525 1.00 50.06 ? 990  PRO A CB  1 
ATOM   7903 C  CG  . PRO A 1 990  ? 43.499 46.652  -38.496 1.00 49.61 ? 990  PRO A CG  1 
ATOM   7904 C  CD  . PRO A 1 990  ? 42.586 47.774  -37.995 1.00 48.64 ? 990  PRO A CD  1 
ATOM   7905 N  N   . GLU A 1 991  ? 45.547 48.649  -35.558 1.00 54.52 ? 991  GLU A N   1 
ATOM   7906 C  CA  . GLU A 1 991  ? 46.455 49.329  -34.632 1.00 56.87 ? 991  GLU A CA  1 
ATOM   7907 C  C   . GLU A 1 991  ? 47.418 48.240  -34.152 1.00 57.52 ? 991  GLU A C   1 
ATOM   7908 O  O   . GLU A 1 991  ? 47.114 47.491  -33.224 1.00 57.96 ? 991  GLU A O   1 
ATOM   7909 C  CB  . GLU A 1 991  ? 45.680 49.912  -33.446 1.00 57.63 ? 991  GLU A CB  1 
ATOM   7910 C  CG  . GLU A 1 991  ? 44.666 50.981  -33.839 1.00 58.97 ? 991  GLU A CG  1 
ATOM   7911 C  CD  . GLU A 1 991  ? 43.985 51.630  -32.640 1.00 59.60 ? 991  GLU A CD  1 
ATOM   7912 O  OE1 . GLU A 1 991  ? 43.174 50.955  -31.959 1.00 59.63 ? 991  GLU A OE1 1 
ATOM   7913 O  OE2 . GLU A 1 991  ? 44.272 52.821  -32.381 1.00 60.00 ? 991  GLU A OE2 1 
ATOM   7914 N  N   . GLU A 1 992  ? 48.575 48.129  -34.785 1.00 58.17 ? 992  GLU A N   1 
ATOM   7915 C  CA  . GLU A 1 992  ? 49.478 47.071  -34.377 1.00 58.66 ? 992  GLU A CA  1 
ATOM   7916 C  C   . GLU A 1 992  ? 50.861 47.509  -33.996 1.00 57.42 ? 992  GLU A C   1 
ATOM   7917 O  O   . GLU A 1 992  ? 51.057 48.592  -33.435 1.00 57.58 ? 992  GLU A O   1 
ATOM   7918 C  CB  . GLU A 1 992  ? 49.574 46.011  -35.478 1.00 60.84 ? 992  GLU A CB  1 
ATOM   7919 C  CG  . GLU A 1 992  ? 48.247 45.314  -35.788 1.00 63.59 ? 992  GLU A CG  1 
ATOM   7920 C  CD  . GLU A 1 992  ? 47.614 44.653  -34.559 1.00 65.24 ? 992  GLU A CD  1 
ATOM   7921 O  OE1 . GLU A 1 992  ? 48.171 44.762  -33.430 1.00 65.95 ? 992  GLU A OE1 1 
ATOM   7922 O  OE2 . GLU A 1 992  ? 46.546 44.019  -34.732 1.00 66.34 ? 992  GLU A OE2 1 
ATOM   7923 N  N   . HIS A 1 993  ? 51.809 46.631  -34.320 1.00 55.66 ? 993  HIS A N   1 
ATOM   7924 C  CA  . HIS A 1 993  ? 53.236 46.806  -34.058 1.00 53.49 ? 993  HIS A CA  1 
ATOM   7925 C  C   . HIS A 1 993  ? 53.632 47.670  -32.869 1.00 50.11 ? 993  HIS A C   1 
ATOM   7926 O  O   . HIS A 1 993  ? 54.019 48.843  -33.032 1.00 50.21 ? 993  HIS A O   1 
ATOM   7927 C  CB  . HIS A 1 993  ? 53.995 47.301  -35.325 1.00 56.27 ? 993  HIS A CB  1 
ATOM   7928 C  CG  . HIS A 1 993  ? 53.498 48.601  -35.892 1.00 58.63 ? 993  HIS A CG  1 
ATOM   7929 N  ND1 . HIS A 1 993  ? 52.327 48.702  -36.617 1.00 59.96 ? 993  HIS A ND1 1 
ATOM   7930 C  CD2 . HIS A 1 993  ? 54.029 49.848  -35.864 1.00 59.78 ? 993  HIS A CD2 1 
ATOM   7931 C  CE1 . HIS A 1 993  ? 52.159 49.953  -37.011 1.00 60.60 ? 993  HIS A CE1 1 
ATOM   7932 N  NE2 . HIS A 1 993  ? 53.178 50.670  -36.567 1.00 60.60 ? 993  HIS A NE2 1 
ATOM   7933 N  N   . THR A 1 994  ? 53.508 47.106  -31.667 1.00 45.29 ? 994  THR A N   1 
ATOM   7934 C  CA  . THR A 1 994  ? 53.954 47.835  -30.490 1.00 40.08 ? 994  THR A CA  1 
ATOM   7935 C  C   . THR A 1 994  ? 54.951 46.971  -29.742 1.00 36.46 ? 994  THR A C   1 
ATOM   7936 O  O   . THR A 1 994  ? 54.947 45.732  -29.834 1.00 36.24 ? 994  THR A O   1 
ATOM   7937 C  CB  . THR A 1 994  ? 52.800 48.268  -29.546 1.00 40.08 ? 994  THR A CB  1 
ATOM   7938 O  OG1 . THR A 1 994  ? 52.066 47.125  -29.100 1.00 39.52 ? 994  THR A OG1 1 
ATOM   7939 C  CG2 . THR A 1 994  ? 51.876 49.227  -30.273 1.00 39.54 ? 994  THR A CG2 1 
ATOM   7940 N  N   . GLN A 1 995  ? 55.807 47.634  -28.981 1.00 31.45 ? 995  GLN A N   1 
ATOM   7941 C  CA  . GLN A 1 995  ? 56.839 46.937  -28.247 1.00 26.70 ? 995  GLN A CA  1 
ATOM   7942 C  C   . GLN A 1 995  ? 56.437 46.577  -26.829 1.00 23.63 ? 995  GLN A C   1 
ATOM   7943 O  O   . GLN A 1 995  ? 55.712 47.324  -26.176 1.00 21.45 ? 995  GLN A O   1 
ATOM   7944 C  CB  . GLN A 1 995  ? 58.067 47.823  -28.175 1.00 26.52 ? 995  GLN A CB  1 
ATOM   7945 C  CG  . GLN A 1 995  ? 58.546 48.285  -29.528 1.00 27.45 ? 995  GLN A CG  1 
ATOM   7946 C  CD  . GLN A 1 995  ? 59.485 49.482  -29.429 1.00 28.60 ? 995  GLN A CD  1 
ATOM   7947 O  OE1 . GLN A 1 995  ? 59.078 50.580  -29.065 1.00 25.41 ? 995  GLN A OE1 1 
ATOM   7948 N  NE2 . GLN A 1 995  ? 60.763 49.264  -29.758 1.00 29.83 ? 995  GLN A NE2 1 
ATOM   7949 N  N   . LYS A 1 996  ? 56.902 45.423  -26.365 1.00 20.95 ? 996  LYS A N   1 
ATOM   7950 C  CA  . LYS A 1 996  ? 56.662 44.992  -25.001 1.00 20.71 ? 996  LYS A CA  1 
ATOM   7951 C  C   . LYS A 1 996  ? 57.362 45.989  -24.062 1.00 18.89 ? 996  LYS A C   1 
ATOM   7952 O  O   . LYS A 1 996  ? 58.541 46.376  -24.274 1.00 18.26 ? 996  LYS A O   1 
ATOM   7953 C  CB  . LYS A 1 996  ? 57.268 43.566  -24.810 1.00 22.50 ? 996  LYS A CB  1 
ATOM   7954 C  CG  . LYS A 1 996  ? 57.221 43.020  -23.382 1.00 26.04 ? 996  LYS A CG  1 
ATOM   7955 C  CD  . LYS A 1 996  ? 57.813 41.570  -23.324 1.00 29.36 ? 996  LYS A CD  1 
ATOM   7956 C  CE  . LYS A 1 996  ? 57.790 40.967  -21.901 1.00 31.11 ? 996  LYS A CE  1 
ATOM   7957 N  NZ  . LYS A 1 996  ? 58.279 39.533  -21.927 1.00 33.86 ? 996  LYS A NZ  1 
ATOM   7958 N  N   . LEU A 1 997  ? 56.642 46.387  -23.008 1.00 17.66 ? 997  LEU A N   1 
ATOM   7959 C  CA  . LEU A 1 997  ? 57.252 47.268  -22.036 1.00 16.32 ? 997  LEU A CA  1 
ATOM   7960 C  C   . LEU A 1 997  ? 57.607 46.451  -20.796 1.00 15.68 ? 997  LEU A C   1 
ATOM   7961 O  O   . LEU A 1 997  ? 56.711 45.876  -20.165 1.00 16.82 ? 997  LEU A O   1 
ATOM   7962 C  CB  . LEU A 1 997  ? 56.280 48.403  -21.665 1.00 16.58 ? 997  LEU A CB  1 
ATOM   7963 C  CG  . LEU A 1 997  ? 56.827 49.261  -20.499 1.00 17.09 ? 997  LEU A CG  1 
ATOM   7964 C  CD1 . LEU A 1 997  ? 58.099 50.041  -20.829 1.00 18.24 ? 997  LEU A CD1 1 
ATOM   7965 C  CD2 . LEU A 1 997  ? 55.758 50.251  -20.151 1.00 17.66 ? 997  LEU A CD2 1 
ATOM   7966 N  N   . ASP A 1 998  ? 58.912 46.376  -20.489 1.00 14.59 ? 998  ASP A N   1 
ATOM   7967 C  CA  . ASP A 1 998  ? 59.376 45.689  -19.271 1.00 14.77 ? 998  ASP A CA  1 
ATOM   7968 C  C   . ASP A 1 998  ? 59.957 46.790  -18.403 1.00 14.47 ? 998  ASP A C   1 
ATOM   7969 O  O   . ASP A 1 998  ? 61.104 47.257  -18.620 1.00 14.09 ? 998  ASP A O   1 
ATOM   7970 C  CB  . ASP A 1 998  ? 60.462 44.652  -19.609 1.00 15.50 ? 998  ASP A CB  1 
ATOM   7971 C  CG  . ASP A 1 998  ? 61.141 44.129  -18.378 1.00 17.91 ? 998  ASP A CG  1 
ATOM   7972 O  OD1 . ASP A 1 998  ? 60.606 44.315  -17.249 1.00 17.44 ? 998  ASP A OD1 1 
ATOM   7973 O  OD2 . ASP A 1 998  ? 62.232 43.517  -18.545 1.00 19.31 ? 998  ASP A OD2 1 
ATOM   7974 N  N   . VAL A 1 999  ? 59.171 47.262  -17.426 1.00 13.57 ? 999  VAL A N   1 
ATOM   7975 C  CA  . VAL A 1 999  ? 59.703 48.378  -16.641 1.00 12.53 ? 999  VAL A CA  1 
ATOM   7976 C  C   . VAL A 1 999  ? 60.954 48.075  -15.851 1.00 12.43 ? 999  VAL A C   1 
ATOM   7977 O  O   . VAL A 1 999  ? 61.732 48.973  -15.500 1.00 12.75 ? 999  VAL A O   1 
ATOM   7978 C  CB  . VAL A 1 999  ? 58.645 48.967  -15.673 1.00 12.28 ? 999  VAL A CB  1 
ATOM   7979 C  CG1 . VAL A 1 999  ? 57.486 49.597  -16.482 1.00 13.58 ? 999  VAL A CG1 1 
ATOM   7980 C  CG2 . VAL A 1 999  ? 58.080 47.903  -14.732 1.00 14.35 ? 999  VAL A CG2 1 
ATOM   7981 N  N   . CYS A 1 1000 ? 61.166 46.786  -15.602 1.00 13.67 ? 1000 CYS A N   1 
ATOM   7982 C  CA  . CYS A 1 1000 ? 62.334 46.454  -14.808 1.00 15.68 ? 1000 CYS A CA  1 
ATOM   7983 C  C   . CYS A 1 1000 ? 63.670 46.660  -15.516 1.00 15.74 ? 1000 CYS A C   1 
ATOM   7984 O  O   . CYS A 1 1000 ? 64.687 46.763  -14.859 1.00 16.62 ? 1000 CYS A O   1 
ATOM   7985 C  CB  . CYS A 1 1000 ? 62.213 45.038  -14.228 1.00 17.33 ? 1000 CYS A CB  1 
ATOM   7986 S  SG  . CYS A 1 1000 ? 61.313 45.070  -12.596 1.00 20.73 ? 1000 CYS A SG  1 
ATOM   7987 N  N   . HIS A 1 1001 ? 63.632 46.814  -16.839 1.00 15.12 ? 1001 HIS A N   1 
ATOM   7988 C  CA  . HIS A 1 1001 ? 64.858 47.045  -17.594 1.00 15.76 ? 1001 HIS A CA  1 
ATOM   7989 C  C   . HIS A 1 1001 ? 64.926 48.494  -18.096 1.00 15.56 ? 1001 HIS A C   1 
ATOM   7990 O  O   . HIS A 1 1001 ? 65.776 48.852  -18.914 1.00 17.57 ? 1001 HIS A O   1 
ATOM   7991 C  CB  . HIS A 1 1001 ? 64.996 46.030  -18.756 1.00 16.71 ? 1001 HIS A CB  1 
ATOM   7992 C  CG  . HIS A 1 1001 ? 65.547 44.707  -18.326 1.00 17.22 ? 1001 HIS A CG  1 
ATOM   7993 N  ND1 . HIS A 1 1001 ? 64.753 43.698  -17.837 1.00 18.36 ? 1001 HIS A ND1 1 
ATOM   7994 C  CD2 . HIS A 1 1001 ? 66.825 44.245  -18.258 1.00 18.42 ? 1001 HIS A CD2 1 
ATOM   7995 C  CE1 . HIS A 1 1001 ? 65.508 42.667  -17.484 1.00 18.27 ? 1001 HIS A CE1 1 
ATOM   7996 N  NE2 . HIS A 1 1001 ? 66.768 42.973  -17.732 1.00 18.09 ? 1001 HIS A NE2 1 
ATOM   7997 N  N   . LEU A 1 1002 ? 64.037 49.372  -17.612 1.00 15.30 ? 1002 LEU A N   1 
ATOM   7998 C  CA  . LEU A 1 1002 ? 64.114 50.777  -18.036 1.00 14.88 ? 1002 LEU A CA  1 
ATOM   7999 C  C   . LEU A 1 1002 ? 65.380 51.458  -17.508 1.00 15.77 ? 1002 LEU A C   1 
ATOM   8000 O  O   . LEU A 1 1002 ? 65.873 52.388  -18.155 1.00 17.71 ? 1002 LEU A O   1 
ATOM   8001 C  CB  . LEU A 1 1002 ? 62.899 51.583  -17.544 1.00 13.95 ? 1002 LEU A CB  1 
ATOM   8002 C  CG  . LEU A 1 1002 ? 61.682 51.391  -18.387 1.00 13.38 ? 1002 LEU A CG  1 
ATOM   8003 C  CD1 . LEU A 1 1002 ? 60.475 52.014  -17.651 1.00 13.10 ? 1002 LEU A CD1 1 
ATOM   8004 C  CD2 . LEU A 1 1002 ? 61.878 52.048  -19.730 1.00 15.59 ? 1002 LEU A CD2 1 
ATOM   8005 N  N   . LEU A 1 1003 ? 65.883 51.046  -16.341 1.00 15.85 ? 1003 LEU A N   1 
ATOM   8006 C  CA  . LEU A 1 1003 ? 67.118 51.592  -15.793 1.00 16.05 ? 1003 LEU A CA  1 
ATOM   8007 C  C   . LEU A 1 1003 ? 68.146 50.477  -15.923 1.00 16.78 ? 1003 LEU A C   1 
ATOM   8008 O  O   . LEU A 1 1003 ? 67.823 49.285  -15.777 1.00 17.39 ? 1003 LEU A O   1 
ATOM   8009 C  CB  . LEU A 1 1003 ? 66.978 52.021  -14.333 1.00 16.52 ? 1003 LEU A CB  1 
ATOM   8010 C  CG  . LEU A 1 1003 ? 66.298 53.395  -14.218 1.00 19.31 ? 1003 LEU A CG  1 
ATOM   8011 C  CD1 . LEU A 1 1003 ? 65.651 53.514  -12.877 1.00 21.39 ? 1003 LEU A CD1 1 
ATOM   8012 C  CD2 . LEU A 1 1003 ? 67.318 54.518  -14.486 1.00 21.01 ? 1003 LEU A CD2 1 
ATOM   8013 N  N   . PRO A 1 1004 ? 69.399 50.859  -16.140 1.00 17.32 ? 1004 PRO A N   1 
ATOM   8014 C  CA  . PRO A 1 1004 ? 70.423 49.827  -16.295 1.00 17.21 ? 1004 PRO A CA  1 
ATOM   8015 C  C   . PRO A 1 1004 ? 70.841 49.120  -15.028 1.00 17.07 ? 1004 PRO A C   1 
ATOM   8016 O  O   . PRO A 1 1004 ? 70.507 49.506  -13.891 1.00 16.47 ? 1004 PRO A O   1 
ATOM   8017 C  CB  . PRO A 1 1004 ? 71.575 50.597  -16.908 1.00 18.05 ? 1004 PRO A CB  1 
ATOM   8018 C  CG  . PRO A 1 1004 ? 71.487 51.923  -16.212 1.00 18.37 ? 1004 PRO A CG  1 
ATOM   8019 C  CD  . PRO A 1 1004 ? 69.975 52.217  -16.222 1.00 17.51 ? 1004 PRO A CD  1 
ATOM   8020 N  N   . ASN A 1 1005 ? 71.582 48.033  -15.254 1.00 17.48 ? 1005 ASN A N   1 
ATOM   8021 C  CA  . ASN A 1 1005 ? 72.153 47.242  -14.171 1.00 17.22 ? 1005 ASN A CA  1 
ATOM   8022 C  C   . ASN A 1 1005 ? 71.122 46.681  -13.215 1.00 16.60 ? 1005 ASN A C   1 
ATOM   8023 O  O   . ASN A 1 1005 ? 71.316 46.709  -12.023 1.00 16.55 ? 1005 ASN A O   1 
ATOM   8024 C  CB  . ASN A 1 1005 ? 73.145 48.087  -13.377 1.00 19.65 ? 1005 ASN A CB  1 
ATOM   8025 C  CG  . ASN A 1 1005 ? 74.104 48.828  -14.271 1.00 22.94 ? 1005 ASN A CG  1 
ATOM   8026 O  OD1 . ASN A 1 1005 ? 74.177 50.061  -14.238 1.00 25.97 ? 1005 ASN A OD1 1 
ATOM   8027 N  ND2 . ASN A 1 1005 ? 74.820 48.096  -15.084 1.00 23.36 ? 1005 ASN A ND2 1 
ATOM   8028 N  N   . VAL A 1 1006 ? 70.015 46.206  -13.751 1.00 17.20 ? 1006 VAL A N   1 
ATOM   8029 C  CA  . VAL A 1 1006 ? 69.024 45.641  -12.879 1.00 17.19 ? 1006 VAL A CA  1 
ATOM   8030 C  C   . VAL A 1 1006 ? 69.590 44.343  -12.275 1.00 17.25 ? 1006 VAL A C   1 
ATOM   8031 O  O   . VAL A 1 1006 ? 70.293 43.565  -12.941 1.00 19.64 ? 1006 VAL A O   1 
ATOM   8032 C  CB  . VAL A 1 1006 ? 67.656 45.396  -13.639 1.00 16.89 ? 1006 VAL A CB  1 
ATOM   8033 C  CG1 . VAL A 1 1006 ? 67.768 44.385  -14.733 1.00 18.09 ? 1006 VAL A CG1 1 
ATOM   8034 C  CG2 . VAL A 1 1006 ? 66.575 44.946  -12.619 1.00 17.35 ? 1006 VAL A CG2 1 
ATOM   8035 N  N   . ALA A 1 1007 ? 69.299 44.154  -11.008 1.00 16.32 ? 1007 ALA A N   1 
ATOM   8036 C  CA  . ALA A 1 1007 ? 69.747 42.979  -10.272 1.00 17.48 ? 1007 ALA A CA  1 
ATOM   8037 C  C   . ALA A 1 1007 ? 68.584 42.165  -9.743  1.00 17.98 ? 1007 ALA A C   1 
ATOM   8038 O  O   . ALA A 1 1007 ? 68.755 41.007  -9.371  1.00 18.94 ? 1007 ALA A O   1 
ATOM   8039 C  CB  . ALA A 1 1007 ? 70.640 43.431  -9.121  1.00 17.46 ? 1007 ALA A CB  1 
ATOM   8040 N  N   . ARG A 1 1008 ? 67.382 42.753  -9.684  1.00 17.51 ? 1008 ARG A N   1 
ATOM   8041 C  CA  . ARG A 1 1008 ? 66.242 42.034  -9.158  1.00 16.90 ? 1008 ARG A CA  1 
ATOM   8042 C  C   . ARG A 1 1008 ? 64.995 42.790  -9.593  1.00 15.64 ? 1008 ARG A C   1 
ATOM   8043 O  O   . ARG A 1 1008 ? 65.046 44.013  -9.713  1.00 15.73 ? 1008 ARG A O   1 
ATOM   8044 C  CB  . ARG A 1 1008 ? 66.305 42.017  -7.639  1.00 18.85 ? 1008 ARG A CB  1 
ATOM   8045 C  CG  . ARG A 1 1008 ? 65.283 41.135  -6.998  1.00 22.17 ? 1008 ARG A CG  1 
ATOM   8046 C  CD  . ARG A 1 1008 ? 65.385 41.324  -5.484  1.00 25.72 ? 1008 ARG A CD  1 
ATOM   8047 N  NE  . ARG A 1 1008 ? 64.648 40.297  -4.757  1.00 30.16 ? 1008 ARG A NE  1 
ATOM   8048 C  CZ  . ARG A 1 1008 ? 65.035 39.026  -4.665  1.00 32.25 ? 1008 ARG A CZ  1 
ATOM   8049 N  NH1 . ARG A 1 1008 ? 66.167 38.626  -5.257  1.00 33.68 ? 1008 ARG A NH1 1 
ATOM   8050 N  NH2 . ARG A 1 1008 ? 64.291 38.152  -3.982  1.00 32.90 ? 1008 ARG A NH2 1 
ATOM   8051 N  N   . CYS A 1 1009 ? 63.911 42.071  -9.822  1.00 14.83 ? 1009 CYS A N   1 
ATOM   8052 C  CA  . CYS A 1 1009 ? 62.631 42.686  -10.222 1.00 15.67 ? 1009 CYS A CA  1 
ATOM   8053 C  C   . CYS A 1 1009 ? 61.577 41.937  -9.397  1.00 14.96 ? 1009 CYS A C   1 
ATOM   8054 O  O   . CYS A 1 1009 ? 61.503 40.701  -9.463  1.00 15.36 ? 1009 CYS A O   1 
ATOM   8055 C  CB  . CYS A 1 1009 ? 62.417 42.461  -11.696 1.00 16.99 ? 1009 CYS A CB  1 
ATOM   8056 S  SG  . CYS A 1 1009 ? 60.833 43.150  -12.310 1.00 21.80 ? 1009 CYS A SG  1 
ATOM   8057 N  N   . GLU A 1 1010 ? 60.742 42.679  -8.649  1.00 13.66 ? 1010 GLU A N   1 
ATOM   8058 C  CA  . GLU A 1 1010 ? 59.723 42.094  -7.821  1.00 13.91 ? 1010 GLU A CA  1 
ATOM   8059 C  C   . GLU A 1 1010 ? 58.355 42.678  -8.108  1.00 12.61 ? 1010 GLU A C   1 
ATOM   8060 O  O   . GLU A 1 1010 ? 58.232 43.864  -8.399  1.00 12.94 ? 1010 GLU A O   1 
ATOM   8061 C  CB  . GLU A 1 1010 ? 60.068 42.384  -6.349  1.00 15.68 ? 1010 GLU A CB  1 
ATOM   8062 C  CG  . GLU A 1 1010 ? 61.321 41.574  -5.900  1.00 20.50 ? 1010 GLU A CG  1 
ATOM   8063 C  CD  . GLU A 1 1010 ? 62.096 42.167  -4.723  1.00 23.20 ? 1010 GLU A CD  1 
ATOM   8064 O  OE1 . GLU A 1 1010 ? 62.555 43.342  -4.772  1.00 23.75 ? 1010 GLU A OE1 1 
ATOM   8065 O  OE2 . GLU A 1 1010 ? 62.260 41.424  -3.721  1.00 26.19 ? 1010 GLU A OE2 1 
ATOM   8066 N  N   . ARG A 1 1011 ? 57.343 41.855  -8.046  1.00 12.69 ? 1011 ARG A N   1 
ATOM   8067 C  CA  . ARG A 1 1011 ? 55.985 42.395  -8.080  1.00 11.43 ? 1011 ARG A CA  1 
ATOM   8068 C  C   . ARG A 1 1011 ? 55.673 42.752  -6.619  1.00 11.11 ? 1011 ARG A C   1 
ATOM   8069 O  O   . ARG A 1 1011 ? 56.001 42.004  -5.669  1.00 11.73 ? 1011 ARG A O   1 
ATOM   8070 C  CB  . ARG A 1 1011 ? 55.008 41.358  -8.602  1.00 13.24 ? 1011 ARG A CB  1 
ATOM   8071 C  CG  . ARG A 1 1011 ? 53.622 42.043  -8.839  1.00 16.42 ? 1011 ARG A CG  1 
ATOM   8072 C  CD  . ARG A 1 1011 ? 52.659 41.156  -9.531  1.00 19.88 ? 1011 ARG A CD  1 
ATOM   8073 N  NE  . ARG A 1 1011 ? 52.353 40.001  -8.715  1.00 23.49 ? 1011 ARG A NE  1 
ATOM   8074 C  CZ  . ARG A 1 1011 ? 51.371 39.956  -7.807  1.00 26.13 ? 1011 ARG A CZ  1 
ATOM   8075 N  NH1 . ARG A 1 1011 ? 50.587 41.028  -7.605  1.00 27.71 ? 1011 ARG A NH1 1 
ATOM   8076 N  NH2 . ARG A 1 1011 ? 51.164 38.843  -7.095  1.00 27.64 ? 1011 ARG A NH2 1 
ATOM   8077 N  N   . THR A 1 1012 ? 55.032 43.907  -6.408  1.00 10.07 ? 1012 THR A N   1 
ATOM   8078 C  CA  . THR A 1 1012 ? 54.707 44.330  -5.050  1.00 9.19  ? 1012 THR A CA  1 
ATOM   8079 C  C   . THR A 1 1012 ? 53.252 44.780  -4.946  1.00 9.28  ? 1012 THR A C   1 
ATOM   8080 O  O   . THR A 1 1012 ? 52.543 44.930  -5.946  1.00 10.34 ? 1012 THR A O   1 
ATOM   8081 C  CB  . THR A 1 1012 ? 55.572 45.557  -4.598  1.00 9.72  ? 1012 THR A CB  1 
ATOM   8082 O  OG1 . THR A 1 1012 ? 55.260 46.701  -5.439  1.00 11.00 ? 1012 THR A OG1 1 
ATOM   8083 C  CG2 . THR A 1 1012 ? 57.067 45.277  -4.831  1.00 11.41 ? 1012 THR A CG2 1 
ATOM   8084 N  N   . THR A 1 1013 ? 52.820 44.986  -3.706  1.00 8.85  ? 1013 THR A N   1 
ATOM   8085 C  CA  . THR A 1 1013 ? 51.527 45.646  -3.524  1.00 9.10  ? 1013 THR A CA  1 
ATOM   8086 C  C   . THR A 1 1013 ? 51.637 47.067  -4.146  1.00 8.53  ? 1013 THR A C   1 
ATOM   8087 O  O   . THR A 1 1013 ? 52.714 47.619  -4.381  1.00 8.38  ? 1013 THR A O   1 
ATOM   8088 C  CB  . THR A 1 1013 ? 51.213 45.793  -2.060  1.00 8.74  ? 1013 THR A CB  1 
ATOM   8089 O  OG1 . THR A 1 1013 ? 52.393 46.225  -1.371  1.00 9.91  ? 1013 THR A OG1 1 
ATOM   8090 C  CG2 . THR A 1 1013 ? 50.703 44.433  -1.478  1.00 11.16 ? 1013 THR A CG2 1 
ATOM   8091 N  N   . LEU A 1 1014 ? 50.479 47.687  -4.400  1.00 8.32  ? 1014 LEU A N   1 
ATOM   8092 C  CA  . LEU A 1 1014 ? 50.510 48.992  -5.105  1.00 7.81  ? 1014 LEU A CA  1 
ATOM   8093 C  C   . LEU A 1 1014 ? 51.166 50.134  -4.394  1.00 6.30  ? 1014 LEU A C   1 
ATOM   8094 O  O   . LEU A 1 1014 ? 51.523 51.131  -5.020  1.00 8.12  ? 1014 LEU A O   1 
ATOM   8095 C  CB  . LEU A 1 1014 ? 49.077 49.430  -5.532  1.00 8.18  ? 1014 LEU A CB  1 
ATOM   8096 C  CG  . LEU A 1 1014 ? 48.299 48.464  -6.428  1.00 7.60  ? 1014 LEU A CG  1 
ATOM   8097 C  CD1 . LEU A 1 1014 ? 46.968 49.155  -6.830  1.00 8.21  ? 1014 LEU A CD1 1 
ATOM   8098 C  CD2 . LEU A 1 1014 ? 49.070 48.119  -7.731  1.00 9.21  ? 1014 LEU A CD2 1 
ATOM   8099 N  N   . THR A 1 1015 ? 51.353 49.988  -3.076  1.00 7.28  ? 1015 THR A N   1 
ATOM   8100 C  CA  . THR A 1 1015 ? 52.011 50.976  -2.215  1.00 7.65  ? 1015 THR A CA  1 
ATOM   8101 C  C   . THR A 1 1015 ? 53.514 50.688  -2.149  1.00 7.36  ? 1015 THR A C   1 
ATOM   8102 O  O   . THR A 1 1015 ? 54.216 51.437  -1.489  1.00 8.75  ? 1015 THR A O   1 
ATOM   8103 C  CB  . THR A 1 1015 ? 51.497 50.835  -0.780  1.00 7.83  ? 1015 THR A CB  1 
ATOM   8104 O  OG1 . THR A 1 1015 ? 51.658 49.455  -0.425  1.00 8.43  ? 1015 THR A OG1 1 
ATOM   8105 C  CG2 . THR A 1 1015 ? 50.005 51.212  -0.689  1.00 9.48  ? 1015 THR A CG2 1 
ATOM   8106 N  N   . PHE A 1 1016 ? 53.970 49.624  -2.824  1.00 7.90  ? 1016 PHE A N   1 
ATOM   8107 C  CA  . PHE A 1 1016 ? 55.392 49.166  -2.856  1.00 8.93  ? 1016 PHE A CA  1 
ATOM   8108 C  C   . PHE A 1 1016 ? 55.880 48.636  -1.512  1.00 10.44 ? 1016 PHE A C   1 
ATOM   8109 O  O   . PHE A 1 1016 ? 57.062 48.324  -1.407  1.00 10.94 ? 1016 PHE A O   1 
ATOM   8110 C  CB  . PHE A 1 1016 ? 56.348 50.307  -3.311  1.00 9.36  ? 1016 PHE A CB  1 
ATOM   8111 C  CG  . PHE A 1 1016 ? 55.996 50.934  -4.640  1.00 9.05  ? 1016 PHE A CG  1 
ATOM   8112 C  CD1 . PHE A 1 1016 ? 55.895 50.170  -5.792  1.00 8.90  ? 1016 PHE A CD1 1 
ATOM   8113 C  CD2 . PHE A 1 1016 ? 55.800 52.321  -4.715  1.00 9.60  ? 1016 PHE A CD2 1 
ATOM   8114 C  CE1 . PHE A 1 1016 ? 55.582 50.802  -7.033  1.00 10.21 ? 1016 PHE A CE1 1 
ATOM   8115 C  CE2 . PHE A 1 1016 ? 55.504 52.941  -5.924  1.00 8.76  ? 1016 PHE A CE2 1 
ATOM   8116 C  CZ  . PHE A 1 1016 ? 55.396 52.149  -7.088  1.00 9.66  ? 1016 PHE A CZ  1 
ATOM   8117 N  N   . LEU A 1 1017 ? 54.969 48.420  -0.559  1.00 9.88  ? 1017 LEU A N   1 
ATOM   8118 C  CA  . LEU A 1 1017 ? 55.394 48.009  0.796   1.00 10.75 ? 1017 LEU A CA  1 
ATOM   8119 C  C   . LEU A 1 1017 ? 55.570 46.528  1.047   1.00 11.85 ? 1017 LEU A C   1 
ATOM   8120 O  O   . LEU A 1 1017 ? 56.194 46.184  2.080   1.00 15.56 ? 1017 LEU A O   1 
ATOM   8121 C  CB  . LEU A 1 1017 ? 54.438 48.631  1.827   1.00 11.15 ? 1017 LEU A CB  1 
ATOM   8122 C  CG  . LEU A 1 1017 ? 54.428 50.150  1.768   1.00 10.39 ? 1017 LEU A CG  1 
ATOM   8123 C  CD1 . LEU A 1 1017 ? 53.377 50.655  2.766   1.00 10.16 ? 1017 LEU A CD1 1 
ATOM   8124 C  CD2 . LEU A 1 1017 ? 55.791 50.740  2.097   1.00 12.14 ? 1017 LEU A CD2 1 
ATOM   8125 N  N   . GLN A 1 1018 ? 55.097 45.672  0.149   1.00 11.34 ? 1018 GLN A N   1 
ATOM   8126 C  CA  . GLN A 1 1018 ? 55.271 44.240  0.350   1.00 12.66 ? 1018 GLN A CA  1 
ATOM   8127 C  C   . GLN A 1 1018 ? 55.612 43.567  -0.965  1.00 12.77 ? 1018 GLN A C   1 
ATOM   8128 O  O   . GLN A 1 1018 ? 54.972 43.822  -1.986  1.00 12.74 ? 1018 GLN A O   1 
ATOM   8129 C  CB  . GLN A 1 1018 ? 53.997 43.605  0.924   1.00 13.81 ? 1018 GLN A CB  1 
ATOM   8130 C  CG  . GLN A 1 1018 ? 54.175 42.063  1.138   1.00 17.73 ? 1018 GLN A CG  1 
ATOM   8131 C  CD  . GLN A 1 1018 ? 52.877 41.317  1.425   1.00 21.49 ? 1018 GLN A CD  1 
ATOM   8132 O  OE1 . GLN A 1 1018 ? 51.803 41.898  1.496   1.00 22.50 ? 1018 GLN A OE1 1 
ATOM   8133 N  NE2 . GLN A 1 1018 ? 52.986 39.985  1.588   1.00 23.20 ? 1018 GLN A NE2 1 
ATOM   8134 N  N   . ASN A 1 1019 ? 56.637 42.697  -0.935  1.00 13.56 ? 1019 ASN A N   1 
ATOM   8135 C  CA  . ASN A 1 1019 ? 57.048 41.951  -2.100  1.00 15.09 ? 1019 ASN A CA  1 
ATOM   8136 C  C   . ASN A 1 1019 ? 56.149 40.760  -2.243  1.00 16.44 ? 1019 ASN A C   1 
ATOM   8137 O  O   . ASN A 1 1019 ? 55.978 39.965  -1.281  1.00 17.65 ? 1019 ASN A O   1 
ATOM   8138 C  CB  . ASN A 1 1019 ? 58.536 41.518  -1.991  1.00 16.62 ? 1019 ASN A CB  1 
ATOM   8139 C  CG  . ASN A 1 1019 ? 59.470 42.711  -1.901  1.00 18.82 ? 1019 ASN A CG  1 
ATOM   8140 O  OD1 . ASN A 1 1019 ? 59.211 43.742  -2.502  1.00 19.84 ? 1019 ASN A OD1 1 
ATOM   8141 N  ND2 . ASN A 1 1019 ? 60.577 42.582  -1.150  1.00 20.32 ? 1019 ASN A ND2 1 
ATOM   8142 N  N   . LEU A 1 1020 ? 55.557 40.610  -3.407  1.00 16.02 ? 1020 LEU A N   1 
ATOM   8143 C  CA  . LEU A 1 1020 ? 54.637 39.511  -3.654  1.00 17.77 ? 1020 LEU A CA  1 
ATOM   8144 C  C   . LEU A 1 1020 ? 55.208 38.407  -4.528  1.00 18.77 ? 1020 LEU A C   1 
ATOM   8145 O  O   . LEU A 1 1020 ? 54.761 37.243  -4.449  1.00 19.84 ? 1020 LEU A O   1 
ATOM   8146 C  CB  . LEU A 1 1020 ? 53.357 40.007  -4.341  1.00 17.54 ? 1020 LEU A CB  1 
ATOM   8147 C  CG  . LEU A 1 1020 ? 52.594 41.104  -3.612  1.00 17.41 ? 1020 LEU A CG  1 
ATOM   8148 C  CD1 . LEU A 1 1020 ? 51.453 41.585  -4.530  1.00 19.29 ? 1020 LEU A CD1 1 
ATOM   8149 C  CD2 . LEU A 1 1020 ? 52.048 40.576  -2.251  1.00 18.09 ? 1020 LEU A CD2 1 
ATOM   8150 N  N   . GLU A 1 1021 ? 56.164 38.745  -5.377  1.00 18.96 ? 1021 GLU A N   1 
ATOM   8151 C  CA  . GLU A 1 1021 ? 56.718 37.756  -6.319  1.00 21.01 ? 1021 GLU A CA  1 
ATOM   8152 C  C   . GLU A 1 1021 ? 58.091 38.175  -6.795  1.00 21.05 ? 1021 GLU A C   1 
ATOM   8153 O  O   . GLU A 1 1021 ? 58.321 39.337  -7.129  1.00 18.94 ? 1021 GLU A O   1 
ATOM   8154 C  CB  . GLU A 1 1021 ? 55.765 37.666  -7.510  1.00 23.57 ? 1021 GLU A CB  1 
ATOM   8155 C  CG  . GLU A 1 1021 ? 56.027 36.602  -8.532  1.00 29.06 ? 1021 GLU A CG  1 
ATOM   8156 C  CD  . GLU A 1 1021 ? 54.984 36.626  -9.647  1.00 31.01 ? 1021 GLU A CD  1 
ATOM   8157 O  OE1 . GLU A 1 1021 ? 54.117 37.555  -9.671  1.00 33.24 ? 1021 GLU A OE1 1 
ATOM   8158 O  OE2 . GLU A 1 1021 ? 55.045 35.710  -10.507 1.00 34.29 ? 1021 GLU A OE2 1 
ATOM   8159 N  N   . HIS A 1 1022 ? 59.036 37.228  -6.829  1.00 21.54 ? 1022 HIS A N   1 
ATOM   8160 C  CA  . HIS A 1 1022 ? 60.385 37.491  -7.282  1.00 22.02 ? 1022 HIS A CA  1 
ATOM   8161 C  C   . HIS A 1 1022 ? 60.333 37.081  -8.740  1.00 21.80 ? 1022 HIS A C   1 
ATOM   8162 O  O   . HIS A 1 1022 ? 60.023 35.932  -9.065  1.00 22.34 ? 1022 HIS A O   1 
ATOM   8163 C  CB  . HIS A 1 1022 ? 61.366 36.631  -6.492  1.00 24.19 ? 1022 HIS A CB  1 
ATOM   8164 C  CG  . HIS A 1 1022 ? 62.778 36.832  -6.908  1.00 26.80 ? 1022 HIS A CG  1 
ATOM   8165 N  ND1 . HIS A 1 1022 ? 63.690 35.795  -6.956  1.00 29.26 ? 1022 HIS A ND1 1 
ATOM   8166 C  CD2 . HIS A 1 1022 ? 63.437 37.941  -7.327  1.00 27.88 ? 1022 HIS A CD2 1 
ATOM   8167 C  CE1 . HIS A 1 1022 ? 64.849 36.256  -7.395  1.00 29.20 ? 1022 HIS A CE1 1 
ATOM   8168 N  NE2 . HIS A 1 1022 ? 64.725 37.554  -7.623  1.00 29.67 ? 1022 HIS A NE2 1 
ATOM   8169 N  N   . LEU A 1 1023 ? 60.653 37.997  -9.636  1.00 20.82 ? 1023 LEU A N   1 
ATOM   8170 C  CA  . LEU A 1 1023 ? 60.441 37.711  -11.028 1.00 21.62 ? 1023 LEU A CA  1 
ATOM   8171 C  C   . LEU A 1 1023 ? 61.605 37.154  -11.817 1.00 22.31 ? 1023 LEU A C   1 
ATOM   8172 O  O   . LEU A 1 1023 ? 62.715 37.716  -11.821 1.00 21.55 ? 1023 LEU A O   1 
ATOM   8173 C  CB  . LEU A 1 1023 ? 59.914 38.980  -11.703 1.00 21.46 ? 1023 LEU A CB  1 
ATOM   8174 C  CG  . LEU A 1 1023 ? 58.616 39.499  -11.086 1.00 22.28 ? 1023 LEU A CG  1 
ATOM   8175 C  CD1 . LEU A 1 1023 ? 58.396 40.937  -11.476 1.00 23.22 ? 1023 LEU A CD1 1 
ATOM   8176 C  CD2 . LEU A 1 1023 ? 57.457 38.610  -11.555 1.00 23.30 ? 1023 LEU A CD2 1 
ATOM   8177 N  N   . ASP A 1 1024 ? 61.297 36.067  -12.524 1.00 25.45 ? 1024 ASP A N   1 
ATOM   8178 C  CA  . ASP A 1 1024 ? 62.265 35.377  -13.375 1.00 26.94 ? 1024 ASP A CA  1 
ATOM   8179 C  C   . ASP A 1 1024 ? 62.786 36.250  -14.472 1.00 26.74 ? 1024 ASP A C   1 
ATOM   8180 O  O   . ASP A 1 1024 ? 62.019 36.961  -15.165 1.00 26.59 ? 1024 ASP A O   1 
ATOM   8181 C  CB  . ASP A 1 1024 ? 61.636 34.157  -14.030 1.00 30.14 ? 1024 ASP A CB  1 
ATOM   8182 C  CG  . ASP A 1 1024 ? 61.461 33.014  -13.065 1.00 32.79 ? 1024 ASP A CG  1 
ATOM   8183 O  OD1 . ASP A 1 1024 ? 62.291 32.926  -12.106 1.00 35.31 ? 1024 ASP A OD1 1 
ATOM   8184 O  OD2 . ASP A 1 1024 ? 60.507 32.211  -13.288 1.00 35.04 ? 1024 ASP A OD2 1 
ATOM   8185 N  N   . GLY A 1 1025 ? 64.094 36.181  -14.638 1.00 25.20 ? 1025 GLY A N   1 
ATOM   8186 C  CA  . GLY A 1 1025 ? 64.732 36.954  -15.675 1.00 24.85 ? 1025 GLY A CA  1 
ATOM   8187 C  C   . GLY A 1 1025 ? 64.707 38.434  -15.414 1.00 23.58 ? 1025 GLY A C   1 
ATOM   8188 O  O   . GLY A 1 1025 ? 65.139 39.202  -16.257 1.00 24.20 ? 1025 GLY A O   1 
ATOM   8189 N  N   . MET A 1 1026 ? 64.234 38.827  -14.231 1.00 22.62 ? 1026 MET A N   1 
ATOM   8190 C  CA  . MET A 1 1026 ? 64.141 40.241  -13.866 1.00 22.34 ? 1026 MET A CA  1 
ATOM   8191 C  C   . MET A 1 1026 ? 63.232 40.929  -14.865 1.00 21.59 ? 1026 MET A C   1 
ATOM   8192 O  O   . MET A 1 1026 ? 63.452 42.104  -15.209 1.00 21.35 ? 1026 MET A O   1 
ATOM   8193 C  CB  . MET A 1 1026 ? 65.520 40.920  -13.859 1.00 22.71 ? 1026 MET A CB  1 
ATOM   8194 C  CG  . MET A 1 1026 ? 66.507 40.244  -12.892 1.00 24.90 ? 1026 MET A CG  1 
ATOM   8195 S  SD  . MET A 1 1026 ? 68.140 40.968  -12.819 1.00 27.96 ? 1026 MET A SD  1 
ATOM   8196 C  CE  . MET A 1 1026 ? 68.762 40.613  -14.527 1.00 27.30 ? 1026 MET A CE  1 
ATOM   8197 N  N   . VAL A 1 1027 ? 62.222 40.217  -15.350 1.00 21.06 ? 1027 VAL A N   1 
ATOM   8198 C  CA  . VAL A 1 1027 ? 61.315 40.800  -16.326 1.00 21.88 ? 1027 VAL A CA  1 
ATOM   8199 C  C   . VAL A 1 1027 ? 59.926 41.038  -15.708 1.00 22.81 ? 1027 VAL A C   1 
ATOM   8200 O  O   . VAL A 1 1027 ? 59.318 40.133  -15.116 1.00 22.92 ? 1027 VAL A O   1 
ATOM   8201 C  CB  . VAL A 1 1027 ? 61.177 39.899  -17.585 1.00 21.58 ? 1027 VAL A CB  1 
ATOM   8202 C  CG1 . VAL A 1 1027 ? 60.077 40.428  -18.502 1.00 23.22 ? 1027 VAL A CG1 1 
ATOM   8203 C  CG2 . VAL A 1 1027 ? 62.499 39.895  -18.371 1.00 22.38 ? 1027 VAL A CG2 1 
ATOM   8204 N  N   . ALA A 1 1028 ? 59.429 42.264  -15.830 1.00 22.49 ? 1028 ALA A N   1 
ATOM   8205 C  CA  . ALA A 1 1028 ? 58.103 42.585  -15.283 1.00 23.21 ? 1028 ALA A CA  1 
ATOM   8206 C  C   . ALA A 1 1028 ? 57.110 42.374  -16.388 1.00 23.44 ? 1028 ALA A C   1 
ATOM   8207 O  O   . ALA A 1 1028 ? 57.123 43.122  -17.369 1.00 24.35 ? 1028 ALA A O   1 
ATOM   8208 C  CB  . ALA A 1 1028 ? 58.042 44.050  -14.834 1.00 22.47 ? 1028 ALA A CB  1 
ATOM   8209 N  N   . PRO A 1 1029 ? 56.243 41.361  -16.263 1.00 23.41 ? 1029 PRO A N   1 
ATOM   8210 C  CA  . PRO A 1 1029 ? 55.253 41.134  -17.327 1.00 24.28 ? 1029 PRO A CA  1 
ATOM   8211 C  C   . PRO A 1 1029 ? 54.186 42.240  -17.404 1.00 23.81 ? 1029 PRO A C   1 
ATOM   8212 O  O   . PRO A 1 1029 ? 53.893 42.905  -16.422 1.00 25.31 ? 1029 PRO A O   1 
ATOM   8213 C  CB  . PRO A 1 1029 ? 54.590 39.815  -16.947 1.00 24.22 ? 1029 PRO A CB  1 
ATOM   8214 C  CG  . PRO A 1 1029 ? 55.194 39.401  -15.595 1.00 24.34 ? 1029 PRO A CG  1 
ATOM   8215 C  CD  . PRO A 1 1029 ? 56.022 40.512  -15.077 1.00 23.23 ? 1029 PRO A CD  1 
ATOM   8216 N  N   . GLU A 1 1030 ? 53.604 42.436  -18.571 1.00 23.93 ? 1030 GLU A N   1 
ATOM   8217 C  CA  . GLU A 1 1030 ? 52.533 43.408  -18.672 1.00 23.79 ? 1030 GLU A CA  1 
ATOM   8218 C  C   . GLU A 1 1030 ? 51.285 42.793  -18.033 1.00 23.37 ? 1030 GLU A C   1 
ATOM   8219 O  O   . GLU A 1 1030 ? 51.149 41.554  -17.875 1.00 25.24 ? 1030 GLU A O   1 
ATOM   8220 C  CB  . GLU A 1 1030 ? 52.263 43.770  -20.139 1.00 23.38 ? 1030 GLU A CB  1 
ATOM   8221 C  CG  . GLU A 1 1030 ? 53.466 44.462  -20.835 1.00 23.46 ? 1030 GLU A CG  1 
ATOM   8222 C  CD  . GLU A 1 1030 ? 53.122 44.901  -22.245 1.00 24.07 ? 1030 GLU A CD  1 
ATOM   8223 O  OE1 . GLU A 1 1030 ? 52.082 44.421  -22.757 1.00 25.84 ? 1030 GLU A OE1 1 
ATOM   8224 O  OE2 . GLU A 1 1030 ? 53.881 45.703  -22.856 1.00 22.24 ? 1030 GLU A OE2 1 
ATOM   8225 N  N   . VAL A 1 1031 ? 50.378 43.676  -17.672 1.00 22.18 ? 1031 VAL A N   1 
ATOM   8226 C  CA  . VAL A 1 1031 ? 49.170 43.291  -16.991 1.00 19.19 ? 1031 VAL A CA  1 
ATOM   8227 C  C   . VAL A 1 1031 ? 47.977 43.111  -17.925 1.00 17.87 ? 1031 VAL A C   1 
ATOM   8228 O  O   . VAL A 1 1031 ? 48.006 43.493  -19.087 1.00 17.37 ? 1031 VAL A O   1 
ATOM   8229 C  CB  . VAL A 1 1031 ? 48.849 44.335  -15.854 1.00 21.13 ? 1031 VAL A CB  1 
ATOM   8230 C  CG1 . VAL A 1 1031 ? 50.125 44.541  -14.983 1.00 22.62 ? 1031 VAL A CG1 1 
ATOM   8231 C  CG2 . VAL A 1 1031 ? 48.383 45.637  -16.425 1.00 20.69 ? 1031 VAL A CG2 1 
ATOM   8232 N  N   . CYS A 1 1032 ? 46.957 42.453  -17.399 1.00 15.16 ? 1032 CYS A N   1 
ATOM   8233 C  CA  . CYS A 1 1032 ? 45.714 42.200  -18.114 1.00 14.03 ? 1032 CYS A CA  1 
ATOM   8234 C  C   . CYS A 1 1032 ? 44.790 43.422  -18.173 1.00 12.25 ? 1032 CYS A C   1 
ATOM   8235 O  O   . CYS A 1 1032 ? 44.943 44.370  -17.388 1.00 11.89 ? 1032 CYS A O   1 
ATOM   8236 C  CB  . CYS A 1 1032 ? 44.950 41.124  -17.384 1.00 14.29 ? 1032 CYS A CB  1 
ATOM   8237 S  SG  . CYS A 1 1032 ? 45.747 39.487  -17.547 1.00 20.77 ? 1032 CYS A SG  1 
ATOM   8238 N  N   . PRO A 1 1033 ? 43.836 43.437  -19.124 1.00 12.02 ? 1033 PRO A N   1 
ATOM   8239 C  CA  . PRO A 1 1033 ? 42.909 44.568  -19.193 1.00 10.69 ? 1033 PRO A CA  1 
ATOM   8240 C  C   . PRO A 1 1033 ? 42.186 44.734  -17.859 1.00 9.81  ? 1033 PRO A C   1 
ATOM   8241 O  O   . PRO A 1 1033 ? 41.684 43.769  -17.236 1.00 10.25 ? 1033 PRO A O   1 
ATOM   8242 C  CB  . PRO A 1 1033 ? 41.904 44.152  -20.296 1.00 11.95 ? 1033 PRO A CB  1 
ATOM   8243 C  CG  . PRO A 1 1033 ? 42.766 43.254  -21.190 1.00 13.76 ? 1033 PRO A CG  1 
ATOM   8244 C  CD  . PRO A 1 1033 ? 43.568 42.444  -20.195 1.00 13.44 ? 1033 PRO A CD  1 
ATOM   8245 N  N   . MET A 1 1034 ? 42.088 46.003  -17.456 1.00 9.38  ? 1034 MET A N   1 
ATOM   8246 C  CA  . MET A 1 1034 ? 41.482 46.470  -16.200 1.00 10.08 ? 1034 MET A CA  1 
ATOM   8247 C  C   . MET A 1 1034 ? 42.271 46.082  -14.966 1.00 11.24 ? 1034 MET A C   1 
ATOM   8248 O  O   . MET A 1 1034 ? 41.800 46.326  -13.855 1.00 15.35 ? 1034 MET A O   1 
ATOM   8249 C  CB  . MET A 1 1034 ? 40.013 46.043  -16.021 1.00 9.86  ? 1034 MET A CB  1 
ATOM   8250 C  CG  . MET A 1 1034 ? 39.160 46.534  -17.149 1.00 11.27 ? 1034 MET A CG  1 
ATOM   8251 S  SD  . MET A 1 1034 ? 39.182 48.351  -17.382 1.00 12.45 ? 1034 MET A SD  1 
ATOM   8252 C  CE  . MET A 1 1034 ? 38.285 48.914  -15.820 1.00 13.45 ? 1034 MET A CE  1 
ATOM   8253 N  N   . GLU A 1 1035 ? 43.501 45.638  -15.133 1.00 9.97  ? 1035 GLU A N   1 
ATOM   8254 C  CA  . GLU A 1 1035 ? 44.325 45.278  -14.001 1.00 10.57 ? 1035 GLU A CA  1 
ATOM   8255 C  C   . GLU A 1 1035 ? 45.382 46.341  -13.790 1.00 9.88  ? 1035 GLU A C   1 
ATOM   8256 O  O   . GLU A 1 1035 ? 45.747 47.101  -14.690 1.00 9.88  ? 1035 GLU A O   1 
ATOM   8257 C  CB  . GLU A 1 1035 ? 44.958 43.903  -14.211 1.00 14.36 ? 1035 GLU A CB  1 
ATOM   8258 C  CG  . GLU A 1 1035 ? 43.934 42.801  -13.882 1.00 20.49 ? 1035 GLU A CG  1 
ATOM   8259 C  CD  . GLU A 1 1035 ? 43.628 42.766  -12.375 1.00 24.79 ? 1035 GLU A CD  1 
ATOM   8260 O  OE1 . GLU A 1 1035 ? 44.436 42.120  -11.648 1.00 28.12 ? 1035 GLU A OE1 1 
ATOM   8261 O  OE2 . GLU A 1 1035 ? 42.645 43.407  -11.929 1.00 27.13 ? 1035 GLU A OE2 1 
ATOM   8262 N  N   . THR A 1 1036 ? 45.836 46.423  -12.544 1.00 9.82  ? 1036 THR A N   1 
ATOM   8263 C  CA  . THR A 1 1036 ? 46.870 47.364  -12.140 1.00 10.34 ? 1036 THR A CA  1 
ATOM   8264 C  C   . THR A 1 1036 ? 47.849 46.532  -11.303 1.00 10.67 ? 1036 THR A C   1 
ATOM   8265 O  O   . THR A 1 1036 ? 47.430 45.780  -10.426 1.00 12.02 ? 1036 THR A O   1 
ATOM   8266 C  CB  . THR A 1 1036 ? 46.284 48.473  -11.260 1.00 10.70 ? 1036 THR A CB  1 
ATOM   8267 O  OG1 . THR A 1 1036 ? 45.203 49.116  -11.958 1.00 10.35 ? 1036 THR A OG1 1 
ATOM   8268 C  CG2 . THR A 1 1036 ? 47.373 49.528  -10.889 1.00 10.60 ? 1036 THR A CG2 1 
ATOM   8269 N  N   . ALA A 1 1037 ? 49.142 46.675  -11.596 1.00 10.56 ? 1037 ALA A N   1 
ATOM   8270 C  CA  . ALA A 1 1037 ? 50.187 45.960  -10.855 1.00 10.07 ? 1037 ALA A CA  1 
ATOM   8271 C  C   . ALA A 1 1037 ? 51.321 46.898  -10.551 1.00 10.04 ? 1037 ALA A C   1 
ATOM   8272 O  O   . ALA A 1 1037 ? 51.468 47.949  -11.194 1.00 11.20 ? 1037 ALA A O   1 
ATOM   8273 C  CB  . ALA A 1 1037 ? 50.744 44.798  -11.706 1.00 13.17 ? 1037 ALA A CB  1 
ATOM   8274 N  N   . ALA A 1 1038 ? 52.093 46.574  -9.528  1.00 8.37  ? 1038 ALA A N   1 
ATOM   8275 C  CA  . ALA A 1 1038 ? 53.232 47.372  -9.183  1.00 9.30  ? 1038 ALA A CA  1 
ATOM   8276 C  C   . ALA A 1 1038 ? 54.484 46.501  -9.207  1.00 9.30  ? 1038 ALA A C   1 
ATOM   8277 O  O   . ALA A 1 1038 ? 54.453 45.323  -8.862  1.00 9.71  ? 1038 ALA A O   1 
ATOM   8278 C  CB  . ALA A 1 1038 ? 53.050 48.006  -7.794  1.00 9.03  ? 1038 ALA A CB  1 
ATOM   8279 N  N   . TYR A 1 1039 ? 55.564 47.105  -9.655  1.00 10.20 ? 1039 TYR A N   1 
ATOM   8280 C  CA  . TYR A 1 1039 ? 56.859 46.421  -9.702  1.00 10.54 ? 1039 TYR A CA  1 
ATOM   8281 C  C   . TYR A 1 1039 ? 57.940 47.287  -9.162  1.00 10.82 ? 1039 TYR A C   1 
ATOM   8282 O  O   . TYR A 1 1039 ? 57.900 48.513  -9.313  1.00 11.93 ? 1039 TYR A O   1 
ATOM   8283 C  CB  . TYR A 1 1039 ? 57.218 46.081  -11.146 1.00 11.99 ? 1039 TYR A CB  1 
ATOM   8284 C  CG  . TYR A 1 1039 ? 56.245 45.193  -11.840 1.00 11.77 ? 1039 TYR A CG  1 
ATOM   8285 C  CD1 . TYR A 1 1039 ? 56.220 43.824  -11.600 1.00 14.06 ? 1039 TYR A CD1 1 
ATOM   8286 C  CD2 . TYR A 1 1039 ? 55.307 45.732  -12.716 1.00 13.64 ? 1039 TYR A CD2 1 
ATOM   8287 C  CE1 . TYR A 1 1039 ? 55.277 42.998  -12.220 1.00 15.42 ? 1039 TYR A CE1 1 
ATOM   8288 C  CE2 . TYR A 1 1039 ? 54.376 44.928  -13.353 1.00 15.38 ? 1039 TYR A CE2 1 
ATOM   8289 C  CZ  . TYR A 1 1039 ? 54.363 43.574  -13.110 1.00 16.85 ? 1039 TYR A CZ  1 
ATOM   8290 O  OH  . TYR A 1 1039 ? 53.483 42.776  -13.834 1.00 20.06 ? 1039 TYR A OH  1 
ATOM   8291 N  N   . VAL A 1 1040 ? 58.934 46.679  -8.507  1.00 11.62 ? 1040 VAL A N   1 
ATOM   8292 C  CA  . VAL A 1 1040 ? 60.094 47.423  -8.031  1.00 11.84 ? 1040 VAL A CA  1 
ATOM   8293 C  C   . VAL A 1 1040 ? 61.328 46.758  -8.663  1.00 11.44 ? 1040 VAL A C   1 
ATOM   8294 O  O   . VAL A 1 1040 ? 61.524 45.532  -8.532  1.00 12.49 ? 1040 VAL A O   1 
ATOM   8295 C  CB  . VAL A 1 1040 ? 60.226 47.372  -6.489  1.00 11.21 ? 1040 VAL A CB  1 
ATOM   8296 C  CG1 . VAL A 1 1040 ? 61.559 48.077  -6.063  1.00 12.96 ? 1040 VAL A CG1 1 
ATOM   8297 C  CG2 . VAL A 1 1040 ? 59.045 48.133  -5.842  1.00 12.46 ? 1040 VAL A CG2 1 
ATOM   8298 N  N   . SER A 1 1041 ? 62.137 47.551  -9.361  1.00 10.45 ? 1041 SER A N   1 
ATOM   8299 C  CA  . SER A 1 1041 ? 63.406 47.072  -9.898  1.00 11.84 ? 1041 SER A CA  1 
ATOM   8300 C  C   . SER A 1 1041 ? 64.513 47.537  -8.949  1.00 12.41 ? 1041 SER A C   1 
ATOM   8301 O  O   . SER A 1 1041 ? 64.504 48.662  -8.398  1.00 12.38 ? 1041 SER A O   1 
ATOM   8302 C  CB  . SER A 1 1041 ? 63.619 47.576  -11.321 1.00 13.01 ? 1041 SER A CB  1 
ATOM   8303 O  OG  . SER A 1 1041 ? 63.672 48.980  -11.395 1.00 14.07 ? 1041 SER A OG  1 
ATOM   8304 N  N   . SER A 1 1042 ? 65.485 46.625  -8.730  1.00 13.56 ? 1042 SER A N   1 
ATOM   8305 C  CA  . SER A 1 1042 ? 66.649 46.910  -7.867  1.00 13.66 ? 1042 SER A CA  1 
ATOM   8306 C  C   . SER A 1 1042 ? 67.895 46.967  -8.763  1.00 14.36 ? 1042 SER A C   1 
ATOM   8307 O  O   . SER A 1 1042 ? 68.013 46.173  -9.690  1.00 15.52 ? 1042 SER A O   1 
ATOM   8308 C  CB  . SER A 1 1042 ? 66.824 45.804  -6.817  1.00 13.94 ? 1042 SER A CB  1 
ATOM   8309 O  OG  . SER A 1 1042 ? 65.722 45.818  -5.915  1.00 14.87 ? 1042 SER A OG  1 
ATOM   8310 N  N   . HIS A 1 1043 ? 68.757 47.937  -8.498  1.00 14.70 ? 1043 HIS A N   1 
ATOM   8311 C  CA  . HIS A 1 1043 ? 69.932 48.197  -9.353  1.00 15.50 ? 1043 HIS A CA  1 
ATOM   8312 C  C   . HIS A 1 1043 ? 71.192 48.314  -8.537  1.00 17.05 ? 1043 HIS A C   1 
ATOM   8313 O  O   . HIS A 1 1043 ? 71.235 48.992  -7.498  1.00 16.96 ? 1043 HIS A O   1 
ATOM   8314 C  CB  . HIS A 1 1043 ? 69.678 49.480  -10.153 1.00 14.12 ? 1043 HIS A CB  1 
ATOM   8315 C  CG  . HIS A 1 1043 ? 68.371 49.448  -10.893 1.00 13.41 ? 1043 HIS A CG  1 
ATOM   8316 N  ND1 . HIS A 1 1043 ? 68.259 48.995  -12.192 1.00 14.04 ? 1043 HIS A ND1 1 
ATOM   8317 C  CD2 . HIS A 1 1043 ? 67.103 49.704  -10.470 1.00 12.34 ? 1043 HIS A CD2 1 
ATOM   8318 C  CE1 . HIS A 1 1043 ? 66.981 48.979  -12.548 1.00 13.67 ? 1043 HIS A CE1 1 
ATOM   8319 N  NE2 . HIS A 1 1043 ? 66.265 49.405  -11.507 1.00 12.92 ? 1043 HIS A NE2 1 
ATOM   8320 N  N   . SER A 1 1044 ? 72.212 47.619  -9.056  1.00 20.20 ? 1044 SER A N   1 
ATOM   8321 C  CA  . SER A 1 1044 ? 73.495 47.556  -8.395  1.00 23.34 ? 1044 SER A CA  1 
ATOM   8322 C  C   . SER A 1 1044 ? 74.449 48.678  -8.754  1.00 24.22 ? 1044 SER A C   1 
ATOM   8323 O  O   . SER A 1 1044 ? 74.185 49.481  -9.693  1.00 25.22 ? 1044 SER A O   1 
ATOM   8324 C  CB  . SER A 1 1044 ? 74.143 46.186  -8.675  1.00 24.03 ? 1044 SER A CB  1 
ATOM   8325 O  OG  . SER A 1 1044 ? 74.169 45.900  -10.072 1.00 26.50 ? 1044 SER A OG  1 
HETATM 8326 C  C1  . NAG B 2 .    ? 58.346 44.912  12.701  1.00 35.36 ? 1802 NAG A C1  1 
HETATM 8327 C  C2  . NAG B 2 .    ? 59.459 44.559  13.666  1.00 38.86 ? 1802 NAG A C2  1 
HETATM 8328 C  C3  . NAG B 2 .    ? 59.950 43.162  13.393  1.00 40.36 ? 1802 NAG A C3  1 
HETATM 8329 C  C4  . NAG B 2 .    ? 58.809 42.182  13.524  1.00 41.30 ? 1802 NAG A C4  1 
HETATM 8330 C  C5  . NAG B 2 .    ? 57.748 42.576  12.487  1.00 41.44 ? 1802 NAG A C5  1 
HETATM 8331 C  C6  . NAG B 2 .    ? 56.519 41.678  12.523  1.00 42.71 ? 1802 NAG A C6  1 
HETATM 8332 C  C7  . NAG B 2 .    ? 60.831 46.361  14.497  1.00 43.50 ? 1802 NAG A C7  1 
HETATM 8333 C  C8  . NAG B 2 .    ? 61.571 45.831  15.712  1.00 45.03 ? 1802 NAG A C8  1 
HETATM 8334 N  N2  . NAG B 2 .    ? 60.556 45.499  13.521  1.00 41.41 ? 1802 NAG A N2  1 
HETATM 8335 O  O3  . NAG B 2 .    ? 60.942 42.861  14.342  1.00 41.02 ? 1802 NAG A O3  1 
HETATM 8336 O  O4  . NAG B 2 .    ? 59.291 40.861  13.297  1.00 42.92 ? 1802 NAG A O4  1 
HETATM 8337 O  O5  . NAG B 2 .    ? 57.292 43.933  12.733  1.00 38.41 ? 1802 NAG A O5  1 
HETATM 8338 O  O6  . NAG B 2 .    ? 56.675 40.549  11.661  1.00 45.67 ? 1802 NAG A O6  1 
HETATM 8339 O  O7  . NAG B 2 .    ? 60.523 47.555  14.447  1.00 45.24 ? 1802 NAG A O7  1 
HETATM 8340 P  P   . PO4 C 3 .    ? 45.237 65.478  -29.819 1.00 21.28 ? 1803 PO4 A P   1 
HETATM 8341 O  O1  . PO4 C 3 .    ? 44.767 66.823  -30.483 1.00 26.96 ? 1803 PO4 A O1  1 
HETATM 8342 O  O2  . PO4 C 3 .    ? 46.608 65.016  -30.310 1.00 26.10 ? 1803 PO4 A O2  1 
HETATM 8343 O  O3  . PO4 C 3 .    ? 44.112 64.407  -30.114 1.00 27.54 ? 1803 PO4 A O3  1 
HETATM 8344 O  O4  . PO4 C 3 .    ? 45.329 65.762  -28.304 1.00 27.61 ? 1803 PO4 A O4  1 
HETATM 8345 ZN ZN  . ZN  D 4 .    ? 34.459 64.087  7.921   1.00 7.92  ? 1805 ZN  A ZN  1 
HETATM 8346 C  C15 . GB1 E 5 .    ? 27.365 67.513  11.671  1.00 15.24 ? 1804 GB1 A C15 1 
HETATM 8347 C  C14 . GB1 E 5 .    ? 27.127 68.895  11.774  1.00 18.26 ? 1804 GB1 A C14 1 
HETATM 8348 C  C13 . GB1 E 5 .    ? 28.038 69.716  12.418  1.00 15.64 ? 1804 GB1 A C13 1 
HETATM 8349 C  C12 . GB1 E 5 .    ? 29.150 69.095  12.941  1.00 16.82 ? 1804 GB1 A C12 1 
HETATM 8350 C  C11 . GB1 E 5 .    ? 29.431 67.727  12.865  1.00 14.67 ? 1804 GB1 A C11 1 
HETATM 8351 C  C10 . GB1 E 5 .    ? 28.509 66.901  12.209  1.00 15.40 ? 1804 GB1 A C10 1 
HETATM 8352 C  C8  . GB1 E 5 .    ? 28.761 65.382  12.122  1.00 13.17 ? 1804 GB1 A C8  1 
HETATM 8353 C  C9  . GB1 E 5 .    ? 28.903 64.845  13.539  1.00 14.59 ? 1804 GB1 A C9  1 
HETATM 8354 O  O9  . GB1 E 5 .    ? 29.026 63.444  13.365  1.00 13.98 ? 1804 GB1 A O9  1 
HETATM 8355 N  N7  . GB1 E 5 .    ? 29.900 65.263  11.183  1.00 12.29 ? 1804 GB1 A N7  1 
HETATM 8356 C  C6  . GB1 E 5 .    ? 29.871 65.714  9.793   1.00 11.58 ? 1804 GB1 A C6  1 
HETATM 8357 C  C5  . GB1 E 5 .    ? 31.019 65.192  8.945   1.00 9.52  ? 1804 GB1 A C5  1 
HETATM 8358 N  N1  . GB1 E 5 .    ? 30.750 65.381  7.506   1.00 10.29 ? 1804 GB1 A N1  1 
HETATM 8359 C  C2  . GB1 E 5 .    ? 31.244 66.641  6.960   1.00 8.93  ? 1804 GB1 A C2  1 
HETATM 8360 C  C3  . GB1 E 5 .    ? 32.602 66.592  7.659   1.00 10.12 ? 1804 GB1 A C3  1 
HETATM 8361 O  O3  . GB1 E 5 .    ? 33.616 65.869  6.994   1.00 9.26  ? 1804 GB1 A O3  1 
HETATM 8362 C  C4  . GB1 E 5 .    ? 32.239 66.104  9.056   1.00 9.69  ? 1804 GB1 A C4  1 
HETATM 8363 O  O4  . GB1 E 5 .    ? 33.221 65.174  9.470   1.00 10.30 ? 1804 GB1 A O4  1 
HETATM 8364 C  C1  . MPD F 6 .    ? 14.744 60.981  10.271  1.00 14.23 ? 1801 MPD A C1  1 
HETATM 8365 C  C2  . MPD F 6 .    ? 16.174 61.008  10.575  1.00 15.83 ? 1801 MPD A C2  1 
HETATM 8366 O  O2  . MPD F 6 .    ? 16.810 59.991  9.703   1.00 20.72 ? 1801 MPD A O2  1 
HETATM 8367 C  CM  . MPD F 6 .    ? 16.764 62.369  10.201  1.00 18.60 ? 1801 MPD A CM  1 
HETATM 8368 C  C3  . MPD F 6 .    ? 16.294 60.678  12.097  1.00 17.16 ? 1801 MPD A C3  1 
HETATM 8369 C  C4  . MPD F 6 .    ? 17.697 60.501  12.715  1.00 16.15 ? 1801 MPD A C4  1 
HETATM 8370 O  O4  . MPD F 6 .    ? 17.596 59.570  13.817  1.00 13.78 ? 1801 MPD A O4  1 
HETATM 8371 C  C5  . MPD F 6 .    ? 18.253 61.862  13.243  1.00 16.77 ? 1801 MPD A C5  1 
HETATM 8372 O  O   . HOH G 7 .    ? 27.930 46.834  -31.294 1.00 29.75 ? 1806 HOH A O   1 
HETATM 8373 O  O   . HOH G 7 .    ? 28.558 43.875  -29.638 1.00 31.79 ? 1807 HOH A O   1 
HETATM 8374 O  O   . HOH G 7 .    ? 26.274 44.240  -27.244 1.00 32.13 ? 1808 HOH A O   1 
HETATM 8375 O  O   . HOH G 7 .    ? 27.009 41.456  -27.610 1.00 37.32 ? 1809 HOH A O   1 
HETATM 8376 O  O   . HOH G 7 .    ? 29.356 40.899  -25.560 1.00 22.29 ? 1810 HOH A O   1 
HETATM 8377 O  O   . HOH G 7 .    ? 28.602 41.105  -21.686 1.00 13.00 ? 1811 HOH A O   1 
HETATM 8378 O  O   . HOH G 7 .    ? 27.810 38.498  -22.663 1.00 31.71 ? 1812 HOH A O   1 
HETATM 8379 O  O   . HOH G 7 .    ? 27.639 36.244  -19.545 1.00 24.13 ? 1813 HOH A O   1 
HETATM 8380 O  O   . HOH G 7 .    ? 29.439 34.917  -16.399 1.00 27.89 ? 1814 HOH A O   1 
HETATM 8381 O  O   . HOH G 7 .    ? 25.630 36.146  -15.498 1.00 30.97 ? 1815 HOH A O   1 
HETATM 8382 O  O   . HOH G 7 .    ? 23.670 37.526  -17.573 1.00 31.42 ? 1816 HOH A O   1 
HETATM 8383 O  O   . HOH G 7 .    ? 23.094 39.109  -15.358 1.00 25.78 ? 1817 HOH A O   1 
HETATM 8384 O  O   . HOH G 7 .    ? 24.106 41.780  -14.601 1.00 20.60 ? 1818 HOH A O   1 
HETATM 8385 O  O   . HOH G 7 .    ? 21.993 42.473  -13.175 1.00 21.30 ? 1819 HOH A O   1 
HETATM 8386 O  O   . HOH G 7 .    ? 22.214 40.560  -11.258 1.00 17.80 ? 1820 HOH A O   1 
HETATM 8387 O  O   . HOH G 7 .    ? 20.167 39.071  -12.158 1.00 40.39 ? 1821 HOH A O   1 
HETATM 8388 O  O   . HOH G 7 .    ? 19.523 41.837  -14.295 1.00 41.75 ? 1822 HOH A O   1 
HETATM 8389 O  O   . HOH G 7 .    ? 17.315 45.501  -14.037 1.00 30.23 ? 1823 HOH A O   1 
HETATM 8390 O  O   . HOH G 7 .    ? 19.889 46.611  -14.225 1.00 15.54 ? 1824 HOH A O   1 
HETATM 8391 O  O   . HOH G 7 .    ? 22.482 45.194  -13.422 1.00 15.45 ? 1825 HOH A O   1 
HETATM 8392 O  O   . HOH G 7 .    ? 23.585 45.766  -15.812 1.00 17.88 ? 1826 HOH A O   1 
HETATM 8393 O  O   . HOH G 7 .    ? 21.367 46.520  -17.420 1.00 27.77 ? 1827 HOH A O   1 
HETATM 8394 O  O   . HOH G 7 .    ? 18.073 48.534  -19.777 1.00 35.44 ? 1828 HOH A O   1 
HETATM 8395 O  O   . HOH G 7 .    ? 16.855 50.725  -19.232 1.00 20.90 ? 1829 HOH A O   1 
HETATM 8396 O  O   . HOH G 7 .    ? 16.331 52.814  -22.463 1.00 29.84 ? 1830 HOH A O   1 
HETATM 8397 O  O   . HOH G 7 .    ? 16.271 52.830  -25.558 1.00 37.59 ? 1831 HOH A O   1 
HETATM 8398 O  O   . HOH G 7 .    ? 19.580 52.410  -27.018 1.00 28.64 ? 1832 HOH A O   1 
HETATM 8399 O  O   . HOH G 7 .    ? 20.019 52.573  -24.230 1.00 15.56 ? 1833 HOH A O   1 
HETATM 8400 O  O   . HOH G 7 .    ? 19.081 50.143  -23.330 1.00 30.54 ? 1834 HOH A O   1 
HETATM 8401 O  O   . HOH G 7 .    ? 22.791 52.914  -24.391 1.00 12.22 ? 1835 HOH A O   1 
HETATM 8402 O  O   . HOH G 7 .    ? 24.655 50.930  -24.079 1.00 12.90 ? 1836 HOH A O   1 
HETATM 8403 O  O   . HOH G 7 .    ? 23.989 48.272  -24.194 1.00 32.31 ? 1837 HOH A O   1 
HETATM 8404 O  O   . HOH G 7 .    ? 22.730 48.094  -26.843 1.00 40.19 ? 1838 HOH A O   1 
HETATM 8405 O  O   . HOH G 7 .    ? 22.452 50.320  -27.295 1.00 37.28 ? 1839 HOH A O   1 
HETATM 8406 O  O   . HOH G 7 .    ? 19.363 51.850  -31.097 1.00 34.34 ? 1840 HOH A O   1 
HETATM 8407 O  O   . HOH G 7 .    ? 22.387 56.657  -34.223 1.00 16.11 ? 1841 HOH A O   1 
HETATM 8408 O  O   . HOH G 7 .    ? 21.516 55.384  -36.461 1.00 28.74 ? 1842 HOH A O   1 
HETATM 8409 O  O   . HOH G 7 .    ? 19.448 58.357  -36.764 1.00 23.63 ? 1843 HOH A O   1 
HETATM 8410 O  O   . HOH G 7 .    ? 18.702 60.518  -37.931 1.00 23.45 ? 1844 HOH A O   1 
HETATM 8411 O  O   . HOH G 7 .    ? 20.662 60.871  -40.329 1.00 30.22 ? 1845 HOH A O   1 
HETATM 8412 O  O   . HOH G 7 .    ? 25.029 58.761  -38.586 1.00 42.04 ? 1846 HOH A O   1 
HETATM 8413 O  O   . HOH G 7 .    ? 24.887 59.258  -36.253 1.00 38.47 ? 1847 HOH A O   1 
HETATM 8414 O  O   . HOH G 7 .    ? 21.698 61.354  -34.834 1.00 27.61 ? 1848 HOH A O   1 
HETATM 8415 O  O   . HOH G 7 .    ? 22.416 63.219  -33.021 1.00 20.10 ? 1849 HOH A O   1 
HETATM 8416 O  O   . HOH G 7 .    ? 20.711 58.806  -34.500 1.00 16.70 ? 1850 HOH A O   1 
HETATM 8417 O  O   . HOH G 7 .    ? 16.722 57.156  -36.125 1.00 38.06 ? 1851 HOH A O   1 
HETATM 8418 O  O   . HOH G 7 .    ? 20.807 51.077  -38.435 1.00 27.17 ? 1852 HOH A O   1 
HETATM 8419 O  O   . HOH G 7 .    ? 21.696 48.682  -38.996 1.00 40.49 ? 1853 HOH A O   1 
HETATM 8420 O  O   . HOH G 7 .    ? 22.877 48.709  -36.382 1.00 33.65 ? 1854 HOH A O   1 
HETATM 8421 O  O   . HOH G 7 .    ? 31.796 51.032  -35.482 1.00 22.25 ? 1855 HOH A O   1 
HETATM 8422 O  O   . HOH G 7 .    ? 34.777 53.457  -33.197 1.00 34.87 ? 1856 HOH A O   1 
HETATM 8423 O  O   . HOH G 7 .    ? 35.436 55.288  -34.749 1.00 36.53 ? 1857 HOH A O   1 
HETATM 8424 O  O   . HOH G 7 .    ? 36.545 56.448  -32.756 1.00 28.18 ? 1858 HOH A O   1 
HETATM 8425 O  O   . HOH G 7 .    ? 36.927 58.795  -33.573 1.00 25.95 ? 1859 HOH A O   1 
HETATM 8426 O  O   . HOH G 7 .    ? 34.746 59.326  -34.933 1.00 22.15 ? 1860 HOH A O   1 
HETATM 8427 O  O   . HOH G 7 .    ? 33.515 56.900  -35.976 1.00 17.49 ? 1861 HOH A O   1 
HETATM 8428 O  O   . HOH G 7 .    ? 30.819 58.127  -40.338 1.00 42.92 ? 1862 HOH A O   1 
HETATM 8429 O  O   . HOH G 7 .    ? 28.064 59.664  -38.847 1.00 30.02 ? 1863 HOH A O   1 
HETATM 8430 O  O   . HOH G 7 .    ? 28.981 62.048  -39.825 1.00 23.15 ? 1864 HOH A O   1 
HETATM 8431 O  O   . HOH G 7 .    ? 34.434 65.770  -42.383 1.00 34.74 ? 1865 HOH A O   1 
HETATM 8432 O  O   . HOH G 7 .    ? 34.257 70.064  -44.884 1.00 39.79 ? 1866 HOH A O   1 
HETATM 8433 O  O   . HOH G 7 .    ? 30.990 69.101  -45.555 1.00 37.50 ? 1867 HOH A O   1 
HETATM 8434 O  O   . HOH G 7 .    ? 28.007 68.051  -47.018 1.00 38.49 ? 1868 HOH A O   1 
HETATM 8435 O  O   . HOH G 7 .    ? 28.795 69.591  -39.609 1.00 23.30 ? 1869 HOH A O   1 
HETATM 8436 O  O   . HOH G 7 .    ? 24.657 71.440  -39.914 1.00 27.30 ? 1870 HOH A O   1 
HETATM 8437 O  O   . HOH G 7 .    ? 26.019 76.095  -39.103 1.00 26.67 ? 1871 HOH A O   1 
HETATM 8438 O  O   . HOH G 7 .    ? 27.311 75.977  -41.430 1.00 36.04 ? 1872 HOH A O   1 
HETATM 8439 O  O   . HOH G 7 .    ? 31.193 78.804  -42.842 1.00 32.63 ? 1873 HOH A O   1 
HETATM 8440 O  O   . HOH G 7 .    ? 29.530 81.106  -43.212 1.00 42.94 ? 1874 HOH A O   1 
HETATM 8441 O  O   . HOH G 7 .    ? 26.059 81.358  -42.841 1.00 35.18 ? 1875 HOH A O   1 
HETATM 8442 O  O   . HOH G 7 .    ? 23.342 82.502  -40.605 1.00 23.78 ? 1876 HOH A O   1 
HETATM 8443 O  O   . HOH G 7 .    ? 22.083 80.608  -42.259 1.00 36.04 ? 1877 HOH A O   1 
HETATM 8444 O  O   . HOH G 7 .    ? 21.995 79.949  -35.955 1.00 25.69 ? 1878 HOH A O   1 
HETATM 8445 O  O   . HOH G 7 .    ? 20.663 79.813  -33.484 1.00 39.24 ? 1879 HOH A O   1 
HETATM 8446 O  O   . HOH G 7 .    ? 22.929 78.388  -30.352 1.00 23.54 ? 1880 HOH A O   1 
HETATM 8447 O  O   . HOH G 7 .    ? 22.887 77.274  -27.326 1.00 24.11 ? 1881 HOH A O   1 
HETATM 8448 O  O   . HOH G 7 .    ? 20.626 77.817  -27.528 1.00 34.23 ? 1882 HOH A O   1 
HETATM 8449 O  O   . HOH G 7 .    ? 19.305 78.900  -25.569 1.00 36.20 ? 1883 HOH A O   1 
HETATM 8450 O  O   . HOH G 7 .    ? 21.000 79.316  -23.479 1.00 21.09 ? 1884 HOH A O   1 
HETATM 8451 O  O   . HOH G 7 .    ? 23.158 78.262  -24.792 1.00 16.53 ? 1885 HOH A O   1 
HETATM 8452 O  O   . HOH G 7 .    ? 19.093 83.238  -25.761 1.00 28.30 ? 1886 HOH A O   1 
HETATM 8453 O  O   . HOH G 7 .    ? 21.496 85.957  -30.988 1.00 28.93 ? 1887 HOH A O   1 
HETATM 8454 O  O   . HOH G 7 .    ? 23.213 86.846  -32.540 1.00 31.71 ? 1888 HOH A O   1 
HETATM 8455 O  O   . HOH G 7 .    ? 25.572 86.044  -31.910 1.00 17.02 ? 1889 HOH A O   1 
HETATM 8456 O  O   . HOH G 7 .    ? 27.158 89.740  -31.691 1.00 37.18 ? 1890 HOH A O   1 
HETATM 8457 O  O   . HOH G 7 .    ? 25.733 91.581  -32.890 1.00 35.66 ? 1891 HOH A O   1 
HETATM 8458 O  O   . HOH G 7 .    ? 26.683 91.589  -27.683 1.00 28.33 ? 1892 HOH A O   1 
HETATM 8459 O  O   . HOH G 7 .    ? 28.063 90.801  -25.363 1.00 20.06 ? 1893 HOH A O   1 
HETATM 8460 O  O   . HOH G 7 .    ? 29.509 88.593  -26.238 1.00 13.45 ? 1894 HOH A O   1 
HETATM 8461 O  O   . HOH G 7 .    ? 27.046 87.793  -23.608 1.00 22.35 ? 1895 HOH A O   1 
HETATM 8462 O  O   . HOH G 7 .    ? 25.157 88.519  -25.411 1.00 31.07 ? 1896 HOH A O   1 
HETATM 8463 O  O   . HOH G 7 .    ? 23.703 90.762  -26.118 1.00 33.44 ? 1897 HOH A O   1 
HETATM 8464 O  O   . HOH G 7 .    ? 22.770 88.702  -18.805 1.00 38.04 ? 1898 HOH A O   1 
HETATM 8465 O  O   . HOH G 7 .    ? 21.596 86.011  -19.256 1.00 27.33 ? 1899 HOH A O   1 
HETATM 8466 O  O   . HOH G 7 .    ? 19.739 84.183  -18.440 1.00 29.84 ? 1900 HOH A O   1 
HETATM 8467 O  O   . HOH G 7 .    ? 17.459 81.306  -17.215 1.00 41.52 ? 1901 HOH A O   1 
HETATM 8468 O  O   . HOH G 7 .    ? 18.840 80.340  -11.713 1.00 34.78 ? 1902 HOH A O   1 
HETATM 8469 O  O   . HOH G 7 .    ? 18.290 82.511  -11.467 1.00 38.54 ? 1903 HOH A O   1 
HETATM 8470 O  O   . HOH G 7 .    ? 18.231 81.822  -8.948  1.00 35.92 ? 1904 HOH A O   1 
HETATM 8471 O  O   . HOH G 7 .    ? 17.277 80.508  -7.318  1.00 21.86 ? 1905 HOH A O   1 
HETATM 8472 O  O   . HOH G 7 .    ? 16.575 81.934  -5.120  1.00 32.56 ? 1906 HOH A O   1 
HETATM 8473 O  O   . HOH G 7 .    ? 18.123 84.465  -5.019  1.00 35.82 ? 1907 HOH A O   1 
HETATM 8474 O  O   . HOH G 7 .    ? 18.202 84.426  -7.993  1.00 40.97 ? 1908 HOH A O   1 
HETATM 8475 O  O   . HOH G 7 .    ? 20.893 83.723  -12.267 1.00 26.81 ? 1909 HOH A O   1 
HETATM 8476 O  O   . HOH G 7 .    ? 24.866 83.036  -16.967 1.00 19.99 ? 1910 HOH A O   1 
HETATM 8477 O  O   . HOH G 7 .    ? 27.682 86.240  -14.626 1.00 26.38 ? 1911 HOH A O   1 
HETATM 8478 O  O   . HOH G 7 .    ? 30.231 87.007  -15.130 1.00 22.28 ? 1912 HOH A O   1 
HETATM 8479 O  O   . HOH G 7 .    ? 29.649 87.163  -17.963 1.00 23.52 ? 1913 HOH A O   1 
HETATM 8480 O  O   . HOH G 7 .    ? 31.643 85.733  -19.868 1.00 21.73 ? 1914 HOH A O   1 
HETATM 8481 O  O   . HOH G 7 .    ? 33.308 84.218  -18.320 1.00 15.70 ? 1915 HOH A O   1 
HETATM 8482 O  O   . HOH G 7 .    ? 35.352 86.014  -17.992 1.00 26.06 ? 1916 HOH A O   1 
HETATM 8483 O  O   . HOH G 7 .    ? 40.051 85.858  -22.020 1.00 25.14 ? 1917 HOH A O   1 
HETATM 8484 O  O   . HOH G 7 .    ? 40.768 83.071  -23.409 1.00 38.98 ? 1918 HOH A O   1 
HETATM 8485 O  O   . HOH G 7 .    ? 39.563 81.402  -22.103 1.00 34.34 ? 1919 HOH A O   1 
HETATM 8486 O  O   . HOH G 7 .    ? 41.781 79.154  -23.586 1.00 27.19 ? 1920 HOH A O   1 
HETATM 8487 O  O   . HOH G 7 .    ? 43.454 80.824  -25.318 1.00 37.52 ? 1921 HOH A O   1 
HETATM 8488 O  O   . HOH G 7 .    ? 45.838 81.982  -25.529 1.00 43.01 ? 1922 HOH A O   1 
HETATM 8489 O  O   . HOH G 7 .    ? 44.288 83.515  -28.071 1.00 26.71 ? 1923 HOH A O   1 
HETATM 8490 O  O   . HOH G 7 .    ? 44.724 82.395  -30.611 1.00 21.61 ? 1924 HOH A O   1 
HETATM 8491 O  O   . HOH G 7 .    ? 41.371 82.548  -28.972 1.00 33.16 ? 1925 HOH A O   1 
HETATM 8492 O  O   . HOH G 7 .    ? 40.543 82.753  -31.337 1.00 26.36 ? 1926 HOH A O   1 
HETATM 8493 O  O   . HOH G 7 .    ? 38.133 81.587  -31.394 1.00 11.28 ? 1927 HOH A O   1 
HETATM 8494 O  O   . HOH G 7 .    ? 39.103 83.102  -27.494 1.00 22.04 ? 1928 HOH A O   1 
HETATM 8495 O  O   . HOH G 7 .    ? 41.400 83.405  -26.175 1.00 33.81 ? 1929 HOH A O   1 
HETATM 8496 O  O   . HOH G 7 .    ? 43.257 79.029  -27.600 1.00 41.33 ? 1930 HOH A O   1 
HETATM 8497 O  O   . HOH G 7 .    ? 42.816 78.327  -29.711 1.00 31.43 ? 1931 HOH A O   1 
HETATM 8498 O  O   . HOH G 7 .    ? 42.413 79.593  -31.745 1.00 28.35 ? 1932 HOH A O   1 
HETATM 8499 O  O   . HOH G 7 .    ? 44.615 79.074  -33.391 1.00 19.53 ? 1933 HOH A O   1 
HETATM 8500 O  O   . HOH G 7 .    ? 44.534 76.110  -28.362 1.00 27.47 ? 1934 HOH A O   1 
HETATM 8501 O  O   . HOH G 7 .    ? 46.321 76.849  -26.136 1.00 25.46 ? 1935 HOH A O   1 
HETATM 8502 O  O   . HOH G 7 .    ? 44.885 71.839  -26.005 1.00 39.14 ? 1936 HOH A O   1 
HETATM 8503 O  O   . HOH G 7 .    ? 47.310 70.555  -24.997 1.00 38.05 ? 1937 HOH A O   1 
HETATM 8504 O  O   . HOH G 7 .    ? 47.129 67.506  -24.728 1.00 20.79 ? 1938 HOH A O   1 
HETATM 8505 O  O   . HOH G 7 .    ? 45.891 67.947  -26.997 1.00 14.87 ? 1939 HOH A O   1 
HETATM 8506 O  O   . HOH G 7 .    ? 47.292 69.829  -28.661 1.00 21.61 ? 1940 HOH A O   1 
HETATM 8507 O  O   . HOH G 7 .    ? 47.364 68.045  -30.900 1.00 17.96 ? 1941 HOH A O   1 
HETATM 8508 O  O   . HOH G 7 .    ? 43.386 66.643  -32.350 1.00 27.71 ? 1942 HOH A O   1 
HETATM 8509 O  O   . HOH G 7 .    ? 41.258 68.133  -32.569 1.00 17.56 ? 1943 HOH A O   1 
HETATM 8510 O  O   . HOH G 7 .    ? 39.282 68.914  -35.390 1.00 15.73 ? 1944 HOH A O   1 
HETATM 8511 O  O   . HOH G 7 .    ? 38.556 68.989  -38.195 1.00 16.76 ? 1945 HOH A O   1 
HETATM 8512 O  O   . HOH G 7 .    ? 39.688 75.377  -40.323 1.00 18.14 ? 1946 HOH A O   1 
HETATM 8513 O  O   . HOH G 7 .    ? 42.118 74.634  -41.468 1.00 27.76 ? 1947 HOH A O   1 
HETATM 8514 O  O   . HOH G 7 .    ? 43.680 72.356  -42.009 1.00 19.69 ? 1948 HOH A O   1 
HETATM 8515 O  O   . HOH G 7 .    ? 44.650 71.861  -44.653 1.00 43.72 ? 1949 HOH A O   1 
HETATM 8516 O  O   . HOH G 7 .    ? 46.324 70.066  -39.897 1.00 36.11 ? 1950 HOH A O   1 
HETATM 8517 O  O   . HOH G 7 .    ? 46.546 70.042  -36.697 1.00 18.38 ? 1951 HOH A O   1 
HETATM 8518 O  O   . HOH G 7 .    ? 48.924 68.947  -36.946 1.00 30.65 ? 1952 HOH A O   1 
HETATM 8519 O  O   . HOH G 7 .    ? 51.515 69.911  -38.180 1.00 27.74 ? 1953 HOH A O   1 
HETATM 8520 O  O   . HOH G 7 .    ? 53.943 71.026  -36.990 1.00 13.41 ? 1954 HOH A O   1 
HETATM 8521 O  O   . HOH G 7 .    ? 55.397 68.764  -37.812 1.00 28.62 ? 1955 HOH A O   1 
HETATM 8522 O  O   . HOH G 7 .    ? 56.745 69.711  -39.791 1.00 29.31 ? 1956 HOH A O   1 
HETATM 8523 O  O   . HOH G 7 .    ? 59.907 68.472  -39.009 1.00 26.08 ? 1957 HOH A O   1 
HETATM 8524 O  O   . HOH G 7 .    ? 61.087 67.210  -36.852 1.00 28.17 ? 1958 HOH A O   1 
HETATM 8525 O  O   . HOH G 7 .    ? 59.403 67.019  -34.881 1.00 25.89 ? 1959 HOH A O   1 
HETATM 8526 O  O   . HOH G 7 .    ? 56.811 67.511  -35.593 1.00 22.55 ? 1960 HOH A O   1 
HETATM 8527 O  O   . HOH G 7 .    ? 56.060 64.982  -36.211 1.00 26.17 ? 1961 HOH A O   1 
HETATM 8528 O  O   . HOH G 7 .    ? 58.639 64.530  -36.889 1.00 34.02 ? 1962 HOH A O   1 
HETATM 8529 O  O   . HOH G 7 .    ? 61.766 63.666  -30.802 1.00 22.56 ? 1963 HOH A O   1 
HETATM 8530 O  O   . HOH G 7 .    ? 64.021 65.582  -30.180 1.00 34.94 ? 1964 HOH A O   1 
HETATM 8531 O  O   . HOH G 7 .    ? 63.371 67.739  -31.760 1.00 23.09 ? 1965 HOH A O   1 
HETATM 8532 O  O   . HOH G 7 .    ? 69.702 63.727  -28.800 1.00 26.59 ? 1966 HOH A O   1 
HETATM 8533 O  O   . HOH G 7 .    ? 72.046 63.334  -27.341 1.00 46.61 ? 1967 HOH A O   1 
HETATM 8534 O  O   . HOH G 7 .    ? 69.893 62.850  -23.792 1.00 33.84 ? 1968 HOH A O   1 
HETATM 8535 O  O   . HOH G 7 .    ? 70.159 61.649  -20.400 1.00 23.59 ? 1969 HOH A O   1 
HETATM 8536 O  O   . HOH G 7 .    ? 71.720 62.448  -18.139 1.00 28.60 ? 1970 HOH A O   1 
HETATM 8537 O  O   . HOH G 7 .    ? 72.735 63.934  -21.050 1.00 31.93 ? 1971 HOH A O   1 
HETATM 8538 O  O   . HOH G 7 .    ? 73.906 65.867  -17.579 1.00 15.79 ? 1972 HOH A O   1 
HETATM 8539 O  O   . HOH G 7 .    ? 75.185 64.159  -16.112 1.00 29.28 ? 1973 HOH A O   1 
HETATM 8540 O  O   . HOH G 7 .    ? 77.636 66.012  -11.924 1.00 32.24 ? 1974 HOH A O   1 
HETATM 8541 O  O   . HOH G 7 .    ? 78.670 68.927  -11.940 1.00 21.95 ? 1975 HOH A O   1 
HETATM 8542 O  O   . HOH G 7 .    ? 81.315 68.342  -11.440 1.00 17.60 ? 1976 HOH A O   1 
HETATM 8543 O  O   . HOH G 7 .    ? 81.656 66.861  -13.658 1.00 17.42 ? 1977 HOH A O   1 
HETATM 8544 O  O   . HOH G 7 .    ? 83.656 66.207  -15.352 1.00 19.24 ? 1978 HOH A O   1 
HETATM 8545 O  O   . HOH G 7 .    ? 84.337 68.140  -17.282 1.00 14.65 ? 1979 HOH A O   1 
HETATM 8546 O  O   . HOH G 7 .    ? 83.679 69.917  -20.113 1.00 22.94 ? 1980 HOH A O   1 
HETATM 8547 O  O   . HOH G 7 .    ? 83.592 67.339  -22.825 1.00 21.36 ? 1981 HOH A O   1 
HETATM 8548 O  O   . HOH G 7 .    ? 80.427 64.018  -21.343 1.00 22.43 ? 1982 HOH A O   1 
HETATM 8549 O  O   . HOH G 7 .    ? 79.205 62.737  -23.528 1.00 40.68 ? 1983 HOH A O   1 
HETATM 8550 O  O   . HOH G 7 .    ? 79.710 67.931  -15.213 1.00 31.83 ? 1984 HOH A O   1 
HETATM 8551 O  O   . HOH G 7 .    ? 79.822 73.856  -17.518 1.00 26.02 ? 1985 HOH A O   1 
HETATM 8552 O  O   . HOH G 7 .    ? 77.639 75.018  -17.620 1.00 34.07 ? 1986 HOH A O   1 
HETATM 8553 O  O   . HOH G 7 .    ? 75.536 73.848  -16.102 1.00 26.05 ? 1987 HOH A O   1 
HETATM 8554 O  O   . HOH G 7 .    ? 74.769 76.196  -14.459 1.00 25.69 ? 1988 HOH A O   1 
HETATM 8555 O  O   . HOH G 7 .    ? 73.734 78.252  -13.314 1.00 42.08 ? 1989 HOH A O   1 
HETATM 8556 O  O   . HOH G 7 .    ? 73.620 80.044  -10.906 1.00 37.98 ? 1990 HOH A O   1 
HETATM 8557 O  O   . HOH G 7 .    ? 74.607 77.923  -16.540 1.00 42.01 ? 1991 HOH A O   1 
HETATM 8558 O  O   . HOH G 7 .    ? 73.216 76.716  -18.520 1.00 27.25 ? 1992 HOH A O   1 
HETATM 8559 O  O   . HOH G 7 .    ? 74.641 77.326  -20.684 1.00 33.15 ? 1993 HOH A O   1 
HETATM 8560 O  O   . HOH G 7 .    ? 75.432 74.063  -19.522 1.00 23.25 ? 1994 HOH A O   1 
HETATM 8561 O  O   . HOH G 7 .    ? 76.722 73.989  -26.760 1.00 33.17 ? 1995 HOH A O   1 
HETATM 8562 O  O   . HOH G 7 .    ? 72.477 75.708  -27.204 1.00 35.94 ? 1996 HOH A O   1 
HETATM 8563 O  O   . HOH G 7 .    ? 71.755 73.733  -29.269 1.00 25.59 ? 1997 HOH A O   1 
HETATM 8564 O  O   . HOH G 7 .    ? 70.502 77.870  -26.262 1.00 21.96 ? 1998 HOH A O   1 
HETATM 8565 O  O   . HOH G 7 .    ? 71.065 79.718  -27.959 1.00 36.92 ? 1999 HOH A O   1 
HETATM 8566 O  O   . HOH G 7 .    ? 71.404 82.295  -27.664 1.00 30.77 ? 2000 HOH A O   1 
HETATM 8567 O  O   . HOH G 7 .    ? 70.071 82.852  -29.893 1.00 20.12 ? 2001 HOH A O   1 
HETATM 8568 O  O   . HOH G 7 .    ? 68.442 79.259  -28.667 1.00 20.48 ? 2002 HOH A O   1 
HETATM 8569 O  O   . HOH G 7 .    ? 67.729 78.761  -25.365 1.00 12.53 ? 2003 HOH A O   1 
HETATM 8570 O  O   . HOH G 7 .    ? 67.783 81.557  -25.722 1.00 12.98 ? 2004 HOH A O   1 
HETATM 8571 O  O   . HOH G 7 .    ? 66.827 84.284  -22.253 1.00 24.78 ? 2005 HOH A O   1 
HETATM 8572 O  O   . HOH G 7 .    ? 64.812 85.170  -22.695 1.00 32.08 ? 2006 HOH A O   1 
HETATM 8573 O  O   . HOH G 7 .    ? 62.269 85.166  -23.172 1.00 31.61 ? 2007 HOH A O   1 
HETATM 8574 O  O   . HOH G 7 .    ? 62.582 83.073  -21.474 1.00 39.24 ? 2008 HOH A O   1 
HETATM 8575 O  O   . HOH G 7 .    ? 62.114 80.577  -18.988 1.00 21.36 ? 2009 HOH A O   1 
HETATM 8576 O  O   . HOH G 7 .    ? 62.629 82.492  -17.220 1.00 38.45 ? 2010 HOH A O   1 
HETATM 8577 O  O   . HOH G 7 .    ? 63.618 82.125  -14.534 1.00 40.31 ? 2011 HOH A O   1 
HETATM 8578 O  O   . HOH G 7 .    ? 66.319 81.732  -14.314 1.00 25.36 ? 2012 HOH A O   1 
HETATM 8579 O  O   . HOH G 7 .    ? 66.666 81.226  -11.235 1.00 23.12 ? 2013 HOH A O   1 
HETATM 8580 O  O   . HOH G 7 .    ? 64.893 79.603  -9.066  1.00 34.87 ? 2014 HOH A O   1 
HETATM 8581 O  O   . HOH G 7 .    ? 65.348 78.731  -5.744  1.00 24.05 ? 2015 HOH A O   1 
HETATM 8582 O  O   . HOH G 7 .    ? 65.515 81.238  -4.866  1.00 29.18 ? 2016 HOH A O   1 
HETATM 8583 O  O   . HOH G 7 .    ? 64.799 78.940  -1.560  1.00 27.72 ? 2017 HOH A O   1 
HETATM 8584 O  O   . HOH G 7 .    ? 64.328 77.311  0.230   1.00 32.66 ? 2018 HOH A O   1 
HETATM 8585 O  O   . HOH G 7 .    ? 65.516 77.722  2.948   1.00 31.27 ? 2019 HOH A O   1 
HETATM 8586 O  O   . HOH G 7 .    ? 65.186 76.908  -3.669  1.00 35.38 ? 2020 HOH A O   1 
HETATM 8587 O  O   . HOH G 7 .    ? 66.742 74.352  -4.449  1.00 24.49 ? 2021 HOH A O   1 
HETATM 8588 O  O   . HOH G 7 .    ? 66.402 71.358  -6.817  1.00 16.06 ? 2022 HOH A O   1 
HETATM 8589 O  O   . HOH G 7 .    ? 64.064 70.613  -5.323  1.00 15.02 ? 2023 HOH A O   1 
HETATM 8590 O  O   . HOH G 7 .    ? 67.931 65.472  -3.366  1.00 14.89 ? 2024 HOH A O   1 
HETATM 8591 O  O   . HOH G 7 .    ? 65.966 66.020  -0.559  1.00 20.97 ? 2025 HOH A O   1 
HETATM 8592 O  O   . HOH G 7 .    ? 66.261 68.631  2.059   1.00 35.00 ? 2026 HOH A O   1 
HETATM 8593 O  O   . HOH G 7 .    ? 69.198 63.607  2.020   1.00 34.05 ? 2027 HOH A O   1 
HETATM 8594 O  O   . HOH G 7 .    ? 70.212 61.849  0.024   1.00 34.78 ? 2028 HOH A O   1 
HETATM 8595 O  O   . HOH G 7 .    ? 69.140 61.306  -2.362  1.00 14.11 ? 2029 HOH A O   1 
HETATM 8596 O  O   . HOH G 7 .    ? 67.453 60.574  -5.642  1.00 10.86 ? 2030 HOH A O   1 
HETATM 8597 O  O   . HOH G 7 .    ? 65.630 60.176  -7.676  1.00 10.69 ? 2031 HOH A O   1 
HETATM 8598 O  O   . HOH G 7 .    ? 63.087 61.200  -7.604  1.00 8.94  ? 2032 HOH A O   1 
HETATM 8599 O  O   . HOH G 7 .    ? 60.984 59.554  -8.266  1.00 8.17  ? 2033 HOH A O   1 
HETATM 8600 O  O   . HOH G 7 .    ? 59.522 60.531  -6.243  1.00 11.75 ? 2034 HOH A O   1 
HETATM 8601 O  O   . HOH G 7 .    ? 60.692 60.764  -3.614  1.00 11.50 ? 2035 HOH A O   1 
HETATM 8602 O  O   . HOH G 7 .    ? 60.754 58.165  -2.850  1.00 11.00 ? 2036 HOH A O   1 
HETATM 8603 O  O   . HOH G 7 .    ? 58.902 56.641  -1.454  1.00 11.63 ? 2037 HOH A O   1 
HETATM 8604 O  O   . HOH G 7 .    ? 60.524 54.653  -0.409  1.00 13.13 ? 2038 HOH A O   1 
HETATM 8605 O  O   . HOH G 7 .    ? 58.711 52.565  -0.133  1.00 12.58 ? 2039 HOH A O   1 
HETATM 8606 O  O   . HOH G 7 .    ? 56.091 53.301  -0.648  1.00 8.13  ? 2040 HOH A O   1 
HETATM 8607 O  O   . HOH G 7 .    ? 56.355 55.654  -2.140  1.00 10.17 ? 2041 HOH A O   1 
HETATM 8608 O  O   . HOH G 7 .    ? 55.000 57.487  -0.526  1.00 14.16 ? 2042 HOH A O   1 
HETATM 8609 O  O   . HOH G 7 .    ? 56.557 58.370  1.351   1.00 21.75 ? 2043 HOH A O   1 
HETATM 8610 O  O   . HOH G 7 .    ? 59.139 58.056  0.946   1.00 21.98 ? 2044 HOH A O   1 
HETATM 8611 O  O   . HOH G 7 .    ? 60.814 56.036  2.040   1.00 30.41 ? 2045 HOH A O   1 
HETATM 8612 O  O   . HOH G 7 .    ? 63.795 56.923  0.828   1.00 30.48 ? 2046 HOH A O   1 
HETATM 8613 O  O   . HOH G 7 .    ? 63.184 58.583  -1.464  1.00 15.67 ? 2047 HOH A O   1 
HETATM 8614 O  O   . HOH G 7 .    ? 64.868 59.195  -3.572  1.00 12.13 ? 2048 HOH A O   1 
HETATM 8615 O  O   . HOH G 7 .    ? 63.111 61.008  -4.843  1.00 12.82 ? 2049 HOH A O   1 
HETATM 8616 O  O   . HOH G 7 .    ? 60.498 62.158  -1.246  1.00 10.91 ? 2050 HOH A O   1 
HETATM 8617 O  O   . HOH G 7 .    ? 62.195 60.652  0.471   1.00 29.07 ? 2051 HOH A O   1 
HETATM 8618 O  O   . HOH G 7 .    ? 56.909 60.994  1.562   1.00 14.53 ? 2052 HOH A O   1 
HETATM 8619 O  O   . HOH G 7 .    ? 55.234 59.034  3.958   1.00 15.60 ? 2053 HOH A O   1 
HETATM 8620 O  O   . HOH G 7 .    ? 57.533 58.449  5.446   1.00 22.46 ? 2054 HOH A O   1 
HETATM 8621 O  O   . HOH G 7 .    ? 58.598 60.582  5.782   1.00 28.15 ? 2055 HOH A O   1 
HETATM 8622 O  O   . HOH G 7 .    ? 57.645 62.344  7.820   1.00 20.53 ? 2056 HOH A O   1 
HETATM 8623 O  O   . HOH G 7 .    ? 56.635 66.948  5.136   1.00 31.67 ? 2057 HOH A O   1 
HETATM 8624 O  O   . HOH G 7 .    ? 54.909 68.546  3.420   1.00 29.43 ? 2058 HOH A O   1 
HETATM 8625 O  O   . HOH G 7 .    ? 51.991 68.893  4.023   1.00 29.29 ? 2059 HOH A O   1 
HETATM 8626 O  O   . HOH G 7 .    ? 49.832 67.480  4.242   1.00 18.71 ? 2060 HOH A O   1 
HETATM 8627 O  O   . HOH G 7 .    ? 49.297 68.040  6.681   1.00 26.66 ? 2061 HOH A O   1 
HETATM 8628 O  O   . HOH G 7 .    ? 50.675 70.429  7.435   1.00 41.40 ? 2062 HOH A O   1 
HETATM 8629 O  O   . HOH G 7 .    ? 52.293 70.878  5.885   1.00 25.60 ? 2063 HOH A O   1 
HETATM 8630 O  O   . HOH G 7 .    ? 52.720 70.768  8.720   1.00 26.58 ? 2064 HOH A O   1 
HETATM 8631 O  O   . HOH G 7 .    ? 50.427 72.138  9.144   1.00 17.42 ? 2065 HOH A O   1 
HETATM 8632 O  O   . HOH G 7 .    ? 51.438 74.518  8.378   1.00 31.45 ? 2066 HOH A O   1 
HETATM 8633 O  O   . HOH G 7 .    ? 48.317 76.513  8.196   1.00 30.65 ? 2067 HOH A O   1 
HETATM 8634 O  O   . HOH G 7 .    ? 46.137 77.528  9.418   1.00 20.23 ? 2068 HOH A O   1 
HETATM 8635 O  O   . HOH G 7 .    ? 47.208 78.262  11.618  1.00 25.49 ? 2069 HOH A O   1 
HETATM 8636 O  O   . HOH G 7 .    ? 47.062 77.372  14.086  1.00 37.18 ? 2070 HOH A O   1 
HETATM 8637 O  O   . HOH G 7 .    ? 51.070 76.282  14.330  1.00 21.19 ? 2071 HOH A O   1 
HETATM 8638 O  O   . HOH G 7 .    ? 51.566 77.710  12.083  1.00 34.88 ? 2072 HOH A O   1 
HETATM 8639 O  O   . HOH G 7 .    ? 49.219 76.361  5.272   1.00 27.90 ? 2073 HOH A O   1 
HETATM 8640 O  O   . HOH G 7 .    ? 50.795 77.255  2.010   1.00 35.17 ? 2074 HOH A O   1 
HETATM 8641 O  O   . HOH G 7 .    ? 52.498 75.318  1.832   1.00 40.10 ? 2075 HOH A O   1 
HETATM 8642 O  O   . HOH G 7 .    ? 52.410 73.106  4.048   1.00 37.55 ? 2076 HOH A O   1 
HETATM 8643 O  O   . HOH G 7 .    ? 56.976 75.916  0.066   1.00 34.52 ? 2077 HOH A O   1 
HETATM 8644 O  O   . HOH G 7 .    ? 59.048 77.832  0.719   1.00 36.56 ? 2078 HOH A O   1 
HETATM 8645 O  O   . HOH G 7 .    ? 60.611 73.603  -0.354  1.00 49.69 ? 2079 HOH A O   1 
HETATM 8646 O  O   . HOH G 7 .    ? 59.843 71.196  0.120   1.00 36.90 ? 2080 HOH A O   1 
HETATM 8647 O  O   . HOH G 7 .    ? 59.260 68.169  2.411   1.00 20.91 ? 2081 HOH A O   1 
HETATM 8648 O  O   . HOH G 7 .    ? 52.998 67.956  9.013   1.00 27.05 ? 2082 HOH A O   1 
HETATM 8649 O  O   . HOH G 7 .    ? 51.211 66.345  8.437   1.00 23.87 ? 2083 HOH A O   1 
HETATM 8650 O  O   . HOH G 7 .    ? 55.484 67.540  13.227  1.00 25.51 ? 2084 HOH A O   1 
HETATM 8651 O  O   . HOH G 7 .    ? 57.500 68.726  13.543  1.00 35.66 ? 2085 HOH A O   1 
HETATM 8652 O  O   . HOH G 7 .    ? 61.331 63.751  14.657  1.00 35.69 ? 2086 HOH A O   1 
HETATM 8653 O  O   . HOH G 7 .    ? 61.577 59.510  14.550  1.00 32.27 ? 2087 HOH A O   1 
HETATM 8654 O  O   . HOH G 7 .    ? 61.173 57.080  15.577  1.00 33.10 ? 2088 HOH A O   1 
HETATM 8655 O  O   . HOH G 7 .    ? 58.978 50.986  14.804  1.00 40.97 ? 2089 HOH A O   1 
HETATM 8656 O  O   . HOH G 7 .    ? 57.685 49.378  16.627  1.00 28.87 ? 2090 HOH A O   1 
HETATM 8657 O  O   . HOH G 7 .    ? 55.252 50.142  16.836  1.00 28.67 ? 2091 HOH A O   1 
HETATM 8658 O  O   . HOH G 7 .    ? 54.319 47.667  15.627  1.00 23.51 ? 2092 HOH A O   1 
HETATM 8659 O  O   . HOH G 7 .    ? 56.835 46.633  15.813  1.00 28.44 ? 2093 HOH A O   1 
HETATM 8660 O  O   . HOH G 7 .    ? 57.318 48.974  21.255  1.00 23.50 ? 2094 HOH A O   1 
HETATM 8661 O  O   . HOH G 7 .    ? 56.860 47.347  23.253  1.00 36.21 ? 2095 HOH A O   1 
HETATM 8662 O  O   . HOH G 7 .    ? 58.746 51.135  22.081  1.00 21.90 ? 2096 HOH A O   1 
HETATM 8663 O  O   . HOH G 7 .    ? 60.241 50.775  20.209  1.00 35.58 ? 2097 HOH A O   1 
HETATM 8664 O  O   . HOH G 7 .    ? 59.623 50.931  24.750  1.00 32.32 ? 2098 HOH A O   1 
HETATM 8665 O  O   . HOH G 7 .    ? 58.116 52.705  26.152  1.00 35.37 ? 2099 HOH A O   1 
HETATM 8666 O  O   . HOH G 7 .    ? 55.838 51.971  27.294  1.00 31.71 ? 2100 HOH A O   1 
HETATM 8667 O  O   . HOH G 7 .    ? 53.340 52.636  26.240  1.00 29.52 ? 2101 HOH A O   1 
HETATM 8668 O  O   . HOH G 7 .    ? 51.895 50.406  27.486  1.00 28.58 ? 2102 HOH A O   1 
HETATM 8669 O  O   . HOH G 7 .    ? 52.360 49.123  25.640  1.00 28.84 ? 2103 HOH A O   1 
HETATM 8670 O  O   . HOH G 7 .    ? 49.151 49.831  28.366  1.00 16.97 ? 2104 HOH A O   1 
HETATM 8671 O  O   . HOH G 7 .    ? 49.878 47.254  28.938  1.00 24.79 ? 2105 HOH A O   1 
HETATM 8672 O  O   . HOH G 7 .    ? 49.505 45.528  30.938  1.00 24.75 ? 2106 HOH A O   1 
HETATM 8673 O  O   . HOH G 7 .    ? 46.477 43.770  28.499  1.00 37.21 ? 2107 HOH A O   1 
HETATM 8674 O  O   . HOH G 7 .    ? 47.322 45.856  26.762  1.00 31.48 ? 2108 HOH A O   1 
HETATM 8675 O  O   . HOH G 7 .    ? 44.151 45.307  25.423  1.00 32.82 ? 2109 HOH A O   1 
HETATM 8676 O  O   . HOH G 7 .    ? 45.677 45.006  23.020  1.00 31.80 ? 2110 HOH A O   1 
HETATM 8677 O  O   . HOH G 7 .    ? 43.917 44.925  19.237  1.00 40.19 ? 2111 HOH A O   1 
HETATM 8678 O  O   . HOH G 7 .    ? 46.209 46.091  16.318  1.00 32.63 ? 2112 HOH A O   1 
HETATM 8679 O  O   . HOH G 7 .    ? 48.058 48.278  16.480  1.00 15.82 ? 2113 HOH A O   1 
HETATM 8680 O  O   . HOH G 7 .    ? 48.010 49.496  13.848  1.00 11.66 ? 2114 HOH A O   1 
HETATM 8681 O  O   . HOH G 7 .    ? 47.026 48.596  11.525  1.00 15.81 ? 2115 HOH A O   1 
HETATM 8682 O  O   . HOH G 7 .    ? 46.681 45.825  11.655  1.00 29.02 ? 2116 HOH A O   1 
HETATM 8683 O  O   . HOH G 7 .    ? 48.448 44.775  10.240  1.00 33.85 ? 2117 HOH A O   1 
HETATM 8684 O  O   . HOH G 7 .    ? 51.022 45.287  10.248  1.00 29.43 ? 2118 HOH A O   1 
HETATM 8685 O  O   . HOH G 7 .    ? 50.006 43.935  7.072   1.00 18.08 ? 2119 HOH A O   1 
HETATM 8686 O  O   . HOH G 7 .    ? 49.126 41.808  8.347   1.00 26.85 ? 2120 HOH A O   1 
HETATM 8687 O  O   . HOH G 7 .    ? 46.558 42.882  9.718   1.00 29.39 ? 2121 HOH A O   1 
HETATM 8688 O  O   . HOH G 7 .    ? 44.481 40.853  7.753   1.00 37.48 ? 2122 HOH A O   1 
HETATM 8689 O  O   . HOH G 7 .    ? 42.450 39.381  7.770   1.00 35.38 ? 2123 HOH A O   1 
HETATM 8690 O  O   . HOH G 7 .    ? 40.138 39.135  9.239   1.00 25.09 ? 2124 HOH A O   1 
HETATM 8691 O  O   . HOH G 7 .    ? 40.053 35.298  11.388  1.00 23.17 ? 2125 HOH A O   1 
HETATM 8692 O  O   . HOH G 7 .    ? 37.184 33.840  5.602   1.00 42.70 ? 2126 HOH A O   1 
HETATM 8693 O  O   . HOH G 7 .    ? 34.611 36.208  3.424   1.00 32.37 ? 2127 HOH A O   1 
HETATM 8694 O  O   . HOH G 7 .    ? 37.157 37.474  3.023   1.00 28.01 ? 2128 HOH A O   1 
HETATM 8695 O  O   . HOH G 7 .    ? 38.295 39.975  1.756   1.00 12.25 ? 2129 HOH A O   1 
HETATM 8696 O  O   . HOH G 7 .    ? 39.934 39.623  -0.377  1.00 21.97 ? 2130 HOH A O   1 
HETATM 8697 O  O   . HOH G 7 .    ? 42.570 39.354  -1.398  1.00 24.07 ? 2131 HOH A O   1 
HETATM 8698 O  O   . HOH G 7 .    ? 44.518 41.714  -0.526  1.00 14.13 ? 2132 HOH A O   1 
HETATM 8699 O  O   . HOH G 7 .    ? 46.169 39.737  0.086   1.00 30.39 ? 2133 HOH A O   1 
HETATM 8700 O  O   . HOH G 7 .    ? 48.539 40.770  -1.001  1.00 22.67 ? 2134 HOH A O   1 
HETATM 8701 O  O   . HOH G 7 .    ? 49.722 41.032  1.388   1.00 35.84 ? 2135 HOH A O   1 
HETATM 8702 O  O   . HOH G 7 .    ? 48.147 41.653  3.671   1.00 18.82 ? 2136 HOH A O   1 
HETATM 8703 O  O   . HOH G 7 .    ? 47.690 40.083  6.001   1.00 32.37 ? 2137 HOH A O   1 
HETATM 8704 O  O   . HOH G 7 .    ? 49.362 44.121  4.429   1.00 14.52 ? 2138 HOH A O   1 
HETATM 8705 O  O   . HOH G 7 .    ? 51.696 44.375  3.037   1.00 20.56 ? 2139 HOH A O   1 
HETATM 8706 O  O   . HOH G 7 .    ? 51.820 46.399  1.239   1.00 11.90 ? 2140 HOH A O   1 
HETATM 8707 O  O   . HOH G 7 .    ? 49.791 48.383  1.371   1.00 9.25  ? 2141 HOH A O   1 
HETATM 8708 O  O   . HOH G 7 .    ? 47.489 45.956  3.641   1.00 11.04 ? 2142 HOH A O   1 
HETATM 8709 O  O   . HOH G 7 .    ? 47.457 42.820  -2.430  1.00 14.15 ? 2143 HOH A O   1 
HETATM 8710 O  O   . HOH G 7 .    ? 47.981 41.589  -5.279  1.00 27.66 ? 2144 HOH A O   1 
HETATM 8711 O  O   . HOH G 7 .    ? 48.715 44.131  -6.228  1.00 14.30 ? 2145 HOH A O   1 
HETATM 8712 O  O   . HOH G 7 .    ? 47.895 43.839  -8.710  1.00 19.59 ? 2146 HOH A O   1 
HETATM 8713 O  O   . HOH G 7 .    ? 45.546 42.027  -8.876  1.00 33.32 ? 2147 HOH A O   1 
HETATM 8714 O  O   . HOH G 7 .    ? 43.501 41.668  -7.665  1.00 23.42 ? 2148 HOH A O   1 
HETATM 8715 O  O   . HOH G 7 .    ? 42.273 40.476  -9.812  1.00 33.64 ? 2149 HOH A O   1 
HETATM 8716 O  O   . HOH G 7 .    ? 41.457 44.615  -6.872  1.00 13.76 ? 2150 HOH A O   1 
HETATM 8717 O  O   . HOH G 7 .    ? 36.683 44.771  -5.431  1.00 9.89  ? 2151 HOH A O   1 
HETATM 8718 O  O   . HOH G 7 .    ? 31.705 46.887  -8.073  1.00 8.22  ? 2152 HOH A O   1 
HETATM 8719 O  O   . HOH G 7 .    ? 33.433 48.000  -10.139 1.00 8.44  ? 2153 HOH A O   1 
HETATM 8720 O  O   . HOH G 7 .    ? 35.082 48.066  -16.457 1.00 31.53 ? 2154 HOH A O   1 
HETATM 8721 O  O   . HOH G 7 .    ? 35.069 50.401  -17.567 1.00 13.15 ? 2155 HOH A O   1 
HETATM 8722 O  O   . HOH G 7 .    ? 37.562 51.343  -18.554 1.00 16.39 ? 2156 HOH A O   1 
HETATM 8723 O  O   . HOH G 7 .    ? 37.571 51.987  -21.073 1.00 11.85 ? 2157 HOH A O   1 
HETATM 8724 O  O   . HOH G 7 .    ? 39.621 53.800  -20.760 1.00 14.28 ? 2158 HOH A O   1 
HETATM 8725 O  O   . HOH G 7 .    ? 40.140 56.137  -19.085 1.00 24.65 ? 2159 HOH A O   1 
HETATM 8726 O  O   . HOH G 7 .    ? 39.632 58.772  -18.011 1.00 16.92 ? 2160 HOH A O   1 
HETATM 8727 O  O   . HOH G 7 .    ? 41.630 58.537  -16.071 1.00 11.52 ? 2161 HOH A O   1 
HETATM 8728 O  O   . HOH G 7 .    ? 44.565 58.568  -15.964 1.00 13.01 ? 2162 HOH A O   1 
HETATM 8729 O  O   . HOH G 7 .    ? 44.471 55.948  -15.357 1.00 14.48 ? 2163 HOH A O   1 
HETATM 8730 O  O   . HOH G 7 .    ? 47.229 55.706  -15.465 1.00 14.55 ? 2164 HOH A O   1 
HETATM 8731 O  O   . HOH G 7 .    ? 46.614 57.132  -18.838 1.00 12.62 ? 2165 HOH A O   1 
HETATM 8732 O  O   . HOH G 7 .    ? 44.986 54.899  -18.320 1.00 26.54 ? 2166 HOH A O   1 
HETATM 8733 O  O   . HOH G 7 .    ? 45.895 52.634  -19.155 1.00 16.17 ? 2167 HOH A O   1 
HETATM 8734 O  O   . HOH G 7 .    ? 46.755 53.703  -21.461 1.00 25.37 ? 2168 HOH A O   1 
HETATM 8735 O  O   . HOH G 7 .    ? 48.700 54.777  -22.789 1.00 17.46 ? 2169 HOH A O   1 
HETATM 8736 O  O   . HOH G 7 .    ? 51.291 53.181  -23.956 1.00 11.39 ? 2170 HOH A O   1 
HETATM 8737 O  O   . HOH G 7 .    ? 50.999 52.662  -28.594 1.00 19.39 ? 2171 HOH A O   1 
HETATM 8738 O  O   . HOH G 7 .    ? 49.780 54.988  -29.139 1.00 18.73 ? 2172 HOH A O   1 
HETATM 8739 O  O   . HOH G 7 .    ? 52.097 56.240  -30.188 1.00 26.18 ? 2173 HOH A O   1 
HETATM 8740 O  O   . HOH G 7 .    ? 53.094 55.030  -31.955 1.00 32.78 ? 2174 HOH A O   1 
HETATM 8741 O  O   . HOH G 7 .    ? 53.239 53.225  -30.018 1.00 25.54 ? 2175 HOH A O   1 
HETATM 8742 O  O   . HOH G 7 .    ? 56.177 50.103  -30.439 1.00 43.48 ? 2176 HOH A O   1 
HETATM 8743 O  O   . HOH G 7 .    ? 59.955 52.865  -30.593 1.00 30.14 ? 2177 HOH A O   1 
HETATM 8744 O  O   . HOH G 7 .    ? 61.310 54.132  -28.890 1.00 23.36 ? 2178 HOH A O   1 
HETATM 8745 O  O   . HOH G 7 .    ? 64.671 55.758  -31.293 1.00 33.54 ? 2179 HOH A O   1 
HETATM 8746 O  O   . HOH G 7 .    ? 66.334 58.108  -31.201 1.00 36.20 ? 2180 HOH A O   1 
HETATM 8747 O  O   . HOH G 7 .    ? 66.785 59.808  -27.142 1.00 18.38 ? 2181 HOH A O   1 
HETATM 8748 O  O   . HOH G 7 .    ? 67.929 58.556  -24.101 1.00 18.34 ? 2182 HOH A O   1 
HETATM 8749 O  O   . HOH G 7 .    ? 66.625 56.099  -20.267 1.00 17.11 ? 2183 HOH A O   1 
HETATM 8750 O  O   . HOH G 7 .    ? 67.596 54.412  -18.392 1.00 22.16 ? 2184 HOH A O   1 
HETATM 8751 O  O   . HOH G 7 .    ? 69.815 53.691  -19.744 1.00 36.32 ? 2185 HOH A O   1 
HETATM 8752 O  O   . HOH G 7 .    ? 65.651 52.399  -21.090 1.00 38.40 ? 2186 HOH A O   1 
HETATM 8753 O  O   . HOH G 7 .    ? 64.406 49.476  -21.642 1.00 36.96 ? 2187 HOH A O   1 
HETATM 8754 O  O   . HOH G 7 .    ? 62.297 48.096  -20.925 1.00 37.64 ? 2188 HOH A O   1 
HETATM 8755 O  O   . HOH G 7 .    ? 60.843 46.684  -22.436 1.00 34.35 ? 2189 HOH A O   1 
HETATM 8756 O  O   . HOH G 7 .    ? 63.036 42.786  -20.917 1.00 26.36 ? 2190 HOH A O   1 
HETATM 8757 O  O   . HOH G 7 .    ? 57.039 43.053  -19.969 1.00 24.99 ? 2191 HOH A O   1 
HETATM 8758 O  O   . HOH G 7 .    ? 56.501 46.105  -17.439 1.00 16.36 ? 2192 HOH A O   1 
HETATM 8759 O  O   . HOH G 7 .    ? 57.146 39.023  -19.448 1.00 39.07 ? 2193 HOH A O   1 
HETATM 8760 O  O   . HOH G 7 .    ? 58.229 37.196  -18.025 1.00 40.67 ? 2194 HOH A O   1 
HETATM 8761 O  O   . HOH G 7 .    ? 59.337 37.571  -15.307 1.00 28.62 ? 2195 HOH A O   1 
HETATM 8762 O  O   . HOH G 7 .    ? 57.124 35.915  -14.341 1.00 31.92 ? 2196 HOH A O   1 
HETATM 8763 O  O   . HOH G 7 .    ? 58.434 34.710  -12.059 1.00 35.07 ? 2197 HOH A O   1 
HETATM 8764 O  O   . HOH G 7 .    ? 58.424 34.714  -6.009  1.00 34.48 ? 2198 HOH A O   1 
HETATM 8765 O  O   . HOH G 7 .    ? 64.413 39.285  -10.220 1.00 21.76 ? 2199 HOH A O   1 
HETATM 8766 O  O   . HOH G 7 .    ? 67.127 38.366  -9.541  1.00 27.59 ? 2200 HOH A O   1 
HETATM 8767 O  O   . HOH G 7 .    ? 63.506 44.547  -6.731  1.00 16.42 ? 2201 HOH A O   1 
HETATM 8768 O  O   . HOH G 7 .    ? 63.550 45.661  -3.026  1.00 42.57 ? 2202 HOH A O   1 
HETATM 8769 O  O   . HOH G 7 .    ? 66.069 45.348  -3.252  1.00 32.62 ? 2203 HOH A O   1 
HETATM 8770 O  O   . HOH G 7 .    ? 67.435 46.483  -1.386  1.00 23.44 ? 2204 HOH A O   1 
HETATM 8771 O  O   . HOH G 7 .    ? 68.160 49.245  -1.087  1.00 22.56 ? 2205 HOH A O   1 
HETATM 8772 O  O   . HOH G 7 .    ? 66.464 50.296  0.504   1.00 34.17 ? 2206 HOH A O   1 
HETATM 8773 O  O   . HOH G 7 .    ? 63.398 51.906  -0.295  1.00 31.08 ? 2207 HOH A O   1 
HETATM 8774 O  O   . HOH G 7 .    ? 59.300 49.907  -0.731  1.00 15.69 ? 2208 HOH A O   1 
HETATM 8775 O  O   . HOH G 7 .    ? 59.353 48.809  2.285   1.00 37.13 ? 2209 HOH A O   1 
HETATM 8776 O  O   . HOH G 7 .    ? 59.359 51.818  2.545   1.00 24.22 ? 2210 HOH A O   1 
HETATM 8777 O  O   . HOH G 7 .    ? 58.395 52.699  4.714   1.00 22.29 ? 2211 HOH A O   1 
HETATM 8778 O  O   . HOH G 7 .    ? 60.221 51.261  6.243   1.00 28.61 ? 2212 HOH A O   1 
HETATM 8779 O  O   . HOH G 7 .    ? 52.112 50.548  6.363   1.00 10.63 ? 2213 HOH A O   1 
HETATM 8780 O  O   . HOH G 7 .    ? 52.901 43.729  7.567   1.00 34.51 ? 2214 HOH A O   1 
HETATM 8781 O  O   . HOH G 7 .    ? 57.927 42.199  1.589   1.00 22.74 ? 2215 HOH A O   1 
HETATM 8782 O  O   . HOH G 7 .    ? 58.894 46.235  -1.461  1.00 21.41 ? 2216 HOH A O   1 
HETATM 8783 O  O   . HOH G 7 .    ? 60.993 45.216  -3.782  1.00 30.67 ? 2217 HOH A O   1 
HETATM 8784 O  O   . HOH G 7 .    ? 51.008 44.160  -8.020  1.00 11.45 ? 2218 HOH A O   1 
HETATM 8785 O  O   . HOH G 7 .    ? 51.856 40.896  -13.033 1.00 31.51 ? 2219 HOH A O   1 
HETATM 8786 O  O   . HOH G 7 .    ? 47.159 41.277  -14.816 1.00 27.87 ? 2220 HOH A O   1 
HETATM 8787 O  O   . HOH G 7 .    ? 42.514 39.236  -15.685 1.00 25.62 ? 2221 HOH A O   1 
HETATM 8788 O  O   . HOH G 7 .    ? 41.513 41.033  -17.525 1.00 16.99 ? 2222 HOH A O   1 
HETATM 8789 O  O   . HOH G 7 .    ? 40.879 40.635  -21.508 1.00 23.99 ? 2223 HOH A O   1 
HETATM 8790 O  O   . HOH G 7 .    ? 38.666 42.062  -22.152 1.00 25.59 ? 2224 HOH A O   1 
HETATM 8791 O  O   . HOH G 7 .    ? 36.867 41.056  -24.687 1.00 27.74 ? 2225 HOH A O   1 
HETATM 8792 O  O   . HOH G 7 .    ? 37.279 45.008  -25.368 1.00 20.34 ? 2226 HOH A O   1 
HETATM 8793 O  O   . HOH G 7 .    ? 35.485 45.010  -27.389 1.00 15.62 ? 2227 HOH A O   1 
HETATM 8794 O  O   . HOH G 7 .    ? 40.793 47.978  -29.259 1.00 31.81 ? 2228 HOH A O   1 
HETATM 8795 O  O   . HOH G 7 .    ? 42.642 47.304  -27.299 1.00 29.25 ? 2229 HOH A O   1 
HETATM 8796 O  O   . HOH G 7 .    ? 42.121 47.138  -24.528 1.00 13.69 ? 2230 HOH A O   1 
HETATM 8797 O  O   . HOH G 7 .    ? 41.406 44.584  -24.317 1.00 20.39 ? 2231 HOH A O   1 
HETATM 8798 O  O   . HOH G 7 .    ? 43.302 40.311  -23.045 1.00 33.81 ? 2232 HOH A O   1 
HETATM 8799 O  O   . HOH G 7 .    ? 46.997 46.142  -26.501 1.00 36.04 ? 2233 HOH A O   1 
HETATM 8800 O  O   . HOH G 7 .    ? 47.226 47.615  -28.728 1.00 31.75 ? 2234 HOH A O   1 
HETATM 8801 O  O   . HOH G 7 .    ? 48.451 49.665  -29.194 1.00 24.26 ? 2235 HOH A O   1 
HETATM 8802 O  O   . HOH G 7 .    ? 49.261 51.477  -30.306 1.00 34.79 ? 2236 HOH A O   1 
HETATM 8803 O  O   . HOH G 7 .    ? 47.848 49.571  -31.520 1.00 39.72 ? 2237 HOH A O   1 
HETATM 8804 O  O   . HOH G 7 .    ? 49.986 46.720  -30.508 1.00 43.44 ? 2238 HOH A O   1 
HETATM 8805 O  O   . HOH G 7 .    ? 52.184 45.119  -27.281 1.00 34.63 ? 2239 HOH A O   1 
HETATM 8806 O  O   . HOH G 7 .    ? 53.272 46.973  -25.199 1.00 18.12 ? 2240 HOH A O   1 
HETATM 8807 O  O   . HOH G 7 .    ? 58.418 43.928  -28.116 1.00 34.47 ? 2241 HOH A O   1 
HETATM 8808 O  O   . HOH G 7 .    ? 58.768 53.523  -22.249 1.00 21.18 ? 2242 HOH A O   1 
HETATM 8809 O  O   . HOH G 7 .    ? 60.390 60.828  -18.155 1.00 10.05 ? 2243 HOH A O   1 
HETATM 8810 O  O   . HOH G 7 .    ? 53.672 64.697  -19.860 1.00 7.98  ? 2244 HOH A O   1 
HETATM 8811 O  O   . HOH G 7 .    ? 53.175 70.583  -17.407 1.00 29.74 ? 2245 HOH A O   1 
HETATM 8812 O  O   . HOH G 7 .    ? 53.535 72.423  -19.334 1.00 14.24 ? 2246 HOH A O   1 
HETATM 8813 O  O   . HOH G 7 .    ? 51.240 71.225  -20.379 1.00 18.70 ? 2247 HOH A O   1 
HETATM 8814 O  O   . HOH G 7 .    ? 49.914 73.365  -21.765 1.00 26.89 ? 2248 HOH A O   1 
HETATM 8815 O  O   . HOH G 7 .    ? 47.517 71.732  -20.265 1.00 24.40 ? 2249 HOH A O   1 
HETATM 8816 O  O   . HOH G 7 .    ? 46.935 72.202  -17.485 1.00 21.65 ? 2250 HOH A O   1 
HETATM 8817 O  O   . HOH G 7 .    ? 45.562 69.853  -18.509 1.00 35.59 ? 2251 HOH A O   1 
HETATM 8818 O  O   . HOH G 7 .    ? 46.408 67.528  -15.673 1.00 13.76 ? 2252 HOH A O   1 
HETATM 8819 O  O   . HOH G 7 .    ? 50.008 70.663  -17.771 1.00 26.40 ? 2253 HOH A O   1 
HETATM 8820 O  O   . HOH G 7 .    ? 51.038 70.762  -23.830 1.00 17.61 ? 2254 HOH A O   1 
HETATM 8821 O  O   . HOH G 7 .    ? 50.490 73.554  -25.519 1.00 19.47 ? 2255 HOH A O   1 
HETATM 8822 O  O   . HOH G 7 .    ? 54.913 80.881  -23.700 1.00 12.37 ? 2256 HOH A O   1 
HETATM 8823 O  O   . HOH G 7 .    ? 55.142 80.340  -19.433 1.00 22.02 ? 2257 HOH A O   1 
HETATM 8824 O  O   . HOH G 7 .    ? 57.262 80.092  -17.987 1.00 37.86 ? 2258 HOH A O   1 
HETATM 8825 O  O   . HOH G 7 .    ? 55.598 81.848  -16.421 1.00 33.33 ? 2259 HOH A O   1 
HETATM 8826 O  O   . HOH G 7 .    ? 56.023 78.597  -14.705 1.00 33.27 ? 2260 HOH A O   1 
HETATM 8827 O  O   . HOH G 7 .    ? 52.922 76.071  -14.248 1.00 37.39 ? 2261 HOH A O   1 
HETATM 8828 O  O   . HOH G 7 .    ? 52.526 76.376  -11.827 1.00 38.02 ? 2262 HOH A O   1 
HETATM 8829 O  O   . HOH G 7 .    ? 50.095 79.574  -11.379 1.00 41.36 ? 2263 HOH A O   1 
HETATM 8830 O  O   . HOH G 7 .    ? 48.380 77.875  -9.797  1.00 25.49 ? 2264 HOH A O   1 
HETATM 8831 O  O   . HOH G 7 .    ? 45.744 79.031  -7.964  1.00 24.29 ? 2265 HOH A O   1 
HETATM 8832 O  O   . HOH G 7 .    ? 48.149 80.137  -4.354  1.00 39.13 ? 2266 HOH A O   1 
HETATM 8833 O  O   . HOH G 7 .    ? 50.057 81.167  -3.047  1.00 38.66 ? 2267 HOH A O   1 
HETATM 8834 O  O   . HOH G 7 .    ? 51.225 79.326  -1.875  1.00 23.27 ? 2268 HOH A O   1 
HETATM 8835 O  O   . HOH G 7 .    ? 51.738 79.986  0.709   1.00 34.91 ? 2269 HOH A O   1 
HETATM 8836 O  O   . HOH G 7 .    ? 46.531 82.617  -0.721  1.00 32.61 ? 2270 HOH A O   1 
HETATM 8837 O  O   . HOH G 7 .    ? 40.994 81.603  -3.478  1.00 45.68 ? 2271 HOH A O   1 
HETATM 8838 O  O   . HOH G 7 .    ? 38.721 80.166  -3.256  1.00 25.89 ? 2272 HOH A O   1 
HETATM 8839 O  O   . HOH G 7 .    ? 37.692 80.345  -0.675  1.00 16.71 ? 2273 HOH A O   1 
HETATM 8840 O  O   . HOH G 7 .    ? 38.142 83.113  -0.978  1.00 23.83 ? 2274 HOH A O   1 
HETATM 8841 O  O   . HOH G 7 .    ? 37.229 83.543  -4.142  1.00 26.68 ? 2275 HOH A O   1 
HETATM 8842 O  O   . HOH G 7 .    ? 35.089 85.106  -1.000  1.00 36.77 ? 2276 HOH A O   1 
HETATM 8843 O  O   . HOH G 7 .    ? 32.988 84.221  0.320   1.00 26.08 ? 2277 HOH A O   1 
HETATM 8844 O  O   . HOH G 7 .    ? 31.409 81.701  0.536   1.00 16.30 ? 2278 HOH A O   1 
HETATM 8845 O  O   . HOH G 7 .    ? 29.874 83.027  2.542   1.00 17.72 ? 2279 HOH A O   1 
HETATM 8846 O  O   . HOH G 7 .    ? 27.578 82.397  3.617   1.00 22.42 ? 2280 HOH A O   1 
HETATM 8847 O  O   . HOH G 7 .    ? 24.787 83.782  2.513   1.00 27.07 ? 2281 HOH A O   1 
HETATM 8848 O  O   . HOH G 7 .    ? 21.791 79.597  5.470   1.00 24.32 ? 2282 HOH A O   1 
HETATM 8849 O  O   . HOH G 7 .    ? 19.270 76.328  4.827   1.00 23.89 ? 2283 HOH A O   1 
HETATM 8850 O  O   . HOH G 7 .    ? 17.717 74.289  3.985   1.00 18.96 ? 2284 HOH A O   1 
HETATM 8851 O  O   . HOH G 7 .    ? 15.695 73.418  5.469   1.00 24.71 ? 2285 HOH A O   1 
HETATM 8852 O  O   . HOH G 7 .    ? 15.725 70.018  6.348   1.00 27.60 ? 2286 HOH A O   1 
HETATM 8853 O  O   . HOH G 7 .    ? 17.880 70.744  6.644   1.00 27.55 ? 2287 HOH A O   1 
HETATM 8854 O  O   . HOH G 7 .    ? 18.667 69.843  4.250   1.00 13.49 ? 2288 HOH A O   1 
HETATM 8855 O  O   . HOH G 7 .    ? 19.298 72.272  3.068   1.00 14.73 ? 2289 HOH A O   1 
HETATM 8856 O  O   . HOH G 7 .    ? 16.927 74.399  -2.994  1.00 13.25 ? 2290 HOH A O   1 
HETATM 8857 O  O   . HOH G 7 .    ? 20.133 74.184  -6.706  1.00 12.18 ? 2291 HOH A O   1 
HETATM 8858 O  O   . HOH G 7 .    ? 24.615 70.455  -8.730  1.00 10.69 ? 2292 HOH A O   1 
HETATM 8859 O  O   . HOH G 7 .    ? 26.757 68.788  -9.219  1.00 8.47  ? 2293 HOH A O   1 
HETATM 8860 O  O   . HOH G 7 .    ? 32.599 64.497  -9.974  1.00 15.58 ? 2294 HOH A O   1 
HETATM 8861 O  O   . HOH G 7 .    ? 34.238 58.439  -8.764  1.00 7.71  ? 2295 HOH A O   1 
HETATM 8862 O  O   . HOH G 7 .    ? 30.158 58.304  -11.768 1.00 7.43  ? 2296 HOH A O   1 
HETATM 8863 O  O   . HOH G 7 .    ? 24.691 52.763  -11.720 1.00 8.57  ? 2297 HOH A O   1 
HETATM 8864 O  O   . HOH G 7 .    ? 22.298 54.274  -12.020 1.00 9.59  ? 2298 HOH A O   1 
HETATM 8865 O  O   . HOH G 7 .    ? 19.641 53.347  -11.794 1.00 9.89  ? 2299 HOH A O   1 
HETATM 8866 O  O   . HOH G 7 .    ? 18.575 50.861  -12.426 1.00 11.57 ? 2300 HOH A O   1 
HETATM 8867 O  O   . HOH G 7 .    ? 22.892 51.606  -8.729  1.00 15.09 ? 2301 HOH A O   1 
HETATM 8868 O  O   . HOH G 7 .    ? 25.509 51.053  -9.469  1.00 11.58 ? 2302 HOH A O   1 
HETATM 8869 O  O   . HOH G 7 .    ? 26.257 48.757  -10.941 1.00 9.46  ? 2303 HOH A O   1 
HETATM 8870 O  O   . HOH G 7 .    ? 26.039 49.487  -13.675 1.00 8.93  ? 2304 HOH A O   1 
HETATM 8871 O  O   . HOH G 7 .    ? 28.823 42.614  -11.935 1.00 11.04 ? 2305 HOH A O   1 
HETATM 8872 O  O   . HOH G 7 .    ? 26.662 41.437  -13.207 1.00 13.11 ? 2306 HOH A O   1 
HETATM 8873 O  O   . HOH G 7 .    ? 24.470 38.946  -11.483 1.00 19.74 ? 2307 HOH A O   1 
HETATM 8874 O  O   . HOH G 7 .    ? 22.773 36.634  -9.688  1.00 39.57 ? 2308 HOH A O   1 
HETATM 8875 O  O   . HOH G 7 .    ? 21.788 40.176  -8.605  1.00 22.30 ? 2309 HOH A O   1 
HETATM 8876 O  O   . HOH G 7 .    ? 20.692 42.564  -7.319  1.00 17.13 ? 2310 HOH A O   1 
HETATM 8877 O  O   . HOH G 7 .    ? 19.711 41.441  -4.945  1.00 21.97 ? 2311 HOH A O   1 
HETATM 8878 O  O   . HOH G 7 .    ? 19.158 42.292  -2.530  1.00 25.71 ? 2312 HOH A O   1 
HETATM 8879 O  O   . HOH G 7 .    ? 16.578 42.760  -2.254  1.00 26.38 ? 2313 HOH A O   1 
HETATM 8880 O  O   . HOH G 7 .    ? 18.634 39.170  -2.573  1.00 34.93 ? 2314 HOH A O   1 
HETATM 8881 O  O   . HOH G 7 .    ? 17.845 37.673  -0.093  1.00 37.22 ? 2315 HOH A O   1 
HETATM 8882 O  O   . HOH G 7 .    ? 21.984 36.708  0.342   1.00 21.20 ? 2316 HOH A O   1 
HETATM 8883 O  O   . HOH G 7 .    ? 24.611 34.180  0.329   1.00 43.72 ? 2317 HOH A O   1 
HETATM 8884 O  O   . HOH G 7 .    ? 27.059 33.655  -3.191  1.00 35.02 ? 2318 HOH A O   1 
HETATM 8885 O  O   . HOH G 7 .    ? 29.962 34.048  -1.486  1.00 25.57 ? 2319 HOH A O   1 
HETATM 8886 O  O   . HOH G 7 .    ? 32.135 34.216  -3.247  1.00 20.36 ? 2320 HOH A O   1 
HETATM 8887 O  O   . HOH G 7 .    ? 33.224 36.517  -4.339  1.00 13.96 ? 2321 HOH A O   1 
HETATM 8888 O  O   . HOH G 7 .    ? 32.326 38.999  -4.886  1.00 10.69 ? 2322 HOH A O   1 
HETATM 8889 O  O   . HOH G 7 .    ? 35.948 35.913  -4.506  1.00 18.88 ? 2323 HOH A O   1 
HETATM 8890 O  O   . HOH G 7 .    ? 39.852 38.665  -3.531  1.00 21.30 ? 2324 HOH A O   1 
HETATM 8891 O  O   . HOH G 7 .    ? 30.441 34.530  -9.639  1.00 28.87 ? 2325 HOH A O   1 
HETATM 8892 O  O   . HOH G 7 .    ? 30.223 34.997  -12.353 1.00 19.63 ? 2326 HOH A O   1 
HETATM 8893 O  O   . HOH G 7 .    ? 28.058 35.138  -6.709  1.00 21.92 ? 2327 HOH A O   1 
HETATM 8894 O  O   . HOH G 7 .    ? 25.242 34.421  -7.096  1.00 39.22 ? 2328 HOH A O   1 
HETATM 8895 O  O   . HOH G 7 .    ? 21.446 35.225  -5.302  1.00 33.78 ? 2329 HOH A O   1 
HETATM 8896 O  O   . HOH G 7 .    ? 18.047 36.746  5.812   1.00 38.08 ? 2330 HOH A O   1 
HETATM 8897 O  O   . HOH G 7 .    ? 17.266 41.507  9.362   1.00 27.75 ? 2331 HOH A O   1 
HETATM 8898 O  O   . HOH G 7 .    ? 12.945 42.424  12.762  1.00 17.97 ? 2332 HOH A O   1 
HETATM 8899 O  O   . HOH G 7 .    ? 10.342 41.660  12.292  1.00 34.85 ? 2333 HOH A O   1 
HETATM 8900 O  O   . HOH G 7 .    ? 8.747  44.353  13.213  1.00 28.05 ? 2334 HOH A O   1 
HETATM 8901 O  O   . HOH G 7 .    ? 8.030  47.983  12.006  1.00 24.48 ? 2335 HOH A O   1 
HETATM 8902 O  O   . HOH G 7 .    ? 7.064  51.216  9.213   1.00 43.25 ? 2336 HOH A O   1 
HETATM 8903 O  O   . HOH G 7 .    ? 9.023  50.247  8.102   1.00 26.76 ? 2337 HOH A O   1 
HETATM 8904 O  O   . HOH G 7 .    ? 8.582  49.274  5.628   1.00 45.44 ? 2338 HOH A O   1 
HETATM 8905 O  O   . HOH G 7 .    ? 10.438 51.512  2.412   1.00 28.51 ? 2339 HOH A O   1 
HETATM 8906 O  O   . HOH G 7 .    ? 10.891 53.477  4.115   1.00 24.12 ? 2340 HOH A O   1 
HETATM 8907 O  O   . HOH G 7 .    ? 11.300 53.007  6.922   1.00 16.43 ? 2341 HOH A O   1 
HETATM 8908 O  O   . HOH G 7 .    ? 12.433 56.149  5.415   1.00 14.88 ? 2342 HOH A O   1 
HETATM 8909 O  O   . HOH G 7 .    ? 13.829 53.996  4.413   1.00 13.01 ? 2343 HOH A O   1 
HETATM 8910 O  O   . HOH G 7 .    ? 13.426 53.320  1.840   1.00 16.84 ? 2344 HOH A O   1 
HETATM 8911 O  O   . HOH G 7 .    ? 14.364 50.527  0.978   1.00 20.39 ? 2345 HOH A O   1 
HETATM 8912 O  O   . HOH G 7 .    ? 13.401 48.163  1.672   1.00 27.98 ? 2346 HOH A O   1 
HETATM 8913 O  O   . HOH G 7 .    ? 13.321 50.619  -1.581  1.00 21.00 ? 2347 HOH A O   1 
HETATM 8914 O  O   . HOH G 7 .    ? 11.617 48.051  -2.379  1.00 32.71 ? 2348 HOH A O   1 
HETATM 8915 O  O   . HOH G 7 .    ? 9.460  47.597  -8.713  1.00 38.54 ? 2349 HOH A O   1 
HETATM 8916 O  O   . HOH G 7 .    ? 7.994  52.704  -7.541  1.00 38.30 ? 2350 HOH A O   1 
HETATM 8917 O  O   . HOH G 7 .    ? 8.702  54.740  -6.092  1.00 22.69 ? 2351 HOH A O   1 
HETATM 8918 O  O   . HOH G 7 .    ? 8.608  57.478  -6.816  1.00 21.56 ? 2352 HOH A O   1 
HETATM 8919 O  O   . HOH G 7 .    ? 10.016 57.731  -3.306  1.00 29.37 ? 2353 HOH A O   1 
HETATM 8920 O  O   . HOH G 7 .    ? 11.704 59.302  -4.973  1.00 18.74 ? 2354 HOH A O   1 
HETATM 8921 O  O   . HOH G 7 .    ? 14.038 59.592  -3.358  1.00 12.84 ? 2355 HOH A O   1 
HETATM 8922 O  O   . HOH G 7 .    ? 13.905 57.843  -1.337  1.00 17.30 ? 2356 HOH A O   1 
HETATM 8923 O  O   . HOH G 7 .    ? 12.938 61.826  -2.259  1.00 21.93 ? 2357 HOH A O   1 
HETATM 8924 O  O   . HOH G 7 .    ? 11.491 61.429  0.043   1.00 40.08 ? 2358 HOH A O   1 
HETATM 8925 O  O   . HOH G 7 .    ? 10.321 62.061  1.910   1.00 33.39 ? 2359 HOH A O   1 
HETATM 8926 O  O   . HOH G 7 .    ? 11.266 62.020  5.265   1.00 30.45 ? 2360 HOH A O   1 
HETATM 8927 O  O   . HOH G 7 .    ? 13.172 62.792  6.714   1.00 37.90 ? 2361 HOH A O   1 
HETATM 8928 O  O   . HOH G 7 .    ? 13.641 60.562  7.738   1.00 23.50 ? 2362 HOH A O   1 
HETATM 8929 O  O   . HOH G 7 .    ? 14.425 59.873  5.152   1.00 12.56 ? 2363 HOH A O   1 
HETATM 8930 O  O   . HOH G 7 .    ? 11.567 58.587  7.878   1.00 25.31 ? 2364 HOH A O   1 
HETATM 8931 O  O   . HOH G 7 .    ? 9.762  59.660  6.599   1.00 32.08 ? 2365 HOH A O   1 
HETATM 8932 O  O   . HOH G 7 .    ? 5.362  57.025  6.991   1.00 32.78 ? 2366 HOH A O   1 
HETATM 8933 O  O   . HOH G 7 .    ? 6.854  59.552  2.339   1.00 51.96 ? 2367 HOH A O   1 
HETATM 8934 O  O   . HOH G 7 .    ? 7.755  58.108  0.055   1.00 35.54 ? 2368 HOH A O   1 
HETATM 8935 O  O   . HOH G 7 .    ? 11.022 62.385  -4.463  1.00 34.16 ? 2369 HOH A O   1 
HETATM 8936 O  O   . HOH G 7 .    ? 13.156 66.687  -4.752  1.00 13.79 ? 2370 HOH A O   1 
HETATM 8937 O  O   . HOH G 7 .    ? 14.080 68.103  -7.719  1.00 16.43 ? 2371 HOH A O   1 
HETATM 8938 O  O   . HOH G 7 .    ? 13.718 69.884  -9.573  1.00 19.85 ? 2372 HOH A O   1 
HETATM 8939 O  O   . HOH G 7 .    ? 11.383 70.740  -7.899  1.00 30.48 ? 2373 HOH A O   1 
HETATM 8940 O  O   . HOH G 7 .    ? 12.680 66.169  -9.608  1.00 16.90 ? 2374 HOH A O   1 
HETATM 8941 O  O   . HOH G 7 .    ? 10.329 64.506  -10.201 1.00 40.32 ? 2375 HOH A O   1 
HETATM 8942 O  O   . HOH G 7 .    ? 12.223 64.434  -12.353 1.00 24.47 ? 2376 HOH A O   1 
HETATM 8943 O  O   . HOH G 7 .    ? 14.241 62.706  -12.079 1.00 16.70 ? 2377 HOH A O   1 
HETATM 8944 O  O   . HOH G 7 .    ? 14.584 61.750  -14.544 1.00 18.69 ? 2378 HOH A O   1 
HETATM 8945 O  O   . HOH G 7 .    ? 14.359 63.792  -16.344 1.00 15.26 ? 2379 HOH A O   1 
HETATM 8946 O  O   . HOH G 7 .    ? 11.681 63.479  -16.828 1.00 19.22 ? 2380 HOH A O   1 
HETATM 8947 O  O   . HOH G 7 .    ? 10.118 62.928  -14.602 1.00 30.99 ? 2381 HOH A O   1 
HETATM 8948 O  O   . HOH G 7 .    ? 8.515  65.101  -14.619 1.00 21.99 ? 2382 HOH A O   1 
HETATM 8949 O  O   . HOH G 7 .    ? 11.398 61.187  -18.381 1.00 18.69 ? 2383 HOH A O   1 
HETATM 8950 O  O   . HOH G 7 .    ? 13.349 62.209  -19.954 1.00 16.94 ? 2384 HOH A O   1 
HETATM 8951 O  O   . HOH G 7 .    ? 13.807 60.677  -22.440 1.00 15.60 ? 2385 HOH A O   1 
HETATM 8952 O  O   . HOH G 7 .    ? 12.892 61.807  -24.968 1.00 29.67 ? 2386 HOH A O   1 
HETATM 8953 O  O   . HOH G 7 .    ? 14.889 63.451  -25.832 1.00 24.92 ? 2387 HOH A O   1 
HETATM 8954 O  O   . HOH G 7 .    ? 14.631 64.485  -28.885 1.00 35.95 ? 2388 HOH A O   1 
HETATM 8955 O  O   . HOH G 7 .    ? 16.605 62.866  -29.552 1.00 38.94 ? 2389 HOH A O   1 
HETATM 8956 O  O   . HOH G 7 .    ? 16.646 60.490  -28.124 1.00 19.96 ? 2390 HOH A O   1 
HETATM 8957 O  O   . HOH G 7 .    ? 18.463 64.831  -26.997 1.00 19.59 ? 2391 HOH A O   1 
HETATM 8958 O  O   . HOH G 7 .    ? 17.076 67.067  -26.003 1.00 25.82 ? 2392 HOH A O   1 
HETATM 8959 O  O   . HOH G 7 .    ? 17.216 69.935  -23.334 1.00 15.62 ? 2393 HOH A O   1 
HETATM 8960 O  O   . HOH G 7 .    ? 14.546 70.337  -22.905 1.00 24.35 ? 2394 HOH A O   1 
HETATM 8961 O  O   . HOH G 7 .    ? 13.086 69.916  -24.924 1.00 41.25 ? 2395 HOH A O   1 
HETATM 8962 O  O   . HOH G 7 .    ? 12.767 74.251  -23.026 1.00 37.18 ? 2396 HOH A O   1 
HETATM 8963 O  O   . HOH G 7 .    ? 14.903 73.540  -21.789 1.00 31.58 ? 2397 HOH A O   1 
HETATM 8964 O  O   . HOH G 7 .    ? 16.202 74.779  -23.988 1.00 38.82 ? 2398 HOH A O   1 
HETATM 8965 O  O   . HOH G 7 .    ? 17.122 74.242  -28.714 1.00 46.14 ? 2399 HOH A O   1 
HETATM 8966 O  O   . HOH G 7 .    ? 18.156 76.260  -29.587 1.00 45.11 ? 2400 HOH A O   1 
HETATM 8967 O  O   . HOH G 7 .    ? 18.215 73.210  -31.231 1.00 36.27 ? 2401 HOH A O   1 
HETATM 8968 O  O   . HOH G 7 .    ? 18.572 70.552  -29.976 1.00 33.91 ? 2402 HOH A O   1 
HETATM 8969 O  O   . HOH G 7 .    ? 20.765 68.640  -31.543 1.00 32.84 ? 2403 HOH A O   1 
HETATM 8970 O  O   . HOH G 7 .    ? 16.894 69.979  -33.694 1.00 45.04 ? 2404 HOH A O   1 
HETATM 8971 O  O   . HOH G 7 .    ? 17.088 72.761  -34.070 1.00 37.57 ? 2405 HOH A O   1 
HETATM 8972 O  O   . HOH G 7 .    ? 30.207 74.716  -29.240 1.00 12.61 ? 2406 HOH A O   1 
HETATM 8973 O  O   . HOH G 7 .    ? 32.335 77.474  -29.697 1.00 13.41 ? 2407 HOH A O   1 
HETATM 8974 O  O   . HOH G 7 .    ? 28.891 81.682  -35.657 1.00 17.13 ? 2408 HOH A O   1 
HETATM 8975 O  O   . HOH G 7 .    ? 28.075 84.348  -35.548 1.00 15.55 ? 2409 HOH A O   1 
HETATM 8976 O  O   . HOH G 7 .    ? 23.240 88.503  -38.356 1.00 32.43 ? 2410 HOH A O   1 
HETATM 8977 O  O   . HOH G 7 .    ? 25.852 87.412  -42.960 1.00 39.56 ? 2411 HOH A O   1 
HETATM 8978 O  O   . HOH G 7 .    ? 28.346 87.584  -41.752 1.00 29.38 ? 2412 HOH A O   1 
HETATM 8979 O  O   . HOH G 7 .    ? 28.329 90.354  -42.770 1.00 26.78 ? 2413 HOH A O   1 
HETATM 8980 O  O   . HOH G 7 .    ? 32.545 88.893  -43.284 1.00 24.98 ? 2414 HOH A O   1 
HETATM 8981 O  O   . HOH G 7 .    ? 34.046 86.608  -43.746 1.00 42.47 ? 2415 HOH A O   1 
HETATM 8982 O  O   . HOH G 7 .    ? 38.921 86.314  -41.597 1.00 30.52 ? 2416 HOH A O   1 
HETATM 8983 O  O   . HOH G 7 .    ? 42.128 87.563  -41.039 1.00 14.39 ? 2417 HOH A O   1 
HETATM 8984 O  O   . HOH G 7 .    ? 43.648 88.202  -38.767 1.00 14.90 ? 2418 HOH A O   1 
HETATM 8985 O  O   . HOH G 7 .    ? 43.496 93.658  -37.740 1.00 19.62 ? 2419 HOH A O   1 
HETATM 8986 O  O   . HOH G 7 .    ? 41.244 94.691  -39.574 1.00 25.50 ? 2420 HOH A O   1 
HETATM 8987 O  O   . HOH G 7 .    ? 40.789 96.225  -37.509 1.00 24.17 ? 2421 HOH A O   1 
HETATM 8988 O  O   . HOH G 7 .    ? 43.069 97.978  -37.319 1.00 33.26 ? 2422 HOH A O   1 
HETATM 8989 O  O   . HOH G 7 .    ? 46.893 95.357  -37.059 1.00 38.25 ? 2423 HOH A O   1 
HETATM 8990 O  O   . HOH G 7 .    ? 48.699 97.694  -33.723 1.00 32.10 ? 2424 HOH A O   1 
HETATM 8991 O  O   . HOH G 7 .    ? 47.348 99.643  -32.731 1.00 33.08 ? 2425 HOH A O   1 
HETATM 8992 O  O   . HOH G 7 .    ? 42.095 101.031 -32.230 1.00 36.04 ? 2426 HOH A O   1 
HETATM 8993 O  O   . HOH G 7 .    ? 40.121 99.814  -32.019 1.00 29.57 ? 2427 HOH A O   1 
HETATM 8994 O  O   . HOH G 7 .    ? 37.738 97.348  -30.851 1.00 49.00 ? 2428 HOH A O   1 
HETATM 8995 O  O   . HOH G 7 .    ? 35.134 94.770  -32.373 1.00 26.37 ? 2429 HOH A O   1 
HETATM 8996 O  O   . HOH G 7 .    ? 35.993 93.454  -30.044 1.00 33.39 ? 2430 HOH A O   1 
HETATM 8997 O  O   . HOH G 7 .    ? 42.582 94.219  -30.337 1.00 39.95 ? 2431 HOH A O   1 
HETATM 8998 O  O   . HOH G 7 .    ? 44.362 95.558  -30.497 1.00 36.04 ? 2432 HOH A O   1 
HETATM 8999 O  O   . HOH G 7 .    ? 45.152 92.555  -25.520 1.00 29.71 ? 2433 HOH A O   1 
HETATM 9000 O  O   . HOH G 7 .    ? 45.039 89.753  -25.584 1.00 18.82 ? 2434 HOH A O   1 
HETATM 9001 O  O   . HOH G 7 .    ? 47.001 89.404  -23.810 1.00 29.32 ? 2435 HOH A O   1 
HETATM 9002 O  O   . HOH G 7 .    ? 49.340 91.699  -24.590 1.00 32.66 ? 2436 HOH A O   1 
HETATM 9003 O  O   . HOH G 7 .    ? 52.678 91.711  -23.599 1.00 31.04 ? 2437 HOH A O   1 
HETATM 9004 O  O   . HOH G 7 .    ? 54.847 89.966  -23.795 1.00 24.78 ? 2438 HOH A O   1 
HETATM 9005 O  O   . HOH G 7 .    ? 56.190 90.769  -25.891 1.00 22.96 ? 2439 HOH A O   1 
HETATM 9006 O  O   . HOH G 7 .    ? 57.621 93.210  -25.136 1.00 33.57 ? 2440 HOH A O   1 
HETATM 9007 O  O   . HOH G 7 .    ? 58.565 93.214  -27.340 1.00 36.11 ? 2441 HOH A O   1 
HETATM 9008 O  O   . HOH G 7 .    ? 60.326 91.749  -28.510 1.00 26.40 ? 2442 HOH A O   1 
HETATM 9009 O  O   . HOH G 7 .    ? 60.321 91.053  -31.323 1.00 29.30 ? 2443 HOH A O   1 
HETATM 9010 O  O   . HOH G 7 .    ? 59.620 90.906  -35.511 1.00 20.63 ? 2444 HOH A O   1 
HETATM 9011 O  O   . HOH G 7 .    ? 61.445 90.643  -37.162 1.00 30.68 ? 2445 HOH A O   1 
HETATM 9012 O  O   . HOH G 7 .    ? 60.447 92.977  -38.309 1.00 38.27 ? 2446 HOH A O   1 
HETATM 9013 O  O   . HOH G 7 .    ? 58.453 91.975  -42.598 1.00 51.13 ? 2447 HOH A O   1 
HETATM 9014 O  O   . HOH G 7 .    ? 56.616 89.666  -43.770 1.00 31.97 ? 2448 HOH A O   1 
HETATM 9015 O  O   . HOH G 7 .    ? 53.928 90.544  -43.135 1.00 36.90 ? 2449 HOH A O   1 
HETATM 9016 O  O   . HOH G 7 .    ? 53.679 92.851  -40.243 1.00 35.10 ? 2450 HOH A O   1 
HETATM 9017 O  O   . HOH G 7 .    ? 53.944 93.807  -33.029 1.00 43.09 ? 2451 HOH A O   1 
HETATM 9018 O  O   . HOH G 7 .    ? 56.450 92.687  -29.791 1.00 26.24 ? 2452 HOH A O   1 
HETATM 9019 O  O   . HOH G 7 .    ? 56.409 89.795  -21.333 1.00 31.65 ? 2453 HOH A O   1 
HETATM 9020 O  O   . HOH G 7 .    ? 56.930 87.495  -20.168 1.00 27.41 ? 2454 HOH A O   1 
HETATM 9021 O  O   . HOH G 7 .    ? 53.157 86.658  -21.420 1.00 24.26 ? 2455 HOH A O   1 
HETATM 9022 O  O   . HOH G 7 .    ? 49.011 84.080  -19.588 1.00 36.96 ? 2456 HOH A O   1 
HETATM 9023 O  O   . HOH G 7 .    ? 47.103 83.106  -21.020 1.00 40.11 ? 2457 HOH A O   1 
HETATM 9024 O  O   . HOH G 7 .    ? 47.266 81.324  -17.192 1.00 30.37 ? 2458 HOH A O   1 
HETATM 9025 O  O   . HOH G 7 .    ? 47.444 79.488  -18.425 1.00 24.98 ? 2459 HOH A O   1 
HETATM 9026 O  O   . HOH G 7 .    ? 50.491 79.026  -15.814 1.00 25.90 ? 2460 HOH A O   1 
HETATM 9027 O  O   . HOH G 7 .    ? 52.503 78.864  -17.524 1.00 20.49 ? 2461 HOH A O   1 
HETATM 9028 O  O   . HOH G 7 .    ? 60.008 83.879  -16.766 1.00 34.16 ? 2462 HOH A O   1 
HETATM 9029 O  O   . HOH G 7 .    ? 61.128 77.293  -13.000 1.00 19.54 ? 2463 HOH A O   1 
HETATM 9030 O  O   . HOH G 7 .    ? 61.806 76.242  -10.662 1.00 16.78 ? 2464 HOH A O   1 
HETATM 9031 O  O   . HOH G 7 .    ? 59.537 76.389  -9.025  1.00 14.29 ? 2465 HOH A O   1 
HETATM 9032 O  O   . HOH G 7 .    ? 59.232 77.008  -4.339  1.00 28.16 ? 2466 HOH A O   1 
HETATM 9033 O  O   . HOH G 7 .    ? 57.270 75.383  -3.077  1.00 31.39 ? 2467 HOH A O   1 
HETATM 9034 O  O   . HOH G 7 .    ? 46.019 70.880  0.021   1.00 13.18 ? 2468 HOH A O   1 
HETATM 9035 O  O   . HOH G 7 .    ? 43.482 73.068  5.699   1.00 11.45 ? 2469 HOH A O   1 
HETATM 9036 O  O   . HOH G 7 .    ? 46.720 74.365  7.708   1.00 10.74 ? 2470 HOH A O   1 
HETATM 9037 O  O   . HOH G 7 .    ? 46.063 79.486  4.869   1.00 23.10 ? 2471 HOH A O   1 
HETATM 9038 O  O   . HOH G 7 .    ? 43.439 80.596  5.150   1.00 21.05 ? 2472 HOH A O   1 
HETATM 9039 O  O   . HOH G 7 .    ? 36.177 80.897  6.318   1.00 16.02 ? 2473 HOH A O   1 
HETATM 9040 O  O   . HOH G 7 .    ? 32.127 80.403  7.423   1.00 26.56 ? 2474 HOH A O   1 
HETATM 9041 O  O   . HOH G 7 .    ? 30.259 82.336  7.311   1.00 36.04 ? 2475 HOH A O   1 
HETATM 9042 O  O   . HOH G 7 .    ? 29.854 75.574  10.781  1.00 23.52 ? 2476 HOH A O   1 
HETATM 9043 O  O   . HOH G 7 .    ? 26.598 74.772  11.043  1.00 24.67 ? 2477 HOH A O   1 
HETATM 9044 O  O   . HOH G 7 .    ? 27.650 73.123  13.085  1.00 39.54 ? 2478 HOH A O   1 
HETATM 9045 O  O   . HOH G 7 .    ? 28.349 71.958  15.222  1.00 39.93 ? 2479 HOH A O   1 
HETATM 9046 O  O   . HOH G 7 .    ? 30.159 72.467  12.224  1.00 26.77 ? 2480 HOH A O   1 
HETATM 9047 O  O   . HOH G 7 .    ? 31.967 71.298  13.552  1.00 24.58 ? 2481 HOH A O   1 
HETATM 9048 O  O   . HOH G 7 .    ? 34.635 70.324  13.060  1.00 11.98 ? 2482 HOH A O   1 
HETATM 9049 O  O   . HOH G 7 .    ? 35.047 71.215  15.523  1.00 25.04 ? 2483 HOH A O   1 
HETATM 9050 O  O   . HOH G 7 .    ? 36.766 70.346  16.625  1.00 35.86 ? 2484 HOH A O   1 
HETATM 9051 O  O   . HOH G 7 .    ? 36.085 70.299  19.242  1.00 39.50 ? 2485 HOH A O   1 
HETATM 9052 O  O   . HOH G 7 .    ? 34.164 68.904  19.588  1.00 40.29 ? 2486 HOH A O   1 
HETATM 9053 O  O   . HOH G 7 .    ? 32.648 70.415  17.890  1.00 34.01 ? 2487 HOH A O   1 
HETATM 9054 O  O   . HOH G 7 .    ? 33.720 68.464  16.863  1.00 39.65 ? 2488 HOH A O   1 
HETATM 9055 O  O   . HOH G 7 .    ? 31.853 65.288  18.622  1.00 13.13 ? 2489 HOH A O   1 
HETATM 9056 O  O   . HOH G 7 .    ? 29.717 65.849  16.905  1.00 27.39 ? 2490 HOH A O   1 
HETATM 9057 O  O   . HOH G 7 .    ? 28.206 67.623  16.029  1.00 36.90 ? 2491 HOH A O   1 
HETATM 9058 O  O   . HOH G 7 .    ? 25.771 66.062  17.474  1.00 26.76 ? 2492 HOH A O   1 
HETATM 9059 O  O   . HOH G 7 .    ? 23.512 66.140  18.666  1.00 35.19 ? 2493 HOH A O   1 
HETATM 9060 O  O   . HOH G 7 .    ? 23.083 63.733  18.110  1.00 38.01 ? 2494 HOH A O   1 
HETATM 9061 O  O   . HOH G 7 .    ? 22.790 62.447  16.200  1.00 26.78 ? 2495 HOH A O   1 
HETATM 9062 O  O   . HOH G 7 .    ? 21.192 63.507  14.662  1.00 31.94 ? 2496 HOH A O   1 
HETATM 9063 O  O   . HOH G 7 .    ? 24.416 63.105  11.405  1.00 37.11 ? 2497 HOH A O   1 
HETATM 9064 O  O   . HOH G 7 .    ? 26.390 62.777  12.792  1.00 28.11 ? 2498 HOH A O   1 
HETATM 9065 O  O   . HOH G 7 .    ? 26.956 63.755  9.847   1.00 19.47 ? 2499 HOH A O   1 
HETATM 9066 O  O   . HOH G 7 .    ? 25.622 65.417  8.405   1.00 19.32 ? 2500 HOH A O   1 
HETATM 9067 O  O   . HOH G 7 .    ? 24.176 63.308  7.465   1.00 10.76 ? 2501 HOH A O   1 
HETATM 9068 O  O   . HOH G 7 .    ? 24.676 61.233  9.193   1.00 14.78 ? 2502 HOH A O   1 
HETATM 9069 O  O   . HOH G 7 .    ? 27.082 59.263  8.471   1.00 17.63 ? 2503 HOH A O   1 
HETATM 9070 O  O   . HOH G 7 .    ? 23.813 57.989  6.320   1.00 10.69 ? 2504 HOH A O   1 
HETATM 9071 O  O   . HOH G 7 .    ? 21.654 56.969  5.037   1.00 10.17 ? 2505 HOH A O   1 
HETATM 9072 O  O   . HOH G 7 .    ? 20.046 55.867  7.160   1.00 10.96 ? 2506 HOH A O   1 
HETATM 9073 O  O   . HOH G 7 .    ? 19.273 53.402  8.206   1.00 10.79 ? 2507 HOH A O   1 
HETATM 9074 O  O   . HOH G 7 .    ? 17.568 52.655  6.374   1.00 10.62 ? 2508 HOH A O   1 
HETATM 9075 O  O   . HOH G 7 .    ? 17.051 56.144  10.315  1.00 11.23 ? 2509 HOH A O   1 
HETATM 9076 O  O   . HOH G 7 .    ? 19.309 55.086  11.511  1.00 11.22 ? 2510 HOH A O   1 
HETATM 9077 O  O   . HOH G 7 .    ? 18.365 54.832  14.177  1.00 11.35 ? 2511 HOH A O   1 
HETATM 9078 O  O   . HOH G 7 .    ? 20.109 54.655  16.232  1.00 11.43 ? 2512 HOH A O   1 
HETATM 9079 O  O   . HOH G 7 .    ? 16.741 56.938  12.982  1.00 12.61 ? 2513 HOH A O   1 
HETATM 9080 O  O   . HOH G 7 .    ? 15.529 60.235  15.502  1.00 13.62 ? 2514 HOH A O   1 
HETATM 9081 O  O   . HOH G 7 .    ? 13.810 62.224  14.707  1.00 23.92 ? 2515 HOH A O   1 
HETATM 9082 O  O   . HOH G 7 .    ? 13.233 62.737  11.887  1.00 26.89 ? 2516 HOH A O   1 
HETATM 9083 O  O   . HOH G 7 .    ? 13.979 58.136  16.395  1.00 14.60 ? 2517 HOH A O   1 
HETATM 9084 O  O   . HOH G 7 .    ? 13.942 57.586  19.051  1.00 18.51 ? 2518 HOH A O   1 
HETATM 9085 O  O   . HOH G 7 .    ? 11.657 58.509  19.996  1.00 30.13 ? 2519 HOH A O   1 
HETATM 9086 O  O   . HOH G 7 .    ? 10.860 57.141  21.734  1.00 40.19 ? 2520 HOH A O   1 
HETATM 9087 O  O   . HOH G 7 .    ? 12.342 55.197  22.541  1.00 25.11 ? 2521 HOH A O   1 
HETATM 9088 O  O   . HOH G 7 .    ? 12.808 54.982  25.292  1.00 29.84 ? 2522 HOH A O   1 
HETATM 9089 O  O   . HOH G 7 .    ? 13.322 52.412  25.942  1.00 36.17 ? 2523 HOH A O   1 
HETATM 9090 O  O   . HOH G 7 .    ? 14.153 50.402  24.286  1.00 19.60 ? 2524 HOH A O   1 
HETATM 9091 O  O   . HOH G 7 .    ? 13.498 51.467  21.821  1.00 17.80 ? 2525 HOH A O   1 
HETATM 9092 O  O   . HOH G 7 .    ? 10.827 51.315  21.446  1.00 24.20 ? 2526 HOH A O   1 
HETATM 9093 O  O   . HOH G 7 .    ? 10.292 50.604  18.953  1.00 21.50 ? 2527 HOH A O   1 
HETATM 9094 O  O   . HOH G 7 .    ? 9.421  52.272  16.952  1.00 19.03 ? 2528 HOH A O   1 
HETATM 9095 O  O   . HOH G 7 .    ? 7.552  54.514  17.380  1.00 33.18 ? 2529 HOH A O   1 
HETATM 9096 O  O   . HOH G 7 .    ? 8.739  56.921  16.211  1.00 48.17 ? 2530 HOH A O   1 
HETATM 9097 O  O   . HOH G 7 .    ? 11.792 51.406  14.410  1.00 14.27 ? 2531 HOH A O   1 
HETATM 9098 O  O   . HOH G 7 .    ? 14.018 48.983  15.417  1.00 14.40 ? 2532 HOH A O   1 
HETATM 9099 O  O   . HOH G 7 .    ? 12.587 49.401  17.871  1.00 19.13 ? 2533 HOH A O   1 
HETATM 9100 O  O   . HOH G 7 .    ? 14.392 49.653  19.957  1.00 16.17 ? 2534 HOH A O   1 
HETATM 9101 O  O   . HOH G 7 .    ? 11.493 46.773  17.954  1.00 20.13 ? 2535 HOH A O   1 
HETATM 9102 O  O   . HOH G 7 .    ? 6.249  46.496  16.306  1.00 36.78 ? 2536 HOH A O   1 
HETATM 9103 O  O   . HOH G 7 .    ? 12.061 41.391  20.067  1.00 30.64 ? 2537 HOH A O   1 
HETATM 9104 O  O   . HOH G 7 .    ? 12.993 43.970  22.869  1.00 37.66 ? 2538 HOH A O   1 
HETATM 9105 O  O   . HOH G 7 .    ? 13.933 45.073  27.253  1.00 30.80 ? 2539 HOH A O   1 
HETATM 9106 O  O   . HOH G 7 .    ? 14.505 47.357  27.037  1.00 40.79 ? 2540 HOH A O   1 
HETATM 9107 O  O   . HOH G 7 .    ? 16.543 49.000  24.145  1.00 15.27 ? 2541 HOH A O   1 
HETATM 9108 O  O   . HOH G 7 .    ? 18.260 43.093  27.479  1.00 31.09 ? 2542 HOH A O   1 
HETATM 9109 O  O   . HOH G 7 .    ? 18.054 41.834  25.442  1.00 28.18 ? 2543 HOH A O   1 
HETATM 9110 O  O   . HOH G 7 .    ? 19.182 39.826  26.649  1.00 31.42 ? 2544 HOH A O   1 
HETATM 9111 O  O   . HOH G 7 .    ? 19.943 35.673  25.750  1.00 29.71 ? 2545 HOH A O   1 
HETATM 9112 O  O   . HOH G 7 .    ? 22.682 31.366  29.773  1.00 29.56 ? 2546 HOH A O   1 
HETATM 9113 O  O   . HOH G 7 .    ? 20.902 31.715  31.638  1.00 35.16 ? 2547 HOH A O   1 
HETATM 9114 O  O   . HOH G 7 .    ? 21.695 29.273  28.305  1.00 34.06 ? 2548 HOH A O   1 
HETATM 9115 O  O   . HOH G 7 .    ? 26.236 32.807  28.967  1.00 25.09 ? 2549 HOH A O   1 
HETATM 9116 O  O   . HOH G 7 .    ? 27.367 35.057  29.583  1.00 22.82 ? 2550 HOH A O   1 
HETATM 9117 O  O   . HOH G 7 .    ? 26.310 37.475  29.542  1.00 18.21 ? 2551 HOH A O   1 
HETATM 9118 O  O   . HOH G 7 .    ? 30.284 36.653  29.125  1.00 22.67 ? 2552 HOH A O   1 
HETATM 9119 O  O   . HOH G 7 .    ? 28.524 35.033  32.406  1.00 36.11 ? 2553 HOH A O   1 
HETATM 9120 O  O   . HOH G 7 .    ? 24.812 34.685  36.000  1.00 35.58 ? 2554 HOH A O   1 
HETATM 9121 O  O   . HOH G 7 .    ? 22.200 35.170  35.073  1.00 34.01 ? 2555 HOH A O   1 
HETATM 9122 O  O   . HOH G 7 .    ? 21.234 41.751  35.300  1.00 27.01 ? 2556 HOH A O   1 
HETATM 9123 O  O   . HOH G 7 .    ? 19.855 43.306  33.925  1.00 23.60 ? 2557 HOH A O   1 
HETATM 9124 O  O   . HOH G 7 .    ? 17.301 41.900  32.260  1.00 35.50 ? 2558 HOH A O   1 
HETATM 9125 O  O   . HOH G 7 .    ? 14.702 47.067  32.372  1.00 26.88 ? 2559 HOH A O   1 
HETATM 9126 O  O   . HOH G 7 .    ? 12.382 47.656  31.449  1.00 30.52 ? 2560 HOH A O   1 
HETATM 9127 O  O   . HOH G 7 .    ? 17.795 52.829  35.927  1.00 33.29 ? 2561 HOH A O   1 
HETATM 9128 O  O   . HOH G 7 .    ? 17.817 50.734  38.421  1.00 41.90 ? 2562 HOH A O   1 
HETATM 9129 O  O   . HOH G 7 .    ? 19.025 48.625  37.820  1.00 19.94 ? 2563 HOH A O   1 
HETATM 9130 O  O   . HOH G 7 .    ? 21.218 47.518  39.136  1.00 20.81 ? 2564 HOH A O   1 
HETATM 9131 O  O   . HOH G 7 .    ? 28.195 49.545  38.514  1.00 25.90 ? 2565 HOH A O   1 
HETATM 9132 O  O   . HOH G 7 .    ? 29.189 47.124  37.173  1.00 22.79 ? 2566 HOH A O   1 
HETATM 9133 O  O   . HOH G 7 .    ? 31.726 47.507  38.014  1.00 46.15 ? 2567 HOH A O   1 
HETATM 9134 O  O   . HOH G 7 .    ? 34.171 48.181  36.487  1.00 38.10 ? 2568 HOH A O   1 
HETATM 9135 O  O   . HOH G 7 .    ? 34.815 51.300  36.028  1.00 33.70 ? 2569 HOH A O   1 
HETATM 9136 O  O   . HOH G 7 .    ? 39.692 49.772  36.172  1.00 30.09 ? 2570 HOH A O   1 
HETATM 9137 O  O   . HOH G 7 .    ? 40.091 52.705  36.267  1.00 28.23 ? 2571 HOH A O   1 
HETATM 9138 O  O   . HOH G 7 .    ? 42.669 53.415  35.552  1.00 21.72 ? 2572 HOH A O   1 
HETATM 9139 O  O   . HOH G 7 .    ? 44.643 55.341  36.088  1.00 38.83 ? 2573 HOH A O   1 
HETATM 9140 O  O   . HOH G 7 .    ? 43.568 56.765  33.474  1.00 35.03 ? 2574 HOH A O   1 
HETATM 9141 O  O   . HOH G 7 .    ? 41.908 58.270  34.625  1.00 28.96 ? 2575 HOH A O   1 
HETATM 9142 O  O   . HOH G 7 .    ? 42.000 61.843  33.808  1.00 37.01 ? 2576 HOH A O   1 
HETATM 9143 O  O   . HOH G 7 .    ? 37.775 62.428  35.362  1.00 30.89 ? 2577 HOH A O   1 
HETATM 9144 O  O   . HOH G 7 .    ? 35.223 62.482  33.959  1.00 25.09 ? 2578 HOH A O   1 
HETATM 9145 O  O   . HOH G 7 .    ? 34.001 59.868  34.995  1.00 40.08 ? 2579 HOH A O   1 
HETATM 9146 O  O   . HOH G 7 .    ? 30.111 59.445  34.998  1.00 36.44 ? 2580 HOH A O   1 
HETATM 9147 O  O   . HOH G 7 .    ? 31.485 57.596  37.372  1.00 26.40 ? 2581 HOH A O   1 
HETATM 9148 O  O   . HOH G 7 .    ? 28.950 55.309  39.982  1.00 29.83 ? 2582 HOH A O   1 
HETATM 9149 O  O   . HOH G 7 .    ? 26.665 57.657  40.331  1.00 40.00 ? 2583 HOH A O   1 
HETATM 9150 O  O   . HOH G 7 .    ? 24.332 57.389  38.782  1.00 29.88 ? 2584 HOH A O   1 
HETATM 9151 O  O   . HOH G 7 .    ? 21.243 58.314  37.818  1.00 50.65 ? 2585 HOH A O   1 
HETATM 9152 O  O   . HOH G 7 .    ? 21.629 55.668  40.218  1.00 23.51 ? 2586 HOH A O   1 
HETATM 9153 O  O   . HOH G 7 .    ? 21.003 54.305  47.206  1.00 37.22 ? 2587 HOH A O   1 
HETATM 9154 O  O   . HOH G 7 .    ? 21.207 51.831  47.736  1.00 25.68 ? 2588 HOH A O   1 
HETATM 9155 O  O   . HOH G 7 .    ? 28.197 47.755  46.174  1.00 42.74 ? 2589 HOH A O   1 
HETATM 9156 O  O   . HOH G 7 .    ? 27.771 52.163  42.483  1.00 34.45 ? 2590 HOH A O   1 
HETATM 9157 O  O   . HOH G 7 .    ? 30.501 51.769  39.668  1.00 44.09 ? 2591 HOH A O   1 
HETATM 9158 O  O   . HOH G 7 .    ? 28.262 44.553  38.292  1.00 27.43 ? 2592 HOH A O   1 
HETATM 9159 O  O   . HOH G 7 .    ? 31.110 44.043  40.902  1.00 35.92 ? 2593 HOH A O   1 
HETATM 9160 O  O   . HOH G 7 .    ? 34.873 45.955  33.341  1.00 17.18 ? 2594 HOH A O   1 
HETATM 9161 O  O   . HOH G 7 .    ? 36.064 45.272  30.917  1.00 16.02 ? 2595 HOH A O   1 
HETATM 9162 O  O   . HOH G 7 .    ? 37.545 47.263  29.727  1.00 17.75 ? 2596 HOH A O   1 
HETATM 9163 O  O   . HOH G 7 .    ? 39.377 49.310  30.111  1.00 18.68 ? 2597 HOH A O   1 
HETATM 9164 O  O   . HOH G 7 .    ? 42.084 48.732  31.277  1.00 20.02 ? 2598 HOH A O   1 
HETATM 9165 O  O   . HOH G 7 .    ? 41.209 50.462  33.159  1.00 18.37 ? 2599 HOH A O   1 
HETATM 9166 O  O   . HOH G 7 .    ? 40.640 57.217  30.996  1.00 22.13 ? 2600 HOH A O   1 
HETATM 9167 O  O   . HOH G 7 .    ? 45.905 58.226  32.943  1.00 38.84 ? 2601 HOH A O   1 
HETATM 9168 O  O   . HOH G 7 .    ? 46.919 63.445  29.741  1.00 41.54 ? 2602 HOH A O   1 
HETATM 9169 O  O   . HOH G 7 .    ? 47.910 66.045  26.870  1.00 26.60 ? 2603 HOH A O   1 
HETATM 9170 O  O   . HOH G 7 .    ? 46.400 68.523  26.460  1.00 29.97 ? 2604 HOH A O   1 
HETATM 9171 O  O   . HOH G 7 .    ? 42.048 67.494  29.292  1.00 23.81 ? 2605 HOH A O   1 
HETATM 9172 O  O   . HOH G 7 .    ? 39.816 67.094  31.343  1.00 21.69 ? 2606 HOH A O   1 
HETATM 9173 O  O   . HOH G 7 .    ? 36.709 66.849  25.568  1.00 20.99 ? 2607 HOH A O   1 
HETATM 9174 O  O   . HOH G 7 .    ? 35.734 68.480  23.175  1.00 26.85 ? 2608 HOH A O   1 
HETATM 9175 O  O   . HOH G 7 .    ? 35.831 65.603  22.205  1.00 20.87 ? 2609 HOH A O   1 
HETATM 9176 O  O   . HOH G 7 .    ? 37.097 68.194  20.338  1.00 21.75 ? 2610 HOH A O   1 
HETATM 9177 O  O   . HOH G 7 .    ? 37.081 72.300  20.163  1.00 36.91 ? 2611 HOH A O   1 
HETATM 9178 O  O   . HOH G 7 .    ? 35.452 71.590  22.050  1.00 42.28 ? 2612 HOH A O   1 
HETATM 9179 O  O   . HOH G 7 .    ? 33.026 73.024  21.194  1.00 33.44 ? 2613 HOH A O   1 
HETATM 9180 O  O   . HOH G 7 .    ? 31.935 75.487  21.147  1.00 33.19 ? 2614 HOH A O   1 
HETATM 9181 O  O   . HOH G 7 .    ? 29.461 75.208  22.245  1.00 19.58 ? 2615 HOH A O   1 
HETATM 9182 O  O   . HOH G 7 .    ? 28.709 72.570  22.516  1.00 17.68 ? 2616 HOH A O   1 
HETATM 9183 O  O   . HOH G 7 .    ? 27.370 71.839  20.442  1.00 39.08 ? 2617 HOH A O   1 
HETATM 9184 O  O   . HOH G 7 .    ? 28.035 69.681  18.907  1.00 37.84 ? 2618 HOH A O   1 
HETATM 9185 O  O   . HOH G 7 .    ? 30.675 69.510  19.865  1.00 23.22 ? 2619 HOH A O   1 
HETATM 9186 O  O   . HOH G 7 .    ? 30.972 71.103  21.811  1.00 25.55 ? 2620 HOH A O   1 
HETATM 9187 O  O   . HOH G 7 .    ? 32.497 69.555  24.333  1.00 20.06 ? 2621 HOH A O   1 
HETATM 9188 O  O   . HOH G 7 .    ? 31.707 67.058  20.873  1.00 23.55 ? 2622 HOH A O   1 
HETATM 9189 O  O   . HOH G 7 .    ? 28.762 65.316  19.686  1.00 17.65 ? 2623 HOH A O   1 
HETATM 9190 O  O   . HOH G 7 .    ? 26.500 66.983  19.864  1.00 31.57 ? 2624 HOH A O   1 
HETATM 9191 O  O   . HOH G 7 .    ? 24.709 68.384  21.811  1.00 20.53 ? 2625 HOH A O   1 
HETATM 9192 O  O   . HOH G 7 .    ? 22.437 68.194  20.416  1.00 25.07 ? 2626 HOH A O   1 
HETATM 9193 O  O   . HOH G 7 .    ? 20.422 68.247  22.150  1.00 23.53 ? 2627 HOH A O   1 
HETATM 9194 O  O   . HOH G 7 .    ? 17.469 67.329  25.548  1.00 43.22 ? 2628 HOH A O   1 
HETATM 9195 O  O   . HOH G 7 .    ? 17.976 66.190  27.884  1.00 26.93 ? 2629 HOH A O   1 
HETATM 9196 O  O   . HOH G 7 .    ? 16.427 66.056  29.519  1.00 32.35 ? 2630 HOH A O   1 
HETATM 9197 O  O   . HOH G 7 .    ? 20.670 65.242  27.354  1.00 21.12 ? 2631 HOH A O   1 
HETATM 9198 O  O   . HOH G 7 .    ? 22.574 65.953  29.239  1.00 26.71 ? 2632 HOH A O   1 
HETATM 9199 O  O   . HOH G 7 .    ? 22.239 65.727  32.281  1.00 27.93 ? 2633 HOH A O   1 
HETATM 9200 O  O   . HOH G 7 .    ? 22.268 62.883  33.590  1.00 30.81 ? 2634 HOH A O   1 
HETATM 9201 O  O   . HOH G 7 .    ? 24.331 60.955  36.122  1.00 33.68 ? 2635 HOH A O   1 
HETATM 9202 O  O   . HOH G 7 .    ? 23.178 56.028  30.828  1.00 16.69 ? 2636 HOH A O   1 
HETATM 9203 O  O   . HOH G 7 .    ? 18.400 59.605  31.738  1.00 33.79 ? 2637 HOH A O   1 
HETATM 9204 O  O   . HOH G 7 .    ? 14.653 55.751  27.361  1.00 26.48 ? 2638 HOH A O   1 
HETATM 9205 O  O   . HOH G 7 .    ? 18.139 60.602  24.407  1.00 17.03 ? 2639 HOH A O   1 
HETATM 9206 O  O   . HOH G 7 .    ? 11.787 62.156  23.001  1.00 35.95 ? 2640 HOH A O   1 
HETATM 9207 O  O   . HOH G 7 .    ? 11.250 69.548  26.507  1.00 29.42 ? 2641 HOH A O   1 
HETATM 9208 O  O   . HOH G 7 .    ? 14.060 69.562  26.759  1.00 21.18 ? 2642 HOH A O   1 
HETATM 9209 O  O   . HOH G 7 .    ? 24.844 71.354  22.814  1.00 35.01 ? 2643 HOH A O   1 
HETATM 9210 O  O   . HOH G 7 .    ? 27.728 67.724  28.228  1.00 19.73 ? 2644 HOH A O   1 
HETATM 9211 O  O   . HOH G 7 .    ? 28.054 65.402  30.858  1.00 48.65 ? 2645 HOH A O   1 
HETATM 9212 O  O   . HOH G 7 .    ? 28.329 66.820  33.232  1.00 36.44 ? 2646 HOH A O   1 
HETATM 9213 O  O   . HOH G 7 .    ? 27.163 72.358  34.061  1.00 30.77 ? 2647 HOH A O   1 
HETATM 9214 O  O   . HOH G 7 .    ? 29.722 72.481  34.383  1.00 22.75 ? 2648 HOH A O   1 
HETATM 9215 O  O   . HOH G 7 .    ? 29.578 73.808  36.635  1.00 35.24 ? 2649 HOH A O   1 
HETATM 9216 O  O   . HOH G 7 .    ? 35.188 75.913  20.299  1.00 42.21 ? 2650 HOH A O   1 
HETATM 9217 O  O   . HOH G 7 .    ? 35.808 74.071  18.405  1.00 41.34 ? 2651 HOH A O   1 
HETATM 9218 O  O   . HOH G 7 .    ? 36.191 73.676  15.683  1.00 29.08 ? 2652 HOH A O   1 
HETATM 9219 O  O   . HOH G 7 .    ? 35.563 76.291  14.935  1.00 31.95 ? 2653 HOH A O   1 
HETATM 9220 O  O   . HOH G 7 .    ? 34.813 77.485  12.338  1.00 21.49 ? 2654 HOH A O   1 
HETATM 9221 O  O   . HOH G 7 .    ? 35.201 80.173  12.726  1.00 34.86 ? 2655 HOH A O   1 
HETATM 9222 O  O   . HOH G 7 .    ? 33.546 80.975  15.094  1.00 38.72 ? 2656 HOH A O   1 
HETATM 9223 O  O   . HOH G 7 .    ? 39.275 80.202  12.205  1.00 36.94 ? 2657 HOH A O   1 
HETATM 9224 O  O   . HOH G 7 .    ? 38.572 76.904  17.928  1.00 33.99 ? 2658 HOH A O   1 
HETATM 9225 O  O   . HOH G 7 .    ? 33.075 73.180  18.071  1.00 37.20 ? 2659 HOH A O   1 
HETATM 9226 O  O   . HOH G 7 .    ? 34.319 67.669  12.422  1.00 9.57  ? 2660 HOH A O   1 
HETATM 9227 O  O   . HOH G 7 .    ? 38.682 62.276  8.409   1.00 9.91  ? 2661 HOH A O   1 
HETATM 9228 O  O   . HOH G 7 .    ? 40.151 62.698  5.978   1.00 8.51  ? 2662 HOH A O   1 
HETATM 9229 O  O   . HOH G 7 .    ? 40.087 56.194  5.731   1.00 11.76 ? 2663 HOH A O   1 
HETATM 9230 O  O   . HOH G 7 .    ? 39.664 55.597  2.986   1.00 12.89 ? 2664 HOH A O   1 
HETATM 9231 O  O   . HOH G 7 .    ? 37.532 56.911  1.666   1.00 8.63  ? 2665 HOH A O   1 
HETATM 9232 O  O   . HOH G 7 .    ? 38.812 52.928  2.149   1.00 24.73 ? 2666 HOH A O   1 
HETATM 9233 O  O   . HOH G 7 .    ? 35.913 52.957  1.319   1.00 9.67  ? 2667 HOH A O   1 
HETATM 9234 O  O   . HOH G 7 .    ? 34.216 52.313  -0.974  1.00 8.15  ? 2668 HOH A O   1 
HETATM 9235 O  O   . HOH G 7 .    ? 36.710 51.495  3.797   1.00 11.43 ? 2669 HOH A O   1 
HETATM 9236 O  O   . HOH G 7 .    ? 41.930 55.068  1.353   1.00 22.38 ? 2670 HOH A O   1 
HETATM 9237 O  O   . HOH G 7 .    ? 42.746 56.473  2.876   1.00 17.47 ? 2671 HOH A O   1 
HETATM 9238 O  O   . HOH G 7 .    ? 42.930 56.709  6.173   1.00 10.39 ? 2672 HOH A O   1 
HETATM 9239 O  O   . HOH G 7 .    ? 37.761 58.976  11.025  1.00 8.68  ? 2673 HOH A O   1 
HETATM 9240 O  O   . HOH G 7 .    ? 36.904 57.633  13.315  1.00 8.35  ? 2674 HOH A O   1 
HETATM 9241 O  O   . HOH G 7 .    ? 39.344 57.291  14.766  1.00 8.76  ? 2675 HOH A O   1 
HETATM 9242 O  O   . HOH G 7 .    ? 41.250 58.929  13.500  1.00 9.13  ? 2676 HOH A O   1 
HETATM 9243 O  O   . HOH G 7 .    ? 43.018 48.032  11.251  1.00 11.49 ? 2677 HOH A O   1 
HETATM 9244 O  O   . HOH G 7 .    ? 44.410 45.968  10.060  1.00 13.13 ? 2678 HOH A O   1 
HETATM 9245 O  O   . HOH G 7 .    ? 41.639 43.165  7.940   1.00 16.54 ? 2679 HOH A O   1 
HETATM 9246 O  O   . HOH G 7 .    ? 44.857 40.263  13.296  1.00 33.69 ? 2680 HOH A O   1 
HETATM 9247 O  O   . HOH G 7 .    ? 41.882 39.187  16.652  1.00 26.93 ? 2681 HOH A O   1 
HETATM 9248 O  O   . HOH G 7 .    ? 39.241 38.895  17.302  1.00 16.79 ? 2682 HOH A O   1 
HETATM 9249 O  O   . HOH G 7 .    ? 39.744 39.671  20.090  1.00 26.95 ? 2683 HOH A O   1 
HETATM 9250 O  O   . HOH G 7 .    ? 38.007 38.304  21.840  1.00 37.57 ? 2684 HOH A O   1 
HETATM 9251 O  O   . HOH G 7 .    ? 37.229 37.653  25.182  1.00 41.63 ? 2685 HOH A O   1 
HETATM 9252 O  O   . HOH G 7 .    ? 37.646 40.432  26.587  1.00 31.57 ? 2686 HOH A O   1 
HETATM 9253 O  O   . HOH G 7 .    ? 39.579 41.452  25.598  1.00 37.80 ? 2687 HOH A O   1 
HETATM 9254 O  O   . HOH G 7 .    ? 39.249 43.585  26.838  1.00 30.61 ? 2688 HOH A O   1 
HETATM 9255 O  O   . HOH G 7 .    ? 39.956 45.266  25.458  1.00 28.61 ? 2689 HOH A O   1 
HETATM 9256 O  O   . HOH G 7 .    ? 37.168 45.625  27.454  1.00 13.41 ? 2690 HOH A O   1 
HETATM 9257 O  O   . HOH G 7 .    ? 35.253 43.746  28.725  1.00 13.53 ? 2691 HOH A O   1 
HETATM 9258 O  O   . HOH G 7 .    ? 39.081 42.990  22.727  1.00 25.85 ? 2692 HOH A O   1 
HETATM 9259 O  O   . HOH G 7 .    ? 34.270 34.337  16.269  1.00 19.16 ? 2693 HOH A O   1 
HETATM 9260 O  O   . HOH G 7 .    ? 31.873 33.565  17.236  1.00 31.58 ? 2694 HOH A O   1 
HETATM 9261 O  O   . HOH G 7 .    ? 30.570 33.950  21.067  1.00 42.30 ? 2695 HOH A O   1 
HETATM 9262 O  O   . HOH G 7 .    ? 29.478 31.547  21.972  1.00 31.42 ? 2696 HOH A O   1 
HETATM 9263 O  O   . HOH G 7 .    ? 24.283 34.294  15.674  1.00 29.25 ? 2697 HOH A O   1 
HETATM 9264 O  O   . HOH G 7 .    ? 25.283 33.236  13.396  1.00 30.67 ? 2698 HOH A O   1 
HETATM 9265 O  O   . HOH G 7 .    ? 24.369 33.072  9.647   1.00 27.84 ? 2699 HOH A O   1 
HETATM 9266 O  O   . HOH G 7 .    ? 24.734 32.862  6.559   1.00 23.44 ? 2700 HOH A O   1 
HETATM 9267 O  O   . HOH G 7 .    ? 30.624 29.570  5.988   1.00 41.77 ? 2701 HOH A O   1 
HETATM 9268 O  O   . HOH G 7 .    ? 31.174 33.417  2.879   1.00 23.33 ? 2702 HOH A O   1 
HETATM 9269 O  O   . HOH G 7 .    ? 25.886 39.654  5.279   1.00 10.21 ? 2703 HOH A O   1 
HETATM 9270 O  O   . HOH G 7 .    ? 26.292 39.985  8.023   1.00 10.71 ? 2704 HOH A O   1 
HETATM 9271 O  O   . HOH G 7 .    ? 24.030 41.849  6.975   1.00 11.06 ? 2705 HOH A O   1 
HETATM 9272 O  O   . HOH G 7 .    ? 28.174 39.565  11.328  1.00 12.58 ? 2706 HOH A O   1 
HETATM 9273 O  O   . HOH G 7 .    ? 27.256 41.271  13.344  1.00 13.04 ? 2707 HOH A O   1 
HETATM 9274 O  O   . HOH G 7 .    ? 28.287 43.789  13.219  1.00 9.20  ? 2708 HOH A O   1 
HETATM 9275 O  O   . HOH G 7 .    ? 27.196 46.298  13.699  1.00 13.04 ? 2709 HOH A O   1 
HETATM 9276 O  O   . HOH G 7 .    ? 27.887 48.454  12.095  1.00 13.76 ? 2710 HOH A O   1 
HETATM 9277 O  O   . HOH G 7 .    ? 27.565 50.848  13.236  1.00 17.59 ? 2711 HOH A O   1 
HETATM 9278 O  O   . HOH G 7 .    ? 25.651 52.133  12.953  1.00 21.14 ? 2712 HOH A O   1 
HETATM 9279 O  O   . HOH G 7 .    ? 25.446 53.574  11.141  1.00 12.55 ? 2713 HOH A O   1 
HETATM 9280 O  O   . HOH G 7 .    ? 30.206 55.720  17.166  1.00 9.38  ? 2714 HOH A O   1 
HETATM 9281 O  O   . HOH G 7 .    ? 27.742 53.349  20.059  1.00 13.17 ? 2715 HOH A O   1 
HETATM 9282 O  O   . HOH G 7 .    ? 27.035 52.379  22.514  1.00 23.46 ? 2716 HOH A O   1 
HETATM 9283 O  O   . HOH G 7 .    ? 27.542 50.045  23.273  1.00 22.49 ? 2717 HOH A O   1 
HETATM 9284 O  O   . HOH G 7 .    ? 27.999 61.004  19.388  1.00 10.08 ? 2718 HOH A O   1 
HETATM 9285 O  O   . HOH G 7 .    ? 26.454 63.651  16.686  1.00 18.98 ? 2719 HOH A O   1 
HETATM 9286 O  O   . HOH G 7 .    ? 24.071 67.466  9.753   1.00 24.29 ? 2720 HOH A O   1 
HETATM 9287 O  O   . HOH G 7 .    ? 20.825 67.904  8.570   1.00 17.13 ? 2721 HOH A O   1 
HETATM 9288 O  O   . HOH G 7 .    ? 20.882 65.175  7.737   1.00 14.27 ? 2722 HOH A O   1 
HETATM 9289 O  O   . HOH G 7 .    ? 27.991 66.267  7.252   1.00 12.27 ? 2723 HOH A O   1 
HETATM 9290 O  O   . HOH G 7 .    ? 26.256 72.500  5.578   1.00 11.38 ? 2724 HOH A O   1 
HETATM 9291 O  O   . HOH G 7 .    ? 25.198 73.436  8.928   1.00 20.97 ? 2725 HOH A O   1 
HETATM 9292 O  O   . HOH G 7 .    ? 23.043 72.412  10.829  1.00 36.93 ? 2726 HOH A O   1 
HETATM 9293 O  O   . HOH G 7 .    ? 22.105 76.363  8.750   1.00 25.78 ? 2727 HOH A O   1 
HETATM 9294 O  O   . HOH G 7 .    ? 26.292 75.709  1.607   1.00 17.23 ? 2728 HOH A O   1 
HETATM 9295 O  O   . HOH G 7 .    ? 21.486 78.328  -1.414  1.00 16.61 ? 2729 HOH A O   1 
HETATM 9296 O  O   . HOH G 7 .    ? 16.361 80.257  -1.336  1.00 38.15 ? 2730 HOH A O   1 
HETATM 9297 O  O   . HOH G 7 .    ? 10.593 76.874  -4.682  1.00 30.95 ? 2731 HOH A O   1 
HETATM 9298 O  O   . HOH G 7 .    ? 7.804  81.173  -4.208  1.00 31.71 ? 2732 HOH A O   1 
HETATM 9299 O  O   . HOH G 7 .    ? 12.258 74.925  -13.375 1.00 28.33 ? 2733 HOH A O   1 
HETATM 9300 O  O   . HOH G 7 .    ? 15.367 76.777  -13.618 1.00 28.95 ? 2734 HOH A O   1 
HETATM 9301 O  O   . HOH G 7 .    ? 15.863 75.032  -11.409 1.00 18.64 ? 2735 HOH A O   1 
HETATM 9302 O  O   . HOH G 7 .    ? 17.056 70.150  -16.217 1.00 12.49 ? 2736 HOH A O   1 
HETATM 9303 O  O   . HOH G 7 .    ? 16.040 71.942  -18.908 1.00 19.81 ? 2737 HOH A O   1 
HETATM 9304 O  O   . HOH G 7 .    ? 12.893 74.462  -18.989 1.00 34.09 ? 2738 HOH A O   1 
HETATM 9305 O  O   . HOH G 7 .    ? 16.439 67.713  -19.877 1.00 17.59 ? 2739 HOH A O   1 
HETATM 9306 O  O   . HOH G 7 .    ? 20.510 66.054  -19.586 1.00 12.03 ? 2740 HOH A O   1 
HETATM 9307 O  O   . HOH G 7 .    ? 20.254 58.639  -21.940 1.00 9.87  ? 2741 HOH A O   1 
HETATM 9308 O  O   . HOH G 7 .    ? 23.755 55.340  -23.386 1.00 9.72  ? 2742 HOH A O   1 
HETATM 9309 O  O   . HOH G 7 .    ? 28.595 49.567  -24.399 1.00 16.59 ? 2743 HOH A O   1 
HETATM 9310 O  O   . HOH G 7 .    ? 31.218 49.748  -23.993 1.00 12.05 ? 2744 HOH A O   1 
HETATM 9311 O  O   . HOH G 7 .    ? 27.471 48.251  -21.570 1.00 15.50 ? 2745 HOH A O   1 
HETATM 9312 O  O   . HOH G 7 .    ? 26.981 47.446  -23.930 1.00 28.83 ? 2746 HOH A O   1 
HETATM 9313 O  O   . HOH G 7 .    ? 25.070 46.762  -20.764 1.00 21.03 ? 2747 HOH A O   1 
HETATM 9314 O  O   . HOH G 7 .    ? 32.920 40.861  -17.823 1.00 23.02 ? 2748 HOH A O   1 
HETATM 9315 O  O   . HOH G 7 .    ? 33.544 38.790  -19.468 1.00 34.22 ? 2749 HOH A O   1 
HETATM 9316 O  O   . HOH G 7 .    ? 36.072 36.040  -18.333 1.00 35.22 ? 2750 HOH A O   1 
HETATM 9317 O  O   . HOH G 7 .    ? 36.815 34.970  -15.858 1.00 29.59 ? 2751 HOH A O   1 
HETATM 9318 O  O   . HOH G 7 .    ? 35.716 38.792  -16.055 1.00 27.21 ? 2752 HOH A O   1 
HETATM 9319 O  O   . HOH G 7 .    ? 36.342 35.232  -23.689 1.00 32.64 ? 2753 HOH A O   1 
HETATM 9320 O  O   . HOH G 7 .    ? 44.916 33.298  -19.202 1.00 43.55 ? 2754 HOH A O   1 
HETATM 9321 O  O   . HOH G 7 .    ? 40.992 52.199  -16.938 1.00 11.86 ? 2755 HOH A O   1 
HETATM 9322 O  O   . HOH G 7 .    ? 42.244 54.705  -17.415 1.00 21.45 ? 2756 HOH A O   1 
HETATM 9323 O  O   . HOH G 7 .    ? 42.979 59.296  -18.937 1.00 19.79 ? 2757 HOH A O   1 
HETATM 9324 O  O   . HOH G 7 .    ? 45.659 59.741  -18.303 1.00 10.98 ? 2758 HOH A O   1 
HETATM 9325 O  O   . HOH G 7 .    ? 39.156 62.736  -19.127 1.00 7.96  ? 2759 HOH A O   1 
HETATM 9326 O  O   . HOH G 7 .    ? 39.224 64.619  -14.823 1.00 10.32 ? 2760 HOH A O   1 
HETATM 9327 O  O   . HOH G 7 .    ? 41.997 63.372  -7.164  1.00 6.27  ? 2761 HOH A O   1 
HETATM 9328 O  O   . HOH G 7 .    ? 49.535 62.222  -8.676  1.00 8.75  ? 2762 HOH A O   1 
HETATM 9329 O  O   . HOH G 7 .    ? 50.821 59.787  -8.972  1.00 10.03 ? 2763 HOH A O   1 
HETATM 9330 O  O   . HOH G 7 .    ? 49.987 59.430  -11.564 1.00 8.91  ? 2764 HOH A O   1 
HETATM 9331 O  O   . HOH G 7 .    ? 53.587 59.748  -9.423  1.00 9.86  ? 2765 HOH A O   1 
HETATM 9332 O  O   . HOH G 7 .    ? 55.562 59.228  -11.518 1.00 8.85  ? 2766 HOH A O   1 
HETATM 9333 O  O   . HOH G 7 .    ? 49.743 57.548  -7.603  1.00 9.34  ? 2767 HOH A O   1 
HETATM 9334 O  O   . HOH G 7 .    ? 51.429 56.617  -5.593  1.00 9.10  ? 2768 HOH A O   1 
HETATM 9335 O  O   . HOH G 7 .    ? 52.144 54.011  -4.830  1.00 8.24  ? 2769 HOH A O   1 
HETATM 9336 O  O   . HOH G 7 .    ? 52.750 58.839  -1.760  1.00 11.92 ? 2770 HOH A O   1 
HETATM 9337 O  O   . HOH G 7 .    ? 67.049 55.289  0.859   1.00 21.70 ? 2771 HOH A O   1 
HETATM 9338 O  O   . HOH G 7 .    ? 71.297 59.579  1.039   1.00 33.21 ? 2772 HOH A O   1 
HETATM 9339 O  O   . HOH G 7 .    ? 73.380 62.984  -0.561  1.00 33.78 ? 2773 HOH A O   1 
HETATM 9340 O  O   . HOH G 7 .    ? 72.998 64.970  -7.707  1.00 21.99 ? 2774 HOH A O   1 
HETATM 9341 O  O   . HOH G 7 .    ? 72.999 66.479  -10.075 1.00 21.70 ? 2775 HOH A O   1 
HETATM 9342 O  O   . HOH G 7 .    ? 69.926 69.867  -12.645 1.00 12.84 ? 2776 HOH A O   1 
HETATM 9343 O  O   . HOH G 7 .    ? 76.296 71.118  -8.463  1.00 28.93 ? 2777 HOH A O   1 
HETATM 9344 O  O   . HOH G 7 .    ? 78.351 71.620  -10.105 1.00 28.54 ? 2778 HOH A O   1 
HETATM 9345 O  O   . HOH G 7 .    ? 73.560 74.050  -5.738  1.00 21.44 ? 2779 HOH A O   1 
HETATM 9346 O  O   . HOH G 7 .    ? 68.566 78.677  -18.179 1.00 17.36 ? 2780 HOH A O   1 
HETATM 9347 O  O   . HOH G 7 .    ? 70.284 83.833  -17.613 1.00 46.48 ? 2781 HOH A O   1 
HETATM 9348 O  O   . HOH G 7 .    ? 71.559 84.575  -20.060 1.00 27.15 ? 2782 HOH A O   1 
HETATM 9349 O  O   . HOH G 7 .    ? 73.278 82.237  -21.193 1.00 24.06 ? 2783 HOH A O   1 
HETATM 9350 O  O   . HOH G 7 .    ? 75.037 83.812  -23.173 1.00 33.44 ? 2784 HOH A O   1 
HETATM 9351 O  O   . HOH G 7 .    ? 74.099 86.597  -22.790 1.00 39.71 ? 2785 HOH A O   1 
HETATM 9352 O  O   . HOH G 7 .    ? 67.547 87.848  -23.455 1.00 18.77 ? 2786 HOH A O   1 
HETATM 9353 O  O   . HOH G 7 .    ? 64.851 87.532  -24.257 1.00 21.31 ? 2787 HOH A O   1 
HETATM 9354 O  O   . HOH G 7 .    ? 69.013 94.047  -25.669 1.00 27.27 ? 2788 HOH A O   1 
HETATM 9355 O  O   . HOH G 7 .    ? 72.299 95.498  -31.345 1.00 27.01 ? 2789 HOH A O   1 
HETATM 9356 O  O   . HOH G 7 .    ? 70.912 95.442  -34.977 1.00 35.60 ? 2790 HOH A O   1 
HETATM 9357 O  O   . HOH G 7 .    ? 68.074 97.768  -34.587 1.00 36.85 ? 2791 HOH A O   1 
HETATM 9358 O  O   . HOH G 7 .    ? 65.473 97.387  -35.853 1.00 33.71 ? 2792 HOH A O   1 
HETATM 9359 O  O   . HOH G 7 .    ? 67.826 88.057  -35.153 1.00 30.67 ? 2793 HOH A O   1 
HETATM 9360 O  O   . HOH G 7 .    ? 70.536 88.268  -35.476 1.00 36.25 ? 2794 HOH A O   1 
HETATM 9361 O  O   . HOH G 7 .    ? 67.371 85.422  -36.090 1.00 31.43 ? 2795 HOH A O   1 
HETATM 9362 O  O   . HOH G 7 .    ? 69.406 83.720  -36.069 1.00 25.91 ? 2796 HOH A O   1 
HETATM 9363 O  O   . HOH G 7 .    ? 69.846 81.736  -34.097 1.00 34.81 ? 2797 HOH A O   1 
HETATM 9364 O  O   . HOH G 7 .    ? 68.345 79.482  -34.936 1.00 22.75 ? 2798 HOH A O   1 
HETATM 9365 O  O   . HOH G 7 .    ? 69.223 76.912  -34.270 1.00 23.36 ? 2799 HOH A O   1 
HETATM 9366 O  O   . HOH G 7 .    ? 67.901 74.869  -35.179 1.00 25.02 ? 2800 HOH A O   1 
HETATM 9367 O  O   . HOH G 7 .    ? 71.479 76.383  -35.727 1.00 39.40 ? 2801 HOH A O   1 
HETATM 9368 O  O   . HOH G 7 .    ? 70.936 72.206  -34.446 1.00 37.76 ? 2802 HOH A O   1 
HETATM 9369 O  O   . HOH G 7 .    ? 67.707 77.033  -38.772 1.00 38.10 ? 2803 HOH A O   1 
HETATM 9370 O  O   . HOH G 7 .    ? 63.978 78.446  -37.982 1.00 28.21 ? 2804 HOH A O   1 
HETATM 9371 O  O   . HOH G 7 .    ? 64.276 77.748  -35.433 1.00 13.02 ? 2805 HOH A O   1 
HETATM 9372 O  O   . HOH G 7 .    ? 63.986 76.867  -40.476 1.00 31.05 ? 2806 HOH A O   1 
HETATM 9373 O  O   . HOH G 7 .    ? 61.372 76.459  -39.836 1.00 19.27 ? 2807 HOH A O   1 
HETATM 9374 O  O   . HOH G 7 .    ? 60.658 78.669  -41.750 1.00 25.65 ? 2808 HOH A O   1 
HETATM 9375 O  O   . HOH G 7 .    ? 62.035 81.252  -44.511 1.00 31.82 ? 2809 HOH A O   1 
HETATM 9376 O  O   . HOH G 7 .    ? 59.213 86.677  -45.993 1.00 38.02 ? 2810 HOH A O   1 
HETATM 9377 O  O   . HOH G 7 .    ? 54.194 82.585  -44.768 1.00 40.72 ? 2811 HOH A O   1 
HETATM 9378 O  O   . HOH G 7 .    ? 53.389 79.018  -44.744 1.00 37.14 ? 2812 HOH A O   1 
HETATM 9379 O  O   . HOH G 7 .    ? 53.408 76.726  -43.687 1.00 37.03 ? 2813 HOH A O   1 
HETATM 9380 O  O   . HOH G 7 .    ? 51.375 76.033  -41.083 1.00 28.81 ? 2814 HOH A O   1 
HETATM 9381 O  O   . HOH G 7 .    ? 47.516 78.785  -40.479 1.00 16.69 ? 2815 HOH A O   1 
HETATM 9382 O  O   . HOH G 7 .    ? 46.556 80.073  -42.658 1.00 21.09 ? 2816 HOH A O   1 
HETATM 9383 O  O   . HOH G 7 .    ? 43.810 79.719  -42.604 1.00 24.58 ? 2817 HOH A O   1 
HETATM 9384 O  O   . HOH G 7 .    ? 45.298 83.519  -43.262 1.00 34.63 ? 2818 HOH A O   1 
HETATM 9385 O  O   . HOH G 7 .    ? 47.083 83.065  -44.778 1.00 40.11 ? 2819 HOH A O   1 
HETATM 9386 O  O   . HOH G 7 .    ? 49.777 82.089  -43.927 1.00 17.80 ? 2820 HOH A O   1 
HETATM 9387 O  O   . HOH G 7 .    ? 51.016 80.050  -45.670 1.00 38.14 ? 2821 HOH A O   1 
HETATM 9388 O  O   . HOH G 7 .    ? 55.188 73.840  -43.122 1.00 37.26 ? 2822 HOH A O   1 
HETATM 9389 O  O   . HOH G 7 .    ? 59.797 70.085  -44.619 1.00 39.08 ? 2823 HOH A O   1 
HETATM 9390 O  O   . HOH G 7 .    ? 62.453 70.626  -45.101 1.00 39.39 ? 2824 HOH A O   1 
HETATM 9391 O  O   . HOH G 7 .    ? 61.557 69.056  -41.987 1.00 27.33 ? 2825 HOH A O   1 
HETATM 9392 O  O   . HOH G 7 .    ? 58.329 77.100  -38.587 1.00 13.46 ? 2826 HOH A O   1 
HETATM 9393 O  O   . HOH G 7 .    ? 61.799 82.907  -38.436 1.00 21.61 ? 2827 HOH A O   1 
HETATM 9394 O  O   . HOH G 7 .    ? 65.448 87.568  -41.263 1.00 38.02 ? 2828 HOH A O   1 
HETATM 9395 O  O   . HOH G 7 .    ? 48.242 89.024  -30.843 1.00 13.58 ? 2829 HOH A O   1 
HETATM 9396 O  O   . HOH G 7 .    ? 43.950 79.530  -21.584 1.00 39.58 ? 2830 HOH A O   1 
HETATM 9397 O  O   . HOH G 7 .    ? 42.144 75.137  -16.056 1.00 12.22 ? 2831 HOH A O   1 
HETATM 9398 O  O   . HOH G 7 .    ? 41.287 77.382  -14.180 1.00 13.15 ? 2832 HOH A O   1 
HETATM 9399 O  O   . HOH G 7 .    ? 40.349 82.660  -10.770 1.00 16.13 ? 2833 HOH A O   1 
HETATM 9400 O  O   . HOH G 7 .    ? 42.981 82.235  -9.980  1.00 24.18 ? 2834 HOH A O   1 
HETATM 9401 O  O   . HOH G 7 .    ? 40.818 85.112  -12.063 1.00 28.99 ? 2835 HOH A O   1 
HETATM 9402 O  O   . HOH G 7 .    ? 36.698 87.930  -11.750 1.00 38.18 ? 2836 HOH A O   1 
HETATM 9403 O  O   . HOH G 7 .    ? 34.187 87.010  -10.519 1.00 26.57 ? 2837 HOH A O   1 
HETATM 9404 O  O   . HOH G 7 .    ? 35.429 85.960  -8.221  1.00 25.93 ? 2838 HOH A O   1 
HETATM 9405 O  O   . HOH G 7 .    ? 32.152 85.037  -8.578  1.00 19.45 ? 2839 HOH A O   1 
HETATM 9406 O  O   . HOH G 7 .    ? 33.580 83.458  -10.420 1.00 13.34 ? 2840 HOH A O   1 
HETATM 9407 O  O   . HOH G 7 .    ? 32.724 80.952  -11.714 1.00 10.02 ? 2841 HOH A O   1 
HETATM 9408 O  O   . HOH G 7 .    ? 34.519 79.016  -9.161  1.00 10.44 ? 2842 HOH A O   1 
HETATM 9409 O  O   . HOH G 7 .    ? 35.808 77.437  -7.330  1.00 11.79 ? 2843 HOH A O   1 
HETATM 9410 O  O   . HOH G 7 .    ? 36.342 79.126  -5.057  1.00 19.31 ? 2844 HOH A O   1 
HETATM 9411 O  O   . HOH G 7 .    ? 33.336 78.529  -5.150  1.00 11.64 ? 2845 HOH A O   1 
HETATM 9412 O  O   . HOH G 7 .    ? 31.358 76.668  -6.313  1.00 9.98  ? 2846 HOH A O   1 
HETATM 9413 O  O   . HOH G 7 .    ? 37.079 71.755  -4.587  1.00 7.62  ? 2847 HOH A O   1 
HETATM 9414 O  O   . HOH G 7 .    ? 37.896 73.269  -2.313  1.00 9.83  ? 2848 HOH A O   1 
HETATM 9415 O  O   . HOH G 7 .    ? 36.632 72.564  0.221   1.00 8.16  ? 2849 HOH A O   1 
HETATM 9416 O  O   . HOH G 7 .    ? 33.071 62.613  0.042   1.00 6.99  ? 2850 HOH A O   1 
HETATM 9417 O  O   . HOH G 7 .    ? 32.550 59.965  -1.858  1.00 7.65  ? 2851 HOH A O   1 
HETATM 9418 O  O   . HOH G 7 .    ? 26.759 60.757  -3.328  1.00 8.72  ? 2852 HOH A O   1 
HETATM 9419 O  O   . HOH G 7 .    ? 24.341 55.528  -1.769  1.00 11.34 ? 2853 HOH A O   1 
HETATM 9420 O  O   . HOH G 7 .    ? 23.282 53.794  -3.635  1.00 12.96 ? 2854 HOH A O   1 
HETATM 9421 O  O   . HOH G 7 .    ? 24.094 53.019  -6.248  1.00 18.56 ? 2855 HOH A O   1 
HETATM 9422 O  O   . HOH G 7 .    ? 20.589 57.325  -5.230  1.00 9.96  ? 2856 HOH A O   1 
HETATM 9423 O  O   . HOH G 7 .    ? 21.510 57.823  -7.803  1.00 9.23  ? 2857 HOH A O   1 
HETATM 9424 O  O   . HOH G 7 .    ? 19.777 57.172  -11.751 1.00 13.00 ? 2858 HOH A O   1 
HETATM 9425 O  O   . HOH G 7 .    ? 14.296 54.190  -16.150 1.00 16.12 ? 2859 HOH A O   1 
HETATM 9426 O  O   . HOH G 7 .    ? 13.149 52.026  -15.061 1.00 28.28 ? 2860 HOH A O   1 
HETATM 9427 O  O   . HOH G 7 .    ? 12.876 51.470  -12.161 1.00 25.89 ? 2861 HOH A O   1 
HETATM 9428 O  O   . HOH G 7 .    ? 11.739 54.929  -12.324 1.00 17.38 ? 2862 HOH A O   1 
HETATM 9429 O  O   . HOH G 7 .    ? 9.560  53.397  -12.140 1.00 27.95 ? 2863 HOH A O   1 
HETATM 9430 O  O   . HOH G 7 .    ? 7.522  53.893  -10.211 1.00 22.13 ? 2864 HOH A O   1 
HETATM 9431 O  O   . HOH G 7 .    ? 7.902  57.722  -11.526 1.00 39.46 ? 2865 HOH A O   1 
HETATM 9432 O  O   . HOH G 7 .    ? 12.240 55.715  -15.114 1.00 16.93 ? 2866 HOH A O   1 
HETATM 9433 O  O   . HOH G 7 .    ? 10.492 57.687  -20.854 1.00 38.92 ? 2867 HOH A O   1 
HETATM 9434 O  O   . HOH G 7 .    ? 9.700  60.177  -20.322 1.00 24.88 ? 2868 HOH A O   1 
HETATM 9435 O  O   . HOH G 7 .    ? 4.268  56.494  -6.331  1.00 31.39 ? 2869 HOH A O   1 
HETATM 9436 O  O   . HOH G 7 .    ? 4.971  52.730  -6.095  1.00 33.88 ? 2870 HOH A O   1 
HETATM 9437 O  O   . HOH G 7 .    ? 15.878 44.790  -11.565 1.00 32.87 ? 2871 HOH A O   1 
HETATM 9438 O  O   . HOH G 7 .    ? 30.839 57.093  4.516   1.00 18.34 ? 2872 HOH A O   1 
HETATM 9439 O  O   . HOH G 7 .    ? 33.733 60.336  23.209  1.00 11.59 ? 2873 HOH A O   1 
HETATM 9440 O  O   . HOH G 7 .    ? 50.854 61.945  26.374  1.00 19.41 ? 2874 HOH A O   1 
HETATM 9441 O  O   . HOH G 7 .    ? 51.895 60.198  28.191  1.00 33.79 ? 2875 HOH A O   1 
HETATM 9442 O  O   . HOH G 7 .    ? 51.917 63.770  24.476  1.00 27.75 ? 2876 HOH A O   1 
HETATM 9443 O  O   . HOH G 7 .    ? 57.040 64.766  24.063  1.00 29.90 ? 2877 HOH A O   1 
HETATM 9444 O  O   . HOH G 7 .    ? 59.456 62.102  25.802  1.00 35.14 ? 2878 HOH A O   1 
HETATM 9445 O  O   . HOH G 7 .    ? 62.456 62.045  25.439  1.00 34.21 ? 2879 HOH A O   1 
HETATM 9446 O  O   . HOH G 7 .    ? 59.254 55.505  27.032  1.00 33.55 ? 2880 HOH A O   1 
HETATM 9447 O  O   . HOH G 7 .    ? 49.605 50.787  32.619  1.00 28.27 ? 2881 HOH A O   1 
HETATM 9448 O  O   . HOH G 7 .    ? 48.148 50.817  35.444  1.00 49.62 ? 2882 HOH A O   1 
HETATM 9449 O  O   . HOH G 7 .    ? 50.424 50.444  36.931  1.00 39.46 ? 2883 HOH A O   1 
HETATM 9450 O  O   . HOH G 7 .    ? 52.074 71.531  22.042  1.00 37.34 ? 2884 HOH A O   1 
HETATM 9451 O  O   . HOH G 7 .    ? 52.683 72.457  18.033  1.00 23.59 ? 2885 HOH A O   1 
HETATM 9452 O  O   . HOH G 7 .    ? 53.034 69.552  18.138  1.00 22.22 ? 2886 HOH A O   1 
HETATM 9453 O  O   . HOH G 7 .    ? 45.948 74.165  22.561  1.00 33.65 ? 2887 HOH A O   1 
HETATM 9454 O  O   . HOH G 7 .    ? 32.861 85.246  -5.604  1.00 17.44 ? 2888 HOH A O   1 
HETATM 9455 O  O   . HOH G 7 .    ? 31.473 87.573  -6.705  1.00 34.29 ? 2889 HOH A O   1 
HETATM 9456 O  O   . HOH G 7 .    ? 26.628 87.875  -3.884  1.00 35.45 ? 2890 HOH A O   1 
HETATM 9457 O  O   . HOH G 7 .    ? 24.064 83.004  -4.043  1.00 26.52 ? 2891 HOH A O   1 
HETATM 9458 O  O   . HOH G 7 .    ? 27.376 88.470  -12.469 1.00 26.39 ? 2892 HOH A O   1 
HETATM 9459 O  O   . HOH G 7 .    ? 27.918 102.163 -19.128 1.00 30.81 ? 2893 HOH A O   1 
HETATM 9460 O  O   . HOH G 7 .    ? 14.016 88.247  -19.818 1.00 34.66 ? 2894 HOH A O   1 
HETATM 9461 O  O   . HOH G 7 .    ? 28.974 93.544  -38.773 1.00 23.29 ? 2895 HOH A O   1 
HETATM 9462 O  O   . HOH G 7 .    ? 32.004 92.248  -36.896 1.00 23.91 ? 2896 HOH A O   1 
HETATM 9463 O  O   . HOH G 7 .    ? 38.757 93.776  -42.385 1.00 22.55 ? 2897 HOH A O   1 
HETATM 9464 O  O   . HOH G 7 .    ? 45.463 91.414  -44.399 1.00 35.97 ? 2898 HOH A O   1 
HETATM 9465 O  O   . HOH G 7 .    ? 46.096 96.824  -43.942 1.00 23.25 ? 2899 HOH A O   1 
HETATM 9466 O  O   . HOH G 7 .    ? 38.610 83.263  -39.736 1.00 21.14 ? 2900 HOH A O   1 
HETATM 9467 O  O   . HOH G 7 .    ? 36.796 82.238  -41.507 1.00 37.18 ? 2901 HOH A O   1 
HETATM 9468 O  O   . HOH G 7 .    ? 35.935 77.361  -43.068 1.00 32.96 ? 2902 HOH A O   1 
HETATM 9469 O  O   . HOH G 7 .    ? 37.569 75.385  -42.304 1.00 22.30 ? 2903 HOH A O   1 
HETATM 9470 O  O   . HOH G 7 .    ? 36.345 62.472  -38.565 1.00 29.03 ? 2904 HOH A O   1 
HETATM 9471 O  O   . HOH G 7 .    ? 36.119 63.387  -33.894 1.00 27.99 ? 2905 HOH A O   1 
HETATM 9472 O  O   . HOH G 7 .    ? 33.960 64.290  -32.305 1.00 13.53 ? 2906 HOH A O   1 
HETATM 9473 O  O   . HOH G 7 .    ? 37.514 61.300  -32.424 1.00 25.32 ? 2907 HOH A O   1 
HETATM 9474 O  O   . HOH G 7 .    ? 40.837 62.533  -31.856 1.00 20.98 ? 2908 HOH A O   1 
HETATM 9475 O  O   . HOH G 7 .    ? 43.358 63.479  -32.331 1.00 29.53 ? 2909 HOH A O   1 
HETATM 9476 O  O   . HOH G 7 .    ? 44.990 63.835  -34.506 1.00 51.92 ? 2910 HOH A O   1 
HETATM 9477 O  O   . HOH G 7 .    ? 44.860 66.227  -34.536 1.00 38.88 ? 2911 HOH A O   1 
HETATM 9478 O  O   . HOH G 7 .    ? 45.772 60.431  -31.081 1.00 51.82 ? 2912 HOH A O   1 
HETATM 9479 O  O   . HOH G 7 .    ? 42.729 59.190  -31.460 1.00 23.29 ? 2913 HOH A O   1 
HETATM 9480 O  O   . HOH G 7 .    ? 42.800 56.511  -31.529 1.00 22.88 ? 2914 HOH A O   1 
HETATM 9481 O  O   . HOH G 7 .    ? 40.779 55.706  -33.252 1.00 27.23 ? 2915 HOH A O   1 
HETATM 9482 O  O   . HOH G 7 .    ? 38.501 54.973  -31.648 1.00 15.02 ? 2916 HOH A O   1 
HETATM 9483 O  O   . HOH G 7 .    ? 37.210 52.606  -32.426 1.00 25.69 ? 2917 HOH A O   1 
HETATM 9484 O  O   . HOH G 7 .    ? 38.387 51.325  -29.859 1.00 19.52 ? 2918 HOH A O   1 
HETATM 9485 O  O   . HOH G 7 .    ? 39.482 48.476  -32.808 1.00 20.20 ? 2919 HOH A O   1 
HETATM 9486 O  O   . HOH G 7 .    ? 38.620 44.955  -33.644 1.00 20.81 ? 2920 HOH A O   1 
HETATM 9487 O  O   . HOH G 7 .    ? 49.492 48.834  -38.339 1.00 53.23 ? 2921 HOH A O   1 
HETATM 9488 O  O   . HOH G 7 .    ? 48.280 53.883  -31.332 1.00 41.44 ? 2922 HOH A O   1 
HETATM 9489 O  O   . HOH G 7 .    ? 50.030 58.281  -30.865 1.00 42.75 ? 2923 HOH A O   1 
HETATM 9490 O  O   . HOH G 7 .    ? 49.046 59.108  -28.649 1.00 26.99 ? 2924 HOH A O   1 
HETATM 9491 O  O   . HOH G 7 .    ? 48.259 61.588  -28.670 1.00 29.31 ? 2925 HOH A O   1 
HETATM 9492 O  O   . HOH G 7 .    ? 47.917 64.612  -27.963 1.00 35.32 ? 2926 HOH A O   1 
HETATM 9493 O  O   . HOH G 7 .    ? 49.861 64.828  -26.874 1.00 34.85 ? 2927 HOH A O   1 
HETATM 9494 O  O   . HOH G 7 .    ? 47.207 62.058  -25.698 1.00 19.93 ? 2928 HOH A O   1 
HETATM 9495 O  O   . HOH G 7 .    ? 47.779 59.224  -25.677 1.00 13.35 ? 2929 HOH A O   1 
HETATM 9496 O  O   . HOH G 7 .    ? 46.832 55.641  -25.515 1.00 17.26 ? 2930 HOH A O   1 
HETATM 9497 O  O   . HOH G 7 .    ? 43.740 54.833  -26.832 1.00 28.66 ? 2931 HOH A O   1 
HETATM 9498 O  O   . HOH G 7 .    ? 41.650 61.043  -29.670 1.00 16.12 ? 2932 HOH A O   1 
HETATM 9499 O  O   . HOH G 7 .    ? 43.588 62.580  -28.440 1.00 19.25 ? 2933 HOH A O   1 
HETATM 9500 O  O   . HOH G 7 .    ? 43.436 68.179  -25.329 1.00 12.60 ? 2934 HOH A O   1 
HETATM 9501 O  O   . HOH G 7 .    ? 50.384 61.205  -30.950 1.00 26.09 ? 2935 HOH A O   1 
HETATM 9502 O  O   . HOH G 7 .    ? 34.041 56.156  -26.300 1.00 10.55 ? 2936 HOH A O   1 
HETATM 9503 O  O   . HOH G 7 .    ? 32.040 58.392  -28.454 1.00 13.20 ? 2937 HOH A O   1 
HETATM 9504 O  O   . HOH G 7 .    ? 10.568 67.794  -2.012  1.00 27.34 ? 2938 HOH A O   1 
HETATM 9505 O  O   . HOH G 7 .    ? 13.206 68.534  1.008   1.00 17.88 ? 2939 HOH A O   1 
HETATM 9506 O  O   . HOH G 7 .    ? 11.594 67.011  2.587   1.00 56.27 ? 2940 HOH A O   1 
HETATM 9507 O  O   . HOH G 7 .    ? 12.683 70.926  -0.321  1.00 19.97 ? 2941 HOH A O   1 
HETATM 9508 O  O   . HOH G 7 .    ? 9.851  53.748  22.231  1.00 33.40 ? 2942 HOH A O   1 
HETATM 9509 O  O   . HOH G 7 .    ? 19.642 39.155  17.726  1.00 17.81 ? 2943 HOH A O   1 
HETATM 9510 O  O   . HOH G 7 .    ? 21.649 37.993  15.765  1.00 30.52 ? 2944 HOH A O   1 
HETATM 9511 O  O   . HOH G 7 .    ? 23.146 37.048  13.569  1.00 31.02 ? 2945 HOH A O   1 
HETATM 9512 O  O   . HOH G 7 .    ? 20.417 37.732  12.281  1.00 26.48 ? 2946 HOH A O   1 
HETATM 9513 O  O   . HOH G 7 .    ? 17.956 35.200  13.351  1.00 36.22 ? 2947 HOH A O   1 
HETATM 9514 O  O   . HOH G 7 .    ? 16.365 33.630  15.783  1.00 37.95 ? 2948 HOH A O   1 
HETATM 9515 O  O   . HOH G 7 .    ? 15.986 36.290  16.340  1.00 26.41 ? 2949 HOH A O   1 
HETATM 9516 O  O   . HOH G 7 .    ? 15.952 30.525  18.363  1.00 38.75 ? 2950 HOH A O   1 
HETATM 9517 O  O   . HOH G 7 .    ? 20.895 30.186  17.850  1.00 38.25 ? 2951 HOH A O   1 
HETATM 9518 O  O   . HOH G 7 .    ? 24.997 39.960  14.282  1.00 15.78 ? 2952 HOH A O   1 
HETATM 9519 O  O   . HOH G 7 .    ? 36.878 29.129  13.149  1.00 28.65 ? 2953 HOH A O   1 
HETATM 9520 O  O   . HOH G 7 .    ? 70.929 49.314  -0.163  1.00 24.55 ? 2954 HOH A O   1 
HETATM 9521 O  O   . HOH G 7 .    ? 74.141 51.995  1.640   1.00 33.25 ? 2955 HOH A O   1 
HETATM 9522 O  O   . HOH G 7 .    ? 79.567 51.263  -0.453  1.00 25.75 ? 2956 HOH A O   1 
HETATM 9523 O  O   . HOH G 7 .    ? 75.796 48.338  -5.656  1.00 33.74 ? 2957 HOH A O   1 
HETATM 9524 O  O   . HOH G 7 .    ? 73.664 46.193  -5.347  1.00 37.06 ? 2958 HOH A O   1 
HETATM 9525 O  O   . HOH G 7 .    ? 76.474 46.930  -11.680 1.00 26.77 ? 2959 HOH A O   1 
HETATM 9526 O  O   . HOH G 7 .    ? 73.024 43.577  -12.311 1.00 38.35 ? 2960 HOH A O   1 
HETATM 9527 O  O   . HOH G 7 .    ? 71.006 42.964  -15.565 1.00 29.74 ? 2961 HOH A O   1 
HETATM 9528 O  O   . HOH G 7 .    ? 69.163 41.627  -17.402 1.00 30.37 ? 2962 HOH A O   1 
HETATM 9529 O  O   . HOH G 7 .    ? 68.605 46.751  -16.546 1.00 25.51 ? 2963 HOH A O   1 
HETATM 9530 O  O   . HOH G 7 .    ? 72.028 47.091  -17.997 1.00 25.96 ? 2964 HOH A O   1 
HETATM 9531 O  O   . HOH G 7 .    ? 70.707 52.042  -12.544 1.00 19.99 ? 2965 HOH A O   1 
HETATM 9532 O  O   . HOH G 7 .    ? 71.139 54.286  -13.948 1.00 28.95 ? 2966 HOH A O   1 
HETATM 9533 O  O   . HOH G 7 .    ? 70.343 56.261  -12.472 1.00 33.30 ? 2967 HOH A O   1 
HETATM 9534 O  O   . HOH G 7 .    ? 72.182 58.645  -11.179 1.00 23.17 ? 2968 HOH A O   1 
HETATM 9535 O  O   . HOH G 7 .    ? 74.320 60.079  -9.507  1.00 35.78 ? 2969 HOH A O   1 
HETATM 9536 O  O   . HOH G 7 .    ? 68.739 58.174  -5.073  1.00 12.89 ? 2970 HOH A O   1 
HETATM 9537 O  O   . HOH G 7 .    ? 70.011 53.453  -10.342 1.00 29.97 ? 2971 HOH A O   1 
HETATM 9538 O  O   . HOH G 7 .    ? 73.842 53.873  -13.765 1.00 38.29 ? 2972 HOH A O   1 
HETATM 9539 O  O   . HOH G 7 .    ? 79.590 50.771  -11.439 1.00 40.32 ? 2973 HOH A O   1 
HETATM 9540 O  O   . HOH G 7 .    ? 79.348 50.575  -9.006  1.00 26.68 ? 2974 HOH A O   1 
HETATM 9541 O  O   . HOH G 7 .    ? 63.794 50.004  -14.022 1.00 11.94 ? 2975 HOH A O   1 
HETATM 9542 O  O   . HOH G 7 .    ? 66.526 62.515  -13.059 1.00 16.68 ? 2976 HOH A O   1 
HETATM 9543 O  O   . HOH G 7 .    ? 46.917 87.794  -13.434 1.00 41.06 ? 2977 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  ASP 341  341  341  ASP ASP 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    1802 1802 NAG NAG A . 
C 3 PO4 1    1803 1803 PO4 PO4 A . 
D 4 ZN  1    1805 1805 ZN  ZN  A . 
E 5 GB1 1    1804 1804 GB1 GB1 A . 
F 6 MPD 1    1801 1801 MPD MPD A . 
G 7 HOH 1    1806 1    HOH HOH A . 
G 7 HOH 2    1807 2    HOH HOH A . 
G 7 HOH 3    1808 3    HOH HOH A . 
G 7 HOH 4    1809 4    HOH HOH A . 
G 7 HOH 5    1810 5    HOH HOH A . 
G 7 HOH 6    1811 6    HOH HOH A . 
G 7 HOH 7    1812 7    HOH HOH A . 
G 7 HOH 8    1813 8    HOH HOH A . 
G 7 HOH 9    1814 9    HOH HOH A . 
G 7 HOH 10   1815 10   HOH HOH A . 
G 7 HOH 11   1816 11   HOH HOH A . 
G 7 HOH 12   1817 12   HOH HOH A . 
G 7 HOH 13   1818 13   HOH HOH A . 
G 7 HOH 14   1819 14   HOH HOH A . 
G 7 HOH 15   1820 15   HOH HOH A . 
G 7 HOH 16   1821 16   HOH HOH A . 
G 7 HOH 17   1822 17   HOH HOH A . 
G 7 HOH 18   1823 18   HOH HOH A . 
G 7 HOH 19   1824 19   HOH HOH A . 
G 7 HOH 20   1825 20   HOH HOH A . 
G 7 HOH 21   1826 21   HOH HOH A . 
G 7 HOH 22   1827 22   HOH HOH A . 
G 7 HOH 23   1828 23   HOH HOH A . 
G 7 HOH 24   1829 24   HOH HOH A . 
G 7 HOH 25   1830 25   HOH HOH A . 
G 7 HOH 26   1831 26   HOH HOH A . 
G 7 HOH 27   1832 27   HOH HOH A . 
G 7 HOH 28   1833 28   HOH HOH A . 
G 7 HOH 29   1834 29   HOH HOH A . 
G 7 HOH 30   1835 30   HOH HOH A . 
G 7 HOH 31   1836 31   HOH HOH A . 
G 7 HOH 32   1837 32   HOH HOH A . 
G 7 HOH 33   1838 33   HOH HOH A . 
G 7 HOH 34   1839 34   HOH HOH A . 
G 7 HOH 35   1840 35   HOH HOH A . 
G 7 HOH 36   1841 36   HOH HOH A . 
G 7 HOH 37   1842 37   HOH HOH A . 
G 7 HOH 38   1843 38   HOH HOH A . 
G 7 HOH 39   1844 39   HOH HOH A . 
G 7 HOH 40   1845 40   HOH HOH A . 
G 7 HOH 41   1846 41   HOH HOH A . 
G 7 HOH 42   1847 42   HOH HOH A . 
G 7 HOH 43   1848 43   HOH HOH A . 
G 7 HOH 44   1849 44   HOH HOH A . 
G 7 HOH 45   1850 45   HOH HOH A . 
G 7 HOH 46   1851 46   HOH HOH A . 
G 7 HOH 47   1852 47   HOH HOH A . 
G 7 HOH 48   1853 48   HOH HOH A . 
G 7 HOH 49   1854 49   HOH HOH A . 
G 7 HOH 50   1855 50   HOH HOH A . 
G 7 HOH 51   1856 51   HOH HOH A . 
G 7 HOH 52   1857 52   HOH HOH A . 
G 7 HOH 53   1858 53   HOH HOH A . 
G 7 HOH 54   1859 54   HOH HOH A . 
G 7 HOH 55   1860 55   HOH HOH A . 
G 7 HOH 56   1861 56   HOH HOH A . 
G 7 HOH 57   1862 57   HOH HOH A . 
G 7 HOH 58   1863 58   HOH HOH A . 
G 7 HOH 59   1864 59   HOH HOH A . 
G 7 HOH 60   1865 60   HOH HOH A . 
G 7 HOH 61   1866 61   HOH HOH A . 
G 7 HOH 62   1867 62   HOH HOH A . 
G 7 HOH 63   1868 63   HOH HOH A . 
G 7 HOH 64   1869 64   HOH HOH A . 
G 7 HOH 65   1870 65   HOH HOH A . 
G 7 HOH 66   1871 66   HOH HOH A . 
G 7 HOH 67   1872 67   HOH HOH A . 
G 7 HOH 68   1873 68   HOH HOH A . 
G 7 HOH 69   1874 69   HOH HOH A . 
G 7 HOH 70   1875 70   HOH HOH A . 
G 7 HOH 71   1876 71   HOH HOH A . 
G 7 HOH 72   1877 72   HOH HOH A . 
G 7 HOH 73   1878 73   HOH HOH A . 
G 7 HOH 74   1879 74   HOH HOH A . 
G 7 HOH 75   1880 75   HOH HOH A . 
G 7 HOH 76   1881 76   HOH HOH A . 
G 7 HOH 77   1882 77   HOH HOH A . 
G 7 HOH 78   1883 78   HOH HOH A . 
G 7 HOH 79   1884 79   HOH HOH A . 
G 7 HOH 80   1885 80   HOH HOH A . 
G 7 HOH 81   1886 81   HOH HOH A . 
G 7 HOH 82   1887 82   HOH HOH A . 
G 7 HOH 83   1888 83   HOH HOH A . 
G 7 HOH 84   1889 84   HOH HOH A . 
G 7 HOH 85   1890 85   HOH HOH A . 
G 7 HOH 86   1891 86   HOH HOH A . 
G 7 HOH 87   1892 87   HOH HOH A . 
G 7 HOH 88   1893 88   HOH HOH A . 
G 7 HOH 89   1894 89   HOH HOH A . 
G 7 HOH 90   1895 90   HOH HOH A . 
G 7 HOH 91   1896 91   HOH HOH A . 
G 7 HOH 92   1897 92   HOH HOH A . 
G 7 HOH 93   1898 93   HOH HOH A . 
G 7 HOH 94   1899 94   HOH HOH A . 
G 7 HOH 95   1900 95   HOH HOH A . 
G 7 HOH 96   1901 96   HOH HOH A . 
G 7 HOH 97   1902 97   HOH HOH A . 
G 7 HOH 98   1903 98   HOH HOH A . 
G 7 HOH 99   1904 99   HOH HOH A . 
G 7 HOH 100  1905 100  HOH HOH A . 
G 7 HOH 101  1906 101  HOH HOH A . 
G 7 HOH 102  1907 102  HOH HOH A . 
G 7 HOH 103  1908 103  HOH HOH A . 
G 7 HOH 104  1909 104  HOH HOH A . 
G 7 HOH 105  1910 105  HOH HOH A . 
G 7 HOH 106  1911 106  HOH HOH A . 
G 7 HOH 107  1912 107  HOH HOH A . 
G 7 HOH 108  1913 108  HOH HOH A . 
G 7 HOH 109  1914 109  HOH HOH A . 
G 7 HOH 110  1915 110  HOH HOH A . 
G 7 HOH 111  1916 111  HOH HOH A . 
G 7 HOH 112  1917 112  HOH HOH A . 
G 7 HOH 113  1918 113  HOH HOH A . 
G 7 HOH 114  1919 114  HOH HOH A . 
G 7 HOH 115  1920 115  HOH HOH A . 
G 7 HOH 116  1921 116  HOH HOH A . 
G 7 HOH 117  1922 117  HOH HOH A . 
G 7 HOH 118  1923 118  HOH HOH A . 
G 7 HOH 119  1924 119  HOH HOH A . 
G 7 HOH 120  1925 120  HOH HOH A . 
G 7 HOH 121  1926 121  HOH HOH A . 
G 7 HOH 122  1927 122  HOH HOH A . 
G 7 HOH 123  1928 123  HOH HOH A . 
G 7 HOH 124  1929 124  HOH HOH A . 
G 7 HOH 125  1930 125  HOH HOH A . 
G 7 HOH 126  1931 126  HOH HOH A . 
G 7 HOH 127  1932 127  HOH HOH A . 
G 7 HOH 128  1933 128  HOH HOH A . 
G 7 HOH 129  1934 129  HOH HOH A . 
G 7 HOH 130  1935 130  HOH HOH A . 
G 7 HOH 131  1936 131  HOH HOH A . 
G 7 HOH 132  1937 132  HOH HOH A . 
G 7 HOH 133  1938 133  HOH HOH A . 
G 7 HOH 134  1939 134  HOH HOH A . 
G 7 HOH 135  1940 135  HOH HOH A . 
G 7 HOH 136  1941 136  HOH HOH A . 
G 7 HOH 137  1942 137  HOH HOH A . 
G 7 HOH 138  1943 138  HOH HOH A . 
G 7 HOH 139  1944 139  HOH HOH A . 
G 7 HOH 140  1945 140  HOH HOH A . 
G 7 HOH 141  1946 141  HOH HOH A . 
G 7 HOH 142  1947 142  HOH HOH A . 
G 7 HOH 143  1948 143  HOH HOH A . 
G 7 HOH 144  1949 144  HOH HOH A . 
G 7 HOH 145  1950 145  HOH HOH A . 
G 7 HOH 146  1951 146  HOH HOH A . 
G 7 HOH 147  1952 147  HOH HOH A . 
G 7 HOH 148  1953 148  HOH HOH A . 
G 7 HOH 149  1954 149  HOH HOH A . 
G 7 HOH 150  1955 150  HOH HOH A . 
G 7 HOH 151  1956 151  HOH HOH A . 
G 7 HOH 152  1957 152  HOH HOH A . 
G 7 HOH 153  1958 153  HOH HOH A . 
G 7 HOH 154  1959 154  HOH HOH A . 
G 7 HOH 155  1960 155  HOH HOH A . 
G 7 HOH 156  1961 156  HOH HOH A . 
G 7 HOH 157  1962 157  HOH HOH A . 
G 7 HOH 158  1963 158  HOH HOH A . 
G 7 HOH 159  1964 159  HOH HOH A . 
G 7 HOH 160  1965 160  HOH HOH A . 
G 7 HOH 161  1966 161  HOH HOH A . 
G 7 HOH 162  1967 162  HOH HOH A . 
G 7 HOH 163  1968 163  HOH HOH A . 
G 7 HOH 164  1969 164  HOH HOH A . 
G 7 HOH 165  1970 165  HOH HOH A . 
G 7 HOH 166  1971 166  HOH HOH A . 
G 7 HOH 167  1972 167  HOH HOH A . 
G 7 HOH 168  1973 168  HOH HOH A . 
G 7 HOH 169  1974 169  HOH HOH A . 
G 7 HOH 170  1975 170  HOH HOH A . 
G 7 HOH 171  1976 171  HOH HOH A . 
G 7 HOH 172  1977 172  HOH HOH A . 
G 7 HOH 173  1978 173  HOH HOH A . 
G 7 HOH 174  1979 174  HOH HOH A . 
G 7 HOH 175  1980 175  HOH HOH A . 
G 7 HOH 176  1981 176  HOH HOH A . 
G 7 HOH 177  1982 177  HOH HOH A . 
G 7 HOH 178  1983 178  HOH HOH A . 
G 7 HOH 179  1984 179  HOH HOH A . 
G 7 HOH 180  1985 180  HOH HOH A . 
G 7 HOH 181  1986 181  HOH HOH A . 
G 7 HOH 182  1987 182  HOH HOH A . 
G 7 HOH 183  1988 183  HOH HOH A . 
G 7 HOH 184  1989 184  HOH HOH A . 
G 7 HOH 185  1990 185  HOH HOH A . 
G 7 HOH 186  1991 186  HOH HOH A . 
G 7 HOH 187  1992 187  HOH HOH A . 
G 7 HOH 188  1993 188  HOH HOH A . 
G 7 HOH 189  1994 189  HOH HOH A . 
G 7 HOH 190  1995 190  HOH HOH A . 
G 7 HOH 191  1996 191  HOH HOH A . 
G 7 HOH 192  1997 192  HOH HOH A . 
G 7 HOH 193  1998 193  HOH HOH A . 
G 7 HOH 194  1999 194  HOH HOH A . 
G 7 HOH 195  2000 195  HOH HOH A . 
G 7 HOH 196  2001 196  HOH HOH A . 
G 7 HOH 197  2002 197  HOH HOH A . 
G 7 HOH 198  2003 198  HOH HOH A . 
G 7 HOH 199  2004 199  HOH HOH A . 
G 7 HOH 200  2005 200  HOH HOH A . 
G 7 HOH 201  2006 201  HOH HOH A . 
G 7 HOH 202  2007 202  HOH HOH A . 
G 7 HOH 203  2008 203  HOH HOH A . 
G 7 HOH 204  2009 204  HOH HOH A . 
G 7 HOH 205  2010 205  HOH HOH A . 
G 7 HOH 206  2011 206  HOH HOH A . 
G 7 HOH 207  2012 207  HOH HOH A . 
G 7 HOH 208  2013 208  HOH HOH A . 
G 7 HOH 209  2014 209  HOH HOH A . 
G 7 HOH 210  2015 210  HOH HOH A . 
G 7 HOH 211  2016 211  HOH HOH A . 
G 7 HOH 212  2017 212  HOH HOH A . 
G 7 HOH 213  2018 213  HOH HOH A . 
G 7 HOH 214  2019 214  HOH HOH A . 
G 7 HOH 215  2020 215  HOH HOH A . 
G 7 HOH 216  2021 216  HOH HOH A . 
G 7 HOH 217  2022 217  HOH HOH A . 
G 7 HOH 218  2023 218  HOH HOH A . 
G 7 HOH 219  2024 219  HOH HOH A . 
G 7 HOH 220  2025 220  HOH HOH A . 
G 7 HOH 221  2026 221  HOH HOH A . 
G 7 HOH 222  2027 222  HOH HOH A . 
G 7 HOH 223  2028 223  HOH HOH A . 
G 7 HOH 224  2029 224  HOH HOH A . 
G 7 HOH 225  2030 225  HOH HOH A . 
G 7 HOH 226  2031 226  HOH HOH A . 
G 7 HOH 227  2032 227  HOH HOH A . 
G 7 HOH 228  2033 228  HOH HOH A . 
G 7 HOH 229  2034 229  HOH HOH A . 
G 7 HOH 230  2035 230  HOH HOH A . 
G 7 HOH 231  2036 231  HOH HOH A . 
G 7 HOH 232  2037 232  HOH HOH A . 
G 7 HOH 233  2038 233  HOH HOH A . 
G 7 HOH 234  2039 234  HOH HOH A . 
G 7 HOH 235  2040 235  HOH HOH A . 
G 7 HOH 236  2041 236  HOH HOH A . 
G 7 HOH 237  2042 237  HOH HOH A . 
G 7 HOH 238  2043 238  HOH HOH A . 
G 7 HOH 239  2044 239  HOH HOH A . 
G 7 HOH 240  2045 240  HOH HOH A . 
G 7 HOH 241  2046 241  HOH HOH A . 
G 7 HOH 242  2047 242  HOH HOH A . 
G 7 HOH 243  2048 243  HOH HOH A . 
G 7 HOH 244  2049 244  HOH HOH A . 
G 7 HOH 245  2050 245  HOH HOH A . 
G 7 HOH 246  2051 246  HOH HOH A . 
G 7 HOH 247  2052 247  HOH HOH A . 
G 7 HOH 248  2053 248  HOH HOH A . 
G 7 HOH 249  2054 249  HOH HOH A . 
G 7 HOH 250  2055 250  HOH HOH A . 
G 7 HOH 251  2056 251  HOH HOH A . 
G 7 HOH 252  2057 252  HOH HOH A . 
G 7 HOH 253  2058 253  HOH HOH A . 
G 7 HOH 254  2059 254  HOH HOH A . 
G 7 HOH 255  2060 255  HOH HOH A . 
G 7 HOH 256  2061 256  HOH HOH A . 
G 7 HOH 257  2062 257  HOH HOH A . 
G 7 HOH 258  2063 258  HOH HOH A . 
G 7 HOH 259  2064 259  HOH HOH A . 
G 7 HOH 260  2065 260  HOH HOH A . 
G 7 HOH 261  2066 261  HOH HOH A . 
G 7 HOH 262  2067 262  HOH HOH A . 
G 7 HOH 263  2068 263  HOH HOH A . 
G 7 HOH 264  2069 264  HOH HOH A . 
G 7 HOH 265  2070 265  HOH HOH A . 
G 7 HOH 266  2071 266  HOH HOH A . 
G 7 HOH 267  2072 267  HOH HOH A . 
G 7 HOH 268  2073 268  HOH HOH A . 
G 7 HOH 269  2074 269  HOH HOH A . 
G 7 HOH 270  2075 270  HOH HOH A . 
G 7 HOH 271  2076 271  HOH HOH A . 
G 7 HOH 272  2077 272  HOH HOH A . 
G 7 HOH 273  2078 273  HOH HOH A . 
G 7 HOH 274  2079 274  HOH HOH A . 
G 7 HOH 275  2080 275  HOH HOH A . 
G 7 HOH 276  2081 276  HOH HOH A . 
G 7 HOH 277  2082 277  HOH HOH A . 
G 7 HOH 278  2083 278  HOH HOH A . 
G 7 HOH 279  2084 279  HOH HOH A . 
G 7 HOH 280  2085 280  HOH HOH A . 
G 7 HOH 281  2086 281  HOH HOH A . 
G 7 HOH 282  2087 282  HOH HOH A . 
G 7 HOH 283  2088 283  HOH HOH A . 
G 7 HOH 284  2089 284  HOH HOH A . 
G 7 HOH 285  2090 285  HOH HOH A . 
G 7 HOH 286  2091 286  HOH HOH A . 
G 7 HOH 287  2092 287  HOH HOH A . 
G 7 HOH 288  2093 288  HOH HOH A . 
G 7 HOH 289  2094 289  HOH HOH A . 
G 7 HOH 290  2095 290  HOH HOH A . 
G 7 HOH 291  2096 291  HOH HOH A . 
G 7 HOH 292  2097 292  HOH HOH A . 
G 7 HOH 293  2098 293  HOH HOH A . 
G 7 HOH 294  2099 294  HOH HOH A . 
G 7 HOH 295  2100 295  HOH HOH A . 
G 7 HOH 296  2101 296  HOH HOH A . 
G 7 HOH 297  2102 297  HOH HOH A . 
G 7 HOH 298  2103 298  HOH HOH A . 
G 7 HOH 299  2104 299  HOH HOH A . 
G 7 HOH 300  2105 300  HOH HOH A . 
G 7 HOH 301  2106 301  HOH HOH A . 
G 7 HOH 302  2107 302  HOH HOH A . 
G 7 HOH 303  2108 303  HOH HOH A . 
G 7 HOH 304  2109 304  HOH HOH A . 
G 7 HOH 305  2110 305  HOH HOH A . 
G 7 HOH 306  2111 306  HOH HOH A . 
G 7 HOH 307  2112 307  HOH HOH A . 
G 7 HOH 308  2113 308  HOH HOH A . 
G 7 HOH 309  2114 309  HOH HOH A . 
G 7 HOH 310  2115 310  HOH HOH A . 
G 7 HOH 311  2116 311  HOH HOH A . 
G 7 HOH 312  2117 312  HOH HOH A . 
G 7 HOH 313  2118 313  HOH HOH A . 
G 7 HOH 314  2119 314  HOH HOH A . 
G 7 HOH 315  2120 315  HOH HOH A . 
G 7 HOH 316  2121 316  HOH HOH A . 
G 7 HOH 317  2122 317  HOH HOH A . 
G 7 HOH 318  2123 318  HOH HOH A . 
G 7 HOH 319  2124 319  HOH HOH A . 
G 7 HOH 320  2125 320  HOH HOH A . 
G 7 HOH 321  2126 321  HOH HOH A . 
G 7 HOH 322  2127 322  HOH HOH A . 
G 7 HOH 323  2128 323  HOH HOH A . 
G 7 HOH 324  2129 324  HOH HOH A . 
G 7 HOH 325  2130 325  HOH HOH A . 
G 7 HOH 326  2131 326  HOH HOH A . 
G 7 HOH 327  2132 327  HOH HOH A . 
G 7 HOH 328  2133 328  HOH HOH A . 
G 7 HOH 329  2134 329  HOH HOH A . 
G 7 HOH 330  2135 330  HOH HOH A . 
G 7 HOH 331  2136 331  HOH HOH A . 
G 7 HOH 332  2137 332  HOH HOH A . 
G 7 HOH 333  2138 333  HOH HOH A . 
G 7 HOH 334  2139 334  HOH HOH A . 
G 7 HOH 335  2140 335  HOH HOH A . 
G 7 HOH 336  2141 336  HOH HOH A . 
G 7 HOH 337  2142 337  HOH HOH A . 
G 7 HOH 338  2143 338  HOH HOH A . 
G 7 HOH 339  2144 339  HOH HOH A . 
G 7 HOH 340  2145 340  HOH HOH A . 
G 7 HOH 341  2146 341  HOH HOH A . 
G 7 HOH 342  2147 342  HOH HOH A . 
G 7 HOH 343  2148 343  HOH HOH A . 
G 7 HOH 344  2149 344  HOH HOH A . 
G 7 HOH 345  2150 345  HOH HOH A . 
G 7 HOH 346  2151 346  HOH HOH A . 
G 7 HOH 347  2152 347  HOH HOH A . 
G 7 HOH 348  2153 348  HOH HOH A . 
G 7 HOH 349  2154 349  HOH HOH A . 
G 7 HOH 350  2155 350  HOH HOH A . 
G 7 HOH 351  2156 351  HOH HOH A . 
G 7 HOH 352  2157 352  HOH HOH A . 
G 7 HOH 353  2158 353  HOH HOH A . 
G 7 HOH 354  2159 354  HOH HOH A . 
G 7 HOH 355  2160 355  HOH HOH A . 
G 7 HOH 356  2161 356  HOH HOH A . 
G 7 HOH 357  2162 357  HOH HOH A . 
G 7 HOH 358  2163 358  HOH HOH A . 
G 7 HOH 359  2164 359  HOH HOH A . 
G 7 HOH 360  2165 360  HOH HOH A . 
G 7 HOH 361  2166 361  HOH HOH A . 
G 7 HOH 362  2167 362  HOH HOH A . 
G 7 HOH 363  2168 363  HOH HOH A . 
G 7 HOH 364  2169 364  HOH HOH A . 
G 7 HOH 365  2170 365  HOH HOH A . 
G 7 HOH 366  2171 366  HOH HOH A . 
G 7 HOH 367  2172 367  HOH HOH A . 
G 7 HOH 368  2173 368  HOH HOH A . 
G 7 HOH 369  2174 369  HOH HOH A . 
G 7 HOH 370  2175 370  HOH HOH A . 
G 7 HOH 371  2176 371  HOH HOH A . 
G 7 HOH 372  2177 372  HOH HOH A . 
G 7 HOH 373  2178 373  HOH HOH A . 
G 7 HOH 374  2179 374  HOH HOH A . 
G 7 HOH 375  2180 375  HOH HOH A . 
G 7 HOH 376  2181 376  HOH HOH A . 
G 7 HOH 377  2182 377  HOH HOH A . 
G 7 HOH 378  2183 378  HOH HOH A . 
G 7 HOH 379  2184 379  HOH HOH A . 
G 7 HOH 380  2185 380  HOH HOH A . 
G 7 HOH 381  2186 381  HOH HOH A . 
G 7 HOH 382  2187 382  HOH HOH A . 
G 7 HOH 383  2188 383  HOH HOH A . 
G 7 HOH 384  2189 384  HOH HOH A . 
G 7 HOH 385  2190 385  HOH HOH A . 
G 7 HOH 386  2191 386  HOH HOH A . 
G 7 HOH 387  2192 387  HOH HOH A . 
G 7 HOH 388  2193 388  HOH HOH A . 
G 7 HOH 389  2194 389  HOH HOH A . 
G 7 HOH 390  2195 390  HOH HOH A . 
G 7 HOH 391  2196 391  HOH HOH A . 
G 7 HOH 392  2197 392  HOH HOH A . 
G 7 HOH 393  2198 393  HOH HOH A . 
G 7 HOH 394  2199 394  HOH HOH A . 
G 7 HOH 395  2200 395  HOH HOH A . 
G 7 HOH 396  2201 396  HOH HOH A . 
G 7 HOH 397  2202 397  HOH HOH A . 
G 7 HOH 398  2203 398  HOH HOH A . 
G 7 HOH 399  2204 399  HOH HOH A . 
G 7 HOH 400  2205 400  HOH HOH A . 
G 7 HOH 401  2206 401  HOH HOH A . 
G 7 HOH 402  2207 402  HOH HOH A . 
G 7 HOH 403  2208 403  HOH HOH A . 
G 7 HOH 404  2209 404  HOH HOH A . 
G 7 HOH 405  2210 405  HOH HOH A . 
G 7 HOH 406  2211 406  HOH HOH A . 
G 7 HOH 407  2212 407  HOH HOH A . 
G 7 HOH 408  2213 408  HOH HOH A . 
G 7 HOH 409  2214 409  HOH HOH A . 
G 7 HOH 410  2215 410  HOH HOH A . 
G 7 HOH 411  2216 411  HOH HOH A . 
G 7 HOH 412  2217 412  HOH HOH A . 
G 7 HOH 413  2218 413  HOH HOH A . 
G 7 HOH 414  2219 414  HOH HOH A . 
G 7 HOH 415  2220 415  HOH HOH A . 
G 7 HOH 416  2221 416  HOH HOH A . 
G 7 HOH 417  2222 417  HOH HOH A . 
G 7 HOH 418  2223 418  HOH HOH A . 
G 7 HOH 419  2224 419  HOH HOH A . 
G 7 HOH 420  2225 420  HOH HOH A . 
G 7 HOH 421  2226 421  HOH HOH A . 
G 7 HOH 422  2227 422  HOH HOH A . 
G 7 HOH 423  2228 423  HOH HOH A . 
G 7 HOH 424  2229 424  HOH HOH A . 
G 7 HOH 425  2230 425  HOH HOH A . 
G 7 HOH 426  2231 426  HOH HOH A . 
G 7 HOH 427  2232 427  HOH HOH A . 
G 7 HOH 428  2233 428  HOH HOH A . 
G 7 HOH 429  2234 429  HOH HOH A . 
G 7 HOH 430  2235 430  HOH HOH A . 
G 7 HOH 431  2236 431  HOH HOH A . 
G 7 HOH 432  2237 432  HOH HOH A . 
G 7 HOH 433  2238 433  HOH HOH A . 
G 7 HOH 434  2239 434  HOH HOH A . 
G 7 HOH 435  2240 435  HOH HOH A . 
G 7 HOH 436  2241 436  HOH HOH A . 
G 7 HOH 437  2242 437  HOH HOH A . 
G 7 HOH 438  2243 438  HOH HOH A . 
G 7 HOH 439  2244 439  HOH HOH A . 
G 7 HOH 440  2245 440  HOH HOH A . 
G 7 HOH 441  2246 441  HOH HOH A . 
G 7 HOH 442  2247 442  HOH HOH A . 
G 7 HOH 443  2248 443  HOH HOH A . 
G 7 HOH 444  2249 444  HOH HOH A . 
G 7 HOH 445  2250 445  HOH HOH A . 
G 7 HOH 446  2251 446  HOH HOH A . 
G 7 HOH 447  2252 447  HOH HOH A . 
G 7 HOH 448  2253 448  HOH HOH A . 
G 7 HOH 449  2254 449  HOH HOH A . 
G 7 HOH 450  2255 450  HOH HOH A . 
G 7 HOH 451  2256 451  HOH HOH A . 
G 7 HOH 452  2257 452  HOH HOH A . 
G 7 HOH 453  2258 453  HOH HOH A . 
G 7 HOH 454  2259 454  HOH HOH A . 
G 7 HOH 455  2260 455  HOH HOH A . 
G 7 HOH 456  2261 456  HOH HOH A . 
G 7 HOH 457  2262 457  HOH HOH A . 
G 7 HOH 458  2263 458  HOH HOH A . 
G 7 HOH 459  2264 459  HOH HOH A . 
G 7 HOH 460  2265 460  HOH HOH A . 
G 7 HOH 461  2266 461  HOH HOH A . 
G 7 HOH 462  2267 462  HOH HOH A . 
G 7 HOH 463  2268 463  HOH HOH A . 
G 7 HOH 464  2269 464  HOH HOH A . 
G 7 HOH 465  2270 465  HOH HOH A . 
G 7 HOH 466  2271 466  HOH HOH A . 
G 7 HOH 467  2272 467  HOH HOH A . 
G 7 HOH 468  2273 468  HOH HOH A . 
G 7 HOH 469  2274 469  HOH HOH A . 
G 7 HOH 470  2275 470  HOH HOH A . 
G 7 HOH 471  2276 471  HOH HOH A . 
G 7 HOH 472  2277 472  HOH HOH A . 
G 7 HOH 473  2278 473  HOH HOH A . 
G 7 HOH 474  2279 474  HOH HOH A . 
G 7 HOH 475  2280 475  HOH HOH A . 
G 7 HOH 476  2281 476  HOH HOH A . 
G 7 HOH 477  2282 477  HOH HOH A . 
G 7 HOH 478  2283 478  HOH HOH A . 
G 7 HOH 479  2284 479  HOH HOH A . 
G 7 HOH 480  2285 480  HOH HOH A . 
G 7 HOH 481  2286 481  HOH HOH A . 
G 7 HOH 482  2287 482  HOH HOH A . 
G 7 HOH 483  2288 483  HOH HOH A . 
G 7 HOH 484  2289 484  HOH HOH A . 
G 7 HOH 485  2290 485  HOH HOH A . 
G 7 HOH 486  2291 486  HOH HOH A . 
G 7 HOH 487  2292 487  HOH HOH A . 
G 7 HOH 488  2293 488  HOH HOH A . 
G 7 HOH 489  2294 489  HOH HOH A . 
G 7 HOH 490  2295 490  HOH HOH A . 
G 7 HOH 491  2296 491  HOH HOH A . 
G 7 HOH 492  2297 492  HOH HOH A . 
G 7 HOH 493  2298 493  HOH HOH A . 
G 7 HOH 494  2299 494  HOH HOH A . 
G 7 HOH 495  2300 495  HOH HOH A . 
G 7 HOH 496  2301 496  HOH HOH A . 
G 7 HOH 497  2302 497  HOH HOH A . 
G 7 HOH 498  2303 498  HOH HOH A . 
G 7 HOH 499  2304 499  HOH HOH A . 
G 7 HOH 500  2305 500  HOH HOH A . 
G 7 HOH 501  2306 501  HOH HOH A . 
G 7 HOH 502  2307 502  HOH HOH A . 
G 7 HOH 503  2308 503  HOH HOH A . 
G 7 HOH 504  2309 504  HOH HOH A . 
G 7 HOH 505  2310 505  HOH HOH A . 
G 7 HOH 506  2311 506  HOH HOH A . 
G 7 HOH 507  2312 507  HOH HOH A . 
G 7 HOH 508  2313 508  HOH HOH A . 
G 7 HOH 509  2314 509  HOH HOH A . 
G 7 HOH 510  2315 510  HOH HOH A . 
G 7 HOH 511  2316 511  HOH HOH A . 
G 7 HOH 512  2317 512  HOH HOH A . 
G 7 HOH 513  2318 513  HOH HOH A . 
G 7 HOH 514  2319 514  HOH HOH A . 
G 7 HOH 515  2320 515  HOH HOH A . 
G 7 HOH 516  2321 516  HOH HOH A . 
G 7 HOH 517  2322 517  HOH HOH A . 
G 7 HOH 518  2323 518  HOH HOH A . 
G 7 HOH 519  2324 519  HOH HOH A . 
G 7 HOH 520  2325 520  HOH HOH A . 
G 7 HOH 521  2326 521  HOH HOH A . 
G 7 HOH 522  2327 522  HOH HOH A . 
G 7 HOH 523  2328 523  HOH HOH A . 
G 7 HOH 524  2329 524  HOH HOH A . 
G 7 HOH 525  2330 525  HOH HOH A . 
G 7 HOH 526  2331 526  HOH HOH A . 
G 7 HOH 527  2332 527  HOH HOH A . 
G 7 HOH 528  2333 528  HOH HOH A . 
G 7 HOH 529  2334 529  HOH HOH A . 
G 7 HOH 530  2335 530  HOH HOH A . 
G 7 HOH 531  2336 531  HOH HOH A . 
G 7 HOH 532  2337 532  HOH HOH A . 
G 7 HOH 533  2338 533  HOH HOH A . 
G 7 HOH 534  2339 534  HOH HOH A . 
G 7 HOH 535  2340 535  HOH HOH A . 
G 7 HOH 536  2341 536  HOH HOH A . 
G 7 HOH 537  2342 537  HOH HOH A . 
G 7 HOH 538  2343 538  HOH HOH A . 
G 7 HOH 539  2344 539  HOH HOH A . 
G 7 HOH 540  2345 540  HOH HOH A . 
G 7 HOH 541  2346 541  HOH HOH A . 
G 7 HOH 542  2347 542  HOH HOH A . 
G 7 HOH 543  2348 543  HOH HOH A . 
G 7 HOH 544  2349 544  HOH HOH A . 
G 7 HOH 545  2350 545  HOH HOH A . 
G 7 HOH 546  2351 546  HOH HOH A . 
G 7 HOH 547  2352 547  HOH HOH A . 
G 7 HOH 548  2353 548  HOH HOH A . 
G 7 HOH 549  2354 549  HOH HOH A . 
G 7 HOH 550  2355 550  HOH HOH A . 
G 7 HOH 551  2356 551  HOH HOH A . 
G 7 HOH 552  2357 552  HOH HOH A . 
G 7 HOH 553  2358 553  HOH HOH A . 
G 7 HOH 554  2359 554  HOH HOH A . 
G 7 HOH 555  2360 555  HOH HOH A . 
G 7 HOH 556  2361 556  HOH HOH A . 
G 7 HOH 557  2362 557  HOH HOH A . 
G 7 HOH 558  2363 558  HOH HOH A . 
G 7 HOH 559  2364 559  HOH HOH A . 
G 7 HOH 560  2365 560  HOH HOH A . 
G 7 HOH 561  2366 561  HOH HOH A . 
G 7 HOH 562  2367 562  HOH HOH A . 
G 7 HOH 563  2368 563  HOH HOH A . 
G 7 HOH 564  2369 564  HOH HOH A . 
G 7 HOH 565  2370 565  HOH HOH A . 
G 7 HOH 566  2371 566  HOH HOH A . 
G 7 HOH 567  2372 567  HOH HOH A . 
G 7 HOH 568  2373 568  HOH HOH A . 
G 7 HOH 569  2374 569  HOH HOH A . 
G 7 HOH 570  2375 570  HOH HOH A . 
G 7 HOH 571  2376 571  HOH HOH A . 
G 7 HOH 572  2377 572  HOH HOH A . 
G 7 HOH 573  2378 573  HOH HOH A . 
G 7 HOH 574  2379 574  HOH HOH A . 
G 7 HOH 575  2380 575  HOH HOH A . 
G 7 HOH 576  2381 576  HOH HOH A . 
G 7 HOH 577  2382 577  HOH HOH A . 
G 7 HOH 578  2383 578  HOH HOH A . 
G 7 HOH 579  2384 579  HOH HOH A . 
G 7 HOH 580  2385 580  HOH HOH A . 
G 7 HOH 581  2386 581  HOH HOH A . 
G 7 HOH 582  2387 582  HOH HOH A . 
G 7 HOH 583  2388 583  HOH HOH A . 
G 7 HOH 584  2389 584  HOH HOH A . 
G 7 HOH 585  2390 585  HOH HOH A . 
G 7 HOH 586  2391 586  HOH HOH A . 
G 7 HOH 587  2392 587  HOH HOH A . 
G 7 HOH 588  2393 588  HOH HOH A . 
G 7 HOH 589  2394 589  HOH HOH A . 
G 7 HOH 590  2395 590  HOH HOH A . 
G 7 HOH 591  2396 591  HOH HOH A . 
G 7 HOH 592  2397 592  HOH HOH A . 
G 7 HOH 593  2398 593  HOH HOH A . 
G 7 HOH 594  2399 594  HOH HOH A . 
G 7 HOH 595  2400 595  HOH HOH A . 
G 7 HOH 596  2401 596  HOH HOH A . 
G 7 HOH 597  2402 597  HOH HOH A . 
G 7 HOH 598  2403 598  HOH HOH A . 
G 7 HOH 599  2404 599  HOH HOH A . 
G 7 HOH 600  2405 600  HOH HOH A . 
G 7 HOH 601  2406 601  HOH HOH A . 
G 7 HOH 602  2407 602  HOH HOH A . 
G 7 HOH 603  2408 603  HOH HOH A . 
G 7 HOH 604  2409 604  HOH HOH A . 
G 7 HOH 605  2410 605  HOH HOH A . 
G 7 HOH 606  2411 606  HOH HOH A . 
G 7 HOH 607  2412 607  HOH HOH A . 
G 7 HOH 608  2413 608  HOH HOH A . 
G 7 HOH 609  2414 609  HOH HOH A . 
G 7 HOH 610  2415 610  HOH HOH A . 
G 7 HOH 611  2416 611  HOH HOH A . 
G 7 HOH 612  2417 612  HOH HOH A . 
G 7 HOH 613  2418 613  HOH HOH A . 
G 7 HOH 614  2419 614  HOH HOH A . 
G 7 HOH 615  2420 615  HOH HOH A . 
G 7 HOH 616  2421 616  HOH HOH A . 
G 7 HOH 617  2422 617  HOH HOH A . 
G 7 HOH 618  2423 618  HOH HOH A . 
G 7 HOH 619  2424 619  HOH HOH A . 
G 7 HOH 620  2425 620  HOH HOH A . 
G 7 HOH 621  2426 621  HOH HOH A . 
G 7 HOH 622  2427 622  HOH HOH A . 
G 7 HOH 623  2428 623  HOH HOH A . 
G 7 HOH 624  2429 624  HOH HOH A . 
G 7 HOH 625  2430 625  HOH HOH A . 
G 7 HOH 626  2431 626  HOH HOH A . 
G 7 HOH 627  2432 627  HOH HOH A . 
G 7 HOH 628  2433 628  HOH HOH A . 
G 7 HOH 629  2434 629  HOH HOH A . 
G 7 HOH 630  2435 630  HOH HOH A . 
G 7 HOH 631  2436 631  HOH HOH A . 
G 7 HOH 632  2437 632  HOH HOH A . 
G 7 HOH 633  2438 633  HOH HOH A . 
G 7 HOH 634  2439 634  HOH HOH A . 
G 7 HOH 635  2440 635  HOH HOH A . 
G 7 HOH 636  2441 636  HOH HOH A . 
G 7 HOH 637  2442 637  HOH HOH A . 
G 7 HOH 638  2443 638  HOH HOH A . 
G 7 HOH 639  2444 639  HOH HOH A . 
G 7 HOH 640  2445 640  HOH HOH A . 
G 7 HOH 641  2446 641  HOH HOH A . 
G 7 HOH 642  2447 642  HOH HOH A . 
G 7 HOH 643  2448 643  HOH HOH A . 
G 7 HOH 644  2449 644  HOH HOH A . 
G 7 HOH 645  2450 645  HOH HOH A . 
G 7 HOH 646  2451 646  HOH HOH A . 
G 7 HOH 647  2452 647  HOH HOH A . 
G 7 HOH 648  2453 648  HOH HOH A . 
G 7 HOH 649  2454 649  HOH HOH A . 
G 7 HOH 650  2455 650  HOH HOH A . 
G 7 HOH 651  2456 651  HOH HOH A . 
G 7 HOH 652  2457 652  HOH HOH A . 
G 7 HOH 653  2458 653  HOH HOH A . 
G 7 HOH 654  2459 654  HOH HOH A . 
G 7 HOH 655  2460 655  HOH HOH A . 
G 7 HOH 656  2461 656  HOH HOH A . 
G 7 HOH 657  2462 657  HOH HOH A . 
G 7 HOH 658  2463 658  HOH HOH A . 
G 7 HOH 659  2464 659  HOH HOH A . 
G 7 HOH 660  2465 660  HOH HOH A . 
G 7 HOH 661  2466 661  HOH HOH A . 
G 7 HOH 662  2467 662  HOH HOH A . 
G 7 HOH 663  2468 663  HOH HOH A . 
G 7 HOH 664  2469 664  HOH HOH A . 
G 7 HOH 665  2470 665  HOH HOH A . 
G 7 HOH 666  2471 666  HOH HOH A . 
G 7 HOH 667  2472 667  HOH HOH A . 
G 7 HOH 668  2473 668  HOH HOH A . 
G 7 HOH 669  2474 669  HOH HOH A . 
G 7 HOH 670  2475 670  HOH HOH A . 
G 7 HOH 671  2476 671  HOH HOH A . 
G 7 HOH 672  2477 672  HOH HOH A . 
G 7 HOH 673  2478 673  HOH HOH A . 
G 7 HOH 674  2479 674  HOH HOH A . 
G 7 HOH 675  2480 675  HOH HOH A . 
G 7 HOH 676  2481 676  HOH HOH A . 
G 7 HOH 677  2482 677  HOH HOH A . 
G 7 HOH 678  2483 678  HOH HOH A . 
G 7 HOH 679  2484 679  HOH HOH A . 
G 7 HOH 680  2485 680  HOH HOH A . 
G 7 HOH 681  2486 681  HOH HOH A . 
G 7 HOH 682  2487 682  HOH HOH A . 
G 7 HOH 683  2488 683  HOH HOH A . 
G 7 HOH 684  2489 684  HOH HOH A . 
G 7 HOH 685  2490 685  HOH HOH A . 
G 7 HOH 686  2491 686  HOH HOH A . 
G 7 HOH 687  2492 687  HOH HOH A . 
G 7 HOH 688  2493 688  HOH HOH A . 
G 7 HOH 689  2494 689  HOH HOH A . 
G 7 HOH 690  2495 690  HOH HOH A . 
G 7 HOH 691  2496 691  HOH HOH A . 
G 7 HOH 692  2497 692  HOH HOH A . 
G 7 HOH 693  2498 693  HOH HOH A . 
G 7 HOH 694  2499 694  HOH HOH A . 
G 7 HOH 695  2500 695  HOH HOH A . 
G 7 HOH 696  2501 696  HOH HOH A . 
G 7 HOH 697  2502 697  HOH HOH A . 
G 7 HOH 698  2503 698  HOH HOH A . 
G 7 HOH 699  2504 699  HOH HOH A . 
G 7 HOH 700  2505 700  HOH HOH A . 
G 7 HOH 701  2506 701  HOH HOH A . 
G 7 HOH 702  2507 702  HOH HOH A . 
G 7 HOH 703  2508 703  HOH HOH A . 
G 7 HOH 704  2509 704  HOH HOH A . 
G 7 HOH 705  2510 705  HOH HOH A . 
G 7 HOH 706  2511 706  HOH HOH A . 
G 7 HOH 707  2512 707  HOH HOH A . 
G 7 HOH 708  2513 708  HOH HOH A . 
G 7 HOH 709  2514 709  HOH HOH A . 
G 7 HOH 710  2515 710  HOH HOH A . 
G 7 HOH 711  2516 711  HOH HOH A . 
G 7 HOH 712  2517 712  HOH HOH A . 
G 7 HOH 713  2518 713  HOH HOH A . 
G 7 HOH 714  2519 714  HOH HOH A . 
G 7 HOH 715  2520 715  HOH HOH A . 
G 7 HOH 716  2521 716  HOH HOH A . 
G 7 HOH 717  2522 717  HOH HOH A . 
G 7 HOH 718  2523 718  HOH HOH A . 
G 7 HOH 719  2524 719  HOH HOH A . 
G 7 HOH 720  2525 720  HOH HOH A . 
G 7 HOH 721  2526 721  HOH HOH A . 
G 7 HOH 722  2527 722  HOH HOH A . 
G 7 HOH 723  2528 723  HOH HOH A . 
G 7 HOH 724  2529 724  HOH HOH A . 
G 7 HOH 725  2530 725  HOH HOH A . 
G 7 HOH 726  2531 726  HOH HOH A . 
G 7 HOH 727  2532 727  HOH HOH A . 
G 7 HOH 728  2533 728  HOH HOH A . 
G 7 HOH 729  2534 729  HOH HOH A . 
G 7 HOH 730  2535 730  HOH HOH A . 
G 7 HOH 731  2536 731  HOH HOH A . 
G 7 HOH 732  2537 732  HOH HOH A . 
G 7 HOH 733  2538 733  HOH HOH A . 
G 7 HOH 734  2539 734  HOH HOH A . 
G 7 HOH 735  2540 735  HOH HOH A . 
G 7 HOH 736  2541 736  HOH HOH A . 
G 7 HOH 737  2542 737  HOH HOH A . 
G 7 HOH 738  2543 738  HOH HOH A . 
G 7 HOH 739  2544 739  HOH HOH A . 
G 7 HOH 740  2545 740  HOH HOH A . 
G 7 HOH 741  2546 741  HOH HOH A . 
G 7 HOH 742  2547 742  HOH HOH A . 
G 7 HOH 743  2548 743  HOH HOH A . 
G 7 HOH 744  2549 744  HOH HOH A . 
G 7 HOH 745  2550 745  HOH HOH A . 
G 7 HOH 746  2551 746  HOH HOH A . 
G 7 HOH 747  2552 747  HOH HOH A . 
G 7 HOH 748  2553 748  HOH HOH A . 
G 7 HOH 749  2554 749  HOH HOH A . 
G 7 HOH 750  2555 750  HOH HOH A . 
G 7 HOH 751  2556 751  HOH HOH A . 
G 7 HOH 752  2557 752  HOH HOH A . 
G 7 HOH 753  2558 753  HOH HOH A . 
G 7 HOH 754  2559 754  HOH HOH A . 
G 7 HOH 755  2560 755  HOH HOH A . 
G 7 HOH 756  2561 756  HOH HOH A . 
G 7 HOH 757  2562 757  HOH HOH A . 
G 7 HOH 758  2563 758  HOH HOH A . 
G 7 HOH 759  2564 759  HOH HOH A . 
G 7 HOH 760  2565 760  HOH HOH A . 
G 7 HOH 761  2566 761  HOH HOH A . 
G 7 HOH 762  2567 762  HOH HOH A . 
G 7 HOH 763  2568 763  HOH HOH A . 
G 7 HOH 764  2569 764  HOH HOH A . 
G 7 HOH 765  2570 765  HOH HOH A . 
G 7 HOH 766  2571 766  HOH HOH A . 
G 7 HOH 767  2572 767  HOH HOH A . 
G 7 HOH 768  2573 768  HOH HOH A . 
G 7 HOH 769  2574 769  HOH HOH A . 
G 7 HOH 770  2575 770  HOH HOH A . 
G 7 HOH 771  2576 771  HOH HOH A . 
G 7 HOH 772  2577 772  HOH HOH A . 
G 7 HOH 773  2578 773  HOH HOH A . 
G 7 HOH 774  2579 774  HOH HOH A . 
G 7 HOH 775  2580 775  HOH HOH A . 
G 7 HOH 776  2581 776  HOH HOH A . 
G 7 HOH 777  2582 777  HOH HOH A . 
G 7 HOH 778  2583 778  HOH HOH A . 
G 7 HOH 779  2584 779  HOH HOH A . 
G 7 HOH 780  2585 780  HOH HOH A . 
G 7 HOH 781  2586 781  HOH HOH A . 
G 7 HOH 782  2587 782  HOH HOH A . 
G 7 HOH 783  2588 783  HOH HOH A . 
G 7 HOH 784  2589 784  HOH HOH A . 
G 7 HOH 785  2590 785  HOH HOH A . 
G 7 HOH 786  2591 786  HOH HOH A . 
G 7 HOH 787  2592 787  HOH HOH A . 
G 7 HOH 788  2593 788  HOH HOH A . 
G 7 HOH 789  2594 789  HOH HOH A . 
G 7 HOH 790  2595 790  HOH HOH A . 
G 7 HOH 791  2596 791  HOH HOH A . 
G 7 HOH 792  2597 792  HOH HOH A . 
G 7 HOH 793  2598 793  HOH HOH A . 
G 7 HOH 794  2599 794  HOH HOH A . 
G 7 HOH 795  2600 795  HOH HOH A . 
G 7 HOH 796  2601 796  HOH HOH A . 
G 7 HOH 797  2602 797  HOH HOH A . 
G 7 HOH 798  2603 798  HOH HOH A . 
G 7 HOH 799  2604 799  HOH HOH A . 
G 7 HOH 800  2605 800  HOH HOH A . 
G 7 HOH 801  2606 801  HOH HOH A . 
G 7 HOH 802  2607 802  HOH HOH A . 
G 7 HOH 803  2608 803  HOH HOH A . 
G 7 HOH 804  2609 804  HOH HOH A . 
G 7 HOH 805  2610 805  HOH HOH A . 
G 7 HOH 806  2611 806  HOH HOH A . 
G 7 HOH 807  2612 807  HOH HOH A . 
G 7 HOH 808  2613 808  HOH HOH A . 
G 7 HOH 809  2614 809  HOH HOH A . 
G 7 HOH 810  2615 810  HOH HOH A . 
G 7 HOH 811  2616 811  HOH HOH A . 
G 7 HOH 812  2617 812  HOH HOH A . 
G 7 HOH 813  2618 813  HOH HOH A . 
G 7 HOH 814  2619 814  HOH HOH A . 
G 7 HOH 815  2620 815  HOH HOH A . 
G 7 HOH 816  2621 816  HOH HOH A . 
G 7 HOH 817  2622 817  HOH HOH A . 
G 7 HOH 818  2623 818  HOH HOH A . 
G 7 HOH 819  2624 819  HOH HOH A . 
G 7 HOH 820  2625 820  HOH HOH A . 
G 7 HOH 821  2626 821  HOH HOH A . 
G 7 HOH 822  2627 822  HOH HOH A . 
G 7 HOH 823  2628 823  HOH HOH A . 
G 7 HOH 824  2629 824  HOH HOH A . 
G 7 HOH 825  2630 825  HOH HOH A . 
G 7 HOH 826  2631 826  HOH HOH A . 
G 7 HOH 827  2632 827  HOH HOH A . 
G 7 HOH 828  2633 828  HOH HOH A . 
G 7 HOH 829  2634 829  HOH HOH A . 
G 7 HOH 830  2635 830  HOH HOH A . 
G 7 HOH 831  2636 831  HOH HOH A . 
G 7 HOH 832  2637 832  HOH HOH A . 
G 7 HOH 833  2638 833  HOH HOH A . 
G 7 HOH 834  2639 834  HOH HOH A . 
G 7 HOH 835  2640 835  HOH HOH A . 
G 7 HOH 836  2641 836  HOH HOH A . 
G 7 HOH 837  2642 837  HOH HOH A . 
G 7 HOH 838  2643 838  HOH HOH A . 
G 7 HOH 839  2644 839  HOH HOH A . 
G 7 HOH 840  2645 840  HOH HOH A . 
G 7 HOH 841  2646 841  HOH HOH A . 
G 7 HOH 842  2647 842  HOH HOH A . 
G 7 HOH 843  2648 843  HOH HOH A . 
G 7 HOH 844  2649 844  HOH HOH A . 
G 7 HOH 845  2650 845  HOH HOH A . 
G 7 HOH 846  2651 846  HOH HOH A . 
G 7 HOH 847  2652 847  HOH HOH A . 
G 7 HOH 848  2653 848  HOH HOH A . 
G 7 HOH 849  2654 849  HOH HOH A . 
G 7 HOH 850  2655 850  HOH HOH A . 
G 7 HOH 851  2656 851  HOH HOH A . 
G 7 HOH 852  2657 852  HOH HOH A . 
G 7 HOH 853  2658 853  HOH HOH A . 
G 7 HOH 854  2659 854  HOH HOH A . 
G 7 HOH 855  2660 855  HOH HOH A . 
G 7 HOH 856  2661 856  HOH HOH A . 
G 7 HOH 857  2662 857  HOH HOH A . 
G 7 HOH 858  2663 858  HOH HOH A . 
G 7 HOH 859  2664 859  HOH HOH A . 
G 7 HOH 860  2665 860  HOH HOH A . 
G 7 HOH 861  2666 861  HOH HOH A . 
G 7 HOH 862  2667 862  HOH HOH A . 
G 7 HOH 863  2668 863  HOH HOH A . 
G 7 HOH 864  2669 864  HOH HOH A . 
G 7 HOH 865  2670 865  HOH HOH A . 
G 7 HOH 866  2671 866  HOH HOH A . 
G 7 HOH 867  2672 867  HOH HOH A . 
G 7 HOH 868  2673 868  HOH HOH A . 
G 7 HOH 869  2674 869  HOH HOH A . 
G 7 HOH 870  2675 870  HOH HOH A . 
G 7 HOH 871  2676 871  HOH HOH A . 
G 7 HOH 872  2677 872  HOH HOH A . 
G 7 HOH 873  2678 873  HOH HOH A . 
G 7 HOH 874  2679 874  HOH HOH A . 
G 7 HOH 875  2680 875  HOH HOH A . 
G 7 HOH 876  2681 876  HOH HOH A . 
G 7 HOH 877  2682 877  HOH HOH A . 
G 7 HOH 878  2683 878  HOH HOH A . 
G 7 HOH 879  2684 879  HOH HOH A . 
G 7 HOH 880  2685 880  HOH HOH A . 
G 7 HOH 881  2686 881  HOH HOH A . 
G 7 HOH 882  2687 882  HOH HOH A . 
G 7 HOH 883  2688 883  HOH HOH A . 
G 7 HOH 884  2689 884  HOH HOH A . 
G 7 HOH 885  2690 885  HOH HOH A . 
G 7 HOH 886  2691 886  HOH HOH A . 
G 7 HOH 887  2692 887  HOH HOH A . 
G 7 HOH 888  2693 888  HOH HOH A . 
G 7 HOH 889  2694 889  HOH HOH A . 
G 7 HOH 890  2695 890  HOH HOH A . 
G 7 HOH 891  2696 891  HOH HOH A . 
G 7 HOH 892  2697 892  HOH HOH A . 
G 7 HOH 893  2698 893  HOH HOH A . 
G 7 HOH 894  2699 894  HOH HOH A . 
G 7 HOH 895  2700 895  HOH HOH A . 
G 7 HOH 896  2701 896  HOH HOH A . 
G 7 HOH 897  2702 897  HOH HOH A . 
G 7 HOH 898  2703 898  HOH HOH A . 
G 7 HOH 899  2704 899  HOH HOH A . 
G 7 HOH 900  2705 900  HOH HOH A . 
G 7 HOH 901  2706 901  HOH HOH A . 
G 7 HOH 902  2707 902  HOH HOH A . 
G 7 HOH 903  2708 903  HOH HOH A . 
G 7 HOH 904  2709 904  HOH HOH A . 
G 7 HOH 905  2710 905  HOH HOH A . 
G 7 HOH 906  2711 906  HOH HOH A . 
G 7 HOH 907  2712 907  HOH HOH A . 
G 7 HOH 908  2713 908  HOH HOH A . 
G 7 HOH 909  2714 909  HOH HOH A . 
G 7 HOH 910  2715 910  HOH HOH A . 
G 7 HOH 911  2716 911  HOH HOH A . 
G 7 HOH 912  2717 912  HOH HOH A . 
G 7 HOH 913  2718 913  HOH HOH A . 
G 7 HOH 914  2719 914  HOH HOH A . 
G 7 HOH 915  2720 915  HOH HOH A . 
G 7 HOH 916  2721 916  HOH HOH A . 
G 7 HOH 917  2722 917  HOH HOH A . 
G 7 HOH 918  2723 918  HOH HOH A . 
G 7 HOH 919  2724 919  HOH HOH A . 
G 7 HOH 920  2725 920  HOH HOH A . 
G 7 HOH 921  2726 921  HOH HOH A . 
G 7 HOH 922  2727 922  HOH HOH A . 
G 7 HOH 923  2728 923  HOH HOH A . 
G 7 HOH 924  2729 924  HOH HOH A . 
G 7 HOH 925  2730 925  HOH HOH A . 
G 7 HOH 926  2731 926  HOH HOH A . 
G 7 HOH 927  2732 927  HOH HOH A . 
G 7 HOH 928  2733 928  HOH HOH A . 
G 7 HOH 929  2734 929  HOH HOH A . 
G 7 HOH 930  2735 930  HOH HOH A . 
G 7 HOH 931  2736 931  HOH HOH A . 
G 7 HOH 932  2737 932  HOH HOH A . 
G 7 HOH 933  2738 933  HOH HOH A . 
G 7 HOH 934  2739 934  HOH HOH A . 
G 7 HOH 935  2740 935  HOH HOH A . 
G 7 HOH 936  2741 936  HOH HOH A . 
G 7 HOH 937  2742 937  HOH HOH A . 
G 7 HOH 938  2743 938  HOH HOH A . 
G 7 HOH 939  2744 939  HOH HOH A . 
G 7 HOH 940  2745 940  HOH HOH A . 
G 7 HOH 941  2746 941  HOH HOH A . 
G 7 HOH 942  2747 942  HOH HOH A . 
G 7 HOH 943  2748 943  HOH HOH A . 
G 7 HOH 944  2749 944  HOH HOH A . 
G 7 HOH 945  2750 945  HOH HOH A . 
G 7 HOH 946  2751 946  HOH HOH A . 
G 7 HOH 947  2752 947  HOH HOH A . 
G 7 HOH 948  2753 948  HOH HOH A . 
G 7 HOH 949  2754 949  HOH HOH A . 
G 7 HOH 950  2755 950  HOH HOH A . 
G 7 HOH 951  2756 951  HOH HOH A . 
G 7 HOH 952  2757 952  HOH HOH A . 
G 7 HOH 953  2758 953  HOH HOH A . 
G 7 HOH 954  2759 954  HOH HOH A . 
G 7 HOH 955  2760 955  HOH HOH A . 
G 7 HOH 956  2761 956  HOH HOH A . 
G 7 HOH 957  2762 957  HOH HOH A . 
G 7 HOH 958  2763 958  HOH HOH A . 
G 7 HOH 959  2764 959  HOH HOH A . 
G 7 HOH 960  2765 960  HOH HOH A . 
G 7 HOH 961  2766 961  HOH HOH A . 
G 7 HOH 962  2767 962  HOH HOH A . 
G 7 HOH 963  2768 963  HOH HOH A . 
G 7 HOH 964  2769 964  HOH HOH A . 
G 7 HOH 965  2770 965  HOH HOH A . 
G 7 HOH 966  2771 966  HOH HOH A . 
G 7 HOH 967  2772 967  HOH HOH A . 
G 7 HOH 968  2773 968  HOH HOH A . 
G 7 HOH 969  2774 969  HOH HOH A . 
G 7 HOH 970  2775 970  HOH HOH A . 
G 7 HOH 971  2776 971  HOH HOH A . 
G 7 HOH 972  2777 972  HOH HOH A . 
G 7 HOH 973  2778 973  HOH HOH A . 
G 7 HOH 974  2779 974  HOH HOH A . 
G 7 HOH 975  2780 975  HOH HOH A . 
G 7 HOH 976  2781 976  HOH HOH A . 
G 7 HOH 977  2782 977  HOH HOH A . 
G 7 HOH 978  2783 978  HOH HOH A . 
G 7 HOH 979  2784 979  HOH HOH A . 
G 7 HOH 980  2785 980  HOH HOH A . 
G 7 HOH 981  2786 981  HOH HOH A . 
G 7 HOH 982  2787 982  HOH HOH A . 
G 7 HOH 983  2788 983  HOH HOH A . 
G 7 HOH 984  2789 984  HOH HOH A . 
G 7 HOH 985  2790 985  HOH HOH A . 
G 7 HOH 986  2791 986  HOH HOH A . 
G 7 HOH 987  2792 987  HOH HOH A . 
G 7 HOH 988  2793 988  HOH HOH A . 
G 7 HOH 989  2794 989  HOH HOH A . 
G 7 HOH 990  2795 990  HOH HOH A . 
G 7 HOH 991  2796 991  HOH HOH A . 
G 7 HOH 992  2797 992  HOH HOH A . 
G 7 HOH 993  2798 993  HOH HOH A . 
G 7 HOH 994  2799 994  HOH HOH A . 
G 7 HOH 995  2800 995  HOH HOH A . 
G 7 HOH 996  2801 996  HOH HOH A . 
G 7 HOH 997  2802 997  HOH HOH A . 
G 7 HOH 998  2803 998  HOH HOH A . 
G 7 HOH 999  2804 999  HOH HOH A . 
G 7 HOH 1000 2805 1000 HOH HOH A . 
G 7 HOH 1001 2806 1001 HOH HOH A . 
G 7 HOH 1002 2807 1002 HOH HOH A . 
G 7 HOH 1003 2808 1003 HOH HOH A . 
G 7 HOH 1004 2809 1004 HOH HOH A . 
G 7 HOH 1005 2810 1005 HOH HOH A . 
G 7 HOH 1006 2811 1006 HOH HOH A . 
G 7 HOH 1007 2812 1007 HOH HOH A . 
G 7 HOH 1008 2813 1008 HOH HOH A . 
G 7 HOH 1009 2814 1009 HOH HOH A . 
G 7 HOH 1010 2815 1010 HOH HOH A . 
G 7 HOH 1011 2816 1011 HOH HOH A . 
G 7 HOH 1012 2817 1012 HOH HOH A . 
G 7 HOH 1013 2818 1013 HOH HOH A . 
G 7 HOH 1014 2819 1014 HOH HOH A . 
G 7 HOH 1015 2820 1015 HOH HOH A . 
G 7 HOH 1016 2821 1016 HOH HOH A . 
G 7 HOH 1017 2822 1017 HOH HOH A . 
G 7 HOH 1018 2823 1018 HOH HOH A . 
G 7 HOH 1019 2824 1019 HOH HOH A . 
G 7 HOH 1020 2825 1020 HOH HOH A . 
G 7 HOH 1021 2826 1021 HOH HOH A . 
G 7 HOH 1022 2827 1022 HOH HOH A . 
G 7 HOH 1023 2828 1023 HOH HOH A . 
G 7 HOH 1024 2829 1024 HOH HOH A . 
G 7 HOH 1025 2830 1025 HOH HOH A . 
G 7 HOH 1026 2831 1026 HOH HOH A . 
G 7 HOH 1027 2832 1027 HOH HOH A . 
G 7 HOH 1028 2833 1028 HOH HOH A . 
G 7 HOH 1029 2834 1029 HOH HOH A . 
G 7 HOH 1030 2835 1030 HOH HOH A . 
G 7 HOH 1031 2836 1031 HOH HOH A . 
G 7 HOH 1032 2837 1032 HOH HOH A . 
G 7 HOH 1033 2838 1033 HOH HOH A . 
G 7 HOH 1034 2839 1034 HOH HOH A . 
G 7 HOH 1035 2840 1035 HOH HOH A . 
G 7 HOH 1036 2841 1036 HOH HOH A . 
G 7 HOH 1037 2842 1037 HOH HOH A . 
G 7 HOH 1038 2843 1038 HOH HOH A . 
G 7 HOH 1039 2844 1039 HOH HOH A . 
G 7 HOH 1040 2845 1040 HOH HOH A . 
G 7 HOH 1041 2846 1041 HOH HOH A . 
G 7 HOH 1042 2847 1042 HOH HOH A . 
G 7 HOH 1043 2848 1043 HOH HOH A . 
G 7 HOH 1044 2849 1044 HOH HOH A . 
G 7 HOH 1045 2850 1045 HOH HOH A . 
G 7 HOH 1046 2851 1046 HOH HOH A . 
G 7 HOH 1047 2852 1047 HOH HOH A . 
G 7 HOH 1048 2853 1048 HOH HOH A . 
G 7 HOH 1049 2854 1049 HOH HOH A . 
G 7 HOH 1050 2855 1050 HOH HOH A . 
G 7 HOH 1051 2856 1051 HOH HOH A . 
G 7 HOH 1052 2857 1052 HOH HOH A . 
G 7 HOH 1053 2858 1053 HOH HOH A . 
G 7 HOH 1054 2859 1054 HOH HOH A . 
G 7 HOH 1055 2860 1055 HOH HOH A . 
G 7 HOH 1056 2861 1056 HOH HOH A . 
G 7 HOH 1057 2862 1057 HOH HOH A . 
G 7 HOH 1058 2863 1058 HOH HOH A . 
G 7 HOH 1059 2864 1059 HOH HOH A . 
G 7 HOH 1060 2865 1060 HOH HOH A . 
G 7 HOH 1061 2866 1061 HOH HOH A . 
G 7 HOH 1062 2867 1062 HOH HOH A . 
G 7 HOH 1063 2868 1063 HOH HOH A . 
G 7 HOH 1064 2869 1064 HOH HOH A . 
G 7 HOH 1065 2870 1065 HOH HOH A . 
G 7 HOH 1066 2871 1066 HOH HOH A . 
G 7 HOH 1067 2872 1067 HOH HOH A . 
G 7 HOH 1068 2873 1068 HOH HOH A . 
G 7 HOH 1069 2874 1069 HOH HOH A . 
G 7 HOH 1070 2875 1070 HOH HOH A . 
G 7 HOH 1071 2876 1071 HOH HOH A . 
G 7 HOH 1072 2877 1072 HOH HOH A . 
G 7 HOH 1073 2878 1073 HOH HOH A . 
G 7 HOH 1074 2879 1074 HOH HOH A . 
G 7 HOH 1075 2880 1075 HOH HOH A . 
G 7 HOH 1076 2881 1076 HOH HOH A . 
G 7 HOH 1077 2882 1077 HOH HOH A . 
G 7 HOH 1078 2883 1078 HOH HOH A . 
G 7 HOH 1079 2884 1079 HOH HOH A . 
G 7 HOH 1080 2885 1080 HOH HOH A . 
G 7 HOH 1081 2886 1081 HOH HOH A . 
G 7 HOH 1082 2887 1082 HOH HOH A . 
G 7 HOH 1083 2888 1083 HOH HOH A . 
G 7 HOH 1084 2889 1084 HOH HOH A . 
G 7 HOH 1085 2890 1085 HOH HOH A . 
G 7 HOH 1086 2891 1086 HOH HOH A . 
G 7 HOH 1087 2892 1087 HOH HOH A . 
G 7 HOH 1088 2893 1088 HOH HOH A . 
G 7 HOH 1089 2894 1089 HOH HOH A . 
G 7 HOH 1090 2895 1090 HOH HOH A . 
G 7 HOH 1091 2896 1091 HOH HOH A . 
G 7 HOH 1092 2897 1092 HOH HOH A . 
G 7 HOH 1093 2898 1093 HOH HOH A . 
G 7 HOH 1094 2899 1094 HOH HOH A . 
G 7 HOH 1095 2900 1095 HOH HOH A . 
G 7 HOH 1096 2901 1096 HOH HOH A . 
G 7 HOH 1097 2902 1097 HOH HOH A . 
G 7 HOH 1098 2903 1098 HOH HOH A . 
G 7 HOH 1099 2904 1099 HOH HOH A . 
G 7 HOH 1100 2905 1100 HOH HOH A . 
G 7 HOH 1101 2906 1101 HOH HOH A . 
G 7 HOH 1102 2907 1102 HOH HOH A . 
G 7 HOH 1103 2908 1103 HOH HOH A . 
G 7 HOH 1104 2909 1104 HOH HOH A . 
G 7 HOH 1105 2910 1105 HOH HOH A . 
G 7 HOH 1106 2911 1106 HOH HOH A . 
G 7 HOH 1107 2912 1107 HOH HOH A . 
G 7 HOH 1108 2913 1108 HOH HOH A . 
G 7 HOH 1109 2914 1109 HOH HOH A . 
G 7 HOH 1110 2915 1110 HOH HOH A . 
G 7 HOH 1111 2916 1111 HOH HOH A . 
G 7 HOH 1112 2917 1112 HOH HOH A . 
G 7 HOH 1113 2918 1113 HOH HOH A . 
G 7 HOH 1114 2919 1114 HOH HOH A . 
G 7 HOH 1115 2920 1115 HOH HOH A . 
G 7 HOH 1116 2921 1116 HOH HOH A . 
G 7 HOH 1117 2922 1117 HOH HOH A . 
G 7 HOH 1118 2923 1118 HOH HOH A . 
G 7 HOH 1119 2924 1119 HOH HOH A . 
G 7 HOH 1120 2925 1120 HOH HOH A . 
G 7 HOH 1121 2926 1121 HOH HOH A . 
G 7 HOH 1122 2927 1122 HOH HOH A . 
G 7 HOH 1123 2928 1123 HOH HOH A . 
G 7 HOH 1124 2929 1124 HOH HOH A . 
G 7 HOH 1125 2930 1125 HOH HOH A . 
G 7 HOH 1126 2931 1126 HOH HOH A . 
G 7 HOH 1127 2932 1127 HOH HOH A . 
G 7 HOH 1128 2933 1128 HOH HOH A . 
G 7 HOH 1129 2934 1129 HOH HOH A . 
G 7 HOH 1130 2935 1130 HOH HOH A . 
G 7 HOH 1131 2936 1131 HOH HOH A . 
G 7 HOH 1132 2937 1132 HOH HOH A . 
G 7 HOH 1133 2938 1133 HOH HOH A . 
G 7 HOH 1134 2939 1134 HOH HOH A . 
G 7 HOH 1135 2940 1135 HOH HOH A . 
G 7 HOH 1136 2941 1136 HOH HOH A . 
G 7 HOH 1137 2942 1137 HOH HOH A . 
G 7 HOH 1138 2943 1138 HOH HOH A . 
G 7 HOH 1139 2944 1139 HOH HOH A . 
G 7 HOH 1140 2945 1140 HOH HOH A . 
G 7 HOH 1141 2946 1141 HOH HOH A . 
G 7 HOH 1142 2947 1142 HOH HOH A . 
G 7 HOH 1143 2948 1143 HOH HOH A . 
G 7 HOH 1144 2949 1144 HOH HOH A . 
G 7 HOH 1145 2950 1145 HOH HOH A . 
G 7 HOH 1146 2951 1146 HOH HOH A . 
G 7 HOH 1147 2952 1147 HOH HOH A . 
G 7 HOH 1148 2953 1148 HOH HOH A . 
G 7 HOH 1149 2954 1149 HOH HOH A . 
G 7 HOH 1150 2955 1150 HOH HOH A . 
G 7 HOH 1151 2956 1151 HOH HOH A . 
G 7 HOH 1152 2957 1152 HOH HOH A . 
G 7 HOH 1153 2958 1153 HOH HOH A . 
G 7 HOH 1154 2959 1154 HOH HOH A . 
G 7 HOH 1155 2960 1155 HOH HOH A . 
G 7 HOH 1156 2961 1156 HOH HOH A . 
G 7 HOH 1157 2962 1157 HOH HOH A . 
G 7 HOH 1158 2963 1158 HOH HOH A . 
G 7 HOH 1159 2964 1159 HOH HOH A . 
G 7 HOH 1160 2965 1160 HOH HOH A . 
G 7 HOH 1161 2966 1161 HOH HOH A . 
G 7 HOH 1162 2967 1162 HOH HOH A . 
G 7 HOH 1163 2968 1163 HOH HOH A . 
G 7 HOH 1164 2969 1164 HOH HOH A . 
G 7 HOH 1165 2970 1165 HOH HOH A . 
G 7 HOH 1166 2971 1166 HOH HOH A . 
G 7 HOH 1167 2972 1167 HOH HOH A . 
G 7 HOH 1168 2973 1168 HOH HOH A . 
G 7 HOH 1169 2974 1169 HOH HOH A . 
G 7 HOH 1170 2975 1170 HOH HOH A . 
G 7 HOH 1171 2976 1171 HOH HOH A . 
G 7 HOH 1172 2977 1172 HOH HOH 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,G 
# 
_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 ? D ZN . ? A ZN 1805 ? 1_555 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 91.7  ? 
2  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 98.4  ? 
3  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 168.6 ? 
4  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 105.4 ? 
5  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 91.9  ? 
6  OD2 ? A ASP 204 ? A ASP 204  ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 90.5  ? 
7  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O3  ? E GB1 .   ? A GB1 1804 ? 1_555 161.4 ? 
8  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O3  ? E GB1 .   ? A GB1 1804 ? 1_555 88.0  ? 
9  OD2 ? A ASP 204 ? A ASP 204  ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O3  ? E GB1 .   ? A GB1 1804 ? 1_555 80.8  ? 
10 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O3  ? E GB1 .   ? A GB1 1804 ? 1_555 93.1  ? 
11 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O4  ? E GB1 .   ? A GB1 1804 ? 1_555 89.7  ? 
12 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O4  ? E GB1 .   ? A GB1 1804 ? 1_555 90.2  ? 
13 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O4  ? E GB1 .   ? A GB1 1804 ? 1_555 84.7  ? 
14 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O4  ? E GB1 .   ? A GB1 1804 ? 1_555 164.6 ? 
15 O3  ? E GB1 .   ? A GB1 1804 ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O4  ? E GB1 .   ? A GB1 1804 ? 1_555 71.7  ? 
# 
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 2006-12-05 
2 'Structure model' 1 1 2007-10-16 
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       1.1 ? 1 
HKL-2000  'data reduction' .   ? 2 
SCALEPACK 'data scaling'   .   ? 3 
CNS       phasing          .   ? 4 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    33 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    2749 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.17 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CA A SER 597 ? ? CB A SER 597 ? B 1.675 1.525 0.150  0.015 N 
2 1 CB A ARG 770 ? ? CG A ARG 770 ? B 1.312 1.521 -0.209 0.027 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 N  A SER 53  ? ? CA A SER 53  ? ? CB  A SER 53  ? B 121.37 110.50 10.87  1.50 N 
2 1 CB A ASN 155 ? B CA A ASN 155 ? ? C   A ASN 155 ? B 124.09 110.40 13.69  2.00 N 
3 1 CB A ASP 316 ? B CA A ASP 316 ? ? C   A ASP 316 ? ? 97.07  110.40 -13.33 2.00 N 
4 1 NE A ARG 565 ? ? CZ A ARG 565 ? ? NH2 A ARG 565 ? ? 116.96 120.30 -3.34  0.50 N 
5 1 CB A ASP 839 ? ? CG A ASP 839 ? ? OD2 A ASP 839 ? ? 112.57 118.30 -5.73  0.90 N 
6 1 NE A ARG 843 ? ? CZ A ARG 843 ? ? NH2 A ARG 843 ? ? 117.07 120.30 -3.23  0.50 N 
7 1 NE A ARG 868 ? ? CZ A ARG 868 ? ? NH2 A ARG 868 ? ? 117.29 120.30 -3.01  0.50 N 
8 1 NE A ARG 963 ? ? CZ A ARG 963 ? ? NH1 A ARG 963 ? ? 123.83 120.30 3.53   0.50 N 
9 1 NE A ARG 963 ? ? CZ A ARG 963 ? ? NH2 A ARG 963 ? ? 116.64 120.30 -3.66  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 56  ? ? -101.09 79.28   
2  1 TRP A 95  ? ? -171.58 -84.67  
3  1 ASP A 106 ? ? -124.13 -57.78  
4  1 ASP A 106 ? ? -134.21 -57.78  
5  1 THR A 162 ? ? 66.51   -65.03  
6  1 GLN A 227 ? ? -135.94 -44.64  
7  1 ASP A 340 ? ? -171.30 -172.07 
8  1 LYS A 345 ? ? -92.17  -71.74  
9  1 SER A 411 ? ? 40.92   -122.13 
10 1 SER A 411 ? ? 61.28   -134.88 
11 1 ILE A 549 ? ? -144.67 -47.84  
12 1 LEU A 550 ? ? -167.98 118.50  
13 1 PRO A 562 ? ? -83.71  39.02   
14 1 PHE A 577 ? ? -100.47 73.71   
15 1 SER A 703 ? ? -48.20  163.92  
16 1 ASN A 732 ? ? -97.18  57.30   
17 1 SER A 762 ? ? 72.49   -1.69   
18 1 ILE A 831 ? ? -116.91 78.02   
19 1 SER A 833 ? ? -151.64 -14.02  
20 1 ASP A 839 ? ? -127.56 -162.59 
21 1 PRO A 990 ? ? -35.07  -74.96  
22 1 GLU A 991 ? ? 58.53   95.49   
23 1 GLU A 992 ? ? -125.01 -145.71 
24 1 HIS A 993 ? ? 27.78   76.71   
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 ASP A 316 ? B -14.59 
2 1 GLN A 766 ? B -13.86 
3 1 THR A 848 ? B -11.55 
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C4 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    A 
_pdbx_validate_chiral.auth_comp_id    MPD 
_pdbx_validate_chiral.auth_seq_id     1801 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         'WRONG HAND' 
_pdbx_validate_chiral.omega           . 
# 
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 'PHOSPHATE ION'                                                                  PO4 
4 'ZINC ION'                                                                       ZN  
5 '(2R,3R,4S)-2-({[(1R)-2-HYDROXY-1-PHENYLETHYL]AMINO}METHYL)PYRROLIDINE-3,4-DIOL' GB1 
6 '(4S)-2-METHYL-2,4-PENTANEDIOL'                                                  MPD 
7 water                                                                            HOH 
# 
