data_2F7O
# 
_entry.id   2F7O 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.286 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   2F7O         
RCSB  RCSB035553   
WWPDB D_1000035553 
# 
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 1PS3 . unspecified 
PDB 1QWN . unspecified 
PDB 1QWU . unspecified 
PDB 1QX1 . unspecified 
PDB 2F7P . unspecified 
PDB 2F7Q . unspecified 
PDB 2F7R . unspecified 
# 
_pdbx_database_status.entry_id                        2F7O 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2005-12-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Kuntz, D.A.' 1 
'Rose, D.R.'  2 
# 
_citation.id                        primary 
_citation.title                     
;Structural Basis of the Inhibition of Golgi alpha-Mannosidase II by Mannostatin A and the Role of the Thiomethyl Moiety in Ligand-Protein Interactions.
;
_citation.journal_abbrev            J.Am.Chem.Soc. 
_citation.journal_volume            128 
_citation.page_first                8310 
_citation.page_last                 8319 
_citation.year                      2006 
_citation.journal_id_ASTM           JACSAT 
_citation.country                   US 
_citation.journal_id_ISSN           0002-7863 
_citation.journal_id_CSD            0004 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   16787095 
_citation.pdbx_database_id_DOI      10.1021/ja061216p 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Kawatkar, S.P.' 1 
primary 'Kuntz, D.A.'    2 
primary 'Woods, R.J.'    3 
primary 'Rose, D.R.'     4 
primary 'Boons, G.J.'    5 
# 
_cell.entry_id           2F7O 
_cell.length_a           69.002 
_cell.length_b           109.301 
_cell.length_c           138.352 
_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                         2F7O 
_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 'ZINC ION'                                                        65.409     1    ?         ? ?                  
? 
4 non-polymer syn 'PHOSPHATE ION'                                                   94.971     1    ?         ? ?                  
? 
5 non-polymer syn '(1R,2R,3R,4S,5R)-4-AMINO-5-(METHYLTHIO)CYCLOPENTANE-1,2,3-TRIOL' 179.237    1    ?         ? ?                  
? 
6 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'                                   118.174    1    ?         ? ?                  
? 
7 water       nat water                                                             18.015     1048 ?         ? ?                  
? 
# 
_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_name_sys.entity_id   1 
_entity_name_sys.name        E.C.3.2.1.114 
# 
_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 cells' 
_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                    UNP 
_struct_ref.db_code                    MAN2_DROME 
_struct_ref.pdbx_db_accession          Q24451 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_align_begin           76 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.pdbx_seq_one_letter_code   ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              2F7O 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 13 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 1045 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q24451 
_struct_ref_seq.db_align_beg                  76 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1108 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       13 
_struct_ref_seq.pdbx_auth_seq_align_end       1045 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 2F7O ARG A 1  ? UNP Q24451 ? ? 'CLONING ATIFACT' 1  1  
1 2F7O SER A 2  ? UNP Q24451 ? ? 'CLONING ATIFACT' 2  2  
1 2F7O SER A 3  ? UNP Q24451 ? ? 'CLONING ATIFACT' 3  3  
1 2F7O HIS A 4  ? UNP Q24451 ? ? 'EXPRESSION TAG'  4  4  
1 2F7O HIS A 5  ? UNP Q24451 ? ? 'EXPRESSION TAG'  5  5  
1 2F7O HIS A 6  ? UNP Q24451 ? ? 'EXPRESSION TAG'  6  6  
1 2F7O HIS A 7  ? UNP Q24451 ? ? 'EXPRESSION TAG'  7  7  
1 2F7O HIS A 8  ? UNP Q24451 ? ? 'EXPRESSION TAG'  8  8  
1 2F7O HIS A 9  ? UNP Q24451 ? ? 'EXPRESSION TAG'  9  9  
1 2F7O GLY A 10 ? UNP Q24451 ? ? 'CLONING ATIFACT' 10 10 
1 2F7O GLU A 11 ? UNP Q24451 ? ? 'CLONING ATIFACT' 11 11 
1 2F7O PHE A 12 ? UNP Q24451 ? ? 'CLONING ATIFACT' 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 
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 
MSN non-polymer         . '(1R,2R,3R,4S,5R)-4-AMINO-5-(METHYLTHIO)CYCLOPENTANE-1,2,3-TRIOL' ? 'C6 H13 N O3 S'  179.237 
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.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.entry_id          2F7O 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.18 
_exptl_crystal.density_percent_sol   43.53 
_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.pH              7 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    'Tris, PEG 6000, MPD, NaCl, pH 7, vapor diffusion, hanging drop, temperature 298K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   2004-11-11 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.91860 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'CHESS BEAMLINE F1' 
_diffrn_source.pdbx_wavelength_list        0.91860 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       CHESS 
_diffrn_source.pdbx_synchrotron_beamline   F1 
# 
_reflns.entry_id                     2F7O 
_reflns.d_resolution_low             30.00 
_reflns.d_resolution_high            1.430 
_reflns.number_obs                   181459 
_reflns.percent_possible_obs         97.200 
_reflns.pdbx_Rmerge_I_obs            0.101 
_reflns.pdbx_chi_squared             1.024 
_reflns.pdbx_redundancy              4.1 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_netI_over_sigmaI        12.3 
_reflns.pdbx_Rsym_value              ? 
_reflns.observed_criterion_sigma_F   1 
_reflns.observed_criterion_sigma_I   1 
_reflns.number_all                   186718 
_reflns.B_iso_Wilson_estimate        14.5 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_low              1.48 
_reflns_shell.d_res_high             1.430 
_reflns_shell.number_unique_all      11355 
_reflns_shell.percent_possible_all   92.300 
_reflns_shell.Rmerge_I_obs           0.463 
_reflns_shell.pdbx_chi_squared       0.882 
_reflns_shell.pdbx_redundancy        3.5 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.meanI_over_sigI_obs    2.93 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.ls_d_res_high                            1.430 
_refine.ls_d_res_low                             29.750 
_refine.pdbx_ls_sigma_F                          2.00 
_refine.pdbx_data_cutoff_high_absF               320802.906 
_refine.pdbx_data_cutoff_low_absF                0.000 
_refine.ls_percent_reflns_obs                    95.200 
_refine.ls_number_reflns_obs                     184146 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.ls_R_factor_R_work                       0.206 
_refine.ls_R_factor_R_free                       0.235 
_refine.ls_percent_reflns_R_free                 2.200 
_refine.ls_number_reflns_R_free                  4103 
_refine.ls_R_factor_R_free_error                 0.004 
_refine.B_iso_mean                               17.000 
_refine.solvent_model_param_bsol                 48.941 
_refine.solvent_model_param_ksol                 0.358 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.aniso_B[1][1]                            -3.310 
_refine.aniso_B[2][2]                            -0.180 
_refine.aniso_B[3][3]                            3.490 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.entry_id                                 2F7O 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     192934 
_refine.ls_R_factor_all                          0.207 
_refine.ls_R_factor_obs                          0.2061 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      1HTY 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.details                                  ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_overall_ESU_R                       ? 
_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_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        2F7O 
_refine_analyze.Luzzati_coordinate_error_obs    0.18 
_refine_analyze.Luzzati_sigma_a_obs             0.18 
_refine_analyze.Luzzati_d_res_low_obs           30.00 
_refine_analyze.Luzzati_coordinate_error_free   0.21 
_refine_analyze.Luzzati_sigma_a_free            0.20 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.occupancy_sum_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         39 
_refine_hist.number_atoms_solvent             1048 
_refine_hist.number_atoms_total               9268 
_refine_hist.d_res_high                       1.430 
_refine_hist.d_res_low                        29.750 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d           ? 0.023  ? ?     'X-RAY DIFFRACTION' ? 
c_angle_deg        ? 2.000  ? ?     'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d ? 25.300 ? ?     'X-RAY DIFFRACTION' ? 
c_improper_angle_d ? 1.420  ? ?     'X-RAY DIFFRACTION' ? 
c_mcbond_it        ? 1.070  ? 1.500 'X-RAY DIFFRACTION' ? 
c_mcangle_it       ? 1.640  ? 2.000 'X-RAY DIFFRACTION' ? 
c_scbond_it        ? 1.730  ? 2.000 'X-RAY DIFFRACTION' ? 
c_scangle_it       ? 2.560  ? 2.500 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.430 
_refine_ls_shell.d_res_low                        1.520 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.percent_reflns_obs               90.800 
_refine_ls_shell.number_reflns_R_work             28336 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.297 
_refine_ls_shell.R_factor_R_free                  0.326 
_refine_ls_shell.percent_reflns_R_free            2.000 
_refine_ls_shell.number_reflns_R_free             588 
_refine_ls_shell.R_factor_R_free_error            0.013 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                28924 
_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.top  protein_rep.param  'X-RAY DIFFRACTION' 
2 carbohydrate.top carbohydrate.param 'X-RAY DIFFRACTION' 
3 cis_peptide.top  cis_peptide.param  'X-RAY DIFFRACTION' 
4 water_rep.top    water_rep.param    'X-RAY DIFFRACTION' 
5 ion.top          ion.param          'X-RAY DIFFRACTION' 
6 MPD.top          MPD.par            'X-RAY DIFFRACTION' 
7 PO4.top          PO4.par            'X-RAY DIFFRACTION' 
8 MSN.top          MSN.par            'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2F7O 
_struct.title                     'Golgi alpha-mannosidase II complex with mannostatin A' 
_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        2F7O 
_struct_keywords.text            'GLYCOSYL HYDROLASE FAMILY 38, HYDROLASE' 
_struct_keywords.pdbx_keywords   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 
# 
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 ? ? ? ? ? ? ? 2.059 ? 
disulf2 disulf ? ? A CYS 275  SG  ? ? ? 1_555 A CYS 282  SG  ? ? A CYS 275  A CYS 282  1_555 ? ? ? ? ? ? ? 2.018 ? 
disulf3 disulf ? ? A CYS 283  SG  ? ? ? 1_555 A CYS 297  SG  ? ? A CYS 283  A CYS 297  1_555 ? ? ? ? ? ? ? 2.068 ? 
disulf4 disulf ? ? A CYS 902  SG  ? ? ? 1_555 A CYS 987  SG  ? ? A CYS 902  A CYS 987  1_555 ? ? ? ? ? ? ? 2.060 ? 
disulf5 disulf ? ? A CYS 1000 SG  ? ? ? 1_555 A CYS 1009 SG  ? ? A CYS 1000 A CYS 1009 1_555 ? ? ? ? ? ? ? 2.026 ? 
covale1 covale ? ? A ASN 194  ND2 ? ? ? 1_555 B NAG .    C1  ? ? A ASN 194  A NAG 5004 1_555 ? ? ? ? ? ? ? 1.450 ? 
metalc1 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 E MSN .    O3  ? ? A ZN  5001 A MSN 5002 1_555 ? ? ? ? ? ? ? 2.183 ? 
metalc2 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 E MSN .    O4  ? ? A ZN  5001 A MSN 5002 1_555 ? ? ? ? ? ? ? 2.231 ? 
metalc3 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 A HIS 471  NE2 ? ? A ZN  5001 A HIS 471  1_555 ? ? ? ? ? ? ? 2.093 ? 
metalc4 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 A HIS 90   NE2 ? ? A ZN  5001 A HIS 90   1_555 ? ? ? ? ? ? ? 2.131 ? 
metalc5 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 A ASP 92   OD1 ? ? A ZN  5001 A ASP 92   1_555 ? ? ? ? ? ? ? 2.138 ? 
metalc6 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 A ASP 204  OD2 ? ? A ZN  5001 A ASP 204  1_555 ? ? ? ? ? ? ? 2.062 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 405 A . ? PHE 405 A THR 406 A ? THR 406 A 1 0.06  
2 TRP 531 A . ? TRP 531 A PRO 532 A ? PRO 532 A 1 -0.96 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 6  ? 
B ? 3  ? 
C ? 2  ? 
D ? 2  ? 
E ? 6  ? 
F ? 5  ? 
G ? 5  ? 
H ? 12 ? 
I ? 5  ? 
J ? 8  ? 
K ? 5  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1  2  ? parallel      
A 2  3  ? parallel      
A 3  4  ? anti-parallel 
A 4  5  ? parallel      
A 5  6  ? parallel      
B 1  2  ? parallel      
B 2  3  ? parallel      
C 1  2  ? parallel      
D 1  2  ? anti-parallel 
E 1  2  ? anti-parallel 
E 2  3  ? anti-parallel 
E 3  4  ? anti-parallel 
E 4  5  ? anti-parallel 
E 5  6  ? anti-parallel 
F 1  2  ? anti-parallel 
F 2  3  ? anti-parallel 
F 3  4  ? anti-parallel 
F 4  5  ? anti-parallel 
G 1  2  ? parallel      
G 2  3  ? anti-parallel 
G 3  4  ? anti-parallel 
G 4  5  ? parallel      
H 1  2  ? parallel      
H 2  3  ? anti-parallel 
H 3  4  ? anti-parallel 
H 4  5  ? anti-parallel 
H 5  6  ? anti-parallel 
H 6  7  ? anti-parallel 
H 7  8  ? anti-parallel 
H 8  9  ? anti-parallel 
H 9  10 ? anti-parallel 
H 10 11 ? anti-parallel 
H 11 12 ? anti-parallel 
I 1  2  ? anti-parallel 
I 2  3  ? anti-parallel 
I 3  4  ? anti-parallel 
I 4  5  ? anti-parallel 
J 1  2  ? anti-parallel 
J 2  3  ? anti-parallel 
J 3  4  ? anti-parallel 
J 4  5  ? anti-parallel 
J 5  6  ? anti-parallel 
J 6  7  ? anti-parallel 
J 7  8  ? anti-parallel 
K 1  2  ? anti-parallel 
K 2  3  ? anti-parallel 
K 3  4  ? anti-parallel 
K 4  5  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  VAL A 43   ? GLN A 44   ? VAL A 43   GLN A 44   
A 2  THR A 399  ? SER A 401  ? THR A 399  SER A 401  
A 3  GLU A 244  ? TRP A 247  ? GLU A 244  TRP A 247  
A 4  LEU A 259  ? MET A 263  ? LEU A 259  MET A 263  
A 5  ASN A 223  ? ILE A 226  ? ASN A 223  ILE A 226  
A 6  ALA A 199  ? ALA A 202  ? ALA A 199  ALA A 202  
B 1  VAL A 333  ? 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  ALA A 408  ? ARG A 410  ? ALA A 408  ARG A 410  
D 2  ASN A 413  ? TYR A 414  ? ASN A 413  TYR A 414  
E 1  PHE A 524  ? ASP A 527  ? PHE A 524  ASP A 527  
E 2  ASP A 930  ? PHE A 934  ? ASP A 930  PHE A 934  
E 3  SER A 552  ? ASN A 559  ? SER A 552  ASN A 559  
E 4  GLY A 628  ? ILE A 636  ? GLY A 628  ILE A 636  
E 5  VAL A 578  ? ASP A 582  ? VAL A 578  ASP A 582  
E 6  PRO A 587  ? VAL A 588  ? PRO A 587  VAL A 588  
F 1  PHE A 524  ? ASP A 527  ? PHE A 524  ASP A 527  
F 2  ASP A 930  ? PHE A 934  ? ASP A 930  PHE A 934  
F 3  SER A 552  ? ASN A 559  ? SER A 552  ASN A 559  
F 4  GLY A 628  ? ILE A 636  ? GLY A 628  ILE A 636  
F 5  GLN A 945  ? PHE A 946  ? GLN A 945  PHE A 946  
G 1  THR A 542  ? ILE A 543  ? THR A 542  ILE A 543  
G 2  ARG A 565  ? VAL A 573  ? ARG A 565  VAL A 573  
G 3  THR A 606  ? VAL A 624  ? THR A 606  VAL A 624  
G 4  ALA A 590  ? ASP A 601  ? ALA A 590  ASP A 601  
G 5  THR A 644  ? TYR A 646  ? THR A 644  TYR A 646  
H 1  LYS A 669  ? GLY A 671  ? LYS A 669  GLY A 671  
H 2  SER A 648  ? LEU A 652  ? SER A 648  LEU A 652  
H 3  VAL A 745  ? LYS A 749  ? VAL A 745  LYS A 749  
H 4  SER A 754  ? LEU A 760  ? SER A 754  LEU A 760  
H 5  VAL A 763  ? MET A 769  ? VAL A 763  MET A 769  
H 6  GLU A 775  ? VAL A 780  ? GLU A 775  VAL A 780  
H 7  VAL A 888  ? LYS A 898  ? VAL A 888  LYS A 898  
H 8  THR A 842  ? THR A 848  ? THR A 842  THR A 848  
H 9  GLY A 834  ? GLU A 838  ? GLY A 834  GLU A 838  
H 10 ILE A 803  ? LEU A 808  ? ILE A 803  LEU A 808  
H 11 GLN A 812  ? ARG A 817  ? GLN A 812  ARG A 817  
H 12 ALA A 911  ? GLY A 912  ? ALA A 911  GLY A 912  
I 1  ILE A 676  ? ARG A 679  ? ILE A 676  ARG A 679  
I 2  THR A 685  ? PHE A 688  ? THR A 685  PHE A 688  
I 3  LEU A 694  ? GLN A 698  ? LEU A 694  GLN A 698  
I 4  VAL A 706  ? TYR A 715  ? VAL A 706  TYR A 715  
I 5  SER A 736  ? PRO A 737  ? SER A 736  PRO A 737  
J 1  ILE A 676  ? ARG A 679  ? ILE A 676  ARG A 679  
J 2  THR A 685  ? PHE A 688  ? THR A 685  PHE A 688  
J 3  LEU A 694  ? GLN A 698  ? LEU A 694  GLN A 698  
J 4  VAL A 706  ? TYR A 715  ? VAL A 706  TYR A 715  
J 5  THR A 788  ? THR A 796  ? THR A 788  THR A 796  
J 6  GLU A 861  ? ARG A 869  ? GLU A 861  ARG A 869  
J 7  LEU A 852  ? SER A 855  ? LEU A 852  SER A 855  
J 8  TYR A 829  ? ILE A 831  ? TYR A 829  ILE A 831  
K 1  LEU A 957  ? ARG A 964  ? LEU A 957  ARG A 964  
K 2  GLN A 973  ? ARG A 981  ? GLN A 973  ARG A 981  
K 3  THR A 1036 ? HIS A 1043 ? THR A 1036 HIS A 1043 
K 4  VAL A 1006 ? THR A 1012 ? VAL A 1006 THR A 1012 
K 5  ASN A 1019 ? HIS A 1022 ? ASN A 1019 HIS A 1022 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1  2  N VAL A 43   ? N VAL A 43   O 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 ILE A 336  ? O ILE A 336  N PHE A 84   ? N PHE A 84   
B 2  3  N VAL A 83   ? N VAL A 83   O GLN A 373  ? O GLN A 373  
C 1  2  N PHE A 126  ? N PHE A 126  O GLU A 159  ? O GLU A 159  
D 1  2  N ARG A 410  ? N ARG A 410  O ASN A 413  ? O ASN A 413  
E 1  2  N THR A 525  ? N THR A 525  O ILE A 933  ? O ILE A 933  
E 2  3  O PHE A 932  ? O PHE A 932  N VAL A 556  ? N VAL A 556  
E 3  4  N VAL A 555  ? N VAL A 555  O TYR A 632  ? O TYR A 632  
E 4  5  O VAL A 633  ? O VAL A 633  N THR A 581  ? N THR A 581  
E 5  6  N VAL A 580  ? N VAL A 580  O VAL A 588  ? O VAL A 588  
F 1  2  N THR A 525  ? N THR A 525  O ILE A 933  ? O ILE A 933  
F 2  3  O PHE A 932  ? O PHE A 932  N VAL A 556  ? N VAL A 556  
F 3  4  N VAL A 555  ? N VAL A 555  O TYR A 632  ? O TYR A 632  
F 4  5  N LEU A 629  ? N LEU A 629  O PHE A 946  ? O PHE A 946  
G 1  2  N ILE A 543  ? N ILE A 543  O TYR A 572  ? O TYR A 572  
G 2  3  N VAL A 573  ? N VAL A 573  O TYR A 616  ? O TYR A 616  
G 3  4  O GLN A 610  ? O GLN A 610  N SER A 597  ? N SER A 597  
G 4  5  N VAL A 592  ? N VAL A 592  O SER A 645  ? O SER A 645  
H 1  2  O LYS A 669  ? O LYS A 669  N LEU A 651  ? N LEU A 651  
H 2  3  N LEU A 652  ? N LEU A 652  O VAL A 745  ? O VAL A 745  
H 3  4  N LEU A 746  ? N LEU A 746  O SER A 757  ? O SER A 757  
H 4  5  N SER A 754  ? N SER A 754  O MET A 769  ? O MET A 769  
H 5  6  N ILE A 768  ? N ILE A 768  O GLU A 775  ? O GLU A 775  
H 6  7  N VAL A 780  ? N VAL A 780  O VAL A 888  ? O VAL A 888  
H 7  8  O VAL A 895  ? O VAL A 895  N THR A 845  ? N THR A 845  
H 8  9  O LEU A 846  ? O LEU A 846  N MET A 835  ? N MET A 835  
H 9  10 O PHE A 836  ? O PHE A 836  N TYR A 805  ? N TYR A 805  
H 10 11 N PHE A 804  ? N PHE A 804  O ARG A 816  ? O ARG A 816  
H 11 12 N PHE A 813  ? N PHE A 813  O GLY A 912  ? O GLY A 912  
I 1  2  N ILE A 676  ? N ILE A 676  O PHE A 688  ? O PHE A 688  
I 2  3  N ALA A 687  ? N ALA A 687  O LYS A 695  ? O LYS A 695  
I 3  4  N ILE A 697  ? N ILE A 697  O VAL A 706  ? O VAL A 706  
I 4  5  N LYS A 714  ? N LYS A 714  O SER A 736  ? O SER A 736  
J 1  2  N ILE A 676  ? N ILE A 676  O PHE A 688  ? O PHE A 688  
J 2  3  N ALA A 687  ? N ALA A 687  O LYS A 695  ? O LYS A 695  
J 3  4  N ILE A 697  ? N ILE A 697  O VAL A 706  ? O VAL A 706  
J 4  5  N LYS A 711  ? N LYS A 711  O ARG A 793  ? O ARG A 793  
J 5  6  N LEU A 794  ? N LEU A 794  O LEU A 862  ? O LEU A 862  
J 6  7  O MET A 865  ? O MET A 865  N GLY A 853  ? N GLY A 853  
J 7  8  O GLY A 854  ? O GLY A 854  N TYR A 829  ? N TYR A 829  
K 1  2  N ARG A 963  ? N ARG A 963  O GLY A 976  ? O GLY A 976  
K 2  3  N LEU A 979  ? N LEU A 979  O ALA A 1037 ? O ALA A 1037 
K 3  4  O SER A 1042 ? O SER A 1042 N ALA A 1007 ? N ALA A 1007 
K 4  5  N ARG A 1011 ? N ARG A 1011 O LEU A 1020 ? O LEU A 1020 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG A 5004' 
AC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN A 5001'  
AC3 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE PO4 A 5005' 
AC4 Software ? ? ? ? 17 'BINDING SITE FOR RESIDUE MSN A 5002' 
AC5 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE MPD A 5003' 
# 
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 5  HIS A 90  ? HIS A 90   . ? 1_555 ? 
3  AC2 5  ASP A 92  ? ASP A 92   . ? 1_555 ? 
4  AC2 5  ASP A 204 ? ASP A 204  . ? 1_555 ? 
5  AC2 5  HIS A 471 ? HIS A 471  . ? 1_555 ? 
6  AC2 5  MSN E .   ? MSN A 5002 . ? 1_555 ? 
7  AC3 9  GLN A 567 ? GLN A 567  . ? 1_555 ? 
8  AC3 9  ARG A 770 ? ARG A 770  . ? 1_555 ? 
9  AC3 9  ARG A 893 ? ARG A 893  . ? 1_555 ? 
10 AC3 9  SER A 924 ? SER A 924  . ? 1_555 ? 
11 AC3 9  HOH G .   ? HOH A 5380 . ? 1_555 ? 
12 AC3 9  HOH G .   ? HOH A 5387 . ? 1_555 ? 
13 AC3 9  HOH G .   ? HOH A 5388 . ? 1_555 ? 
14 AC3 9  HOH G .   ? HOH A 5458 . ? 1_555 ? 
15 AC3 9  HOH G .   ? HOH A 5460 . ? 1_555 ? 
16 AC4 17 HIS A 90  ? HIS A 90   . ? 1_555 ? 
17 AC4 17 ASP A 92  ? ASP A 92   . ? 1_555 ? 
18 AC4 17 TRP A 95  ? TRP A 95   . ? 1_555 ? 
19 AC4 17 ASP A 204 ? ASP A 204  . ? 1_555 ? 
20 AC4 17 PHE A 206 ? PHE A 206  . ? 1_555 ? 
21 AC4 17 ARG A 228 ? ARG A 228  . ? 1_555 ? 
22 AC4 17 TYR A 269 ? TYR A 269  . ? 1_555 ? 
23 AC4 17 ASP A 341 ? ASP A 341  . ? 1_555 ? 
24 AC4 17 TRP A 415 ? TRP A 415  . ? 1_555 ? 
25 AC4 17 HIS A 471 ? HIS A 471  . ? 1_555 ? 
26 AC4 17 ASP A 472 ? ASP A 472  . ? 1_555 ? 
27 AC4 17 TYR A 727 ? TYR A 727  . ? 1_555 ? 
28 AC4 17 ARG A 876 ? ARG A 876  . ? 1_555 ? 
29 AC4 17 ZN  C .   ? ZN  A 5001 . ? 1_555 ? 
30 AC4 17 HOH G .   ? HOH A 5084 . ? 1_555 ? 
31 AC4 17 HOH G .   ? HOH A 5085 . ? 1_555 ? 
32 AC4 17 HOH G .   ? HOH A 5164 . ? 1_555 ? 
33 AC5 8  LYS A 63  ? LYS A 63   . ? 1_555 ? 
34 AC5 8  GLN A 64  ? GLN A 64   . ? 1_555 ? 
35 AC5 8  TYR A 267 ? TYR A 267  . ? 1_555 ? 
36 AC5 8  HIS A 273 ? HIS A 273  . ? 1_555 ? 
37 AC5 8  HOH G .   ? HOH A 5289 . ? 1_555 ? 
38 AC5 8  HOH G .   ? HOH A 5299 . ? 1_555 ? 
39 AC5 8  HOH G .   ? HOH A 5301 . ? 1_555 ? 
40 AC5 8  HOH G .   ? HOH A 5302 . ? 1_555 ? 
# 
_atom_sites.entry_id                    2F7O 
_atom_sites.fract_transf_matrix[1][1]   0.014492 
_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]   0.009149 
_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]   0.007228 
_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   ? 44.371 36.138  -19.080 1.00 24.01 ? 31   CYS A N   1 
ATOM   2    C  CA  . CYS A 1 31   ? 43.594 37.350  -18.651 1.00 21.19 ? 31   CYS A CA  1 
ATOM   3    C  C   . CYS A 1 31   ? 42.113 37.132  -18.757 1.00 21.19 ? 31   CYS A C   1 
ATOM   4    O  O   . CYS A 1 31   ? 41.615 36.579  -19.747 1.00 20.97 ? 31   CYS A O   1 
ATOM   5    C  CB  . CYS A 1 31   ? 43.899 38.567  -19.529 1.00 21.78 ? 31   CYS A CB  1 
ATOM   6    S  SG  . CYS A 1 31   ? 45.613 39.176  -19.510 1.00 22.59 ? 31   CYS A SG  1 
ATOM   7    N  N   . GLN A 1 32   ? 41.403 37.610  -17.753 1.00 19.28 ? 32   GLN A N   1 
ATOM   8    C  CA  . GLN A 1 32   ? 39.947 37.536  -17.705 1.00 20.63 ? 32   GLN A CA  1 
ATOM   9    C  C   . GLN A 1 32   ? 39.383 38.501  -18.792 1.00 19.33 ? 32   GLN A C   1 
ATOM   10   O  O   . GLN A 1 32   ? 39.949 39.596  -19.038 1.00 18.68 ? 32   GLN A O   1 
ATOM   11   C  CB  . GLN A 1 32   ? 39.481 37.982  -16.305 1.00 23.47 ? 32   GLN A CB  1 
ATOM   12   C  CG  . GLN A 1 32   ? 38.148 37.499  -15.942 1.00 28.24 ? 32   GLN A CG  1 
ATOM   13   C  CD  . GLN A 1 32   ? 37.808 37.663  -14.446 1.00 29.86 ? 32   GLN A CD  1 
ATOM   14   O  OE1 . GLN A 1 32   ? 36.738 37.247  -14.014 1.00 33.60 ? 32   GLN A OE1 1 
ATOM   15   N  NE2 . GLN A 1 32   ? 38.708 38.272  -13.662 1.00 31.47 ? 32   GLN A NE2 1 
ATOM   16   N  N   . ASP A 1 33   ? 38.312 38.094  -19.480 1.00 18.38 ? 33   ASP A N   1 
ATOM   17   C  CA  . ASP A 1 33   ? 37.653 38.928  -20.483 1.00 17.92 ? 33   ASP A CA  1 
ATOM   18   C  C   . ASP A 1 33   ? 36.706 39.885  -19.719 1.00 17.67 ? 33   ASP A C   1 
ATOM   19   O  O   . ASP A 1 33   ? 35.732 39.458  -19.078 1.00 17.55 ? 33   ASP A O   1 
ATOM   20   C  CB  . ASP A 1 33   ? 36.874 38.001  -21.450 1.00 19.26 ? 33   ASP A CB  1 
ATOM   21   C  CG  . ASP A 1 33   ? 36.199 38.753  -22.581 1.00 21.09 ? 33   ASP A CG  1 
ATOM   22   O  OD1 . ASP A 1 33   ? 35.747 39.898  -22.363 1.00 19.84 ? 33   ASP A OD1 1 
ATOM   23   O  OD2 . ASP A 1 33   ? 36.091 38.172  -23.710 1.00 22.43 ? 33   ASP A OD2 1 
ATOM   24   N  N   . VAL A 1 34   ? 36.975 41.176  -19.795 1.00 13.69 ? 34   VAL A N   1 
ATOM   25   C  CA  . VAL A 1 34   ? 36.174 42.139  -19.024 1.00 12.84 ? 34   VAL A CA  1 
ATOM   26   C  C   . VAL A 1 34   ? 34.985 42.746  -19.766 1.00 12.78 ? 34   VAL A C   1 
ATOM   27   O  O   . VAL A 1 34   ? 34.247 43.625  -19.256 1.00 12.56 ? 34   VAL A O   1 
ATOM   28   C  CB  . VAL A 1 34   ? 37.078 43.260  -18.492 1.00 12.74 ? 34   VAL A CB  1 
ATOM   29   C  CG1 . VAL A 1 34   ? 38.347 42.677  -17.841 1.00 12.65 ? 34   VAL A CG1 1 
ATOM   30   C  CG2 . VAL A 1 34   ? 37.513 44.180  -19.649 1.00 10.59 ? 34   VAL A CG2 1 
ATOM   31   N  N   . VAL A 1 35   ? 34.717 42.197  -20.957 1.00 10.20 ? 35   VAL A N   1 
ATOM   32   C  CA  . VAL A 1 35   ? 33.632 42.708  -21.760 1.00 12.49 ? 35   VAL A CA  1 
ATOM   33   C  C   . VAL A 1 35   ? 32.482 41.757  -21.997 1.00 11.30 ? 35   VAL A C   1 
ATOM   34   O  O   . VAL A 1 35   ? 31.335 42.157  -21.923 1.00 12.41 ? 35   VAL A O   1 
ATOM   35   C  CB  . VAL A 1 35   ? 34.179 43.080  -23.148 1.00 14.24 ? 35   VAL A CB  1 
ATOM   36   C  CG1 . VAL A 1 35   ? 33.021 43.478  -24.095 1.00 14.41 ? 35   VAL A CG1 1 
ATOM   37   C  CG2 . VAL A 1 35   ? 35.283 44.129  -23.062 1.00 13.84 ? 35   VAL A CG2 1 
ATOM   38   N  N   . GLN A 1 36   ? 32.823 40.497  -22.271 1.00 13.59 ? 36   GLN A N   1 
ATOM   39   C  CA  . GLN A 1 36   ? 31.845 39.479  -22.696 1.00 17.48 ? 36   GLN A CA  1 
ATOM   40   C  C   . GLN A 1 36   ? 31.197 38.559  -21.720 1.00 19.39 ? 36   GLN A C   1 
ATOM   41   O  O   . GLN A 1 36   ? 30.233 37.862  -22.065 1.00 20.73 ? 36   GLN A O   1 
ATOM   42   C  CB  . GLN A 1 36   ? 32.503 38.633  -23.788 1.00 16.08 ? 36   GLN A CB  1 
ATOM   43   C  CG  . GLN A 1 36   ? 32.900 39.495  -24.959 1.00 16.50 ? 36   GLN A CG  1 
ATOM   44   C  CD  . GLN A 1 36   ? 33.477 38.736  -26.153 1.00 18.13 ? 36   GLN A CD  1 
ATOM   45   O  OE1 . GLN A 1 36   ? 32.846 38.651  -27.238 1.00 19.34 ? 36   GLN A OE1 1 
ATOM   46   N  NE2 . GLN A 1 36   ? 34.668 38.212  -25.981 1.00 16.99 ? 36   GLN A NE2 1 
ATOM   47   N  N   . ASP A 1 37   ? 31.734 38.511  -20.516 1.00 19.96 ? 37   ASP A N   1 
ATOM   48   C  CA  . ASP A 1 37   ? 31.211 37.665  -19.464 1.00 21.05 ? 37   ASP A CA  1 
ATOM   49   C  C   . ASP A 1 37   ? 30.562 38.495  -18.327 1.00 19.87 ? 37   ASP A C   1 
ATOM   50   O  O   . ASP A 1 37   ? 31.273 39.148  -17.540 1.00 21.03 ? 37   ASP A O   1 
ATOM   51   C  CB  . ASP A 1 37   ? 32.367 36.817  -18.890 1.00 23.11 ? 37   ASP A CB  1 
ATOM   52   C  CG  . ASP A 1 37   ? 33.000 35.922  -19.938 1.00 24.97 ? 37   ASP A CG  1 
ATOM   53   O  OD1 . ASP A 1 37   ? 32.231 35.386  -20.762 1.00 25.98 ? 37   ASP A OD1 1 
ATOM   54   O  OD2 . ASP A 1 37   ? 34.240 35.754  -19.942 1.00 23.77 ? 37   ASP A OD2 1 
ATOM   55   N  N   . VAL A 1 38   ? 29.240 38.460  -18.250 1.00 18.34 ? 38   VAL A N   1 
ATOM   56   C  CA  . VAL A 1 38   ? 28.544 39.194  -17.194 1.00 17.95 ? 38   VAL A CA  1 
ATOM   57   C  C   . VAL A 1 38   ? 28.709 38.463  -15.844 1.00 17.31 ? 38   VAL A C   1 
ATOM   58   O  O   . VAL A 1 38   ? 28.283 37.308  -15.699 1.00 18.63 ? 38   VAL A O   1 
ATOM   59   C  CB  . VAL A 1 38   ? 27.066 39.324  -17.513 1.00 16.84 ? 38   VAL A CB  1 
ATOM   60   C  CG1 . VAL A 1 38   ? 26.337 40.116  -16.413 1.00 19.34 ? 38   VAL A CG1 1 
ATOM   61   C  CG2 . VAL A 1 38   ? 26.915 39.996  -18.946 1.00 15.93 ? 38   VAL A CG2 1 
ATOM   62   N  N   . PRO A 1 39   ? 29.322 39.116  -14.842 1.00 15.13 ? 39   PRO A N   1 
ATOM   63   C  CA  . PRO A 1 39   ? 29.482 38.432  -13.547 1.00 14.92 ? 39   PRO A CA  1 
ATOM   64   C  C   . PRO A 1 39   ? 28.144 38.069  -12.934 1.00 15.24 ? 39   PRO A C   1 
ATOM   65   O  O   . PRO A 1 39   ? 27.148 38.807  -13.034 1.00 14.71 ? 39   PRO A O   1 
ATOM   66   C  CB  . PRO A 1 39   ? 30.231 39.453  -12.661 1.00 13.26 ? 39   PRO A CB  1 
ATOM   67   C  CG  . PRO A 1 39   ? 31.034 40.298  -13.699 1.00 10.43 ? 39   PRO A CG  1 
ATOM   68   C  CD  . PRO A 1 39   ? 30.058 40.397  -14.897 1.00 13.82 ? 39   PRO A CD  1 
ATOM   69   N  N   . ASN A 1 40   ? 28.144 36.923  -12.241 1.00 15.97 ? 40   ASN A N   1 
ATOM   70   C  CA  . ASN A 1 40   ? 26.974 36.469  -11.521 1.00 17.01 ? 40   ASN A CA  1 
ATOM   71   C  C   . ASN A 1 40   ? 27.236 36.820  -10.036 1.00 15.99 ? 40   ASN A C   1 
ATOM   72   O  O   . ASN A 1 40   ? 28.122 36.253  -9.408  1.00 17.28 ? 40   ASN A O   1 
ATOM   73   C  CB  . ASN A 1 40   ? 26.830 34.971  -11.732 1.00 21.22 ? 40   ASN A CB  1 
ATOM   74   C  CG  . ASN A 1 40   ? 25.637 34.410  -11.013 1.00 26.75 ? 40   ASN A CG  1 
ATOM   75   O  OD1 . ASN A 1 40   ? 24.509 34.911  -11.166 1.00 31.75 ? 40   ASN A OD1 1 
ATOM   76   N  ND2 . ASN A 1 40   ? 25.864 33.372  -10.204 1.00 30.02 ? 40   ASN A ND2 1 
ATOM   77   N  N   . VAL A 1 41   ? 26.500 37.803  -9.519  1.00 14.45 ? 41   VAL A N   1 
ATOM   78   C  CA  . VAL A 1 41   ? 26.681 38.241  -8.135  1.00 13.18 ? 41   VAL A CA  1 
ATOM   79   C  C   . VAL A 1 41   ? 25.320 38.251  -7.473  1.00 13.29 ? 41   VAL A C   1 
ATOM   80   O  O   . VAL A 1 41   ? 24.292 38.320  -8.164  1.00 13.32 ? 41   VAL A O   1 
ATOM   81   C  CB  . VAL A 1 41   ? 27.327 39.648  -8.072  1.00 12.12 ? 41   VAL A CB  1 
ATOM   82   C  CG1 . VAL A 1 41   ? 28.739 39.598  -8.634  1.00 13.95 ? 41   VAL A CG1 1 
ATOM   83   C  CG2 . VAL A 1 41   ? 26.480 40.695  -8.869  1.00 11.82 ? 41   VAL A CG2 1 
ATOM   84   N  N   . ASP A 1 42   ? 25.283 38.136  -6.151  1.00 13.70 ? 42   ASP A N   1 
ATOM   85   C  CA  . ASP A 1 42   ? 24.027 38.131  -5.428  1.00 12.90 ? 42   ASP A CA  1 
ATOM   86   C  C   . ASP A 1 42   ? 23.348 39.498  -5.430  1.00 12.53 ? 42   ASP A C   1 
ATOM   87   O  O   . ASP A 1 42   ? 22.135 39.577  -5.394  1.00 14.17 ? 42   ASP A O   1 
ATOM   88   C  CB  . ASP A 1 42   ? 24.233 37.637  -3.962  1.00 13.55 ? 42   ASP A CB  1 
ATOM   89   C  CG  . ASP A 1 42   ? 24.785 36.254  -3.903  1.00 15.54 ? 42   ASP A CG  1 
ATOM   90   O  OD1 . ASP A 1 42   ? 24.157 35.384  -4.546  1.00 18.26 ? 42   ASP A OD1 1 
ATOM   91   O  OD2 . ASP A 1 42   ? 25.822 35.977  -3.241  1.00 13.77 ? 42   ASP A OD2 1 
ATOM   92   N  N   . VAL A 1 43   ? 24.127 40.571  -5.444  1.00 11.87 ? 43   VAL A N   1 
ATOM   93   C  CA  . VAL A 1 43   ? 23.584 41.911  -5.423  1.00 12.25 ? 43   VAL A CA  1 
ATOM   94   C  C   . VAL A 1 43   ? 24.368 42.708  -6.460  1.00 9.30  ? 43   VAL A C   1 
ATOM   95   O  O   . VAL A 1 43   ? 25.608 42.796  -6.381  1.00 10.89 ? 43   VAL A O   1 
ATOM   96   C  CB  . VAL A 1 43   ? 23.812 42.609  -4.049  1.00 11.34 ? 43   VAL A CB  1 
ATOM   97   C  CG1 . VAL A 1 43   ? 23.306 44.056  -4.070  1.00 12.56 ? 43   VAL A CG1 1 
ATOM   98   C  CG2 . VAL A 1 43   ? 23.067 41.763  -2.897  1.00 11.37 ? 43   VAL A CG2 1 
ATOM   99   N  N   . GLN A 1 44   ? 23.682 43.210  -7.453  1.00 10.82 ? 44   GLN A N   1 
ATOM   100  C  CA  . GLN A 1 44   ? 24.318 44.045  -8.478  1.00 9.88  ? 44   GLN A CA  1 
ATOM   101  C  C   . GLN A 1 44   ? 23.587 45.357  -8.291  1.00 9.86  ? 44   GLN A C   1 
ATOM   102  O  O   . GLN A 1 44   ? 22.357 45.431  -8.480  1.00 8.01  ? 44   GLN A O   1 
ATOM   103  C  CB  . GLN A 1 44   ? 24.130 43.395  -9.878  1.00 10.28 ? 44   GLN A CB  1 
ATOM   104  C  CG  . GLN A 1 44   ? 25.239 43.835  -10.857 1.00 11.05 ? 44   GLN A CG  1 
ATOM   105  C  CD  . GLN A 1 44   ? 25.269 45.387  -10.956 1.00 9.89  ? 44   GLN A CD  1 
ATOM   106  O  OE1 . GLN A 1 44   ? 24.251 46.020  -11.237 1.00 11.23 ? 44   GLN A OE1 1 
ATOM   107  N  NE2 . GLN A 1 44   ? 26.433 45.972  -10.719 1.00 7.82  ? 44   GLN A NE2 1 
ATOM   108  N  N   . MET A 1 45   ? 24.299 46.454  -7.920  1.00 7.62  ? 45   MET A N   1 
ATOM   109  C  CA  . MET A 1 45   ? 23.593 47.669  -7.555  1.00 8.52  ? 45   MET A CA  1 
ATOM   110  C  C   . MET A 1 45   ? 22.718 48.333  -8.618  1.00 7.96  ? 45   MET A C   1 
ATOM   111  O  O   . MET A 1 45   ? 21.715 48.935  -8.224  1.00 9.72  ? 45   MET A O   1 
ATOM   112  C  CB  . MET A 1 45   ? 24.561 48.677  -6.893  1.00 10.01 ? 45   MET A CB  1 
ATOM   113  C  CG  . MET A 1 45   ? 25.201 48.153  -5.603  1.00 9.75  ? 45   MET A CG  1 
ATOM   114  S  SD  . MET A 1 45   ? 23.992 47.893  -4.286  1.00 11.26 ? 45   MET A SD  1 
ATOM   115  C  CE  . MET A 1 45   ? 23.270 49.643  -4.158  1.00 13.61 ? 45   MET A CE  1 
ATOM   116  N  N   . LEU A 1 46   ? 23.081 48.275  -9.905  1.00 8.95  ? 46   LEU A N   1 
ATOM   117  C  CA  . LEU A 1 46   ? 22.193 48.840  -10.949 1.00 9.89  ? 46   LEU A CA  1 
ATOM   118  C  C   . LEU A 1 46   ? 20.870 48.020  -10.996 1.00 9.81  ? 46   LEU A C   1 
ATOM   119  O  O   . LEU A 1 46   ? 19.770 48.599  -11.102 1.00 11.74 ? 46   LEU A O   1 
ATOM   120  C  CB  . LEU A 1 46   ? 22.855 48.812  -12.332 1.00 11.70 ? 46   LEU A CB  1 
ATOM   121  C  CG  . LEU A 1 46   ? 22.098 49.593  -13.422 1.00 11.30 ? 46   LEU A CG  1 
ATOM   122  C  CD1 . LEU A 1 46   ? 22.131 51.142  -13.214 1.00 11.76 ? 46   LEU A CD1 1 
ATOM   123  C  CD2 . LEU A 1 46   ? 22.683 49.178  -14.779 1.00 11.52 ? 46   LEU A CD2 1 
ATOM   124  N  N   . GLU A 1 47   ? 20.976 46.688  -10.837 1.00 10.00 ? 47   GLU A N   1 
ATOM   125  C  CA  . GLU A 1 47   ? 19.761 45.873  -10.888 1.00 11.68 ? 47   GLU A CA  1 
ATOM   126  C  C   . GLU A 1 47   ? 18.937 46.139  -9.641  1.00 11.81 ? 47   GLU A C   1 
ATOM   127  O  O   . GLU A 1 47   ? 17.715 46.273  -9.707  1.00 12.42 ? 47   GLU A O   1 
ATOM   128  C  CB  . GLU A 1 47   ? 20.108 44.388  -11.028 1.00 13.76 ? 47   GLU A CB  1 
ATOM   129  C  CG  . GLU A 1 47   ? 18.882 43.465  -11.223 1.00 19.88 ? 47   GLU A CG  1 
ATOM   130  C  CD  . GLU A 1 47   ? 18.210 43.059  -9.931  1.00 25.46 ? 47   GLU A CD  1 
ATOM   131  O  OE1 . GLU A 1 47   ? 18.791 43.247  -8.834  1.00 23.39 ? 47   GLU A OE1 1 
ATOM   132  O  OE2 . GLU A 1 47   ? 17.072 42.533  -10.006 1.00 29.68 ? 47   GLU A OE2 1 
ATOM   133  N  N   . LEU A 1 48   ? 19.596 46.297  -8.501  1.00 9.57  ? 48   LEU A N   1 
ATOM   134  C  CA  . LEU A 1 48   ? 18.895 46.577  -7.254  1.00 10.15 ? 48   LEU A CA  1 
ATOM   135  C  C   . LEU A 1 48   ? 18.147 47.874  -7.348  1.00 10.58 ? 48   LEU A C   1 
ATOM   136  O  O   . LEU A 1 48   ? 16.976 47.981  -6.915  1.00 13.68 ? 48   LEU A O   1 
ATOM   137  C  CB  . LEU A 1 48   ? 19.876 46.630  -6.050  1.00 9.63  ? 48   LEU A CB  1 
ATOM   138  C  CG  . LEU A 1 48   ? 19.116 46.849  -4.731  1.00 13.04 ? 48   LEU A CG  1 
ATOM   139  C  CD1 . LEU A 1 48   ? 17.996 45.758  -4.638  1.00 16.23 ? 48   LEU A CD1 1 
ATOM   140  C  CD2 . LEU A 1 48   ? 20.086 46.821  -3.546  1.00 13.57 ? 48   LEU A CD2 1 
ATOM   141  N  N   . TYR A 1 49   ? 18.816 48.897  -7.879  1.00 10.77 ? 49   TYR A N   1 
ATOM   142  C  CA  . TYR A 1 49   ? 18.169 50.227  -8.053  1.00 11.73 ? 49   TYR A CA  1 
ATOM   143  C  C   . TYR A 1 49   ? 16.910 50.130  -8.930  1.00 10.96 ? 49   TYR A C   1 
ATOM   144  O  O   . TYR A 1 49   ? 15.896 50.755  -8.619  1.00 10.12 ? 49   TYR A O   1 
ATOM   145  C  CB  . TYR A 1 49   ? 19.206 51.167  -8.684  1.00 10.97 ? 49   TYR A CB  1 
ATOM   146  C  CG  . TYR A 1 49   ? 19.763 52.120  -7.666  1.00 10.72 ? 49   TYR A CG  1 
ATOM   147  C  CD1 . TYR A 1 49   ? 20.222 51.631  -6.422  1.00 10.67 ? 49   TYR A CD1 1 
ATOM   148  C  CD2 . TYR A 1 49   ? 19.768 53.511  -7.879  1.00 10.80 ? 49   TYR A CD2 1 
ATOM   149  C  CE1 . TYR A 1 49   ? 20.650 52.453  -5.458  1.00 11.00 ? 49   TYR A CE1 1 
ATOM   150  C  CE2 . TYR A 1 49   ? 20.172 54.390  -6.882  1.00 11.18 ? 49   TYR A CE2 1 
ATOM   151  C  CZ  . TYR A 1 49   ? 20.622 53.864  -5.651  1.00 10.44 ? 49   TYR A CZ  1 
ATOM   152  O  OH  . TYR A 1 49   ? 20.949 54.645  -4.573  1.00 10.20 ? 49   TYR A OH  1 
ATOM   153  N  N   . ASP A 1 50   ? 16.995 49.296  -9.962  1.00 13.60 ? 50   ASP A N   1 
ATOM   154  C  CA  . ASP A 1 50   ? 15.866 49.153  -10.908 1.00 14.84 ? 50   ASP A CA  1 
ATOM   155  C  C   . ASP A 1 50   ? 14.643 48.616  -10.160 1.00 17.17 ? 50   ASP A C   1 
ATOM   156  O  O   . ASP A 1 50   ? 13.519 49.102  -10.361 1.00 16.85 ? 50   ASP A O   1 
ATOM   157  C  CB  . ASP A 1 50   ? 16.294 48.226  -12.039 1.00 17.54 ? 50   ASP A CB  1 
ATOM   158  C  CG  . ASP A 1 50   ? 15.516 48.438  -13.303 1.00 22.53 ? 50   ASP A CG  1 
ATOM   159  O  OD1 . ASP A 1 50   ? 14.863 49.488  -13.474 1.00 24.03 ? 50   ASP A OD1 1 
ATOM   160  O  OD2 . ASP A 1 50   ? 15.601 47.527  -14.157 1.00 27.04 ? 50   ASP A OD2 1 
ATOM   161  N  N   . ARG A 1 51   ? 14.863 47.622  -9.305  1.00 16.88 ? 51   ARG A N   1 
ATOM   162  C  CA  . ARG A 1 51   ? 13.753 47.009  -8.514  1.00 17.45 ? 51   ARG A CA  1 
ATOM   163  C  C   . ARG A 1 51   ? 13.246 47.732  -7.273  1.00 17.13 ? 51   ARG A C   1 
ATOM   164  O  O   . ARG A 1 51   ? 12.086 47.568  -6.925  1.00 17.93 ? 51   ARG A O   1 
ATOM   165  C  CB  . ARG A 1 51   ? 14.120 45.624  -7.978  1.00 19.72 ? 51   ARG A CB  1 
ATOM   166  C  CG  . ARG A 1 51   ? 14.682 44.666  -8.901  1.00 23.90 ? 51   ARG A CG  1 
ATOM   167  C  CD  . ARG A 1 51   ? 14.721 43.322  -8.223  1.00 27.06 ? 51   ARG A CD  1 
ATOM   168  N  NE  . ARG A 1 51   ? 16.057 43.037  -7.740  1.00 29.58 ? 51   ARG A NE  1 
ATOM   169  C  CZ  . ARG A 1 51   ? 16.442 43.007  -6.474  1.00 31.37 ? 51   ARG A CZ  1 
ATOM   170  N  NH1 . ARG A 1 51   ? 15.579 43.255  -5.479  1.00 33.15 ? 51   ARG A NH1 1 
ATOM   171  N  NH2 . ARG A 1 51   ? 17.712 42.699  -6.213  1.00 31.61 ? 51   ARG A NH2 1 
ATOM   172  N  N   . MET A 1 52   ? 14.115 48.419  -6.538  1.00 15.69 ? 52   MET A N   1 
ATOM   173  C  CA  . MET A 1 52   ? 13.747 49.112  -5.283  1.00 18.55 ? 52   MET A CA  1 
ATOM   174  C  C   . MET A 1 52   ? 12.735 50.212  -5.419  1.00 17.51 ? 52   MET A C   1 
ATOM   175  O  O   . MET A 1 52   ? 12.755 50.917  -6.422  1.00 18.24 ? 52   MET A O   1 
ATOM   176  C  CB  . MET A 1 52   ? 14.978 49.800  -4.685  1.00 18.63 ? 52   MET A CB  1 
ATOM   177  C  CG  . MET A 1 52   ? 15.891 48.893  -3.990  1.00 19.15 ? 52   MET A CG  1 
ATOM   178  S  SD  . MET A 1 52   ? 17.447 49.808  -3.633  1.00 20.22 ? 52   MET A SD  1 
ATOM   179  C  CE  . MET A 1 52   ? 16.770 51.005  -2.434  1.00 16.78 ? 52   MET A CE  1 
ATOM   180  N  N   . SER A 1 53   ? 11.883 50.420  -4.413  1.00 18.65 ? 53   SER A N   1 
ATOM   181  C  CA  . SER A 1 53   ? 10.901 51.508  -4.501  1.00 19.05 ? 53   SER A CA  1 
ATOM   182  C  C   . SER A 1 53   ? 11.361 52.883  -3.991  1.00 18.39 ? 53   SER A C   1 
ATOM   183  O  O   A SER A 1 53   ? 10.857 53.936  -4.441  0.50 19.81 ? 53   SER A O   1 
ATOM   184  O  O   B SER A 1 53   ? 10.566 53.867  -4.116  0.50 18.98 ? 53   SER A O   1 
ATOM   185  C  CB  . SER A 1 53   ? 9.610  51.109  -3.773  1.00 19.56 ? 53   SER A CB  1 
ATOM   186  O  OG  A SER A 1 53   ? 8.936  50.113  -4.531  0.50 19.21 ? 53   SER A OG  1 
ATOM   187  O  OG  B SER A 1 53   ? 9.476  51.611  -2.451  0.50 15.57 ? 53   SER A OG  1 
ATOM   188  N  N   . PHE A 1 54   ? 12.287 52.876  -3.041  1.00 17.16 ? 54   PHE A N   1 
ATOM   189  C  CA  . PHE A 1 54   ? 12.783 54.132  -2.461  1.00 16.53 ? 54   PHE A CA  1 
ATOM   190  C  C   . PHE A 1 54   ? 11.753 54.943  -1.647  1.00 16.75 ? 54   PHE A C   1 
ATOM   191  O  O   . PHE A 1 54   ? 11.925 56.141  -1.429  1.00 16.88 ? 54   PHE A O   1 
ATOM   192  C  CB  . PHE A 1 54   ? 13.350 55.040  -3.575  1.00 14.83 ? 54   PHE A CB  1 
ATOM   193  C  CG  . PHE A 1 54   ? 14.628 54.538  -4.165  1.00 13.46 ? 54   PHE A CG  1 
ATOM   194  C  CD1 . PHE A 1 54   ? 15.862 54.775  -3.549  1.00 12.34 ? 54   PHE A CD1 1 
ATOM   195  C  CD2 . PHE A 1 54   ? 14.604 53.795  -5.334  1.00 13.07 ? 54   PHE A CD2 1 
ATOM   196  C  CE1 . PHE A 1 54   ? 17.063 54.267  -4.108  1.00 12.27 ? 54   PHE A CE1 1 
ATOM   197  C  CE2 . PHE A 1 54   ? 15.815 53.268  -5.906  1.00 12.82 ? 54   PHE A CE2 1 
ATOM   198  C  CZ  . PHE A 1 54   ? 17.042 53.509  -5.286  1.00 11.42 ? 54   PHE A CZ  1 
ATOM   199  N  N   . LYS A 1 55   ? 10.654 54.318  -1.234  1.00 17.31 ? 55   LYS A N   1 
ATOM   200  C  CA  . LYS A 1 55   ? 9.672  55.051  -0.395  1.00 18.22 ? 55   LYS A CA  1 
ATOM   201  C  C   . LYS A 1 55   ? 10.285 55.431  0.920   1.00 17.75 ? 55   LYS A C   1 
ATOM   202  O  O   . LYS A 1 55   ? 10.991 54.648  1.528   1.00 19.33 ? 55   LYS A O   1 
ATOM   203  C  CB  . LYS A 1 55   ? 8.439  54.184  -0.038  1.00 20.27 ? 55   LYS A CB  1 
ATOM   204  C  CG  . LYS A 1 55   ? 7.667  53.693  -1.217  1.00 23.53 ? 55   LYS A CG  1 
ATOM   205  C  CD  . LYS A 1 55   ? 7.525  54.788  -2.253  1.00 23.30 ? 55   LYS A CD  1 
ATOM   206  C  CE  . LYS A 1 55   ? 6.682  54.331  -3.416  1.00 26.38 ? 55   LYS A CE  1 
ATOM   207  N  NZ  . LYS A 1 55   ? 6.380  55.516  -4.272  1.00 25.04 ? 55   LYS A NZ  1 
ATOM   208  N  N   . ASP A 1 56   ? 9.977  56.622  1.394   1.00 17.29 ? 56   ASP A N   1 
ATOM   209  C  CA  . ASP A 1 56   ? 10.536 57.127  2.629   1.00 16.30 ? 56   ASP A CA  1 
ATOM   210  C  C   . ASP A 1 56   ? 9.502  57.097  3.778   1.00 17.87 ? 56   ASP A C   1 
ATOM   211  O  O   . ASP A 1 56   ? 8.967  58.118  4.207   1.00 17.99 ? 56   ASP A O   1 
ATOM   212  C  CB  . ASP A 1 56   ? 11.039 58.546  2.356   1.00 14.92 ? 56   ASP A CB  1 
ATOM   213  C  CG  . ASP A 1 56   ? 11.693 59.191  3.571   1.00 12.60 ? 56   ASP A CG  1 
ATOM   214  O  OD1 . ASP A 1 56   ? 12.186 58.509  4.508   1.00 14.08 ? 56   ASP A OD1 1 
ATOM   215  O  OD2 . ASP A 1 56   ? 11.742 60.446  3.560   1.00 14.68 ? 56   ASP A OD2 1 
ATOM   216  N  N   . ILE A 1 57   ? 9.238  55.910  4.294   1.00 18.91 ? 57   ILE A N   1 
ATOM   217  C  CA  A ILE A 1 57   ? 8.262  55.817  5.353   0.50 20.48 ? 57   ILE A CA  1 
ATOM   218  C  CA  B ILE A 1 57   ? 8.341  55.624  5.352   0.50 20.45 ? 57   ILE A CA  1 
ATOM   219  C  C   . ILE A 1 57   ? 8.860  55.825  6.733   1.00 20.56 ? 57   ILE A C   1 
ATOM   220  O  O   . ILE A 1 57   ? 10.016 55.462  6.946   1.00 20.69 ? 57   ILE A O   1 
ATOM   221  C  CB  A ILE A 1 57   ? 7.393  54.583  5.205   0.50 21.62 ? 57   ILE A CB  1 
ATOM   222  C  CB  B ILE A 1 57   ? 7.772  54.211  5.131   0.50 22.03 ? 57   ILE A CB  1 
ATOM   223  C  CG1 A ILE A 1 57   ? 8.285  53.359  4.963   0.50 21.89 ? 57   ILE A CG1 1 
ATOM   224  C  CG1 B ILE A 1 57   ? 6.991  54.209  3.809   0.50 21.43 ? 57   ILE A CG1 1 
ATOM   225  C  CG2 A ILE A 1 57   ? 6.366  54.820  4.107   0.50 20.38 ? 57   ILE A CG2 1 
ATOM   226  C  CG2 B ILE A 1 57   ? 6.957  53.753  6.354   0.50 20.25 ? 57   ILE A CG2 1 
ATOM   227  C  CD1 A ILE A 1 57   ? 7.536  52.043  4.999   0.50 22.38 ? 57   ILE A CD1 1 
ATOM   228  C  CD1 B ILE A 1 57   ? 6.695  52.830  3.227   0.50 23.57 ? 57   ILE A CD1 1 
ATOM   229  N  N   . ASP A 1 58   ? 8.033  56.239  7.679   1.00 20.47 ? 58   ASP A N   1 
ATOM   230  C  CA  . ASP A 1 58   ? 8.433  56.345  9.044   1.00 20.15 ? 58   ASP A CA  1 
ATOM   231  C  C   . ASP A 1 58   ? 8.491  54.918  9.566   1.00 19.82 ? 58   ASP A C   1 
ATOM   232  O  O   . ASP A 1 58   ? 7.488  54.231  9.614   1.00 19.30 ? 58   ASP A O   1 
ATOM   233  C  CB  . ASP A 1 58   ? 7.415  57.178  9.846   1.00 21.84 ? 58   ASP A CB  1 
ATOM   234  C  CG  . ASP A 1 58   ? 7.890  57.466  11.268  1.00 24.67 ? 58   ASP A CG  1 
ATOM   235  O  OD1 . ASP A 1 58   ? 8.841  56.815  11.748  1.00 23.68 ? 58   ASP A OD1 1 
ATOM   236  O  OD2 . ASP A 1 58   ? 7.321  58.360  11.940  1.00 27.26 ? 58   ASP A OD2 1 
ATOM   237  N  N   . GLY A 1 59   ? 9.677  54.454  9.940   1.00 17.96 ? 59   GLY A N   1 
ATOM   238  C  CA  . GLY A 1 59   ? 9.776  53.107  10.417  1.00 16.90 ? 59   GLY A CA  1 
ATOM   239  C  C   . GLY A 1 59   ? 9.723  52.968  11.932  1.00 13.75 ? 59   GLY A C   1 
ATOM   240  O  O   . GLY A 1 59   ? 9.946  51.858  12.439  1.00 15.53 ? 59   GLY A O   1 
ATOM   241  N  N   . GLY A 1 60   ? 9.409  54.050  12.657  1.00 14.67 ? 60   GLY A N   1 
ATOM   242  C  CA  . GLY A 1 60   ? 9.341  54.016  14.111  1.00 15.79 ? 60   GLY A CA  1 
ATOM   243  C  C   . GLY A 1 60   ? 10.622 54.592  14.693  1.00 15.35 ? 60   GLY A C   1 
ATOM   244  O  O   . GLY A 1 60   ? 11.188 55.516  14.090  1.00 15.44 ? 60   GLY A O   1 
ATOM   245  N  N   . VAL A 1 61   ? 11.112 54.058  15.810  1.00 15.46 ? 61   VAL A N   1 
ATOM   246  C  CA  . VAL A 1 61   ? 12.315 54.624  16.417  1.00 14.28 ? 61   VAL A CA  1 
ATOM   247  C  C   . VAL A 1 61   ? 13.507 54.499  15.425  1.00 13.63 ? 61   VAL A C   1 
ATOM   248  O  O   . VAL A 1 61   ? 14.357 55.392  15.388  1.00 12.61 ? 61   VAL A O   1 
ATOM   249  C  CB  . VAL A 1 61   ? 12.612 54.011  17.747  1.00 14.35 ? 61   VAL A CB  1 
ATOM   250  C  CG1 . VAL A 1 61   ? 11.404 54.254  18.701  1.00 14.25 ? 61   VAL A CG1 1 
ATOM   251  C  CG2 . VAL A 1 61   ? 12.856 52.542  17.583  1.00 15.83 ? 61   VAL A CG2 1 
ATOM   252  N  N   . TRP A 1 62   ? 13.564 53.431  14.631  1.00 12.57 ? 62   TRP A N   1 
ATOM   253  C  CA  . TRP A 1 62   ? 14.602 53.341  13.574  1.00 12.20 ? 62   TRP A CA  1 
ATOM   254  C  C   . TRP A 1 62   ? 13.839 54.042  12.432  1.00 13.08 ? 62   TRP A C   1 
ATOM   255  O  O   . TRP A 1 62   ? 13.045 53.428  11.691  1.00 12.59 ? 62   TRP A O   1 
ATOM   256  C  CB  . TRP A 1 62   ? 14.946 51.889  13.215  1.00 11.64 ? 62   TRP A CB  1 
ATOM   257  C  CG  . TRP A 1 62   ? 15.986 51.801  12.110  1.00 10.13 ? 62   TRP A CG  1 
ATOM   258  C  CD1 . TRP A 1 62   ? 16.673 52.862  11.531  1.00 8.50  ? 62   TRP A CD1 1 
ATOM   259  C  CD2 . TRP A 1 62   ? 16.350 50.636  11.352  1.00 10.01 ? 62   TRP A CD2 1 
ATOM   260  N  NE1 . TRP A 1 62   ? 17.405 52.415  10.461  1.00 9.85  ? 62   TRP A NE1 1 
ATOM   261  C  CE2 . TRP A 1 62   ? 17.235 51.057  10.332  1.00 11.34 ? 62   TRP A CE2 1 
ATOM   262  C  CE3 . TRP A 1 62   ? 16.003 49.275  11.440  1.00 10.68 ? 62   TRP A CE3 1 
ATOM   263  C  CZ2 . TRP A 1 62   ? 17.771 50.169  9.401   1.00 10.13 ? 62   TRP A CZ2 1 
ATOM   264  C  CZ3 . TRP A 1 62   ? 16.519 48.403  10.527  1.00 12.39 ? 62   TRP A CZ3 1 
ATOM   265  C  CH2 . TRP A 1 62   ? 17.408 48.850  9.497   1.00 12.06 ? 62   TRP A CH2 1 
ATOM   266  N  N   . LYS A 1 63   ? 14.030 55.353  12.281  1.00 12.62 ? 63   LYS A N   1 
ATOM   267  C  CA  . LYS A 1 63   ? 13.185 56.063  11.306  1.00 13.74 ? 63   LYS A CA  1 
ATOM   268  C  C   . LYS A 1 63   ? 13.190 55.553  9.874   1.00 14.27 ? 63   LYS A C   1 
ATOM   269  O  O   . LYS A 1 63   ? 12.155 55.600  9.166   1.00 14.20 ? 63   LYS A O   1 
ATOM   270  C  CB  . LYS A 1 63   ? 13.545 57.558  11.317  1.00 15.94 ? 63   LYS A CB  1 
ATOM   271  C  CG  . LYS A 1 63   ? 12.871 58.376  12.430  1.00 19.13 ? 63   LYS A CG  1 
ATOM   272  C  CD  . LYS A 1 63   ? 11.372 58.665  12.068  1.00 22.20 ? 63   LYS A CD  1 
ATOM   273  C  CE  . LYS A 1 63   ? 10.393 58.559  13.236  1.00 26.79 ? 63   LYS A CE  1 
ATOM   274  N  NZ  . LYS A 1 63   ? 10.956 58.991  14.564  1.00 28.99 ? 63   LYS A NZ  1 
ATOM   275  N  N   . GLN A 1 64   ? 14.328 55.070  9.422   1.00 12.34 ? 64   GLN A N   1 
ATOM   276  C  CA  . GLN A 1 64   ? 14.422 54.641  8.033   1.00 12.48 ? 64   GLN A CA  1 
ATOM   277  C  C   . GLN A 1 64   ? 14.424 53.134  7.879   1.00 11.65 ? 64   GLN A C   1 
ATOM   278  O  O   . GLN A 1 64   ? 14.720 52.591  6.833   1.00 11.62 ? 64   GLN A O   1 
ATOM   279  C  CB  . GLN A 1 64   ? 15.676 55.263  7.389   1.00 11.99 ? 64   GLN A CB  1 
ATOM   280  C  CG  . GLN A 1 64   ? 15.543 56.802  7.374   1.00 11.74 ? 64   GLN A CG  1 
ATOM   281  C  CD  . GLN A 1 64   ? 16.876 57.500  7.299   1.00 12.70 ? 64   GLN A CD  1 
ATOM   282  O  OE1 . GLN A 1 64   ? 17.783 57.207  8.080   1.00 12.22 ? 64   GLN A OE1 1 
ATOM   283  N  NE2 . GLN A 1 64   ? 16.976 58.469  6.368   1.00 11.46 ? 64   GLN A NE2 1 
ATOM   284  N  N   . GLY A 1 65   ? 14.077 52.475  8.982   1.00 12.56 ? 65   GLY A N   1 
ATOM   285  C  CA  . GLY A 1 65   ? 14.010 51.024  8.976   1.00 12.39 ? 65   GLY A CA  1 
ATOM   286  C  C   . GLY A 1 65   ? 12.643 50.470  9.372   1.00 13.12 ? 65   GLY A C   1 
ATOM   287  O  O   . GLY A 1 65   ? 11.628 50.811  8.739   1.00 13.66 ? 65   GLY A O   1 
ATOM   288  N  N   . TRP A 1 66   ? 12.629 49.615  10.390  1.00 12.21 ? 66   TRP A N   1 
ATOM   289  C  CA  . TRP A 1 66   ? 11.384 49.008  10.873  1.00 13.14 ? 66   TRP A CA  1 
ATOM   290  C  C   . TRP A 1 66   ? 11.643 48.585  12.310  1.00 13.14 ? 66   TRP A C   1 
ATOM   291  O  O   . TRP A 1 66   ? 12.773 48.680  12.771  1.00 12.92 ? 66   TRP A O   1 
ATOM   292  C  CB  . TRP A 1 66   ? 11.008 47.802  9.978   1.00 13.46 ? 66   TRP A CB  1 
ATOM   293  C  CG  . TRP A 1 66   ? 11.949 46.622  10.117  1.00 13.18 ? 66   TRP A CG  1 
ATOM   294  C  CD1 . TRP A 1 66   ? 11.828 45.605  11.016  1.00 12.22 ? 66   TRP A CD1 1 
ATOM   295  C  CD2 . TRP A 1 66   ? 13.167 46.363  9.399   1.00 13.07 ? 66   TRP A CD2 1 
ATOM   296  N  NE1 . TRP A 1 66   ? 12.879 44.726  10.939  1.00 14.61 ? 66   TRP A NE1 1 
ATOM   297  C  CE2 . TRP A 1 66   ? 13.725 45.158  9.943   1.00 12.49 ? 66   TRP A CE2 1 
ATOM   298  C  CE3 . TRP A 1 66   ? 13.846 47.009  8.341   1.00 13.29 ? 66   TRP A CE3 1 
ATOM   299  C  CZ2 . TRP A 1 66   ? 14.921 44.591  9.477   1.00 14.23 ? 66   TRP A CZ2 1 
ATOM   300  C  CZ3 . TRP A 1 66   ? 15.044 46.426  7.872   1.00 13.71 ? 66   TRP A CZ3 1 
ATOM   301  C  CH2 . TRP A 1 66   ? 15.567 45.239  8.437   1.00 14.56 ? 66   TRP A CH2 1 
ATOM   302  N  N   . ASN A 1 67   ? 10.603 48.144  13.031  1.00 13.65 ? 67   ASN A N   1 
ATOM   303  C  CA  . ASN A 1 67   ? 10.773 47.655  14.429  1.00 14.00 ? 67   ASN A CA  1 
ATOM   304  C  C   . ASN A 1 67   ? 11.403 46.255  14.400  1.00 14.99 ? 67   ASN A C   1 
ATOM   305  O  O   . ASN A 1 67   ? 10.751 45.274  14.076  1.00 14.21 ? 67   ASN A O   1 
ATOM   306  C  CB  . ASN A 1 67   ? 9.415  47.553  15.121  1.00 18.61 ? 67   ASN A CB  1 
ATOM   307  C  CG  . ASN A 1 67   ? 8.846  48.892  15.482  1.00 19.99 ? 67   ASN A CG  1 
ATOM   308  O  OD1 . ASN A 1 67   ? 9.478  49.934  15.341  1.00 22.67 ? 67   ASN A OD1 1 
ATOM   309  N  ND2 . ASN A 1 67   ? 7.626  48.872  15.986  1.00 22.66 ? 67   ASN A ND2 1 
ATOM   310  N  N   . ILE A 1 68   ? 12.685 46.165  14.745  1.00 14.13 ? 68   ILE A N   1 
ATOM   311  C  CA  . ILE A 1 68   ? 13.399 44.897  14.652  1.00 14.69 ? 68   ILE A CA  1 
ATOM   312  C  C   . ILE A 1 68   ? 12.961 43.976  15.794  1.00 15.32 ? 68   ILE A C   1 
ATOM   313  O  O   . ILE A 1 68   ? 12.817 44.396  16.944  1.00 15.21 ? 68   ILE A O   1 
ATOM   314  C  CB  . ILE A 1 68   ? 14.969 45.121  14.726  1.00 12.86 ? 68   ILE A CB  1 
ATOM   315  C  CG1 . ILE A 1 68   ? 15.482 45.991  13.554  1.00 13.05 ? 68   ILE A CG1 1 
ATOM   316  C  CG2 . ILE A 1 68   ? 15.697 43.731  14.747  1.00 15.06 ? 68   ILE A CG2 1 
ATOM   317  C  CD1 . ILE A 1 68   ? 16.955 46.469  13.747  1.00 13.31 ? 68   ILE A CD1 1 
ATOM   318  N  N   . LYS A 1 69   ? 12.748 42.707  15.435  1.00 17.22 ? 69   LYS A N   1 
ATOM   319  C  CA  . LYS A 1 69   ? 12.355 41.679  16.401  1.00 19.16 ? 69   LYS A CA  1 
ATOM   320  C  C   . LYS A 1 69   ? 13.413 40.595  16.409  1.00 18.51 ? 69   LYS A C   1 
ATOM   321  O  O   . LYS A 1 69   ? 14.041 40.308  15.396  1.00 19.67 ? 69   LYS A O   1 
ATOM   322  C  CB  . LYS A 1 69   ? 11.020 41.018  16.008  1.00 21.65 ? 69   LYS A CB  1 
ATOM   323  C  CG  . LYS A 1 69   ? 9.841  41.974  15.935  1.00 23.89 ? 69   LYS A CG  1 
ATOM   324  C  CD  . LYS A 1 69   ? 9.631  42.684  17.244  1.00 25.49 ? 69   LYS A CD  1 
ATOM   325  C  CE  . LYS A 1 69   ? 8.470  43.650  17.120  1.00 29.26 ? 69   LYS A CE  1 
ATOM   326  N  NZ  . LYS A 1 69   ? 7.285  42.899  16.607  1.00 30.04 ? 69   LYS A NZ  1 
ATOM   327  N  N   . TYR A 1 70   ? 13.647 40.008  17.566  1.00 18.85 ? 70   TYR A N   1 
ATOM   328  C  CA  . TYR A 1 70   ? 14.594 38.897  17.640  1.00 16.90 ? 70   TYR A CA  1 
ATOM   329  C  C   . TYR A 1 70   ? 14.033 37.797  18.556  1.00 19.70 ? 70   TYR A C   1 
ATOM   330  O  O   . TYR A 1 70   ? 13.099 38.043  19.336  1.00 18.29 ? 70   TYR A O   1 
ATOM   331  C  CB  . TYR A 1 70   ? 16.000 39.380  18.129  1.00 16.32 ? 70   TYR A CB  1 
ATOM   332  C  CG  . TYR A 1 70   ? 16.062 39.960  19.525  1.00 14.30 ? 70   TYR A CG  1 
ATOM   333  C  CD1 . TYR A 1 70   ? 16.230 39.137  20.670  1.00 14.41 ? 70   TYR A CD1 1 
ATOM   334  C  CD2 . TYR A 1 70   ? 15.948 41.320  19.712  1.00 14.70 ? 70   TYR A CD2 1 
ATOM   335  C  CE1 . TYR A 1 70   ? 16.259 39.703  21.974  1.00 12.66 ? 70   TYR A CE1 1 
ATOM   336  C  CE2 . TYR A 1 70   ? 15.988 41.890  20.966  1.00 15.32 ? 70   TYR A CE2 1 
ATOM   337  C  CZ  . TYR A 1 70   ? 16.122 41.098  22.095  1.00 13.95 ? 70   TYR A CZ  1 
ATOM   338  O  OH  . TYR A 1 70   ? 16.008 41.686  23.343  1.00 14.61 ? 70   TYR A OH  1 
ATOM   339  N  N   . ASP A 1 71   ? 14.576 36.594  18.430  1.00 20.43 ? 71   ASP A N   1 
ATOM   340  C  CA  . ASP A 1 71   ? 14.132 35.496  19.267  1.00 21.63 ? 71   ASP A CA  1 
ATOM   341  C  C   . ASP A 1 71   ? 15.088 35.452  20.448  1.00 21.91 ? 71   ASP A C   1 
ATOM   342  O  O   . ASP A 1 71   ? 16.270 35.188  20.272  1.00 21.25 ? 71   ASP A O   1 
ATOM   343  C  CB  . ASP A 1 71   ? 14.186 34.205  18.455  1.00 23.01 ? 71   ASP A CB  1 
ATOM   344  C  CG  . ASP A 1 71   ? 13.898 32.978  19.299  1.00 26.03 ? 71   ASP A CG  1 
ATOM   345  O  OD1 . ASP A 1 71   ? 13.539 33.153  20.492  1.00 27.67 ? 71   ASP A OD1 1 
ATOM   346  O  OD2 . ASP A 1 71   ? 14.047 31.846  18.784  1.00 29.46 ? 71   ASP A OD2 1 
ATOM   347  N  N   . PRO A 1 72   ? 14.582 35.719  21.675  1.00 22.81 ? 72   PRO A N   1 
ATOM   348  C  CA  . PRO A 1 72   ? 15.515 35.689  22.807  1.00 22.53 ? 72   PRO A CA  1 
ATOM   349  C  C   . PRO A 1 72   ? 16.301 34.390  22.943  1.00 22.43 ? 72   PRO A C   1 
ATOM   350  O  O   . PRO A 1 72   ? 17.397 34.397  23.491  1.00 24.27 ? 72   PRO A O   1 
ATOM   351  C  CB  . PRO A 1 72   ? 14.625 35.992  24.035  1.00 23.48 ? 72   PRO A CB  1 
ATOM   352  C  CG  . PRO A 1 72   ? 13.236 35.753  23.565  1.00 24.83 ? 72   PRO A CG  1 
ATOM   353  C  CD  . PRO A 1 72   ? 13.244 36.148  22.105  1.00 22.97 ? 72   PRO A CD  1 
ATOM   354  N  N   . LEU A 1 73   ? 15.783 33.287  22.411  1.00 23.09 ? 73   LEU A N   1 
ATOM   355  C  CA  . LEU A 1 73   ? 16.502 32.003  22.555  1.00 24.20 ? 73   LEU A CA  1 
ATOM   356  C  C   . LEU A 1 73   ? 17.578 31.744  21.506  1.00 23.62 ? 73   LEU A C   1 
ATOM   357  O  O   . LEU A 1 73   ? 18.172 30.674  21.483  1.00 23.45 ? 73   LEU A O   1 
ATOM   358  C  CB  . LEU A 1 73   ? 15.511 30.815  22.586  1.00 25.09 ? 73   LEU A CB  1 
ATOM   359  C  CG  . LEU A 1 73   ? 14.384 30.930  23.632  1.00 26.24 ? 73   LEU A CG  1 
ATOM   360  C  CD1 . LEU A 1 73   ? 13.368 29.803  23.441  1.00 28.07 ? 73   LEU A CD1 1 
ATOM   361  C  CD2 . LEU A 1 73   ? 14.979 30.947  25.054  1.00 27.66 ? 73   LEU A CD2 1 
ATOM   362  N  N   . LYS A 1 74   ? 17.837 32.731  20.641  1.00 22.49 ? 74   LYS A N   1 
ATOM   363  C  CA  . LYS A 1 74   ? 18.838 32.558  19.605  1.00 21.64 ? 74   LYS A CA  1 
ATOM   364  C  C   . LYS A 1 74   ? 20.225 32.421  20.244  1.00 21.92 ? 74   LYS A C   1 
ATOM   365  O  O   . LYS A 1 74   ? 21.068 31.627  19.817  1.00 22.12 ? 74   LYS A O   1 
ATOM   366  C  CB  . LYS A 1 74   ? 18.767 33.738  18.606  1.00 21.27 ? 74   LYS A CB  1 
ATOM   367  C  CG  . LYS A 1 74   ? 19.905 33.768  17.601  1.00 22.15 ? 74   LYS A CG  1 
ATOM   368  C  CD  . LYS A 1 74   ? 19.753 34.938  16.619  1.00 22.74 ? 74   LYS A CD  1 
ATOM   369  C  CE  . LYS A 1 74   ? 20.638 34.746  15.368  1.00 23.38 ? 74   LYS A CE  1 
ATOM   370  N  NZ  . LYS A 1 74   ? 20.371 35.735  14.265  1.00 21.93 ? 74   LYS A NZ  1 
ATOM   371  N  N   . TYR A 1 75   ? 20.464 33.204  21.284  1.00 21.54 ? 75   TYR A N   1 
ATOM   372  C  CA  . TYR A 1 75   ? 21.737 33.126  21.973  1.00 21.86 ? 75   TYR A CA  1 
ATOM   373  C  C   . TYR A 1 75   ? 21.512 32.327  23.291  1.00 22.04 ? 75   TYR A C   1 
ATOM   374  O  O   . TYR A 1 75   ? 20.480 32.473  23.940  1.00 23.99 ? 75   TYR A O   1 
ATOM   375  C  CB  . TYR A 1 75   ? 22.269 34.570  22.180  1.00 21.56 ? 75   TYR A CB  1 
ATOM   376  C  CG  . TYR A 1 75   ? 22.663 35.243  20.854  1.00 19.29 ? 75   TYR A CG  1 
ATOM   377  C  CD1 . TYR A 1 75   ? 23.716 34.725  20.091  1.00 21.21 ? 75   TYR A CD1 1 
ATOM   378  C  CD2 . TYR A 1 75   ? 21.914 36.297  20.311  1.00 19.19 ? 75   TYR A CD2 1 
ATOM   379  C  CE1 . TYR A 1 75   ? 24.029 35.222  18.802  1.00 21.65 ? 75   TYR A CE1 1 
ATOM   380  C  CE2 . TYR A 1 75   ? 22.198 36.802  19.034  1.00 20.58 ? 75   TYR A CE2 1 
ATOM   381  C  CZ  . TYR A 1 75   ? 23.267 36.247  18.277  1.00 22.30 ? 75   TYR A CZ  1 
ATOM   382  O  OH  . TYR A 1 75   ? 23.535 36.657  16.971  1.00 24.29 ? 75   TYR A OH  1 
ATOM   383  N  N   . ASN A 1 76   ? 22.459 31.446  23.621  1.00 23.22 ? 76   ASN A N   1 
ATOM   384  C  CA  . ASN A 1 76   ? 22.412 30.582  24.806  1.00 23.89 ? 76   ASN A CA  1 
ATOM   385  C  C   . ASN A 1 76   ? 23.827 30.276  25.262  1.00 24.52 ? 76   ASN A C   1 
ATOM   386  O  O   . ASN A 1 76   ? 24.779 30.690  24.605  1.00 23.64 ? 76   ASN A O   1 
ATOM   387  C  CB  . ASN A 1 76   ? 21.695 29.268  24.501  1.00 23.04 ? 76   ASN A CB  1 
ATOM   388  C  CG  . ASN A 1 76   ? 22.289 28.547  23.325  1.00 23.97 ? 76   ASN A CG  1 
ATOM   389  O  OD1 . ASN A 1 76   ? 23.477 28.212  23.294  1.00 24.90 ? 76   ASN A OD1 1 
ATOM   390  N  ND2 . ASN A 1 76   ? 21.455 28.303  22.327  1.00 27.82 ? 76   ASN A ND2 1 
ATOM   391  N  N   . ALA A 1 77   ? 23.986 29.512  26.350  1.00 25.13 ? 77   ALA A N   1 
ATOM   392  C  CA  . ALA A 1 77   ? 25.328 29.238  26.885  1.00 26.66 ? 77   ALA A CA  1 
ATOM   393  C  C   . ALA A 1 77   ? 26.307 28.726  25.866  1.00 27.30 ? 77   ALA A C   1 
ATOM   394  O  O   . ALA A 1 77   ? 27.496 29.037  25.935  1.00 27.62 ? 77   ALA A O   1 
ATOM   395  C  CB  . ALA A 1 77   ? 25.265 28.263  28.074  1.00 27.13 ? 77   ALA A CB  1 
ATOM   396  N  N   . HIS A 1 78   ? 25.804 27.967  24.899  1.00 28.89 ? 78   HIS A N   1 
ATOM   397  C  CA  . HIS A 1 78   ? 26.669 27.397  23.868  1.00 30.01 ? 78   HIS A CA  1 
ATOM   398  C  C   . HIS A 1 78   ? 26.766 28.236  22.585  1.00 28.82 ? 78   HIS A C   1 
ATOM   399  O  O   . HIS A 1 78   ? 27.405 27.829  21.598  1.00 28.84 ? 78   HIS A O   1 
ATOM   400  C  CB  . HIS A 1 78   ? 26.174 25.986  23.548  1.00 33.16 ? 78   HIS A CB  1 
ATOM   401  C  CG  . HIS A 1 78   ? 25.998 25.148  24.771  1.00 36.51 ? 78   HIS A CG  1 
ATOM   402  N  ND1 . HIS A 1 78   ? 27.066 24.601  25.453  1.00 37.65 ? 78   HIS A ND1 1 
ATOM   403  C  CD2 . HIS A 1 78   ? 24.896 24.891  25.519  1.00 37.71 ? 78   HIS A CD2 1 
ATOM   404  C  CE1 . HIS A 1 78   ? 26.630 24.050  26.575  1.00 39.08 ? 78   HIS A CE1 1 
ATOM   405  N  NE2 . HIS A 1 78   ? 25.318 24.213  26.640  1.00 39.47 ? 78   HIS A NE2 1 
ATOM   406  N  N   . HIS A 1 79   ? 26.159 29.417  22.605  1.00 25.32 ? 79   HIS A N   1 
ATOM   407  C  CA  . HIS A 1 79   ? 26.200 30.268  21.422  1.00 22.61 ? 79   HIS A CA  1 
ATOM   408  C  C   . HIS A 1 79   ? 25.911 31.675  21.905  1.00 19.29 ? 79   HIS A C   1 
ATOM   409  O  O   . HIS A 1 79   ? 24.769 32.128  21.917  1.00 17.86 ? 79   HIS A O   1 
ATOM   410  C  CB  . HIS A 1 79   ? 25.127 29.808  20.417  1.00 22.45 ? 79   HIS A CB  1 
ATOM   411  C  CG  . HIS A 1 79   ? 25.166 30.530  19.101  1.00 24.06 ? 79   HIS A CG  1 
ATOM   412  N  ND1 . HIS A 1 79   ? 26.207 30.395  18.204  1.00 25.13 ? 79   HIS A ND1 1 
ATOM   413  C  CD2 . HIS A 1 79   ? 24.316 31.430  18.561  1.00 23.22 ? 79   HIS A CD2 1 
ATOM   414  C  CE1 . HIS A 1 79   ? 25.994 31.186  17.164  1.00 24.13 ? 79   HIS A CE1 1 
ATOM   415  N  NE2 . HIS A 1 79   ? 24.851 31.827  17.357  1.00 25.85 ? 79   HIS A NE2 1 
ATOM   416  N  N   . LYS A 1 80   ? 26.973 32.330  22.352  1.00 18.20 ? 80   LYS A N   1 
ATOM   417  C  CA  . LYS A 1 80   ? 26.853 33.669  22.897  1.00 17.75 ? 80   LYS A CA  1 
ATOM   418  C  C   . LYS A 1 80   ? 27.084 34.713  21.826  1.00 16.25 ? 80   LYS A C   1 
ATOM   419  O  O   . LYS A 1 80   ? 27.737 34.449  20.809  1.00 17.31 ? 80   LYS A O   1 
ATOM   420  C  CB  . LYS A 1 80   ? 27.905 33.886  23.978  1.00 18.12 ? 80   LYS A CB  1 
ATOM   421  C  CG  . LYS A 1 80   ? 27.815 32.872  25.131  1.00 19.43 ? 80   LYS A CG  1 
ATOM   422  C  CD  . LYS A 1 80   ? 29.049 32.933  25.993  1.00 22.46 ? 80   LYS A CD  1 
ATOM   423  C  CE  . LYS A 1 80   ? 29.025 34.165  26.905  1.00 24.13 ? 80   LYS A CE  1 
ATOM   424  N  NZ  . LYS A 1 80   ? 29.867 33.887  28.157  1.00 26.21 ? 80   LYS A NZ  1 
ATOM   425  N  N   . LEU A 1 81   ? 26.525 35.885  22.060  1.00 13.89 ? 81   LEU A N   1 
ATOM   426  C  CA  . LEU A 1 81   ? 26.751 37.019  21.167  1.00 12.33 ? 81   LEU A CA  1 
ATOM   427  C  C   . LEU A 1 81   ? 28.049 37.716  21.664  1.00 12.01 ? 81   LEU A C   1 
ATOM   428  O  O   . LEU A 1 81   ? 28.095 38.154  22.824  1.00 11.78 ? 81   LEU A O   1 
ATOM   429  C  CB  . LEU A 1 81   ? 25.579 38.020  21.265  1.00 12.36 ? 81   LEU A CB  1 
ATOM   430  C  CG  . LEU A 1 81   ? 25.622 39.306  20.394  1.00 10.94 ? 81   LEU A CG  1 
ATOM   431  C  CD1 . LEU A 1 81   ? 25.736 38.949  18.855  1.00 9.67  ? 81   LEU A CD1 1 
ATOM   432  C  CD2 . LEU A 1 81   ? 24.377 40.187  20.705  1.00 12.24 ? 81   LEU A CD2 1 
ATOM   433  N  N   . LYS A 1 82   ? 29.087 37.825  20.829  1.00 10.04 ? 82   LYS A N   1 
ATOM   434  C  CA  . LYS A 1 82   ? 30.352 38.467  21.185  1.00 11.34 ? 82   LYS A CA  1 
ATOM   435  C  C   . LYS A 1 82   ? 30.233 39.883  20.657  1.00 11.35 ? 82   LYS A C   1 
ATOM   436  O  O   . LYS A 1 82   ? 29.961 40.076  19.510  1.00 13.26 ? 82   LYS A O   1 
ATOM   437  C  CB  . LYS A 1 82   ? 31.533 37.728  20.531  1.00 14.18 ? 82   LYS A CB  1 
ATOM   438  C  CG  . LYS A 1 82   ? 31.633 36.262  20.940  1.00 17.84 ? 82   LYS A CG  1 
ATOM   439  C  CD  . LYS A 1 82   ? 32.661 35.438  20.143  1.00 22.88 ? 82   LYS A CD  1 
ATOM   440  C  CE  . LYS A 1 82   ? 32.465 33.953  20.434  1.00 24.27 ? 82   LYS A CE  1 
ATOM   441  N  NZ  . LYS A 1 82   ? 32.958 33.037  19.362  1.00 27.64 ? 82   LYS A NZ  1 
ATOM   442  N  N   . VAL A 1 83   ? 30.420 40.857  21.545  1.00 9.67  ? 83   VAL A N   1 
ATOM   443  C  CA  . VAL A 1 83   ? 30.272 42.269  21.207  1.00 8.84  ? 83   VAL A CA  1 
ATOM   444  C  C   . VAL A 1 83   ? 31.579 43.005  21.392  1.00 9.92  ? 83   VAL A C   1 
ATOM   445  O  O   . VAL A 1 83   ? 32.168 42.935  22.469  1.00 9.49  ? 83   VAL A O   1 
ATOM   446  C  CB  . VAL A 1 83   ? 29.208 42.915  22.117  1.00 10.94 ? 83   VAL A CB  1 
ATOM   447  C  CG1 . VAL A 1 83   ? 28.987 44.413  21.721  1.00 11.42 ? 83   VAL A CG1 1 
ATOM   448  C  CG2 . VAL A 1 83   ? 27.850 42.121  21.961  1.00 10.38 ? 83   VAL A CG2 1 
ATOM   449  N  N   . PHE A 1 84   ? 32.024 43.673  20.333  1.00 9.56  ? 84   PHE A N   1 
ATOM   450  C  CA  . PHE A 1 84   ? 33.236 44.472  20.334  1.00 10.18 ? 84   PHE A CA  1 
ATOM   451  C  C   . PHE A 1 84   ? 32.859 45.936  20.250  1.00 10.20 ? 84   PHE A C   1 
ATOM   452  O  O   . PHE A 1 84   ? 32.328 46.371  19.213  1.00 9.86  ? 84   PHE A O   1 
ATOM   453  C  CB  . PHE A 1 84   ? 34.120 44.103  19.116  1.00 11.35 ? 84   PHE A CB  1 
ATOM   454  C  CG  . PHE A 1 84   ? 34.784 42.753  19.252  1.00 12.75 ? 84   PHE A CG  1 
ATOM   455  C  CD1 . PHE A 1 84   ? 35.881 42.554  20.096  1.00 14.58 ? 84   PHE A CD1 1 
ATOM   456  C  CD2 . PHE A 1 84   ? 34.281 41.674  18.579  1.00 11.99 ? 84   PHE A CD2 1 
ATOM   457  C  CE1 . PHE A 1 84   ? 36.455 41.275  20.244  1.00 13.38 ? 84   PHE A CE1 1 
ATOM   458  C  CE2 . PHE A 1 84   ? 34.862 40.386  18.728  1.00 14.54 ? 84   PHE A CE2 1 
ATOM   459  C  CZ  . PHE A 1 84   ? 35.937 40.212  19.556  1.00 12.70 ? 84   PHE A CZ  1 
ATOM   460  N  N   . VAL A 1 85   ? 33.178 46.668  21.329  1.00 8.93  ? 85   VAL A N   1 
ATOM   461  C  CA  . VAL A 1 85   ? 32.937 48.101  21.396  1.00 8.82  ? 85   VAL A CA  1 
ATOM   462  C  C   . VAL A 1 85   ? 34.257 48.741  21.024  1.00 7.40  ? 85   VAL A C   1 
ATOM   463  O  O   . VAL A 1 85   ? 35.257 48.561  21.748  1.00 9.24  ? 85   VAL A O   1 
ATOM   464  C  CB  . VAL A 1 85   ? 32.461 48.487  22.808  1.00 8.94  ? 85   VAL A CB  1 
ATOM   465  C  CG1 . VAL A 1 85   ? 32.212 50.015  22.911  1.00 10.18 ? 85   VAL A CG1 1 
ATOM   466  C  CG2 . VAL A 1 85   ? 31.129 47.716  23.099  1.00 10.53 ? 85   VAL A CG2 1 
ATOM   467  N  N   . VAL A 1 86   ? 34.225 49.501  19.910  1.00 7.79  ? 86   VAL A N   1 
ATOM   468  C  CA  . VAL A 1 86   ? 35.439 50.048  19.322  1.00 6.98  ? 86   VAL A CA  1 
ATOM   469  C  C   . VAL A 1 86   ? 35.511 51.561  19.425  1.00 8.42  ? 86   VAL A C   1 
ATOM   470  O  O   . VAL A 1 86   ? 34.866 52.266  18.668  1.00 7.38  ? 86   VAL A O   1 
ATOM   471  C  CB  . VAL A 1 86   ? 35.544 49.547  17.820  1.00 6.85  ? 86   VAL A CB  1 
ATOM   472  C  CG1 . VAL A 1 86   ? 36.843 50.034  17.191  1.00 7.80  ? 86   VAL A CG1 1 
ATOM   473  C  CG2 . VAL A 1 86   ? 35.485 48.005  17.762  1.00 6.77  ? 86   VAL A CG2 1 
ATOM   474  N  N   . PRO A 1 87   ? 36.306 52.060  20.384  1.00 8.86  ? 87   PRO A N   1 
ATOM   475  C  CA  . PRO A 1 87   ? 36.443 53.520  20.562  1.00 9.90  ? 87   PRO A CA  1 
ATOM   476  C  C   . PRO A 1 87   ? 37.161 54.158  19.352  1.00 8.63  ? 87   PRO A C   1 
ATOM   477  O  O   . PRO A 1 87   ? 38.127 53.601  18.799  1.00 8.91  ? 87   PRO A O   1 
ATOM   478  C  CB  . PRO A 1 87   ? 37.257 53.650  21.855  1.00 8.83  ? 87   PRO A CB  1 
ATOM   479  C  CG  . PRO A 1 87   ? 36.993 52.318  22.585  1.00 11.97 ? 87   PRO A CG  1 
ATOM   480  C  CD  . PRO A 1 87   ? 37.008 51.319  21.453  1.00 9.54  ? 87   PRO A CD  1 
ATOM   481  N  N   . HIS A 1 88   ? 36.695 55.334  18.968  1.00 7.66  ? 88   HIS A N   1 
ATOM   482  C  CA  . HIS A 1 88   ? 37.256 56.013  17.800  1.00 7.22  ? 88   HIS A CA  1 
ATOM   483  C  C   . HIS A 1 88   ? 37.027 57.504  17.884  1.00 9.01  ? 88   HIS A C   1 
ATOM   484  O  O   . HIS A 1 88   ? 36.150 57.985  18.637  1.00 8.71  ? 88   HIS A O   1 
ATOM   485  C  CB  . HIS A 1 88   ? 36.641 55.387  16.491  1.00 7.88  ? 88   HIS A CB  1 
ATOM   486  C  CG  . HIS A 1 88   ? 35.198 55.740  16.220  1.00 8.13  ? 88   HIS A CG  1 
ATOM   487  N  ND1 . HIS A 1 88   ? 34.822 56.811  15.417  1.00 8.69  ? 88   HIS A ND1 1 
ATOM   488  C  CD2 . HIS A 1 88   ? 34.036 55.181  16.660  1.00 7.92  ? 88   HIS A CD2 1 
ATOM   489  C  CE1 . HIS A 1 88   ? 33.506 56.877  15.369  1.00 8.78  ? 88   HIS A CE1 1 
ATOM   490  N  NE2 . HIS A 1 88   ? 33.008 55.904  16.114  1.00 8.23  ? 88   HIS A NE2 1 
ATOM   491  N  N   . SER A 1 89   ? 37.769 58.246  17.071  1.00 7.89  ? 89   SER A N   1 
ATOM   492  C  CA  . SER A 1 89   ? 37.646 59.729  17.055  1.00 7.95  ? 89   SER A CA  1 
ATOM   493  C  C   . SER A 1 89   ? 37.821 60.180  15.643  1.00 8.13  ? 89   SER A C   1 
ATOM   494  O  O   . SER A 1 89   ? 38.911 60.017  15.100  1.00 6.44  ? 89   SER A O   1 
ATOM   495  C  CB  . SER A 1 89   ? 38.715 60.332  17.969  1.00 10.39 ? 89   SER A CB  1 
ATOM   496  O  OG  . SER A 1 89   ? 38.657 61.742  17.931  1.00 7.86  ? 89   SER A OG  1 
ATOM   497  N  N   . HIS A 1 90   ? 36.785 60.724  15.015  1.00 7.23  ? 90   HIS A N   1 
ATOM   498  C  CA  . HIS A 1 90   ? 36.913 61.170  13.634  1.00 8.15  ? 90   HIS A CA  1 
ATOM   499  C  C   . HIS A 1 90   ? 37.574 62.559  13.573  1.00 8.09  ? 90   HIS A C   1 
ATOM   500  O  O   . HIS A 1 90   ? 37.009 63.551  14.036  1.00 8.64  ? 90   HIS A O   1 
ATOM   501  C  CB  . HIS A 1 90   ? 35.517 61.181  13.013  1.00 7.68  ? 90   HIS A CB  1 
ATOM   502  C  CG  . HIS A 1 90   ? 35.494 61.558  11.557  1.00 6.77  ? 90   HIS A CG  1 
ATOM   503  N  ND1 . HIS A 1 90   ? 36.014 60.746  10.571  1.00 7.32  ? 90   HIS A ND1 1 
ATOM   504  C  CD2 . HIS A 1 90   ? 34.980 62.639  10.921  1.00 5.88  ? 90   HIS A CD2 1 
ATOM   505  C  CE1 . HIS A 1 90   ? 35.799 61.307  9.389   1.00 8.01  ? 90   HIS A CE1 1 
ATOM   506  N  NE2 . HIS A 1 90   ? 35.181 62.461  9.575   1.00 6.58  ? 90   HIS A NE2 1 
ATOM   507  N  N   . ASN A 1 91   ? 38.746 62.623  12.956  1.00 8.23  ? 91   ASN A N   1 
ATOM   508  C  CA  . ASN A 1 91   ? 39.514 63.879  12.884  1.00 6.67  ? 91   ASN A CA  1 
ATOM   509  C  C   . ASN A 1 91   ? 39.680 64.351  11.452  1.00 9.90  ? 91   ASN A C   1 
ATOM   510  O  O   . ASN A 1 91   ? 40.520 63.807  10.708  1.00 12.79 ? 91   ASN A O   1 
ATOM   511  C  CB  . ASN A 1 91   ? 40.895 63.643  13.532  1.00 8.35  ? 91   ASN A CB  1 
ATOM   512  C  CG  . ASN A 1 91   ? 40.823 63.575  15.045  1.00 9.40  ? 91   ASN A CG  1 
ATOM   513  O  OD1 . ASN A 1 91   ? 41.379 64.415  15.747  1.00 11.74 ? 91   ASN A OD1 1 
ATOM   514  N  ND2 . ASN A 1 91   ? 40.165 62.546  15.568  1.00 8.09  ? 91   ASN A ND2 1 
ATOM   515  N  N   . ASP A 1 92   ? 38.939 65.382  11.103  1.00 6.38  ? 92   ASP A N   1 
ATOM   516  C  CA  . ASP A 1 92   ? 39.055 65.920  9.736   1.00 7.98  ? 92   ASP A CA  1 
ATOM   517  C  C   . ASP A 1 92   ? 40.275 66.774  9.603   1.00 8.47  ? 92   ASP A C   1 
ATOM   518  O  O   . ASP A 1 92   ? 40.485 67.705  10.400  1.00 8.87  ? 92   ASP A O   1 
ATOM   519  C  CB  . ASP A 1 92   ? 37.836 66.805  9.471   1.00 6.97  ? 92   ASP A CB  1 
ATOM   520  C  CG  . ASP A 1 92   ? 36.548 65.995  9.532   1.00 9.41  ? 92   ASP A CG  1 
ATOM   521  O  OD1 . ASP A 1 92   ? 36.334 65.156  8.645   1.00 9.05  ? 92   ASP A OD1 1 
ATOM   522  O  OD2 . ASP A 1 92   ? 35.808 66.247  10.519  1.00 10.78 ? 92   ASP A OD2 1 
ATOM   523  N  N   . PRO A 1 93   ? 41.090 66.491  8.545   1.00 6.81  ? 93   PRO A N   1 
ATOM   524  C  CA  . PRO A 1 93   ? 42.322 67.294  8.264   1.00 10.87 ? 93   PRO A CA  1 
ATOM   525  C  C   . PRO A 1 93   ? 41.883 68.571  7.462   1.00 9.33  ? 93   PRO A C   1 
ATOM   526  O  O   . PRO A 1 93   ? 42.191 68.765  6.266   1.00 8.68  ? 93   PRO A O   1 
ATOM   527  C  CB  . PRO A 1 93   ? 43.176 66.345  7.415   1.00 10.49 ? 93   PRO A CB  1 
ATOM   528  C  CG  . PRO A 1 93   ? 42.644 64.953  7.751   1.00 10.84 ? 93   PRO A CG  1 
ATOM   529  C  CD  . PRO A 1 93   ? 41.113 65.215  7.791   1.00 8.81  ? 93   PRO A CD  1 
ATOM   530  N  N   . GLY A 1 94   ? 41.062 69.357  8.133   1.00 10.99 ? 94   GLY A N   1 
ATOM   531  C  CA  . GLY A 1 94   ? 40.487 70.571  7.599   1.00 8.64  ? 94   GLY A CA  1 
ATOM   532  C  C   . GLY A 1 94   ? 38.988 70.389  7.404   1.00 8.12  ? 94   GLY A C   1 
ATOM   533  O  O   . GLY A 1 94   ? 38.562 69.333  6.789   1.00 10.09 ? 94   GLY A O   1 
ATOM   534  N  N   . TRP A 1 95   ? 38.193 71.369  7.888   1.00 8.82  ? 95   TRP A N   1 
ATOM   535  C  CA  . TRP A 1 95   ? 36.770 71.431  7.655   1.00 8.48  ? 95   TRP A CA  1 
ATOM   536  C  C   . TRP A 1 95   ? 36.285 72.836  8.109   1.00 10.05 ? 95   TRP A C   1 
ATOM   537  O  O   . TRP A 1 95   ? 36.221 73.712  7.275   1.00 9.32  ? 95   TRP A O   1 
ATOM   538  C  CB  . TRP A 1 95   ? 35.971 70.259  8.306   1.00 7.19  ? 95   TRP A CB  1 
ATOM   539  C  CG  . TRP A 1 95   ? 34.474 70.408  7.931   1.00 8.19  ? 95   TRP A CG  1 
ATOM   540  C  CD1 . TRP A 1 95   ? 33.936 70.739  6.692   1.00 8.15  ? 95   TRP A CD1 1 
ATOM   541  C  CD2 . TRP A 1 95   ? 33.387 70.231  8.812   1.00 10.87 ? 95   TRP A CD2 1 
ATOM   542  N  NE1 . TRP A 1 95   ? 32.561 70.779  6.785   1.00 8.53  ? 95   TRP A NE1 1 
ATOM   543  C  CE2 . TRP A 1 95   ? 32.207 70.460  8.076   1.00 7.32  ? 95   TRP A CE2 1 
ATOM   544  C  CE3 . TRP A 1 95   ? 33.288 69.883  10.168  1.00 8.20  ? 95   TRP A CE3 1 
ATOM   545  C  CZ2 . TRP A 1 95   ? 30.920 70.341  8.678   1.00 9.74  ? 95   TRP A CZ2 1 
ATOM   546  C  CZ3 . TRP A 1 95   ? 32.008 69.764  10.755  1.00 11.86 ? 95   TRP A CZ3 1 
ATOM   547  C  CH2 . TRP A 1 95   ? 30.856 69.996  9.987   1.00 7.92  ? 95   TRP A CH2 1 
ATOM   548  N  N   . ILE A 1 96   ? 35.898 72.965  9.374   1.00 10.75 ? 96   ILE A N   1 
ATOM   549  C  CA  . ILE A 1 96   ? 35.458 74.252  9.950   1.00 13.78 ? 96   ILE A CA  1 
ATOM   550  C  C   . ILE A 1 96   ? 36.713 75.020  10.340  1.00 15.05 ? 96   ILE A C   1 
ATOM   551  O  O   . ILE A 1 96   ? 36.612 76.213  10.620  1.00 15.94 ? 96   ILE A O   1 
ATOM   552  C  CB  . ILE A 1 96   ? 34.619 74.074  11.261  1.00 15.45 ? 96   ILE A CB  1 
ATOM   553  C  CG1 . ILE A 1 96   ? 33.335 73.315  10.976  1.00 18.18 ? 96   ILE A CG1 1 
ATOM   554  C  CG2 . ILE A 1 96   ? 34.335 75.430  11.908  1.00 16.61 ? 96   ILE A CG2 1 
ATOM   555  C  CD1 . ILE A 1 96   ? 32.693 73.754  9.755   1.00 16.04 ? 96   ILE A CD1 1 
ATOM   556  N  N   . GLN A 1 97   ? 37.846 74.335  10.472  1.00 11.10 ? 97   GLN A N   1 
ATOM   557  C  CA  . GLN A 1 97   ? 39.142 74.947  10.856  1.00 13.03 ? 97   GLN A CA  1 
ATOM   558  C  C   . GLN A 1 97   ? 40.141 74.328  9.897   1.00 11.73 ? 97   GLN A C   1 
ATOM   559  O  O   . GLN A 1 97   ? 39.812 73.349  9.219   1.00 11.29 ? 97   GLN A O   1 
ATOM   560  C  CB  . GLN A 1 97   ? 39.541 74.595  12.332  1.00 12.54 ? 97   GLN A CB  1 
ATOM   561  C  CG  . GLN A 1 97   ? 38.509 75.025  13.410  1.00 18.62 ? 97   GLN A CG  1 
ATOM   562  C  CD  . GLN A 1 97   ? 39.022 74.851  14.861  1.00 21.09 ? 97   GLN A CD  1 
ATOM   563  O  OE1 . GLN A 1 97   ? 40.161 75.203  15.184  1.00 23.34 ? 97   GLN A OE1 1 
ATOM   564  N  NE2 . GLN A 1 97   ? 38.191 74.266  15.725  1.00 24.62 ? 97   GLN A NE2 1 
ATOM   565  N  N   . THR A 1 98   ? 41.360 74.869  9.792   1.00 11.39 ? 98   THR A N   1 
ATOM   566  C  CA  . THR A 1 98   ? 42.362 74.301  8.918   1.00 10.25 ? 98   THR A CA  1 
ATOM   567  C  C   . THR A 1 98   ? 42.996 73.120  9.660   1.00 10.63 ? 98   THR A C   1 
ATOM   568  O  O   . THR A 1 98   ? 42.772 72.894  10.851  1.00 8.88  ? 98   THR A O   1 
ATOM   569  C  CB  . THR A 1 98   ? 43.466 75.316  8.686   1.00 11.67 ? 98   THR A CB  1 
ATOM   570  O  OG1 . THR A 1 98   ? 44.072 75.622  9.973   1.00 12.47 ? 98   THR A OG1 1 
ATOM   571  C  CG2 . THR A 1 98   ? 42.902 76.628  8.128   1.00 9.12  ? 98   THR A CG2 1 
ATOM   572  N  N   . PHE A 1 99   ? 43.781 72.350  8.952   1.00 8.89  ? 99   PHE A N   1 
ATOM   573  C  CA  . PHE A 1 99   ? 44.498 71.230  9.575   1.00 11.18 ? 99   PHE A CA  1 
ATOM   574  C  C   . PHE A 1 99   ? 45.288 71.702  10.830  1.00 12.41 ? 99   PHE A C   1 
ATOM   575  O  O   . PHE A 1 99   ? 45.228 71.086  11.905  1.00 12.03 ? 99   PHE A O   1 
ATOM   576  C  CB  . PHE A 1 99   ? 45.488 70.748  8.550   1.00 9.70  ? 99   PHE A CB  1 
ATOM   577  C  CG  . PHE A 1 99   ? 46.351 69.616  9.041   1.00 9.45  ? 99   PHE A CG  1 
ATOM   578  C  CD1 . PHE A 1 99   ? 45.944 68.260  8.899   1.00 9.31  ? 99   PHE A CD1 1 
ATOM   579  C  CD2 . PHE A 1 99   ? 47.592 69.897  9.622   1.00 11.27 ? 99   PHE A CD2 1 
ATOM   580  C  CE1 . PHE A 1 99   ? 46.802 67.194  9.332   1.00 8.82  ? 99   PHE A CE1 1 
ATOM   581  C  CE2 . PHE A 1 99   ? 48.424 68.855  10.056  1.00 9.31  ? 99   PHE A CE2 1 
ATOM   582  C  CZ  . PHE A 1 99   ? 48.041 67.521  9.909   1.00 9.96  ? 99   PHE A CZ  1 
ATOM   583  N  N   . GLU A 1 100  ? 46.057 72.795  10.664  1.00 10.89 ? 100  GLU A N   1 
ATOM   584  C  CA  . GLU A 1 100  ? 46.871 73.221  11.803  1.00 11.58 ? 100  GLU A CA  1 
ATOM   585  C  C   . GLU A 1 100  ? 46.061 73.747  12.954  1.00 12.57 ? 100  GLU A C   1 
ATOM   586  O  O   . GLU A 1 100  ? 46.383 73.474  14.127  1.00 12.86 ? 100  GLU A O   1 
ATOM   587  C  CB  . GLU A 1 100  ? 47.937 74.240  11.368  1.00 10.90 ? 100  GLU A CB  1 
ATOM   588  C  CG  . GLU A 1 100  ? 49.000 74.599  12.446  1.00 12.75 ? 100  GLU A CG  1 
ATOM   589  C  CD  . GLU A 1 100  ? 49.871 73.451  12.900  1.00 16.52 ? 100  GLU A CD  1 
ATOM   590  O  OE1 . GLU A 1 100  ? 50.001 72.437  12.168  1.00 15.91 ? 100  GLU A OE1 1 
ATOM   591  O  OE2 . GLU A 1 100  ? 50.483 73.595  14.010  1.00 18.06 ? 100  GLU A OE2 1 
ATOM   592  N  N   . GLU A 1 101  ? 44.974 74.468  12.657  1.00 10.81 ? 101  GLU A N   1 
ATOM   593  C  CA  . GLU A 1 101  ? 44.135 74.925  13.749  1.00 11.32 ? 101  GLU A CA  1 
ATOM   594  C  C   . GLU A 1 101  ? 43.522 73.724  14.538  1.00 11.18 ? 101  GLU A C   1 
ATOM   595  O  O   . GLU A 1 101  ? 43.489 73.717  15.762  1.00 10.44 ? 101  GLU A O   1 
ATOM   596  C  CB  . GLU A 1 101  ? 42.987 75.820  13.229  1.00 13.79 ? 101  GLU A CB  1 
ATOM   597  C  CG  . GLU A 1 101  ? 43.457 77.198  12.704  1.00 14.65 ? 101  GLU A CG  1 
ATOM   598  C  CD  . GLU A 1 101  ? 42.385 77.983  11.927  1.00 19.77 ? 101  GLU A CD  1 
ATOM   599  O  OE1 . GLU A 1 101  ? 41.404 77.409  11.409  1.00 15.68 ? 101  GLU A OE1 1 
ATOM   600  O  OE2 . GLU A 1 101  ? 42.548 79.228  11.805  1.00 21.00 ? 101  GLU A OE2 1 
ATOM   601  N  N   . TYR A 1 102  ? 42.989 72.715  13.842  1.00 10.62 ? 102  TYR A N   1 
ATOM   602  C  CA  . TYR A 1 102  ? 42.418 71.549  14.566  1.00 10.50 ? 102  TYR A CA  1 
ATOM   603  C  C   . TYR A 1 102  ? 43.511 70.779  15.324  1.00 8.62  ? 102  TYR A C   1 
ATOM   604  O  O   . TYR A 1 102  ? 43.274 70.256  16.368  1.00 11.88 ? 102  TYR A O   1 
ATOM   605  C  CB  . TYR A 1 102  ? 41.776 70.535  13.607  1.00 11.10 ? 102  TYR A CB  1 
ATOM   606  C  CG  . TYR A 1 102  ? 40.368 70.850  13.143  1.00 6.41  ? 102  TYR A CG  1 
ATOM   607  C  CD1 . TYR A 1 102  ? 39.339 71.071  14.008  1.00 10.21 ? 102  TYR A CD1 1 
ATOM   608  C  CD2 . TYR A 1 102  ? 40.048 70.754  11.763  1.00 10.47 ? 102  TYR A CD2 1 
ATOM   609  C  CE1 . TYR A 1 102  ? 38.006 71.177  13.546  1.00 10.01 ? 102  TYR A CE1 1 
ATOM   610  C  CE2 . TYR A 1 102  ? 38.737 70.823  11.285  1.00 9.05  ? 102  TYR A CE2 1 
ATOM   611  C  CZ  . TYR A 1 102  ? 37.715 71.036  12.204  1.00 10.98 ? 102  TYR A CZ  1 
ATOM   612  O  OH  . TYR A 1 102  ? 36.406 71.077  11.793  1.00 11.92 ? 102  TYR A OH  1 
ATOM   613  N  N   . TYR A 1 103  ? 44.694 70.700  14.754  1.00 8.71  ? 103  TYR A N   1 
ATOM   614  C  CA  . TYR A 1 103  ? 45.754 69.982  15.444  1.00 11.24 ? 103  TYR A CA  1 
ATOM   615  C  C   . TYR A 1 103  ? 46.058 70.694  16.747  1.00 11.88 ? 103  TYR A C   1 
ATOM   616  O  O   . TYR A 1 103  ? 46.225 70.056  17.770  1.00 11.26 ? 103  TYR A O   1 
ATOM   617  C  CB  . TYR A 1 103  ? 47.023 69.941  14.594  1.00 10.95 ? 103  TYR A CB  1 
ATOM   618  C  CG  . TYR A 1 103  ? 48.178 69.338  15.308  1.00 12.52 ? 103  TYR A CG  1 
ATOM   619  C  CD1 . TYR A 1 103  ? 48.202 67.980  15.580  1.00 12.68 ? 103  TYR A CD1 1 
ATOM   620  C  CD2 . TYR A 1 103  ? 49.243 70.153  15.796  1.00 12.72 ? 103  TYR A CD2 1 
ATOM   621  C  CE1 . TYR A 1 103  ? 49.221 67.408  16.328  1.00 13.95 ? 103  TYR A CE1 1 
ATOM   622  C  CE2 . TYR A 1 103  ? 50.277 69.573  16.551  1.00 13.74 ? 103  TYR A CE2 1 
ATOM   623  C  CZ  . TYR A 1 103  ? 50.249 68.218  16.813  1.00 13.94 ? 103  TYR A CZ  1 
ATOM   624  O  OH  . TYR A 1 103  ? 51.239 67.674  17.641  1.00 18.71 ? 103  TYR A OH  1 
ATOM   625  N  N   . GLN A 1 104  ? 46.116 72.032  16.692  1.00 12.93 ? 104  GLN A N   1 
ATOM   626  C  CA  . GLN A 1 104  ? 46.452 72.790  17.903  1.00 13.50 ? 104  GLN A CA  1 
ATOM   627  C  C   . GLN A 1 104  ? 45.345 72.803  18.928  1.00 14.78 ? 104  GLN A C   1 
ATOM   628  O  O   . GLN A 1 104  ? 45.599 72.651  20.109  1.00 16.74 ? 104  GLN A O   1 
ATOM   629  C  CB  . GLN A 1 104  ? 46.789 74.249  17.560  1.00 13.74 ? 104  GLN A CB  1 
ATOM   630  C  CG  . GLN A 1 104  ? 48.153 74.512  16.898  1.00 12.92 ? 104  GLN A CG  1 
ATOM   631  C  CD  . GLN A 1 104  ? 49.349 73.922  17.694  1.00 15.37 ? 104  GLN A CD  1 
ATOM   632  O  OE1 . GLN A 1 104  ? 49.336 73.942  18.906  1.00 15.34 ? 104  GLN A OE1 1 
ATOM   633  N  NE2 . GLN A 1 104  ? 50.351 73.408  17.002  1.00 14.55 ? 104  GLN A NE2 1 
ATOM   634  N  N   . HIS A 1 105  ? 44.116 72.943  18.468  1.00 14.50 ? 105  HIS A N   1 
ATOM   635  C  CA  . HIS A 1 105  ? 42.995 73.041  19.382  1.00 16.33 ? 105  HIS A CA  1 
ATOM   636  C  C   . HIS A 1 105  ? 42.422 71.715  19.843  1.00 15.22 ? 105  HIS A C   1 
ATOM   637  O  O   . HIS A 1 105  ? 41.891 71.626  20.953  1.00 16.06 ? 105  HIS A O   1 
ATOM   638  C  CB  . HIS A 1 105  ? 41.876 73.834  18.713  1.00 17.98 ? 105  HIS A CB  1 
ATOM   639  C  CG  . HIS A 1 105  ? 42.302 75.192  18.245  1.00 21.00 ? 105  HIS A CG  1 
ATOM   640  N  ND1 . HIS A 1 105  ? 41.675 75.851  17.210  1.00 22.13 ? 105  HIS A ND1 1 
ATOM   641  C  CD2 . HIS A 1 105  ? 43.319 75.996  18.645  1.00 21.90 ? 105  HIS A CD2 1 
ATOM   642  C  CE1 . HIS A 1 105  ? 42.291 77.003  16.991  1.00 24.23 ? 105  HIS A CE1 1 
ATOM   643  N  NE2 . HIS A 1 105  ? 43.289 77.117  17.854  1.00 22.62 ? 105  HIS A NE2 1 
ATOM   644  N  N   . ASP A 1 106  ? 42.521 70.694  18.989  1.00 15.04 ? 106  ASP A N   1 
ATOM   645  C  CA  . ASP A 1 106  ? 41.903 69.424  19.326  1.00 14.32 ? 106  ASP A CA  1 
ATOM   646  C  C   . ASP A 1 106  ? 42.733 68.154  19.191  1.00 12.73 ? 106  ASP A C   1 
ATOM   647  O  O   . ASP A 1 106  ? 42.868 67.433  20.183  1.00 12.59 ? 106  ASP A O   1 
ATOM   648  C  CB  . ASP A 1 106  ? 40.617 69.204  18.498  1.00 16.32 ? 106  ASP A CB  1 
ATOM   649  C  CG  . ASP A 1 106  ? 39.651 70.348  18.612  1.00 19.35 ? 106  ASP A CG  1 
ATOM   650  O  OD1 . ASP A 1 106  ? 38.871 70.357  19.576  1.00 20.95 ? 106  ASP A OD1 1 
ATOM   651  O  OD2 . ASP A 1 106  ? 39.680 71.246  17.740  1.00 20.14 ? 106  ASP A OD2 1 
ATOM   652  N  N   . THR A 1 107  ? 43.243 67.881  17.979  1.00 12.35 ? 107  THR A N   1 
ATOM   653  C  CA  . THR A 1 107  ? 43.904 66.591  17.701  1.00 10.58 ? 107  THR A CA  1 
ATOM   654  C  C   . THR A 1 107  ? 45.160 66.345  18.515  1.00 12.48 ? 107  THR A C   1 
ATOM   655  O  O   . THR A 1 107  ? 45.340 65.235  18.995  1.00 10.90 ? 107  THR A O   1 
ATOM   656  C  CB  . THR A 1 107  ? 44.180 66.446  16.205  1.00 12.48 ? 107  THR A CB  1 
ATOM   657  O  OG1 . THR A 1 107  ? 42.921 66.635  15.539  1.00 10.57 ? 107  THR A OG1 1 
ATOM   658  C  CG2 . THR A 1 107  ? 44.812 65.039  15.858  1.00 9.67  ? 107  THR A CG2 1 
ATOM   659  N  N   . LYS A 1 108  ? 46.001 67.361  18.746  1.00 10.88 ? 108  LYS A N   1 
ATOM   660  C  CA  . LYS A 1 108  ? 47.209 67.052  19.550  1.00 11.67 ? 108  LYS A CA  1 
ATOM   661  C  C   . LYS A 1 108  ? 46.791 66.635  20.978  1.00 10.42 ? 108  LYS A C   1 
ATOM   662  O  O   . LYS A 1 108  ? 47.462 65.830  21.606  1.00 11.30 ? 108  LYS A O   1 
ATOM   663  C  CB  . LYS A 1 108  ? 48.198 68.240  19.569  1.00 12.74 ? 108  LYS A CB  1 
ATOM   664  C  CG  . LYS A 1 108  ? 47.881 69.330  20.575  1.00 14.82 ? 108  LYS A CG  1 
ATOM   665  C  CD  . LYS A 1 108  ? 48.966 70.427  20.404  1.00 15.01 ? 108  LYS A CD  1 
ATOM   666  C  CE  . LYS A 1 108  ? 48.775 71.624  21.324  1.00 18.94 ? 108  LYS A CE  1 
ATOM   667  N  NZ  . LYS A 1 108  ? 49.872 72.614  21.197  1.00 18.06 ? 108  LYS A NZ  1 
ATOM   668  N  N   . HIS A 1 109  ? 45.665 67.163  21.461  1.00 12.89 ? 109  HIS A N   1 
ATOM   669  C  CA  . HIS A 1 109  ? 45.167 66.796  22.792  1.00 12.05 ? 109  HIS A CA  1 
ATOM   670  C  C   . HIS A 1 109  ? 44.540 65.386  22.805  1.00 13.12 ? 109  HIS A C   1 
ATOM   671  O  O   . HIS A 1 109  ? 44.721 64.621  23.748  1.00 13.63 ? 109  HIS A O   1 
ATOM   672  C  CB  . HIS A 1 109  ? 44.146 67.826  23.268  1.00 15.14 ? 109  HIS A CB  1 
ATOM   673  C  CG  . HIS A 1 109  ? 44.737 69.177  23.462  1.00 19.23 ? 109  HIS A CG  1 
ATOM   674  N  ND1 . HIS A 1 109  ? 45.696 69.434  24.432  1.00 22.41 ? 109  HIS A ND1 1 
ATOM   675  C  CD2 . HIS A 1 109  ? 44.558 70.338  22.789  1.00 21.70 ? 109  HIS A CD2 1 
ATOM   676  C  CE1 . HIS A 1 109  ? 46.076 70.697  24.334  1.00 21.28 ? 109  HIS A CE1 1 
ATOM   677  N  NE2 . HIS A 1 109  ? 45.403 71.265  23.355  1.00 20.96 ? 109  HIS A NE2 1 
ATOM   678  N  N   . ILE A 1 110  ? 43.773 65.071  21.759  1.00 11.32 ? 110  ILE A N   1 
ATOM   679  C  CA  . ILE A 1 110  ? 43.174 63.741  21.642  1.00 10.27 ? 110  ILE A CA  1 
ATOM   680  C  C   . ILE A 1 110  ? 44.311 62.679  21.630  1.00 11.14 ? 110  ILE A C   1 
ATOM   681  O  O   . ILE A 1 110  ? 44.255 61.644  22.341  1.00 10.23 ? 110  ILE A O   1 
ATOM   682  C  CB  . ILE A 1 110  ? 42.359 63.641  20.336  1.00 10.28 ? 110  ILE A CB  1 
ATOM   683  C  CG1 . ILE A 1 110  ? 41.143 64.583  20.384  1.00 12.13 ? 110  ILE A CG1 1 
ATOM   684  C  CG2 . ILE A 1 110  ? 42.001 62.159  20.065  1.00 8.54  ? 110  ILE A CG2 1 
ATOM   685  C  CD1 . ILE A 1 110  ? 40.460 64.807  19.018  1.00 8.25  ? 110  ILE A CD1 1 
ATOM   686  N  N   . LEU A 1 111  ? 45.351 62.924  20.839  1.00 10.70 ? 111  LEU A N   1 
ATOM   687  C  CA  . LEU A 1 111  ? 46.418 61.935  20.744  1.00 10.97 ? 111  LEU A CA  1 
ATOM   688  C  C   . LEU A 1 111  ? 47.247 61.846  21.990  1.00 11.20 ? 111  LEU A C   1 
ATOM   689  O  O   . LEU A 1 111  ? 47.708 60.787  22.334  1.00 11.88 ? 111  LEU A O   1 
ATOM   690  C  CB  . LEU A 1 111  ? 47.310 62.235  19.545  1.00 9.65  ? 111  LEU A CB  1 
ATOM   691  C  CG  . LEU A 1 111  ? 46.544 61.855  18.239  1.00 9.30  ? 111  LEU A CG  1 
ATOM   692  C  CD1 . LEU A 1 111  ? 47.278 62.321  17.023  1.00 11.66 ? 111  LEU A CD1 1 
ATOM   693  C  CD2 . LEU A 1 111  ? 46.317 60.344  18.198  1.00 12.90 ? 111  LEU A CD2 1 
ATOM   694  N  N   . SER A 1 112  ? 47.467 62.985  22.620  1.00 12.35 ? 112  SER A N   1 
ATOM   695  C  CA  . SER A 1 112  ? 48.245 63.014  23.845  1.00 13.28 ? 112  SER A CA  1 
ATOM   696  C  C   . SER A 1 112  ? 47.510 62.287  24.961  1.00 14.51 ? 112  SER A C   1 
ATOM   697  O  O   . SER A 1 112  ? 48.108 61.484  25.676  1.00 15.31 ? 112  SER A O   1 
ATOM   698  C  CB  . SER A 1 112  ? 48.534 64.468  24.255  1.00 15.44 ? 112  SER A CB  1 
ATOM   699  O  OG  . SER A 1 112  ? 49.326 64.476  25.416  1.00 18.37 ? 112  SER A OG  1 
ATOM   700  N  N   . ASN A 1 113  ? 46.208 62.506  25.053  1.00 13.64 ? 113  ASN A N   1 
ATOM   701  C  CA  . ASN A 1 113  ? 45.475 61.820  26.103  1.00 14.50 ? 113  ASN A CA  1 
ATOM   702  C  C   . ASN A 1 113  ? 45.200 60.352  25.740  1.00 13.78 ? 113  ASN A C   1 
ATOM   703  O  O   . ASN A 1 113  ? 45.096 59.525  26.658  1.00 14.59 ? 113  ASN A O   1 
ATOM   704  C  CB  . ASN A 1 113  ? 44.221 62.604  26.460  1.00 14.82 ? 113  ASN A CB  1 
ATOM   705  C  CG  . ASN A 1 113  ? 44.578 63.938  27.117  1.00 17.30 ? 113  ASN A CG  1 
ATOM   706  O  OD1 . ASN A 1 113  ? 45.642 64.042  27.801  1.00 22.02 ? 113  ASN A OD1 1 
ATOM   707  N  ND2 . ASN A 1 113  ? 43.758 64.940  26.934  1.00 16.83 ? 113  ASN A ND2 1 
ATOM   708  N  N   . ALA A 1 114  ? 45.156 60.001  24.437  1.00 13.12 ? 114  ALA A N   1 
ATOM   709  C  CA  . ALA A 1 114  ? 45.008 58.582  24.056  1.00 11.60 ? 114  ALA A CA  1 
ATOM   710  C  C   . ALA A 1 114  ? 46.297 57.884  24.516  1.00 13.10 ? 114  ALA A C   1 
ATOM   711  O  O   . ALA A 1 114  ? 46.231 56.808  25.106  1.00 11.50 ? 114  ALA A O   1 
ATOM   712  C  CB  . ALA A 1 114  ? 44.831 58.427  22.522  1.00 9.73  ? 114  ALA A CB  1 
ATOM   713  N  N   . LEU A 1 115  ? 47.474 58.464  24.250  1.00 11.87 ? 115  LEU A N   1 
ATOM   714  C  CA  . LEU A 1 115  ? 48.703 57.791  24.703  1.00 13.04 ? 115  LEU A CA  1 
ATOM   715  C  C   . LEU A 1 115  ? 48.689 57.561  26.232  1.00 12.41 ? 115  LEU A C   1 
ATOM   716  O  O   . LEU A 1 115  ? 48.983 56.466  26.707  1.00 14.63 ? 115  LEU A O   1 
ATOM   717  C  CB  . LEU A 1 115  ? 49.966 58.583  24.256  1.00 13.20 ? 115  LEU A CB  1 
ATOM   718  C  CG  . LEU A 1 115  ? 51.346 58.093  24.709  1.00 11.51 ? 115  LEU A CG  1 
ATOM   719  C  CD1 . LEU A 1 115  ? 51.572 56.630  24.379  1.00 13.34 ? 115  LEU A CD1 1 
ATOM   720  C  CD2 . LEU A 1 115  ? 52.420 58.961  24.084  1.00 12.43 ? 115  LEU A CD2 1 
ATOM   721  N  N   . ARG A 1 116  ? 48.275 58.582  26.999  1.00 13.78 ? 116  ARG A N   1 
ATOM   722  C  CA  . ARG A 1 116  ? 48.264 58.471  28.459  1.00 13.73 ? 116  ARG A CA  1 
ATOM   723  C  C   . ARG A 1 116  ? 47.265 57.442  28.950  1.00 13.15 ? 116  ARG A C   1 
ATOM   724  O  O   . ARG A 1 116  ? 47.615 56.557  29.732  1.00 12.88 ? 116  ARG A O   1 
ATOM   725  C  CB  . ARG A 1 116  ? 47.933 59.815  29.095  1.00 16.70 ? 116  ARG A CB  1 
ATOM   726  C  CG  . ARG A 1 116  ? 47.831 59.760  30.632  1.00 21.69 ? 116  ARG A CG  1 
ATOM   727  C  CD  . ARG A 1 116  ? 46.422 59.370  31.119  1.00 26.79 ? 116  ARG A CD  1 
ATOM   728  N  NE  . ARG A 1 116  ? 46.111 59.906  32.462  1.00 33.87 ? 116  ARG A NE  1 
ATOM   729  C  CZ  . ARG A 1 116  ? 46.018 61.209  32.747  1.00 34.77 ? 116  ARG A CZ  1 
ATOM   730  N  NH1 . ARG A 1 116  ? 46.208 62.112  31.780  1.00 37.43 ? 116  ARG A NH1 1 
ATOM   731  N  NH2 . ARG A 1 116  ? 45.744 61.622  33.995  1.00 36.69 ? 116  ARG A NH2 1 
ATOM   732  N  N   . HIS A 1 117  ? 46.039 57.522  28.442  1.00 12.28 ? 117  HIS A N   1 
ATOM   733  C  CA  . HIS A 1 117  ? 45.013 56.605  28.890  1.00 13.10 ? 117  HIS A CA  1 
ATOM   734  C  C   . HIS A 1 117  ? 45.197 55.176  28.448  1.00 12.74 ? 117  HIS A C   1 
ATOM   735  O  O   . HIS A 1 117  ? 44.895 54.273  29.185  1.00 11.28 ? 117  HIS A O   1 
ATOM   736  C  CB  . HIS A 1 117  ? 43.640 57.161  28.516  1.00 13.60 ? 117  HIS A CB  1 
ATOM   737  C  CG  A HIS A 1 117  ? 43.236 58.316  29.376  0.50 15.18 ? 117  HIS A CG  1 
ATOM   738  C  CG  B HIS A 1 117  ? 42.786 57.532  29.526  0.50 19.85 ? 117  HIS A CG  1 
ATOM   739  N  ND1 A HIS A 1 117  ? 42.527 58.153  30.551  0.50 15.29 ? 117  HIS A ND1 1 
ATOM   740  N  ND1 B HIS A 1 117  ? 42.036 56.675  30.299  0.50 21.89 ? 117  HIS A ND1 1 
ATOM   741  C  CD2 A HIS A 1 117  ? 43.574 59.627  29.320  0.50 16.07 ? 117  HIS A CD2 1 
ATOM   742  C  CD2 B HIS A 1 117  ? 42.590 58.768  30.034  0.50 21.10 ? 117  HIS A CD2 1 
ATOM   743  C  CE1 A HIS A 1 117  ? 42.455 59.315  31.182  0.50 16.58 ? 117  HIS A CE1 1 
ATOM   744  C  CE1 B HIS A 1 117  ? 41.412 57.364  31.235  0.50 20.33 ? 117  HIS A CE1 1 
ATOM   745  N  NE2 A HIS A 1 117  ? 43.083 60.223  30.459  0.50 15.58 ? 117  HIS A NE2 1 
ATOM   746  N  NE2 B HIS A 1 117  ? 41.734 58.638  31.097  0.50 21.92 ? 117  HIS A NE2 1 
ATOM   747  N  N   . LEU A 1 118  ? 45.685 54.945  27.238  1.00 10.76 ? 118  LEU A N   1 
ATOM   748  C  CA  . LEU A 1 118  ? 45.916 53.567  26.840  1.00 12.21 ? 118  LEU A CA  1 
ATOM   749  C  C   . LEU A 1 118  ? 47.149 53.047  27.592  1.00 12.74 ? 118  LEU A C   1 
ATOM   750  O  O   . LEU A 1 118  ? 47.170 51.934  28.065  1.00 12.64 ? 118  LEU A O   1 
ATOM   751  C  CB  . LEU A 1 118  ? 46.118 53.506  25.327  1.00 11.08 ? 118  LEU A CB  1 
ATOM   752  C  CG  . LEU A 1 118  ? 44.844 53.931  24.531  1.00 12.61 ? 118  LEU A CG  1 
ATOM   753  C  CD1 . LEU A 1 118  ? 45.304 53.844  23.018  1.00 14.08 ? 118  LEU A CD1 1 
ATOM   754  C  CD2 . LEU A 1 118  ? 43.604 53.145  24.756  1.00 13.78 ? 118  LEU A CD2 1 
ATOM   755  N  N   . HIS A 1 119  ? 48.179 53.872  27.758  1.00 13.18 ? 119  HIS A N   1 
ATOM   756  C  CA  . HIS A 1 119  ? 49.349 53.421  28.511  1.00 14.30 ? 119  HIS A CA  1 
ATOM   757  C  C   . HIS A 1 119  ? 48.899 52.960  29.921  1.00 15.08 ? 119  HIS A C   1 
ATOM   758  O  O   . HIS A 1 119  ? 49.225 51.870  30.369  1.00 16.40 ? 119  HIS A O   1 
ATOM   759  C  CB  . HIS A 1 119  ? 50.323 54.590  28.668  1.00 15.88 ? 119  HIS A CB  1 
ATOM   760  C  CG  . HIS A 1 119  ? 51.525 54.267  29.501  1.00 17.71 ? 119  HIS A CG  1 
ATOM   761  N  ND1 . HIS A 1 119  ? 51.594 54.581  30.842  1.00 18.61 ? 119  HIS A ND1 1 
ATOM   762  C  CD2 . HIS A 1 119  ? 52.666 53.609  29.206  1.00 18.12 ? 119  HIS A CD2 1 
ATOM   763  C  CE1 . HIS A 1 119  ? 52.740 54.132  31.334  1.00 19.34 ? 119  HIS A CE1 1 
ATOM   764  N  NE2 . HIS A 1 119  ? 53.407 53.538  30.365  1.00 19.28 ? 119  HIS A NE2 1 
ATOM   765  N  N   . ASP A 1 120  ? 48.092 53.792  30.585  1.00 15.71 ? 120  ASP A N   1 
ATOM   766  C  CA  . ASP A 1 120  ? 47.628 53.493  31.962  1.00 16.41 ? 120  ASP A CA  1 
ATOM   767  C  C   . ASP A 1 120  ? 46.483 52.488  32.177  1.00 16.99 ? 120  ASP A C   1 
ATOM   768  O  O   . ASP A 1 120  ? 46.258 52.040  33.310  1.00 17.30 ? 120  ASP A O   1 
ATOM   769  C  CB  . ASP A 1 120  ? 47.236 54.796  32.660  1.00 17.39 ? 120  ASP A CB  1 
ATOM   770  C  CG  . ASP A 1 120  ? 48.420 55.751  32.855  1.00 19.99 ? 120  ASP A CG  1 
ATOM   771  O  OD1 . ASP A 1 120  ? 49.612 55.337  32.760  1.00 19.87 ? 120  ASP A OD1 1 
ATOM   772  O  OD2 . ASP A 1 120  ? 48.136 56.937  33.134  1.00 20.13 ? 120  ASP A OD2 1 
ATOM   773  N  N   . ASN A 1 121  ? 45.728 52.165  31.122  1.00 14.03 ? 121  ASN A N   1 
ATOM   774  C  CA  . ASN A 1 121  ? 44.600 51.241  31.195  1.00 14.38 ? 121  ASN A CA  1 
ATOM   775  C  C   . ASN A 1 121  ? 44.741 50.185  30.090  1.00 14.13 ? 121  ASN A C   1 
ATOM   776  O  O   . ASN A 1 121  ? 44.161 50.314  29.037  1.00 13.97 ? 121  ASN A O   1 
ATOM   777  C  CB  . ASN A 1 121  ? 43.288 52.016  31.005  1.00 11.56 ? 121  ASN A CB  1 
ATOM   778  C  CG  . ASN A 1 121  ? 43.078 53.027  32.121  1.00 15.53 ? 121  ASN A CG  1 
ATOM   779  O  OD1 . ASN A 1 121  ? 42.577 52.665  33.216  1.00 14.68 ? 121  ASN A OD1 1 
ATOM   780  N  ND2 . ASN A 1 121  ? 43.453 54.278  31.868  1.00 13.93 ? 121  ASN A ND2 1 
ATOM   781  N  N   . PRO A 1 122  ? 45.496 49.107  30.343  1.00 14.44 ? 122  PRO A N   1 
ATOM   782  C  CA  . PRO A 1 122  ? 45.793 48.001  29.407  1.00 14.91 ? 122  PRO A CA  1 
ATOM   783  C  C   . PRO A 1 122  ? 44.666 47.409  28.612  1.00 13.65 ? 122  PRO A C   1 
ATOM   784  O  O   . PRO A 1 122  ? 44.893 46.945  27.487  1.00 14.53 ? 122  PRO A O   1 
ATOM   785  C  CB  . PRO A 1 122  ? 46.509 46.961  30.295  1.00 16.17 ? 122  PRO A CB  1 
ATOM   786  C  CG  . PRO A 1 122  ? 46.251 47.389  31.653  1.00 17.94 ? 122  PRO A CG  1 
ATOM   787  C  CD  . PRO A 1 122  ? 46.047 48.847  31.685  1.00 15.85 ? 122  PRO A CD  1 
ATOM   788  N  N   . GLU A 1 123  ? 43.462 47.405  29.187  1.00 13.32 ? 123  GLU A N   1 
ATOM   789  C  CA  . GLU A 1 123  ? 42.285 46.857  28.512  1.00 13.03 ? 123  GLU A CA  1 
ATOM   790  C  C   . GLU A 1 123  ? 41.579 47.785  27.525  1.00 12.18 ? 123  GLU A C   1 
ATOM   791  O  O   . GLU A 1 123  ? 40.726 47.318  26.743  1.00 13.51 ? 123  GLU A O   1 
ATOM   792  C  CB  . GLU A 1 123  ? 41.223 46.440  29.566  1.00 15.97 ? 123  GLU A CB  1 
ATOM   793  C  CG  . GLU A 1 123  ? 40.372 47.647  30.137  1.00 19.35 ? 123  GLU A CG  1 
ATOM   794  C  CD  . GLU A 1 123  ? 41.096 48.600  31.119  1.00 19.60 ? 123  GLU A CD  1 
ATOM   795  O  OE1 . GLU A 1 123  ? 42.323 48.523  31.319  1.00 17.05 ? 123  GLU A OE1 1 
ATOM   796  O  OE2 . GLU A 1 123  ? 40.398 49.458  31.741  1.00 24.29 ? 123  GLU A OE2 1 
ATOM   797  N  N   . MET A 1 124  ? 41.881 49.090  27.603  1.00 11.69 ? 124  MET A N   1 
ATOM   798  C  CA  . MET A 1 124  ? 41.220 50.080  26.748  1.00 12.38 ? 124  MET A CA  1 
ATOM   799  C  C   . MET A 1 124  ? 41.838 49.924  25.363  1.00 10.81 ? 124  MET A C   1 
ATOM   800  O  O   . MET A 1 124  ? 43.022 49.630  25.254  1.00 10.99 ? 124  MET A O   1 
ATOM   801  C  CB  . MET A 1 124  ? 41.510 51.490  27.283  1.00 11.77 ? 124  MET A CB  1 
ATOM   802  C  CG  . MET A 1 124  ? 40.686 52.638  26.568  1.00 12.34 ? 124  MET A CG  1 
ATOM   803  S  SD  . MET A 1 124  ? 38.931 52.248  26.538  1.00 13.62 ? 124  MET A SD  1 
ATOM   804  C  CE  . MET A 1 124  ? 38.241 53.730  25.884  1.00 12.82 ? 124  MET A CE  1 
ATOM   805  N  N   . LYS A 1 125  ? 41.044 50.213  24.345  1.00 11.86 ? 125  LYS A N   1 
ATOM   806  C  CA  . LYS A 1 125  ? 41.396 50.155  22.914  1.00 10.24 ? 125  LYS A CA  1 
ATOM   807  C  C   . LYS A 1 125  ? 41.010 51.455  22.199  1.00 9.23  ? 125  LYS A C   1 
ATOM   808  O  O   . LYS A 1 125  ? 40.144 52.177  22.653  1.00 8.99  ? 125  LYS A O   1 
ATOM   809  C  CB  . LYS A 1 125  ? 40.640 48.958  22.287  1.00 12.82 ? 125  LYS A CB  1 
ATOM   810  C  CG  . LYS A 1 125  ? 40.936 47.569  22.806  1.00 16.63 ? 125  LYS A CG  1 
ATOM   811  C  CD  . LYS A 1 125  ? 42.395 47.194  22.675  1.00 18.47 ? 125  LYS A CD  1 
ATOM   812  C  CE  . LYS A 1 125  ? 42.751 45.795  23.166  1.00 22.94 ? 125  LYS A CE  1 
ATOM   813  N  NZ  . LYS A 1 125  ? 41.647 44.891  22.881  1.00 25.04 ? 125  LYS A NZ  1 
ATOM   814  N  N   . PHE A 1 126  ? 41.623 51.721  21.032  1.00 9.34  ? 126  PHE A N   1 
ATOM   815  C  CA  . PHE A 1 126  ? 41.310 52.898  20.276  1.00 9.39  ? 126  PHE A CA  1 
ATOM   816  C  C   . PHE A 1 126  ? 41.813 52.644  18.848  1.00 8.49  ? 126  PHE A C   1 
ATOM   817  O  O   . PHE A 1 126  ? 42.867 52.030  18.672  1.00 9.78  ? 126  PHE A O   1 
ATOM   818  C  CB  . PHE A 1 126  ? 42.065 54.099  20.917  1.00 8.08  ? 126  PHE A CB  1 
ATOM   819  C  CG  . PHE A 1 126  ? 41.702 55.469  20.411  1.00 10.04 ? 126  PHE A CG  1 
ATOM   820  C  CD1 . PHE A 1 126  ? 40.361 55.903  20.364  1.00 9.59  ? 126  PHE A CD1 1 
ATOM   821  C  CD2 . PHE A 1 126  ? 42.749 56.420  20.091  1.00 8.79  ? 126  PHE A CD2 1 
ATOM   822  C  CE1 . PHE A 1 126  ? 40.063 57.215  20.012  1.00 9.81  ? 126  PHE A CE1 1 
ATOM   823  C  CE2 . PHE A 1 126  ? 42.452 57.741  19.750  1.00 8.25  ? 126  PHE A CE2 1 
ATOM   824  C  CZ  . PHE A 1 126  ? 41.120 58.138  19.702  1.00 6.31  ? 126  PHE A CZ  1 
ATOM   825  N  N   . ILE A 1 127  ? 41.061 53.117  17.850  1.00 6.85  ? 127  ILE A N   1 
ATOM   826  C  CA  . ILE A 1 127  ? 41.476 53.034  16.443  1.00 6.59  ? 127  ILE A CA  1 
ATOM   827  C  C   . ILE A 1 127  ? 41.765 54.452  15.948  1.00 7.08  ? 127  ILE A C   1 
ATOM   828  O  O   . ILE A 1 127  ? 41.108 55.421  16.328  1.00 8.03  ? 127  ILE A O   1 
ATOM   829  C  CB  . ILE A 1 127  ? 40.452 52.290  15.527  1.00 7.08  ? 127  ILE A CB  1 
ATOM   830  C  CG1 . ILE A 1 127  ? 39.052 52.872  15.502  1.00 6.70  ? 127  ILE A CG1 1 
ATOM   831  C  CG2 . ILE A 1 127  ? 40.389 50.804  15.960  1.00 8.18  ? 127  ILE A CG2 1 
ATOM   832  C  CD1 . ILE A 1 127  ? 38.124 52.285  14.412  1.00 6.03  ? 127  ILE A CD1 1 
ATOM   833  N  N   . TRP A 1 128  ? 42.670 54.550  15.000  1.00 7.31  ? 128  TRP A N   1 
ATOM   834  C  CA  . TRP A 1 128  ? 43.098 55.820  14.427  1.00 7.15  ? 128  TRP A CA  1 
ATOM   835  C  C   . TRP A 1 128  ? 43.204 55.704  12.899  1.00 7.68  ? 128  TRP A C   1 
ATOM   836  O  O   . TRP A 1 128  ? 43.833 54.733  12.420  1.00 7.42  ? 128  TRP A O   1 
ATOM   837  C  CB  . TRP A 1 128  ? 44.439 56.221  14.987  1.00 8.07  ? 128  TRP A CB  1 
ATOM   838  C  CG  . TRP A 1 128  ? 44.693 57.666  14.651  1.00 8.69  ? 128  TRP A CG  1 
ATOM   839  C  CD1 . TRP A 1 128  ? 45.416 58.167  13.558  1.00 5.67  ? 128  TRP A CD1 1 
ATOM   840  C  CD2 . TRP A 1 128  ? 44.130 58.791  15.302  1.00 7.38  ? 128  TRP A CD2 1 
ATOM   841  N  NE1 . TRP A 1 128  ? 45.321 59.551  13.527  1.00 7.27  ? 128  TRP A NE1 1 
ATOM   842  C  CE2 . TRP A 1 128  ? 44.543 59.964  14.578  1.00 5.02  ? 128  TRP A CE2 1 
ATOM   843  C  CE3 . TRP A 1 128  ? 43.296 58.939  16.414  1.00 8.07  ? 128  TRP A CE3 1 
ATOM   844  C  CZ2 . TRP A 1 128  ? 44.160 61.240  14.962  1.00 6.59  ? 128  TRP A CZ2 1 
ATOM   845  C  CZ3 . TRP A 1 128  ? 42.910 60.207  16.783  1.00 9.26  ? 128  TRP A CZ3 1 
ATOM   846  C  CH2 . TRP A 1 128  ? 43.351 61.358  16.064  1.00 8.58  ? 128  TRP A CH2 1 
ATOM   847  N  N   . ALA A 1 129  ? 42.642 56.674  12.155  1.00 7.48  ? 129  ALA A N   1 
ATOM   848  C  CA  . ALA A 1 129  ? 42.636 56.607  10.718  1.00 8.36  ? 129  ALA A CA  1 
ATOM   849  C  C   . ALA A 1 129  ? 43.534 57.590  9.995   1.00 8.29  ? 129  ALA A C   1 
ATOM   850  O  O   . ALA A 1 129  ? 44.114 57.204  8.994   1.00 8.46  ? 129  ALA A O   1 
ATOM   851  C  CB  . ALA A 1 129  ? 41.166 56.824  10.192  1.00 6.89  ? 129  ALA A CB  1 
ATOM   852  N  N   . GLU A 1 130  ? 43.602 58.842  10.437  1.00 9.57  ? 130  GLU A N   1 
ATOM   853  C  CA  . GLU A 1 130  ? 44.269 59.910  9.645   1.00 7.90  ? 130  GLU A CA  1 
ATOM   854  C  C   . GLU A 1 130  ? 45.739 60.032  10.004  1.00 7.91  ? 130  GLU A C   1 
ATOM   855  O  O   . GLU A 1 130  ? 46.116 60.634  11.053  1.00 9.47  ? 130  GLU A O   1 
ATOM   856  C  CB  . GLU A 1 130  ? 43.502 61.234  9.851   1.00 7.97  ? 130  GLU A CB  1 
ATOM   857  C  CG  . GLU A 1 130  ? 41.950 61.125  9.566   1.00 9.11  ? 130  GLU A CG  1 
ATOM   858  C  CD  . GLU A 1 130  ? 41.103 60.644  10.769  1.00 10.32 ? 130  GLU A CD  1 
ATOM   859  O  OE1 . GLU A 1 130  ? 41.622 60.440  11.882  1.00 9.89  ? 130  GLU A OE1 1 
ATOM   860  O  OE2 . GLU A 1 130  ? 39.838 60.552  10.592  1.00 12.81 ? 130  GLU A OE2 1 
ATOM   861  N  N   . ILE A 1 131  ? 46.590 59.517  9.103   1.00 6.72  ? 131  ILE A N   1 
ATOM   862  C  CA  . ILE A 1 131  ? 48.008 59.491  9.425   1.00 8.00  ? 131  ILE A CA  1 
ATOM   863  C  C   . ILE A 1 131  ? 48.623 60.914  9.298   1.00 9.07  ? 131  ILE A C   1 
ATOM   864  O  O   . ILE A 1 131  ? 49.604 61.198  9.953   1.00 9.72  ? 131  ILE A O   1 
ATOM   865  C  CB  . ILE A 1 131  ? 48.749 58.427  8.577   1.00 7.68  ? 131  ILE A CB  1 
ATOM   866  C  CG1 . ILE A 1 131  ? 48.113 57.028  8.892   1.00 7.83  ? 131  ILE A CG1 1 
ATOM   867  C  CG2 . ILE A 1 131  ? 50.247 58.455  8.914   1.00 8.20  ? 131  ILE A CG2 1 
ATOM   868  C  CD1 . ILE A 1 131  ? 47.925 56.779  10.450  1.00 11.74 ? 131  ILE A CD1 1 
ATOM   869  N  N   . SER A 1 132  ? 48.058 61.829  8.493   1.00 7.45  ? 132  SER A N   1 
ATOM   870  C  CA  . SER A 1 132  ? 48.587 63.228  8.413   1.00 8.03  ? 132  SER A CA  1 
ATOM   871  C  C   . SER A 1 132  ? 48.690 63.796  9.830   1.00 6.95  ? 132  SER A C   1 
ATOM   872  O  O   . SER A 1 132  ? 49.731 64.321  10.197  1.00 9.90  ? 132  SER A O   1 
ATOM   873  C  CB  . SER A 1 132  ? 47.636 64.044  7.538   1.00 7.02  ? 132  SER A CB  1 
ATOM   874  O  OG  . SER A 1 132  ? 46.284 64.011  7.918   1.00 7.92  ? 132  SER A OG  1 
ATOM   875  N  N   . TYR A 1 133  ? 47.613 63.690  10.616  1.00 8.38  ? 133  TYR A N   1 
ATOM   876  C  CA  . TYR A 1 133  ? 47.596 64.120  12.004  1.00 8.58  ? 133  TYR A CA  1 
ATOM   877  C  C   . TYR A 1 133  ? 48.553 63.308  12.891  1.00 9.85  ? 133  TYR A C   1 
ATOM   878  O  O   . TYR A 1 133  ? 49.230 63.888  13.764  1.00 11.51 ? 133  TYR A O   1 
ATOM   879  C  CB  . TYR A 1 133  ? 46.203 64.014  12.583  1.00 10.56 ? 133  TYR A CB  1 
ATOM   880  C  CG  . TYR A 1 133  ? 45.334 65.159  12.274  1.00 9.01  ? 133  TYR A CG  1 
ATOM   881  C  CD1 . TYR A 1 133  ? 45.737 66.457  12.554  1.00 11.79 ? 133  TYR A CD1 1 
ATOM   882  C  CD2 . TYR A 1 133  ? 44.092 64.968  11.721  1.00 9.16  ? 133  TYR A CD2 1 
ATOM   883  C  CE1 . TYR A 1 133  ? 44.884 67.539  12.283  1.00 11.08 ? 133  TYR A CE1 1 
ATOM   884  C  CE2 . TYR A 1 133  ? 43.253 66.027  11.469  1.00 10.36 ? 133  TYR A CE2 1 
ATOM   885  C  CZ  . TYR A 1 133  ? 43.655 67.316  11.746  1.00 10.73 ? 133  TYR A CZ  1 
ATOM   886  O  OH  . TYR A 1 133  ? 42.790 68.364  11.481  1.00 10.85 ? 133  TYR A OH  1 
ATOM   887  N  N   . PHE A 1 134  ? 48.612 61.989  12.696  1.00 8.85  ? 134  PHE A N   1 
ATOM   888  C  CA  . PHE A 1 134  ? 49.473 61.184  13.564  1.00 10.03 ? 134  PHE A CA  1 
ATOM   889  C  C   . PHE A 1 134  ? 50.951 61.499  13.364  1.00 10.07 ? 134  PHE A C   1 
ATOM   890  O  O   . PHE A 1 134  ? 51.709 61.556  14.354  1.00 11.34 ? 134  PHE A O   1 
ATOM   891  C  CB  . PHE A 1 134  ? 49.193 59.699  13.390  1.00 9.92  ? 134  PHE A CB  1 
ATOM   892  C  CG  . PHE A 1 134  ? 49.734 58.868  14.525  1.00 11.49 ? 134  PHE A CG  1 
ATOM   893  C  CD1 . PHE A 1 134  ? 48.938 58.632  15.673  1.00 13.05 ? 134  PHE A CD1 1 
ATOM   894  C  CD2 . PHE A 1 134  ? 51.024 58.336  14.454  1.00 11.82 ? 134  PHE A CD2 1 
ATOM   895  C  CE1 . PHE A 1 134  ? 49.434 57.887  16.704  1.00 12.17 ? 134  PHE A CE1 1 
ATOM   896  C  CE2 . PHE A 1 134  ? 51.531 57.589  15.494  1.00 12.38 ? 134  PHE A CE2 1 
ATOM   897  C  CZ  . PHE A 1 134  ? 50.741 57.365  16.618  1.00 10.61 ? 134  PHE A CZ  1 
ATOM   898  N  N   . ALA A 1 135  ? 51.354 61.631  12.100  1.00 12.03 ? 135  ALA A N   1 
ATOM   899  C  CA  . ALA A 1 135  ? 52.735 61.983  11.763  1.00 12.19 ? 135  ALA A CA  1 
ATOM   900  C  C   . ALA A 1 135  ? 53.024 63.368  12.370  1.00 13.09 ? 135  ALA A C   1 
ATOM   901  O  O   . ALA A 1 135  ? 54.105 63.549  12.965  1.00 15.21 ? 135  ALA A O   1 
ATOM   902  C  CB  . ALA A 1 135  ? 52.951 61.997  10.239  1.00 12.09 ? 135  ALA A CB  1 
ATOM   903  N  N   . ARG A 1 136  ? 52.100 64.314  12.243  1.00 11.76 ? 136  ARG A N   1 
ATOM   904  C  CA  . ARG A 1 136  ? 52.270 65.687  12.759  1.00 13.92 ? 136  ARG A CA  1 
ATOM   905  C  C   . ARG A 1 136  ? 52.510 65.610  14.272  1.00 13.89 ? 136  ARG A C   1 
ATOM   906  O  O   . ARG A 1 136  ? 53.359 66.307  14.827  1.00 18.36 ? 136  ARG A O   1 
ATOM   907  C  CB  . ARG A 1 136  ? 51.033 66.546  12.456  1.00 14.75 ? 136  ARG A CB  1 
ATOM   908  C  CG  . ARG A 1 136  ? 50.954 67.882  13.248  1.00 16.35 ? 136  ARG A CG  1 
ATOM   909  C  CD  . ARG A 1 136  ? 51.876 68.942  12.563  1.00 19.48 ? 136  ARG A CD  1 
ATOM   910  N  NE  . ARG A 1 136  ? 51.799 70.255  13.205  1.00 17.73 ? 136  ARG A NE  1 
ATOM   911  C  CZ  . ARG A 1 136  ? 52.562 70.592  14.238  1.00 19.33 ? 136  ARG A CZ  1 
ATOM   912  N  NH1 . ARG A 1 136  ? 53.439 69.710  14.708  1.00 20.56 ? 136  ARG A NH1 1 
ATOM   913  N  NH2 . ARG A 1 136  ? 52.455 71.785  14.791  1.00 15.93 ? 136  ARG A NH2 1 
ATOM   914  N  N   . PHE A 1 137  ? 51.794 64.728  14.953  1.00 14.45 ? 137  PHE A N   1 
ATOM   915  C  CA  . PHE A 1 137  ? 51.904 64.565  16.392  1.00 13.13 ? 137  PHE A CA  1 
ATOM   916  C  C   . PHE A 1 137  ? 53.182 63.843  16.824  1.00 14.63 ? 137  PHE A C   1 
ATOM   917  O  O   . PHE A 1 137  ? 53.968 64.323  17.685  1.00 16.19 ? 137  PHE A O   1 
ATOM   918  C  CB  . PHE A 1 137  ? 50.685 63.762  16.847  1.00 12.00 ? 137  PHE A CB  1 
ATOM   919  C  CG  . PHE A 1 137  ? 50.666 63.474  18.314  1.00 11.43 ? 137  PHE A CG  1 
ATOM   920  C  CD1 . PHE A 1 137  ? 50.331 64.454  19.249  1.00 12.69 ? 137  PHE A CD1 1 
ATOM   921  C  CD2 . PHE A 1 137  ? 51.033 62.205  18.773  1.00 12.81 ? 137  PHE A CD2 1 
ATOM   922  C  CE1 . PHE A 1 137  ? 50.367 64.169  20.645  1.00 13.84 ? 137  PHE A CE1 1 
ATOM   923  C  CE2 . PHE A 1 137  ? 51.077 61.951  20.179  1.00 13.74 ? 137  PHE A CE2 1 
ATOM   924  C  CZ  . PHE A 1 137  ? 50.739 62.954  21.090  1.00 13.30 ? 137  PHE A CZ  1 
ATOM   925  N  N   . TYR A 1 138  ? 53.421 62.695  16.203  1.00 16.50 ? 138  TYR A N   1 
ATOM   926  C  CA  . TYR A 1 138  ? 54.539 61.859  16.574  1.00 18.98 ? 138  TYR A CA  1 
ATOM   927  C  C   . TYR A 1 138  ? 55.899 62.524  16.391  1.00 19.96 ? 138  TYR A C   1 
ATOM   928  O  O   . TYR A 1 138  ? 56.841 62.277  17.181  1.00 21.45 ? 138  TYR A O   1 
ATOM   929  C  CB  . TYR A 1 138  ? 54.481 60.548  15.792  1.00 16.80 ? 138  TYR A CB  1 
ATOM   930  C  CG  . TYR A 1 138  ? 55.540 59.550  16.161  1.00 18.12 ? 138  TYR A CG  1 
ATOM   931  C  CD1 . TYR A 1 138  ? 56.756 59.526  15.488  1.00 17.77 ? 138  TYR A CD1 1 
ATOM   932  C  CD2 . TYR A 1 138  ? 55.286 58.577  17.129  1.00 18.37 ? 138  TYR A CD2 1 
ATOM   933  C  CE1 . TYR A 1 138  ? 57.724 58.529  15.762  1.00 17.48 ? 138  TYR A CE1 1 
ATOM   934  C  CE2 . TYR A 1 138  ? 56.228 57.589  17.415  1.00 19.54 ? 138  TYR A CE2 1 
ATOM   935  C  CZ  . TYR A 1 138  ? 57.440 57.572  16.730  1.00 17.99 ? 138  TYR A CZ  1 
ATOM   936  O  OH  . TYR A 1 138  ? 58.347 56.572  17.044  1.00 20.64 ? 138  TYR A OH  1 
ATOM   937  N  N   . HIS A 1 139  ? 56.043 63.357  15.383  1.00 22.45 ? 139  HIS A N   1 
ATOM   938  C  CA  . HIS A 1 139  ? 57.353 63.957  15.213  1.00 24.06 ? 139  HIS A CA  1 
ATOM   939  C  C   . HIS A 1 139  ? 57.613 65.006  16.262  1.00 24.45 ? 139  HIS A C   1 
ATOM   940  O  O   . HIS A 1 139  ? 58.754 65.426  16.444  1.00 25.86 ? 139  HIS A O   1 
ATOM   941  C  CB  . HIS A 1 139  ? 57.514 64.500  13.799  1.00 25.57 ? 139  HIS A CB  1 
ATOM   942  C  CG  . HIS A 1 139  ? 57.682 63.419  12.776  1.00 28.37 ? 139  HIS A CG  1 
ATOM   943  N  ND1 . HIS A 1 139  ? 58.822 62.638  12.698  1.00 28.34 ? 139  HIS A ND1 1 
ATOM   944  C  CD2 . HIS A 1 139  ? 56.836 62.955  11.818  1.00 27.47 ? 139  HIS A CD2 1 
ATOM   945  C  CE1 . HIS A 1 139  ? 58.672 61.746  11.734  1.00 30.03 ? 139  HIS A CE1 1 
ATOM   946  N  NE2 . HIS A 1 139  ? 57.481 61.919  11.182  1.00 30.09 ? 139  HIS A NE2 1 
ATOM   947  N  N   . ASP A 1 140  ? 56.561 65.449  16.943  1.00 22.54 ? 140  ASP A N   1 
ATOM   948  C  CA  . ASP A 1 140  ? 56.707 66.419  18.012  1.00 23.74 ? 140  ASP A CA  1 
ATOM   949  C  C   . ASP A 1 140  ? 56.924 65.752  19.387  1.00 21.88 ? 140  ASP A C   1 
ATOM   950  O  O   . ASP A 1 140  ? 57.172 66.430  20.383  1.00 21.16 ? 140  ASP A O   1 
ATOM   951  C  CB  . ASP A 1 140  ? 55.513 67.369  18.049  1.00 24.34 ? 140  ASP A CB  1 
ATOM   952  C  CG  . ASP A 1 140  ? 55.633 68.471  16.998  1.00 28.63 ? 140  ASP A CG  1 
ATOM   953  O  OD1 . ASP A 1 140  ? 56.163 68.196  15.895  1.00 29.48 ? 140  ASP A OD1 1 
ATOM   954  O  OD2 . ASP A 1 140  ? 55.210 69.599  17.254  1.00 27.99 ? 140  ASP A OD2 1 
ATOM   955  N  N   . LEU A 1 141  ? 56.847 64.423  19.432  1.00 20.29 ? 141  LEU A N   1 
ATOM   956  C  CA  . LEU A 1 141  ? 57.080 63.723  20.704  1.00 19.98 ? 141  LEU A CA  1 
ATOM   957  C  C   . LEU A 1 141  ? 58.558 63.498  21.026  1.00 20.22 ? 141  LEU A C   1 
ATOM   958  O  O   . LEU A 1 141  ? 59.413 63.272  20.139  1.00 20.10 ? 141  LEU A O   1 
ATOM   959  C  CB  . LEU A 1 141  ? 56.447 62.328  20.745  1.00 20.35 ? 141  LEU A CB  1 
ATOM   960  C  CG  . LEU A 1 141  ? 54.927 62.081  20.776  1.00 19.45 ? 141  LEU A CG  1 
ATOM   961  C  CD1 . LEU A 1 141  ? 54.726 60.553  20.607  1.00 16.46 ? 141  LEU A CD1 1 
ATOM   962  C  CD2 . LEU A 1 141  ? 54.280 62.602  22.073  1.00 20.10 ? 141  LEU A CD2 1 
ATOM   963  N  N   . GLY A 1 142  ? 58.807 63.498  22.335  1.00 20.59 ? 142  GLY A N   1 
ATOM   964  C  CA  . GLY A 1 142  ? 60.146 63.214  22.840  1.00 21.28 ? 142  GLY A CA  1 
ATOM   965  C  C   . GLY A 1 142  ? 60.327 61.720  22.714  1.00 22.01 ? 142  GLY A C   1 
ATOM   966  O  O   . GLY A 1 142  ? 59.340 60.977  22.638  1.00 22.35 ? 142  GLY A O   1 
ATOM   967  N  N   . GLU A 1 143  ? 61.575 61.266  22.717  1.00 22.63 ? 143  GLU A N   1 
ATOM   968  C  CA  . GLU A 1 143  ? 61.889 59.864  22.558  1.00 23.37 ? 143  GLU A CA  1 
ATOM   969  C  C   . GLU A 1 143  ? 61.182 58.979  23.563  1.00 23.31 ? 143  GLU A C   1 
ATOM   970  O  O   . GLU A 1 143  ? 60.765 57.855  23.218  1.00 22.32 ? 143  GLU A O   1 
ATOM   971  C  CB  . GLU A 1 143  ? 63.397 59.629  22.655  1.00 25.13 ? 143  GLU A CB  1 
ATOM   972  C  CG  . GLU A 1 143  ? 63.906 58.291  22.061  1.00 29.55 ? 143  GLU A CG  1 
ATOM   973  C  CD  . GLU A 1 143  ? 63.466 58.026  20.606  1.00 32.04 ? 143  GLU A CD  1 
ATOM   974  O  OE1 . GLU A 1 143  ? 63.611 58.924  19.733  1.00 33.93 ? 143  GLU A OE1 1 
ATOM   975  O  OE2 . GLU A 1 143  ? 62.993 56.892  20.333  1.00 35.28 ? 143  GLU A OE2 1 
ATOM   976  N  N   . ASN A 1 144  ? 61.007 59.453  24.788  1.00 22.67 ? 144  ASN A N   1 
ATOM   977  C  CA  . ASN A 1 144  ? 60.346 58.578  25.736  1.00 23.09 ? 144  ASN A CA  1 
ATOM   978  C  C   . ASN A 1 144  ? 58.878 58.296  25.319  1.00 21.51 ? 144  ASN A C   1 
ATOM   979  O  O   . ASN A 1 144  ? 58.431 57.155  25.366  1.00 21.16 ? 144  ASN A O   1 
ATOM   980  C  CB  . ASN A 1 144  ? 60.425 59.148  27.146  1.00 26.00 ? 144  ASN A CB  1 
ATOM   981  C  CG  . ASN A 1 144  ? 59.673 58.291  28.153  1.00 29.79 ? 144  ASN A CG  1 
ATOM   982  O  OD1 . ASN A 1 144  ? 58.444 58.382  28.262  1.00 33.61 ? 144  ASN A OD1 1 
ATOM   983  N  ND2 . ASN A 1 144  ? 60.399 57.424  28.867  1.00 29.79 ? 144  ASN A ND2 1 
ATOM   984  N  N   . LYS A 1 145  ? 58.144 59.340  24.937  1.00 20.94 ? 145  LYS A N   1 
ATOM   985  C  CA  . LYS A 1 145  ? 56.763 59.157  24.511  1.00 19.82 ? 145  LYS A CA  1 
ATOM   986  C  C   . LYS A 1 145  ? 56.718 58.361  23.199  1.00 19.64 ? 145  LYS A C   1 
ATOM   987  O  O   . LYS A 1 145  ? 55.795 57.554  22.983  1.00 18.25 ? 145  LYS A O   1 
ATOM   988  C  CB  . LYS A 1 145  ? 56.058 60.504  24.340  1.00 21.63 ? 145  LYS A CB  1 
ATOM   989  C  CG  . LYS A 1 145  ? 55.903 61.280  25.645  1.00 24.51 ? 145  LYS A CG  1 
ATOM   990  C  CD  . LYS A 1 145  ? 55.398 60.415  26.750  1.00 26.54 ? 145  LYS A CD  1 
ATOM   991  C  CE  . LYS A 1 145  ? 55.216 61.231  28.033  1.00 27.86 ? 145  LYS A CE  1 
ATOM   992  N  NZ  . LYS A 1 145  ? 54.593 60.300  29.016  1.00 30.63 ? 145  LYS A NZ  1 
ATOM   993  N  N   . LYS A 1 146  ? 57.698 58.549  22.316  1.00 17.81 ? 146  LYS A N   1 
ATOM   994  C  CA  . LYS A 1 146  ? 57.666 57.748  21.087  1.00 18.57 ? 146  LYS A CA  1 
ATOM   995  C  C   . LYS A 1 146  ? 57.709 56.255  21.444  1.00 16.64 ? 146  LYS A C   1 
ATOM   996  O  O   . LYS A 1 146  ? 56.992 55.425  20.869  1.00 16.51 ? 146  LYS A O   1 
ATOM   997  C  CB  . LYS A 1 146  ? 58.835 58.084  20.155  1.00 17.56 ? 146  LYS A CB  1 
ATOM   998  C  CG  . LYS A 1 146  ? 58.752 59.486  19.528  1.00 21.18 ? 146  LYS A CG  1 
ATOM   999  C  CD  . LYS A 1 146  ? 59.859 59.735  18.518  1.00 21.65 ? 146  LYS A CD  1 
ATOM   1000 C  CE  . LYS A 1 146  ? 59.857 61.168  18.042  1.00 25.35 ? 146  LYS A CE  1 
ATOM   1001 N  NZ  . LYS A 1 146  ? 60.970 61.276  17.066  1.00 28.35 ? 146  LYS A NZ  1 
ATOM   1002 N  N   . LEU A 1 147  ? 58.570 55.904  22.388  1.00 16.72 ? 147  LEU A N   1 
ATOM   1003 C  CA  . LEU A 1 147  ? 58.690 54.518  22.768  1.00 16.08 ? 147  LEU A CA  1 
ATOM   1004 C  C   . LEU A 1 147  ? 57.391 54.007  23.408  1.00 15.43 ? 147  LEU A C   1 
ATOM   1005 O  O   . LEU A 1 147  ? 56.970 52.895  23.112  1.00 15.78 ? 147  LEU A O   1 
ATOM   1006 C  CB  . LEU A 1 147  ? 59.903 54.332  23.711  1.00 18.61 ? 147  LEU A CB  1 
ATOM   1007 C  CG  . LEU A 1 147  ? 61.304 54.410  23.084  1.00 20.15 ? 147  LEU A CG  1 
ATOM   1008 C  CD1 . LEU A 1 147  ? 62.389 54.387  24.163  1.00 22.84 ? 147  LEU A CD1 1 
ATOM   1009 C  CD2 . LEU A 1 147  ? 61.469 53.226  22.144  1.00 21.88 ? 147  LEU A CD2 1 
ATOM   1010 N  N   . GLN A 1 148  ? 56.764 54.820  24.262  1.00 15.98 ? 148  GLN A N   1 
ATOM   1011 C  CA  . GLN A 1 148  ? 55.500 54.405  24.834  1.00 14.16 ? 148  GLN A CA  1 
ATOM   1012 C  C   . GLN A 1 148  ? 54.432 54.203  23.740  1.00 13.22 ? 148  GLN A C   1 
ATOM   1013 O  O   . GLN A 1 148  ? 53.604 53.260  23.841  1.00 12.78 ? 148  GLN A O   1 
ATOM   1014 C  CB  . GLN A 1 148  ? 54.985 55.464  25.793  1.00 16.18 ? 148  GLN A CB  1 
ATOM   1015 C  CG  . GLN A 1 148  ? 55.760 55.614  27.043  1.00 20.04 ? 148  GLN A CG  1 
ATOM   1016 C  CD  . GLN A 1 148  ? 54.999 56.458  27.998  1.00 22.58 ? 148  GLN A CD  1 
ATOM   1017 O  OE1 . GLN A 1 148  ? 53.947 57.041  27.654  1.00 26.19 ? 148  GLN A OE1 1 
ATOM   1018 N  NE2 . GLN A 1 148  ? 55.491 56.525  29.214  1.00 24.20 ? 148  GLN A NE2 1 
ATOM   1019 N  N   . MET A 1 149  ? 54.448 55.069  22.719  1.00 13.81 ? 149  MET A N   1 
ATOM   1020 C  CA  . MET A 1 149  ? 53.455 54.985  21.619  1.00 12.80 ? 149  MET A CA  1 
ATOM   1021 C  C   . MET A 1 149  ? 53.666 53.718  20.792  1.00 14.29 ? 149  MET A C   1 
ATOM   1022 O  O   . MET A 1 149  ? 52.709 52.995  20.494  1.00 11.25 ? 149  MET A O   1 
ATOM   1023 C  CB  . MET A 1 149  ? 53.542 56.262  20.722  1.00 13.73 ? 149  MET A CB  1 
ATOM   1024 C  CG  . MET A 1 149  ? 52.540 56.279  19.566  1.00 11.27 ? 149  MET A CG  1 
ATOM   1025 S  SD  . MET A 1 149  ? 50.870 56.387  20.153  1.00 15.84 ? 149  MET A SD  1 
ATOM   1026 C  CE  . MET A 1 149  ? 50.624 58.085  20.566  1.00 18.27 ? 149  MET A CE  1 
ATOM   1027 N  N   . LYS A 1 150  ? 54.932 53.438  20.462  1.00 13.07 ? 150  LYS A N   1 
ATOM   1028 C  CA  . LYS A 1 150  ? 55.271 52.231  19.697  1.00 12.41 ? 150  LYS A CA  1 
ATOM   1029 C  C   . LYS A 1 150  ? 54.831 51.005  20.470  1.00 13.61 ? 150  LYS A C   1 
ATOM   1030 O  O   . LYS A 1 150  ? 54.334 50.043  19.892  1.00 13.39 ? 150  LYS A O   1 
ATOM   1031 C  CB  . LYS A 1 150  ? 56.778 52.157  19.387  1.00 12.66 ? 150  LYS A CB  1 
ATOM   1032 C  CG  . LYS A 1 150  ? 57.154 53.175  18.276  1.00 16.45 ? 150  LYS A CG  1 
ATOM   1033 C  CD  . LYS A 1 150  ? 58.519 52.873  17.712  1.00 21.91 ? 150  LYS A CD  1 
ATOM   1034 C  CE  . LYS A 1 150  ? 59.579 53.345  18.654  1.00 25.42 ? 150  LYS A CE  1 
ATOM   1035 N  NZ  . LYS A 1 150  ? 60.942 53.112  18.074  1.00 27.03 ? 150  LYS A NZ  1 
ATOM   1036 N  N   . SER A 1 151  ? 54.967 51.069  21.797  1.00 13.82 ? 151  SER A N   1 
ATOM   1037 C  CA  . SER A 1 151  ? 54.570 49.941  22.629  1.00 14.48 ? 151  SER A CA  1 
ATOM   1038 C  C   . SER A 1 151  ? 53.043 49.692  22.661  1.00 14.25 ? 151  SER A C   1 
ATOM   1039 O  O   . SER A 1 151  ? 52.615 48.538  22.653  1.00 14.89 ? 151  SER A O   1 
ATOM   1040 C  CB  . SER A 1 151  ? 55.136 50.097  24.045  1.00 14.78 ? 151  SER A CB  1 
ATOM   1041 O  OG  . SER A 1 151  ? 54.896 48.904  24.759  1.00 20.01 ? 151  SER A OG  1 
ATOM   1042 N  N   . ILE A 1 152  ? 52.214 50.739  22.672  1.00 12.61 ? 152  ILE A N   1 
ATOM   1043 C  CA  . ILE A 1 152  ? 50.770 50.529  22.654  1.00 11.86 ? 152  ILE A CA  1 
ATOM   1044 C  C   . ILE A 1 152  ? 50.276 50.164  21.280  1.00 12.29 ? 152  ILE A C   1 
ATOM   1045 O  O   . ILE A 1 152  ? 49.216 49.596  21.157  1.00 13.19 ? 152  ILE A O   1 
ATOM   1046 C  CB  . ILE A 1 152  ? 49.913 51.706  23.247  1.00 14.73 ? 152  ILE A CB  1 
ATOM   1047 C  CG1 . ILE A 1 152  ? 50.224 53.056  22.643  1.00 12.61 ? 152  ILE A CG1 1 
ATOM   1048 C  CG2 . ILE A 1 152  ? 50.133 51.742  24.750  1.00 13.50 ? 152  ILE A CG2 1 
ATOM   1049 C  CD1 . ILE A 1 152  ? 49.078 54.038  22.848  1.00 12.27 ? 152  ILE A CD1 1 
ATOM   1050 N  N   . VAL A 1 153  ? 51.068 50.440  20.254  1.00 11.46 ? 153  VAL A N   1 
ATOM   1051 C  CA  . VAL A 1 153  ? 50.698 49.998  18.934  1.00 12.62 ? 153  VAL A CA  1 
ATOM   1052 C  C   . VAL A 1 153  ? 51.107 48.510  18.818  1.00 13.08 ? 153  VAL A C   1 
ATOM   1053 O  O   . VAL A 1 153  ? 50.296 47.661  18.443  1.00 13.10 ? 153  VAL A O   1 
ATOM   1054 C  CB  . VAL A 1 153  ? 51.363 50.875  17.870  1.00 12.63 ? 153  VAL A CB  1 
ATOM   1055 C  CG1 . VAL A 1 153  ? 51.163 50.238  16.462  1.00 16.38 ? 153  VAL A CG1 1 
ATOM   1056 C  CG2 . VAL A 1 153  ? 50.696 52.234  17.870  1.00 12.89 ? 153  VAL A CG2 1 
ATOM   1057 N  N   . LYS A 1 154  ? 52.342 48.185  19.216  1.00 14.59 ? 154  LYS A N   1 
ATOM   1058 C  CA  . LYS A 1 154  ? 52.819 46.804  19.119  1.00 15.89 ? 154  LYS A CA  1 
ATOM   1059 C  C   . LYS A 1 154  ? 51.983 45.818  19.919  1.00 15.87 ? 154  LYS A C   1 
ATOM   1060 O  O   . LYS A 1 154  ? 51.765 44.690  19.486  1.00 15.92 ? 154  LYS A O   1 
ATOM   1061 C  CB  . LYS A 1 154  ? 54.263 46.746  19.569  1.00 19.88 ? 154  LYS A CB  1 
ATOM   1062 C  CG  . LYS A 1 154  ? 54.879 45.373  19.390  1.00 23.49 ? 154  LYS A CG  1 
ATOM   1063 C  CD  . LYS A 1 154  ? 56.353 45.558  19.092  1.00 28.62 ? 154  LYS A CD  1 
ATOM   1064 C  CE  . LYS A 1 154  ? 57.043 46.274  20.205  1.00 31.50 ? 154  LYS A CE  1 
ATOM   1065 N  NZ  . LYS A 1 154  ? 58.457 46.587  19.822  1.00 34.31 ? 154  LYS A NZ  1 
ATOM   1066 N  N   . ASN A 1 155  ? 51.491 46.238  21.076  1.00 15.99 ? 155  ASN A N   1 
ATOM   1067 C  CA  . ASN A 1 155  ? 50.655 45.403  21.930  1.00 16.81 ? 155  ASN A CA  1 
ATOM   1068 C  C   . ASN A 1 155  ? 49.163 45.370  21.559  1.00 15.50 ? 155  ASN A C   1 
ATOM   1069 O  O   . ASN A 1 155  ? 48.386 44.771  22.273  1.00 17.71 ? 155  ASN A O   1 
ATOM   1070 C  CB  . ASN A 1 155  ? 50.836 45.788  23.420  1.00 19.46 ? 155  ASN A CB  1 
ATOM   1071 C  CG  . ASN A 1 155  ? 49.952 47.003  23.852  1.00 23.15 ? 155  ASN A CG  1 
ATOM   1072 O  OD1 . ASN A 1 155  ? 49.170 47.532  23.036  1.00 24.75 ? 155  ASN A OD1 1 
ATOM   1073 N  ND2 . ASN A 1 155  ? 50.074 47.441  25.128  1.00 21.07 ? 155  ASN A ND2 1 
ATOM   1074 N  N   . GLY A 1 156  ? 48.739 46.024  20.472  1.00 13.73 ? 156  GLY A N   1 
ATOM   1075 C  CA  . GLY A 1 156  ? 47.344 45.936  20.099  1.00 12.62 ? 156  GLY A CA  1 
ATOM   1076 C  C   . GLY A 1 156  ? 46.331 46.877  20.719  1.00 11.91 ? 156  GLY A C   1 
ATOM   1077 O  O   . GLY A 1 156  ? 45.165 46.835  20.307  1.00 15.32 ? 156  GLY A O   1 
ATOM   1078 N  N   . GLN A 1 157  ? 46.722 47.799  21.605  1.00 10.84 ? 157  GLN A N   1 
ATOM   1079 C  CA  . GLN A 1 157  ? 45.717 48.708  22.176  1.00 10.20 ? 157  GLN A CA  1 
ATOM   1080 C  C   . GLN A 1 157  ? 45.321 49.819  21.183  1.00 9.59  ? 157  GLN A C   1 
ATOM   1081 O  O   . GLN A 1 157  ? 44.135 50.138  21.055  1.00 10.59 ? 157  GLN A O   1 
ATOM   1082 C  CB  . GLN A 1 157  ? 46.260 49.351  23.427  1.00 11.30 ? 157  GLN A CB  1 
ATOM   1083 C  CG  . GLN A 1 157  ? 46.242 48.468  24.606  1.00 13.04 ? 157  GLN A CG  1 
ATOM   1084 C  CD  . GLN A 1 157  ? 46.734 49.240  25.822  1.00 11.56 ? 157  GLN A CD  1 
ATOM   1085 O  OE1 . GLN A 1 157  ? 47.918 49.227  26.159  1.00 14.23 ? 157  GLN A OE1 1 
ATOM   1086 N  NE2 . GLN A 1 157  ? 45.848 49.967  26.425  1.00 11.26 ? 157  GLN A NE2 1 
ATOM   1087 N  N   . LEU A 1 158  ? 46.311 50.417  20.518  1.00 10.43 ? 158  LEU A N   1 
ATOM   1088 C  CA  . LEU A 1 158  ? 46.077 51.439  19.505  1.00 10.62 ? 158  LEU A CA  1 
ATOM   1089 C  C   . LEU A 1 158  ? 46.227 50.737  18.152  1.00 10.41 ? 158  LEU A C   1 
ATOM   1090 O  O   A LEU A 1 158  ? 47.285 50.149  17.854  0.50 11.16 ? 158  LEU A O   1 
ATOM   1091 O  O   B LEU A 1 158  ? 47.387 50.449  17.795  0.50 9.50  ? 158  LEU A O   1 
ATOM   1092 C  CB  . LEU A 1 158  ? 47.110 52.571  19.642  1.00 12.48 ? 158  LEU A CB  1 
ATOM   1093 C  CG  A LEU A 1 158  ? 46.981 53.849  18.799  0.50 14.09 ? 158  LEU A CG  1 
ATOM   1094 C  CG  B LEU A 1 158  ? 47.043 53.702  18.631  0.50 11.67 ? 158  LEU A CG  1 
ATOM   1095 C  CD1 A LEU A 1 158  ? 48.239 54.685  19.009  0.50 15.94 ? 158  LEU A CD1 1 
ATOM   1096 C  CD1 B LEU A 1 158  ? 45.679 54.343  18.593  0.50 11.09 ? 158  LEU A CD1 1 
ATOM   1097 C  CD2 A LEU A 1 158  ? 46.852 53.557  17.345  0.50 13.80 ? 158  LEU A CD2 1 
ATOM   1098 C  CD2 B LEU A 1 158  ? 48.123 54.750  18.910  0.50 13.34 ? 158  LEU A CD2 1 
ATOM   1099 N  N   . GLU A 1 159  ? 45.200 50.804  17.316  1.00 8.49  ? 159  GLU A N   1 
ATOM   1100 C  CA  . GLU A 1 159  ? 45.289 50.141  16.023  1.00 8.18  ? 159  GLU A CA  1 
ATOM   1101 C  C   . GLU A 1 159  ? 44.977 51.130  14.896  1.00 7.99  ? 159  GLU A C   1 
ATOM   1102 O  O   . GLU A 1 159  ? 43.957 51.816  14.940  1.00 8.25  ? 159  GLU A O   1 
ATOM   1103 C  CB  . GLU A 1 159  ? 44.260 49.020  15.944  1.00 10.11 ? 159  GLU A CB  1 
ATOM   1104 C  CG  . GLU A 1 159  ? 44.272 48.254  14.597  1.00 10.42 ? 159  GLU A CG  1 
ATOM   1105 C  CD  . GLU A 1 159  ? 43.298 47.129  14.687  1.00 13.29 ? 159  GLU A CD  1 
ATOM   1106 O  OE1 . GLU A 1 159  ? 43.607 46.115  15.407  1.00 11.39 ? 159  GLU A OE1 1 
ATOM   1107 O  OE2 . GLU A 1 159  ? 42.221 47.278  14.071  1.00 10.91 ? 159  GLU A OE2 1 
ATOM   1108 N  N   . PHE A 1 160  ? 45.825 51.163  13.848  1.00 7.96  ? 160  PHE A N   1 
ATOM   1109 C  CA  . PHE A 1 160  ? 45.554 52.020  12.726  1.00 6.54  ? 160  PHE A CA  1 
ATOM   1110 C  C   . PHE A 1 160  ? 44.637 51.296  11.782  1.00 7.00  ? 160  PHE A C   1 
ATOM   1111 O  O   . PHE A 1 160  ? 44.778 50.106  11.499  1.00 7.91  ? 160  PHE A O   1 
ATOM   1112 C  CB  . PHE A 1 160  ? 46.882 52.407  12.052  1.00 6.40  ? 160  PHE A CB  1 
ATOM   1113 C  CG  . PHE A 1 160  ? 47.772 53.247  12.946  1.00 6.94  ? 160  PHE A CG  1 
ATOM   1114 C  CD1 . PHE A 1 160  ? 47.458 54.612  13.163  1.00 8.88  ? 160  PHE A CD1 1 
ATOM   1115 C  CD2 . PHE A 1 160  ? 48.877 52.655  13.603  1.00 10.24 ? 160  PHE A CD2 1 
ATOM   1116 C  CE1 . PHE A 1 160  ? 48.247 55.357  14.043  1.00 11.28 ? 160  PHE A CE1 1 
ATOM   1117 C  CE2 . PHE A 1 160  ? 49.660 53.422  14.487  1.00 12.97 ? 160  PHE A CE2 1 
ATOM   1118 C  CZ  . PHE A 1 160  ? 49.331 54.755  14.701  1.00 11.99 ? 160  PHE A CZ  1 
ATOM   1119 N  N   . VAL A 1 161  ? 43.639 52.041  11.320  1.00 5.96  ? 161  VAL A N   1 
ATOM   1120 C  CA  . VAL A 1 161  ? 42.669 51.546  10.350  1.00 7.36  ? 161  VAL A CA  1 
ATOM   1121 C  C   . VAL A 1 161  ? 42.898 52.372  9.077   1.00 6.37  ? 161  VAL A C   1 
ATOM   1122 O  O   . VAL A 1 161  ? 42.993 53.608  9.131   1.00 7.40  ? 161  VAL A O   1 
ATOM   1123 C  CB  . VAL A 1 161  ? 41.209 51.663  10.921  1.00 9.02  ? 161  VAL A CB  1 
ATOM   1124 C  CG1 . VAL A 1 161  ? 41.080 50.603  12.132  1.00 8.14  ? 161  VAL A CG1 1 
ATOM   1125 C  CG2 . VAL A 1 161  ? 40.921 53.099  11.474  1.00 8.45  ? 161  VAL A CG2 1 
ATOM   1126 N  N   . THR A 1 162  ? 42.946 51.662  7.930   1.00 6.21  ? 162  THR A N   1 
ATOM   1127 C  CA  . THR A 1 162  ? 43.295 52.185  6.589   1.00 8.15  ? 162  THR A CA  1 
ATOM   1128 C  C   . THR A 1 162  ? 44.776 52.666  6.539   1.00 7.26  ? 162  THR A C   1 
ATOM   1129 O  O   . THR A 1 162  ? 45.608 52.099  5.764   1.00 7.03  ? 162  THR A O   1 
ATOM   1130 C  CB  . THR A 1 162  ? 42.407 53.351  6.089   1.00 6.42  ? 162  THR A CB  1 
ATOM   1131 O  OG1 . THR A 1 162  ? 41.035 52.977  6.119   1.00 9.39  ? 162  THR A OG1 1 
ATOM   1132 C  CG2 . THR A 1 162  ? 42.715 53.589  4.591   1.00 7.71  ? 162  THR A CG2 1 
ATOM   1133 N  N   . GLY A 1 163  ? 45.093 53.691  7.352   1.00 7.11  ? 163  GLY A N   1 
ATOM   1134 C  CA  . GLY A 1 163  ? 46.453 54.201  7.396   1.00 7.31  ? 163  GLY A CA  1 
ATOM   1135 C  C   . GLY A 1 163  ? 46.799 55.157  6.261   1.00 7.64  ? 163  GLY A C   1 
ATOM   1136 O  O   . GLY A 1 163  ? 47.987 55.323  5.950   1.00 8.88  ? 163  GLY A O   1 
ATOM   1137 N  N   . GLY A 1 164  ? 45.795 55.703  5.598   1.00 5.86  ? 164  GLY A N   1 
ATOM   1138 C  CA  . GLY A 1 164  ? 46.080 56.704  4.563   1.00 7.51  ? 164  GLY A CA  1 
ATOM   1139 C  C   . GLY A 1 164  ? 46.383 58.033  5.227   1.00 7.40  ? 164  GLY A C   1 
ATOM   1140 O  O   . GLY A 1 164  ? 46.098 58.242  6.441   1.00 6.78  ? 164  GLY A O   1 
ATOM   1141 N  N   . TRP A 1 165  ? 47.016 58.928  4.456   1.00 6.53  ? 165  TRP A N   1 
ATOM   1142 C  CA  . TRP A 1 165  ? 47.246 60.288  4.957   1.00 6.72  ? 165  TRP A CA  1 
ATOM   1143 C  C   . TRP A 1 165  ? 45.896 60.943  5.440   1.00 7.67  ? 165  TRP A C   1 
ATOM   1144 O  O   . TRP A 1 165  ? 45.890 61.655  6.423   1.00 7.21  ? 165  TRP A O   1 
ATOM   1145 C  CB  . TRP A 1 165  ? 47.905 61.064  3.837   1.00 5.83  ? 165  TRP A CB  1 
ATOM   1146 C  CG  . TRP A 1 165  ? 48.684 62.255  4.279   1.00 7.60  ? 165  TRP A CG  1 
ATOM   1147 C  CD1 . TRP A 1 165  ? 48.435 63.555  3.982   1.00 10.14 ? 165  TRP A CD1 1 
ATOM   1148 C  CD2 . TRP A 1 165  ? 49.881 62.229  5.061   1.00 10.18 ? 165  TRP A CD2 1 
ATOM   1149 N  NE1 . TRP A 1 165  ? 49.429 64.378  4.549   1.00 10.67 ? 165  TRP A NE1 1 
ATOM   1150 C  CE2 . TRP A 1 165  ? 50.321 63.587  5.210   1.00 10.57 ? 165  TRP A CE2 1 
ATOM   1151 C  CE3 . TRP A 1 165  ? 50.630 61.202  5.660   1.00 10.09 ? 165  TRP A CE3 1 
ATOM   1152 C  CZ2 . TRP A 1 165  ? 51.484 63.937  5.951   1.00 10.72 ? 165  TRP A CZ2 1 
ATOM   1153 C  CZ3 . TRP A 1 165  ? 51.800 61.553  6.381   1.00 10.25 ? 165  TRP A CZ3 1 
ATOM   1154 C  CH2 . TRP A 1 165  ? 52.203 62.936  6.510   1.00 11.69 ? 165  TRP A CH2 1 
ATOM   1155 N  N   . VAL A 1 166  ? 44.799 60.605  4.733   1.00 7.20  ? 166  VAL A N   1 
ATOM   1156 C  CA  . VAL A 1 166  ? 43.447 61.102  5.020   1.00 8.08  ? 166  VAL A CA  1 
ATOM   1157 C  C   . VAL A 1 166  ? 42.438 60.003  4.826   1.00 7.13  ? 166  VAL A C   1 
ATOM   1158 O  O   . VAL A 1 166  ? 42.837 58.852  4.539   1.00 7.02  ? 166  VAL A O   1 
ATOM   1159 C  CB  . VAL A 1 166  ? 43.029 62.263  4.030   1.00 6.26  ? 166  VAL A CB  1 
ATOM   1160 C  CG1 . VAL A 1 166  ? 44.070 63.440  4.077   1.00 7.88  ? 166  VAL A CG1 1 
ATOM   1161 C  CG2 . VAL A 1 166  ? 42.982 61.768  2.586   1.00 10.14 ? 166  VAL A CG2 1 
ATOM   1162 N  N   . MET A 1 167  ? 41.167 60.314  5.025   1.00 7.31  ? 167  MET A N   1 
ATOM   1163 C  CA  . MET A 1 167  ? 40.064 59.327  4.713   1.00 7.48  ? 167  MET A CA  1 
ATOM   1164 C  C   . MET A 1 167  ? 39.536 60.084  3.485   1.00 6.74  ? 167  MET A C   1 
ATOM   1165 O  O   . MET A 1 167  ? 38.768 61.061  3.613   1.00 6.51  ? 167  MET A O   1 
ATOM   1166 C  CB  . MET A 1 167  ? 39.063 59.326  5.830   1.00 6.86  ? 167  MET A CB  1 
ATOM   1167 C  CG  . MET A 1 167  ? 37.798 58.629  5.509   1.00 6.00  ? 167  MET A CG  1 
ATOM   1168 S  SD  . MET A 1 167  ? 36.600 58.613  6.931   1.00 8.29  ? 167  MET A SD  1 
ATOM   1169 C  CE  . MET A 1 167  ? 37.618 57.849  8.279   1.00 7.45  ? 167  MET A CE  1 
ATOM   1170 N  N   . PRO A 1 168  ? 39.929 59.662  2.267   1.00 6.42  ? 168  PRO A N   1 
ATOM   1171 C  CA  . PRO A 1 168  ? 39.514 60.407  1.102   1.00 7.34  ? 168  PRO A CA  1 
ATOM   1172 C  C   . PRO A 1 168  ? 38.095 60.427  0.675   1.00 5.79  ? 168  PRO A C   1 
ATOM   1173 O  O   . PRO A 1 168  ? 37.330 59.515  0.902   1.00 6.04  ? 168  PRO A O   1 
ATOM   1174 C  CB  . PRO A 1 168  ? 40.424 59.830  -0.023  1.00 6.91  ? 168  PRO A CB  1 
ATOM   1175 C  CG  . PRO A 1 168  ? 40.485 58.362  0.386   1.00 5.09  ? 168  PRO A CG  1 
ATOM   1176 C  CD  . PRO A 1 168  ? 40.664 58.432  1.893   1.00 5.63  ? 168  PRO A CD  1 
ATOM   1177 N  N   . ASP A 1 169  ? 37.776 61.524  -0.015  1.00 7.64  ? 169  ASP A N   1 
ATOM   1178 C  CA  . ASP A 1 169  ? 36.533 61.564  -0.779  1.00 8.05  ? 169  ASP A CA  1 
ATOM   1179 C  C   . ASP A 1 169  ? 36.638 60.372  -1.771  1.00 7.68  ? 169  ASP A C   1 
ATOM   1180 O  O   . ASP A 1 169  ? 37.739 60.033  -2.242  1.00 6.32  ? 169  ASP A O   1 
ATOM   1181 C  CB  . ASP A 1 169  ? 36.535 62.881  -1.590  1.00 7.36  ? 169  ASP A CB  1 
ATOM   1182 C  CG  . ASP A 1 169  ? 35.393 62.960  -2.594  1.00 7.36  ? 169  ASP A CG  1 
ATOM   1183 O  OD1 . ASP A 1 169  ? 34.294 62.407  -2.280  1.00 8.52  ? 169  ASP A OD1 1 
ATOM   1184 O  OD2 . ASP A 1 169  ? 35.546 63.520  -3.700  1.00 7.72  ? 169  ASP A OD2 1 
ATOM   1185 N  N   . GLU A 1 170  ? 35.506 59.776  -2.129  1.00 6.67  ? 170  GLU A N   1 
ATOM   1186 C  CA  . GLU A 1 170  ? 35.504 58.662  -3.073  1.00 7.07  ? 170  GLU A CA  1 
ATOM   1187 C  C   . GLU A 1 170  ? 34.788 59.041  -4.374  1.00 5.76  ? 170  GLU A C   1 
ATOM   1188 O  O   . GLU A 1 170  ? 34.814 58.248  -5.291  1.00 6.10  ? 170  GLU A O   1 
ATOM   1189 C  CB  . GLU A 1 170  ? 34.861 57.438  -2.414  1.00 6.69  ? 170  GLU A CB  1 
ATOM   1190 C  CG  . GLU A 1 170  ? 35.656 57.010  -1.203  1.00 6.84  ? 170  GLU A CG  1 
ATOM   1191 C  CD  . GLU A 1 170  ? 35.087 55.773  -0.490  1.00 7.00  ? 170  GLU A CD  1 
ATOM   1192 O  OE1 . GLU A 1 170  ? 34.292 55.040  -1.096  1.00 8.17  ? 170  GLU A OE1 1 
ATOM   1193 O  OE2 . GLU A 1 170  ? 35.482 55.556  0.698   1.00 7.59  ? 170  GLU A OE2 1 
ATOM   1194 N  N   . ALA A 1 171  ? 34.155 60.249  -4.450  1.00 6.10  ? 171  ALA A N   1 
ATOM   1195 C  CA  . ALA A 1 171  ? 33.450 60.679  -5.667  1.00 7.41  ? 171  ALA A CA  1 
ATOM   1196 C  C   . ALA A 1 171  ? 34.330 61.454  -6.699  1.00 4.94  ? 171  ALA A C   1 
ATOM   1197 O  O   . ALA A 1 171  ? 34.374 61.092  -7.858  1.00 7.97  ? 171  ALA A O   1 
ATOM   1198 C  CB  . ALA A 1 171  ? 32.251 61.553  -5.291  1.00 8.80  ? 171  ALA A CB  1 
ATOM   1199 N  N   . ASN A 1 172  ? 35.034 62.471  -6.211  1.00 7.90  ? 172  ASN A N   1 
ATOM   1200 C  CA  . ASN A 1 172  ? 35.821 63.348  -7.087  1.00 7.22  ? 172  ASN A CA  1 
ATOM   1201 C  C   . ASN A 1 172  ? 37.273 62.988  -7.243  1.00 7.98  ? 172  ASN A C   1 
ATOM   1202 O  O   . ASN A 1 172  ? 37.948 63.429  -8.200  1.00 6.02  ? 172  ASN A O   1 
ATOM   1203 C  CB  . ASN A 1 172  ? 35.751 64.772  -6.573  1.00 7.99  ? 172  ASN A CB  1 
ATOM   1204 C  CG  . ASN A 1 172  ? 34.346 65.298  -6.423  1.00 9.03  ? 172  ASN A CG  1 
ATOM   1205 O  OD1 . ASN A 1 172  ? 33.664 65.508  -7.425  1.00 9.78  ? 172  ASN A OD1 1 
ATOM   1206 N  ND2 . ASN A 1 172  ? 33.948 65.546  -5.180  1.00 7.70  ? 172  ASN A ND2 1 
ATOM   1207 N  N   . SER A 1 173  ? 37.762 62.145  -6.331  1.00 7.11  ? 173  SER A N   1 
ATOM   1208 C  CA  . SER A 1 173  ? 39.189 61.784  -6.360  1.00 5.68  ? 173  SER A CA  1 
ATOM   1209 C  C   . SER A 1 173  ? 39.597 60.860  -7.476  1.00 7.68  ? 173  SER A C   1 
ATOM   1210 O  O   . SER A 1 173  ? 38.857 59.962  -7.881  1.00 8.50  ? 173  SER A O   1 
ATOM   1211 C  CB  . SER A 1 173  ? 39.506 61.124  -4.992  1.00 6.66  ? 173  SER A CB  1 
ATOM   1212 O  OG  . SER A 1 173  ? 38.563 60.014  -4.812  1.00 6.32  ? 173  SER A OG  1 
ATOM   1213 N  N   . HIS A 1 174  ? 40.783 61.143  -8.039  1.00 6.76  ? 174  HIS A N   1 
ATOM   1214 C  CA  . HIS A 1 174  ? 41.332 60.274  -9.049  1.00 6.54  ? 174  HIS A CA  1 
ATOM   1215 C  C   . HIS A 1 174  ? 41.956 59.056  -8.339  1.00 4.51  ? 174  HIS A C   1 
ATOM   1216 O  O   . HIS A 1 174  ? 42.581 59.229  -7.290  1.00 5.75  ? 174  HIS A O   1 
ATOM   1217 C  CB  . HIS A 1 174  ? 42.392 61.009  -9.874  1.00 7.31  ? 174  HIS A CB  1 
ATOM   1218 C  CG  . HIS A 1 174  ? 42.614 60.375  -11.212 1.00 7.57  ? 174  HIS A CG  1 
ATOM   1219 N  ND1 . HIS A 1 174  ? 43.307 59.184  -11.347 1.00 8.18  ? 174  HIS A ND1 1 
ATOM   1220 C  CD2 . HIS A 1 174  ? 42.188 60.713  -12.458 1.00 7.54  ? 174  HIS A CD2 1 
ATOM   1221 C  CE1 . HIS A 1 174  ? 43.298 58.829  -12.619 1.00 9.81  ? 174  HIS A CE1 1 
ATOM   1222 N  NE2 . HIS A 1 174  ? 42.612 59.730  -13.308 1.00 8.68  ? 174  HIS A NE2 1 
ATOM   1223 N  N   . TRP A 1 175  ? 41.764 57.865  -8.880  1.00 4.53  ? 175  TRP A N   1 
ATOM   1224 C  CA  . TRP A 1 175  ? 42.366 56.687  -8.255  1.00 5.91  ? 175  TRP A CA  1 
ATOM   1225 C  C   . TRP A 1 175  ? 43.881 56.873  -8.007  1.00 6.06  ? 175  TRP A C   1 
ATOM   1226 O  O   . TRP A 1 175  ? 44.430 56.360  -7.012  1.00 5.98  ? 175  TRP A O   1 
ATOM   1227 C  CB  . TRP A 1 175  ? 42.069 55.415  -9.096  1.00 4.75  ? 175  TRP A CB  1 
ATOM   1228 C  CG  . TRP A 1 175  ? 42.939 55.263  -10.337 1.00 4.32  ? 175  TRP A CG  1 
ATOM   1229 C  CD1 . TRP A 1 175  ? 42.616 55.583  -11.672 1.00 6.01  ? 175  TRP A CD1 1 
ATOM   1230 C  CD2 . TRP A 1 175  ? 44.227 54.664  -10.390 1.00 6.29  ? 175  TRP A CD2 1 
ATOM   1231 N  NE1 . TRP A 1 175  ? 43.658 55.226  -12.508 1.00 6.61  ? 175  TRP A NE1 1 
ATOM   1232 C  CE2 . TRP A 1 175  ? 44.654 54.642  -11.751 1.00 8.70  ? 175  TRP A CE2 1 
ATOM   1233 C  CE3 . TRP A 1 175  ? 45.063 54.107  -9.406  1.00 10.69 ? 175  TRP A CE3 1 
ATOM   1234 C  CZ2 . TRP A 1 175  ? 45.908 54.079  -12.141 1.00 8.54  ? 175  TRP A CZ2 1 
ATOM   1235 C  CZ3 . TRP A 1 175  ? 46.301 53.556  -9.810  1.00 8.99  ? 175  TRP A CZ3 1 
ATOM   1236 C  CH2 . TRP A 1 175  ? 46.701 53.549  -11.151 1.00 9.46  ? 175  TRP A CH2 1 
ATOM   1237 N  N   . ARG A 1 176  ? 44.575 57.574  -8.936  1.00 5.70  ? 176  ARG A N   1 
ATOM   1238 C  CA  . ARG A 1 176  ? 46.021 57.738  -8.764  1.00 6.14  ? 176  ARG A CA  1 
ATOM   1239 C  C   . ARG A 1 176  ? 46.288 58.506  -7.456  1.00 5.85  ? 176  ARG A C   1 
ATOM   1240 O  O   . ARG A 1 176  ? 47.310 58.215  -6.778  1.00 7.05  ? 176  ARG A O   1 
ATOM   1241 C  CB  . ARG A 1 176  ? 46.575 58.537  -9.976  1.00 7.28  ? 176  ARG A CB  1 
ATOM   1242 C  CG  . ARG A 1 176  ? 46.634 57.695  -11.228 1.00 10.60 ? 176  ARG A CG  1 
ATOM   1243 C  CD  . ARG A 1 176  ? 46.620 58.475  -12.565 1.00 9.92  ? 176  ARG A CD  1 
ATOM   1244 N  NE  . ARG A 1 176  ? 47.728 59.401  -12.611 1.00 9.48  ? 176  ARG A NE  1 
ATOM   1245 C  CZ  . ARG A 1 176  ? 47.867 60.293  -13.596 1.00 6.96  ? 176  ARG A CZ  1 
ATOM   1246 N  NH1 . ARG A 1 176  ? 46.958 60.309  -14.614 1.00 8.67  ? 176  ARG A NH1 1 
ATOM   1247 N  NH2 . ARG A 1 176  ? 48.848 61.177  -13.549 1.00 9.97  ? 176  ARG A NH2 1 
ATOM   1248 N  N   . ASN A 1 177  ? 45.438 59.476  -7.108  1.00 5.85  ? 177  ASN A N   1 
ATOM   1249 C  CA  . ASN A 1 177  ? 45.686 60.237  -5.880  1.00 5.09  ? 177  ASN A CA  1 
ATOM   1250 C  C   . ASN A 1 177  ? 45.179 59.512  -4.611  1.00 7.97  ? 177  ASN A C   1 
ATOM   1251 O  O   . ASN A 1 177  ? 45.674 59.726  -3.489  1.00 6.74  ? 177  ASN A O   1 
ATOM   1252 C  CB  . ASN A 1 177  ? 45.062 61.621  -5.965  1.00 7.88  ? 177  ASN A CB  1 
ATOM   1253 C  CG  . ASN A 1 177  ? 45.742 62.493  -7.019  1.00 7.94  ? 177  ASN A CG  1 
ATOM   1254 O  OD1 . ASN A 1 177  ? 46.902 62.277  -7.358  1.00 8.33  ? 177  ASN A OD1 1 
ATOM   1255 N  ND2 . ASN A 1 177  ? 45.017 63.466  -7.551  1.00 10.18 ? 177  ASN A ND2 1 
ATOM   1256 N  N   . VAL A 1 178  ? 44.176 58.660  -4.823  1.00 7.57  ? 178  VAL A N   1 
ATOM   1257 C  CA  . VAL A 1 178  ? 43.729 57.820  -3.701  1.00 7.88  ? 178  VAL A CA  1 
ATOM   1258 C  C   . VAL A 1 178  ? 44.923 56.891  -3.340  1.00 6.25  ? 178  VAL A C   1 
ATOM   1259 O  O   . VAL A 1 178  ? 45.248 56.694  -2.153  1.00 5.79  ? 178  VAL A O   1 
ATOM   1260 C  CB  . VAL A 1 178  ? 42.501 56.957  -4.086  1.00 5.40  ? 178  VAL A CB  1 
ATOM   1261 C  CG1 . VAL A 1 178  ? 42.162 55.963  -2.957  1.00 6.04  ? 178  VAL A CG1 1 
ATOM   1262 C  CG2 . VAL A 1 178  ? 41.290 57.835  -4.244  1.00 6.24  ? 178  VAL A CG2 1 
ATOM   1263 N  N   . LEU A 1 179  ? 45.614 56.356  -4.359  1.00 5.22  ? 179  LEU A N   1 
ATOM   1264 C  CA  . LEU A 1 179  ? 46.777 55.492  -4.110  1.00 6.53  ? 179  LEU A CA  1 
ATOM   1265 C  C   . LEU A 1 179  ? 47.925 56.315  -3.529  1.00 7.24  ? 179  LEU A C   1 
ATOM   1266 O  O   . LEU A 1 179  ? 48.562 55.917  -2.524  1.00 7.54  ? 179  LEU A O   1 
ATOM   1267 C  CB  . LEU A 1 179  ? 47.223 54.804  -5.404  1.00 7.33  ? 179  LEU A CB  1 
ATOM   1268 C  CG  . LEU A 1 179  ? 48.584 54.025  -5.310  1.00 6.02  ? 179  LEU A CG  1 
ATOM   1269 C  CD1 . LEU A 1 179  ? 48.447 52.862  -4.262  1.00 7.23  ? 179  LEU A CD1 1 
ATOM   1270 C  CD2 . LEU A 1 179  ? 48.920 53.417  -6.698  1.00 9.43  ? 179  LEU A CD2 1 
ATOM   1271 N  N   . LEU A 1 180  ? 48.116 57.532  -4.056  1.00 5.28  ? 180  LEU A N   1 
ATOM   1272 C  CA  . LEU A 1 180  ? 49.216 58.394  -3.580  1.00 7.21  ? 180  LEU A CA  1 
ATOM   1273 C  C   . LEU A 1 180  ? 49.044 58.600  -2.068  1.00 5.53  ? 180  LEU A C   1 
ATOM   1274 O  O   . LEU A 1 180  ? 49.972 58.405  -1.263  1.00 9.21  ? 180  LEU A O   1 
ATOM   1275 C  CB  . LEU A 1 180  ? 49.146 59.759  -4.268  1.00 6.55  ? 180  LEU A CB  1 
ATOM   1276 C  CG  . LEU A 1 180  ? 50.292 60.710  -3.901  1.00 7.61  ? 180  LEU A CG  1 
ATOM   1277 C  CD1 . LEU A 1 180  ? 51.615 60.213  -4.479  1.00 8.88  ? 180  LEU A CD1 1 
ATOM   1278 C  CD2 . LEU A 1 180  ? 49.950 62.110  -4.445  1.00 8.75  ? 180  LEU A CD2 1 
ATOM   1279 N  N   . GLN A 1 181  ? 47.847 58.977  -1.618  1.00 8.52  ? 181  GLN A N   1 
ATOM   1280 C  CA  . GLN A 1 181  ? 47.649 59.299  -0.165  1.00 4.54  ? 181  GLN A CA  1 
ATOM   1281 C  C   . GLN A 1 181  ? 47.716 58.036  0.734   1.00 6.74  ? 181  GLN A C   1 
ATOM   1282 O  O   . GLN A 1 181  ? 48.222 58.065  1.862   1.00 5.85  ? 181  GLN A O   1 
ATOM   1283 C  CB  . GLN A 1 181  ? 46.336 60.147  0.009   1.00 6.77  ? 181  GLN A CB  1 
ATOM   1284 C  CG  . GLN A 1 181  ? 44.990 59.437  -0.210  1.00 5.30  ? 181  GLN A CG  1 
ATOM   1285 C  CD  . GLN A 1 181  ? 44.624 58.459  0.971   1.00 7.51  ? 181  GLN A CD  1 
ATOM   1286 O  OE1 . GLN A 1 181  ? 44.937 58.729  2.145   1.00 6.70  ? 181  GLN A OE1 1 
ATOM   1287 N  NE2 . GLN A 1 181  ? 43.976 57.329  0.630   1.00 8.34  ? 181  GLN A NE2 1 
ATOM   1288 N  N   . LEU A 1 182  ? 47.219 56.929  0.192   1.00 6.94  ? 182  LEU A N   1 
ATOM   1289 C  CA  . LEU A 1 182  ? 47.292 55.687  0.920   1.00 7.82  ? 182  LEU A CA  1 
ATOM   1290 C  C   . LEU A 1 182  ? 48.759 55.322  1.131   1.00 8.26  ? 182  LEU A C   1 
ATOM   1291 O  O   . LEU A 1 182  ? 49.175 54.998  2.235   1.00 5.82  ? 182  LEU A O   1 
ATOM   1292 C  CB  . LEU A 1 182  ? 46.578 54.564  0.154   1.00 6.28  ? 182  LEU A CB  1 
ATOM   1293 C  CG  . LEU A 1 182  ? 46.661 53.171  0.822   1.00 5.72  ? 182  LEU A CG  1 
ATOM   1294 C  CD1 . LEU A 1 182  ? 45.897 53.186  2.187   1.00 7.72  ? 182  LEU A CD1 1 
ATOM   1295 C  CD2 . LEU A 1 182  ? 46.072 52.065  -0.137  1.00 7.14  ? 182  LEU A CD2 1 
ATOM   1296 N  N   . THR A 1 183  ? 49.537 55.493  0.060   1.00 6.25  ? 183  THR A N   1 
ATOM   1297 C  CA  . THR A 1 183  ? 50.956 55.135  0.133   1.00 7.12  ? 183  THR A CA  1 
ATOM   1298 C  C   . THR A 1 183  ? 51.688 56.084  1.061   1.00 8.05  ? 183  THR A C   1 
ATOM   1299 O  O   . THR A 1 183  ? 52.614 55.678  1.797   1.00 7.80  ? 183  THR A O   1 
ATOM   1300 C  CB  . THR A 1 183  ? 51.575 55.232  -1.276  1.00 5.82  ? 183  THR A CB  1 
ATOM   1301 O  OG1 . THR A 1 183  ? 50.900 54.337  -2.156  1.00 6.78  ? 183  THR A OG1 1 
ATOM   1302 C  CG2 . THR A 1 183  ? 53.064 54.868  -1.224  1.00 8.83  ? 183  THR A CG2 1 
ATOM   1303 N  N   . GLU A 1 184  ? 51.323 57.357  1.050   1.00 5.67  ? 184  GLU A N   1 
ATOM   1304 C  CA  . GLU A 1 184  ? 52.001 58.311  1.920   1.00 7.07  ? 184  GLU A CA  1 
ATOM   1305 C  C   . GLU A 1 184  ? 51.798 57.938  3.381   1.00 6.63  ? 184  GLU A C   1 
ATOM   1306 O  O   . GLU A 1 184  ? 52.753 57.897  4.203   1.00 9.53  ? 184  GLU A O   1 
ATOM   1307 C  CB  . GLU A 1 184  ? 51.456 59.732  1.688   1.00 7.27  ? 184  GLU A CB  1 
ATOM   1308 C  CG  . GLU A 1 184  ? 52.321 60.891  2.129   1.00 9.91  ? 184  GLU A CG  1 
ATOM   1309 C  CD  . GLU A 1 184  ? 53.710 60.909  1.562   1.00 7.69  ? 184  GLU A CD  1 
ATOM   1310 O  OE1 . GLU A 1 184  ? 53.914 60.493  0.424   1.00 11.41 ? 184  GLU A OE1 1 
ATOM   1311 O  OE2 . GLU A 1 184  ? 54.605 61.411  2.304   1.00 13.81 ? 184  GLU A OE2 1 
ATOM   1312 N  N   . GLY A 1 185  ? 50.574 57.618  3.775   1.00 6.83  ? 185  GLY A N   1 
ATOM   1313 C  CA  . GLY A 1 185  ? 50.380 57.271  5.179   1.00 6.24  ? 185  GLY A CA  1 
ATOM   1314 C  C   . GLY A 1 185  ? 50.915 55.910  5.528   1.00 6.79  ? 185  GLY A C   1 
ATOM   1315 O  O   . GLY A 1 185  ? 51.517 55.745  6.575   1.00 7.32  ? 185  GLY A O   1 
ATOM   1316 N  N   . GLN A 1 186  ? 50.784 54.954  4.636   1.00 7.47  ? 186  GLN A N   1 
ATOM   1317 C  CA  . GLN A 1 186  ? 51.257 53.606  4.974   1.00 7.01  ? 186  GLN A CA  1 
ATOM   1318 C  C   . GLN A 1 186  ? 52.783 53.548  5.009   1.00 7.41  ? 186  GLN A C   1 
ATOM   1319 O  O   . GLN A 1 186  ? 53.353 52.806  5.805   1.00 8.26  ? 186  GLN A O   1 
ATOM   1320 C  CB  . GLN A 1 186  ? 50.653 52.527  4.017   1.00 7.02  ? 186  GLN A CB  1 
ATOM   1321 C  CG  . GLN A 1 186  ? 49.106 52.353  4.252   1.00 7.55  ? 186  GLN A CG  1 
ATOM   1322 C  CD  . GLN A 1 186  ? 48.737 50.923  4.050   1.00 8.27  ? 186  GLN A CD  1 
ATOM   1323 O  OE1 . GLN A 1 186  ? 49.411 50.237  3.288   1.00 9.82  ? 186  GLN A OE1 1 
ATOM   1324 N  NE2 . GLN A 1 186  ? 47.678 50.458  4.687   1.00 7.80  ? 186  GLN A NE2 1 
ATOM   1325 N  N   . THR A 1 187  ? 53.471 54.280  4.133   1.00 8.14  ? 187  THR A N   1 
ATOM   1326 C  CA  . THR A 1 187  ? 54.945 54.288  4.153   1.00 8.35  ? 187  THR A CA  1 
ATOM   1327 C  C   . THR A 1 187  ? 55.406 54.899  5.477   1.00 8.82  ? 187  THR A C   1 
ATOM   1328 O  O   . THR A 1 187  ? 56.410 54.390  6.065   1.00 9.91  ? 187  THR A O   1 
ATOM   1329 C  CB  . THR A 1 187  ? 55.460 55.074  2.951   1.00 7.05  ? 187  THR A CB  1 
ATOM   1330 O  OG1 . THR A 1 187  ? 54.935 54.464  1.755   1.00 9.80  ? 187  THR A OG1 1 
ATOM   1331 C  CG2 . THR A 1 187  ? 57.031 55.037  2.896   1.00 9.06  ? 187  THR A CG2 1 
ATOM   1332 N  N   . TRP A 1 188  ? 54.707 55.937  5.966   1.00 8.47  ? 188  TRP A N   1 
ATOM   1333 C  CA  . TRP A 1 188  ? 55.060 56.551  7.241   1.00 9.26  ? 188  TRP A CA  1 
ATOM   1334 C  C   . TRP A 1 188  ? 54.838 55.494  8.333   1.00 8.58  ? 188  TRP A C   1 
ATOM   1335 O  O   . TRP A 1 188  ? 55.721 55.245  9.161   1.00 9.08  ? 188  TRP A O   1 
ATOM   1336 C  CB  . TRP A 1 188  ? 54.160 57.750  7.484   1.00 8.52  ? 188  TRP A CB  1 
ATOM   1337 C  CG  . TRP A 1 188  ? 54.626 58.553  8.757   1.00 10.48 ? 188  TRP A CG  1 
ATOM   1338 C  CD1 . TRP A 1 188  ? 55.560 59.583  8.766   1.00 11.70 ? 188  TRP A CD1 1 
ATOM   1339 C  CD2 . TRP A 1 188  ? 54.312 58.273  10.127  1.00 9.68  ? 188  TRP A CD2 1 
ATOM   1340 N  NE1 . TRP A 1 188  ? 55.833 59.936  10.069  1.00 9.91  ? 188  TRP A NE1 1 
ATOM   1341 C  CE2 . TRP A 1 188  ? 55.093 59.143  10.922  1.00 12.32 ? 188  TRP A CE2 1 
ATOM   1342 C  CE3 . TRP A 1 188  ? 53.455 57.352  10.758  1.00 11.79 ? 188  TRP A CE3 1 
ATOM   1343 C  CZ2 . TRP A 1 188  ? 55.041 59.125  12.322  1.00 10.96 ? 188  TRP A CZ2 1 
ATOM   1344 C  CZ3 . TRP A 1 188  ? 53.406 57.320  12.162  1.00 11.28 ? 188  TRP A CZ3 1 
ATOM   1345 C  CH2 . TRP A 1 188  ? 54.200 58.212  12.932  1.00 13.79 ? 188  TRP A CH2 1 
ATOM   1346 N  N   . LEU A 1 189  ? 53.720 54.795  8.287   1.00 9.92  ? 189  LEU A N   1 
ATOM   1347 C  CA  . LEU A 1 189  ? 53.447 53.799  9.308   1.00 9.25  ? 189  LEU A CA  1 
ATOM   1348 C  C   . LEU A 1 189  ? 54.470 52.672  9.352   1.00 10.08 ? 189  LEU A C   1 
ATOM   1349 O  O   . LEU A 1 189  ? 54.865 52.260  10.446  1.00 11.35 ? 189  LEU A O   1 
ATOM   1350 C  CB  . LEU A 1 189  ? 51.997 53.187  9.196   1.00 8.61  ? 189  LEU A CB  1 
ATOM   1351 C  CG  . LEU A 1 189  ? 50.847 54.075  9.649   1.00 8.00  ? 189  LEU A CG  1 
ATOM   1352 C  CD1 . LEU A 1 189  ? 49.504 53.307  9.325   1.00 9.88  ? 189  LEU A CD1 1 
ATOM   1353 C  CD2 . LEU A 1 189  ? 50.945 54.285  11.176  1.00 6.91  ? 189  LEU A CD2 1 
ATOM   1354 N  N   . LYS A 1 190  ? 54.879 52.139  8.199   1.00 11.46 ? 190  LYS A N   1 
ATOM   1355 C  CA  . LYS A 1 190  ? 55.848 51.049  8.173   1.00 10.20 ? 190  LYS A CA  1 
ATOM   1356 C  C   . LYS A 1 190  ? 57.167 51.550  8.741   1.00 12.11 ? 190  LYS A C   1 
ATOM   1357 O  O   . LYS A 1 190  ? 57.771 50.872  9.616   1.00 13.44 ? 190  LYS A O   1 
ATOM   1358 C  CB  . LYS A 1 190  ? 56.005 50.512  6.740   1.00 12.98 ? 190  LYS A CB  1 
ATOM   1359 C  CG  . LYS A 1 190  ? 57.001 49.298  6.691   1.00 15.12 ? 190  LYS A CG  1 
ATOM   1360 C  CD  . LYS A 1 190  ? 57.110 48.683  5.317   1.00 21.72 ? 190  LYS A CD  1 
ATOM   1361 C  CE  . LYS A 1 190  ? 57.929 47.370  5.343   1.00 24.10 ? 190  LYS A CE  1 
ATOM   1362 N  NZ  . LYS A 1 190  ? 58.361 46.950  3.947   1.00 26.28 ? 190  LYS A NZ  1 
ATOM   1363 N  N   . GLN A 1 191  ? 57.589 52.743  8.353   1.00 10.76 ? 191  GLN A N   1 
ATOM   1364 C  CA  . GLN A 1 191  ? 58.881 53.243  8.813   1.00 14.65 ? 191  GLN A CA  1 
ATOM   1365 C  C   . GLN A 1 191  ? 58.943 53.487  10.302  1.00 15.24 ? 191  GLN A C   1 
ATOM   1366 O  O   . GLN A 1 191  ? 59.917 53.061  11.001  1.00 16.87 ? 191  GLN A O   1 
ATOM   1367 C  CB  . GLN A 1 191  ? 59.178 54.548  8.044   1.00 17.94 ? 191  GLN A CB  1 
ATOM   1368 C  CG  . GLN A 1 191  ? 60.621 55.037  8.062   1.00 24.07 ? 191  GLN A CG  1 
ATOM   1369 C  CD  . GLN A 1 191  ? 60.789 56.346  7.260   1.00 26.44 ? 191  GLN A CD  1 
ATOM   1370 O  OE1 . GLN A 1 191  ? 59.941 56.706  6.400   1.00 30.41 ? 191  GLN A OE1 1 
ATOM   1371 N  NE2 . GLN A 1 191  ? 61.889 57.054  7.517   1.00 29.58 ? 191  GLN A NE2 1 
ATOM   1372 N  N   . PHE A 1 192  ? 57.943 54.174  10.819  1.00 14.37 ? 192  PHE A N   1 
ATOM   1373 C  CA  . PHE A 1 192  ? 57.932 54.567  12.225  1.00 13.61 ? 192  PHE A CA  1 
ATOM   1374 C  C   . PHE A 1 192  ? 57.194 53.735  13.265  1.00 14.41 ? 192  PHE A C   1 
ATOM   1375 O  O   . PHE A 1 192  ? 57.568 53.750  14.446  1.00 15.47 ? 192  PHE A O   1 
ATOM   1376 C  CB  . PHE A 1 192  ? 57.465 56.031  12.342  1.00 14.58 ? 192  PHE A CB  1 
ATOM   1377 C  CG  . PHE A 1 192  ? 58.379 56.985  11.644  1.00 12.47 ? 192  PHE A CG  1 
ATOM   1378 C  CD1 . PHE A 1 192  ? 59.624 57.256  12.192  1.00 14.13 ? 192  PHE A CD1 1 
ATOM   1379 C  CD2 . PHE A 1 192  ? 58.055 57.546  10.386  1.00 13.14 ? 192  PHE A CD2 1 
ATOM   1380 C  CE1 . PHE A 1 192  ? 60.534 58.051  11.528  1.00 14.41 ? 192  PHE A CE1 1 
ATOM   1381 C  CE2 . PHE A 1 192  ? 58.982 58.368  9.691   1.00 13.08 ? 192  PHE A CE2 1 
ATOM   1382 C  CZ  . PHE A 1 192  ? 60.238 58.609  10.294  1.00 15.28 ? 192  PHE A CZ  1 
ATOM   1383 N  N   . MET A 1 193  ? 56.164 52.997  12.850  1.00 11.76 ? 193  MET A N   1 
ATOM   1384 C  CA  . MET A 1 193  ? 55.352 52.184  13.774  1.00 11.60 ? 193  MET A CA  1 
ATOM   1385 C  C   . MET A 1 193  ? 55.475 50.698  13.466  1.00 11.31 ? 193  MET A C   1 
ATOM   1386 O  O   . MET A 1 193  ? 54.970 49.844  14.216  1.00 12.61 ? 193  MET A O   1 
ATOM   1387 C  CB  . MET A 1 193  ? 53.873 52.564  13.655  1.00 10.57 ? 193  MET A CB  1 
ATOM   1388 C  CG  A MET A 1 193  ? 53.460 53.913  14.291  0.50 10.16 ? 193  MET A CG  1 
ATOM   1389 C  CG  B MET A 1 193  ? 53.753 54.184  13.796  0.50 13.94 ? 193  MET A CG  1 
ATOM   1390 S  SD  A MET A 1 193  ? 53.576 53.922  16.126  0.50 11.06 ? 193  MET A SD  1 
ATOM   1391 S  SD  B MET A 1 193  ? 54.707 54.901  15.130  0.50 17.43 ? 193  MET A SD  1 
ATOM   1392 C  CE  A MET A 1 193  ? 55.017 54.934  16.405  0.50 13.27 ? 193  MET A CE  1 
ATOM   1393 C  CE  B MET A 1 193  ? 53.811 54.070  16.435  0.50 13.70 ? 193  MET A CE  1 
ATOM   1394 N  N   . ASN A 1 194  ? 56.156 50.369  12.374  1.00 11.09 ? 194  ASN A N   1 
ATOM   1395 C  CA  . ASN A 1 194  ? 56.321 48.977  11.958  1.00 12.84 ? 194  ASN A CA  1 
ATOM   1396 C  C   . ASN A 1 194  ? 55.013 48.182  11.833  1.00 12.75 ? 194  ASN A C   1 
ATOM   1397 O  O   . ASN A 1 194  ? 54.919 47.012  12.250  1.00 13.93 ? 194  ASN A O   1 
ATOM   1398 C  CB  . ASN A 1 194  ? 57.284 48.266  12.911  1.00 15.90 ? 194  ASN A CB  1 
ATOM   1399 C  CG  . ASN A 1 194  ? 57.771 46.937  12.369  1.00 20.68 ? 194  ASN A CG  1 
ATOM   1400 O  OD1 . ASN A 1 194  ? 57.892 46.759  11.149  1.00 20.03 ? 194  ASN A OD1 1 
ATOM   1401 N  ND2 . ASN A 1 194  ? 58.066 46.034  13.295  1.00 26.96 ? 194  ASN A ND2 1 
ATOM   1402 N  N   . VAL A 1 195  ? 53.991 48.811  11.255  1.00 11.06 ? 195  VAL A N   1 
ATOM   1403 C  CA  . VAL A 1 195  ? 52.711 48.125  11.024  1.00 11.65 ? 195  VAL A CA  1 
ATOM   1404 C  C   . VAL A 1 195  ? 52.172 48.562  9.658   1.00 10.17 ? 195  VAL A C   1 
ATOM   1405 O  O   . VAL A 1 195  ? 52.428 49.697  9.222   1.00 9.31  ? 195  VAL A O   1 
ATOM   1406 C  CB  . VAL A 1 195  ? 51.570 48.454  12.114  1.00 11.09 ? 195  VAL A CB  1 
ATOM   1407 C  CG1 . VAL A 1 195  ? 52.010 48.039  13.536  1.00 15.24 ? 195  VAL A CG1 1 
ATOM   1408 C  CG2 . VAL A 1 195  ? 51.251 49.915  12.129  1.00 12.24 ? 195  VAL A CG2 1 
ATOM   1409 N  N   . THR A 1 196  ? 51.386 47.687  9.057   1.00 8.79  ? 196  THR A N   1 
ATOM   1410 C  CA  . THR A 1 196  ? 50.689 47.960  7.790   1.00 10.01 ? 196  THR A CA  1 
ATOM   1411 C  C   . THR A 1 196  ? 49.226 47.478  7.959   1.00 8.73  ? 196  THR A C   1 
ATOM   1412 O  O   . THR A 1 196  ? 48.985 46.247  7.994   1.00 9.81  ? 196  THR A O   1 
ATOM   1413 C  CB  . THR A 1 196  ? 51.316 47.214  6.553   1.00 8.57  ? 196  THR A CB  1 
ATOM   1414 O  OG1 . THR A 1 196  ? 52.680 47.613  6.392   1.00 12.23 ? 196  THR A OG1 1 
ATOM   1415 C  CG2 . THR A 1 196  ? 50.527 47.506  5.318   1.00 11.57 ? 196  THR A CG2 1 
ATOM   1416 N  N   . PRO A 1 197  ? 48.242 48.410  8.082   1.00 8.76  ? 197  PRO A N   1 
ATOM   1417 C  CA  . PRO A 1 197  ? 46.820 48.033  8.226   1.00 7.82  ? 197  PRO A CA  1 
ATOM   1418 C  C   . PRO A 1 197  ? 46.328 47.187  7.105   1.00 7.84  ? 197  PRO A C   1 
ATOM   1419 O  O   . PRO A 1 197  ? 46.660 47.442  5.934   1.00 8.86  ? 197  PRO A O   1 
ATOM   1420 C  CB  . PRO A 1 197  ? 46.088 49.381  8.224   1.00 8.35  ? 197  PRO A CB  1 
ATOM   1421 C  CG  . PRO A 1 197  ? 47.096 50.375  8.818   1.00 7.31  ? 197  PRO A CG  1 
ATOM   1422 C  CD  . PRO A 1 197  ? 48.421 49.877  8.221   1.00 7.16  ? 197  PRO A CD  1 
ATOM   1423 N  N   . THR A 1 198  ? 45.474 46.197  7.446   1.00 7.25  ? 198  THR A N   1 
ATOM   1424 C  CA  . THR A 1 198  ? 44.868 45.346  6.453   1.00 6.37  ? 198  THR A CA  1 
ATOM   1425 C  C   . THR A 1 198  ? 43.317 45.485  6.528   1.00 6.58  ? 198  THR A C   1 
ATOM   1426 O  O   . THR A 1 198  ? 42.592 44.798  5.804   1.00 6.68  ? 198  THR A O   1 
ATOM   1427 C  CB  . THR A 1 198  ? 45.236 43.891  6.625   1.00 9.30  ? 198  THR A CB  1 
ATOM   1428 O  OG1 . THR A 1 198  ? 44.735 43.467  7.866   1.00 9.87  ? 198  THR A OG1 1 
ATOM   1429 C  CG2 . THR A 1 198  ? 46.761 43.681  6.533   1.00 9.65  ? 198  THR A CG2 1 
ATOM   1430 N  N   . ALA A 1 199  ? 42.827 46.356  7.426   1.00 7.67  ? 199  ALA A N   1 
ATOM   1431 C  CA  . ALA A 1 199  ? 41.396 46.670  7.548   1.00 6.79  ? 199  ALA A CA  1 
ATOM   1432 C  C   . ALA A 1 199  ? 41.191 48.183  7.299   1.00 7.28  ? 199  ALA A C   1 
ATOM   1433 O  O   . ALA A 1 199  ? 41.948 48.968  7.826   1.00 8.05  ? 199  ALA A O   1 
ATOM   1434 C  CB  . ALA A 1 199  ? 40.854 46.355  8.940   1.00 6.72  ? 199  ALA A CB  1 
ATOM   1435 N  N   . SER A 1 200  ? 40.205 48.540  6.497   1.00 6.42  ? 200  SER A N   1 
ATOM   1436 C  CA  . SER A 1 200  ? 39.926 49.953  6.176   1.00 6.42  ? 200  SER A CA  1 
ATOM   1437 C  C   . SER A 1 200  ? 38.667 50.431  6.870   1.00 7.31  ? 200  SER A C   1 
ATOM   1438 O  O   . SER A 1 200  ? 37.681 49.661  6.996   1.00 8.04  ? 200  SER A O   1 
ATOM   1439 C  CB  . SER A 1 200  ? 39.737 50.106  4.628   1.00 6.19  ? 200  SER A CB  1 
ATOM   1440 O  OG  . SER A 1 200  ? 39.632 51.478  4.231   1.00 10.12 ? 200  SER A OG  1 
ATOM   1441 N  N   . TRP A 1 201  ? 38.667 51.691  7.271   1.00 5.90  ? 201  TRP A N   1 
ATOM   1442 C  CA  . TRP A 1 201  ? 37.586 52.385  7.999   1.00 6.75  ? 201  TRP A CA  1 
ATOM   1443 C  C   . TRP A 1 201  ? 37.261 53.680  7.217   1.00 7.55  ? 201  TRP A C   1 
ATOM   1444 O  O   . TRP A 1 201  ? 38.081 54.554  7.188   1.00 7.93  ? 201  TRP A O   1 
ATOM   1445 C  CB  . TRP A 1 201  ? 38.110 52.655  9.437   1.00 7.13  ? 201  TRP A CB  1 
ATOM   1446 C  CG  . TRP A 1 201  ? 37.281 53.468  10.318  1.00 8.18  ? 201  TRP A CG  1 
ATOM   1447 C  CD1 . TRP A 1 201  ? 37.428 54.794  10.569  1.00 7.50  ? 201  TRP A CD1 1 
ATOM   1448 C  CD2 . TRP A 1 201  ? 36.305 52.984  11.260  1.00 8.57  ? 201  TRP A CD2 1 
ATOM   1449 N  NE1 . TRP A 1 201  ? 36.627 55.171  11.647  1.00 8.71  ? 201  TRP A NE1 1 
ATOM   1450 C  CE2 . TRP A 1 201  ? 35.925 54.087  12.078  1.00 8.21  ? 201  TRP A CE2 1 
ATOM   1451 C  CE3 . TRP A 1 201  ? 35.714 51.731  11.505  1.00 8.24  ? 201  TRP A CE3 1 
ATOM   1452 C  CZ2 . TRP A 1 201  ? 34.987 53.967  13.136  1.00 8.96  ? 201  TRP A CZ2 1 
ATOM   1453 C  CZ3 . TRP A 1 201  ? 34.803 51.610  12.547  1.00 8.47  ? 201  TRP A CZ3 1 
ATOM   1454 C  CH2 . TRP A 1 201  ? 34.438 52.703  13.360  1.00 8.82  ? 201  TRP A CH2 1 
ATOM   1455 N  N   . ALA A 1 202  ? 36.093 53.724  6.574   1.00 7.32  ? 202  ALA A N   1 
ATOM   1456 C  CA  . ALA A 1 202  ? 35.665 54.920  5.806   1.00 7.64  ? 202  ALA A CA  1 
ATOM   1457 C  C   . ALA A 1 202  ? 34.239 55.245  6.281   1.00 8.45  ? 202  ALA A C   1 
ATOM   1458 O  O   . ALA A 1 202  ? 33.229 54.851  5.625   1.00 7.54  ? 202  ALA A O   1 
ATOM   1459 C  CB  . ALA A 1 202  ? 35.735 54.599  4.281   1.00 8.34  ? 202  ALA A CB  1 
ATOM   1460 N  N   . ILE A 1 203  ? 34.113 55.989  7.370   1.00 6.70  ? 203  ILE A N   1 
ATOM   1461 C  CA  . ILE A 1 203  ? 32.800 56.297  7.950   1.00 5.61  ? 203  ILE A CA  1 
ATOM   1462 C  C   . ILE A 1 203  ? 32.163 57.637  7.496   1.00 7.78  ? 203  ILE A C   1 
ATOM   1463 O  O   . ILE A 1 203  ? 30.969 57.813  7.720   1.00 6.76  ? 203  ILE A O   1 
ATOM   1464 C  CB  . ILE A 1 203  ? 32.874 56.392  9.480   1.00 6.75  ? 203  ILE A CB  1 
ATOM   1465 C  CG1 . ILE A 1 203  ? 34.032 57.296  9.957   1.00 8.31  ? 203  ILE A CG1 1 
ATOM   1466 C  CG2 . ILE A 1 203  ? 33.139 54.997  10.079  1.00 7.96  ? 203  ILE A CG2 1 
ATOM   1467 C  CD1 . ILE A 1 203  ? 33.949 57.516  11.523  1.00 6.35  ? 203  ILE A CD1 1 
ATOM   1468 N  N   . ASP A 1 204  ? 32.933 58.534  6.861   1.00 7.34  ? 204  ASP A N   1 
ATOM   1469 C  CA  . ASP A 1 204  ? 32.384 59.829  6.483   1.00 7.85  ? 204  ASP A CA  1 
ATOM   1470 C  C   . ASP A 1 204  ? 32.327 60.245  4.993   1.00 7.52  ? 204  ASP A C   1 
ATOM   1471 O  O   . ASP A 1 204  ? 31.575 61.188  4.679   1.00 9.08  ? 204  ASP A O   1 
ATOM   1472 C  CB  . ASP A 1 204  ? 33.060 60.954  7.325   1.00 7.43  ? 204  ASP A CB  1 
ATOM   1473 C  CG  . ASP A 1 204  ? 32.126 62.130  7.657   1.00 7.14  ? 204  ASP A CG  1 
ATOM   1474 O  OD1 . ASP A 1 204  ? 30.870 61.941  7.660   1.00 7.19  ? 204  ASP A OD1 1 
ATOM   1475 O  OD2 . ASP A 1 204  ? 32.680 63.244  8.006   1.00 6.89  ? 204  ASP A OD2 1 
ATOM   1476 N  N   . PRO A 1 205  ? 33.087 59.619  4.049   1.00 6.75  ? 205  PRO A N   1 
ATOM   1477 C  CA  . PRO A 1 205  ? 32.941 60.065  2.666   1.00 7.90  ? 205  PRO A CA  1 
ATOM   1478 C  C   . PRO A 1 205  ? 31.445 60.001  2.270   1.00 7.08  ? 205  PRO A C   1 
ATOM   1479 O  O   . PRO A 1 205  ? 30.694 59.092  2.698   1.00 8.03  ? 205  PRO A O   1 
ATOM   1480 C  CB  . PRO A 1 205  ? 33.808 59.095  1.910   1.00 5.81  ? 205  PRO A CB  1 
ATOM   1481 C  CG  . PRO A 1 205  ? 34.882 58.691  2.930   1.00 11.52 ? 205  PRO A CG  1 
ATOM   1482 C  CD  . PRO A 1 205  ? 34.091 58.550  4.160   1.00 9.68  ? 205  PRO A CD  1 
ATOM   1483 N  N   . PHE A 1 206  ? 31.018 60.896  1.395   1.00 7.99  ? 206  PHE A N   1 
ATOM   1484 C  CA  . PHE A 1 206  ? 29.556 61.033  1.075   1.00 5.74  ? 206  PHE A CA  1 
ATOM   1485 C  C   . PHE A 1 206  ? 29.131 60.175  -0.090  1.00 7.85  ? 206  PHE A C   1 
ATOM   1486 O  O   . PHE A 1 206  ? 28.916 60.645  -1.196  1.00 7.39  ? 206  PHE A O   1 
ATOM   1487 C  CB  . PHE A 1 206  ? 29.238 62.541  0.793   1.00 6.83  ? 206  PHE A CB  1 
ATOM   1488 C  CG  . PHE A 1 206  ? 30.070 63.528  1.635   1.00 6.65  ? 206  PHE A CG  1 
ATOM   1489 C  CD1 . PHE A 1 206  ? 30.255 63.321  2.994   1.00 4.87  ? 206  PHE A CD1 1 
ATOM   1490 C  CD2 . PHE A 1 206  ? 30.664 64.652  1.028   1.00 5.40  ? 206  PHE A CD2 1 
ATOM   1491 C  CE1 . PHE A 1 206  ? 31.027 64.164  3.786   1.00 7.27  ? 206  PHE A CE1 1 
ATOM   1492 C  CE2 . PHE A 1 206  ? 31.455 65.523  1.830   1.00 6.60  ? 206  PHE A CE2 1 
ATOM   1493 C  CZ  . PHE A 1 206  ? 31.646 65.271  3.199   1.00 4.08  ? 206  PHE A CZ  1 
ATOM   1494 N  N   . GLY A 1 207  ? 29.023 58.874  0.167   1.00 6.81  ? 207  GLY A N   1 
ATOM   1495 C  CA  . GLY A 1 207  ? 28.786 57.887  -0.889  1.00 6.71  ? 207  GLY A CA  1 
ATOM   1496 C  C   . GLY A 1 207  ? 30.139 57.167  -1.031  1.00 5.27  ? 207  GLY A C   1 
ATOM   1497 O  O   . GLY A 1 207  ? 31.222 57.682  -0.666  1.00 8.86  ? 207  GLY A O   1 
ATOM   1498 N  N   . HIS A 1 208  ? 30.092 55.980  -1.601  1.00 5.69  ? 208  HIS A N   1 
ATOM   1499 C  CA  . HIS A 1 208  ? 31.272 55.105  -1.707  1.00 5.37  ? 208  HIS A CA  1 
ATOM   1500 C  C   . HIS A 1 208  ? 31.472 54.499  -3.061  1.00 6.35  ? 208  HIS A C   1 
ATOM   1501 O  O   . HIS A 1 208  ? 30.525 54.097  -3.747  1.00 7.03  ? 208  HIS A O   1 
ATOM   1502 C  CB  . HIS A 1 208  ? 31.165 53.967  -0.626  1.00 6.45  ? 208  HIS A CB  1 
ATOM   1503 C  CG  . HIS A 1 208  ? 31.201 54.441  0.793   1.00 5.34  ? 208  HIS A CG  1 
ATOM   1504 N  ND1 . HIS A 1 208  ? 32.391 54.731  1.436   1.00 7.42  ? 208  HIS A ND1 1 
ATOM   1505 C  CD2 . HIS A 1 208  ? 30.216 54.723  1.676   1.00 8.24  ? 208  HIS A CD2 1 
ATOM   1506 C  CE1 . HIS A 1 208  ? 32.124 55.147  2.660   1.00 6.13  ? 208  HIS A CE1 1 
ATOM   1507 N  NE2 . HIS A 1 208  ? 30.821 55.159  2.835   1.00 5.65  ? 208  HIS A NE2 1 
ATOM   1508 N  N   . SER A 1 209  ? 32.758 54.372  -3.402  1.00 4.75  ? 209  SER A N   1 
ATOM   1509 C  CA  . SER A 1 209  ? 33.193 53.852  -4.697  1.00 7.08  ? 209  SER A CA  1 
ATOM   1510 C  C   . SER A 1 209  ? 33.901 52.520  -4.659  1.00 5.11  ? 209  SER A C   1 
ATOM   1511 O  O   . SER A 1 209  ? 34.668 52.273  -3.761  1.00 6.05  ? 209  SER A O   1 
ATOM   1512 C  CB  . SER A 1 209  ? 34.222 54.804  -5.328  1.00 6.80  ? 209  SER A CB  1 
ATOM   1513 O  OG  . SER A 1 209  ? 34.675 54.357  -6.598  1.00 7.25  ? 209  SER A OG  1 
ATOM   1514 N  N   . PRO A 1 210  ? 33.646 51.659  -5.652  1.00 5.93  ? 210  PRO A N   1 
ATOM   1515 C  CA  . PRO A 1 210  ? 34.341 50.352  -5.703  1.00 5.86  ? 210  PRO A CA  1 
ATOM   1516 C  C   . PRO A 1 210  ? 35.834 50.539  -6.075  1.00 7.04  ? 210  PRO A C   1 
ATOM   1517 O  O   . PRO A 1 210  ? 36.645 49.572  -6.034  1.00 7.12  ? 210  PRO A O   1 
ATOM   1518 C  CB  . PRO A 1 210  ? 33.618 49.568  -6.812  1.00 6.92  ? 210  PRO A CB  1 
ATOM   1519 C  CG  . PRO A 1 210  ? 33.036 50.652  -7.640  1.00 7.67  ? 210  PRO A CG  1 
ATOM   1520 C  CD  . PRO A 1 210  ? 32.690 51.783  -6.767  1.00 6.65  ? 210  PRO A CD  1 
ATOM   1521 N  N   . THR A 1 211  ? 36.243 51.785  -6.380  1.00 6.17  ? 211  THR A N   1 
ATOM   1522 C  CA  . THR A 1 211  ? 37.678 51.995  -6.619  1.00 8.37  ? 211  THR A CA  1 
ATOM   1523 C  C   . THR A 1 211  ? 38.436 51.749  -5.320  1.00 7.38  ? 211  THR A C   1 
ATOM   1524 O  O   . THR A 1 211  ? 39.580 51.331  -5.370  1.00 7.16  ? 211  THR A O   1 
ATOM   1525 C  CB  . THR A 1 211  ? 37.917 53.433  -7.062  1.00 5.97  ? 211  THR A CB  1 
ATOM   1526 O  OG1 . THR A 1 211  ? 37.360 53.536  -8.376  1.00 7.63  ? 211  THR A OG1 1 
ATOM   1527 C  CG2 . THR A 1 211  ? 39.403 53.767  -7.053  1.00 8.50  ? 211  THR A CG2 1 
ATOM   1528 N  N   . MET A 1 212  ? 37.779 51.907  -4.168  1.00 6.33  ? 212  MET A N   1 
ATOM   1529 C  CA  . MET A 1 212  ? 38.481 51.677  -2.913  1.00 7.36  ? 212  MET A CA  1 
ATOM   1530 C  C   . MET A 1 212  ? 38.816 50.183  -2.721  1.00 5.95  ? 212  MET A C   1 
ATOM   1531 O  O   . MET A 1 212  ? 39.975 49.865  -2.516  1.00 7.82  ? 212  MET A O   1 
ATOM   1532 C  CB  . MET A 1 212  ? 37.676 52.265  -1.749  1.00 6.48  ? 212  MET A CB  1 
ATOM   1533 C  CG  . MET A 1 212  ? 37.364 53.738  -1.874  1.00 8.54  ? 212  MET A CG  1 
ATOM   1534 S  SD  . MET A 1 212  ? 38.839 54.752  -2.086  1.00 12.33 ? 212  MET A SD  1 
ATOM   1535 C  CE  . MET A 1 212  ? 39.532 54.880  -0.473  1.00 12.97 ? 212  MET A CE  1 
ATOM   1536 N  N   . PRO A 1 213  ? 37.858 49.237  -2.796  1.00 6.83  ? 213  PRO A N   1 
ATOM   1537 C  CA  . PRO A 1 213  ? 38.281 47.838  -2.635  1.00 5.79  ? 213  PRO A CA  1 
ATOM   1538 C  C   . PRO A 1 213  ? 39.252 47.434  -3.726  1.00 6.74  ? 213  PRO A C   1 
ATOM   1539 O  O   . PRO A 1 213  ? 40.107 46.569  -3.460  1.00 8.02  ? 213  PRO A O   1 
ATOM   1540 C  CB  . PRO A 1 213  ? 36.964 47.043  -2.619  1.00 5.16  ? 213  PRO A CB  1 
ATOM   1541 C  CG  . PRO A 1 213  ? 35.916 47.971  -3.279  1.00 6.09  ? 213  PRO A CG  1 
ATOM   1542 C  CD  . PRO A 1 213  ? 36.381 49.343  -2.787  1.00 7.21  ? 213  PRO A CD  1 
ATOM   1543 N  N   . TYR A 1 214  ? 39.161 48.035  -4.922  1.00 7.59  ? 214  TYR A N   1 
ATOM   1544 C  CA  . TYR A 1 214  ? 40.090 47.711  -6.003  1.00 6.38  ? 214  TYR A CA  1 
ATOM   1545 C  C   . TYR A 1 214  ? 41.518 48.021  -5.531  1.00 8.51  ? 214  TYR A C   1 
ATOM   1546 O  O   . TYR A 1 214  ? 42.369 47.151  -5.603  1.00 7.43  ? 214  TYR A O   1 
ATOM   1547 C  CB  . TYR A 1 214  ? 39.750 48.551  -7.267  1.00 7.09  ? 214  TYR A CB  1 
ATOM   1548 C  CG  . TYR A 1 214  ? 40.731 48.307  -8.440  1.00 10.09 ? 214  TYR A CG  1 
ATOM   1549 C  CD1 . TYR A 1 214  ? 40.517 47.242  -9.323  1.00 11.45 ? 214  TYR A CD1 1 
ATOM   1550 C  CD2 . TYR A 1 214  ? 41.824 49.159  -8.658  1.00 9.80  ? 214  TYR A CD2 1 
ATOM   1551 C  CE1 . TYR A 1 214  ? 41.374 47.042  -10.411 1.00 12.86 ? 214  TYR A CE1 1 
ATOM   1552 C  CE2 . TYR A 1 214  ? 42.663 48.938  -9.765  1.00 9.63  ? 214  TYR A CE2 1 
ATOM   1553 C  CZ  . TYR A 1 214  ? 42.422 47.906  -10.608 1.00 11.91 ? 214  TYR A CZ  1 
ATOM   1554 O  OH  . TYR A 1 214  ? 43.205 47.833  -11.766 1.00 13.27 ? 214  TYR A OH  1 
ATOM   1555 N  N   . ILE A 1 215  ? 41.759 49.254  -5.088  1.00 6.04  ? 215  ILE A N   1 
ATOM   1556 C  CA  . ILE A 1 215  ? 43.070 49.652  -4.593  1.00 6.47  ? 215  ILE A CA  1 
ATOM   1557 C  C   . ILE A 1 215  ? 43.473 48.927  -3.300  1.00 6.16  ? 215  ILE A C   1 
ATOM   1558 O  O   . ILE A 1 215  ? 44.627 48.436  -3.193  1.00 7.22  ? 215  ILE A O   1 
ATOM   1559 C  CB  . ILE A 1 215  ? 43.135 51.156  -4.378  1.00 4.77  ? 215  ILE A CB  1 
ATOM   1560 C  CG1 . ILE A 1 215  ? 42.907 51.888  -5.727  1.00 6.40  ? 215  ILE A CG1 1 
ATOM   1561 C  CG2 . ILE A 1 215  ? 44.498 51.533  -3.691  1.00 7.56  ? 215  ILE A CG2 1 
ATOM   1562 C  CD1 . ILE A 1 215  ? 42.875 53.376  -5.521  1.00 10.27 ? 215  ILE A CD1 1 
ATOM   1563 N  N   . LEU A 1 216  ? 42.557 48.757  -2.355  1.00 6.31  ? 216  LEU A N   1 
ATOM   1564 C  CA  . LEU A 1 216  ? 42.890 48.114  -1.095  1.00 6.43  ? 216  LEU A CA  1 
ATOM   1565 C  C   . LEU A 1 216  ? 43.268 46.642  -1.258  1.00 6.39  ? 216  LEU A C   1 
ATOM   1566 O  O   . LEU A 1 216  ? 44.246 46.209  -0.684  1.00 6.78  ? 216  LEU A O   1 
ATOM   1567 C  CB  . LEU A 1 216  ? 41.690 48.251  -0.119  1.00 6.90  ? 216  LEU A CB  1 
ATOM   1568 C  CG  . LEU A 1 216  ? 41.332 49.735  0.264   1.00 8.02  ? 216  LEU A CG  1 
ATOM   1569 C  CD1 . LEU A 1 216  ? 39.973 49.728  1.000   1.00 8.26  ? 216  LEU A CD1 1 
ATOM   1570 C  CD2 . LEU A 1 216  ? 42.425 50.439  1.173   1.00 10.60 ? 216  LEU A CD2 1 
ATOM   1571 N  N   . GLN A 1 217  ? 42.497 45.915  -2.055  1.00 6.74  ? 217  GLN A N   1 
ATOM   1572 C  CA  . GLN A 1 217  ? 42.762 44.498  -2.219  1.00 7.75  ? 217  GLN A CA  1 
ATOM   1573 C  C   . GLN A 1 217  ? 44.143 44.298  -2.910  1.00 7.29  ? 217  GLN A C   1 
ATOM   1574 O  O   . GLN A 1 217  ? 44.803 43.264  -2.696  1.00 10.41 ? 217  GLN A O   1 
ATOM   1575 C  CB  . GLN A 1 217  ? 41.608 43.879  -2.996  1.00 8.13  ? 217  GLN A CB  1 
ATOM   1576 C  CG  . GLN A 1 217  ? 41.635 42.345  -3.115  1.00 9.27  ? 217  GLN A CG  1 
ATOM   1577 C  CD  . GLN A 1 217  ? 42.512 41.836  -4.193  1.00 14.14 ? 217  GLN A CD  1 
ATOM   1578 O  OE1 . GLN A 1 217  ? 42.644 42.458  -5.247  1.00 13.93 ? 217  GLN A OE1 1 
ATOM   1579 N  NE2 . GLN A 1 217  ? 43.088 40.653  -3.968  1.00 14.54 ? 217  GLN A NE2 1 
ATOM   1580 N  N   . LYS A 1 218  ? 44.603 45.252  -3.704  1.00 7.84  ? 218  LYS A N   1 
ATOM   1581 C  CA  . LYS A 1 218  ? 45.927 45.157  -4.352  1.00 7.23  ? 218  LYS A CA  1 
ATOM   1582 C  C   . LYS A 1 218  ? 47.037 45.747  -3.488  1.00 8.25  ? 218  LYS A C   1 
ATOM   1583 O  O   . LYS A 1 218  ? 48.193 45.827  -3.922  1.00 7.77  ? 218  LYS A O   1 
ATOM   1584 C  CB  . LYS A 1 218  ? 45.868 45.874  -5.738  1.00 6.55  ? 218  LYS A CB  1 
ATOM   1585 C  CG  . LYS A 1 218  ? 45.051 45.096  -6.777  1.00 10.15 ? 218  LYS A CG  1 
ATOM   1586 C  CD  . LYS A 1 218  ? 44.753 45.955  -7.972  1.00 10.44 ? 218  LYS A CD  1 
ATOM   1587 C  CE  . LYS A 1 218  ? 44.328 45.198  -9.187  1.00 12.99 ? 218  LYS A CE  1 
ATOM   1588 N  NZ  . LYS A 1 218  ? 43.265 44.217  -8.908  1.00 15.98 ? 218  LYS A NZ  1 
ATOM   1589 N  N   . SER A 1 219  ? 46.692 46.203  -2.276  1.00 7.96  ? 219  SER A N   1 
ATOM   1590 C  CA  . SER A 1 219  ? 47.598 46.805  -1.296  1.00 8.48  ? 219  SER A CA  1 
ATOM   1591 C  C   . SER A 1 219  ? 47.620 45.992  0.029   1.00 6.73  ? 219  SER A C   1 
ATOM   1592 O  O   . SER A 1 219  ? 47.924 46.531  1.096   1.00 7.05  ? 219  SER A O   1 
ATOM   1593 C  CB  . SER A 1 219  ? 47.229 48.285  -1.042  1.00 9.17  ? 219  SER A CB  1 
ATOM   1594 O  OG  . SER A 1 219  ? 47.261 49.028  -2.279  1.00 9.58  ? 219  SER A OG  1 
ATOM   1595 N  N   . GLY A 1 220  ? 47.228 44.704  -0.061  1.00 7.70  ? 220  GLY A N   1 
ATOM   1596 C  CA  . GLY A 1 220  ? 47.305 43.854  1.123   1.00 7.42  ? 220  GLY A CA  1 
ATOM   1597 C  C   . GLY A 1 220  ? 46.086 43.799  2.019   1.00 9.78  ? 220  GLY A C   1 
ATOM   1598 O  O   . GLY A 1 220  ? 46.108 43.036  2.953   1.00 9.02  ? 220  GLY A O   1 
ATOM   1599 N  N   . PHE A 1 221  ? 45.014 44.508  1.693   1.00 8.01  ? 221  PHE A N   1 
ATOM   1600 C  CA  . PHE A 1 221  ? 43.897 44.533  2.604   1.00 8.49  ? 221  PHE A CA  1 
ATOM   1601 C  C   . PHE A 1 221  ? 43.067 43.299  2.548   1.00 8.37  ? 221  PHE A C   1 
ATOM   1602 O  O   . PHE A 1 221  ? 42.983 42.643  1.497   1.00 7.07  ? 221  PHE A O   1 
ATOM   1603 C  CB  . PHE A 1 221  ? 43.025 45.767  2.306   1.00 6.45  ? 221  PHE A CB  1 
ATOM   1604 C  CG  . PHE A 1 221  ? 43.576 47.013  2.888   1.00 7.45  ? 221  PHE A CG  1 
ATOM   1605 C  CD1 . PHE A 1 221  ? 44.690 47.649  2.314   1.00 5.75  ? 221  PHE A CD1 1 
ATOM   1606 C  CD2 . PHE A 1 221  ? 42.981 47.590  4.021   1.00 6.38  ? 221  PHE A CD2 1 
ATOM   1607 C  CE1 . PHE A 1 221  ? 45.185 48.854  2.883   1.00 7.29  ? 221  PHE A CE1 1 
ATOM   1608 C  CE2 . PHE A 1 221  ? 43.483 48.773  4.572   1.00 7.25  ? 221  PHE A CE2 1 
ATOM   1609 C  CZ  . PHE A 1 221  ? 44.582 49.416  4.015   1.00 5.84  ? 221  PHE A CZ  1 
ATOM   1610 N  N   . LYS A 1 222  ? 42.425 43.018  3.674   1.00 8.92  ? 222  LYS A N   1 
ATOM   1611 C  CA  . LYS A 1 222  ? 41.525 41.855  3.738   1.00 8.95  ? 222  LYS A CA  1 
ATOM   1612 C  C   . LYS A 1 222  ? 40.106 42.230  4.079   1.00 8.29  ? 222  LYS A C   1 
ATOM   1613 O  O   . LYS A 1 222  ? 39.190 41.461  3.872   1.00 7.52  ? 222  LYS A O   1 
ATOM   1614 C  CB  . LYS A 1 222  ? 42.051 40.829  4.751   1.00 12.96 ? 222  LYS A CB  1 
ATOM   1615 C  CG  . LYS A 1 222  ? 43.373 40.279  4.302   1.00 16.75 ? 222  LYS A CG  1 
ATOM   1616 C  CD  . LYS A 1 222  ? 44.054 39.377  5.276   1.00 24.02 ? 222  LYS A CD  1 
ATOM   1617 C  CE  . LYS A 1 222  ? 44.998 38.413  4.469   1.00 25.91 ? 222  LYS A CE  1 
ATOM   1618 N  NZ  . LYS A 1 222  ? 45.626 39.025  3.211   1.00 28.27 ? 222  LYS A NZ  1 
ATOM   1619 N  N   . ASN A 1 223  ? 39.889 43.458  4.576   1.00 6.44  ? 223  ASN A N   1 
ATOM   1620 C  CA  . ASN A 1 223  ? 38.564 43.883  5.007   1.00 6.90  ? 223  ASN A CA  1 
ATOM   1621 C  C   . ASN A 1 223  ? 38.424 45.373  4.941   1.00 7.03  ? 223  ASN A C   1 
ATOM   1622 O  O   . ASN A 1 223  ? 39.400 46.078  5.121   1.00 6.54  ? 223  ASN A O   1 
ATOM   1623 C  CB  . ASN A 1 223  ? 38.357 43.540  6.492   1.00 6.48  ? 223  ASN A CB  1 
ATOM   1624 C  CG  . ASN A 1 223  ? 38.409 42.021  6.758   1.00 8.21  ? 223  ASN A CG  1 
ATOM   1625 O  OD1 . ASN A 1 223  ? 39.475 41.494  7.206   1.00 11.44 ? 223  ASN A OD1 1 
ATOM   1626 N  ND2 . ASN A 1 223  ? 37.321 41.329  6.473   1.00 6.86  ? 223  ASN A ND2 1 
ATOM   1627 N  N   . MET A 1 224  ? 37.191 45.835  4.698   1.00 8.17  ? 224  MET A N   1 
ATOM   1628 C  CA  . MET A 1 224  ? 36.891 47.271  4.746   1.00 6.86  ? 224  MET A CA  1 
ATOM   1629 C  C   . MET A 1 224  ? 35.492 47.547  5.307   1.00 6.79  ? 224  MET A C   1 
ATOM   1630 O  O   . MET A 1 224  ? 34.609 46.676  5.273   1.00 7.65  ? 224  MET A O   1 
ATOM   1631 C  CB  . MET A 1 224  ? 37.020 47.896  3.358   1.00 8.27  ? 224  MET A CB  1 
ATOM   1632 C  CG  . MET A 1 224  ? 35.969 47.370  2.355   1.00 8.76  ? 224  MET A CG  1 
ATOM   1633 S  SD  . MET A 1 224  ? 36.154 48.114  0.676   1.00 9.06  ? 224  MET A SD  1 
ATOM   1634 C  CE  . MET A 1 224  ? 35.796 49.794  1.139   1.00 14.33 ? 224  MET A CE  1 
ATOM   1635 N  N   . LEU A 1 225  ? 35.313 48.782  5.774   1.00 5.86  ? 225  LEU A N   1 
ATOM   1636 C  CA  . LEU A 1 225  ? 34.026 49.216  6.376   1.00 6.11  ? 225  LEU A CA  1 
ATOM   1637 C  C   . LEU A 1 225  ? 33.613 50.542  5.758   1.00 7.23  ? 225  LEU A C   1 
ATOM   1638 O  O   . LEU A 1 225  ? 34.460 51.428  5.540   1.00 7.33  ? 225  LEU A O   1 
ATOM   1639 C  CB  . LEU A 1 225  ? 34.176 49.366  7.925   1.00 7.35  ? 225  LEU A CB  1 
ATOM   1640 C  CG  . LEU A 1 225  ? 32.929 49.951  8.628   1.00 8.46  ? 225  LEU A CG  1 
ATOM   1641 C  CD1 . LEU A 1 225  ? 32.899 49.467  10.095  1.00 8.36  ? 225  LEU A CD1 1 
ATOM   1642 C  CD2 . LEU A 1 225  ? 33.051 51.512  8.694   1.00 7.81  ? 225  LEU A CD2 1 
ATOM   1643 N  N   . ILE A 1 226  ? 32.314 50.655  5.456   1.00 6.09  ? 226  ILE A N   1 
ATOM   1644 C  CA  . ILE A 1 226  ? 31.703 51.864  4.910   1.00 6.65  ? 226  ILE A CA  1 
ATOM   1645 C  C   . ILE A 1 226  ? 30.458 52.204  5.689   1.00 8.08  ? 226  ILE A C   1 
ATOM   1646 O  O   . ILE A 1 226  ? 29.924 51.336  6.389   1.00 6.80  ? 226  ILE A O   1 
ATOM   1647 C  CB  . ILE A 1 226  ? 31.396 51.750  3.415   1.00 7.60  ? 226  ILE A CB  1 
ATOM   1648 C  CG1 . ILE A 1 226  ? 30.388 50.623  3.160   1.00 8.37  ? 226  ILE A CG1 1 
ATOM   1649 C  CG2 . ILE A 1 226  ? 32.701 51.378  2.705   1.00 8.08  ? 226  ILE A CG2 1 
ATOM   1650 C  CD1 . ILE A 1 226  ? 29.931 50.523  1.726   1.00 7.61  ? 226  ILE A CD1 1 
ATOM   1651 N  N   . GLN A 1 227  ? 30.024 53.463  5.534   1.00 7.11  ? 227  GLN A N   1 
ATOM   1652 C  CA  . GLN A 1 227  ? 28.882 53.972  6.292   1.00 8.04  ? 227  GLN A CA  1 
ATOM   1653 C  C   . GLN A 1 227  ? 27.892 54.810  5.509   1.00 6.88  ? 227  GLN A C   1 
ATOM   1654 O  O   . GLN A 1 227  ? 26.680 54.615  5.658   1.00 6.72  ? 227  GLN A O   1 
ATOM   1655 C  CB  . GLN A 1 227  ? 29.386 54.780  7.522   1.00 8.04  ? 227  GLN A CB  1 
ATOM   1656 C  CG  . GLN A 1 227  ? 28.353 55.854  8.030   1.00 8.64  ? 227  GLN A CG  1 
ATOM   1657 C  CD  . GLN A 1 227  ? 27.047 55.321  8.528   1.00 7.62  ? 227  GLN A CD  1 
ATOM   1658 O  OE1 . GLN A 1 227  ? 26.925 54.168  8.863   1.00 10.02 ? 227  GLN A OE1 1 
ATOM   1659 N  NE2 . GLN A 1 227  ? 26.056 56.202  8.569   1.00 8.31  ? 227  GLN A NE2 1 
ATOM   1660 N  N   . ARG A 1 228  ? 28.340 55.754  4.690   1.00 7.71  ? 228  ARG A N   1 
ATOM   1661 C  CA  . ARG A 1 228  ? 27.360 56.636  4.076   1.00 7.93  ? 228  ARG A CA  1 
ATOM   1662 C  C   . ARG A 1 228  ? 26.819 56.118  2.779   1.00 8.15  ? 228  ARG A C   1 
ATOM   1663 O  O   . ARG A 1 228  ? 27.359 56.380  1.698   1.00 8.11  ? 228  ARG A O   1 
ATOM   1664 C  CB  . ARG A 1 228  ? 27.978 58.041  3.885   1.00 7.97  ? 228  ARG A CB  1 
ATOM   1665 C  CG  . ARG A 1 228  ? 28.115 58.823  5.201   1.00 6.95  ? 228  ARG A CG  1 
ATOM   1666 C  CD  . ARG A 1 228  ? 28.389 60.271  4.893   1.00 8.54  ? 228  ARG A CD  1 
ATOM   1667 N  NE  . ARG A 1 228  ? 28.713 61.129  6.030   1.00 7.85  ? 228  ARG A NE  1 
ATOM   1668 C  CZ  . ARG A 1 228  ? 27.806 61.856  6.701   1.00 11.75 ? 228  ARG A CZ  1 
ATOM   1669 N  NH1 . ARG A 1 228  ? 26.499 61.796  6.376   1.00 10.36 ? 228  ARG A NH1 1 
ATOM   1670 N  NH2 . ARG A 1 228  ? 28.224 62.651  7.650   1.00 12.19 ? 228  ARG A NH2 1 
ATOM   1671 N  N   . THR A 1 229  ? 25.729 55.356  2.915   1.00 7.78  ? 229  THR A N   1 
ATOM   1672 C  CA  . THR A 1 229  ? 25.053 54.823  1.752   1.00 6.57  ? 229  THR A CA  1 
ATOM   1673 C  C   . THR A 1 229  ? 23.585 55.223  1.881   1.00 6.55  ? 229  THR A C   1 
ATOM   1674 O  O   . THR A 1 229  ? 23.129 55.501  3.015   1.00 8.81  ? 229  THR A O   1 
ATOM   1675 C  CB  . THR A 1 229  ? 25.208 53.267  1.660   1.00 6.92  ? 229  THR A CB  1 
ATOM   1676 O  OG1 . THR A 1 229  ? 24.522 52.677  2.757   1.00 8.97  ? 229  THR A OG1 1 
ATOM   1677 C  CG2 . THR A 1 229  ? 26.674 52.870  1.561   1.00 8.78  ? 229  THR A CG2 1 
ATOM   1678 N  N   . HIS A 1 230  ? 22.877 55.296  0.743   1.00 6.86  ? 230  HIS A N   1 
ATOM   1679 C  CA  . HIS A 1 230  ? 21.465 55.708  0.710   1.00 6.81  ? 230  HIS A CA  1 
ATOM   1680 C  C   . HIS A 1 230  ? 20.643 54.983  1.788   1.00 8.21  ? 230  HIS A C   1 
ATOM   1681 O  O   . HIS A 1 230  ? 20.766 53.766  1.925   1.00 7.14  ? 230  HIS A O   1 
ATOM   1682 C  CB  . HIS A 1 230  ? 20.903 55.438  -0.680  1.00 8.81  ? 230  HIS A CB  1 
ATOM   1683 C  CG  . HIS A 1 230  ? 19.623 56.157  -0.976  1.00 10.68 ? 230  HIS A CG  1 
ATOM   1684 N  ND1 . HIS A 1 230  ? 18.448 55.924  -0.280  1.00 9.60  ? 230  HIS A ND1 1 
ATOM   1685 C  CD2 . HIS A 1 230  ? 19.338 57.091  -1.909  1.00 10.31 ? 230  HIS A CD2 1 
ATOM   1686 C  CE1 . HIS A 1 230  ? 17.497 56.700  -0.768  1.00 10.70 ? 230  HIS A CE1 1 
ATOM   1687 N  NE2 . HIS A 1 230  ? 18.008 57.409  -1.768  1.00 10.52 ? 230  HIS A NE2 1 
ATOM   1688 N  N   . TYR A 1 231  ? 19.824 55.721  2.536   1.00 8.28  ? 231  TYR A N   1 
ATOM   1689 C  CA  . TYR A 1 231  ? 19.027 55.091  3.558   1.00 9.03  ? 231  TYR A CA  1 
ATOM   1690 C  C   . TYR A 1 231  ? 18.141 53.987  2.994   1.00 9.89  ? 231  TYR A C   1 
ATOM   1691 O  O   . TYR A 1 231  ? 17.878 53.022  3.732   1.00 10.40 ? 231  TYR A O   1 
ATOM   1692 C  CB  . TYR A 1 231  ? 18.174 56.120  4.329   1.00 8.23  ? 231  TYR A CB  1 
ATOM   1693 C  CG  . TYR A 1 231  ? 17.168 56.896  3.475   1.00 10.38 ? 231  TYR A CG  1 
ATOM   1694 C  CD1 . TYR A 1 231  ? 15.863 56.418  3.293   1.00 10.63 ? 231  TYR A CD1 1 
ATOM   1695 C  CD2 . TYR A 1 231  ? 17.507 58.140  2.873   1.00 9.46  ? 231  TYR A CD2 1 
ATOM   1696 C  CE1 . TYR A 1 231  ? 14.949 57.155  2.552   1.00 11.25 ? 231  TYR A CE1 1 
ATOM   1697 C  CE2 . TYR A 1 231  ? 16.605 58.874  2.110   1.00 9.21  ? 231  TYR A CE2 1 
ATOM   1698 C  CZ  . TYR A 1 231  ? 15.299 58.374  1.953   1.00 9.27  ? 231  TYR A CZ  1 
ATOM   1699 O  OH  . TYR A 1 231  ? 14.413 59.147  1.230   1.00 10.99 ? 231  TYR A OH  1 
ATOM   1700 N  N   . SER A 1 232  ? 17.659 54.093  1.769   1.00 9.53  ? 232  SER A N   1 
ATOM   1701 C  CA  . SER A 1 232  ? 16.854 52.993  1.196   1.00 10.98 ? 232  SER A CA  1 
ATOM   1702 C  C   . SER A 1 232  ? 17.713 51.752  0.931   1.00 10.97 ? 232  SER A C   1 
ATOM   1703 O  O   . SER A 1 232  ? 17.227 50.606  0.995   1.00 10.51 ? 232  SER A O   1 
ATOM   1704 C  CB  . SER A 1 232  ? 16.225 53.417  -0.103  1.00 12.26 ? 232  SER A CB  1 
ATOM   1705 O  OG  . SER A 1 232  ? 15.286 54.446  0.107   1.00 13.29 ? 232  SER A OG  1 
ATOM   1706 N  N   . VAL A 1 233  ? 19.001 51.986  0.587   1.00 9.86  ? 233  VAL A N   1 
ATOM   1707 C  CA  . VAL A 1 233  ? 19.898 50.849  0.379   1.00 9.51  ? 233  VAL A CA  1 
ATOM   1708 C  C   . VAL A 1 233  ? 20.185 50.126  1.715   1.00 8.00  ? 233  VAL A C   1 
ATOM   1709 O  O   . VAL A 1 233  ? 20.154 48.869  1.731   1.00 9.39  ? 233  VAL A O   1 
ATOM   1710 C  CB  . VAL A 1 233  ? 21.220 51.285  -0.267  1.00 8.65  ? 233  VAL A CB  1 
ATOM   1711 C  CG1 . VAL A 1 233  ? 22.193 50.124  -0.314  1.00 10.84 ? 233  VAL A CG1 1 
ATOM   1712 C  CG2 . VAL A 1 233  ? 20.918 51.768  -1.655  1.00 10.16 ? 233  VAL A CG2 1 
ATOM   1713 N  N   . LYS A 1 234  ? 20.402 50.889  2.782   1.00 10.05 ? 234  LYS A N   1 
ATOM   1714 C  CA  . LYS A 1 234  ? 20.624 50.291  4.118   1.00 8.43  ? 234  LYS A CA  1 
ATOM   1715 C  C   . LYS A 1 234  ? 19.399 49.424  4.509   1.00 9.71  ? 234  LYS A C   1 
ATOM   1716 O  O   . LYS A 1 234  ? 19.565 48.310  4.959   1.00 10.28 ? 234  LYS A O   1 
ATOM   1717 C  CB  . LYS A 1 234  ? 20.875 51.342  5.177   1.00 9.92  ? 234  LYS A CB  1 
ATOM   1718 C  CG  . LYS A 1 234  ? 22.288 51.944  5.167   1.00 10.77 ? 234  LYS A CG  1 
ATOM   1719 C  CD  . LYS A 1 234  ? 22.273 53.263  5.861   1.00 10.72 ? 234  LYS A CD  1 
ATOM   1720 C  CE  . LYS A 1 234  ? 23.652 53.909  5.866   1.00 8.00  ? 234  LYS A CE  1 
ATOM   1721 N  NZ  . LYS A 1 234  ? 24.526 53.356  6.906   1.00 9.06  ? 234  LYS A NZ  1 
ATOM   1722 N  N   . LYS A 1 235  ? 18.192 49.924  4.246   1.00 10.35 ? 235  LYS A N   1 
ATOM   1723 C  CA  . LYS A 1 235  ? 16.973 49.161  4.598   1.00 10.98 ? 235  LYS A CA  1 
ATOM   1724 C  C   . LYS A 1 235  ? 16.859 47.860  3.787   1.00 11.12 ? 235  LYS A C   1 
ATOM   1725 O  O   . LYS A 1 235  ? 16.583 46.762  4.364   1.00 13.01 ? 235  LYS A O   1 
ATOM   1726 C  CB  . LYS A 1 235  ? 15.741 50.048  4.408   1.00 10.17 ? 235  LYS A CB  1 
ATOM   1727 C  CG  . LYS A 1 235  ? 14.453 49.341  4.855   1.00 14.66 ? 235  LYS A CG  1 
ATOM   1728 C  CD  . LYS A 1 235  ? 13.251 50.292  4.666   1.00 15.07 ? 235  LYS A CD  1 
ATOM   1729 C  CE  . LYS A 1 235  ? 11.943 49.651  5.165   1.00 18.82 ? 235  LYS A CE  1 
ATOM   1730 N  NZ  . LYS A 1 235  ? 10.747 50.600  5.230   1.00 22.80 ? 235  LYS A NZ  1 
ATOM   1731 N  N   . GLU A 1 236  ? 17.099 47.942  2.489   1.00 11.14 ? 236  GLU A N   1 
ATOM   1732 C  CA  . GLU A 1 236  ? 16.995 46.800  1.574   1.00 11.44 ? 236  GLU A CA  1 
ATOM   1733 C  C   . GLU A 1 236  ? 18.032 45.723  1.935   1.00 12.59 ? 236  GLU A C   1 
ATOM   1734 O  O   . GLU A 1 236  ? 17.723 44.539  2.110   1.00 10.80 ? 236  GLU A O   1 
ATOM   1735 C  CB  . GLU A 1 236  ? 17.179 47.318  0.120   1.00 16.41 ? 236  GLU A CB  1 
ATOM   1736 C  CG  . GLU A 1 236  ? 16.908 46.276  -0.933  1.00 22.81 ? 236  GLU A CG  1 
ATOM   1737 C  CD  . GLU A 1 236  ? 15.400 45.951  -1.007  1.00 25.30 ? 236  GLU A CD  1 
ATOM   1738 O  OE1 . GLU A 1 236  ? 14.552 46.803  -0.606  1.00 27.45 ? 236  GLU A OE1 1 
ATOM   1739 O  OE2 . GLU A 1 236  ? 15.081 44.858  -1.477  1.00 29.19 ? 236  GLU A OE2 1 
ATOM   1740 N  N   . LEU A 1 237  ? 19.287 46.124  2.077   1.00 8.75  ? 237  LEU A N   1 
ATOM   1741 C  CA  . LEU A 1 237  ? 20.291 45.177  2.430   1.00 10.55 ? 237  LEU A CA  1 
ATOM   1742 C  C   . LEU A 1 237  ? 20.107 44.627  3.847   1.00 10.43 ? 237  LEU A C   1 
ATOM   1743 O  O   . LEU A 1 237  ? 20.335 43.403  4.041   1.00 11.55 ? 237  LEU A O   1 
ATOM   1744 C  CB  . LEU A 1 237  ? 21.720 45.775  2.249   1.00 9.25  ? 237  LEU A CB  1 
ATOM   1745 C  CG  . LEU A 1 237  ? 22.054 46.195  0.792   1.00 10.98 ? 237  LEU A CG  1 
ATOM   1746 C  CD1 . LEU A 1 237  ? 23.537 46.732  0.804   1.00 11.28 ? 237  LEU A CD1 1 
ATOM   1747 C  CD2 . LEU A 1 237  ? 21.932 45.089  -0.228  1.00 12.23 ? 237  LEU A CD2 1 
ATOM   1748 N  N   . ALA A 1 238  ? 19.671 45.434  4.823   1.00 11.09 ? 238  ALA A N   1 
ATOM   1749 C  CA  . ALA A 1 238  ? 19.465 44.933  6.179   1.00 10.97 ? 238  ALA A CA  1 
ATOM   1750 C  C   . ALA A 1 238  ? 18.413 43.812  6.167   1.00 12.66 ? 238  ALA A C   1 
ATOM   1751 O  O   . ALA A 1 238  ? 18.564 42.808  6.894   1.00 11.81 ? 238  ALA A O   1 
ATOM   1752 C  CB  . ALA A 1 238  ? 18.975 46.061  7.074   1.00 10.56 ? 238  ALA A CB  1 
ATOM   1753 N  N   . GLN A 1 239  ? 17.339 44.025  5.416   1.00 11.91 ? 239  GLN A N   1 
ATOM   1754 C  CA  . GLN A 1 239  ? 16.249 43.046  5.360   1.00 13.74 ? 239  GLN A CA  1 
ATOM   1755 C  C   . GLN A 1 239  ? 16.700 41.680  4.914   1.00 14.15 ? 239  GLN A C   1 
ATOM   1756 O  O   . GLN A 1 239  ? 16.121 40.700  5.368   1.00 16.45 ? 239  GLN A O   1 
ATOM   1757 C  CB  . GLN A 1 239  ? 15.120 43.542  4.474   1.00 13.96 ? 239  GLN A CB  1 
ATOM   1758 C  CG  . GLN A 1 239  ? 14.284 44.589  5.195   1.00 19.26 ? 239  GLN A CG  1 
ATOM   1759 C  CD  . GLN A 1 239  ? 13.243 45.225  4.307   1.00 20.80 ? 239  GLN A CD  1 
ATOM   1760 O  OE1 . GLN A 1 239  ? 13.412 45.270  3.123   1.00 23.66 ? 239  GLN A OE1 1 
ATOM   1761 N  NE2 . GLN A 1 239  ? 12.171 45.751  4.899   1.00 23.18 ? 239  GLN A NE2 1 
ATOM   1762 N  N   . GLN A 1 240  ? 17.702 41.607  4.043   1.00 13.48 ? 240  GLN A N   1 
ATOM   1763 C  CA  . GLN A 1 240  ? 18.230 40.364  3.488   1.00 13.05 ? 240  GLN A CA  1 
ATOM   1764 C  C   . GLN A 1 240  ? 19.535 39.946  4.163   1.00 12.24 ? 240  GLN A C   1 
ATOM   1765 O  O   . GLN A 1 240  ? 20.178 38.951  3.803   1.00 12.00 ? 240  GLN A O   1 
ATOM   1766 C  CB  . GLN A 1 240  ? 18.496 40.603  1.997   1.00 15.62 ? 240  GLN A CB  1 
ATOM   1767 C  CG  . GLN A 1 240  ? 17.285 41.125  1.258   1.00 20.29 ? 240  GLN A CG  1 
ATOM   1768 C  CD  . GLN A 1 240  ? 16.143 40.141  1.296   1.00 22.48 ? 240  GLN A CD  1 
ATOM   1769 O  OE1 . GLN A 1 240  ? 16.359 38.899  1.312   1.00 24.04 ? 240  GLN A OE1 1 
ATOM   1770 N  NE2 . GLN A 1 240  ? 14.917 40.667  1.297   1.00 22.49 ? 240  GLN A NE2 1 
ATOM   1771 N  N   . ARG A 1 241  ? 19.908 40.669  5.226   1.00 11.83 ? 241  ARG A N   1 
ATOM   1772 C  CA  . ARG A 1 241  ? 21.207 40.448  5.878   1.00 10.21 ? 241  ARG A CA  1 
ATOM   1773 C  C   . ARG A 1 241  ? 22.338 40.408  4.841   1.00 9.96  ? 241  ARG A C   1 
ATOM   1774 O  O   . ARG A 1 241  ? 23.190 39.492  4.813   1.00 10.71 ? 241  ARG A O   1 
ATOM   1775 C  CB  . ARG A 1 241  ? 21.206 39.218  6.817   1.00 10.25 ? 241  ARG A CB  1 
ATOM   1776 C  CG  . ARG A 1 241  ? 20.112 39.304  7.915   1.00 12.39 ? 241  ARG A CG  1 
ATOM   1777 C  CD  . ARG A 1 241  ? 20.164 38.143  8.948   1.00 15.45 ? 241  ARG A CD  1 
ATOM   1778 N  NE  . ARG A 1 241  ? 20.224 36.861  8.281   1.00 20.09 ? 241  ARG A NE  1 
ATOM   1779 C  CZ  . ARG A 1 241  ? 20.680 35.730  8.831   1.00 22.26 ? 241  ARG A CZ  1 
ATOM   1780 N  NH1 . ARG A 1 241  ? 21.108 35.710  10.103  1.00 21.91 ? 241  ARG A NH1 1 
ATOM   1781 N  NH2 . ARG A 1 241  ? 20.781 34.635  8.065   1.00 22.84 ? 241  ARG A NH2 1 
ATOM   1782 N  N   . GLN A 1 242  ? 22.355 41.484  4.032   1.00 11.23 ? 242  GLN A N   1 
ATOM   1783 C  CA  . GLN A 1 242  ? 23.388 41.643  2.972   1.00 8.95  ? 242  GLN A CA  1 
ATOM   1784 C  C   . GLN A 1 242  ? 24.258 42.884  3.217   1.00 9.26  ? 242  GLN A C   1 
ATOM   1785 O  O   . GLN A 1 242  ? 24.842 43.416  2.271   1.00 10.21 ? 242  GLN A O   1 
ATOM   1786 C  CB  . GLN A 1 242  ? 22.725 41.699  1.574   1.00 10.67 ? 242  GLN A CB  1 
ATOM   1787 C  CG  . GLN A 1 242  ? 22.055 40.394  1.140   1.00 10.35 ? 242  GLN A CG  1 
ATOM   1788 C  CD  . GLN A 1 242  ? 21.249 40.542  -0.140  1.00 10.06 ? 242  GLN A CD  1 
ATOM   1789 O  OE1 . GLN A 1 242  ? 20.715 41.566  -0.381  1.00 11.20 ? 242  GLN A OE1 1 
ATOM   1790 N  NE2 . GLN A 1 242  ? 21.164 39.453  -0.944  1.00 14.06 ? 242  GLN A NE2 1 
ATOM   1791 N  N   . LEU A 1 243  ? 24.414 43.256  4.500   1.00 8.60  ? 243  LEU A N   1 
ATOM   1792 C  CA  . LEU A 1 243  ? 25.212 44.428  4.863   1.00 8.63  ? 243  LEU A CA  1 
ATOM   1793 C  C   . LEU A 1 243  ? 26.652 44.044  4.891   1.00 8.70  ? 243  LEU A C   1 
ATOM   1794 O  O   . LEU A 1 243  ? 27.526 44.929  4.941   1.00 9.53  ? 243  LEU A O   1 
ATOM   1795 C  CB  . LEU A 1 243  ? 24.713 44.920  6.228   1.00 6.67  ? 243  LEU A CB  1 
ATOM   1796 C  CG  . LEU A 1 243  ? 23.319 45.558  6.226   1.00 9.35  ? 243  LEU A CG  1 
ATOM   1797 C  CD1 . LEU A 1 243  ? 22.908 45.773  7.678   1.00 8.10  ? 243  LEU A CD1 1 
ATOM   1798 C  CD2 . LEU A 1 243  ? 23.350 46.943  5.492   1.00 10.23 ? 243  LEU A CD2 1 
ATOM   1799 N  N   . GLU A 1 244  ? 26.936 42.750  4.989   1.00 7.65  ? 244  GLU A N   1 
ATOM   1800 C  CA  . GLU A 1 244  ? 28.333 42.270  4.865   1.00 5.86  ? 244  GLU A CA  1 
ATOM   1801 C  C   . GLU A 1 244  ? 28.390 41.468  3.602   1.00 8.43  ? 244  GLU A C   1 
ATOM   1802 O  O   . GLU A 1 244  ? 27.588 40.507  3.410   1.00 8.59  ? 244  GLU A O   1 
ATOM   1803 C  CB  . GLU A 1 244  ? 28.761 41.409  6.064   1.00 9.13  ? 244  GLU A CB  1 
ATOM   1804 C  CG  . GLU A 1 244  ? 29.131 42.341  7.225   1.00 9.87  ? 244  GLU A CG  1 
ATOM   1805 C  CD  . GLU A 1 244  ? 29.427 41.667  8.596   1.00 10.01 ? 244  GLU A CD  1 
ATOM   1806 O  OE1 . GLU A 1 244  ? 28.842 40.580  8.897   1.00 9.26  ? 244  GLU A OE1 1 
ATOM   1807 O  OE2 . GLU A 1 244  ? 30.260 42.228  9.380   1.00 8.73  ? 244  GLU A OE2 1 
ATOM   1808 N  N   . PHE A 1 245  ? 29.352 41.816  2.749   1.00 6.75  ? 245  PHE A N   1 
ATOM   1809 C  CA  . PHE A 1 245  ? 29.424 41.185  1.413   1.00 6.71  ? 245  PHE A CA  1 
ATOM   1810 C  C   . PHE A 1 245  ? 30.815 41.153  0.848   1.00 7.17  ? 245  PHE A C   1 
ATOM   1811 O  O   . PHE A 1 245  ? 31.681 41.900  1.338   1.00 8.07  ? 245  PHE A O   1 
ATOM   1812 C  CB  . PHE A 1 245  ? 28.479 41.948  0.411   1.00 7.80  ? 245  PHE A CB  1 
ATOM   1813 C  CG  . PHE A 1 245  ? 28.599 43.436  0.480   1.00 8.92  ? 245  PHE A CG  1 
ATOM   1814 C  CD1 . PHE A 1 245  ? 29.539 44.113  -0.316  1.00 7.46  ? 245  PHE A CD1 1 
ATOM   1815 C  CD2 . PHE A 1 245  ? 27.790 44.163  1.355   1.00 10.02 ? 245  PHE A CD2 1 
ATOM   1816 C  CE1 . PHE A 1 245  ? 29.673 45.535  -0.247  1.00 6.05  ? 245  PHE A CE1 1 
ATOM   1817 C  CE2 . PHE A 1 245  ? 27.925 45.567  1.422   1.00 9.43  ? 245  PHE A CE2 1 
ATOM   1818 C  CZ  . PHE A 1 245  ? 28.861 46.245  0.621   1.00 7.76  ? 245  PHE A CZ  1 
ATOM   1819 N  N   . LEU A 1 246  ? 31.056 40.333  -0.184  1.00 7.24  ? 246  LEU A N   1 
ATOM   1820 C  CA  . LEU A 1 246  ? 32.372 40.271  -0.832  1.00 6.58  ? 246  LEU A CA  1 
ATOM   1821 C  C   . LEU A 1 246  ? 32.222 41.222  -2.025  1.00 7.55  ? 246  LEU A C   1 
ATOM   1822 O  O   . LEU A 1 246  ? 31.550 40.927  -3.012  1.00 8.11  ? 246  LEU A O   1 
ATOM   1823 C  CB  . LEU A 1 246  ? 32.654 38.809  -1.265  1.00 8.00  ? 246  LEU A CB  1 
ATOM   1824 C  CG  . LEU A 1 246  ? 33.015 37.909  -0.025  1.00 10.67 ? 246  LEU A CG  1 
ATOM   1825 C  CD1 . LEU A 1 246  ? 32.838 36.429  -0.384  1.00 14.19 ? 246  LEU A CD1 1 
ATOM   1826 C  CD2 . LEU A 1 246  ? 34.484 38.139  0.337   1.00 13.19 ? 246  LEU A CD2 1 
ATOM   1827 N  N   . TRP A 1 247  ? 32.830 42.410  -1.890  1.00 7.88  ? 247  TRP A N   1 
ATOM   1828 C  CA  . TRP A 1 247  ? 32.660 43.399  -2.945  1.00 7.78  ? 247  TRP A CA  1 
ATOM   1829 C  C   . TRP A 1 247  ? 33.696 43.209  -4.055  1.00 6.85  ? 247  TRP A C   1 
ATOM   1830 O  O   . TRP A 1 247  ? 34.881 43.414  -3.842  1.00 7.76  ? 247  TRP A O   1 
ATOM   1831 C  CB  . TRP A 1 247  ? 32.773 44.781  -2.296  1.00 8.34  ? 247  TRP A CB  1 
ATOM   1832 C  CG  . TRP A 1 247  ? 32.317 46.012  -3.113  1.00 7.23  ? 247  TRP A CG  1 
ATOM   1833 C  CD1 . TRP A 1 247  ? 31.745 46.040  -4.361  1.00 8.14  ? 247  TRP A CD1 1 
ATOM   1834 C  CD2 . TRP A 1 247  ? 32.347 47.359  -2.664  1.00 7.11  ? 247  TRP A CD2 1 
ATOM   1835 N  NE1 . TRP A 1 247  ? 31.406 47.340  -4.708  1.00 8.28  ? 247  TRP A NE1 1 
ATOM   1836 C  CE2 . TRP A 1 247  ? 31.762 48.158  -3.675  1.00 6.82  ? 247  TRP A CE2 1 
ATOM   1837 C  CE3 . TRP A 1 247  ? 32.804 47.981  -1.481  1.00 6.81  ? 247  TRP A CE3 1 
ATOM   1838 C  CZ2 . TRP A 1 247  ? 31.611 49.542  -3.545  1.00 8.93  ? 247  TRP A CZ2 1 
ATOM   1839 C  CZ3 . TRP A 1 247  ? 32.652 49.385  -1.354  1.00 5.75  ? 247  TRP A CZ3 1 
ATOM   1840 C  CH2 . TRP A 1 247  ? 32.057 50.153  -2.388  1.00 5.66  ? 247  TRP A CH2 1 
ATOM   1841 N  N   . ARG A 1 248  ? 33.205 42.856  -5.248  1.00 7.13  ? 248  ARG A N   1 
ATOM   1842 C  CA  . ARG A 1 248  ? 34.085 42.666  -6.423  1.00 8.62  ? 248  ARG A CA  1 
ATOM   1843 C  C   . ARG A 1 248  ? 33.776 43.750  -7.489  1.00 6.23  ? 248  ARG A C   1 
ATOM   1844 O  O   . ARG A 1 248  ? 32.732 44.435  -7.427  1.00 7.16  ? 248  ARG A O   1 
ATOM   1845 C  CB  . ARG A 1 248  ? 33.856 41.319  -7.112  1.00 8.46  ? 248  ARG A CB  1 
ATOM   1846 C  CG  . ARG A 1 248  ? 32.473 41.153  -7.742  1.00 9.52  ? 248  ARG A CG  1 
ATOM   1847 C  CD  . ARG A 1 248  ? 32.419 39.924  -8.648  1.00 14.72 ? 248  ARG A CD  1 
ATOM   1848 N  NE  . ARG A 1 248  ? 32.508 38.734  -7.796  1.00 12.06 ? 248  ARG A NE  1 
ATOM   1849 C  CZ  . ARG A 1 248  ? 32.421 37.475  -8.250  1.00 15.69 ? 248  ARG A CZ  1 
ATOM   1850 N  NH1 . ARG A 1 248  ? 32.264 37.265  -9.566  1.00 15.87 ? 248  ARG A NH1 1 
ATOM   1851 N  NH2 . ARG A 1 248  ? 32.378 36.454  -7.365  1.00 15.76 ? 248  ARG A NH2 1 
ATOM   1852 N  N   . GLN A 1 249  ? 34.724 43.934  -8.400  1.00 8.08  ? 249  GLN A N   1 
ATOM   1853 C  CA  . GLN A 1 249  ? 34.539 44.918  -9.444  1.00 8.57  ? 249  GLN A CA  1 
ATOM   1854 C  C   . GLN A 1 249  ? 33.448 44.497  -10.406 1.00 9.29  ? 249  GLN A C   1 
ATOM   1855 O  O   . GLN A 1 249  ? 33.196 43.324  -10.594 1.00 8.95  ? 249  GLN A O   1 
ATOM   1856 C  CB  . GLN A 1 249  ? 35.880 45.059  -10.154 1.00 8.26  ? 249  GLN A CB  1 
ATOM   1857 C  CG  . GLN A 1 249  ? 36.989 45.592  -9.213  1.00 9.27  ? 249  GLN A CG  1 
ATOM   1858 C  CD  . GLN A 1 249  ? 36.557 46.932  -8.544  1.00 9.87  ? 249  GLN A CD  1 
ATOM   1859 O  OE1 . GLN A 1 249  ? 36.247 47.917  -9.253  1.00 9.31  ? 249  GLN A OE1 1 
ATOM   1860 N  NE2 . GLN A 1 249  ? 36.574 46.986  -7.214  1.00 7.76  ? 249  GLN A NE2 1 
ATOM   1861 N  N   . ILE A 1 250  ? 32.834 45.457  -11.061 1.00 8.60  ? 250  ILE A N   1 
ATOM   1862 C  CA  . ILE A 1 250  ? 31.702 45.134  -11.918 1.00 10.07 ? 250  ILE A CA  1 
ATOM   1863 C  C   . ILE A 1 250  ? 31.990 44.250  -13.099 1.00 11.64 ? 250  ILE A C   1 
ATOM   1864 O  O   . ILE A 1 250  ? 31.067 43.606  -13.607 1.00 9.57  ? 250  ILE A O   1 
ATOM   1865 C  CB  . ILE A 1 250  ? 30.965 46.451  -12.410 1.00 9.56  ? 250  ILE A CB  1 
ATOM   1866 C  CG1 . ILE A 1 250  ? 31.929 47.362  -13.197 1.00 11.07 ? 250  ILE A CG1 1 
ATOM   1867 C  CG2 . ILE A 1 250  ? 30.368 47.236  -11.254 1.00 8.75  ? 250  ILE A CG2 1 
ATOM   1868 C  CD1 . ILE A 1 250  ? 31.287 48.765  -13.634 1.00 12.30 ? 250  ILE A CD1 1 
ATOM   1869 N  N   . TRP A 1 251  ? 33.237 44.237  -13.535 1.00 11.29 ? 251  TRP A N   1 
ATOM   1870 C  CA  . TRP A 1 251  ? 33.601 43.401  -14.673 1.00 12.95 ? 251  TRP A CA  1 
ATOM   1871 C  C   . TRP A 1 251  ? 34.291 42.102  -14.263 1.00 14.87 ? 251  TRP A C   1 
ATOM   1872 O  O   . TRP A 1 251  ? 34.745 41.366  -15.154 1.00 16.49 ? 251  TRP A O   1 
ATOM   1873 C  CB  . TRP A 1 251  ? 34.607 44.092  -15.574 1.00 13.72 ? 251  TRP A CB  1 
ATOM   1874 C  CG  . TRP A 1 251  ? 35.872 44.220  -14.885 1.00 16.77 ? 251  TRP A CG  1 
ATOM   1875 C  CD1 . TRP A 1 251  ? 36.868 43.251  -14.719 1.00 17.93 ? 251  TRP A CD1 1 
ATOM   1876 C  CD2 . TRP A 1 251  ? 36.286 45.329  -14.162 1.00 14.61 ? 251  TRP A CD2 1 
ATOM   1877 N  NE1 . TRP A 1 251  ? 37.865 43.728  -13.926 1.00 16.41 ? 251  TRP A NE1 1 
ATOM   1878 C  CE2 . TRP A 1 251  ? 37.535 45.013  -13.563 1.00 15.95 ? 251  TRP A CE2 1 
ATOM   1879 C  CE3 . TRP A 1 251  ? 35.727 46.580  -13.947 1.00 14.87 ? 251  TRP A CE3 1 
ATOM   1880 C  CZ2 . TRP A 1 251  ? 38.226 45.907  -12.770 1.00 16.85 ? 251  TRP A CZ2 1 
ATOM   1881 C  CZ3 . TRP A 1 251  ? 36.413 47.470  -13.154 1.00 15.51 ? 251  TRP A CZ3 1 
ATOM   1882 C  CH2 . TRP A 1 251  ? 37.647 47.128  -12.578 1.00 17.72 ? 251  TRP A CH2 1 
ATOM   1883 N  N   . ASP A 1 252  ? 34.406 41.836  -12.966 1.00 13.78 ? 252  ASP A N   1 
ATOM   1884 C  CA  . ASP A 1 252  ? 35.149 40.679  -12.491 1.00 14.74 ? 252  ASP A CA  1 
ATOM   1885 C  C   . ASP A 1 252  ? 34.308 39.426  -12.387 1.00 15.23 ? 252  ASP A C   1 
ATOM   1886 O  O   . ASP A 1 252  ? 33.522 39.192  -11.483 1.00 14.60 ? 252  ASP A O   1 
ATOM   1887 C  CB  . ASP A 1 252  ? 35.754 41.042  -11.152 1.00 14.61 ? 252  ASP A CB  1 
ATOM   1888 C  CG  . ASP A 1 252  ? 36.514 39.918  -10.510 1.00 17.25 ? 252  ASP A CG  1 
ATOM   1889 O  OD1 . ASP A 1 252  ? 36.788 38.885  -11.164 1.00 18.77 ? 252  ASP A OD1 1 
ATOM   1890 O  OD2 . ASP A 1 252  ? 36.848 40.059  -9.312  1.00 15.11 ? 252  ASP A OD2 1 
ATOM   1891 N  N   . ASN A 1 253  ? 34.511 38.580  -13.367 1.00 17.04 ? 253  ASN A N   1 
ATOM   1892 C  CA  . ASN A 1 253  ? 33.730 37.386  -13.451 1.00 16.19 ? 253  ASN A CA  1 
ATOM   1893 C  C   . ASN A 1 253  ? 34.095 36.280  -12.458 1.00 17.01 ? 253  ASN A C   1 
ATOM   1894 O  O   . ASN A 1 253  ? 33.208 35.556  -12.003 1.00 17.61 ? 253  ASN A O   1 
ATOM   1895 C  CB  . ASN A 1 253  ? 33.880 36.836  -14.866 1.00 18.99 ? 253  ASN A CB  1 
ATOM   1896 C  CG  . ASN A 1 253  ? 32.988 35.683  -15.099 1.00 21.36 ? 253  ASN A CG  1 
ATOM   1897 O  OD1 . ASN A 1 253  ? 31.777 35.786  -14.912 1.00 22.96 ? 253  ASN A OD1 1 
ATOM   1898 N  ND2 . ASN A 1 253  ? 33.567 34.558  -15.509 1.00 23.15 ? 253  ASN A ND2 1 
ATOM   1899 N  N   . LYS A 1 254  ? 35.392 36.183  -12.177 1.00 18.72 ? 254  LYS A N   1 
ATOM   1900 C  CA  . LYS A 1 254  ? 35.958 35.177  -11.304 1.00 20.92 ? 254  LYS A CA  1 
ATOM   1901 C  C   . LYS A 1 254  ? 35.836 35.516  -9.826  1.00 19.88 ? 254  LYS A C   1 
ATOM   1902 O  O   . LYS A 1 254  ? 35.563 34.651  -8.983  1.00 21.49 ? 254  LYS A O   1 
ATOM   1903 C  CB  . LYS A 1 254  ? 37.435 34.991  -11.669 1.00 23.89 ? 254  LYS A CB  1 
ATOM   1904 C  CG  . LYS A 1 254  ? 38.050 33.709  -11.157 1.00 29.17 ? 254  LYS A CG  1 
ATOM   1905 C  CD  . LYS A 1 254  ? 39.367 33.429  -11.906 1.00 32.56 ? 254  LYS A CD  1 
ATOM   1906 C  CE  . LYS A 1 254  ? 40.126 32.242  -11.278 1.00 34.35 ? 254  LYS A CE  1 
ATOM   1907 N  NZ  . LYS A 1 254  ? 40.362 32.456  -9.820  1.00 35.41 ? 254  LYS A NZ  1 
ATOM   1908 N  N   . GLY A 1 255  ? 36.004 36.802  -9.535  1.00 18.78 ? 255  GLY A N   1 
ATOM   1909 C  CA  . GLY A 1 255  ? 35.958 37.263  -8.161  1.00 17.19 ? 255  GLY A CA  1 
ATOM   1910 C  C   . GLY A 1 255  ? 37.316 37.497  -7.515  1.00 16.62 ? 255  GLY A C   1 
ATOM   1911 O  O   . GLY A 1 255  ? 37.344 37.676  -6.294  1.00 16.96 ? 255  GLY A O   1 
ATOM   1912 N  N   . ASP A 1 256  ? 38.421 37.554  -8.269  1.00 15.70 ? 256  ASP A N   1 
ATOM   1913 C  CA  . ASP A 1 256  ? 39.734 37.755  -7.631  1.00 18.35 ? 256  ASP A CA  1 
ATOM   1914 C  C   . ASP A 1 256  ? 39.939 39.140  -7.044  1.00 15.77 ? 256  ASP A C   1 
ATOM   1915 O  O   . ASP A 1 256  ? 40.821 39.351  -6.255  1.00 14.69 ? 256  ASP A O   1 
ATOM   1916 C  CB  . ASP A 1 256  ? 40.908 37.575  -8.593  1.00 24.53 ? 256  ASP A CB  1 
ATOM   1917 C  CG  . ASP A 1 256  ? 41.065 36.168  -9.102  1.00 29.04 ? 256  ASP A CG  1 
ATOM   1918 O  OD1 . ASP A 1 256  ? 40.651 35.205  -8.396  1.00 31.85 ? 256  ASP A OD1 1 
ATOM   1919 O  OD2 . ASP A 1 256  ? 41.635 36.062  -10.216 1.00 32.22 ? 256  ASP A OD2 1 
ATOM   1920 N  N   . THR A 1 257  ? 39.121 40.100  -7.427  1.00 11.88 ? 257  THR A N   1 
ATOM   1921 C  CA  . THR A 1 257  ? 39.234 41.437  -6.868  1.00 11.83 ? 257  THR A CA  1 
ATOM   1922 C  C   . THR A 1 257  ? 38.396 41.594  -5.591  1.00 12.24 ? 257  THR A C   1 
ATOM   1923 O  O   . THR A 1 257  ? 38.467 42.642  -4.956  1.00 11.70 ? 257  THR A O   1 
ATOM   1924 C  CB  . THR A 1 257  ? 38.696 42.510  -7.838  1.00 11.38 ? 257  THR A CB  1 
ATOM   1925 O  OG1 . THR A 1 257  ? 37.282 42.310  -8.054  1.00 10.82 ? 257  THR A OG1 1 
ATOM   1926 C  CG2 . THR A 1 257  ? 39.446 42.414  -9.188  1.00 13.66 ? 257  THR A CG2 1 
ATOM   1927 N  N   . ALA A 1 258  ? 37.651 40.553  -5.206  1.00 12.86 ? 258  ALA A N   1 
ATOM   1928 C  CA  . ALA A 1 258  ? 36.743 40.690  -4.066  1.00 10.68 ? 258  ALA A CA  1 
ATOM   1929 C  C   . ALA A 1 258  ? 37.372 41.075  -2.723  1.00 10.16 ? 258  ALA A C   1 
ATOM   1930 O  O   . ALA A 1 258  ? 38.495 40.605  -2.357  1.00 9.14  ? 258  ALA A O   1 
ATOM   1931 C  CB  . ALA A 1 258  ? 35.935 39.450  -3.901  1.00 11.79 ? 258  ALA A CB  1 
ATOM   1932 N  N   . LEU A 1 259  ? 36.698 41.968  -2.002  1.00 7.88  ? 259  LEU A N   1 
ATOM   1933 C  CA  . LEU A 1 259  ? 37.171 42.371  -0.654  1.00 7.45  ? 259  LEU A CA  1 
ATOM   1934 C  C   . LEU A 1 259  ? 35.997 42.376  0.284   1.00 8.99  ? 259  LEU A C   1 
ATOM   1935 O  O   . LEU A 1 259  ? 34.957 42.939  -0.041  1.00 7.05  ? 259  LEU A O   1 
ATOM   1936 C  CB  . LEU A 1 259  ? 37.844 43.766  -0.730  1.00 9.86  ? 259  LEU A CB  1 
ATOM   1937 C  CG  . LEU A 1 259  ? 38.553 44.154  0.558   1.00 8.24  ? 259  LEU A CG  1 
ATOM   1938 C  CD1 . LEU A 1 259  ? 39.849 43.254  0.729   1.00 9.59  ? 259  LEU A CD1 1 
ATOM   1939 C  CD2 . LEU A 1 259  ? 39.023 45.610  0.448   1.00 11.34 ? 259  LEU A CD2 1 
ATOM   1940 N  N   . PHE A 1 260  ? 36.150 41.630  1.389   1.00 7.93  ? 260  PHE A N   1 
ATOM   1941 C  CA  . PHE A 1 260  ? 35.096 41.607  2.416   1.00 7.92  ? 260  PHE A CA  1 
ATOM   1942 C  C   . PHE A 1 260  ? 34.784 43.028  2.886   1.00 7.44  ? 260  PHE A C   1 
ATOM   1943 O  O   . PHE A 1 260  ? 35.696 43.744  3.313   1.00 8.58  ? 260  PHE A O   1 
ATOM   1944 C  CB  . PHE A 1 260  ? 35.503 40.769  3.640   1.00 8.24  ? 260  PHE A CB  1 
ATOM   1945 C  CG  . PHE A 1 260  ? 34.368 40.585  4.631   1.00 7.66  ? 260  PHE A CG  1 
ATOM   1946 C  CD1 . PHE A 1 260  ? 33.405 39.599  4.409   1.00 8.68  ? 260  PHE A CD1 1 
ATOM   1947 C  CD2 . PHE A 1 260  ? 34.280 41.366  5.767   1.00 8.48  ? 260  PHE A CD2 1 
ATOM   1948 C  CE1 . PHE A 1 260  ? 32.370 39.430  5.374   1.00 11.26 ? 260  PHE A CE1 1 
ATOM   1949 C  CE2 . PHE A 1 260  ? 33.267 41.203  6.695   1.00 8.31  ? 260  PHE A CE2 1 
ATOM   1950 C  CZ  . PHE A 1 260  ? 32.319 40.215  6.479   1.00 10.02 ? 260  PHE A CZ  1 
ATOM   1951 N  N   . THR A 1 261  ? 33.501 43.375  2.883   1.00 5.17  ? 261  THR A N   1 
ATOM   1952 C  CA  . THR A 1 261  ? 33.066 44.726  3.219   1.00 6.60  ? 261  THR A CA  1 
ATOM   1953 C  C   . THR A 1 261  ? 31.942 44.711  4.234   1.00 6.40  ? 261  THR A C   1 
ATOM   1954 O  O   . THR A 1 261  ? 30.950 43.966  4.114   1.00 8.32  ? 261  THR A O   1 
ATOM   1955 C  CB  . THR A 1 261  ? 32.537 45.436  1.949   1.00 8.18  ? 261  THR A CB  1 
ATOM   1956 O  OG1 . THR A 1 261  ? 33.588 45.543  0.977   1.00 7.64  ? 261  THR A OG1 1 
ATOM   1957 C  CG2 . THR A 1 261  ? 32.098 46.866  2.228   1.00 6.92  ? 261  THR A CG2 1 
ATOM   1958 N  N   . HIS A 1 262  ? 32.061 45.588  5.230   1.00 7.70  ? 262  HIS A N   1 
ATOM   1959 C  CA  . HIS A 1 262  ? 30.983 45.715  6.249   1.00 6.57  ? 262  HIS A CA  1 
ATOM   1960 C  C   . HIS A 1 262  ? 30.307 47.105  6.106   1.00 6.60  ? 262  HIS A C   1 
ATOM   1961 O  O   . HIS A 1 262  ? 30.999 48.142  6.205   1.00 8.53  ? 262  HIS A O   1 
ATOM   1962 C  CB  . HIS A 1 262  ? 31.597 45.618  7.630   1.00 7.30  ? 262  HIS A CB  1 
ATOM   1963 C  CG  . HIS A 1 262  ? 30.646 45.956  8.742   1.00 6.07  ? 262  HIS A CG  1 
ATOM   1964 N  ND1 . HIS A 1 262  ? 30.024 44.991  9.520   1.00 7.35  ? 262  HIS A ND1 1 
ATOM   1965 C  CD2 . HIS A 1 262  ? 30.197 47.163  9.179   1.00 6.14  ? 262  HIS A CD2 1 
ATOM   1966 C  CE1 . HIS A 1 262  ? 29.222 45.610  10.380  1.00 6.33  ? 262  HIS A CE1 1 
ATOM   1967 N  NE2 . HIS A 1 262  ? 29.300 46.924  10.201  1.00 6.85  ? 262  HIS A NE2 1 
ATOM   1968 N  N   . MET A 1 263  ? 29.029 47.142  5.756   1.00 6.02  ? 263  MET A N   1 
ATOM   1969 C  CA  . MET A 1 263  ? 28.328 48.387  5.686   1.00 7.62  ? 263  MET A CA  1 
ATOM   1970 C  C   . MET A 1 263  ? 27.563 48.595  7.037   1.00 6.94  ? 263  MET A C   1 
ATOM   1971 O  O   . MET A 1 263  ? 26.810 47.714  7.445   1.00 9.69  ? 263  MET A O   1 
ATOM   1972 C  CB  . MET A 1 263  ? 27.352 48.372  4.496   1.00 8.25  ? 263  MET A CB  1 
ATOM   1973 C  CG  . MET A 1 263  ? 26.464 49.629  4.476   1.00 7.04  ? 263  MET A CG  1 
ATOM   1974 S  SD  . MET A 1 263  ? 25.134 49.545  3.199   1.00 8.97  ? 263  MET A SD  1 
ATOM   1975 C  CE  . MET A 1 263  ? 26.050 49.217  1.630   1.00 8.47  ? 263  MET A CE  1 
ATOM   1976 N  N   . MET A 1 264  ? 27.782 49.727  7.690   1.00 7.57  ? 264  MET A N   1 
ATOM   1977 C  CA  . MET A 1 264  ? 27.076 50.034  8.933   1.00 7.69  ? 264  MET A CA  1 
ATOM   1978 C  C   . MET A 1 264  ? 25.602 50.243  8.518   1.00 6.87  ? 264  MET A C   1 
ATOM   1979 O  O   . MET A 1 264  ? 25.300 50.706  7.414   1.00 7.42  ? 264  MET A O   1 
ATOM   1980 C  CB  . MET A 1 264  ? 27.710 51.269  9.581   1.00 5.78  ? 264  MET A CB  1 
ATOM   1981 C  CG  A MET A 1 264  ? 29.193 51.032  9.838   0.50 6.10  ? 264  MET A CG  1 
ATOM   1982 C  CG  B MET A 1 264  ? 29.189 50.791  10.083  0.50 11.80 ? 264  MET A CG  1 
ATOM   1983 S  SD  A MET A 1 264  ? 30.078 52.469  10.590  0.50 7.22  ? 264  MET A SD  1 
ATOM   1984 S  SD  B MET A 1 264  ? 29.738 51.472  11.662  0.50 15.43 ? 264  MET A SD  1 
ATOM   1985 C  CE  A MET A 1 264  ? 28.866 52.969  11.869  0.50 7.41  ? 264  MET A CE  1 
ATOM   1986 C  CE  B MET A 1 264  ? 29.390 53.124  11.412  0.50 14.13 ? 264  MET A CE  1 
ATOM   1987 N  N   . PRO A 1 265  ? 24.644 49.866  9.393   1.00 8.09  ? 265  PRO A N   1 
ATOM   1988 C  CA  . PRO A 1 265  ? 23.211 49.976  9.091   1.00 9.90  ? 265  PRO A CA  1 
ATOM   1989 C  C   . PRO A 1 265  ? 22.404 51.180  9.290   1.00 8.07  ? 265  PRO A C   1 
ATOM   1990 O  O   . PRO A 1 265  ? 21.323 51.255  8.690   1.00 9.31  ? 265  PRO A O   1 
ATOM   1991 C  CB  . PRO A 1 265  ? 22.616 48.863  9.941   1.00 10.42 ? 265  PRO A CB  1 
ATOM   1992 C  CG  . PRO A 1 265  ? 23.462 48.853  11.180  1.00 10.73 ? 265  PRO A CG  1 
ATOM   1993 C  CD  . PRO A 1 265  ? 24.902 49.341  10.737  1.00 7.95  ? 265  PRO A CD  1 
ATOM   1994 N  N   . PHE A 1 266  ? 22.919 52.121  10.085  1.00 9.09  ? 266  PHE A N   1 
ATOM   1995 C  CA  . PHE A 1 266  ? 22.143 53.274  10.502  1.00 7.53  ? 266  PHE A CA  1 
ATOM   1996 C  C   . PHE A 1 266  ? 22.496 54.640  9.951   1.00 9.31  ? 266  PHE A C   1 
ATOM   1997 O  O   . PHE A 1 266  ? 23.369 54.755  9.098   1.00 10.01 ? 266  PHE A O   1 
ATOM   1998 C  CB  . PHE A 1 266  ? 22.103 53.267  12.015  1.00 7.42  ? 266  PHE A CB  1 
ATOM   1999 C  CG  . PHE A 1 266  ? 21.522 51.972  12.616  1.00 10.86 ? 266  PHE A CG  1 
ATOM   2000 C  CD1 . PHE A 1 266  ? 20.399 51.372  12.053  1.00 8.84  ? 266  PHE A CD1 1 
ATOM   2001 C  CD2 . PHE A 1 266  ? 22.160 51.345  13.716  1.00 7.69  ? 266  PHE A CD2 1 
ATOM   2002 C  CE1 . PHE A 1 266  ? 19.883 50.139  12.562  1.00 8.14  ? 266  PHE A CE1 1 
ATOM   2003 C  CE2 . PHE A 1 266  ? 21.646 50.108  14.214  1.00 9.48  ? 266  PHE A CE2 1 
ATOM   2004 C  CZ  . PHE A 1 266  ? 20.505 49.522  13.625  1.00 9.45  ? 266  PHE A CZ  1 
ATOM   2005 N  N   . TYR A 1 267  ? 21.788 55.653  10.371  1.00 9.22  ? 267  TYR A N   1 
ATOM   2006 C  CA  . TYR A 1 267  ? 21.910 56.972  9.770   1.00 9.08  ? 267  TYR A CA  1 
ATOM   2007 C  C   . TYR A 1 267  ? 23.236 57.685  9.978   1.00 9.30  ? 267  TYR A C   1 
ATOM   2008 O  O   . TYR A 1 267  ? 23.644 58.490  9.136   1.00 9.12  ? 267  TYR A O   1 
ATOM   2009 C  CB  . TYR A 1 267  ? 20.678 57.799  10.233  1.00 10.81 ? 267  TYR A CB  1 
ATOM   2010 C  CG  . TYR A 1 267  ? 20.782 59.292  10.125  1.00 11.13 ? 267  TYR A CG  1 
ATOM   2011 C  CD1 . TYR A 1 267  ? 20.408 59.978  8.967   1.00 11.41 ? 267  TYR A CD1 1 
ATOM   2012 C  CD2 . TYR A 1 267  ? 21.245 60.029  11.222  1.00 10.20 ? 267  TYR A CD2 1 
ATOM   2013 C  CE1 . TYR A 1 267  ? 20.487 61.381  8.938   1.00 12.98 ? 267  TYR A CE1 1 
ATOM   2014 C  CE2 . TYR A 1 267  ? 21.323 61.442  11.199  1.00 12.14 ? 267  TYR A CE2 1 
ATOM   2015 C  CZ  . TYR A 1 267  ? 20.943 62.086  10.064  1.00 13.25 ? 267  TYR A CZ  1 
ATOM   2016 O  OH  . TYR A 1 267  ? 21.009 63.483  10.060  1.00 18.03 ? 267  TYR A OH  1 
ATOM   2017 N  N   . SER A 1 268  ? 23.916 57.395  11.061  1.00 8.14  ? 268  SER A N   1 
ATOM   2018 C  CA  . SER A 1 268  ? 25.195 58.062  11.362  1.00 9.39  ? 268  SER A CA  1 
ATOM   2019 C  C   . SER A 1 268  ? 26.152 57.099  12.033  1.00 9.18  ? 268  SER A C   1 
ATOM   2020 O  O   . SER A 1 268  ? 25.736 56.034  12.443  1.00 9.46  ? 268  SER A O   1 
ATOM   2021 C  CB  . SER A 1 268  ? 24.901 59.220  12.342  1.00 10.13 ? 268  SER A CB  1 
ATOM   2022 O  OG  . SER A 1 268  ? 26.105 59.920  12.697  1.00 12.61 ? 268  SER A OG  1 
ATOM   2023 N  N   . TYR A 1 269  ? 27.420 57.496  12.172  1.00 8.82  ? 269  TYR A N   1 
ATOM   2024 C  CA  . TYR A 1 269  ? 28.394 56.704  12.932  1.00 9.12  ? 269  TYR A CA  1 
ATOM   2025 C  C   . TYR A 1 269  ? 28.508 57.209  14.360  1.00 8.99  ? 269  TYR A C   1 
ATOM   2026 O  O   . TYR A 1 269  ? 29.356 56.719  15.147  1.00 10.02 ? 269  TYR A O   1 
ATOM   2027 C  CB  . TYR A 1 269  ? 29.798 56.768  12.278  1.00 9.66  ? 269  TYR A CB  1 
ATOM   2028 C  CG  . TYR A 1 269  ? 30.298 58.174  11.988  1.00 10.39 ? 269  TYR A CG  1 
ATOM   2029 C  CD1 . TYR A 1 269  ? 30.745 58.977  13.030  1.00 8.85  ? 269  TYR A CD1 1 
ATOM   2030 C  CD2 . TYR A 1 269  ? 30.297 58.698  10.683  1.00 8.53  ? 269  TYR A CD2 1 
ATOM   2031 C  CE1 . TYR A 1 269  ? 31.190 60.309  12.827  1.00 8.69  ? 269  TYR A CE1 1 
ATOM   2032 C  CE2 . TYR A 1 269  ? 30.746 60.011  10.455  1.00 9.58  ? 269  TYR A CE2 1 
ATOM   2033 C  CZ  . TYR A 1 269  ? 31.179 60.789  11.517  1.00 10.06 ? 269  TYR A CZ  1 
ATOM   2034 O  OH  . TYR A 1 269  ? 31.613 62.071  11.190  1.00 11.34 ? 269  TYR A OH  1 
ATOM   2035 N  N   . ASP A 1 270  ? 27.720 58.247  14.707  1.00 9.28  ? 270  ASP A N   1 
ATOM   2036 C  CA  . ASP A 1 270  ? 27.804 58.720  16.074  1.00 9.28  ? 270  ASP A CA  1 
ATOM   2037 C  C   . ASP A 1 270  ? 27.224 57.694  17.076  1.00 10.23 ? 270  ASP A C   1 
ATOM   2038 O  O   . ASP A 1 270  ? 26.646 56.667  16.681  1.00 9.46  ? 270  ASP A O   1 
ATOM   2039 C  CB  . ASP A 1 270  ? 27.148 60.126  16.230  1.00 11.17 ? 270  ASP A CB  1 
ATOM   2040 C  CG  . ASP A 1 270  ? 25.625 60.149  16.002  1.00 14.46 ? 270  ASP A CG  1 
ATOM   2041 O  OD1 . ASP A 1 270  ? 24.941 59.110  15.813  1.00 14.30 ? 270  ASP A OD1 1 
ATOM   2042 O  OD2 . ASP A 1 270  ? 25.115 61.304  16.025  1.00 14.23 ? 270  ASP A OD2 1 
ATOM   2043 N  N   . ILE A 1 271  ? 27.400 57.932  18.382  1.00 10.58 ? 271  ILE A N   1 
ATOM   2044 C  CA  . ILE A 1 271  ? 26.923 56.945  19.372  1.00 11.29 ? 271  ILE A CA  1 
ATOM   2045 C  C   . ILE A 1 271  ? 25.413 56.679  19.310  1.00 11.78 ? 271  ILE A C   1 
ATOM   2046 O  O   . ILE A 1 271  ? 25.008 55.501  19.368  1.00 11.11 ? 271  ILE A O   1 
ATOM   2047 C  CB  . ILE A 1 271  ? 27.467 57.305  20.729  1.00 11.02 ? 271  ILE A CB  1 
ATOM   2048 C  CG1 . ILE A 1 271  ? 28.980 57.117  20.634  1.00 10.56 ? 271  ILE A CG1 1 
ATOM   2049 C  CG2 . ILE A 1 271  ? 26.963 56.320  21.846  1.00 8.84  ? 271  ILE A CG2 1 
ATOM   2050 C  CD1 . ILE A 1 271  ? 29.718 57.628  21.818  1.00 10.12 ? 271  ILE A CD1 1 
ATOM   2051 N  N   . PRO A 1 272  ? 24.577 57.729  19.200  1.00 11.26 ? 272  PRO A N   1 
ATOM   2052 C  CA  . PRO A 1 272  ? 23.125 57.508  19.106  1.00 11.43 ? 272  PRO A CA  1 
ATOM   2053 C  C   . PRO A 1 272  ? 22.742 56.548  17.959  1.00 12.50 ? 272  PRO A C   1 
ATOM   2054 O  O   . PRO A 1 272  ? 21.694 55.910  18.032  1.00 13.44 ? 272  PRO A O   1 
ATOM   2055 C  CB  . PRO A 1 272  ? 22.547 58.907  18.888  1.00 10.03 ? 272  PRO A CB  1 
ATOM   2056 C  CG  . PRO A 1 272  ? 23.475 59.740  19.718  1.00 11.96 ? 272  PRO A CG  1 
ATOM   2057 C  CD  . PRO A 1 272  ? 24.879 59.148  19.403  1.00 10.99 ? 272  PRO A CD  1 
ATOM   2058 N  N   . HIS A 1 273  ? 23.578 56.419  16.910  1.00 11.51 ? 273  HIS A N   1 
ATOM   2059 C  CA  . HIS A 1 273  ? 23.202 55.576  15.792  1.00 10.37 ? 273  HIS A CA  1 
ATOM   2060 C  C   . HIS A 1 273  ? 24.126 54.358  15.606  1.00 10.92 ? 273  HIS A C   1 
ATOM   2061 O  O   . HIS A 1 273  ? 24.211 53.809  14.496  1.00 10.39 ? 273  HIS A O   1 
ATOM   2062 C  CB  . HIS A 1 273  ? 23.125 56.403  14.489  1.00 10.17 ? 273  HIS A CB  1 
ATOM   2063 C  CG  . HIS A 1 273  ? 22.060 57.456  14.538  1.00 11.80 ? 273  HIS A CG  1 
ATOM   2064 N  ND1 . HIS A 1 273  ? 22.288 58.724  15.034  1.00 11.94 ? 273  HIS A ND1 1 
ATOM   2065 C  CD2 . HIS A 1 273  ? 20.740 57.402  14.225  1.00 11.25 ? 273  HIS A CD2 1 
ATOM   2066 C  CE1 . HIS A 1 273  ? 21.143 59.402  15.030  1.00 13.35 ? 273  HIS A CE1 1 
ATOM   2067 N  NE2 . HIS A 1 273  ? 20.196 58.623  14.551  1.00 8.74  ? 273  HIS A NE2 1 
ATOM   2068 N  N   . THR A 1 274  ? 24.829 53.990  16.663  1.00 10.34 ? 274  THR A N   1 
ATOM   2069 C  CA  . THR A 1 274  ? 25.717 52.859  16.539  1.00 10.63 ? 274  THR A CA  1 
ATOM   2070 C  C   . THR A 1 274  ? 25.454 51.770  17.563  1.00 11.45 ? 274  THR A C   1 
ATOM   2071 O  O   . THR A 1 274  ? 25.931 50.658  17.405  1.00 10.43 ? 274  THR A O   1 
ATOM   2072 C  CB  . THR A 1 274  ? 27.238 53.272  16.548  1.00 10.51 ? 274  THR A CB  1 
ATOM   2073 O  OG1 . THR A 1 274  ? 27.492 54.229  17.582  1.00 9.34  ? 274  THR A OG1 1 
ATOM   2074 C  CG2 . THR A 1 274  ? 27.637 53.785  15.164  1.00 9.40  ? 274  THR A CG2 1 
ATOM   2075 N  N   . CYS A 1 275  ? 24.699 52.023  18.621  1.00 10.84 ? 275  CYS A N   1 
ATOM   2076 C  CA  . CYS A 1 275  ? 24.446 50.922  19.541  1.00 12.05 ? 275  CYS A CA  1 
ATOM   2077 C  C   . CYS A 1 275  ? 23.265 50.000  19.177  1.00 11.01 ? 275  CYS A C   1 
ATOM   2078 O  O   . CYS A 1 275  ? 23.217 48.885  19.673  1.00 12.47 ? 275  CYS A O   1 
ATOM   2079 C  CB  . CYS A 1 275  ? 24.191 51.427  20.978  1.00 11.96 ? 275  CYS A CB  1 
ATOM   2080 S  SG  . CYS A 1 275  ? 22.417 51.592  21.512  1.00 14.20 ? 275  CYS A SG  1 
ATOM   2081 N  N   . GLY A 1 276  ? 22.374 50.456  18.298  1.00 11.59 ? 276  GLY A N   1 
ATOM   2082 C  CA  . GLY A 1 276  ? 21.156 49.731  17.953  1.00 10.54 ? 276  GLY A CA  1 
ATOM   2083 C  C   . GLY A 1 276  ? 20.276 50.674  17.156  1.00 11.56 ? 276  GLY A C   1 
ATOM   2084 O  O   . GLY A 1 276  ? 20.617 51.839  16.916  1.00 10.84 ? 276  GLY A O   1 
ATOM   2085 N  N   . PRO A 1 277  ? 19.069 50.237  16.827  1.00 11.39 ? 277  PRO A N   1 
ATOM   2086 C  CA  . PRO A 1 277  ? 18.102 51.009  16.029  1.00 10.63 ? 277  PRO A CA  1 
ATOM   2087 C  C   . PRO A 1 277  ? 17.410 52.223  16.668  1.00 10.67 ? 277  PRO A C   1 
ATOM   2088 O  O   . PRO A 1 277  ? 16.855 53.013  15.936  1.00 11.91 ? 277  PRO A O   1 
ATOM   2089 C  CB  . PRO A 1 277  ? 17.054 49.923  15.621  1.00 11.54 ? 277  PRO A CB  1 
ATOM   2090 C  CG  . PRO A 1 277  ? 17.089 49.002  16.927  1.00 10.96 ? 277  PRO A CG  1 
ATOM   2091 C  CD  . PRO A 1 277  ? 18.540 48.891  17.175  1.00 11.55 ? 277  PRO A CD  1 
ATOM   2092 N  N   . ASP A 1 278  ? 17.431 52.336  17.993  1.00 13.08 ? 278  ASP A N   1 
ATOM   2093 C  CA  . ASP A 1 278  ? 16.725 53.450  18.687  1.00 12.69 ? 278  ASP A CA  1 
ATOM   2094 C  C   . ASP A 1 278  ? 17.711 54.489  19.250  1.00 13.35 ? 278  ASP A C   1 
ATOM   2095 O  O   . ASP A 1 278  ? 18.293 54.288  20.326  1.00 12.11 ? 278  ASP A O   1 
ATOM   2096 C  CB  . ASP A 1 278  ? 15.851 52.910  19.824  1.00 13.20 ? 278  ASP A CB  1 
ATOM   2097 C  CG  . ASP A 1 278  ? 14.929 53.991  20.382  1.00 13.32 ? 278  ASP A CG  1 
ATOM   2098 O  OD1 . ASP A 1 278  ? 15.116 55.187  20.034  1.00 15.07 ? 278  ASP A OD1 1 
ATOM   2099 O  OD2 . ASP A 1 278  ? 13.996 53.630  21.121  1.00 15.38 ? 278  ASP A OD2 1 
ATOM   2100 N  N   . PRO A 1 279  ? 17.813 55.636  18.558  1.00 12.83 ? 279  PRO A N   1 
ATOM   2101 C  CA  . PRO A 1 279  ? 18.764 56.638  19.038  1.00 14.33 ? 279  PRO A CA  1 
ATOM   2102 C  C   . PRO A 1 279  ? 18.391 57.228  20.378  1.00 13.95 ? 279  PRO A C   1 
ATOM   2103 O  O   . PRO A 1 279  ? 19.263 57.693  21.126  1.00 15.03 ? 279  PRO A O   1 
ATOM   2104 C  CB  . PRO A 1 279  ? 18.842 57.651  17.863  1.00 12.86 ? 279  PRO A CB  1 
ATOM   2105 C  CG  . PRO A 1 279  ? 17.471 57.580  17.254  1.00 12.46 ? 279  PRO A CG  1 
ATOM   2106 C  CD  . PRO A 1 279  ? 17.092 56.080  17.336  1.00 13.97 ? 279  PRO A CD  1 
ATOM   2107 N  N   . LYS A 1 280  ? 17.104 57.186  20.734  1.00 14.54 ? 280  LYS A N   1 
ATOM   2108 C  CA  . LYS A 1 280  ? 16.737 57.724  22.050  1.00 14.73 ? 280  LYS A CA  1 
ATOM   2109 C  C   . LYS A 1 280  ? 17.339 56.888  23.151  1.00 15.07 ? 280  LYS A C   1 
ATOM   2110 O  O   . LYS A 1 280  ? 17.630 57.408  24.222  1.00 14.87 ? 280  LYS A O   1 
ATOM   2111 C  CB  . LYS A 1 280  ? 15.210 57.785  22.218  1.00 16.45 ? 280  LYS A CB  1 
ATOM   2112 C  CG  . LYS A 1 280  ? 14.748 58.181  23.619  1.00 19.98 ? 280  LYS A CG  1 
ATOM   2113 C  CD  . LYS A 1 280  ? 13.248 58.462  23.662  1.00 23.84 ? 280  LYS A CD  1 
ATOM   2114 C  CE  . LYS A 1 280  ? 12.781 58.468  25.114  1.00 25.61 ? 280  LYS A CE  1 
ATOM   2115 N  NZ  . LYS A 1 280  ? 13.228 57.189  25.788  1.00 30.26 ? 280  LYS A NZ  1 
ATOM   2116 N  N   . VAL A 1 281  ? 17.509 55.574  22.935  1.00 12.89 ? 281  VAL A N   1 
ATOM   2117 C  CA  . VAL A 1 281  ? 18.146 54.713  23.912  1.00 14.38 ? 281  VAL A CA  1 
ATOM   2118 C  C   . VAL A 1 281  ? 19.684 54.826  23.775  1.00 13.26 ? 281  VAL A C   1 
ATOM   2119 O  O   . VAL A 1 281  ? 20.376 54.979  24.802  1.00 14.61 ? 281  VAL A O   1 
ATOM   2120 C  CB  . VAL A 1 281  ? 17.685 53.224  23.699  1.00 14.66 ? 281  VAL A CB  1 
ATOM   2121 C  CG1 . VAL A 1 281  ? 18.388 52.275  24.649  1.00 16.24 ? 281  VAL A CG1 1 
ATOM   2122 C  CG2 . VAL A 1 281  ? 16.135 53.169  23.833  1.00 17.08 ? 281  VAL A CG2 1 
ATOM   2123 N  N   . CYS A 1 282  ? 20.211 54.765  22.537  1.00 13.45 ? 282  CYS A N   1 
ATOM   2124 C  CA  . CYS A 1 282  ? 21.689 54.807  22.378  1.00 11.92 ? 282  CYS A CA  1 
ATOM   2125 C  C   . CYS A 1 282  ? 22.336 56.062  22.862  1.00 12.47 ? 282  CYS A C   1 
ATOM   2126 O  O   . CYS A 1 282  ? 23.454 55.996  23.436  1.00 12.16 ? 282  CYS A O   1 
ATOM   2127 C  CB  . CYS A 1 282  ? 22.124 54.556  20.929  1.00 12.11 ? 282  CYS A CB  1 
ATOM   2128 S  SG  . CYS A 1 282  ? 21.591 52.936  20.254  1.00 13.88 ? 282  CYS A SG  1 
ATOM   2129 N  N   . CYS A 1 283  ? 21.625 57.188  22.692  1.00 12.51 ? 283  CYS A N   1 
ATOM   2130 C  CA  . CYS A 1 283  ? 22.150 58.454  23.163  1.00 13.57 ? 283  CYS A CA  1 
ATOM   2131 C  C   . CYS A 1 283  ? 22.417 58.362  24.662  1.00 12.96 ? 283  CYS A C   1 
ATOM   2132 O  O   . CYS A 1 283  ? 23.332 59.003  25.141  1.00 13.07 ? 283  CYS A O   1 
ATOM   2133 C  CB  . CYS A 1 283  ? 21.165 59.602  22.841  1.00 12.52 ? 283  CYS A CB  1 
ATOM   2134 S  SG  . CYS A 1 283  ? 22.032 61.209  22.990  1.00 17.20 ? 283  CYS A SG  1 
ATOM   2135 N  N   . GLN A 1 284  ? 21.640 57.566  25.406  1.00 13.65 ? 284  GLN A N   1 
ATOM   2136 C  CA  . GLN A 1 284  ? 21.881 57.414  26.828  1.00 13.09 ? 284  GLN A CA  1 
ATOM   2137 C  C   . GLN A 1 284  ? 23.161 56.662  27.189  1.00 13.42 ? 284  GLN A C   1 
ATOM   2138 O  O   . GLN A 1 284  ? 23.529 56.575  28.371  1.00 13.91 ? 284  GLN A O   1 
ATOM   2139 C  CB  . GLN A 1 284  ? 20.662 56.758  27.501  1.00 15.15 ? 284  GLN A CB  1 
ATOM   2140 C  CG  . GLN A 1 284  ? 19.360 57.490  27.249  1.00 15.06 ? 284  GLN A CG  1 
ATOM   2141 C  CD  . GLN A 1 284  ? 18.172 56.739  27.800  1.00 17.80 ? 284  GLN A CD  1 
ATOM   2142 O  OE1 . GLN A 1 284  ? 18.171 56.338  28.956  1.00 17.63 ? 284  GLN A OE1 1 
ATOM   2143 N  NE2 . GLN A 1 284  ? 17.153 56.533  26.966  1.00 16.95 ? 284  GLN A NE2 1 
ATOM   2144 N  N   . PHE A 1 285  ? 23.866 56.161  26.154  1.00 12.03 ? 285  PHE A N   1 
ATOM   2145 C  CA  . PHE A 1 285  ? 25.111 55.456  26.360  1.00 12.34 ? 285  PHE A CA  1 
ATOM   2146 C  C   . PHE A 1 285  ? 26.314 56.171  25.756  1.00 11.85 ? 285  PHE A C   1 
ATOM   2147 O  O   . PHE A 1 285  ? 27.391 55.597  25.604  1.00 13.32 ? 285  PHE A O   1 
ATOM   2148 C  CB  . PHE A 1 285  ? 24.957 53.994  25.915  1.00 12.57 ? 285  PHE A CB  1 
ATOM   2149 C  CG  . PHE A 1 285  ? 23.931 53.233  26.771  1.00 12.77 ? 285  PHE A CG  1 
ATOM   2150 C  CD1 . PHE A 1 285  ? 24.308 52.647  27.980  1.00 10.52 ? 285  PHE A CD1 1 
ATOM   2151 C  CD2 . PHE A 1 285  ? 22.576 53.217  26.391  1.00 11.62 ? 285  PHE A CD2 1 
ATOM   2152 C  CE1 . PHE A 1 285  ? 23.347 52.062  28.825  1.00 13.83 ? 285  PHE A CE1 1 
ATOM   2153 C  CE2 . PHE A 1 285  ? 21.615 52.633  27.211  1.00 15.31 ? 285  PHE A CE2 1 
ATOM   2154 C  CZ  . PHE A 1 285  ? 22.002 52.065  28.432  1.00 12.61 ? 285  PHE A CZ  1 
ATOM   2155 N  N   . ASP A 1 286  ? 26.116 57.467  25.527  1.00 12.35 ? 286  ASP A N   1 
ATOM   2156 C  CA  . ASP A 1 286  ? 27.212 58.344  25.134  1.00 11.17 ? 286  ASP A CA  1 
ATOM   2157 C  C   . ASP A 1 286  ? 27.441 59.164  26.434  1.00 10.33 ? 286  ASP A C   1 
ATOM   2158 O  O   . ASP A 1 286  ? 26.756 60.167  26.687  1.00 12.34 ? 286  ASP A O   1 
ATOM   2159 C  CB  . ASP A 1 286  ? 26.777 59.232  23.991  1.00 11.00 ? 286  ASP A CB  1 
ATOM   2160 C  CG  . ASP A 1 286  ? 27.901 60.141  23.485  1.00 10.03 ? 286  ASP A CG  1 
ATOM   2161 O  OD1 . ASP A 1 286  ? 28.943 60.219  24.206  1.00 12.26 ? 286  ASP A OD1 1 
ATOM   2162 O  OD2 . ASP A 1 286  ? 27.701 60.761  22.435  1.00 13.19 ? 286  ASP A OD2 1 
ATOM   2163 N  N   . PHE A 1 287  ? 28.419 58.756  27.231  1.00 11.22 ? 287  PHE A N   1 
ATOM   2164 C  CA  . PHE A 1 287  ? 28.618 59.396  28.508  1.00 11.14 ? 287  PHE A CA  1 
ATOM   2165 C  C   . PHE A 1 287  ? 29.208 60.778  28.511  1.00 12.89 ? 287  PHE A C   1 
ATOM   2166 O  O   . PHE A 1 287  ? 29.331 61.366  29.598  1.00 14.34 ? 287  PHE A O   1 
ATOM   2167 C  CB  . PHE A 1 287  ? 29.349 58.428  29.457  1.00 12.66 ? 287  PHE A CB  1 
ATOM   2168 C  CG  . PHE A 1 287  ? 28.546 57.172  29.728  1.00 14.53 ? 287  PHE A CG  1 
ATOM   2169 C  CD1 . PHE A 1 287  ? 27.553 57.177  30.729  1.00 14.52 ? 287  PHE A CD1 1 
ATOM   2170 C  CD2 . PHE A 1 287  ? 28.698 56.031  28.953  1.00 13.96 ? 287  PHE A CD2 1 
ATOM   2171 C  CE1 . PHE A 1 287  ? 26.727 56.062  30.938  1.00 15.74 ? 287  PHE A CE1 1 
ATOM   2172 C  CE2 . PHE A 1 287  ? 27.863 54.910  29.178  1.00 14.75 ? 287  PHE A CE2 1 
ATOM   2173 C  CZ  . PHE A 1 287  ? 26.873 54.940  30.179  1.00 15.56 ? 287  PHE A CZ  1 
ATOM   2174 N  N   . LYS A 1 288  ? 29.491 61.298  27.312  1.00 13.19 ? 288  LYS A N   1 
ATOM   2175 C  CA  . LYS A 1 288  ? 29.991 62.670  27.185  1.00 14.00 ? 288  LYS A CA  1 
ATOM   2176 C  C   . LYS A 1 288  ? 28.759 63.611  27.130  1.00 13.99 ? 288  LYS A C   1 
ATOM   2177 O  O   . LYS A 1 288  ? 28.893 64.808  27.127  1.00 15.12 ? 288  LYS A O   1 
ATOM   2178 C  CB  . LYS A 1 288  ? 30.839 62.847  25.898  1.00 12.15 ? 288  LYS A CB  1 
ATOM   2179 C  CG  . LYS A 1 288  ? 31.739 64.065  25.948  1.00 12.90 ? 288  LYS A CG  1 
ATOM   2180 C  CD  . LYS A 1 288  ? 32.558 64.260  24.705  1.00 10.71 ? 288  LYS A CD  1 
ATOM   2181 C  CE  . LYS A 1 288  ? 33.456 65.471  24.965  1.00 13.83 ? 288  LYS A CE  1 
ATOM   2182 N  NZ  . LYS A 1 288  ? 34.424 65.736  23.824  1.00 14.61 ? 288  LYS A NZ  1 
ATOM   2183 N  N   . ARG A 1 289  ? 27.545 63.068  27.106  1.00 16.02 ? 289  ARG A N   1 
ATOM   2184 C  CA  . ARG A 1 289  ? 26.381 63.923  27.006  1.00 16.97 ? 289  ARG A CA  1 
ATOM   2185 C  C   . ARG A 1 289  ? 25.581 64.223  28.284  1.00 17.37 ? 289  ARG A C   1 
ATOM   2186 O  O   . ARG A 1 289  ? 24.398 64.513  28.147  1.00 17.40 ? 289  ARG A O   1 
ATOM   2187 C  CB  . ARG A 1 289  ? 25.418 63.361  25.952  1.00 14.43 ? 289  ARG A CB  1 
ATOM   2188 C  CG  . ARG A 1 289  ? 26.014 63.267  24.539  1.00 15.02 ? 289  ARG A CG  1 
ATOM   2189 C  CD  . ARG A 1 289  ? 25.004 62.716  23.583  1.00 13.19 ? 289  ARG A CD  1 
ATOM   2190 N  NE  . ARG A 1 289  ? 25.535 62.446  22.252  1.00 12.32 ? 289  ARG A NE  1 
ATOM   2191 C  CZ  . ARG A 1 289  ? 25.125 63.026  21.143  1.00 12.53 ? 289  ARG A CZ  1 
ATOM   2192 N  NH1 . ARG A 1 289  ? 24.179 63.963  21.152  1.00 13.59 ? 289  ARG A NH1 1 
ATOM   2193 N  NH2 . ARG A 1 289  ? 25.577 62.615  19.989  1.00 12.02 ? 289  ARG A NH2 1 
ATOM   2194 N  N   . MET A 1 290  ? 26.183 64.194  29.480  1.00 21.31 ? 290  MET A N   1 
ATOM   2195 C  CA  . MET A 1 290  ? 25.438 64.469  30.727  1.00 24.23 ? 290  MET A CA  1 
ATOM   2196 C  C   . MET A 1 290  ? 25.462 65.911  31.212  1.00 25.52 ? 290  MET A C   1 
ATOM   2197 O  O   . MET A 1 290  ? 24.797 66.240  32.231  1.00 28.19 ? 290  MET A O   1 
ATOM   2198 C  CB  . MET A 1 290  ? 25.898 63.568  31.868  1.00 24.24 ? 290  MET A CB  1 
ATOM   2199 C  CG  . MET A 1 290  ? 25.656 62.091  31.572  1.00 25.88 ? 290  MET A CG  1 
ATOM   2200 S  SD  . MET A 1 290  ? 26.214 60.950  32.872  1.00 26.72 ? 290  MET A SD  1 
ATOM   2201 C  CE  . MET A 1 290  ? 27.916 61.079  32.752  1.00 24.49 ? 290  MET A CE  1 
ATOM   2202 N  N   . GLY A 1 291  ? 26.212 66.783  30.530  1.00 24.60 ? 291  GLY A N   1 
ATOM   2203 C  CA  . GLY A 1 291  ? 26.207 68.175  30.954  1.00 24.07 ? 291  GLY A CA  1 
ATOM   2204 C  C   . GLY A 1 291  ? 27.463 69.040  30.957  1.00 22.99 ? 291  GLY A C   1 
ATOM   2205 O  O   . GLY A 1 291  ? 27.509 70.083  30.282  1.00 23.10 ? 291  GLY A O   1 
ATOM   2206 N  N   . SER A 1 292  ? 28.452 68.609  31.730  1.00 21.87 ? 292  SER A N   1 
ATOM   2207 C  CA  . SER A 1 292  ? 29.705 69.321  31.875  1.00 19.78 ? 292  SER A CA  1 
ATOM   2208 C  C   . SER A 1 292  ? 30.536 69.518  30.581  1.00 19.69 ? 292  SER A C   1 
ATOM   2209 O  O   . SER A 1 292  ? 31.458 70.347  30.529  1.00 17.54 ? 292  SER A O   1 
ATOM   2210 C  CB  . SER A 1 292  ? 30.534 68.611  32.921  1.00 20.12 ? 292  SER A CB  1 
ATOM   2211 O  OG  . SER A 1 292  ? 30.931 67.355  32.396  1.00 19.18 ? 292  SER A OG  1 
ATOM   2212 N  N   . PHE A 1 293  ? 30.220 68.749  29.537  1.00 17.49 ? 293  PHE A N   1 
ATOM   2213 C  CA  . PHE A 1 293  ? 30.890 68.844  28.242  1.00 17.46 ? 293  PHE A CA  1 
ATOM   2214 C  C   . PHE A 1 293  ? 30.102 69.646  27.233  1.00 16.89 ? 293  PHE A C   1 
ATOM   2215 O  O   . PHE A 1 293  ? 30.514 69.756  26.072  1.00 18.40 ? 293  PHE A O   1 
ATOM   2216 C  CB  . PHE A 1 293  ? 31.105 67.426  27.655  1.00 17.00 ? 293  PHE A CB  1 
ATOM   2217 C  CG  . PHE A 1 293  ? 32.033 66.595  28.443  1.00 14.94 ? 293  PHE A CG  1 
ATOM   2218 C  CD1 . PHE A 1 293  ? 33.406 66.763  28.322  1.00 17.10 ? 293  PHE A CD1 1 
ATOM   2219 C  CD2 . PHE A 1 293  ? 31.531 65.653  29.356  1.00 15.50 ? 293  PHE A CD2 1 
ATOM   2220 C  CE1 . PHE A 1 293  ? 34.301 66.001  29.099  1.00 17.29 ? 293  PHE A CE1 1 
ATOM   2221 C  CE2 . PHE A 1 293  ? 32.410 64.880  30.146  1.00 14.58 ? 293  PHE A CE2 1 
ATOM   2222 C  CZ  . PHE A 1 293  ? 33.806 65.062  30.011  1.00 14.89 ? 293  PHE A CZ  1 
ATOM   2223 N  N   . GLY A 1 294  ? 28.958 70.204  27.643  1.00 18.83 ? 294  GLY A N   1 
ATOM   2224 C  CA  . GLY A 1 294  ? 28.184 70.990  26.691  1.00 20.40 ? 294  GLY A CA  1 
ATOM   2225 C  C   . GLY A 1 294  ? 27.530 70.230  25.544  1.00 21.23 ? 294  GLY A C   1 
ATOM   2226 O  O   . GLY A 1 294  ? 27.250 70.787  24.444  1.00 23.90 ? 294  GLY A O   1 
ATOM   2227 N  N   . LEU A 1 295  ? 27.278 68.953  25.772  1.00 18.27 ? 295  LEU A N   1 
ATOM   2228 C  CA  . LEU A 1 295  ? 26.583 68.158  24.758  1.00 16.47 ? 295  LEU A CA  1 
ATOM   2229 C  C   . LEU A 1 295  ? 25.377 67.590  25.511  1.00 16.31 ? 295  LEU A C   1 
ATOM   2230 O  O   . LEU A 1 295  ? 25.419 67.409  26.741  1.00 13.73 ? 295  LEU A O   1 
ATOM   2231 C  CB  . LEU A 1 295  ? 27.495 67.062  24.258  1.00 16.30 ? 295  LEU A CB  1 
ATOM   2232 C  CG  . LEU A 1 295  ? 28.818 67.464  23.574  1.00 14.58 ? 295  LEU A CG  1 
ATOM   2233 C  CD1 . LEU A 1 295  ? 29.592 66.191  23.297  1.00 15.39 ? 295  LEU A CD1 1 
ATOM   2234 C  CD2 . LEU A 1 295  ? 28.559 68.215  22.250  1.00 15.95 ? 295  LEU A CD2 1 
ATOM   2235 N  N   . SER A 1 296  ? 24.303 67.323  24.788  1.00 15.39 ? 296  SER A N   1 
ATOM   2236 C  CA  . SER A 1 296  ? 23.094 66.812  25.406  1.00 15.84 ? 296  SER A CA  1 
ATOM   2237 C  C   . SER A 1 296  ? 22.478 65.836  24.421  1.00 16.40 ? 296  SER A C   1 
ATOM   2238 O  O   . SER A 1 296  ? 23.002 65.677  23.317  1.00 15.89 ? 296  SER A O   1 
ATOM   2239 C  CB  . SER A 1 296  ? 22.122 67.977  25.662  1.00 12.39 ? 296  SER A CB  1 
ATOM   2240 O  OG  . SER A 1 296  ? 21.883 68.653  24.464  1.00 16.68 ? 296  SER A OG  1 
ATOM   2241 N  N   . CYS A 1 297  ? 21.365 65.197  24.806  1.00 17.70 ? 297  CYS A N   1 
ATOM   2242 C  CA  . CYS A 1 297  ? 20.644 64.270  23.911  1.00 18.08 ? 297  CYS A CA  1 
ATOM   2243 C  C   . CYS A 1 297  ? 19.396 64.932  23.300  1.00 17.52 ? 297  CYS A C   1 
ATOM   2244 O  O   . CYS A 1 297  ? 18.484 65.306  24.038  1.00 20.90 ? 297  CYS A O   1 
ATOM   2245 C  CB  . CYS A 1 297  ? 20.223 63.009  24.667  1.00 18.86 ? 297  CYS A CB  1 
ATOM   2246 S  SG  . CYS A 1 297  ? 21.635 61.865  24.911  1.00 19.56 ? 297  CYS A SG  1 
ATOM   2247 N  N   . PRO A 1 298  ? 19.303 65.007  21.970  1.00 19.51 ? 298  PRO A N   1 
ATOM   2248 C  CA  . PRO A 1 298  ? 18.109 65.654  21.416  1.00 18.05 ? 298  PRO A CA  1 
ATOM   2249 C  C   . PRO A 1 298  ? 16.798 64.879  21.558  1.00 20.18 ? 298  PRO A C   1 
ATOM   2250 O  O   . PRO A 1 298  ? 15.701 65.449  21.280  1.00 18.99 ? 298  PRO A O   1 
ATOM   2251 C  CB  . PRO A 1 298  ? 18.493 65.911  19.965  1.00 19.84 ? 298  PRO A CB  1 
ATOM   2252 C  CG  . PRO A 1 298  ? 19.418 64.839  19.655  1.00 20.01 ? 298  PRO A CG  1 
ATOM   2253 C  CD  . PRO A 1 298  ? 20.274 64.714  20.899  1.00 18.09 ? 298  PRO A CD  1 
ATOM   2254 N  N   . TRP A 1 299  ? 16.904 63.617  21.989  1.00 18.39 ? 299  TRP A N   1 
ATOM   2255 C  CA  . TRP A 1 299  ? 15.713 62.776  22.149  1.00 20.07 ? 299  TRP A CA  1 
ATOM   2256 C  C   . TRP A 1 299  ? 15.199 62.966  23.563  1.00 21.78 ? 299  TRP A C   1 
ATOM   2257 O  O   . TRP A 1 299  ? 14.291 62.248  24.024  1.00 21.59 ? 299  TRP A O   1 
ATOM   2258 C  CB  . TRP A 1 299  ? 16.024 61.296  21.843  1.00 18.41 ? 299  TRP A CB  1 
ATOM   2259 C  CG  . TRP A 1 299  ? 16.390 61.073  20.403  1.00 16.46 ? 299  TRP A CG  1 
ATOM   2260 C  CD1 . TRP A 1 299  ? 15.562 60.861  19.355  1.00 15.99 ? 299  TRP A CD1 1 
ATOM   2261 C  CD2 . TRP A 1 299  ? 17.710 61.195  19.848  1.00 15.02 ? 299  TRP A CD2 1 
ATOM   2262 N  NE1 . TRP A 1 299  ? 16.270 60.844  18.162  1.00 16.18 ? 299  TRP A NE1 1 
ATOM   2263 C  CE2 . TRP A 1 299  ? 17.598 61.058  18.445  1.00 16.08 ? 299  TRP A CE2 1 
ATOM   2264 C  CE3 . TRP A 1 299  ? 18.970 61.416  20.411  1.00 13.89 ? 299  TRP A CE3 1 
ATOM   2265 C  CZ2 . TRP A 1 299  ? 18.710 61.141  17.587  1.00 15.28 ? 299  TRP A CZ2 1 
ATOM   2266 C  CZ3 . TRP A 1 299  ? 20.064 61.497  19.558  1.00 13.65 ? 299  TRP A CZ3 1 
ATOM   2267 C  CH2 . TRP A 1 299  ? 19.928 61.366  18.180  1.00 14.31 ? 299  TRP A CH2 1 
ATOM   2268 N  N   . LYS A 1 300  ? 15.805 63.942  24.261  1.00 22.46 ? 300  LYS A N   1 
ATOM   2269 C  CA  . LYS A 1 300  ? 15.368 64.324  25.605  1.00 24.25 ? 300  LYS A CA  1 
ATOM   2270 C  C   . LYS A 1 300  ? 15.605 63.431  26.821  1.00 23.05 ? 300  LYS A C   1 
ATOM   2271 O  O   . LYS A 1 300  ? 15.123 63.735  27.928  1.00 23.99 ? 300  LYS A O   1 
ATOM   2272 C  CB  . LYS A 1 300  ? 13.873 64.705  25.526  1.00 26.05 ? 300  LYS A CB  1 
ATOM   2273 C  CG  . LYS A 1 300  ? 13.623 65.759  24.515  1.00 27.64 ? 300  LYS A CG  1 
ATOM   2274 C  CD  . LYS A 1 300  ? 12.141 66.032  24.309  1.00 29.98 ? 300  LYS A CD  1 
ATOM   2275 C  CE  . LYS A 1 300  ? 11.961 66.966  23.098  1.00 30.95 ? 300  LYS A CE  1 
ATOM   2276 N  NZ  . LYS A 1 300  ? 10.536 67.143  22.645  1.00 32.58 ? 300  LYS A NZ  1 
ATOM   2277 N  N   . VAL A 1 301  ? 16.348 62.346  26.673  1.00 21.96 ? 301  VAL A N   1 
ATOM   2278 C  CA  . VAL A 1 301  ? 16.628 61.507  27.832  1.00 21.59 ? 301  VAL A CA  1 
ATOM   2279 C  C   . VAL A 1 301  ? 18.154 61.458  27.910  1.00 21.97 ? 301  VAL A C   1 
ATOM   2280 O  O   . VAL A 1 301  ? 18.825 60.917  27.044  1.00 22.84 ? 301  VAL A O   1 
ATOM   2281 C  CB  . VAL A 1 301  ? 16.042 60.075  27.696  1.00 22.09 ? 301  VAL A CB  1 
ATOM   2282 C  CG1 . VAL A 1 301  ? 16.382 59.266  28.915  1.00 20.69 ? 301  VAL A CG1 1 
ATOM   2283 C  CG2 . VAL A 1 301  ? 14.508 60.164  27.461  1.00 23.12 ? 301  VAL A CG2 1 
ATOM   2284 N  N   . PRO A 1 302  ? 18.719 61.991  28.970  1.00 22.14 ? 302  PRO A N   1 
ATOM   2285 C  CA  . PRO A 1 302  ? 20.171 61.996  29.071  1.00 21.80 ? 302  PRO A CA  1 
ATOM   2286 C  C   . PRO A 1 302  ? 20.812 60.743  29.600  1.00 21.77 ? 302  PRO A C   1 
ATOM   2287 O  O   . PRO A 1 302  ? 20.168 59.871  30.177  1.00 21.99 ? 302  PRO A O   1 
ATOM   2288 C  CB  . PRO A 1 302  ? 20.408 63.145  30.006  1.00 21.77 ? 302  PRO A CB  1 
ATOM   2289 C  CG  . PRO A 1 302  ? 19.306 62.863  31.055  1.00 23.96 ? 302  PRO A CG  1 
ATOM   2290 C  CD  . PRO A 1 302  ? 18.100 62.554  30.184  1.00 22.81 ? 302  PRO A CD  1 
ATOM   2291 N  N   . PRO A 1 303  ? 22.122 60.629  29.397  1.00 19.58 ? 303  PRO A N   1 
ATOM   2292 C  CA  . PRO A 1 303  ? 22.750 59.436  29.942  1.00 20.35 ? 303  PRO A CA  1 
ATOM   2293 C  C   . PRO A 1 303  ? 22.791 59.630  31.469  1.00 21.44 ? 303  PRO A C   1 
ATOM   2294 O  O   . PRO A 1 303  ? 22.676 60.763  31.991  1.00 20.97 ? 303  PRO A O   1 
ATOM   2295 C  CB  . PRO A 1 303  ? 24.144 59.458  29.314  1.00 19.94 ? 303  PRO A CB  1 
ATOM   2296 C  CG  . PRO A 1 303  ? 24.370 60.863  28.914  1.00 20.54 ? 303  PRO A CG  1 
ATOM   2297 C  CD  . PRO A 1 303  ? 23.034 61.409  28.534  1.00 20.40 ? 303  PRO A CD  1 
ATOM   2298 N  N   . ARG A 1 304  ? 22.938 58.537  32.181  1.00 21.27 ? 304  ARG A N   1 
ATOM   2299 C  CA  . ARG A 1 304  ? 23.024 58.606  33.611  1.00 23.02 ? 304  ARG A CA  1 
ATOM   2300 C  C   . ARG A 1 304  ? 24.175 57.716  33.994  1.00 22.34 ? 304  ARG A C   1 
ATOM   2301 O  O   . ARG A 1 304  ? 24.388 56.654  33.374  1.00 20.77 ? 304  ARG A O   1 
ATOM   2302 C  CB  . ARG A 1 304  ? 21.730 58.116  34.253  1.00 26.26 ? 304  ARG A CB  1 
ATOM   2303 C  CG  . ARG A 1 304  ? 20.537 59.008  34.012  1.00 30.15 ? 304  ARG A CG  1 
ATOM   2304 C  CD  . ARG A 1 304  ? 19.434 58.613  34.959  1.00 35.28 ? 304  ARG A CD  1 
ATOM   2305 N  NE  . ARG A 1 304  ? 19.332 57.155  35.049  1.00 39.02 ? 304  ARG A NE  1 
ATOM   2306 C  CZ  . ARG A 1 304  ? 18.567 56.394  34.267  1.00 40.39 ? 304  ARG A CZ  1 
ATOM   2307 N  NH1 . ARG A 1 304  ? 17.808 56.941  33.323  1.00 41.36 ? 304  ARG A NH1 1 
ATOM   2308 N  NH2 . ARG A 1 304  ? 18.579 55.074  34.427  1.00 42.16 ? 304  ARG A NH2 1 
ATOM   2309 N  N   . THR A 1 305  ? 24.931 58.142  34.999  1.00 21.62 ? 305  THR A N   1 
ATOM   2310 C  CA  . THR A 1 305  ? 26.062 57.384  35.450  1.00 21.94 ? 305  THR A CA  1 
ATOM   2311 C  C   . THR A 1 305  ? 25.644 55.981  35.831  1.00 21.46 ? 305  THR A C   1 
ATOM   2312 O  O   . THR A 1 305  ? 24.585 55.774  36.434  1.00 22.86 ? 305  THR A O   1 
ATOM   2313 C  CB  . THR A 1 305  ? 26.755 58.091  36.629  1.00 21.73 ? 305  THR A CB  1 
ATOM   2314 O  OG1 . THR A 1 305  ? 27.180 59.384  36.182  1.00 26.02 ? 305  THR A OG1 1 
ATOM   2315 C  CG2 . THR A 1 305  ? 27.951 57.311  37.137  1.00 22.10 ? 305  THR A CG2 1 
ATOM   2316 N  N   . ILE A 1 306  ? 26.438 54.998  35.438  1.00 18.77 ? 306  ILE A N   1 
ATOM   2317 C  CA  . ILE A 1 306  ? 26.124 53.626  35.753  1.00 17.63 ? 306  ILE A CA  1 
ATOM   2318 C  C   . ILE A 1 306  ? 26.511 53.358  37.218  1.00 17.59 ? 306  ILE A C   1 
ATOM   2319 O  O   . ILE A 1 306  ? 27.583 53.756  37.669  1.00 17.88 ? 306  ILE A O   1 
ATOM   2320 C  CB  . ILE A 1 306  ? 26.864 52.620  34.788  1.00 16.00 ? 306  ILE A CB  1 
ATOM   2321 C  CG1 . ILE A 1 306  ? 26.506 52.893  33.317  1.00 15.44 ? 306  ILE A CG1 1 
ATOM   2322 C  CG2 . ILE A 1 306  ? 26.518 51.162  35.159  1.00 14.56 ? 306  ILE A CG2 1 
ATOM   2323 C  CD1 . ILE A 1 306  ? 25.043 52.823  33.016  1.00 12.99 ? 306  ILE A CD1 1 
ATOM   2324 N  N   . SER A 1 307  ? 25.600 52.727  37.965  1.00 18.65 ? 307  SER A N   1 
ATOM   2325 C  CA  . SER A 1 307  ? 25.827 52.432  39.383  1.00 20.46 ? 307  SER A CA  1 
ATOM   2326 C  C   . SER A 1 307  ? 25.292 51.035  39.654  1.00 21.15 ? 307  SER A C   1 
ATOM   2327 O  O   . SER A 1 307  ? 24.569 50.476  38.802  1.00 20.71 ? 307  SER A O   1 
ATOM   2328 C  CB  . SER A 1 307  ? 25.021 53.397  40.256  1.00 20.46 ? 307  SER A CB  1 
ATOM   2329 O  OG  . SER A 1 307  ? 23.633 53.175  40.022  1.00 21.80 ? 307  SER A OG  1 
ATOM   2330 N  N   . ASP A 1 308  ? 25.562 50.500  40.852  1.00 22.18 ? 308  ASP A N   1 
ATOM   2331 C  CA  . ASP A 1 308  ? 25.051 49.180  41.152  1.00 23.74 ? 308  ASP A CA  1 
ATOM   2332 C  C   . ASP A 1 308  ? 23.537 49.139  41.188  1.00 22.45 ? 308  ASP A C   1 
ATOM   2333 O  O   . ASP A 1 308  ? 22.965 48.104  40.879  1.00 23.04 ? 308  ASP A O   1 
ATOM   2334 C  CB  . ASP A 1 308  ? 25.635 48.680  42.463  1.00 27.16 ? 308  ASP A CB  1 
ATOM   2335 C  CG  . ASP A 1 308  ? 27.137 48.496  42.375  1.00 32.12 ? 308  ASP A CG  1 
ATOM   2336 O  OD1 . ASP A 1 308  ? 27.718 49.053  41.411  1.00 35.43 ? 308  ASP A OD1 1 
ATOM   2337 O  OD2 . ASP A 1 308  ? 27.742 47.821  43.255  1.00 34.25 ? 308  ASP A OD2 1 
ATOM   2338 N  N   . GLN A 1 309  ? 22.889 50.261  41.507  1.00 21.59 ? 309  GLN A N   1 
ATOM   2339 C  CA  . GLN A 1 309  ? 21.430 50.320  41.574  1.00 21.65 ? 309  GLN A CA  1 
ATOM   2340 C  C   . GLN A 1 309  ? 20.761 50.452  40.230  1.00 20.59 ? 309  GLN A C   1 
ATOM   2341 O  O   . GLN A 1 309  ? 19.574 50.173  40.111  1.00 19.76 ? 309  GLN A O   1 
ATOM   2342 C  CB  . GLN A 1 309  ? 20.953 51.506  42.429  1.00 21.69 ? 309  GLN A CB  1 
ATOM   2343 C  CG  . GLN A 1 309  ? 21.394 51.479  43.874  1.00 23.41 ? 309  GLN A CG  1 
ATOM   2344 C  CD  . GLN A 1 309  ? 22.914 51.580  44.014  1.00 25.08 ? 309  GLN A CD  1 
ATOM   2345 O  OE1 . GLN A 1 309  ? 23.545 52.522  43.492  1.00 25.96 ? 309  GLN A OE1 1 
ATOM   2346 N  NE2 . GLN A 1 309  ? 23.516 50.610  44.737  1.00 24.90 ? 309  GLN A NE2 1 
ATOM   2347 N  N   . ASN A 1 310  ? 21.477 50.900  39.208  1.00 19.74 ? 310  ASN A N   1 
ATOM   2348 C  CA  . ASN A 1 310  ? 20.810 51.019  37.921  1.00 18.92 ? 310  ASN A CA  1 
ATOM   2349 C  C   . ASN A 1 310  ? 21.446 50.158  36.847  1.00 18.42 ? 310  ASN A C   1 
ATOM   2350 O  O   . ASN A 1 310  ? 20.892 50.054  35.757  1.00 17.71 ? 310  ASN A O   1 
ATOM   2351 C  CB  . ASN A 1 310  ? 20.726 52.513  37.457  1.00 20.24 ? 310  ASN A CB  1 
ATOM   2352 C  CG  . ASN A 1 310  ? 22.074 53.084  36.989  1.00 20.87 ? 310  ASN A CG  1 
ATOM   2353 O  OD1 . ASN A 1 310  ? 23.020 52.339  36.699  1.00 22.22 ? 310  ASN A OD1 1 
ATOM   2354 N  ND2 . ASN A 1 310  ? 22.151 54.411  36.905  1.00 21.00 ? 310  ASN A ND2 1 
ATOM   2355 N  N   . VAL A 1 311  ? 22.537 49.476  37.174  1.00 16.86 ? 311  VAL A N   1 
ATOM   2356 C  CA  . VAL A 1 311  ? 23.247 48.703  36.129  1.00 17.09 ? 311  VAL A CA  1 
ATOM   2357 C  C   . VAL A 1 311  ? 22.401 47.601  35.478  1.00 16.94 ? 311  VAL A C   1 
ATOM   2358 O  O   . VAL A 1 311  ? 22.571 47.315  34.274  1.00 18.88 ? 311  VAL A O   1 
ATOM   2359 C  CB  . VAL A 1 311  ? 24.601 48.094  36.663  1.00 17.25 ? 311  VAL A CB  1 
ATOM   2360 C  CG1 . VAL A 1 311  ? 24.342 46.967  37.630  1.00 18.36 ? 311  VAL A CG1 1 
ATOM   2361 C  CG2 . VAL A 1 311  ? 25.472 47.587  35.494  1.00 18.41 ? 311  VAL A CG2 1 
ATOM   2362 N  N   . ALA A 1 312  ? 21.453 47.017  36.210  1.00 17.16 ? 312  ALA A N   1 
ATOM   2363 C  CA  . ALA A 1 312  ? 20.637 45.951  35.609  1.00 16.81 ? 312  ALA A CA  1 
ATOM   2364 C  C   . ALA A 1 312  ? 19.691 46.469  34.578  1.00 18.87 ? 312  ALA A C   1 
ATOM   2365 O  O   . ALA A 1 312  ? 19.587 45.918  33.492  1.00 18.98 ? 312  ALA A O   1 
ATOM   2366 C  CB  . ALA A 1 312  ? 19.851 45.188  36.702  1.00 18.34 ? 312  ALA A CB  1 
ATOM   2367 N  N   . ALA A 1 313  ? 18.987 47.542  34.903  1.00 18.64 ? 313  ALA A N   1 
ATOM   2368 C  CA  . ALA A 1 313  ? 18.030 48.142  34.021  1.00 18.71 ? 313  ALA A CA  1 
ATOM   2369 C  C   . ALA A 1 313  ? 18.757 48.727  32.799  1.00 19.30 ? 313  ALA A C   1 
ATOM   2370 O  O   . ALA A 1 313  ? 18.285 48.580  31.680  1.00 19.48 ? 313  ALA A O   1 
ATOM   2371 C  CB  . ALA A 1 313  ? 17.256 49.224  34.777  1.00 17.65 ? 313  ALA A CB  1 
ATOM   2372 N  N   . ARG A 1 314  ? 19.912 49.348  33.000  1.00 18.75 ? 314  ARG A N   1 
ATOM   2373 C  CA  . ARG A 1 314  ? 20.656 49.946  31.890  1.00 18.46 ? 314  ARG A CA  1 
ATOM   2374 C  C   . ARG A 1 314  ? 21.161 48.823  30.949  1.00 17.02 ? 314  ARG A C   1 
ATOM   2375 O  O   . ARG A 1 314  ? 21.104 48.988  29.716  1.00 17.23 ? 314  ARG A O   1 
ATOM   2376 C  CB  . ARG A 1 314  ? 21.844 50.709  32.442  1.00 17.38 ? 314  ARG A CB  1 
ATOM   2377 C  CG  . ARG A 1 314  ? 21.453 51.845  33.414  1.00 21.44 ? 314  ARG A CG  1 
ATOM   2378 C  CD  . ARG A 1 314  ? 21.242 53.122  32.652  1.00 20.66 ? 314  ARG A CD  1 
ATOM   2379 N  NE  . ARG A 1 314  ? 19.890 53.208  32.118  1.00 20.47 ? 314  ARG A NE  1 
ATOM   2380 C  CZ  . ARG A 1 314  ? 19.501 54.097  31.205  1.00 22.14 ? 314  ARG A CZ  1 
ATOM   2381 N  NH1 . ARG A 1 314  ? 20.360 54.978  30.696  1.00 22.45 ? 314  ARG A NH1 1 
ATOM   2382 N  NH2 . ARG A 1 314  ? 18.227 54.145  30.810  1.00 21.15 ? 314  ARG A NH2 1 
ATOM   2383 N  N   . SER A 1 315  ? 21.660 47.732  31.540  1.00 17.67 ? 315  SER A N   1 
ATOM   2384 C  CA  . SER A 1 315  ? 22.150 46.574  30.755  1.00 18.31 ? 315  SER A CA  1 
ATOM   2385 C  C   . SER A 1 315  ? 20.987 45.971  29.995  1.00 19.00 ? 315  SER A C   1 
ATOM   2386 O  O   . SER A 1 315  ? 21.146 45.610  28.833  1.00 20.12 ? 315  SER A O   1 
ATOM   2387 C  CB  . SER A 1 315  ? 22.809 45.511  31.637  1.00 18.03 ? 315  SER A CB  1 
ATOM   2388 O  OG  . SER A 1 315  ? 23.944 46.058  32.302  1.00 19.31 ? 315  SER A OG  1 
ATOM   2389 N  N   . ASP A 1 316  ? 19.817 45.830  30.615  1.00 18.34 ? 316  ASP A N   1 
ATOM   2390 C  CA  . ASP A 1 316  ? 18.649 45.301  29.899  1.00 18.73 ? 316  ASP A CA  1 
ATOM   2391 C  C   . ASP A 1 316  ? 18.391 46.099  28.627  1.00 17.81 ? 316  ASP A C   1 
ATOM   2392 O  O   . ASP A 1 316  ? 18.093 45.539  27.552  1.00 17.51 ? 316  ASP A O   1 
ATOM   2393 C  CB  . ASP A 1 316  ? 17.355 45.471  30.708  1.00 21.23 ? 316  ASP A CB  1 
ATOM   2394 C  CG  . ASP A 1 316  ? 17.293 44.622  31.942  1.00 22.41 ? 316  ASP A CG  1 
ATOM   2395 O  OD1 . ASP A 1 316  ? 18.074 43.655  32.066  1.00 20.14 ? 316  ASP A OD1 1 
ATOM   2396 O  OD2 . ASP A 1 316  ? 16.388 44.946  32.778  1.00 23.23 ? 316  ASP A OD2 1 
ATOM   2397 N  N   . LEU A 1 317  ? 18.458 47.419  28.773  1.00 16.81 ? 317  LEU A N   1 
ATOM   2398 C  CA  . LEU A 1 317  ? 18.165 48.309  27.674  1.00 16.21 ? 317  LEU A CA  1 
ATOM   2399 C  C   . LEU A 1 317  ? 19.207 48.219  26.553  1.00 14.16 ? 317  LEU A C   1 
ATOM   2400 O  O   . LEU A 1 317  ? 18.842 48.181  25.359  1.00 15.34 ? 317  LEU A O   1 
ATOM   2401 C  CB  . LEU A 1 317  ? 18.115 49.752  28.163  1.00 17.32 ? 317  LEU A CB  1 
ATOM   2402 C  CG  . LEU A 1 317  ? 16.805 50.346  28.615  1.00 20.86 ? 317  LEU A CG  1 
ATOM   2403 C  CD1 . LEU A 1 317  ? 17.095 51.758  29.160  1.00 20.62 ? 317  LEU A CD1 1 
ATOM   2404 C  CD2 . LEU A 1 317  ? 15.811 50.372  27.454  1.00 21.71 ? 317  LEU A CD2 1 
ATOM   2405 N  N   . LEU A 1 318  ? 20.473 48.185  26.960  1.00 14.48 ? 318  LEU A N   1 
ATOM   2406 C  CA  . LEU A 1 318  ? 21.588 48.186  26.007  1.00 13.23 ? 318  LEU A CA  1 
ATOM   2407 C  C   . LEU A 1 318  ? 21.707 46.863  25.282  1.00 12.96 ? 318  LEU A C   1 
ATOM   2408 O  O   . LEU A 1 318  ? 21.824 46.867  24.032  1.00 13.38 ? 318  LEU A O   1 
ATOM   2409 C  CB  . LEU A 1 318  ? 22.903 48.524  26.761  1.00 13.21 ? 318  LEU A CB  1 
ATOM   2410 C  CG  . LEU A 1 318  ? 24.156 48.622  25.858  1.00 10.30 ? 318  LEU A CG  1 
ATOM   2411 C  CD1 . LEU A 1 318  ? 23.968 49.723  24.768  1.00 11.13 ? 318  LEU A CD1 1 
ATOM   2412 C  CD2 . LEU A 1 318  ? 25.391 48.914  26.718  1.00 13.10 ? 318  LEU A CD2 1 
ATOM   2413 N  N   . VAL A 1 319  ? 21.671 45.740  26.021  1.00 11.65 ? 319  VAL A N   1 
ATOM   2414 C  CA  . VAL A 1 319  ? 21.735 44.414  25.394  1.00 12.03 ? 319  VAL A CA  1 
ATOM   2415 C  C   . VAL A 1 319  ? 20.578 44.255  24.412  1.00 10.13 ? 319  VAL A C   1 
ATOM   2416 O  O   . VAL A 1 319  ? 20.735 43.683  23.307  1.00 12.53 ? 319  VAL A O   1 
ATOM   2417 C  CB  . VAL A 1 319  ? 21.715 43.313  26.491  1.00 12.35 ? 319  VAL A CB  1 
ATOM   2418 C  CG1 . VAL A 1 319  ? 21.594 41.907  25.869  1.00 13.78 ? 319  VAL A CG1 1 
ATOM   2419 C  CG2 . VAL A 1 319  ? 22.978 43.428  27.319  1.00 14.25 ? 319  VAL A CG2 1 
ATOM   2420 N  N   . ASP A 1 320  ? 19.401 44.754  24.768  1.00 12.27 ? 320  ASP A N   1 
ATOM   2421 C  CA  . ASP A 1 320  ? 18.261 44.707  23.837  1.00 12.86 ? 320  ASP A CA  1 
ATOM   2422 C  C   . ASP A 1 320  ? 18.594 45.433  22.496  1.00 11.49 ? 320  ASP A C   1 
ATOM   2423 O  O   . ASP A 1 320  ? 18.236 44.943  21.395  1.00 11.77 ? 320  ASP A O   1 
ATOM   2424 C  CB  . ASP A 1 320  ? 16.981 45.297  24.494  1.00 15.61 ? 320  ASP A CB  1 
ATOM   2425 C  CG  . ASP A 1 320  ? 15.790 45.377  23.536  1.00 15.01 ? 320  ASP A CG  1 
ATOM   2426 O  OD1 . ASP A 1 320  ? 15.251 44.292  23.136  1.00 16.83 ? 320  ASP A OD1 1 
ATOM   2427 O  OD2 . ASP A 1 320  ? 15.344 46.513  23.203  1.00 16.93 ? 320  ASP A OD2 1 
ATOM   2428 N  N   . GLN A 1 321  ? 19.262 46.603  22.564  1.00 11.75 ? 321  GLN A N   1 
ATOM   2429 C  CA  . GLN A 1 321  ? 19.626 47.342  21.314  1.00 10.65 ? 321  GLN A CA  1 
ATOM   2430 C  C   . GLN A 1 321  ? 20.641 46.487  20.539  1.00 7.90  ? 321  GLN A C   1 
ATOM   2431 O  O   . GLN A 1 321  ? 20.523 46.342  19.318  1.00 10.55 ? 321  GLN A O   1 
ATOM   2432 C  CB  . GLN A 1 321  ? 20.286 48.702  21.651  1.00 11.19 ? 321  GLN A CB  1 
ATOM   2433 C  CG  . GLN A 1 321  ? 19.248 49.748  22.121  1.00 13.57 ? 321  GLN A CG  1 
ATOM   2434 C  CD  . GLN A 1 321  ? 18.193 49.988  21.088  1.00 14.29 ? 321  GLN A CD  1 
ATOM   2435 O  OE1 . GLN A 1 321  ? 18.500 50.393  19.979  1.00 13.88 ? 321  GLN A OE1 1 
ATOM   2436 N  NE2 . GLN A 1 321  ? 16.899 49.764  21.445  1.00 14.90 ? 321  GLN A NE2 1 
ATOM   2437 N  N   . TRP A 1 322  ? 21.644 45.994  21.250  1.00 9.42  ? 322  TRP A N   1 
ATOM   2438 C  CA  . TRP A 1 322  ? 22.654 45.108  20.610  1.00 9.42  ? 322  TRP A CA  1 
ATOM   2439 C  C   . TRP A 1 322  ? 22.080 43.874  19.939  1.00 8.57  ? 322  TRP A C   1 
ATOM   2440 O  O   . TRP A 1 322  ? 22.430 43.533  18.827  1.00 11.03 ? 322  TRP A O   1 
ATOM   2441 C  CB  . TRP A 1 322  ? 23.669 44.607  21.638  1.00 9.64  ? 322  TRP A CB  1 
ATOM   2442 C  CG  . TRP A 1 322  ? 24.589 45.653  22.233  1.00 10.20 ? 322  TRP A CG  1 
ATOM   2443 C  CD1 . TRP A 1 322  ? 24.778 46.944  21.790  1.00 11.76 ? 322  TRP A CD1 1 
ATOM   2444 C  CD2 . TRP A 1 322  ? 25.499 45.463  23.337  1.00 8.94  ? 322  TRP A CD2 1 
ATOM   2445 N  NE1 . TRP A 1 322  ? 25.777 47.558  22.561  1.00 11.79 ? 322  TRP A NE1 1 
ATOM   2446 C  CE2 . TRP A 1 322  ? 26.223 46.677  23.504  1.00 10.34 ? 322  TRP A CE2 1 
ATOM   2447 C  CE3 . TRP A 1 322  ? 25.771 44.372  24.200  1.00 13.12 ? 322  TRP A CE3 1 
ATOM   2448 C  CZ2 . TRP A 1 322  ? 27.202 46.835  24.498  1.00 12.11 ? 322  TRP A CZ2 1 
ATOM   2449 C  CZ3 . TRP A 1 322  ? 26.733 44.527  25.177  1.00 13.49 ? 322  TRP A CZ3 1 
ATOM   2450 C  CH2 . TRP A 1 322  ? 27.446 45.770  25.316  1.00 11.30 ? 322  TRP A CH2 1 
ATOM   2451 N  N   . LYS A 1 323  ? 21.103 43.242  20.578  1.00 9.78  ? 323  LYS A N   1 
ATOM   2452 C  CA  . LYS A 1 323  ? 20.517 42.038  19.955  1.00 11.44 ? 323  LYS A CA  1 
ATOM   2453 C  C   . LYS A 1 323  ? 19.678 42.402  18.731  1.00 11.49 ? 323  LYS A C   1 
ATOM   2454 O  O   . LYS A 1 323  ? 19.578 41.622  17.801  1.00 11.49 ? 323  LYS A O   1 
ATOM   2455 C  CB  . LYS A 1 323  ? 19.729 41.216  21.004  1.00 11.42 ? 323  LYS A CB  1 
ATOM   2456 C  CG  . LYS A 1 323  ? 20.696 40.614  21.976  1.00 13.50 ? 323  LYS A CG  1 
ATOM   2457 C  CD  . LYS A 1 323  ? 20.005 39.810  23.071  1.00 17.63 ? 323  LYS A CD  1 
ATOM   2458 C  CE  . LYS A 1 323  ? 21.010 38.805  23.710  1.00 19.93 ? 323  LYS A CE  1 
ATOM   2459 N  NZ  . LYS A 1 323  ? 20.250 37.907  24.647  1.00 21.25 ? 323  LYS A NZ  1 
ATOM   2460 N  N   . LYS A 1 324  ? 19.086 43.598  18.718  1.00 9.57  ? 324  LYS A N   1 
ATOM   2461 C  CA  . LYS A 1 324  ? 18.323 44.078  17.578  1.00 10.49 ? 324  LYS A CA  1 
ATOM   2462 C  C   . LYS A 1 324  ? 19.310 44.371  16.418  1.00 10.65 ? 324  LYS A C   1 
ATOM   2463 O  O   . LYS A 1 324  ? 19.059 43.940  15.258  1.00 12.22 ? 324  LYS A O   1 
ATOM   2464 C  CB  . LYS A 1 324  ? 17.506 45.329  17.964  1.00 11.22 ? 324  LYS A CB  1 
ATOM   2465 C  CG  . LYS A 1 324  ? 16.234 44.939  18.789  1.00 10.32 ? 324  LYS A CG  1 
ATOM   2466 C  CD  . LYS A 1 324  ? 15.593 46.225  19.356  1.00 11.94 ? 324  LYS A CD  1 
ATOM   2467 C  CE  . LYS A 1 324  ? 14.305 45.780  20.090  1.00 13.12 ? 324  LYS A CE  1 
ATOM   2468 N  NZ  . LYS A 1 324  ? 13.740 46.884  20.874  1.00 16.08 ? 324  LYS A NZ  1 
ATOM   2469 N  N   . LYS A 1 325  ? 20.432 45.058  16.723  1.00 9.57  ? 325  LYS A N   1 
ATOM   2470 C  CA  . LYS A 1 325  ? 21.419 45.364  15.706  1.00 7.86  ? 325  LYS A CA  1 
ATOM   2471 C  C   . LYS A 1 325  ? 21.971 43.999  15.175  1.00 9.49  ? 325  LYS A C   1 
ATOM   2472 O  O   . LYS A 1 325  ? 22.175 43.848  13.971  1.00 9.55  ? 325  LYS A O   1 
ATOM   2473 C  CB  . LYS A 1 325  ? 22.542 46.211  16.321  1.00 9.21  ? 325  LYS A CB  1 
ATOM   2474 C  CG  . LYS A 1 325  ? 23.475 46.698  15.246  1.00 10.10 ? 325  LYS A CG  1 
ATOM   2475 C  CD  . LYS A 1 325  ? 24.512 47.694  15.763  1.00 10.46 ? 325  LYS A CD  1 
ATOM   2476 C  CE  . LYS A 1 325  ? 25.326 48.328  14.596  1.00 10.90 ? 325  LYS A CE  1 
ATOM   2477 N  NZ  . LYS A 1 325  ? 26.534 49.007  15.178  1.00 10.65 ? 325  LYS A NZ  1 
ATOM   2478 N  N   . ALA A 1 326  ? 22.172 43.027  16.059  1.00 9.74  ? 326  ALA A N   1 
ATOM   2479 C  CA  . ALA A 1 326  ? 22.742 41.725  15.653  1.00 10.51 ? 326  ALA A CA  1 
ATOM   2480 C  C   . ALA A 1 326  ? 21.804 40.978  14.700  1.00 11.39 ? 326  ALA A C   1 
ATOM   2481 O  O   . ALA A 1 326  ? 22.265 40.168  13.909  1.00 10.94 ? 326  ALA A O   1 
ATOM   2482 C  CB  . ALA A 1 326  ? 23.012 40.901  16.852  1.00 9.26  ? 326  ALA A CB  1 
ATOM   2483 N  N   . GLU A 1 327  ? 20.519 41.287  14.734  1.00 10.83 ? 327  GLU A N   1 
ATOM   2484 C  CA  . GLU A 1 327  ? 19.591 40.647  13.783  1.00 12.41 ? 327  GLU A CA  1 
ATOM   2485 C  C   . GLU A 1 327  ? 19.839 40.997  12.322  1.00 12.66 ? 327  GLU A C   1 
ATOM   2486 O  O   . GLU A 1 327  ? 19.387 40.251  11.430  1.00 13.90 ? 327  GLU A O   1 
ATOM   2487 C  CB  . GLU A 1 327  ? 18.144 41.031  14.058  1.00 14.07 ? 327  GLU A CB  1 
ATOM   2488 C  CG  . GLU A 1 327  ? 17.479 40.237  15.117  1.00 17.99 ? 327  GLU A CG  1 
ATOM   2489 C  CD  . GLU A 1 327  ? 17.499 38.728  14.839  1.00 18.48 ? 327  GLU A CD  1 
ATOM   2490 O  OE1 . GLU A 1 327  ? 16.845 38.222  13.901  1.00 19.26 ? 327  GLU A OE1 1 
ATOM   2491 O  OE2 . GLU A 1 327  ? 18.220 38.044  15.548  1.00 16.87 ? 327  GLU A OE2 1 
ATOM   2492 N  N   . LEU A 1 328  ? 20.554 42.107  12.052  1.00 10.86 ? 328  LEU A N   1 
ATOM   2493 C  CA  . LEU A 1 328  ? 20.775 42.573  10.689  1.00 10.15 ? 328  LEU A CA  1 
ATOM   2494 C  C   . LEU A 1 328  ? 21.980 41.943  10.056  1.00 10.49 ? 328  LEU A C   1 
ATOM   2495 O  O   . LEU A 1 328  ? 22.281 42.217  8.899   1.00 11.01 ? 328  LEU A O   1 
ATOM   2496 C  CB  . LEU A 1 328  ? 20.960 44.115  10.693  1.00 9.22  ? 328  LEU A CB  1 
ATOM   2497 C  CG  . LEU A 1 328  ? 19.845 44.876  11.444  1.00 9.37  ? 328  LEU A CG  1 
ATOM   2498 C  CD1 . LEU A 1 328  ? 20.084 46.386  11.296  1.00 10.16 ? 328  LEU A CD1 1 
ATOM   2499 C  CD2 . LEU A 1 328  ? 18.447 44.437  10.983  1.00 11.52 ? 328  LEU A CD2 1 
ATOM   2500 N  N   . TYR A 1 329  ? 22.666 41.100  10.808  1.00 8.77  ? 329  TYR A N   1 
ATOM   2501 C  CA  . TYR A 1 329  ? 23.918 40.471  10.356  1.00 9.17  ? 329  TYR A CA  1 
ATOM   2502 C  C   . TYR A 1 329  ? 23.916 38.949  10.525  1.00 10.19 ? 329  TYR A C   1 
ATOM   2503 O  O   . TYR A 1 329  ? 23.091 38.434  11.281  1.00 11.39 ? 329  TYR A O   1 
ATOM   2504 C  CB  . TYR A 1 329  ? 25.145 41.141  11.100  1.00 8.14  ? 329  TYR A CB  1 
ATOM   2505 C  CG  . TYR A 1 329  ? 25.361 42.602  10.749  1.00 10.02 ? 329  TYR A CG  1 
ATOM   2506 C  CD1 . TYR A 1 329  ? 26.140 42.966  9.636   1.00 9.36  ? 329  TYR A CD1 1 
ATOM   2507 C  CD2 . TYR A 1 329  ? 24.772 43.635  11.494  1.00 12.17 ? 329  TYR A CD2 1 
ATOM   2508 C  CE1 . TYR A 1 329  ? 26.310 44.312  9.268   1.00 10.44 ? 329  TYR A CE1 1 
ATOM   2509 C  CE2 . TYR A 1 329  ? 24.963 44.987  11.142  1.00 11.44 ? 329  TYR A CE2 1 
ATOM   2510 C  CZ  . TYR A 1 329  ? 25.722 45.298  10.013  1.00 9.13  ? 329  TYR A CZ  1 
ATOM   2511 O  OH  . TYR A 1 329  ? 25.739 46.610  9.605   1.00 10.39 ? 329  TYR A OH  1 
ATOM   2512 N  N   . ARG A 1 330  ? 24.853 38.265  9.877   1.00 9.30  ? 330  ARG A N   1 
ATOM   2513 C  CA  . ARG A 1 330  ? 24.866 36.806  9.870   1.00 10.96 ? 330  ARG A CA  1 
ATOM   2514 C  C   . ARG A 1 330  ? 25.676 36.073  10.915  1.00 12.23 ? 330  ARG A C   1 
ATOM   2515 O  O   . ARG A 1 330  ? 25.496 34.856  11.056  1.00 12.44 ? 330  ARG A O   1 
ATOM   2516 C  CB  . ARG A 1 330  ? 25.302 36.306  8.479   1.00 11.97 ? 330  ARG A CB  1 
ATOM   2517 C  CG  . ARG A 1 330  ? 24.370 36.831  7.397   1.00 9.62  ? 330  ARG A CG  1 
ATOM   2518 C  CD  . ARG A 1 330  ? 24.700 36.306  6.003   1.00 12.06 ? 330  ARG A CD  1 
ATOM   2519 N  NE  . ARG A 1 330  ? 23.721 36.825  5.051   1.00 11.22 ? 330  ARG A NE  1 
ATOM   2520 C  CZ  . ARG A 1 330  ? 23.483 36.341  3.835   1.00 13.77 ? 330  ARG A CZ  1 
ATOM   2521 N  NH1 . ARG A 1 330  ? 24.174 35.291  3.387   1.00 14.61 ? 330  ARG A NH1 1 
ATOM   2522 N  NH2 . ARG A 1 330  ? 22.604 36.948  3.043   1.00 13.38 ? 330  ARG A NH2 1 
ATOM   2523 N  N   . THR A 1 331  ? 26.614 36.713  11.606  1.00 11.46 ? 331  THR A N   1 
ATOM   2524 C  CA  . THR A 1 331  ? 27.385 35.953  12.605  1.00 9.71  ? 331  THR A CA  1 
ATOM   2525 C  C   . THR A 1 331  ? 26.976 36.317  13.999  1.00 10.20 ? 331  THR A C   1 
ATOM   2526 O  O   . THR A 1 331  ? 26.079 37.125  14.172  1.00 11.96 ? 331  THR A O   1 
ATOM   2527 C  CB  . THR A 1 331  ? 28.925 36.164  12.470  1.00 11.96 ? 331  THR A CB  1 
ATOM   2528 O  OG1 . THR A 1 331  ? 29.324 37.465  12.971  1.00 10.92 ? 331  THR A OG1 1 
ATOM   2529 C  CG2 . THR A 1 331  ? 29.299 35.993  10.968  1.00 10.92 ? 331  THR A CG2 1 
ATOM   2530 N  N   . ASN A 1 332  ? 27.664 35.706  14.977  1.00 10.70 ? 332  ASN A N   1 
ATOM   2531 C  CA  . ASN A 1 332  ? 27.420 35.979  16.408  1.00 12.62 ? 332  ASN A CA  1 
ATOM   2532 C  C   . ASN A 1 332  ? 28.482 36.946  16.948  1.00 13.13 ? 332  ASN A C   1 
ATOM   2533 O  O   . ASN A 1 332  ? 28.751 36.940  18.169  1.00 10.44 ? 332  ASN A O   1 
ATOM   2534 C  CB  . ASN A 1 332  ? 27.416 34.682  17.262  1.00 12.95 ? 332  ASN A CB  1 
ATOM   2535 C  CG  . ASN A 1 332  ? 28.765 34.035  17.359  1.00 16.26 ? 332  ASN A CG  1 
ATOM   2536 O  OD1 . ASN A 1 332  ? 29.592 34.157  16.455  1.00 18.88 ? 332  ASN A OD1 1 
ATOM   2537 N  ND2 . ASN A 1 332  ? 29.015 33.320  18.476  1.00 20.01 ? 332  ASN A ND2 1 
ATOM   2538 N  N   . VAL A 1 333  ? 29.082 37.751  16.053  1.00 9.73  ? 333  VAL A N   1 
ATOM   2539 C  CA  . VAL A 1 333  ? 30.105 38.726  16.395  1.00 10.49 ? 333  VAL A CA  1 
ATOM   2540 C  C   . VAL A 1 333  ? 29.530 40.085  15.965  1.00 9.94  ? 333  VAL A C   1 
ATOM   2541 O  O   . VAL A 1 333  ? 29.191 40.260  14.768  1.00 11.88 ? 333  VAL A O   1 
ATOM   2542 C  CB  . VAL A 1 333  ? 31.395 38.441  15.592  1.00 10.00 ? 333  VAL A CB  1 
ATOM   2543 C  CG1 . VAL A 1 333  ? 32.480 39.505  15.909  1.00 12.58 ? 333  VAL A CG1 1 
ATOM   2544 C  CG2 . VAL A 1 333  ? 31.888 37.035  15.859  1.00 12.43 ? 333  VAL A CG2 1 
ATOM   2545 N  N   . LEU A 1 334  ? 29.391 41.014  16.931  1.00 9.25  ? 334  LEU A N   1 
ATOM   2546 C  CA  . LEU A 1 334  ? 28.759 42.328  16.715  1.00 7.43  ? 334  LEU A CA  1 
ATOM   2547 C  C   . LEU A 1 334  ? 29.734 43.521  16.873  1.00 8.38  ? 334  LEU A C   1 
ATOM   2548 O  O   . LEU A 1 334  ? 30.457 43.592  17.865  1.00 10.35 ? 334  LEU A O   1 
ATOM   2549 C  CB  . LEU A 1 334  ? 27.553 42.475  17.673  1.00 7.58  ? 334  LEU A CB  1 
ATOM   2550 C  CG  . LEU A 1 334  ? 26.708 43.721  17.452  1.00 8.56  ? 334  LEU A CG  1 
ATOM   2551 C  CD1 . LEU A 1 334  ? 25.914 43.621  16.098  1.00 10.03 ? 334  LEU A CD1 1 
ATOM   2552 C  CD2 . LEU A 1 334  ? 25.764 43.889  18.752  1.00 9.48  ? 334  LEU A CD2 1 
ATOM   2553 N  N   . LEU A 1 335  ? 29.753 44.415  15.902  1.00 8.91  ? 335  LEU A N   1 
ATOM   2554 C  CA  . LEU A 1 335  ? 30.625 45.598  15.895  1.00 6.66  ? 335  LEU A CA  1 
ATOM   2555 C  C   . LEU A 1 335  ? 29.803 46.777  16.479  1.00 8.07  ? 335  LEU A C   1 
ATOM   2556 O  O   . LEU A 1 335  ? 28.753 47.084  15.957  1.00 7.63  ? 335  LEU A O   1 
ATOM   2557 C  CB  . LEU A 1 335  ? 31.060 45.960  14.440  1.00 8.23  ? 335  LEU A CB  1 
ATOM   2558 C  CG  . LEU A 1 335  ? 31.895 47.242  14.349  1.00 8.33  ? 335  LEU A CG  1 
ATOM   2559 C  CD1 . LEU A 1 335  ? 33.198 47.120  15.086  1.00 11.71 ? 335  LEU A CD1 1 
ATOM   2560 C  CD2 . LEU A 1 335  ? 32.006 47.591  12.948  1.00 10.48 ? 335  LEU A CD2 1 
ATOM   2561 N  N   . ILE A 1 336  ? 30.301 47.384  17.550  1.00 7.02  ? 336  ILE A N   1 
ATOM   2562 C  CA  . ILE A 1 336  ? 29.659 48.553  18.100  1.00 8.09  ? 336  ILE A CA  1 
ATOM   2563 C  C   . ILE A 1 336  ? 30.679 49.714  18.134  1.00 7.46  ? 336  ILE A C   1 
ATOM   2564 O  O   . ILE A 1 336  ? 31.464 49.814  19.061  1.00 9.67  ? 336  ILE A O   1 
ATOM   2565 C  CB  . ILE A 1 336  ? 29.184 48.274  19.566  1.00 9.06  ? 336  ILE A CB  1 
ATOM   2566 C  CG1 . ILE A 1 336  ? 28.143 47.130  19.586  1.00 10.27 ? 336  ILE A CG1 1 
ATOM   2567 C  CG2 . ILE A 1 336  ? 28.497 49.537  20.112  1.00 10.08 ? 336  ILE A CG2 1 
ATOM   2568 C  CD1 . ILE A 1 336  ? 26.826 47.400  18.797  1.00 8.20  ? 336  ILE A CD1 1 
ATOM   2569 N  N   . PRO A 1 337  ? 30.727 50.548  17.093  1.00 7.44  ? 337  PRO A N   1 
ATOM   2570 C  CA  . PRO A 1 337  ? 31.682 51.680  17.165  1.00 8.23  ? 337  PRO A CA  1 
ATOM   2571 C  C   . PRO A 1 337  ? 31.260 52.574  18.373  1.00 9.23  ? 337  PRO A C   1 
ATOM   2572 O  O   . PRO A 1 337  ? 30.068 52.696  18.693  1.00 9.61  ? 337  PRO A O   1 
ATOM   2573 C  CB  . PRO A 1 337  ? 31.450 52.447  15.863  1.00 7.28  ? 337  PRO A CB  1 
ATOM   2574 C  CG  . PRO A 1 337  ? 30.915 51.398  14.940  1.00 8.63  ? 337  PRO A CG  1 
ATOM   2575 C  CD  . PRO A 1 337  ? 29.931 50.625  15.861  1.00 8.87  ? 337  PRO A CD  1 
ATOM   2576 N  N   . LEU A 1 338  ? 32.247 53.173  19.038  1.00 9.74  ? 338  LEU A N   1 
ATOM   2577 C  CA  . LEU A 1 338  ? 31.989 54.133  20.122  1.00 9.20  ? 338  LEU A CA  1 
ATOM   2578 C  C   . LEU A 1 338  ? 32.802 55.423  19.919  1.00 8.73  ? 338  LEU A C   1 
ATOM   2579 O  O   . LEU A 1 338  ? 33.963 55.540  20.347  1.00 9.51  ? 338  LEU A O   1 
ATOM   2580 C  CB  . LEU A 1 338  ? 32.298 53.477  21.466  1.00 9.81  ? 338  LEU A CB  1 
ATOM   2581 C  CG  . LEU A 1 338  ? 31.909 54.373  22.664  1.00 8.66  ? 338  LEU A CG  1 
ATOM   2582 C  CD1 . LEU A 1 338  ? 30.389 54.167  22.979  1.00 10.49 ? 338  LEU A CD1 1 
ATOM   2583 C  CD2 . LEU A 1 338  ? 32.670 53.853  23.904  1.00 10.54 ? 338  LEU A CD2 1 
ATOM   2584 N  N   . GLY A 1 339  ? 32.202 56.376  19.195  1.00 9.97  ? 339  GLY A N   1 
ATOM   2585 C  CA  . GLY A 1 339  ? 32.958 57.617  18.910  1.00 7.53  ? 339  GLY A CA  1 
ATOM   2586 C  C   . GLY A 1 339  ? 32.137 58.602  18.081  1.00 8.33  ? 339  GLY A C   1 
ATOM   2587 O  O   . GLY A 1 339  ? 30.921 58.384  17.817  1.00 9.39  ? 339  GLY A O   1 
ATOM   2588 N  N   . ASP A 1 340  ? 32.767 59.744  17.720  1.00 8.32  ? 340  ASP A N   1 
ATOM   2589 C  CA  . ASP A 1 340  ? 32.129 60.809  16.973  1.00 9.00  ? 340  ASP A CA  1 
ATOM   2590 C  C   . ASP A 1 340  ? 33.276 61.745  16.556  1.00 7.90  ? 340  ASP A C   1 
ATOM   2591 O  O   . ASP A 1 340  ? 34.467 61.423  16.740  1.00 9.46  ? 340  ASP A O   1 
ATOM   2592 C  CB  . ASP A 1 340  ? 31.102 61.501  17.894  1.00 8.53  ? 340  ASP A CB  1 
ATOM   2593 C  CG  . ASP A 1 340  ? 29.994 62.265  17.169  1.00 10.01 ? 340  ASP A CG  1 
ATOM   2594 O  OD1 . ASP A 1 340  ? 30.122 62.697  15.998  1.00 10.31 ? 340  ASP A OD1 1 
ATOM   2595 O  OD2 . ASP A 1 340  ? 28.954 62.422  17.797  1.00 12.67 ? 340  ASP A OD2 1 
ATOM   2596 N  N   . ASP A 1 341  ? 32.909 62.932  16.148  1.00 8.94  ? 341  ASP A N   1 
ATOM   2597 C  CA  . ASP A 1 341  ? 33.908 63.848  15.632  1.00 9.40  ? 341  ASP A CA  1 
ATOM   2598 C  C   . ASP A 1 341  ? 34.750 64.448  16.730  1.00 9.88  ? 341  ASP A C   1 
ATOM   2599 O  O   . ASP A 1 341  ? 34.231 64.953  17.699  1.00 10.30 ? 341  ASP A O   1 
ATOM   2600 C  CB  . ASP A 1 341  ? 33.196 64.962  14.796  1.00 9.56  ? 341  ASP A CB  1 
ATOM   2601 C  CG  . ASP A 1 341  ? 32.593 64.447  13.489  1.00 12.73 ? 341  ASP A CG  1 
ATOM   2602 O  OD1 . ASP A 1 341  ? 32.627 63.228  13.218  1.00 11.22 ? 341  ASP A OD1 1 
ATOM   2603 O  OD2 . ASP A 1 341  ? 32.144 65.277  12.661  1.00 11.41 ? 341  ASP A OD2 1 
ATOM   2604 N  N   . PHE A 1 342  ? 36.074 64.417  16.531  1.00 8.56  ? 342  PHE A N   1 
ATOM   2605 C  CA  . PHE A 1 342  ? 37.051 64.982  17.437  1.00 9.81  ? 342  PHE A CA  1 
ATOM   2606 C  C   . PHE A 1 342  ? 36.766 64.565  18.896  1.00 10.41 ? 342  PHE A C   1 
ATOM   2607 O  O   . PHE A 1 342  ? 36.957 65.345  19.853  1.00 12.33 ? 342  PHE A O   1 
ATOM   2608 C  CB  . PHE A 1 342  ? 37.095 66.525  17.240  1.00 8.59  ? 342  PHE A CB  1 
ATOM   2609 C  CG  . PHE A 1 342  ? 37.758 66.933  15.961  1.00 10.42 ? 342  PHE A CG  1 
ATOM   2610 C  CD1 . PHE A 1 342  ? 39.148 66.865  15.814  1.00 8.49  ? 342  PHE A CD1 1 
ATOM   2611 C  CD2 . PHE A 1 342  ? 36.985 67.355  14.879  1.00 8.69  ? 342  PHE A CD2 1 
ATOM   2612 C  CE1 . PHE A 1 342  ? 39.706 67.248  14.565  1.00 8.97  ? 342  PHE A CE1 1 
ATOM   2613 C  CE2 . PHE A 1 342  ? 37.524 67.708  13.682  1.00 9.74  ? 342  PHE A CE2 1 
ATOM   2614 C  CZ  . PHE A 1 342  ? 38.862 67.671  13.497  1.00 9.31  ? 342  PHE A CZ  1 
ATOM   2615 N  N   . ARG A 1 343  ? 36.327 63.309  19.060  1.00 10.15 ? 343  ARG A N   1 
ATOM   2616 C  CA  . ARG A 1 343  ? 36.090 62.775  20.406  1.00 9.32  ? 343  ARG A CA  1 
ATOM   2617 C  C   . ARG A 1 343  ? 37.392 62.303  21.132  1.00 10.95 ? 343  ARG A C   1 
ATOM   2618 O  O   . ARG A 1 343  ? 38.511 62.284  20.574  1.00 9.20  ? 343  ARG A O   1 
ATOM   2619 C  CB  . ARG A 1 343  ? 35.085 61.594  20.345  1.00 9.11  ? 343  ARG A CB  1 
ATOM   2620 C  CG  . ARG A 1 343  ? 33.637 62.029  20.145  1.00 10.97 ? 343  ARG A CG  1 
ATOM   2621 C  CD  . ARG A 1 343  ? 33.157 63.013  21.227  1.00 10.25 ? 343  ARG A CD  1 
ATOM   2622 N  NE  . ARG A 1 343  ? 31.705 63.247  21.152  1.00 10.21 ? 343  ARG A NE  1 
ATOM   2623 C  CZ  . ARG A 1 343  ? 30.773 62.551  21.818  1.00 11.36 ? 343  ARG A CZ  1 
ATOM   2624 N  NH1 . ARG A 1 343  ? 31.086 61.551  22.600  1.00 9.13  ? 343  ARG A NH1 1 
ATOM   2625 N  NH2 . ARG A 1 343  ? 29.502 62.943  21.755  1.00 9.51  ? 343  ARG A NH2 1 
ATOM   2626 N  N   . PHE A 1 344  ? 37.245 61.949  22.405  1.00 10.98 ? 344  PHE A N   1 
ATOM   2627 C  CA  . PHE A 1 344  ? 38.351 61.441  23.249  1.00 11.64 ? 344  PHE A CA  1 
ATOM   2628 C  C   . PHE A 1 344  ? 39.446 62.465  23.390  1.00 11.97 ? 344  PHE A C   1 
ATOM   2629 O  O   . PHE A 1 344  ? 40.659 62.178  23.307  1.00 13.36 ? 344  PHE A O   1 
ATOM   2630 C  CB  . PHE A 1 344  ? 38.803 60.095  22.671  1.00 9.43  ? 344  PHE A CB  1 
ATOM   2631 C  CG  . PHE A 1 344  ? 37.779 59.037  22.905  1.00 10.42 ? 344  PHE A CG  1 
ATOM   2632 C  CD1 . PHE A 1 344  ? 37.597 58.535  24.206  1.00 12.31 ? 344  PHE A CD1 1 
ATOM   2633 C  CD2 . PHE A 1 344  ? 36.980 58.592  21.874  1.00 9.81  ? 344  PHE A CD2 1 
ATOM   2634 C  CE1 . PHE A 1 344  ? 36.565 57.556  24.463  1.00 13.32 ? 344  PHE A CE1 1 
ATOM   2635 C  CE2 . PHE A 1 344  ? 35.972 57.635  22.101  1.00 12.45 ? 344  PHE A CE2 1 
ATOM   2636 C  CZ  . PHE A 1 344  ? 35.775 57.136  23.391  1.00 12.65 ? 344  PHE A CZ  1 
ATOM   2637 N  N   . LYS A 1 345  ? 38.987 63.687  23.600  1.00 12.48 ? 345  LYS A N   1 
ATOM   2638 C  CA  . LYS A 1 345  ? 39.833 64.834  23.782  1.00 13.53 ? 345  LYS A CA  1 
ATOM   2639 C  C   . LYS A 1 345  ? 40.159 65.012  25.294  1.00 15.31 ? 345  LYS A C   1 
ATOM   2640 O  O   . LYS A 1 345  ? 41.284 64.813  25.714  1.00 20.06 ? 345  LYS A O   1 
ATOM   2641 C  CB  . LYS A 1 345  ? 39.156 66.083  23.226  1.00 12.77 ? 345  LYS A CB  1 
ATOM   2642 C  CG  . LYS A 1 345  ? 40.064 67.305  23.308  1.00 17.41 ? 345  LYS A CG  1 
ATOM   2643 C  CD  . LYS A 1 345  ? 39.304 68.549  22.865  1.00 20.10 ? 345  LYS A CD  1 
ATOM   2644 C  CE  . LYS A 1 345  ? 40.148 69.817  22.925  1.00 21.85 ? 345  LYS A CE  1 
ATOM   2645 N  NZ  . LYS A 1 345  ? 39.186 70.875  22.453  1.00 23.76 ? 345  LYS A NZ  1 
ATOM   2646 N  N   . GLN A 1 346  ? 39.164 65.319  26.103  1.00 15.69 ? 346  GLN A N   1 
ATOM   2647 C  CA  . GLN A 1 346  ? 39.402 65.531  27.530  1.00 15.80 ? 346  GLN A CA  1 
ATOM   2648 C  C   . GLN A 1 346  ? 39.761 64.273  28.329  1.00 15.80 ? 346  GLN A C   1 
ATOM   2649 O  O   . GLN A 1 346  ? 39.190 63.207  28.153  1.00 15.44 ? 346  GLN A O   1 
ATOM   2650 C  CB  . GLN A 1 346  ? 38.152 66.140  28.169  1.00 17.17 ? 346  GLN A CB  1 
ATOM   2651 C  CG  . GLN A 1 346  ? 37.796 67.529  27.683  1.00 18.89 ? 346  GLN A CG  1 
ATOM   2652 C  CD  . GLN A 1 346  ? 36.818 67.556  26.527  1.00 22.39 ? 346  GLN A CD  1 
ATOM   2653 O  OE1 . GLN A 1 346  ? 36.600 66.558  25.827  1.00 20.24 ? 346  GLN A OE1 1 
ATOM   2654 N  NE2 . GLN A 1 346  ? 36.224 68.723  26.304  1.00 24.80 ? 346  GLN A NE2 1 
ATOM   2655 N  N   . ASN A 1 347  ? 40.667 64.403  29.295  1.00 17.82 ? 347  ASN A N   1 
ATOM   2656 C  CA  . ASN A 1 347  ? 40.973 63.253  30.148  1.00 18.21 ? 347  ASN A CA  1 
ATOM   2657 C  C   . ASN A 1 347  ? 39.712 62.767  30.866  1.00 17.40 ? 347  ASN A C   1 
ATOM   2658 O  O   . ASN A 1 347  ? 39.502 61.570  31.031  1.00 17.05 ? 347  ASN A O   1 
ATOM   2659 C  CB  . ASN A 1 347  ? 41.998 63.609  31.216  1.00 22.40 ? 347  ASN A CB  1 
ATOM   2660 C  CG  . ASN A 1 347  ? 43.351 63.754  30.649  1.00 25.48 ? 347  ASN A CG  1 
ATOM   2661 O  OD1 . ASN A 1 347  ? 43.787 62.915  29.844  1.00 25.92 ? 347  ASN A OD1 1 
ATOM   2662 N  ND2 . ASN A 1 347  ? 44.061 64.833  31.049  1.00 27.05 ? 347  ASN A ND2 1 
ATOM   2663 N  N   . THR A 1 348  ? 38.854 63.701  31.254  1.00 16.15 ? 348  THR A N   1 
ATOM   2664 C  CA  . THR A 1 348  ? 37.637 63.321  31.943  1.00 16.43 ? 348  THR A CA  1 
ATOM   2665 C  C   . THR A 1 348  ? 36.705 62.568  31.002  1.00 14.04 ? 348  THR A C   1 
ATOM   2666 O  O   . THR A 1 348  ? 35.878 61.803  31.471  1.00 13.36 ? 348  THR A O   1 
ATOM   2667 C  CB  . THR A 1 348  ? 36.898 64.566  32.508  1.00 18.36 ? 348  THR A CB  1 
ATOM   2668 O  OG1 . THR A 1 348  ? 36.745 65.551  31.467  1.00 21.01 ? 348  THR A OG1 1 
ATOM   2669 C  CG2 . THR A 1 348  ? 37.678 65.147  33.695  1.00 19.39 ? 348  THR A CG2 1 
ATOM   2670 N  N   . GLU A 1 349  ? 36.805 62.810  29.686  1.00 13.52 ? 349  GLU A N   1 
ATOM   2671 C  CA  . GLU A 1 349  ? 35.970 62.130  28.688  1.00 10.84 ? 349  GLU A CA  1 
ATOM   2672 C  C   . GLU A 1 349  ? 36.413 60.661  28.557  1.00 10.50 ? 349  GLU A C   1 
ATOM   2673 O  O   . GLU A 1 349  ? 35.587 59.788  28.473  1.00 10.69 ? 349  GLU A O   1 
ATOM   2674 C  CB  . GLU A 1 349  ? 36.093 62.826  27.326  1.00 12.78 ? 349  GLU A CB  1 
ATOM   2675 C  CG  . GLU A 1 349  ? 35.292 62.089  26.250  1.00 13.33 ? 349  GLU A CG  1 
ATOM   2676 C  CD  . GLU A 1 349  ? 35.493 62.660  24.884  1.00 14.50 ? 349  GLU A CD  1 
ATOM   2677 O  OE1 . GLU A 1 349  ? 36.197 63.680  24.789  1.00 13.36 ? 349  GLU A OE1 1 
ATOM   2678 O  OE2 . GLU A 1 349  ? 34.930 62.106  23.900  1.00 14.56 ? 349  GLU A OE2 1 
ATOM   2679 N  N   . TRP A 1 350  ? 37.718 60.419  28.522  1.00 10.87 ? 350  TRP A N   1 
ATOM   2680 C  CA  . TRP A 1 350  ? 38.234 59.058  28.505  1.00 11.81 ? 350  TRP A CA  1 
ATOM   2681 C  C   . TRP A 1 350  ? 37.722 58.320  29.716  1.00 12.21 ? 350  TRP A C   1 
ATOM   2682 O  O   . TRP A 1 350  ? 37.216 57.203  29.604  1.00 12.34 ? 350  TRP A O   1 
ATOM   2683 C  CB  . TRP A 1 350  ? 39.781 59.034  28.542  1.00 10.85 ? 350  TRP A CB  1 
ATOM   2684 C  CG  . TRP A 1 350  ? 40.446 59.276  27.177  1.00 12.38 ? 350  TRP A CG  1 
ATOM   2685 C  CD1 . TRP A 1 350  ? 40.813 60.494  26.619  1.00 11.97 ? 350  TRP A CD1 1 
ATOM   2686 C  CD2 . TRP A 1 350  ? 40.753 58.277  26.202  1.00 12.49 ? 350  TRP A CD2 1 
ATOM   2687 N  NE1 . TRP A 1 350  ? 41.338 60.302  25.339  1.00 13.43 ? 350  TRP A NE1 1 
ATOM   2688 C  CE2 . TRP A 1 350  ? 41.300 58.957  25.056  1.00 11.83 ? 350  TRP A CE2 1 
ATOM   2689 C  CE3 . TRP A 1 350  ? 40.612 56.875  26.154  1.00 13.03 ? 350  TRP A CE3 1 
ATOM   2690 C  CZ2 . TRP A 1 350  ? 41.694 58.267  23.900  1.00 13.49 ? 350  TRP A CZ2 1 
ATOM   2691 C  CZ3 . TRP A 1 350  ? 40.996 56.208  24.989  1.00 13.48 ? 350  TRP A CZ3 1 
ATOM   2692 C  CH2 . TRP A 1 350  ? 41.528 56.906  23.885  1.00 13.80 ? 350  TRP A CH2 1 
ATOM   2693 N  N   . ASP A 1 351  ? 37.824 58.939  30.890  1.00 14.53 ? 351  ASP A N   1 
ATOM   2694 C  CA  . ASP A 1 351  ? 37.344 58.276  32.079  1.00 13.73 ? 351  ASP A CA  1 
ATOM   2695 C  C   . ASP A 1 351  ? 35.847 58.025  32.105  1.00 13.46 ? 351  ASP A C   1 
ATOM   2696 O  O   . ASP A 1 351  ? 35.434 56.923  32.460  1.00 12.78 ? 351  ASP A O   1 
ATOM   2697 C  CB  . ASP A 1 351  ? 37.685 59.058  33.346  1.00 15.00 ? 351  ASP A CB  1 
ATOM   2698 C  CG  . ASP A 1 351  ? 39.147 59.140  33.594  1.00 18.93 ? 351  ASP A CG  1 
ATOM   2699 O  OD1 . ASP A 1 351  ? 39.820 58.088  33.527  1.00 21.32 ? 351  ASP A OD1 1 
ATOM   2700 O  OD2 . ASP A 1 351  ? 39.595 60.260  33.901  1.00 26.13 ? 351  ASP A OD2 1 
ATOM   2701 N  N   . VAL A 1 352  ? 35.048 58.989  31.674  1.00 12.57 ? 352  VAL A N   1 
ATOM   2702 C  CA  . VAL A 1 352  ? 33.612 58.785  31.781  1.00 14.45 ? 352  VAL A CA  1 
ATOM   2703 C  C   . VAL A 1 352  ? 33.157 57.680  30.820  1.00 13.82 ? 352  VAL A C   1 
ATOM   2704 O  O   . VAL A 1 352  ? 32.217 56.952  31.101  1.00 15.31 ? 352  VAL A O   1 
ATOM   2705 C  CB  . VAL A 1 352  ? 32.824 60.162  31.610  1.00 15.56 ? 352  VAL A CB  1 
ATOM   2706 C  CG1 . VAL A 1 352  ? 32.658 60.561  30.181  1.00 15.64 ? 352  VAL A CG1 1 
ATOM   2707 C  CG2 . VAL A 1 352  ? 31.495 60.099  32.329  1.00 18.38 ? 352  VAL A CG2 1 
ATOM   2708 N  N   . GLN A 1 353  ? 33.768 57.594  29.633  1.00 13.12 ? 353  GLN A N   1 
ATOM   2709 C  CA  . GLN A 1 353  ? 33.363 56.535  28.701  1.00 11.92 ? 353  GLN A CA  1 
ATOM   2710 C  C   . GLN A 1 353  ? 33.902 55.201  29.184  1.00 12.93 ? 353  GLN A C   1 
ATOM   2711 O  O   . GLN A 1 353  ? 33.167 54.227  29.267  1.00 12.15 ? 353  GLN A O   1 
ATOM   2712 C  CB  . GLN A 1 353  ? 33.859 56.849  27.236  1.00 10.90 ? 353  GLN A CB  1 
ATOM   2713 C  CG  . GLN A 1 353  ? 33.318 58.148  26.636  1.00 12.40 ? 353  GLN A CG  1 
ATOM   2714 C  CD  . GLN A 1 353  ? 31.838 58.094  26.178  1.00 12.91 ? 353  GLN A CD  1 
ATOM   2715 O  OE1 . GLN A 1 353  ? 31.027 57.376  26.758  1.00 13.02 ? 353  GLN A OE1 1 
ATOM   2716 N  NE2 . GLN A 1 353  ? 31.480 58.871  25.165  1.00 13.51 ? 353  GLN A NE2 1 
ATOM   2717 N  N   . ARG A 1 354  ? 35.183 55.145  29.512  1.00 12.86 ? 354  ARG A N   1 
ATOM   2718 C  CA  . ARG A 1 354  ? 35.767 53.879  29.929  1.00 11.78 ? 354  ARG A CA  1 
ATOM   2719 C  C   . ARG A 1 354  ? 35.125 53.261  31.171  1.00 14.57 ? 354  ARG A C   1 
ATOM   2720 O  O   . ARG A 1 354  ? 34.744 52.094  31.168  1.00 13.31 ? 354  ARG A O   1 
ATOM   2721 C  CB  . ARG A 1 354  ? 37.258 54.056  30.191  1.00 12.37 ? 354  ARG A CB  1 
ATOM   2722 C  CG  . ARG A 1 354  ? 37.941 52.697  30.597  1.00 13.33 ? 354  ARG A CG  1 
ATOM   2723 C  CD  . ARG A 1 354  ? 39.486 52.891  30.840  1.00 14.93 ? 354  ARG A CD  1 
ATOM   2724 N  NE  . ARG A 1 354  ? 39.796 53.862  31.891  1.00 13.41 ? 354  ARG A NE  1 
ATOM   2725 C  CZ  . ARG A 1 354  ? 39.623 53.652  33.196  1.00 14.46 ? 354  ARG A CZ  1 
ATOM   2726 N  NH1 . ARG A 1 354  ? 39.125 52.492  33.640  1.00 14.35 ? 354  ARG A NH1 1 
ATOM   2727 N  NH2 . ARG A 1 354  ? 39.979 54.603  34.058  1.00 16.62 ? 354  ARG A NH2 1 
ATOM   2728 N  N   . VAL A 1 355  ? 35.011 54.041  32.248  1.00 12.54 ? 355  VAL A N   1 
ATOM   2729 C  CA  . VAL A 1 355  ? 34.449 53.493  33.453  1.00 12.08 ? 355  VAL A CA  1 
ATOM   2730 C  C   . VAL A 1 355  ? 32.983 53.050  33.378  1.00 12.07 ? 355  VAL A C   1 
ATOM   2731 O  O   . VAL A 1 355  ? 32.657 52.011  33.945  1.00 12.24 ? 355  VAL A O   1 
ATOM   2732 C  CB  . VAL A 1 355  ? 34.682 54.502  34.591  1.00 14.87 ? 355  VAL A CB  1 
ATOM   2733 C  CG1 . VAL A 1 355  ? 34.083 53.997  35.918  1.00 18.97 ? 355  VAL A CG1 1 
ATOM   2734 C  CG2 . VAL A 1 355  ? 36.184 54.710  34.740  1.00 16.91 ? 355  VAL A CG2 1 
ATOM   2735 N  N   . ASN A 1 356  ? 32.127 53.797  32.681  1.00 12.08 ? 356  ASN A N   1 
ATOM   2736 C  CA  . ASN A 1 356  ? 30.722 53.426  32.620  1.00 13.53 ? 356  ASN A CA  1 
ATOM   2737 C  C   . ASN A 1 356  ? 30.618 52.204  31.754  1.00 13.03 ? 356  ASN A C   1 
ATOM   2738 O  O   . ASN A 1 356  ? 29.843 51.291  32.042  1.00 12.92 ? 356  ASN A O   1 
ATOM   2739 C  CB  . ASN A 1 356  ? 29.899 54.622  32.148  1.00 13.04 ? 356  ASN A CB  1 
ATOM   2740 C  CG  . ASN A 1 356  ? 29.711 55.626  33.268  1.00 15.91 ? 356  ASN A CG  1 
ATOM   2741 O  OD1 . ASN A 1 356  ? 29.121 55.284  34.316  1.00 14.45 ? 356  ASN A OD1 1 
ATOM   2742 N  ND2 . ASN A 1 356  ? 30.216 56.864  33.087  1.00 14.63 ? 356  ASN A ND2 1 
ATOM   2743 N  N   . TYR A 1 357  ? 31.428 52.120  30.704  1.00 12.85 ? 357  TYR A N   1 
ATOM   2744 C  CA  . TYR A 1 357  ? 31.314 50.900  29.889  1.00 11.85 ? 357  TYR A CA  1 
ATOM   2745 C  C   . TYR A 1 357  ? 31.889 49.704  30.633  1.00 13.75 ? 357  TYR A C   1 
ATOM   2746 O  O   . TYR A 1 357  ? 31.347 48.584  30.550  1.00 13.15 ? 357  TYR A O   1 
ATOM   2747 C  CB  . TYR A 1 357  ? 31.963 51.117  28.508  1.00 12.13 ? 357  TYR A CB  1 
ATOM   2748 C  CG  . TYR A 1 357  ? 30.950 51.649  27.502  1.00 10.21 ? 357  TYR A CG  1 
ATOM   2749 C  CD1 . TYR A 1 357  ? 30.174 50.736  26.790  1.00 12.03 ? 357  TYR A CD1 1 
ATOM   2750 C  CD2 . TYR A 1 357  ? 30.718 53.007  27.322  1.00 10.90 ? 357  TYR A CD2 1 
ATOM   2751 C  CE1 . TYR A 1 357  ? 29.192 51.173  25.943  1.00 10.94 ? 357  TYR A CE1 1 
ATOM   2752 C  CE2 . TYR A 1 357  ? 29.750 53.430  26.478  1.00 9.98  ? 357  TYR A CE2 1 
ATOM   2753 C  CZ  . TYR A 1 357  ? 28.986 52.518  25.799  1.00 10.37 ? 357  TYR A CZ  1 
ATOM   2754 O  OH  . TYR A 1 357  ? 28.007 52.929  24.925  1.00 10.94 ? 357  TYR A OH  1 
ATOM   2755 N  N   . GLU A 1 358  ? 32.957 49.887  31.414  1.00 13.21 ? 358  GLU A N   1 
ATOM   2756 C  CA  . GLU A 1 358  ? 33.441 48.723  32.144  1.00 13.18 ? 358  GLU A CA  1 
ATOM   2757 C  C   . GLU A 1 358  ? 32.444 48.229  33.182  1.00 13.75 ? 358  GLU A C   1 
ATOM   2758 O  O   . GLU A 1 358  ? 32.394 47.027  33.402  1.00 13.56 ? 358  GLU A O   1 
ATOM   2759 C  CB  . GLU A 1 358  ? 34.786 49.017  32.774  1.00 14.25 ? 358  GLU A CB  1 
ATOM   2760 C  CG  . GLU A 1 358  ? 35.748 49.211  31.618  1.00 17.66 ? 358  GLU A CG  1 
ATOM   2761 C  CD  . GLU A 1 358  ? 37.179 49.475  31.987  1.00 20.29 ? 358  GLU A CD  1 
ATOM   2762 O  OE1 . GLU A 1 358  ? 37.455 49.970  33.063  1.00 20.44 ? 358  GLU A OE1 1 
ATOM   2763 O  OE2 . GLU A 1 358  ? 38.075 49.230  31.126  1.00 24.28 ? 358  GLU A OE2 1 
ATOM   2764 N  N   . ARG A 1 359  ? 31.626 49.118  33.768  1.00 13.20 ? 359  ARG A N   1 
ATOM   2765 C  CA  . ARG A 1 359  ? 30.604 48.629  34.732  1.00 13.84 ? 359  ARG A CA  1 
ATOM   2766 C  C   . ARG A 1 359  ? 29.531 47.819  33.950  1.00 12.25 ? 359  ARG A C   1 
ATOM   2767 O  O   . ARG A 1 359  ? 29.080 46.759  34.420  1.00 15.34 ? 359  ARG A O   1 
ATOM   2768 C  CB  . ARG A 1 359  ? 29.930 49.797  35.501  1.00 17.43 ? 359  ARG A CB  1 
ATOM   2769 C  CG  . ARG A 1 359  ? 30.782 50.443  36.567  1.00 21.19 ? 359  ARG A CG  1 
ATOM   2770 C  CD  . ARG A 1 359  ? 30.070 51.696  37.136  1.00 25.04 ? 359  ARG A CD  1 
ATOM   2771 N  NE  . ARG A 1 359  ? 31.039 52.559  37.824  1.00 27.21 ? 359  ARG A NE  1 
ATOM   2772 C  CZ  . ARG A 1 359  ? 31.144 53.887  37.667  1.00 28.43 ? 359  ARG A CZ  1 
ATOM   2773 N  NH1 . ARG A 1 359  ? 30.328 54.579  36.841  1.00 26.94 ? 359  ARG A NH1 1 
ATOM   2774 N  NH2 . ARG A 1 359  ? 32.119 54.519  38.321  1.00 30.75 ? 359  ARG A NH2 1 
ATOM   2775 N  N   . LEU A 1 360  ? 29.142 48.309  32.756  1.00 12.42 ? 360  LEU A N   1 
ATOM   2776 C  CA  . LEU A 1 360  ? 28.129 47.629  31.972  1.00 10.72 ? 360  LEU A CA  1 
ATOM   2777 C  C   . LEU A 1 360  ? 28.710 46.280  31.581  1.00 11.70 ? 360  LEU A C   1 
ATOM   2778 O  O   . LEU A 1 360  ? 28.027 45.277  31.689  1.00 13.61 ? 360  LEU A O   1 
ATOM   2779 C  CB  . LEU A 1 360  ? 27.744 48.453  30.752  1.00 13.85 ? 360  LEU A CB  1 
ATOM   2780 C  CG  . LEU A 1 360  ? 26.902 49.690  31.129  1.00 13.96 ? 360  LEU A CG  1 
ATOM   2781 C  CD1 . LEU A 1 360  ? 26.933 50.734  30.076  1.00 15.76 ? 360  LEU A CD1 1 
ATOM   2782 C  CD2 . LEU A 1 360  ? 25.440 49.232  31.414  1.00 16.69 ? 360  LEU A CD2 1 
ATOM   2783 N  N   . PHE A 1 361  ? 29.970 46.198  31.119  1.00 10.71 ? 361  PHE A N   1 
ATOM   2784 C  CA  . PHE A 1 361  ? 30.534 44.874  30.773  1.00 12.79 ? 361  PHE A CA  1 
ATOM   2785 C  C   . PHE A 1 361  ? 30.623 43.921  31.945  1.00 13.42 ? 361  PHE A C   1 
ATOM   2786 O  O   . PHE A 1 361  ? 30.342 42.738  31.808  1.00 13.81 ? 361  PHE A O   1 
ATOM   2787 C  CB  . PHE A 1 361  ? 31.990 44.956  30.211  1.00 11.00 ? 361  PHE A CB  1 
ATOM   2788 C  CG  . PHE A 1 361  ? 32.158 45.797  28.958  1.00 12.32 ? 361  PHE A CG  1 
ATOM   2789 C  CD1 . PHE A 1 361  ? 31.108 46.006  28.075  1.00 11.37 ? 361  PHE A CD1 1 
ATOM   2790 C  CD2 . PHE A 1 361  ? 33.398 46.396  28.692  1.00 11.62 ? 361  PHE A CD2 1 
ATOM   2791 C  CE1 . PHE A 1 361  ? 31.271 46.810  26.929  1.00 13.27 ? 361  PHE A CE1 1 
ATOM   2792 C  CE2 . PHE A 1 361  ? 33.559 47.196  27.559  1.00 14.32 ? 361  PHE A CE2 1 
ATOM   2793 C  CZ  . PHE A 1 361  ? 32.510 47.404  26.688  1.00 12.44 ? 361  PHE A CZ  1 
ATOM   2794 N  N   . GLU A 1 362  ? 31.090 44.397  33.104  1.00 13.64 ? 362  GLU A N   1 
ATOM   2795 C  CA  . GLU A 1 362  ? 31.184 43.456  34.233  1.00 14.45 ? 362  GLU A CA  1 
ATOM   2796 C  C   . GLU A 1 362  ? 29.800 42.875  34.583  1.00 12.44 ? 362  GLU A C   1 
ATOM   2797 O  O   . GLU A 1 362  ? 29.692 41.692  34.837  1.00 14.52 ? 362  GLU A O   1 
ATOM   2798 C  CB  . GLU A 1 362  ? 31.757 44.087  35.511  1.00 16.28 ? 362  GLU A CB  1 
ATOM   2799 C  CG  . GLU A 1 362  ? 31.998 43.001  36.630  1.00 19.81 ? 362  GLU A CG  1 
ATOM   2800 C  CD  . GLU A 1 362  ? 32.426 43.614  37.971  1.00 23.43 ? 362  GLU A CD  1 
ATOM   2801 O  OE1 . GLU A 1 362  ? 32.871 44.779  37.959  1.00 24.45 ? 362  GLU A OE1 1 
ATOM   2802 O  OE2 . GLU A 1 362  ? 32.314 42.931  39.025  1.00 21.71 ? 362  GLU A OE2 1 
ATOM   2803 N  N   . HIS A 1 363  ? 28.754 43.681  34.578  1.00 14.63 ? 363  HIS A N   1 
ATOM   2804 C  CA  . HIS A 1 363  ? 27.428 43.142  34.896  1.00 15.24 ? 363  HIS A CA  1 
ATOM   2805 C  C   . HIS A 1 363  ? 26.951 42.203  33.744  1.00 14.68 ? 363  HIS A C   1 
ATOM   2806 O  O   . HIS A 1 363  ? 26.595 41.024  33.998  1.00 13.83 ? 363  HIS A O   1 
ATOM   2807 C  CB  . HIS A 1 363  ? 26.425 44.278  35.143  1.00 17.82 ? 363  HIS A CB  1 
ATOM   2808 C  CG  . HIS A 1 363  ? 25.005 43.822  35.334  1.00 18.45 ? 363  HIS A CG  1 
ATOM   2809 N  ND1 . HIS A 1 363  ? 24.556 43.269  36.516  1.00 20.15 ? 363  HIS A ND1 1 
ATOM   2810 C  CD2 . HIS A 1 363  ? 23.949 43.798  34.481  1.00 20.62 ? 363  HIS A CD2 1 
ATOM   2811 C  CE1 . HIS A 1 363  ? 23.288 42.921  36.388  1.00 18.78 ? 363  HIS A CE1 1 
ATOM   2812 N  NE2 . HIS A 1 363  ? 22.891 43.231  35.164  1.00 21.88 ? 363  HIS A NE2 1 
ATOM   2813 N  N   . ILE A 1 364  ? 26.900 42.686  32.508  1.00 13.85 ? 364  ILE A N   1 
ATOM   2814 C  CA  . ILE A 1 364  ? 26.416 41.869  31.384  1.00 14.50 ? 364  ILE A CA  1 
ATOM   2815 C  C   . ILE A 1 364  ? 27.158 40.569  31.254  1.00 12.52 ? 364  ILE A C   1 
ATOM   2816 O  O   . ILE A 1 364  ? 26.554 39.490  31.135  1.00 14.03 ? 364  ILE A O   1 
ATOM   2817 C  CB  . ILE A 1 364  ? 26.541 42.626  30.057  1.00 14.06 ? 364  ILE A CB  1 
ATOM   2818 C  CG1 . ILE A 1 364  ? 25.626 43.853  30.107  1.00 14.37 ? 364  ILE A CG1 1 
ATOM   2819 C  CG2 . ILE A 1 364  ? 26.267 41.654  28.840  1.00 13.69 ? 364  ILE A CG2 1 
ATOM   2820 C  CD1 . ILE A 1 364  ? 25.928 44.913  29.058  1.00 13.15 ? 364  ILE A CD1 1 
ATOM   2821 N  N   . ASN A 1 365  ? 28.459 40.615  31.336  1.00 12.43 ? 365  ASN A N   1 
ATOM   2822 C  CA  . ASN A 1 365  ? 29.224 39.386  31.152  1.00 13.66 ? 365  ASN A CA  1 
ATOM   2823 C  C   . ASN A 1 365  ? 29.028 38.329  32.230  1.00 16.17 ? 365  ASN A C   1 
ATOM   2824 O  O   . ASN A 1 365  ? 29.269 37.153  31.965  1.00 16.40 ? 365  ASN A O   1 
ATOM   2825 C  CB  . ASN A 1 365  ? 30.711 39.700  30.964  1.00 13.65 ? 365  ASN A CB  1 
ATOM   2826 C  CG  . ASN A 1 365  ? 30.973 40.504  29.628  1.00 11.15 ? 365  ASN A CG  1 
ATOM   2827 O  OD1 . ASN A 1 365  ? 30.075 40.699  28.791  1.00 13.77 ? 365  ASN A OD1 1 
ATOM   2828 N  ND2 . ASN A 1 365  ? 32.177 41.010  29.494  1.00 11.24 ? 365  ASN A ND2 1 
ATOM   2829 N  N   . SER A 1 366  ? 28.536 38.777  33.391  1.00 18.44 ? 366  SER A N   1 
ATOM   2830 C  CA  . SER A 1 366  ? 28.299 37.916  34.559  1.00 19.58 ? 366  SER A CA  1 
ATOM   2831 C  C   . SER A 1 366  ? 26.867 37.411  34.672  1.00 21.24 ? 366  SER A C   1 
ATOM   2832 O  O   . SER A 1 366  ? 26.576 36.526  35.477  1.00 22.91 ? 366  SER A O   1 
ATOM   2833 C  CB  . SER A 1 366  ? 28.680 38.694  35.851  1.00 20.25 ? 366  SER A CB  1 
ATOM   2834 O  OG  . SER A 1 366  ? 27.778 39.783  36.096  1.00 20.22 ? 366  SER A OG  1 
ATOM   2835 N  N   . GLN A 1 367  ? 25.972 37.950  33.854  1.00 21.60 ? 367  GLN A N   1 
ATOM   2836 C  CA  . GLN A 1 367  ? 24.571 37.573  33.871  1.00 23.11 ? 367  GLN A CA  1 
ATOM   2837 C  C   . GLN A 1 367  ? 24.361 36.619  32.715  1.00 22.40 ? 367  GLN A C   1 
ATOM   2838 O  O   . GLN A 1 367  ? 24.148 37.028  31.551  1.00 21.24 ? 367  GLN A O   1 
ATOM   2839 C  CB  . GLN A 1 367  ? 23.690 38.803  33.698  1.00 24.28 ? 367  GLN A CB  1 
ATOM   2840 C  CG  . GLN A 1 367  ? 23.600 39.671  34.929  1.00 29.40 ? 367  GLN A CG  1 
ATOM   2841 C  CD  . GLN A 1 367  ? 23.032 38.878  36.076  1.00 31.70 ? 367  GLN A CD  1 
ATOM   2842 O  OE1 . GLN A 1 367  ? 23.796 38.752  37.150  1.00 34.66 ? 367  GLN A OE1 1 
ATOM   2843 N  NE2 . GLN A 1 367  ? 21.932 38.343  35.976  1.00 33.76 ? 367  GLN A NE2 1 
ATOM   2844 N  N   . ALA A 1 368  ? 24.420 35.331  33.038  1.00 21.83 ? 368  ALA A N   1 
ATOM   2845 C  CA  . ALA A 1 368  ? 24.256 34.257  32.051  1.00 20.72 ? 368  ALA A CA  1 
ATOM   2846 C  C   . ALA A 1 368  ? 23.020 34.381  31.144  1.00 21.02 ? 368  ALA A C   1 
ATOM   2847 O  O   . ALA A 1 368  ? 23.091 34.008  29.975  1.00 20.63 ? 368  ALA A O   1 
ATOM   2848 C  CB  . ALA A 1 368  ? 24.232 32.873  32.771  1.00 21.16 ? 368  ALA A CB  1 
ATOM   2849 N  N   . HIS A 1 369  ? 21.895 34.879  31.667  1.00 19.85 ? 369  HIS A N   1 
ATOM   2850 C  CA  . HIS A 1 369  ? 20.699 34.991  30.853  1.00 20.36 ? 369  HIS A CA  1 
ATOM   2851 C  C   . HIS A 1 369  ? 20.811 35.936  29.636  1.00 20.21 ? 369  HIS A C   1 
ATOM   2852 O  O   . HIS A 1 369  ? 19.942 35.933  28.753  1.00 20.61 ? 369  HIS A O   1 
ATOM   2853 C  CB  . HIS A 1 369  ? 19.508 35.416  31.728  1.00 22.41 ? 369  HIS A CB  1 
ATOM   2854 C  CG  . HIS A 1 369  ? 19.646 36.786  32.316  1.00 23.83 ? 369  HIS A CG  1 
ATOM   2855 N  ND1 . HIS A 1 369  ? 19.182 37.925  31.686  1.00 25.42 ? 369  HIS A ND1 1 
ATOM   2856 C  CD2 . HIS A 1 369  ? 20.238 37.200  33.458  1.00 23.51 ? 369  HIS A CD2 1 
ATOM   2857 C  CE1 . HIS A 1 369  ? 19.493 38.983  32.412  1.00 24.93 ? 369  HIS A CE1 1 
ATOM   2858 N  NE2 . HIS A 1 369  ? 20.136 38.572  33.493  1.00 25.72 ? 369  HIS A NE2 1 
ATOM   2859 N  N   . PHE A 1 370  ? 21.871 36.750  29.573  1.00 19.74 ? 370  PHE A N   1 
ATOM   2860 C  CA  . PHE A 1 370  ? 22.018 37.624  28.391  1.00 18.55 ? 370  PHE A CA  1 
ATOM   2861 C  C   . PHE A 1 370  ? 22.751 36.867  27.300  1.00 14.63 ? 370  PHE A C   1 
ATOM   2862 O  O   . PHE A 1 370  ? 22.574 37.177  26.120  1.00 15.97 ? 370  PHE A O   1 
ATOM   2863 C  CB  . PHE A 1 370  ? 22.868 38.865  28.676  1.00 18.04 ? 370  PHE A CB  1 
ATOM   2864 C  CG  . PHE A 1 370  ? 22.185 39.906  29.500  1.00 18.75 ? 370  PHE A CG  1 
ATOM   2865 C  CD1 . PHE A 1 370  ? 20.916 40.413  29.143  1.00 20.80 ? 370  PHE A CD1 1 
ATOM   2866 C  CD2 . PHE A 1 370  ? 22.824 40.428  30.613  1.00 19.22 ? 370  PHE A CD2 1 
ATOM   2867 C  CE1 . PHE A 1 370  ? 20.314 41.427  29.891  1.00 22.77 ? 370  PHE A CE1 1 
ATOM   2868 C  CE2 . PHE A 1 370  ? 22.237 41.435  31.361  1.00 19.70 ? 370  PHE A CE2 1 
ATOM   2869 C  CZ  . PHE A 1 370  ? 20.999 41.934  31.013  1.00 20.48 ? 370  PHE A CZ  1 
ATOM   2870 N  N   . ASN A 1 371  ? 23.560 35.904  27.714  1.00 15.56 ? 371  ASN A N   1 
ATOM   2871 C  CA  . ASN A 1 371  ? 24.385 35.111  26.845  1.00 13.93 ? 371  ASN A CA  1 
ATOM   2872 C  C   . ASN A 1 371  ? 25.189 36.034  25.928  1.00 13.70 ? 371  ASN A C   1 
ATOM   2873 O  O   . ASN A 1 371  ? 25.212 35.841  24.723  1.00 12.98 ? 371  ASN A O   1 
ATOM   2874 C  CB  . ASN A 1 371  ? 23.538 34.122  26.031  1.00 16.13 ? 371  ASN A CB  1 
ATOM   2875 C  CG  . ASN A 1 371  ? 22.858 33.111  26.952  1.00 14.73 ? 371  ASN A CG  1 
ATOM   2876 O  OD1 . ASN A 1 371  ? 23.539 32.283  27.553  1.00 17.68 ? 371  ASN A OD1 1 
ATOM   2877 N  ND2 . ASN A 1 371  ? 21.541 33.231  27.100  1.00 15.49 ? 371  ASN A ND2 1 
ATOM   2878 N  N   . VAL A 1 372  ? 25.812 37.049  26.524  1.00 12.37 ? 372  VAL A N   1 
ATOM   2879 C  CA  . VAL A 1 372  ? 26.649 38.035  25.809  1.00 12.88 ? 372  VAL A CA  1 
ATOM   2880 C  C   . VAL A 1 372  ? 28.034 38.091  26.396  1.00 12.92 ? 372  VAL A C   1 
ATOM   2881 O  O   . VAL A 1 372  ? 28.199 37.914  27.600  1.00 13.36 ? 372  VAL A O   1 
ATOM   2882 C  CB  . VAL A 1 372  ? 25.998 39.429  25.932  1.00 13.48 ? 372  VAL A CB  1 
ATOM   2883 C  CG1 . VAL A 1 372  ? 26.953 40.544  25.430  1.00 14.17 ? 372  VAL A CG1 1 
ATOM   2884 C  CG2 . VAL A 1 372  ? 24.681 39.422  25.099  1.00 13.86 ? 372  VAL A CG2 1 
ATOM   2885 N  N   . GLN A 1 373  ? 29.074 38.289  25.585  1.00 11.49 ? 373  GLN A N   1 
ATOM   2886 C  CA  . GLN A 1 373  ? 30.420 38.524  26.126  1.00 13.09 ? 373  GLN A CA  1 
ATOM   2887 C  C   . GLN A 1 373  ? 30.825 39.849  25.417  1.00 11.38 ? 373  GLN A C   1 
ATOM   2888 O  O   . GLN A 1 373  ? 31.097 39.862  24.186  1.00 12.41 ? 373  GLN A O   1 
ATOM   2889 C  CB  . GLN A 1 373  ? 31.381 37.386  25.736  1.00 11.51 ? 373  GLN A CB  1 
ATOM   2890 C  CG  . GLN A 1 373  ? 32.883 37.611  26.118  1.00 15.31 ? 373  GLN A CG  1 
ATOM   2891 C  CD  . GLN A 1 373  ? 33.108 37.954  27.608  1.00 15.99 ? 373  GLN A CD  1 
ATOM   2892 O  OE1 . GLN A 1 373  ? 32.412 37.454  28.499  1.00 19.68 ? 373  GLN A OE1 1 
ATOM   2893 N  NE2 . GLN A 1 373  ? 34.108 38.811  27.871  1.00 15.02 ? 373  GLN A NE2 1 
ATOM   2894 N  N   . ALA A 1 374  ? 30.865 40.956  26.160  1.00 11.01 ? 374  ALA A N   1 
ATOM   2895 C  CA  . ALA A 1 374  ? 31.192 42.260  25.610  1.00 9.25  ? 374  ALA A CA  1 
ATOM   2896 C  C   . ALA A 1 374  ? 32.496 42.790  26.109  1.00 10.81 ? 374  ALA A C   1 
ATOM   2897 O  O   . ALA A 1 374  ? 32.857 42.575  27.287  1.00 10.95 ? 374  ALA A O   1 
ATOM   2898 C  CB  . ALA A 1 374  ? 30.084 43.230  25.952  1.00 10.57 ? 374  ALA A CB  1 
ATOM   2899 N  N   . GLN A 1 375  ? 33.251 43.435  25.208  1.00 10.28 ? 375  GLN A N   1 
ATOM   2900 C  CA  . GLN A 1 375  ? 34.571 43.978  25.622  1.00 11.66 ? 375  GLN A CA  1 
ATOM   2901 C  C   . GLN A 1 375  ? 34.981 45.066  24.636  1.00 11.57 ? 375  GLN A C   1 
ATOM   2902 O  O   . GLN A 1 375  ? 34.397 45.150  23.525  1.00 10.93 ? 375  GLN A O   1 
ATOM   2903 C  CB  . GLN A 1 375  ? 35.670 42.890  25.539  1.00 13.49 ? 375  GLN A CB  1 
ATOM   2904 C  CG  . GLN A 1 375  ? 35.641 42.204  24.159  1.00 15.90 ? 375  GLN A CG  1 
ATOM   2905 C  CD  . GLN A 1 375  ? 34.851 40.899  24.251  1.00 21.31 ? 375  GLN A CD  1 
ATOM   2906 O  OE1 . GLN A 1 375  ? 35.253 39.984  24.997  1.00 21.30 ? 375  GLN A OE1 1 
ATOM   2907 N  NE2 . GLN A 1 375  ? 33.715 40.803  23.518  1.00 20.94 ? 375  GLN A NE2 1 
ATOM   2908 N  N   . PHE A 1 376  ? 35.938 45.911  25.027  1.00 10.56 ? 376  PHE A N   1 
ATOM   2909 C  CA  . PHE A 1 376  ? 36.495 46.892  24.074  1.00 10.46 ? 376  PHE A CA  1 
ATOM   2910 C  C   . PHE A 1 376  ? 37.293 46.089  23.047  1.00 12.40 ? 376  PHE A C   1 
ATOM   2911 O  O   . PHE A 1 376  ? 37.926 45.060  23.403  1.00 14.08 ? 376  PHE A O   1 
ATOM   2912 C  CB  . PHE A 1 376  ? 37.471 47.838  24.795  1.00 10.02 ? 376  PHE A CB  1 
ATOM   2913 C  CG  . PHE A 1 376  ? 36.809 48.739  25.730  1.00 11.45 ? 376  PHE A CG  1 
ATOM   2914 C  CD1 . PHE A 1 376  ? 35.802 49.563  25.304  1.00 10.17 ? 376  PHE A CD1 1 
ATOM   2915 C  CD2 . PHE A 1 376  ? 37.192 48.736  27.075  1.00 10.02 ? 376  PHE A CD2 1 
ATOM   2916 C  CE1 . PHE A 1 376  ? 35.149 50.432  26.238  1.00 12.60 ? 376  PHE A CE1 1 
ATOM   2917 C  CE2 . PHE A 1 376  ? 36.550 49.590  27.992  1.00 11.81 ? 376  PHE A CE2 1 
ATOM   2918 C  CZ  . PHE A 1 376  ? 35.538 50.433  27.577  1.00 10.94 ? 376  PHE A CZ  1 
ATOM   2919 N  N   . GLY A 1 377  ? 37.291 46.553  21.803  1.00 11.25 ? 377  GLY A N   1 
ATOM   2920 C  CA  . GLY A 1 377  ? 38.063 45.842  20.788  1.00 11.00 ? 377  GLY A CA  1 
ATOM   2921 C  C   . GLY A 1 377  ? 38.530 46.808  19.738  1.00 10.98 ? 377  GLY A C   1 
ATOM   2922 O  O   . GLY A 1 377  ? 38.222 48.025  19.835  1.00 10.98 ? 377  GLY A O   1 
ATOM   2923 N  N   . THR A 1 378  ? 39.239 46.252  18.745  1.00 11.24 ? 378  THR A N   1 
ATOM   2924 C  CA  . THR A 1 378  ? 39.723 47.002  17.605  1.00 11.78 ? 378  THR A CA  1 
ATOM   2925 C  C   . THR A 1 378  ? 38.977 46.508  16.395  1.00 9.96  ? 378  THR A C   1 
ATOM   2926 O  O   . THR A 1 378  ? 38.234 45.502  16.456  1.00 10.37 ? 378  THR A O   1 
ATOM   2927 C  CB  . THR A 1 378  ? 41.243 46.874  17.362  1.00 10.95 ? 378  THR A CB  1 
ATOM   2928 O  OG1 . THR A 1 378  ? 41.564 45.538  16.978  1.00 12.13 ? 378  THR A OG1 1 
ATOM   2929 C  CG2 . THR A 1 378  ? 42.039 47.335  18.588  1.00 12.73 ? 378  THR A CG2 1 
ATOM   2930 N  N   . LEU A 1 379  ? 39.131 47.202  15.283  1.00 9.29  ? 379  LEU A N   1 
ATOM   2931 C  CA  . LEU A 1 379  ? 38.466 46.830  14.037  1.00 9.69  ? 379  LEU A CA  1 
ATOM   2932 C  C   . LEU A 1 379  ? 38.962 45.474  13.535  1.00 8.21  ? 379  LEU A C   1 
ATOM   2933 O  O   . LEU A 1 379  ? 38.160 44.617  13.123  1.00 9.83  ? 379  LEU A O   1 
ATOM   2934 C  CB  . LEU A 1 379  ? 38.683 47.924  12.971  1.00 10.19 ? 379  LEU A CB  1 
ATOM   2935 C  CG  . LEU A 1 379  ? 37.850 47.737  11.687  1.00 9.48  ? 379  LEU A CG  1 
ATOM   2936 C  CD1 . LEU A 1 379  ? 36.314 47.709  11.932  1.00 7.08  ? 379  LEU A CD1 1 
ATOM   2937 C  CD2 . LEU A 1 379  ? 38.247 48.914  10.718  1.00 9.77  ? 379  LEU A CD2 1 
ATOM   2938 N  N   . GLN A 1 380  ? 40.285 45.267  13.574  1.00 7.95  ? 380  GLN A N   1 
ATOM   2939 C  CA  . GLN A 1 380  ? 40.822 43.998  13.148  1.00 10.05 ? 380  GLN A CA  1 
ATOM   2940 C  C   . GLN A 1 380  ? 40.317 42.860  14.004  1.00 10.70 ? 380  GLN A C   1 
ATOM   2941 O  O   . GLN A 1 380  ? 40.068 41.768  13.487  1.00 9.45  ? 380  GLN A O   1 
ATOM   2942 C  CB  . GLN A 1 380  ? 42.340 44.015  13.200  1.00 11.96 ? 380  GLN A CB  1 
ATOM   2943 C  CG  . GLN A 1 380  ? 42.985 42.739  12.572  1.00 12.24 ? 380  GLN A CG  1 
ATOM   2944 C  CD  . GLN A 1 380  ? 42.681 42.578  11.089  1.00 16.58 ? 380  GLN A CD  1 
ATOM   2945 O  OE1 . GLN A 1 380  ? 42.701 43.558  10.320  1.00 15.37 ? 380  GLN A OE1 1 
ATOM   2946 N  NE2 . GLN A 1 380  ? 42.402 41.338  10.663  1.00 17.42 ? 380  GLN A NE2 1 
ATOM   2947 N  N   . GLU A 1 381  ? 40.173 43.124  15.305  1.00 9.65  ? 381  GLU A N   1 
ATOM   2948 C  CA  . GLU A 1 381  ? 39.677 42.066  16.169  1.00 8.91  ? 381  GLU A CA  1 
ATOM   2949 C  C   . GLU A 1 381  ? 38.251 41.664  15.751  1.00 8.37  ? 381  GLU A C   1 
ATOM   2950 O  O   . GLU A 1 381  ? 37.956 40.452  15.752  1.00 9.06  ? 381  GLU A O   1 
ATOM   2951 C  CB  . GLU A 1 381  ? 39.639 42.491  17.631  1.00 11.13 ? 381  GLU A CB  1 
ATOM   2952 C  CG  . GLU A 1 381  ? 40.948 42.553  18.353  1.00 15.34 ? 381  GLU A CG  1 
ATOM   2953 C  CD  . GLU A 1 381  ? 40.609 42.823  19.828  1.00 20.00 ? 381  GLU A CD  1 
ATOM   2954 O  OE1 . GLU A 1 381  ? 40.100 41.926  20.562  1.00 24.41 ? 381  GLU A OE1 1 
ATOM   2955 O  OE2 . GLU A 1 381  ? 40.795 43.944  20.230  1.00 19.69 ? 381  GLU A OE2 1 
ATOM   2956 N  N   . TYR A 1 382  ? 37.419 42.631  15.368  1.00 8.01  ? 382  TYR A N   1 
ATOM   2957 C  CA  . TYR A 1 382  ? 36.083 42.320  14.959  1.00 8.29  ? 382  TYR A CA  1 
ATOM   2958 C  C   . TYR A 1 382  ? 36.124 41.439  13.705  1.00 8.32  ? 382  TYR A C   1 
ATOM   2959 O  O   . TYR A 1 382  ? 35.509 40.335  13.657  1.00 10.93 ? 382  TYR A O   1 
ATOM   2960 C  CB  . TYR A 1 382  ? 35.262 43.609  14.704  1.00 7.43  ? 382  TYR A CB  1 
ATOM   2961 C  CG  . TYR A 1 382  ? 33.985 43.326  13.944  1.00 7.39  ? 382  TYR A CG  1 
ATOM   2962 C  CD1 . TYR A 1 382  ? 32.890 42.754  14.591  1.00 8.36  ? 382  TYR A CD1 1 
ATOM   2963 C  CD2 . TYR A 1 382  ? 33.846 43.576  12.563  1.00 6.76  ? 382  TYR A CD2 1 
ATOM   2964 C  CE1 . TYR A 1 382  ? 31.747 42.444  13.917  1.00 8.60  ? 382  TYR A CE1 1 
ATOM   2965 C  CE2 . TYR A 1 382  ? 32.675 43.265  11.874  1.00 6.93  ? 382  TYR A CE2 1 
ATOM   2966 C  CZ  . TYR A 1 382  ? 31.623 42.695  12.577  1.00 8.56  ? 382  TYR A CZ  1 
ATOM   2967 O  OH  . TYR A 1 382  ? 30.435 42.358  11.969  1.00 8.38  ? 382  TYR A OH  1 
ATOM   2968 N  N   . PHE A 1 383  ? 36.863 41.891  12.674  1.00 8.84  ? 383  PHE A N   1 
ATOM   2969 C  CA  . PHE A 1 383  ? 36.898 41.108  11.426  1.00 9.11  ? 383  PHE A CA  1 
ATOM   2970 C  C   . PHE A 1 383  ? 37.498 39.717  11.641  1.00 9.25  ? 383  PHE A C   1 
ATOM   2971 O  O   . PHE A 1 383  ? 37.011 38.740  11.044  1.00 11.59 ? 383  PHE A O   1 
ATOM   2972 C  CB  . PHE A 1 383  ? 37.675 41.837  10.306  1.00 8.31  ? 383  PHE A CB  1 
ATOM   2973 C  CG  . PHE A 1 383  ? 36.906 43.030  9.705   1.00 9.05  ? 383  PHE A CG  1 
ATOM   2974 C  CD1 . PHE A 1 383  ? 35.715 42.816  9.049   1.00 10.40 ? 383  PHE A CD1 1 
ATOM   2975 C  CD2 . PHE A 1 383  ? 37.412 44.336  9.790   1.00 7.95  ? 383  PHE A CD2 1 
ATOM   2976 C  CE1 . PHE A 1 383  ? 34.969 43.875  8.432   1.00 9.91  ? 383  PHE A CE1 1 
ATOM   2977 C  CE2 . PHE A 1 383  ? 36.699 45.401  9.198   1.00 7.45  ? 383  PHE A CE2 1 
ATOM   2978 C  CZ  . PHE A 1 383  ? 35.471 45.168  8.514   1.00 9.24  ? 383  PHE A CZ  1 
ATOM   2979 N  N   . ASP A 1 384  ? 38.544 39.643  12.484  1.00 8.33  ? 384  ASP A N   1 
ATOM   2980 C  CA  . ASP A 1 384  ? 39.142 38.329  12.681  1.00 8.67  ? 384  ASP A CA  1 
ATOM   2981 C  C   . ASP A 1 384  ? 38.064 37.404  13.258  1.00 10.15 ? 384  ASP A C   1 
ATOM   2982 O  O   . ASP A 1 384  ? 37.977 36.209  12.847  1.00 9.62  ? 384  ASP A O   1 
ATOM   2983 C  CB  . ASP A 1 384  ? 40.310 38.407  13.687  1.00 11.67 ? 384  ASP A CB  1 
ATOM   2984 C  CG  . ASP A 1 384  ? 41.559 39.003  13.086  1.00 14.76 ? 384  ASP A CG  1 
ATOM   2985 O  OD1 . ASP A 1 384  ? 41.689 39.038  11.827  1.00 17.62 ? 384  ASP A OD1 1 
ATOM   2986 O  OD2 . ASP A 1 384  ? 42.407 39.418  13.902  1.00 19.14 ? 384  ASP A OD2 1 
ATOM   2987 N  N   . ALA A 1 385  ? 37.246 37.916  14.205  1.00 9.01  ? 385  ALA A N   1 
ATOM   2988 C  CA  . ALA A 1 385  ? 36.246 37.038  14.833  1.00 10.30 ? 385  ALA A CA  1 
ATOM   2989 C  C   . ALA A 1 385  ? 35.162 36.643  13.845  1.00 9.80  ? 385  ALA A C   1 
ATOM   2990 O  O   . ALA A 1 385  ? 34.622 35.529  13.883  1.00 11.69 ? 385  ALA A O   1 
ATOM   2991 C  CB  . ALA A 1 385  ? 35.637 37.716  16.058  1.00 10.20 ? 385  ALA A CB  1 
ATOM   2992 N  N   . VAL A 1 386  ? 34.806 37.580  12.963  1.00 10.52 ? 386  VAL A N   1 
ATOM   2993 C  CA  . VAL A 1 386  ? 33.777 37.295  11.969  1.00 9.45  ? 386  VAL A CA  1 
ATOM   2994 C  C   . VAL A 1 386  ? 34.255 36.163  11.051  1.00 12.41 ? 386  VAL A C   1 
ATOM   2995 O  O   . VAL A 1 386  ? 33.517 35.209  10.763  1.00 12.26 ? 386  VAL A O   1 
ATOM   2996 C  CB  . VAL A 1 386  ? 33.509 38.558  11.122  1.00 11.66 ? 386  VAL A CB  1 
ATOM   2997 C  CG1 . VAL A 1 386  ? 32.663 38.245  9.823   1.00 11.02 ? 386  VAL A CG1 1 
ATOM   2998 C  CG2 . VAL A 1 386  ? 32.783 39.577  11.985  1.00 11.94 ? 386  VAL A CG2 1 
ATOM   2999 N  N   . HIS A 1 387  ? 35.487 36.269  10.564  1.00 11.94 ? 387  HIS A N   1 
ATOM   3000 C  CA  . HIS A 1 387  ? 35.993 35.247  9.694   1.00 13.21 ? 387  HIS A CA  1 
ATOM   3001 C  C   . HIS A 1 387  ? 36.213 33.910  10.369  1.00 13.45 ? 387  HIS A C   1 
ATOM   3002 O  O   . HIS A 1 387  ? 36.123 32.890  9.697   1.00 12.65 ? 387  HIS A O   1 
ATOM   3003 C  CB  . HIS A 1 387  ? 37.232 35.716  8.949   1.00 11.27 ? 387  HIS A CB  1 
ATOM   3004 C  CG  . HIS A 1 387  ? 36.946 36.825  7.984   1.00 11.78 ? 387  HIS A CG  1 
ATOM   3005 N  ND1 . HIS A 1 387  ? 36.032 36.712  6.956   1.00 13.78 ? 387  HIS A ND1 1 
ATOM   3006 C  CD2 . HIS A 1 387  ? 37.397 38.108  7.950   1.00 12.40 ? 387  HIS A CD2 1 
ATOM   3007 C  CE1 . HIS A 1 387  ? 35.916 37.882  6.344   1.00 11.40 ? 387  HIS A CE1 1 
ATOM   3008 N  NE2 . HIS A 1 387  ? 36.727 38.743  6.934   1.00 13.46 ? 387  HIS A NE2 1 
ATOM   3009 N  N   . GLN A 1 388  ? 36.476 33.898  11.672  1.00 13.35 ? 388  GLN A N   1 
ATOM   3010 C  CA  . GLN A 1 388  ? 36.586 32.604  12.386  1.00 15.10 ? 388  GLN A CA  1 
ATOM   3011 C  C   . GLN A 1 388  ? 35.217 31.974  12.406  1.00 14.71 ? 388  GLN A C   1 
ATOM   3012 O  O   . GLN A 1 388  ? 35.099 30.752  12.312  1.00 16.15 ? 388  GLN A O   1 
ATOM   3013 C  CB  . GLN A 1 388  ? 37.077 32.817  13.816  1.00 16.05 ? 388  GLN A CB  1 
ATOM   3014 C  CG  . GLN A 1 388  ? 38.600 32.948  13.938  1.00 22.41 ? 388  GLN A CG  1 
ATOM   3015 C  CD  . GLN A 1 388  ? 39.051 33.857  15.088  1.00 26.09 ? 388  GLN A CD  1 
ATOM   3016 O  OE1 . GLN A 1 388  ? 38.252 34.225  15.948  1.00 28.15 ? 388  GLN A OE1 1 
ATOM   3017 N  NE2 . GLN A 1 388  ? 40.352 34.223  15.099  1.00 26.28 ? 388  GLN A NE2 1 
ATOM   3018 N  N   . ALA A 1 389  ? 34.153 32.763  12.527  1.00 13.60 ? 389  ALA A N   1 
ATOM   3019 C  CA  . ALA A 1 389  ? 32.792 32.217  12.515  1.00 14.40 ? 389  ALA A CA  1 
ATOM   3020 C  C   . ALA A 1 389  ? 32.447 31.690  11.134  1.00 16.33 ? 389  ALA A C   1 
ATOM   3021 O  O   . ALA A 1 389  ? 31.830 30.648  11.014  1.00 16.39 ? 389  ALA A O   1 
ATOM   3022 C  CB  . ALA A 1 389  ? 31.775 33.263  12.957  1.00 14.95 ? 389  ALA A CB  1 
ATOM   3023 N  N   . GLU A 1 390  ? 32.830 32.428  10.080  1.00 16.18 ? 390  GLU A N   1 
ATOM   3024 C  CA  . GLU A 1 390  ? 32.618 32.001  8.692   1.00 17.61 ? 390  GLU A CA  1 
ATOM   3025 C  C   . GLU A 1 390  ? 33.312 30.623  8.496   1.00 19.62 ? 390  GLU A C   1 
ATOM   3026 O  O   . GLU A 1 390  ? 32.700 29.668  7.985   1.00 18.90 ? 390  GLU A O   1 
ATOM   3027 C  CB  . GLU A 1 390  ? 33.279 33.046  7.755   1.00 15.23 ? 390  GLU A CB  1 
ATOM   3028 C  CG  . GLU A 1 390  ? 33.099 32.797  6.268   1.00 16.47 ? 390  GLU A CG  1 
ATOM   3029 C  CD  . GLU A 1 390  ? 33.824 33.825  5.426   1.00 21.24 ? 390  GLU A CD  1 
ATOM   3030 O  OE1 . GLU A 1 390  ? 34.715 34.526  5.953   1.00 20.59 ? 390  GLU A OE1 1 
ATOM   3031 O  OE2 . GLU A 1 390  ? 33.513 33.939  4.218   1.00 23.05 ? 390  GLU A OE2 1 
ATOM   3032 N  N   . ARG A 1 391  ? 34.587 30.542  8.868   1.00 20.41 ? 391  ARG A N   1 
ATOM   3033 C  CA  . ARG A 1 391  ? 35.331 29.304  8.732   1.00 22.09 ? 391  ARG A CA  1 
ATOM   3034 C  C   . ARG A 1 391  ? 34.683 28.166  9.501   1.00 23.45 ? 391  ARG A C   1 
ATOM   3035 O  O   . ARG A 1 391  ? 34.743 27.012  9.039   1.00 26.44 ? 391  ARG A O   1 
ATOM   3036 C  CB  . ARG A 1 391  ? 36.764 29.465  9.173   1.00 22.36 ? 391  ARG A CB  1 
ATOM   3037 C  CG  . ARG A 1 391  ? 37.594 30.250  8.168   1.00 25.13 ? 391  ARG A CG  1 
ATOM   3038 C  CD  . ARG A 1 391  ? 39.072 30.140  8.446   1.00 28.31 ? 391  ARG A CD  1 
ATOM   3039 N  NE  . ARG A 1 391  ? 39.426 30.551  9.805   1.00 31.18 ? 391  ARG A NE  1 
ATOM   3040 C  CZ  . ARG A 1 391  ? 39.674 31.812  10.161  1.00 32.77 ? 391  ARG A CZ  1 
ATOM   3041 N  NH1 . ARG A 1 391  ? 39.612 32.798  9.255   1.00 31.98 ? 391  ARG A NH1 1 
ATOM   3042 N  NH2 . ARG A 1 391  ? 39.984 32.080  11.424  1.00 34.36 ? 391  ARG A NH2 1 
ATOM   3043 N  N   . ALA A 1 392  ? 34.104 28.443  10.664  1.00 23.76 ? 392  ALA A N   1 
ATOM   3044 C  CA  . ALA A 1 392  ? 33.426 27.383  11.426  1.00 24.44 ? 392  ALA A CA  1 
ATOM   3045 C  C   . ALA A 1 392  ? 32.101 27.003  10.721  1.00 25.25 ? 392  ALA A C   1 
ATOM   3046 O  O   . ALA A 1 392  ? 31.343 26.152  11.221  1.00 27.48 ? 392  ALA A O   1 
ATOM   3047 C  CB  . ALA A 1 392  ? 33.145 27.838  12.843  1.00 23.87 ? 392  ALA A CB  1 
ATOM   3048 N  N   . GLY A 1 393  ? 31.841 27.601  9.551   1.00 24.72 ? 393  GLY A N   1 
ATOM   3049 C  CA  . GLY A 1 393  ? 30.617 27.286  8.820   1.00 22.62 ? 393  GLY A CA  1 
ATOM   3050 C  C   . GLY A 1 393  ? 29.356 27.901  9.394   1.00 20.64 ? 393  GLY A C   1 
ATOM   3051 O  O   . GLY A 1 393  ? 28.241 27.493  9.082   1.00 22.04 ? 393  GLY A O   1 
ATOM   3052 N  N   . GLN A 1 394  ? 29.524 28.956  10.169  1.00 21.37 ? 394  GLN A N   1 
ATOM   3053 C  CA  . GLN A 1 394  ? 28.374 29.576  10.804  1.00 22.02 ? 394  GLN A CA  1 
ATOM   3054 C  C   . GLN A 1 394  ? 27.655 30.637  9.960   1.00 21.44 ? 394  GLN A C   1 
ATOM   3055 O  O   . GLN A 1 394  ? 26.552 31.076  10.283  1.00 22.44 ? 394  GLN A O   1 
ATOM   3056 C  CB  . GLN A 1 394  ? 28.840 30.133  12.157  1.00 24.06 ? 394  GLN A CB  1 
ATOM   3057 C  CG  . GLN A 1 394  ? 27.800 30.871  12.960  1.00 25.20 ? 394  GLN A CG  1 
ATOM   3058 C  CD  . GLN A 1 394  ? 28.451 31.781  13.996  1.00 26.50 ? 394  GLN A CD  1 
ATOM   3059 O  OE1 . GLN A 1 394  ? 28.228 32.992  13.980  1.00 23.57 ? 394  GLN A OE1 1 
ATOM   3060 N  NE2 . GLN A 1 394  ? 29.284 31.200  14.884  1.00 26.07 ? 394  GLN A NE2 1 
ATOM   3061 N  N   . ALA A 1 395  ? 28.289 31.036  8.867   1.00 19.65 ? 395  ALA A N   1 
ATOM   3062 C  CA  . ALA A 1 395  ? 27.723 32.023  7.967   1.00 18.59 ? 395  ALA A CA  1 
ATOM   3063 C  C   . ALA A 1 395  ? 28.421 31.971  6.617   1.00 17.91 ? 395  ALA A C   1 
ATOM   3064 O  O   . ALA A 1 395  ? 29.578 31.569  6.504   1.00 17.52 ? 395  ALA A O   1 
ATOM   3065 C  CB  . ALA A 1 395  ? 27.878 33.435  8.568   1.00 19.33 ? 395  ALA A CB  1 
ATOM   3066 N  N   . GLU A 1 396  ? 27.694 32.371  5.591   1.00 19.53 ? 396  GLU A N   1 
ATOM   3067 C  CA  . GLU A 1 396  ? 28.259 32.480  4.247   1.00 19.85 ? 396  GLU A CA  1 
ATOM   3068 C  C   . GLU A 1 396  ? 27.844 33.881  3.838   1.00 17.25 ? 396  GLU A C   1 
ATOM   3069 O  O   . GLU A 1 396  ? 26.790 34.380  4.256   1.00 19.08 ? 396  GLU A O   1 
ATOM   3070 C  CB  . GLU A 1 396  ? 27.663 31.439  3.302   1.00 23.77 ? 396  GLU A CB  1 
ATOM   3071 C  CG  . GLU A 1 396  ? 26.161 31.523  3.310   1.00 30.05 ? 396  GLU A CG  1 
ATOM   3072 C  CD  . GLU A 1 396  ? 25.493 30.204  2.954   1.00 32.92 ? 396  GLU A CD  1 
ATOM   3073 O  OE1 . GLU A 1 396  ? 26.165 29.375  2.301   1.00 34.65 ? 396  GLU A OE1 1 
ATOM   3074 O  OE2 . GLU A 1 396  ? 24.304 30.019  3.327   1.00 35.51 ? 396  GLU A OE2 1 
ATOM   3075 N  N   . PHE A 1 397  ? 28.669 34.523  3.037   1.00 14.12 ? 397  PHE A N   1 
ATOM   3076 C  CA  . PHE A 1 397  ? 28.348 35.884  2.692   1.00 12.15 ? 397  PHE A CA  1 
ATOM   3077 C  C   . PHE A 1 397  ? 28.022 36.096  1.225   1.00 11.20 ? 397  PHE A C   1 
ATOM   3078 O  O   . PHE A 1 397  ? 28.663 35.504  0.390   1.00 13.24 ? 397  PHE A O   1 
ATOM   3079 C  CB  . PHE A 1 397  ? 29.561 36.776  3.043   1.00 12.96 ? 397  PHE A CB  1 
ATOM   3080 C  CG  . PHE A 1 397  ? 29.884 36.800  4.499   1.00 11.12 ? 397  PHE A CG  1 
ATOM   3081 C  CD1 . PHE A 1 397  ? 29.060 37.522  5.383   1.00 11.54 ? 397  PHE A CD1 1 
ATOM   3082 C  CD2 . PHE A 1 397  ? 30.949 36.060  5.019   1.00 12.57 ? 397  PHE A CD2 1 
ATOM   3083 C  CE1 . PHE A 1 397  ? 29.250 37.518  6.794   1.00 9.85  ? 397  PHE A CE1 1 
ATOM   3084 C  CE2 . PHE A 1 397  ? 31.158 36.044  6.447   1.00 12.73 ? 397  PHE A CE2 1 
ATOM   3085 C  CZ  . PHE A 1 397  ? 30.301 36.771  7.321   1.00 12.00 ? 397  PHE A CZ  1 
ATOM   3086 N  N   . PRO A 1 398  ? 27.109 37.038  0.924   1.00 10.41 ? 398  PRO A N   1 
ATOM   3087 C  CA  . PRO A 1 398  ? 26.734 37.350  -0.478  1.00 9.76  ? 398  PRO A CA  1 
ATOM   3088 C  C   . PRO A 1 398  ? 27.829 38.128  -1.219  1.00 10.68 ? 398  PRO A C   1 
ATOM   3089 O  O   . PRO A 1 398  ? 28.684 38.787  -0.593  1.00 10.10 ? 398  PRO A O   1 
ATOM   3090 C  CB  . PRO A 1 398  ? 25.506 38.212  -0.324  1.00 9.42  ? 398  PRO A CB  1 
ATOM   3091 C  CG  . PRO A 1 398  ? 25.761 38.942  1.002   1.00 10.15 ? 398  PRO A CG  1 
ATOM   3092 C  CD  . PRO A 1 398  ? 26.400 37.906  1.886   1.00 11.72 ? 398  PRO A CD  1 
ATOM   3093 N  N   . THR A 1 399  ? 27.824 37.990  -2.530  1.00 8.63  ? 399  THR A N   1 
ATOM   3094 C  CA  . THR A 1 399  ? 28.748 38.716  -3.418  1.00 9.27  ? 399  THR A CA  1 
ATOM   3095 C  C   . THR A 1 399  ? 27.973 39.949  -3.928  1.00 8.74  ? 399  THR A C   1 
ATOM   3096 O  O   . THR A 1 399  ? 26.723 39.947  -4.061  1.00 9.16  ? 399  THR A O   1 
ATOM   3097 C  CB  . THR A 1 399  ? 29.177 37.866  -4.623  1.00 10.10 ? 399  THR A CB  1 
ATOM   3098 O  OG1 . THR A 1 399  ? 28.029 37.505  -5.389  1.00 11.07 ? 399  THR A OG1 1 
ATOM   3099 C  CG2 . THR A 1 399  ? 29.936 36.633  -4.158  1.00 11.40 ? 399  THR A CG2 1 
ATOM   3100 N  N   . LEU A 1 400  ? 28.739 41.007  -4.225  1.00 7.75  ? 400  LEU A N   1 
ATOM   3101 C  CA  . LEU A 1 400  ? 28.116 42.276  -4.624  1.00 8.25  ? 400  LEU A CA  1 
ATOM   3102 C  C   . LEU A 1 400  ? 29.023 43.052  -5.543  1.00 8.22  ? 400  LEU A C   1 
ATOM   3103 O  O   . LEU A 1 400  ? 30.264 42.992  -5.392  1.00 10.36 ? 400  LEU A O   1 
ATOM   3104 C  CB  . LEU A 1 400  ? 27.862 43.207  -3.385  1.00 7.37  ? 400  LEU A CB  1 
ATOM   3105 C  CG  . LEU A 1 400  ? 27.198 44.589  -3.610  1.00 7.20  ? 400  LEU A CG  1 
ATOM   3106 C  CD1 . LEU A 1 400  ? 26.356 44.962  -2.384  1.00 7.83  ? 400  LEU A CD1 1 
ATOM   3107 C  CD2 . LEU A 1 400  ? 28.288 45.665  -3.840  1.00 7.89  ? 400  LEU A CD2 1 
ATOM   3108 N  N   . SER A 1 401  ? 28.431 43.690  -6.552  1.00 7.75  ? 401  SER A N   1 
ATOM   3109 C  CA  . SER A 1 401  ? 29.240 44.624  -7.396  1.00 7.69  ? 401  SER A CA  1 
ATOM   3110 C  C   . SER A 1 401  ? 28.360 45.859  -7.582  1.00 9.39  ? 401  SER A C   1 
ATOM   3111 O  O   . SER A 1 401  ? 27.133 45.828  -7.381  1.00 6.85  ? 401  SER A O   1 
ATOM   3112 C  CB  . SER A 1 401  ? 29.600 44.096  -8.788  1.00 9.48  ? 401  SER A CB  1 
ATOM   3113 O  OG  . SER A 1 401  ? 28.444 44.042  -9.656  1.00 7.78  ? 401  SER A OG  1 
ATOM   3114 N  N   . GLY A 1 402  ? 29.034 46.948  -7.940  1.00 7.51  ? 402  GLY A N   1 
ATOM   3115 C  CA  . GLY A 1 402  ? 28.399 48.265  -8.142  1.00 6.98  ? 402  GLY A CA  1 
ATOM   3116 C  C   . GLY A 1 402  ? 28.984 49.330  -7.230  1.00 7.54  ? 402  GLY A C   1 
ATOM   3117 O  O   . GLY A 1 402  ? 30.054 49.133  -6.632  1.00 7.66  ? 402  GLY A O   1 
ATOM   3118 N  N   . ASP A 1 403  ? 28.307 50.475  -7.142  1.00 7.34  ? 403  ASP A N   1 
ATOM   3119 C  CA  . ASP A 1 403  ? 28.761 51.629  -6.310  1.00 7.63  ? 403  ASP A CA  1 
ATOM   3120 C  C   . ASP A 1 403  ? 27.656 52.104  -5.385  1.00 6.51  ? 403  ASP A C   1 
ATOM   3121 O  O   . ASP A 1 403  ? 26.549 51.524  -5.397  1.00 7.79  ? 403  ASP A O   1 
ATOM   3122 C  CB  . ASP A 1 403  ? 29.308 52.764  -7.219  1.00 5.90  ? 403  ASP A CB  1 
ATOM   3123 C  CG  . ASP A 1 403  ? 28.245 53.544  -7.923  1.00 9.84  ? 403  ASP A CG  1 
ATOM   3124 O  OD1 . ASP A 1 403  ? 27.110 53.075  -8.060  1.00 10.80 ? 403  ASP A OD1 1 
ATOM   3125 O  OD2 . ASP A 1 403  ? 28.595 54.656  -8.364  1.00 10.43 ? 403  ASP A OD2 1 
ATOM   3126 N  N   . PHE A 1 404  ? 27.951 53.099  -4.565  1.00 6.47  ? 404  PHE A N   1 
ATOM   3127 C  CA  . PHE A 1 404  ? 26.998 53.602  -3.643  1.00 5.20  ? 404  PHE A CA  1 
ATOM   3128 C  C   . PHE A 1 404  ? 26.876 55.101  -3.790  1.00 6.29  ? 404  PHE A C   1 
ATOM   3129 O  O   . PHE A 1 404  ? 26.990 55.829  -2.825  1.00 6.02  ? 404  PHE A O   1 
ATOM   3130 C  CB  . PHE A 1 404  ? 27.382 53.157  -2.220  1.00 5.51  ? 404  PHE A CB  1 
ATOM   3131 C  CG  . PHE A 1 404  ? 27.333 51.693  -2.059  1.00 5.42  ? 404  PHE A CG  1 
ATOM   3132 C  CD1 . PHE A 1 404  ? 26.062 51.056  -1.949  1.00 7.02  ? 404  PHE A CD1 1 
ATOM   3133 C  CD2 . PHE A 1 404  ? 28.497 50.958  -2.042  1.00 6.79  ? 404  PHE A CD2 1 
ATOM   3134 C  CE1 . PHE A 1 404  ? 25.975 49.660  -1.796  1.00 6.84  ? 404  PHE A CE1 1 
ATOM   3135 C  CE2 . PHE A 1 404  ? 28.456 49.583  -1.918  1.00 6.55  ? 404  PHE A CE2 1 
ATOM   3136 C  CZ  . PHE A 1 404  ? 27.172 48.948  -1.789  1.00 6.40  ? 404  PHE A CZ  1 
ATOM   3137 N  N   . PHE A 1 405  ? 26.624 55.503  -5.039  1.00 6.90  ? 405  PHE A N   1 
ATOM   3138 C  CA  . PHE A 1 405  ? 26.297 56.927  -5.384  1.00 7.03  ? 405  PHE A CA  1 
ATOM   3139 C  C   . PHE A 1 405  ? 24.931 56.861  -6.111  1.00 7.50  ? 405  PHE A C   1 
ATOM   3140 O  O   . PHE A 1 405  ? 24.639 55.888  -6.832  1.00 8.26  ? 405  PHE A O   1 
ATOM   3141 C  CB  . PHE A 1 405  ? 27.341 57.516  -6.364  1.00 6.46  ? 405  PHE A CB  1 
ATOM   3142 C  CG  . PHE A 1 405  ? 28.733 57.644  -5.763  1.00 6.39  ? 405  PHE A CG  1 
ATOM   3143 C  CD1 . PHE A 1 405  ? 28.972 58.443  -4.671  1.00 6.54  ? 405  PHE A CD1 1 
ATOM   3144 C  CD2 . PHE A 1 405  ? 29.747 56.949  -6.333  1.00 7.18  ? 405  PHE A CD2 1 
ATOM   3145 C  CE1 . PHE A 1 405  ? 30.302 58.545  -4.145  1.00 4.50  ? 405  PHE A CE1 1 
ATOM   3146 C  CE2 . PHE A 1 405  ? 31.054 57.031  -5.838  1.00 9.02  ? 405  PHE A CE2 1 
ATOM   3147 C  CZ  . PHE A 1 405  ? 31.319 57.831  -4.741  1.00 5.85  ? 405  PHE A CZ  1 
ATOM   3148 N  N   . THR A 1 406  ? 24.080 57.879  -5.964  1.00 7.80  ? 406  THR A N   1 
ATOM   3149 C  CA  . THR A 1 406  ? 24.318 59.075  -5.168  1.00 9.27  ? 406  THR A CA  1 
ATOM   3150 C  C   . THR A 1 406  ? 23.683 58.985  -3.806  1.00 8.92  ? 406  THR A C   1 
ATOM   3151 O  O   . THR A 1 406  ? 22.496 58.586  -3.672  1.00 9.84  ? 406  THR A O   1 
ATOM   3152 C  CB  . THR A 1 406  ? 23.779 60.297  -5.948  1.00 9.17  ? 406  THR A CB  1 
ATOM   3153 O  OG1 . THR A 1 406  ? 24.716 60.509  -7.030  1.00 8.58  ? 406  THR A OG1 1 
ATOM   3154 C  CG2 . THR A 1 406  ? 23.709 61.587  -5.133  1.00 8.71  ? 406  THR A CG2 1 
ATOM   3155 N  N   . TYR A 1 407  ? 24.448 59.317  -2.788  1.00 8.03  ? 407  TYR A N   1 
ATOM   3156 C  CA  . TYR A 1 407  ? 24.036 59.234  -1.418  1.00 7.13  ? 407  TYR A CA  1 
ATOM   3157 C  C   . TYR A 1 407  ? 22.894 60.193  -0.985  1.00 7.50  ? 407  TYR A C   1 
ATOM   3158 O  O   . TYR A 1 407  ? 22.890 61.323  -1.447  1.00 8.73  ? 407  TYR A O   1 
ATOM   3159 C  CB  . TYR A 1 407  ? 25.290 59.485  -0.547  1.00 7.82  ? 407  TYR A CB  1 
ATOM   3160 C  CG  . TYR A 1 407  ? 25.015 59.623  0.900   1.00 6.21  ? 407  TYR A CG  1 
ATOM   3161 C  CD1 . TYR A 1 407  ? 24.545 58.542  1.654   1.00 7.92  ? 407  TYR A CD1 1 
ATOM   3162 C  CD2 . TYR A 1 407  ? 25.320 60.822  1.570   1.00 8.71  ? 407  TYR A CD2 1 
ATOM   3163 C  CE1 . TYR A 1 407  ? 24.415 58.627  3.044   1.00 6.83  ? 407  TYR A CE1 1 
ATOM   3164 C  CE2 . TYR A 1 407  ? 25.193 60.954  2.974   1.00 5.52  ? 407  TYR A CE2 1 
ATOM   3165 C  CZ  . TYR A 1 407  ? 24.737 59.835  3.737   1.00 8.52  ? 407  TYR A CZ  1 
ATOM   3166 O  OH  . TYR A 1 407  ? 24.736 59.962  5.093   1.00 7.24  ? 407  TYR A OH  1 
ATOM   3167 N  N   . ALA A 1 408  ? 21.929 59.752  -0.146  1.00 8.87  ? 408  ALA A N   1 
ATOM   3168 C  CA  . ALA A 1 408  ? 20.968 60.668  0.415   1.00 8.33  ? 408  ALA A CA  1 
ATOM   3169 C  C   . ALA A 1 408  ? 20.911 60.125  1.858   1.00 7.80  ? 408  ALA A C   1 
ATOM   3170 O  O   . ALA A 1 408  ? 20.794 58.873  2.049   1.00 8.89  ? 408  ALA A O   1 
ATOM   3171 C  CB  . ALA A 1 408  ? 19.571 60.576  -0.233  1.00 9.40  ? 408  ALA A CB  1 
ATOM   3172 N  N   . ASP A 1 409  ? 20.964 61.026  2.847   1.00 10.01 ? 409  ASP A N   1 
ATOM   3173 C  CA  . ASP A 1 409  ? 20.924 60.680  4.289   1.00 9.88  ? 409  ASP A CA  1 
ATOM   3174 C  C   . ASP A 1 409  ? 19.513 60.742  4.827   1.00 11.88 ? 409  ASP A C   1 
ATOM   3175 O  O   . ASP A 1 409  ? 19.214 60.080  5.833   1.00 10.92 ? 409  ASP A O   1 
ATOM   3176 C  CB  . ASP A 1 409  ? 21.875 61.563  5.119   1.00 9.51  ? 409  ASP A CB  1 
ATOM   3177 C  CG  . ASP A 1 409  ? 21.568 63.096  5.040   1.00 8.29  ? 409  ASP A CG  1 
ATOM   3178 O  OD1 . ASP A 1 409  ? 20.956 63.548  4.050   1.00 10.02 ? 409  ASP A OD1 1 
ATOM   3179 O  OD2 . ASP A 1 409  ? 22.031 63.799  5.998   1.00 11.87 ? 409  ASP A OD2 1 
ATOM   3180 N  N   . ARG A 1 410  ? 18.646 61.473  4.108   1.00 9.74  ? 410  ARG A N   1 
ATOM   3181 C  CA  . ARG A 1 410  ? 17.199 61.528  4.503   1.00 12.89 ? 410  ARG A CA  1 
ATOM   3182 C  C   . ARG A 1 410  ? 16.381 62.162  3.386   1.00 12.16 ? 410  ARG A C   1 
ATOM   3183 O  O   . ARG A 1 410  ? 16.923 62.919  2.536   1.00 13.40 ? 410  ARG A O   1 
ATOM   3184 C  CB  . ARG A 1 410  ? 16.975 62.298  5.803   1.00 13.23 ? 410  ARG A CB  1 
ATOM   3185 C  CG  . ARG A 1 410  ? 17.517 63.722  5.792   1.00 15.52 ? 410  ARG A CG  1 
ATOM   3186 C  CD  . ARG A 1 410  ? 17.500 64.269  7.223   1.00 16.78 ? 410  ARG A CD  1 
ATOM   3187 N  NE  . ARG A 1 410  ? 18.023 65.641  7.353   1.00 18.72 ? 410  ARG A NE  1 
ATOM   3188 C  CZ  . ARG A 1 410  ? 17.357 66.748  7.031   1.00 20.49 ? 410  ARG A CZ  1 
ATOM   3189 N  NH1 . ARG A 1 410  ? 16.115 66.676  6.533   1.00 21.45 ? 410  ARG A NH1 1 
ATOM   3190 N  NH2 . ARG A 1 410  ? 17.939 67.937  7.234   1.00 20.18 ? 410  ARG A NH2 1 
ATOM   3191 N  N   . SER A 1 411  ? 15.081 61.860  3.389   1.00 13.35 ? 411  SER A N   1 
ATOM   3192 C  CA  . SER A 1 411  ? 14.112 62.378  2.402   1.00 14.43 ? 411  SER A CA  1 
ATOM   3193 C  C   . SER A 1 411  ? 14.663 62.527  0.981   1.00 13.45 ? 411  SER A C   1 
ATOM   3194 O  O   . SER A 1 411  ? 15.138 61.540  0.434   1.00 13.60 ? 411  SER A O   1 
ATOM   3195 C  CB  . SER A 1 411  ? 13.486 63.708  2.898   1.00 16.39 ? 411  SER A CB  1 
ATOM   3196 O  OG  A SER A 1 411  ? 14.330 64.818  2.687   0.50 17.21 ? 411  SER A OG  1 
ATOM   3197 O  OG  B SER A 1 411  ? 14.252 64.310  3.951   0.50 14.37 ? 411  SER A OG  1 
ATOM   3198 N  N   . ASP A 1 412  ? 14.597 63.734  0.391   1.00 11.91 ? 412  ASP A N   1 
ATOM   3199 C  CA  . ASP A 1 412  ? 15.092 63.957  -0.972  1.00 13.04 ? 412  ASP A CA  1 
ATOM   3200 C  C   . ASP A 1 412  ? 16.437 64.700  -0.955  1.00 10.20 ? 412  ASP A C   1 
ATOM   3201 O  O   . ASP A 1 412  ? 16.835 65.268  -1.984  1.00 11.42 ? 412  ASP A O   1 
ATOM   3202 C  CB  . ASP A 1 412  ? 14.091 64.789  -1.803  1.00 14.75 ? 412  ASP A CB  1 
ATOM   3203 C  CG  . ASP A 1 412  ? 13.884 66.203  -1.257  1.00 15.15 ? 412  ASP A CG  1 
ATOM   3204 O  OD1 . ASP A 1 412  ? 14.340 66.546  -0.170  1.00 13.69 ? 412  ASP A OD1 1 
ATOM   3205 O  OD2 . ASP A 1 412  ? 13.216 66.994  -1.974  1.00 17.42 ? 412  ASP A OD2 1 
ATOM   3206 N  N   . ASN A 1 413  ? 17.114 64.669  0.191   1.00 10.16 ? 413  ASN A N   1 
ATOM   3207 C  CA  . ASN A 1 413  ? 18.403 65.381  0.337   1.00 10.22 ? 413  ASN A CA  1 
ATOM   3208 C  C   . ASN A 1 413  ? 19.544 64.496  -0.247  1.00 9.60  ? 413  ASN A C   1 
ATOM   3209 O  O   . ASN A 1 413  ? 20.176 63.745  0.480   1.00 10.30 ? 413  ASN A O   1 
ATOM   3210 C  CB  . ASN A 1 413  ? 18.682 65.732  1.821   1.00 9.29  ? 413  ASN A CB  1 
ATOM   3211 C  CG  . ASN A 1 413  ? 17.694 66.770  2.441   1.00 10.68 ? 413  ASN A CG  1 
ATOM   3212 O  OD1 . ASN A 1 413  ? 17.971 67.264  3.511   1.00 10.63 ? 413  ASN A OD1 1 
ATOM   3213 N  ND2 . ASN A 1 413  ? 16.589 67.087  1.762   1.00 10.76 ? 413  ASN A ND2 1 
ATOM   3214 N  N   . TYR A 1 414  ? 19.742 64.581  -1.559  1.00 10.36 ? 414  TYR A N   1 
ATOM   3215 C  CA  . TYR A 1 414  ? 20.791 63.848  -2.328  1.00 9.12  ? 414  TYR A CA  1 
ATOM   3216 C  C   . TYR A 1 414  ? 22.039 64.748  -2.367  1.00 9.29  ? 414  TYR A C   1 
ATOM   3217 O  O   . TYR A 1 414  ? 21.960 65.955  -2.643  1.00 10.15 ? 414  TYR A O   1 
ATOM   3218 C  CB  . TYR A 1 414  ? 20.344 63.532  -3.762  1.00 8.99  ? 414  TYR A CB  1 
ATOM   3219 C  CG  . TYR A 1 414  ? 19.348 62.384  -3.783  1.00 11.30 ? 414  TYR A CG  1 
ATOM   3220 C  CD1 . TYR A 1 414  ? 17.983 62.619  -3.568  1.00 13.28 ? 414  TYR A CD1 1 
ATOM   3221 C  CD2 . TYR A 1 414  ? 19.778 61.087  -3.941  1.00 11.06 ? 414  TYR A CD2 1 
ATOM   3222 C  CE1 . TYR A 1 414  ? 17.103 61.579  -3.526  1.00 11.73 ? 414  TYR A CE1 1 
ATOM   3223 C  CE2 . TYR A 1 414  ? 18.895 60.045  -3.872  1.00 10.52 ? 414  TYR A CE2 1 
ATOM   3224 C  CZ  . TYR A 1 414  ? 17.562 60.301  -3.671  1.00 11.05 ? 414  TYR A CZ  1 
ATOM   3225 O  OH  . TYR A 1 414  ? 16.714 59.224  -3.637  1.00 11.43 ? 414  TYR A OH  1 
ATOM   3226 N  N   . TRP A 1 415  ? 23.176 64.129  -2.035  1.00 6.71  ? 415  TRP A N   1 
ATOM   3227 C  CA  . TRP A 1 415  ? 24.452 64.840  -1.918  1.00 8.43  ? 415  TRP A CA  1 
ATOM   3228 C  C   . TRP A 1 415  ? 25.222 64.915  -3.238  1.00 9.82  ? 415  TRP A C   1 
ATOM   3229 O  O   . TRP A 1 415  ? 26.351 64.452  -3.356  1.00 9.33  ? 415  TRP A O   1 
ATOM   3230 C  CB  . TRP A 1 415  ? 25.261 64.123  -0.835  1.00 7.35  ? 415  TRP A CB  1 
ATOM   3231 C  CG  . TRP A 1 415  ? 24.659 64.217  0.561   1.00 6.93  ? 415  TRP A CG  1 
ATOM   3232 C  CD1 . TRP A 1 415  ? 23.339 63.979  0.935   1.00 7.30  ? 415  TRP A CD1 1 
ATOM   3233 C  CD2 . TRP A 1 415  ? 25.376 64.439  1.782   1.00 7.01  ? 415  TRP A CD2 1 
ATOM   3234 N  NE1 . TRP A 1 415  ? 23.241 64.043  2.309   1.00 6.94  ? 415  TRP A NE1 1 
ATOM   3235 C  CE2 . TRP A 1 415  ? 24.459 64.327  2.856   1.00 10.06 ? 415  TRP A CE2 1 
ATOM   3236 C  CE3 . TRP A 1 415  ? 26.744 64.715  2.067   1.00 8.82  ? 415  TRP A CE3 1 
ATOM   3237 C  CZ2 . TRP A 1 415  ? 24.831 64.480  4.199   1.00 8.63  ? 415  TRP A CZ2 1 
ATOM   3238 C  CZ3 . TRP A 1 415  ? 27.131 64.856  3.374   1.00 6.96  ? 415  TRP A CZ3 1 
ATOM   3239 C  CH2 . TRP A 1 415  ? 26.175 64.744  4.475   1.00 8.73  ? 415  TRP A CH2 1 
ATOM   3240 N  N   . SER A 1 416  ? 24.591 65.459  -4.247  1.00 7.52  ? 416  SER A N   1 
ATOM   3241 C  CA  . SER A 1 416  ? 25.242 65.626  -5.538  1.00 6.47  ? 416  SER A CA  1 
ATOM   3242 C  C   . SER A 1 416  ? 25.838 67.034  -5.706  1.00 7.15  ? 416  SER A C   1 
ATOM   3243 O  O   . SER A 1 416  ? 26.510 67.261  -6.707  1.00 7.28  ? 416  SER A O   1 
ATOM   3244 C  CB  . SER A 1 416  ? 24.264 65.310  -6.699  1.00 7.00  ? 416  SER A CB  1 
ATOM   3245 O  OG  . SER A 1 416  ? 22.907 65.785  -6.500  1.00 8.08  ? 416  SER A OG  1 
ATOM   3246 N  N   . GLY A 1 417  ? 25.604 67.928  -4.746  1.00 7.27  ? 417  GLY A N   1 
ATOM   3247 C  CA  . GLY A 1 417  ? 26.167 69.252  -4.922  1.00 7.72  ? 417  GLY A CA  1 
ATOM   3248 C  C   . GLY A 1 417  ? 27.690 69.249  -4.852  1.00 8.48  ? 417  GLY A C   1 
ATOM   3249 O  O   . GLY A 1 417  ? 28.345 69.987  -5.585  1.00 7.87  ? 417  GLY A O   1 
ATOM   3250 N  N   . TYR A 1 418  ? 28.255 68.428  -3.979  1.00 7.84  ? 418  TYR A N   1 
ATOM   3251 C  CA  . TYR A 1 418  ? 29.709 68.457  -3.807  1.00 6.73  ? 418  TYR A CA  1 
ATOM   3252 C  C   . TYR A 1 418  ? 30.426 67.818  -4.975  1.00 6.58  ? 418  TYR A C   1 
ATOM   3253 O  O   . TYR A 1 418  ? 31.666 67.848  -5.051  1.00 8.01  ? 418  TYR A O   1 
ATOM   3254 C  CB  . TYR A 1 418  ? 30.085 67.802  -2.481  1.00 8.17  ? 418  TYR A CB  1 
ATOM   3255 C  CG  . TYR A 1 418  ? 30.199 66.296  -2.504  1.00 7.58  ? 418  TYR A CG  1 
ATOM   3256 C  CD1 . TYR A 1 418  ? 29.077 65.477  -2.299  1.00 8.03  ? 418  TYR A CD1 1 
ATOM   3257 C  CD2 . TYR A 1 418  ? 31.443 65.706  -2.720  1.00 6.59  ? 418  TYR A CD2 1 
ATOM   3258 C  CE1 . TYR A 1 418  ? 29.200 64.066  -2.316  1.00 7.52  ? 418  TYR A CE1 1 
ATOM   3259 C  CE2 . TYR A 1 418  ? 31.581 64.328  -2.747  1.00 6.76  ? 418  TYR A CE2 1 
ATOM   3260 C  CZ  . TYR A 1 418  ? 30.467 63.522  -2.541  1.00 5.68  ? 418  TYR A CZ  1 
ATOM   3261 O  OH  . TYR A 1 418  ? 30.631 62.144  -2.574  1.00 6.23  ? 418  TYR A OH  1 
ATOM   3262 N  N   . TYR A 1 419  ? 29.711 67.288  -5.957  1.00 4.96  ? 419  TYR A N   1 
ATOM   3263 C  CA  . TYR A 1 419  ? 30.409 66.825  -7.151  1.00 6.44  ? 419  TYR A CA  1 
ATOM   3264 C  C   . TYR A 1 419  ? 30.920 68.085  -7.912  1.00 6.96  ? 419  TYR A C   1 
ATOM   3265 O  O   . TYR A 1 419  ? 31.733 67.940  -8.811  1.00 7.07  ? 419  TYR A O   1 
ATOM   3266 C  CB  . TYR A 1 419  ? 29.461 66.054  -8.110  1.00 6.58  ? 419  TYR A CB  1 
ATOM   3267 C  CG  . TYR A 1 419  ? 28.758 64.876  -7.463  1.00 8.38  ? 419  TYR A CG  1 
ATOM   3268 C  CD1 . TYR A 1 419  ? 29.333 64.210  -6.351  1.00 6.80  ? 419  TYR A CD1 1 
ATOM   3269 C  CD2 . TYR A 1 419  ? 27.603 64.370  -7.989  1.00 6.77  ? 419  TYR A CD2 1 
ATOM   3270 C  CE1 . TYR A 1 419  ? 28.770 63.028  -5.763  1.00 7.87  ? 419  TYR A CE1 1 
ATOM   3271 C  CE2 . TYR A 1 419  ? 27.029 63.198  -7.446  1.00 8.37  ? 419  TYR A CE2 1 
ATOM   3272 C  CZ  . TYR A 1 419  ? 27.627 62.552  -6.340  1.00 8.22  ? 419  TYR A CZ  1 
ATOM   3273 O  OH  . TYR A 1 419  ? 27.040 61.411  -5.824  1.00 8.06  ? 419  TYR A OH  1 
ATOM   3274 N  N   . THR A 1 420  ? 30.392 69.277  -7.586  1.00 6.87  ? 420  THR A N   1 
ATOM   3275 C  CA  . THR A 1 420  ? 30.812 70.496  -8.278  1.00 8.60  ? 420  THR A CA  1 
ATOM   3276 C  C   . THR A 1 420  ? 31.352 71.594  -7.406  1.00 8.92  ? 420  THR A C   1 
ATOM   3277 O  O   . THR A 1 420  ? 32.143 72.413  -7.863  1.00 8.47  ? 420  THR A O   1 
ATOM   3278 C  CB  . THR A 1 420  ? 29.580 71.020  -9.103  1.00 7.46  ? 420  THR A CB  1 
ATOM   3279 O  OG1 . THR A 1 420  ? 29.082 69.990  -9.958  1.00 8.83  ? 420  THR A OG1 1 
ATOM   3280 C  CG2 . THR A 1 420  ? 29.946 72.350  -9.850  1.00 9.10  ? 420  THR A CG2 1 
ATOM   3281 N  N   . SER A 1 421  ? 30.967 71.635  -6.139  1.00 7.68  ? 421  SER A N   1 
ATOM   3282 C  CA  . SER A 1 421  ? 31.393 72.740  -5.254  1.00 9.42  ? 421  SER A CA  1 
ATOM   3283 C  C   . SER A 1 421  ? 32.876 73.076  -5.314  1.00 10.18 ? 421  SER A C   1 
ATOM   3284 O  O   . SER A 1 421  ? 33.738 72.150  -5.319  1.00 9.08  ? 421  SER A O   1 
ATOM   3285 C  CB  . SER A 1 421  ? 31.005 72.448  -3.814  1.00 8.33  ? 421  SER A CB  1 
ATOM   3286 O  OG  . SER A 1 421  ? 29.588 72.228  -3.705  1.00 8.68  ? 421  SER A OG  1 
ATOM   3287 N  N   . ARG A 1 422  ? 33.173 74.390  -5.288  1.00 8.43  ? 422  ARG A N   1 
ATOM   3288 C  CA  . ARG A 1 422  ? 34.580 74.913  -5.363  1.00 8.30  ? 422  ARG A CA  1 
ATOM   3289 C  C   . ARG A 1 422  ? 35.302 74.267  -6.560  1.00 7.96  ? 422  ARG A C   1 
ATOM   3290 O  O   . ARG A 1 422  ? 36.350 73.602  -6.368  1.00 7.13  ? 422  ARG A O   1 
ATOM   3291 C  CB  . ARG A 1 422  ? 35.345 74.665  -4.032  1.00 11.13 ? 422  ARG A CB  1 
ATOM   3292 C  CG  . ARG A 1 422  ? 35.065 75.647  -2.906  1.00 9.70  ? 422  ARG A CG  1 
ATOM   3293 C  CD  . ARG A 1 422  ? 33.578 75.722  -2.546  1.00 10.10 ? 422  ARG A CD  1 
ATOM   3294 N  NE  . ARG A 1 422  ? 33.515 76.730  -1.513  1.00 8.09  ? 422  ARG A NE  1 
ATOM   3295 C  CZ  . ARG A 1 422  ? 33.539 76.487  -0.179  1.00 9.66  ? 422  ARG A CZ  1 
ATOM   3296 N  NH1 . ARG A 1 422  ? 33.545 75.245  0.266   1.00 10.07 ? 422  ARG A NH1 1 
ATOM   3297 N  NH2 . ARG A 1 422  ? 33.813 77.418  0.725   1.00 11.48 ? 422  ARG A NH2 1 
ATOM   3298 N  N   . PRO A 1 423  ? 34.795 74.436  -7.783  1.00 8.09  ? 423  PRO A N   1 
ATOM   3299 C  CA  . PRO A 1 423  ? 35.390 73.836  -8.972  1.00 7.75  ? 423  PRO A CA  1 
ATOM   3300 C  C   . PRO A 1 423  ? 36.822 74.282  -9.325  1.00 9.23  ? 423  PRO A C   1 
ATOM   3301 O  O   . PRO A 1 423  ? 37.526 73.554  -10.018 1.00 7.22  ? 423  PRO A O   1 
ATOM   3302 C  CB  . PRO A 1 423  ? 34.344 74.137  -10.074 1.00 7.45  ? 423  PRO A CB  1 
ATOM   3303 C  CG  . PRO A 1 423  ? 33.806 75.533  -9.677  1.00 7.42  ? 423  PRO A CG  1 
ATOM   3304 C  CD  . PRO A 1 423  ? 33.676 75.369  -8.135  1.00 6.77  ? 423  PRO A CD  1 
ATOM   3305 N  N   . TYR A 1 424  ? 37.210 75.468  -8.898  1.00 9.65  ? 424  TYR A N   1 
ATOM   3306 C  CA  . TYR A 1 424  ? 38.571 75.921  -9.166  1.00 8.31  ? 424  TYR A CA  1 
ATOM   3307 C  C   . TYR A 1 424  ? 39.568 74.949  -8.548  1.00 10.42 ? 424  TYR A C   1 
ATOM   3308 O  O   . TYR A 1 424  ? 40.543 74.558  -9.177  1.00 9.16  ? 424  TYR A O   1 
ATOM   3309 C  CB  . TYR A 1 424  ? 38.777 77.266  -8.493  1.00 9.32  ? 424  TYR A CB  1 
ATOM   3310 C  CG  . TYR A 1 424  ? 40.161 77.831  -8.758  1.00 10.19 ? 424  TYR A CG  1 
ATOM   3311 C  CD1 . TYR A 1 424  ? 40.413 78.636  -9.891  1.00 12.60 ? 424  TYR A CD1 1 
ATOM   3312 C  CD2 . TYR A 1 424  ? 41.227 77.537  -7.902  1.00 10.70 ? 424  TYR A CD2 1 
ATOM   3313 C  CE1 . TYR A 1 424  ? 41.707 79.134  -10.148 1.00 13.52 ? 424  TYR A CE1 1 
ATOM   3314 C  CE2 . TYR A 1 424  ? 42.557 78.056  -8.144  1.00 13.87 ? 424  TYR A CE2 1 
ATOM   3315 C  CZ  . TYR A 1 424  ? 42.750 78.853  -9.283  1.00 13.40 ? 424  TYR A CZ  1 
ATOM   3316 O  OH  . TYR A 1 424  ? 43.992 79.444  -9.566  1.00 15.14 ? 424  TYR A OH  1 
ATOM   3317 N  N   . HIS A 1 425  ? 39.298 74.577  -7.308  1.00 7.86  ? 425  HIS A N   1 
ATOM   3318 C  CA  . HIS A 1 425  ? 40.214 73.635  -6.639  1.00 8.63  ? 425  HIS A CA  1 
ATOM   3319 C  C   . HIS A 1 425  ? 40.102 72.191  -7.158  1.00 8.44  ? 425  HIS A C   1 
ATOM   3320 O  O   . HIS A 1 425  ? 41.075 71.412  -7.117  1.00 8.01  ? 425  HIS A O   1 
ATOM   3321 C  CB  . HIS A 1 425  ? 39.951 73.704  -5.157  1.00 8.79  ? 425  HIS A CB  1 
ATOM   3322 C  CG  . HIS A 1 425  ? 40.052 75.100  -4.642  1.00 9.14  ? 425  HIS A CG  1 
ATOM   3323 N  ND1 . HIS A 1 425  ? 38.977 75.972  -4.692  1.00 12.41 ? 425  HIS A ND1 1 
ATOM   3324 C  CD2 . HIS A 1 425  ? 41.140 75.860  -4.364  1.00 11.23 ? 425  HIS A CD2 1 
ATOM   3325 C  CE1 . HIS A 1 425  ? 39.399 77.203  -4.490  1.00 12.95 ? 425  HIS A CE1 1 
ATOM   3326 N  NE2 . HIS A 1 425  ? 40.712 77.160  -4.294  1.00 11.59 ? 425  HIS A NE2 1 
ATOM   3327 N  N   . LYS A 1 426  ? 38.897 71.790  -7.603  1.00 6.71  ? 426  LYS A N   1 
ATOM   3328 C  CA  . LYS A 1 426  ? 38.744 70.493  -8.207  1.00 7.79  ? 426  LYS A CA  1 
ATOM   3329 C  C   . LYS A 1 426  ? 39.644 70.452  -9.492  1.00 8.25  ? 426  LYS A C   1 
ATOM   3330 O  O   . LYS A 1 426  ? 40.234 69.406  -9.814  1.00 8.52  ? 426  LYS A O   1 
ATOM   3331 C  CB  . LYS A 1 426  ? 37.255 70.329  -8.579  1.00 6.36  ? 426  LYS A CB  1 
ATOM   3332 C  CG  . LYS A 1 426  ? 36.426 69.882  -7.445  1.00 8.64  ? 426  LYS A CG  1 
ATOM   3333 C  CD  . LYS A 1 426  ? 34.974 69.979  -7.882  1.00 6.14  ? 426  LYS A CD  1 
ATOM   3334 C  CE  . LYS A 1 426  ? 34.037 69.080  -6.991  1.00 9.53  ? 426  LYS A CE  1 
ATOM   3335 N  NZ  . LYS A 1 426  ? 33.967 69.489  -5.520  1.00 8.24  ? 426  LYS A NZ  1 
ATOM   3336 N  N   . ARG A 1 427  ? 39.701 71.559  -10.259 1.00 7.90  ? 427  ARG A N   1 
ATOM   3337 C  CA  . ARG A 1 427  ? 40.571 71.510  -11.438 1.00 8.08  ? 427  ARG A CA  1 
ATOM   3338 C  C   . ARG A 1 427  ? 42.083 71.519  -10.992 1.00 8.97  ? 427  ARG A C   1 
ATOM   3339 O  O   . ARG A 1 427  ? 42.948 70.834  -11.561 1.00 8.33  ? 427  ARG A O   1 
ATOM   3340 C  CB  . ARG A 1 427  ? 40.220 72.758  -12.298 1.00 8.81  ? 427  ARG A CB  1 
ATOM   3341 C  CG  . ARG A 1 427  ? 41.216 73.070  -13.388 1.00 10.19 ? 427  ARG A CG  1 
ATOM   3342 C  CD  . ARG A 1 427  ? 41.326 72.025  -14.454 1.00 13.42 ? 427  ARG A CD  1 
ATOM   3343 N  NE  . ARG A 1 427  ? 42.356 72.382  -15.452 1.00 12.13 ? 427  ARG A NE  1 
ATOM   3344 C  CZ  . ARG A 1 427  ? 43.147 71.515  -16.056 1.00 12.20 ? 427  ARG A CZ  1 
ATOM   3345 N  NH1 . ARG A 1 427  ? 43.069 70.204  -15.843 1.00 11.41 ? 427  ARG A NH1 1 
ATOM   3346 N  NH2 . ARG A 1 427  ? 44.142 71.956  -16.841 1.00 14.05 ? 427  ARG A NH2 1 
ATOM   3347 N  N   . MET A 1 428  ? 42.341 72.308  -9.960  1.00 8.72  ? 428  MET A N   1 
ATOM   3348 C  CA  . MET A 1 428  ? 43.715 72.376  -9.464  1.00 8.85  ? 428  MET A CA  1 
ATOM   3349 C  C   . MET A 1 428  ? 44.220 71.006  -9.046  1.00 8.84  ? 428  MET A C   1 
ATOM   3350 O  O   . MET A 1 428  ? 45.379 70.706  -9.225  1.00 6.60  ? 428  MET A O   1 
ATOM   3351 C  CB  . MET A 1 428  ? 43.761 73.325  -8.313  1.00 8.69  ? 428  MET A CB  1 
ATOM   3352 C  CG  . MET A 1 428  ? 45.213 73.731  -7.974  1.00 9.32  ? 428  MET A CG  1 
ATOM   3353 S  SD  . MET A 1 428  ? 45.130 75.086  -6.640  1.00 11.88 ? 428  MET A SD  1 
ATOM   3354 C  CE  . MET A 1 428  ? 46.876 75.646  -6.555  1.00 8.44  ? 428  MET A CE  1 
ATOM   3355 N  N   . ASP A 1 429  ? 43.333 70.200  -8.446  1.00 7.87  ? 429  ASP A N   1 
ATOM   3356 C  CA  . ASP A 1 429  ? 43.657 68.860  -8.032  1.00 6.62  ? 429  ASP A CA  1 
ATOM   3357 C  C   . ASP A 1 429  ? 44.240 68.073  -9.197  1.00 7.30  ? 429  ASP A C   1 
ATOM   3358 O  O   . ASP A 1 429  ? 45.253 67.370  -9.052  1.00 7.12  ? 429  ASP A O   1 
ATOM   3359 C  CB  . ASP A 1 429  ? 42.386 68.124  -7.480  1.00 7.88  ? 429  ASP A CB  1 
ATOM   3360 C  CG  . ASP A 1 429  ? 42.657 66.647  -7.164  1.00 8.93  ? 429  ASP A CG  1 
ATOM   3361 O  OD1 . ASP A 1 429  ? 43.189 66.429  -6.092  1.00 6.73  ? 429  ASP A OD1 1 
ATOM   3362 O  OD2 . ASP A 1 429  ? 42.389 65.791  -8.014  1.00 6.23  ? 429  ASP A OD2 1 
ATOM   3363 N  N   . ARG A 1 430  ? 43.649 68.169  -10.368 1.00 7.67  ? 430  ARG A N   1 
ATOM   3364 C  CA  . ARG A 1 430  ? 44.120 67.386  -11.495 1.00 7.51  ? 430  ARG A CA  1 
ATOM   3365 C  C   . ARG A 1 430  ? 45.423 67.960  -12.073 1.00 7.57  ? 430  ARG A C   1 
ATOM   3366 O  O   . ARG A 1 430  ? 46.248 67.183  -12.605 1.00 8.35  ? 430  ARG A O   1 
ATOM   3367 C  CB  . ARG A 1 430  ? 43.052 67.380  -12.611 1.00 7.46  ? 430  ARG A CB  1 
ATOM   3368 C  CG  . ARG A 1 430  ? 41.703 66.754  -12.163 1.00 7.90  ? 430  ARG A CG  1 
ATOM   3369 C  CD  . ARG A 1 430  ? 41.938 65.298  -11.812 1.00 8.22  ? 430  ARG A CD  1 
ATOM   3370 N  NE  . ARG A 1 430  ? 40.698 64.487  -11.873 1.00 7.20  ? 430  ARG A NE  1 
ATOM   3371 C  CZ  . ARG A 1 430  ? 40.020 64.123  -10.802 1.00 6.43  ? 430  ARG A CZ  1 
ATOM   3372 N  NH1 . ARG A 1 430  ? 40.440 64.447  -9.548  1.00 6.21  ? 430  ARG A NH1 1 
ATOM   3373 N  NH2 . ARG A 1 430  ? 38.856 63.442  -10.982 1.00 7.50  ? 430  ARG A NH2 1 
ATOM   3374 N  N   . VAL A 1 431  ? 45.587 69.282  -11.987 1.00 8.09  ? 431  VAL A N   1 
ATOM   3375 C  CA  . VAL A 1 431  ? 46.844 69.880  -12.487 1.00 7.42  ? 431  VAL A CA  1 
ATOM   3376 C  C   . VAL A 1 431  ? 47.989 69.364  -11.540 1.00 9.81  ? 431  VAL A C   1 
ATOM   3377 O  O   . VAL A 1 431  ? 48.996 68.845  -11.976 1.00 6.95  ? 431  VAL A O   1 
ATOM   3378 C  CB  . VAL A 1 431  ? 46.735 71.406  -12.423 1.00 7.76  ? 431  VAL A CB  1 
ATOM   3379 C  CG1 . VAL A 1 431  ? 48.112 72.030  -12.721 1.00 8.90  ? 431  VAL A CG1 1 
ATOM   3380 C  CG2 . VAL A 1 431  ? 45.692 71.891  -13.419 1.00 9.38  ? 431  VAL A CG2 1 
ATOM   3381 N  N   . LEU A 1 432  ? 47.777 69.414  -10.236 1.00 7.15  ? 432  LEU A N   1 
ATOM   3382 C  CA  . LEU A 1 432  ? 48.838 69.015  -9.325  1.00 9.56  ? 432  LEU A CA  1 
ATOM   3383 C  C   . LEU A 1 432  ? 49.029 67.499  -9.482  1.00 7.19  ? 432  LEU A C   1 
ATOM   3384 O  O   . LEU A 1 432  ? 50.152 66.998  -9.377  1.00 6.84  ? 432  LEU A O   1 
ATOM   3385 C  CB  . LEU A 1 432  ? 48.495 69.470  -7.909  1.00 8.64  ? 432  LEU A CB  1 
ATOM   3386 C  CG  . LEU A 1 432  ? 49.491 69.043  -6.845  1.00 8.83  ? 432  LEU A CG  1 
ATOM   3387 C  CD1 . LEU A 1 432  ? 50.861 69.652  -7.083  1.00 9.10  ? 432  LEU A CD1 1 
ATOM   3388 C  CD2 . LEU A 1 432  ? 49.016 69.546  -5.521  1.00 8.65  ? 432  LEU A CD2 1 
ATOM   3389 N  N   . MET A 1 433  ? 47.961 66.736  -9.673  1.00 6.42  ? 433  MET A N   1 
ATOM   3390 C  CA  . MET A 1 433  ? 48.091 65.289  -9.839  1.00 7.03  ? 433  MET A CA  1 
ATOM   3391 C  C   . MET A 1 433  ? 49.173 64.987  -10.899 1.00 7.01  ? 433  MET A C   1 
ATOM   3392 O  O   . MET A 1 433  ? 50.054 64.150  -10.725 1.00 7.13  ? 433  MET A O   1 
ATOM   3393 C  CB  . MET A 1 433  ? 46.784 64.694  -10.389 1.00 6.74  ? 433  MET A CB  1 
ATOM   3394 C  CG  . MET A 1 433  ? 46.917 63.158  -10.632 1.00 6.43  ? 433  MET A CG  1 
ATOM   3395 S  SD  . MET A 1 433  ? 45.343 62.503  -11.366 1.00 8.30  ? 433  MET A SD  1 
ATOM   3396 C  CE  . MET A 1 433  ? 45.533 63.266  -12.983 1.00 12.64 ? 433  MET A CE  1 
ATOM   3397 N  N   . HIS A 1 434  ? 49.064 65.663  -12.025 1.00 8.68  ? 434  HIS A N   1 
ATOM   3398 C  CA  . HIS A 1 434  ? 49.997 65.465  -13.119 1.00 7.97  ? 434  HIS A CA  1 
ATOM   3399 C  C   . HIS A 1 434  ? 51.394 65.976  -12.817 1.00 11.02 ? 434  HIS A C   1 
ATOM   3400 O  O   . HIS A 1 434  ? 52.402 65.284  -13.155 1.00 6.93  ? 434  HIS A O   1 
ATOM   3401 C  CB  . HIS A 1 434  ? 49.473 66.172  -14.355 1.00 9.45  ? 434  HIS A CB  1 
ATOM   3402 C  CG  . HIS A 1 434  ? 50.478 66.209  -15.441 1.00 7.08  ? 434  HIS A CG  1 
ATOM   3403 N  ND1 . HIS A 1 434  ? 50.844 65.095  -16.157 1.00 9.32  ? 434  HIS A ND1 1 
ATOM   3404 C  CD2 . HIS A 1 434  ? 51.296 67.209  -15.835 1.00 8.49  ? 434  HIS A CD2 1 
ATOM   3405 C  CE1 . HIS A 1 434  ? 51.844 65.403  -16.969 1.00 9.31  ? 434  HIS A CE1 1 
ATOM   3406 N  NE2 . HIS A 1 434  ? 52.130 66.678  -16.804 1.00 10.17 ? 434  HIS A NE2 1 
ATOM   3407 N  N   . TYR A 1 435  ? 51.470 67.154  -12.205 1.00 8.29  ? 435  TYR A N   1 
ATOM   3408 C  CA  . TYR A 1 435  ? 52.795 67.739  -11.817 1.00 10.00 ? 435  TYR A CA  1 
ATOM   3409 C  C   . TYR A 1 435  ? 53.514 66.787  -10.843 1.00 10.21 ? 435  TYR A C   1 
ATOM   3410 O  O   . TYR A 1 435  ? 54.755 66.587  -10.964 1.00 10.72 ? 435  TYR A O   1 
ATOM   3411 C  CB  . TYR A 1 435  ? 52.624 69.111  -11.151 1.00 11.19 ? 435  TYR A CB  1 
ATOM   3412 C  CG  . TYR A 1 435  ? 52.554 70.271  -12.131 1.00 14.62 ? 435  TYR A CG  1 
ATOM   3413 C  CD1 . TYR A 1 435  ? 51.591 70.303  -13.153 1.00 15.52 ? 435  TYR A CD1 1 
ATOM   3414 C  CD2 . TYR A 1 435  ? 53.387 71.366  -11.980 1.00 18.38 ? 435  TYR A CD2 1 
ATOM   3415 C  CE1 . TYR A 1 435  ? 51.466 71.386  -13.996 1.00 16.65 ? 435  TYR A CE1 1 
ATOM   3416 C  CE2 . TYR A 1 435  ? 53.271 72.475  -12.813 1.00 19.96 ? 435  TYR A CE2 1 
ATOM   3417 C  CZ  . TYR A 1 435  ? 52.306 72.469  -13.823 1.00 21.38 ? 435  TYR A CZ  1 
ATOM   3418 O  OH  . TYR A 1 435  ? 52.197 73.559  -14.680 1.00 22.85 ? 435  TYR A OH  1 
ATOM   3419 N  N   . VAL A 1 436  ? 52.793 66.186  -9.893  1.00 9.05  ? 436  VAL A N   1 
ATOM   3420 C  CA  . VAL A 1 436  ? 53.480 65.268  -8.981  1.00 8.58  ? 436  VAL A CA  1 
ATOM   3421 C  C   . VAL A 1 436  ? 54.010 64.065  -9.789  1.00 9.96  ? 436  VAL A C   1 
ATOM   3422 O  O   . VAL A 1 436  ? 55.198 63.668  -9.626  1.00 8.98  ? 436  VAL A O   1 
ATOM   3423 C  CB  . VAL A 1 436  ? 52.514 64.822  -7.844  1.00 8.36  ? 436  VAL A CB  1 
ATOM   3424 C  CG1 . VAL A 1 436  ? 53.020 63.565  -7.189  1.00 9.19  ? 436  VAL A CG1 1 
ATOM   3425 C  CG2 . VAL A 1 436  ? 52.369 65.972  -6.862  1.00 9.11  ? 436  VAL A CG2 1 
ATOM   3426 N  N   . ARG A 1 437  ? 53.207 63.504  -10.680 1.00 8.40  ? 437  ARG A N   1 
ATOM   3427 C  CA  . ARG A 1 437  ? 53.644 62.382  -11.456 1.00 8.93  ? 437  ARG A CA  1 
ATOM   3428 C  C   . ARG A 1 437  ? 54.882 62.764  -12.249 1.00 8.23  ? 437  ARG A C   1 
ATOM   3429 O  O   . ARG A 1 437  ? 55.887 62.073  -12.191 1.00 8.00  ? 437  ARG A O   1 
ATOM   3430 C  CB  . ARG A 1 437  ? 52.545 61.827  -12.392 1.00 8.44  ? 437  ARG A CB  1 
ATOM   3431 C  CG  . ARG A 1 437  ? 53.133 60.865  -13.441 1.00 8.83  ? 437  ARG A CG  1 
ATOM   3432 C  CD  . ARG A 1 437  ? 52.027 60.357  -14.368 1.00 5.80  ? 437  ARG A CD  1 
ATOM   3433 N  NE  . ARG A 1 437  ? 52.514 59.657  -15.516 1.00 7.57  ? 437  ARG A NE  1 
ATOM   3434 C  CZ  . ARG A 1 437  ? 51.739 58.872  -16.240 1.00 9.53  ? 437  ARG A CZ  1 
ATOM   3435 N  NH1 . ARG A 1 437  ? 50.464 58.640  -15.917 1.00 8.68  ? 437  ARG A NH1 1 
ATOM   3436 N  NH2 . ARG A 1 437  ? 52.197 58.388  -17.390 1.00 9.86  ? 437  ARG A NH2 1 
ATOM   3437 N  N   . ALA A 1 438  ? 54.850 63.904  -12.941 1.00 9.76  ? 438  ALA A N   1 
ATOM   3438 C  CA  . ALA A 1 438  ? 55.969 64.345  -13.775 1.00 8.42  ? 438  ALA A CA  1 
ATOM   3439 C  C   . ALA A 1 438  ? 57.231 64.626  -12.960 1.00 8.25  ? 438  ALA A C   1 
ATOM   3440 O  O   . ALA A 1 438  ? 58.317 64.235  -13.433 1.00 7.87  ? 438  ALA A O   1 
ATOM   3441 C  CB  . ALA A 1 438  ? 55.529 65.645  -14.581 1.00 8.25  ? 438  ALA A CB  1 
ATOM   3442 N  N   . ALA A 1 439  ? 57.115 65.249  -11.771 1.00 7.26  ? 439  ALA A N   1 
ATOM   3443 C  CA  . ALA A 1 439  ? 58.276 65.538  -10.970 1.00 7.94  ? 439  ALA A CA  1 
ATOM   3444 C  C   . ALA A 1 439  ? 58.896 64.234  -10.443 1.00 8.04  ? 439  ALA A C   1 
ATOM   3445 O  O   . ALA A 1 439  ? 60.113 64.112  -10.482 1.00 9.19  ? 439  ALA A O   1 
ATOM   3446 C  CB  . ALA A 1 439  ? 57.947 66.502  -9.872  1.00 5.95  ? 439  ALA A CB  1 
ATOM   3447 N  N   . GLU A 1 440  ? 58.094 63.278  -9.999  1.00 6.87  ? 440  GLU A N   1 
ATOM   3448 C  CA  . GLU A 1 440  ? 58.644 62.036  -9.510  1.00 7.50  ? 440  GLU A CA  1 
ATOM   3449 C  C   . GLU A 1 440  ? 59.282 61.254  -10.613 1.00 8.31  ? 440  GLU A C   1 
ATOM   3450 O  O   . GLU A 1 440  ? 60.348 60.693  -10.379 1.00 10.49 ? 440  GLU A O   1 
ATOM   3451 C  CB  . GLU A 1 440  ? 57.535 61.226  -8.796  1.00 7.41  ? 440  GLU A CB  1 
ATOM   3452 C  CG  . GLU A 1 440  ? 57.051 61.841  -7.521  1.00 8.88  ? 440  GLU A CG  1 
ATOM   3453 C  CD  . GLU A 1 440  ? 56.361 60.840  -6.605  1.00 12.05 ? 440  GLU A CD  1 
ATOM   3454 O  OE1 . GLU A 1 440  ? 55.227 60.418  -6.903  1.00 9.86  ? 440  GLU A OE1 1 
ATOM   3455 O  OE2 . GLU A 1 440  ? 57.009 60.495  -5.600  1.00 12.34 ? 440  GLU A OE2 1 
ATOM   3456 N  N   . MET A 1 441  ? 58.708 61.179  -11.805 1.00 8.30  ? 441  MET A N   1 
ATOM   3457 C  CA  . MET A 1 441  ? 59.285 60.468  -12.916 1.00 9.63  ? 441  MET A CA  1 
ATOM   3458 C  C   . MET A 1 441  ? 60.552 61.096  -13.478 1.00 10.63 ? 441  MET A C   1 
ATOM   3459 O  O   . MET A 1 441  ? 61.572 60.406  -13.675 1.00 9.73  ? 441  MET A O   1 
ATOM   3460 C  CB  . MET A 1 441  ? 58.237 60.340  -14.017 1.00 9.03  ? 441  MET A CB  1 
ATOM   3461 C  CG  . MET A 1 441  ? 58.706 59.609  -15.279 1.00 10.53 ? 441  MET A CG  1 
ATOM   3462 S  SD  . MET A 1 441  ? 57.438 59.347  -16.565 1.00 9.25  ? 441  MET A SD  1 
ATOM   3463 C  CE  . MET A 1 441  ? 56.357 58.064  -15.767 1.00 10.17 ? 441  MET A CE  1 
ATOM   3464 N  N   . LEU A 1 442  ? 60.498 62.399  -13.725 1.00 10.97 ? 442  LEU A N   1 
ATOM   3465 C  CA  . LEU A 1 442  ? 61.694 63.112  -14.243 1.00 11.75 ? 442  LEU A CA  1 
ATOM   3466 C  C   . LEU A 1 442  ? 62.906 62.969  -13.342 1.00 12.03 ? 442  LEU A C   1 
ATOM   3467 O  O   . LEU A 1 442  ? 64.026 62.814  -13.835 1.00 11.47 ? 442  LEU A O   1 
ATOM   3468 C  CB  . LEU A 1 442  ? 61.407 64.633  -14.473 1.00 11.40 ? 442  LEU A CB  1 
ATOM   3469 C  CG  . LEU A 1 442  ? 60.821 64.872  -15.877 1.00 11.73 ? 442  LEU A CG  1 
ATOM   3470 C  CD1 . LEU A 1 442  ? 60.261 66.247  -15.910 1.00 7.39  ? 442  LEU A CD1 1 
ATOM   3471 C  CD2 . LEU A 1 442  ? 61.905 64.638  -16.989 1.00 11.34 ? 442  LEU A CD2 1 
ATOM   3472 N  N   . SER A 1 443  ? 62.694 62.995  -12.035 1.00 9.41  ? 443  SER A N   1 
ATOM   3473 C  CA  . SER A 1 443  ? 63.824 62.923  -11.101 1.00 10.29 ? 443  SER A CA  1 
ATOM   3474 C  C   . SER A 1 443  ? 64.200 61.516  -10.739 1.00 10.87 ? 443  SER A C   1 
ATOM   3475 O  O   . SER A 1 443  ? 65.316 61.328  -10.207 1.00 11.01 ? 443  SER A O   1 
ATOM   3476 C  CB  . SER A 1 443  ? 63.560 63.711  -9.837  1.00 8.40  ? 443  SER A CB  1 
ATOM   3477 O  OG  . SER A 1 443  ? 62.420 63.249  -9.053  1.00 11.47 ? 443  SER A OG  1 
ATOM   3478 N  N   . ALA A 1 444  ? 63.345 60.546  -11.041 1.00 11.18 ? 444  ALA A N   1 
ATOM   3479 C  CA  . ALA A 1 444  ? 63.626 59.148  -10.724 1.00 11.45 ? 444  ALA A CA  1 
ATOM   3480 C  C   . ALA A 1 444  ? 64.797 58.613  -11.513 1.00 10.80 ? 444  ALA A C   1 
ATOM   3481 O  O   . ALA A 1 444  ? 65.448 57.649  -11.080 1.00 11.71 ? 444  ALA A O   1 
ATOM   3482 C  CB  . ALA A 1 444  ? 62.462 58.292  -11.035 1.00 10.20 ? 444  ALA A CB  1 
ATOM   3483 N  N   . TRP A 1 445  ? 65.076 59.195  -12.678 1.00 11.64 ? 445  TRP A N   1 
ATOM   3484 C  CA  . TRP A 1 445  ? 66.130 58.680  -13.513 1.00 11.77 ? 445  TRP A CA  1 
ATOM   3485 C  C   . TRP A 1 445  ? 67.536 58.664  -12.938 1.00 13.31 ? 445  TRP A C   1 
ATOM   3486 O  O   . TRP A 1 445  ? 68.353 57.835  -13.395 1.00 12.98 ? 445  TRP A O   1 
ATOM   3487 C  CB  . TRP A 1 445  ? 66.141 59.456  -14.854 1.00 11.25 ? 445  TRP A CB  1 
ATOM   3488 C  CG  . TRP A 1 445  ? 64.869 59.241  -15.686 1.00 9.52  ? 445  TRP A CG  1 
ATOM   3489 C  CD1 . TRP A 1 445  ? 63.852 60.155  -15.852 1.00 12.18 ? 445  TRP A CD1 1 
ATOM   3490 C  CD2 . TRP A 1 445  ? 64.442 58.051  -16.378 1.00 10.07 ? 445  TRP A CD2 1 
ATOM   3491 N  NE1 . TRP A 1 445  ? 62.872 59.628  -16.592 1.00 9.30  ? 445  TRP A NE1 1 
ATOM   3492 C  CE2 . TRP A 1 445  ? 63.177 58.337  -16.935 1.00 10.52 ? 445  TRP A CE2 1 
ATOM   3493 C  CE3 . TRP A 1 445  ? 64.995 56.782  -16.565 1.00 11.89 ? 445  TRP A CE3 1 
ATOM   3494 C  CZ2 . TRP A 1 445  ? 62.465 57.414  -17.667 1.00 11.46 ? 445  TRP A CZ2 1 
ATOM   3495 C  CZ3 . TRP A 1 445  ? 64.282 55.838  -17.325 1.00 13.06 ? 445  TRP A CZ3 1 
ATOM   3496 C  CH2 . TRP A 1 445  ? 63.017 56.172  -17.870 1.00 13.97 ? 445  TRP A CH2 1 
ATOM   3497 N  N   . HIS A 1 446  ? 67.762 59.534  -11.961 1.00 12.28 ? 446  HIS A N   1 
ATOM   3498 C  CA  . HIS A 1 446  ? 69.073 59.651  -11.316 1.00 16.32 ? 446  HIS A CA  1 
ATOM   3499 C  C   . HIS A 1 446  ? 68.917 59.687  -9.796  1.00 15.61 ? 446  HIS A C   1 
ATOM   3500 O  O   . HIS A 1 446  ? 67.837 59.956  -9.263  1.00 16.84 ? 446  HIS A O   1 
ATOM   3501 C  CB  . HIS A 1 446  ? 69.746 61.017  -11.598 1.00 16.54 ? 446  HIS A CB  1 
ATOM   3502 C  CG  . HIS A 1 446  ? 70.214 61.227  -12.993 1.00 21.32 ? 446  HIS A CG  1 
ATOM   3503 N  ND1 . HIS A 1 446  ? 69.506 61.987  -13.905 1.00 21.56 ? 446  HIS A ND1 1 
ATOM   3504 C  CD2 . HIS A 1 446  ? 71.333 60.802  -13.630 1.00 21.37 ? 446  HIS A CD2 1 
ATOM   3505 C  CE1 . HIS A 1 446  ? 70.175 62.019  -15.047 1.00 23.86 ? 446  HIS A CE1 1 
ATOM   3506 N  NE2 . HIS A 1 446  ? 71.281 61.315  -14.909 1.00 21.45 ? 446  HIS A NE2 1 
ATOM   3507 N  N   . SER A 1 447  ? 70.046 59.458  -9.114  1.00 15.61 ? 447  SER A N   1 
ATOM   3508 C  CA  . SER A 1 447  ? 70.151 59.568  -7.668  1.00 15.08 ? 447  SER A CA  1 
ATOM   3509 C  C   . SER A 1 447  ? 70.622 61.008  -7.499  1.00 15.81 ? 447  SER A C   1 
ATOM   3510 O  O   . SER A 1 447  ? 71.478 61.489  -8.272  1.00 16.60 ? 447  SER A O   1 
ATOM   3511 C  CB  A SER A 1 447  ? 71.243 58.635  -7.109  0.50 14.59 ? 447  SER A CB  1 
ATOM   3512 C  CB  B SER A 1 447  ? 71.039 58.549  -6.982  0.50 17.21 ? 447  SER A CB  1 
ATOM   3513 O  OG  A SER A 1 447  ? 70.721 57.757  -6.144  0.50 9.93  ? 447  SER A OG  1 
ATOM   3514 O  OG  B SER A 1 447  ? 71.174 58.855  -5.614  0.50 20.44 ? 447  SER A OG  1 
ATOM   3515 N  N   . TRP A 1 448  ? 70.084 61.701  -6.512  1.00 13.98 ? 448  TRP A N   1 
ATOM   3516 C  CA  . TRP A 1 448  ? 70.457 63.074  -6.256  1.00 15.91 ? 448  TRP A CA  1 
ATOM   3517 C  C   . TRP A 1 448  ? 71.141 63.262  -4.927  1.00 18.15 ? 448  TRP A C   1 
ATOM   3518 O  O   . TRP A 1 448  ? 70.775 62.626  -3.924  1.00 17.09 ? 448  TRP A O   1 
ATOM   3519 C  CB  . TRP A 1 448  ? 69.221 64.023  -6.302  1.00 14.77 ? 448  TRP A CB  1 
ATOM   3520 C  CG  . TRP A 1 448  ? 68.511 64.058  -7.673  1.00 15.78 ? 448  TRP A CG  1 
ATOM   3521 C  CD1 . TRP A 1 448  ? 67.677 63.078  -8.195  1.00 11.78 ? 448  TRP A CD1 1 
ATOM   3522 C  CD2 . TRP A 1 448  ? 68.669 65.042  -8.698  1.00 15.65 ? 448  TRP A CD2 1 
ATOM   3523 N  NE1 . TRP A 1 448  ? 67.313 63.410  -9.494  1.00 15.06 ? 448  TRP A NE1 1 
ATOM   3524 C  CE2 . TRP A 1 448  ? 67.912 64.604  -9.817  1.00 13.55 ? 448  TRP A CE2 1 
ATOM   3525 C  CE3 . TRP A 1 448  ? 69.388 66.262  -8.786  1.00 16.26 ? 448  TRP A CE3 1 
ATOM   3526 C  CZ2 . TRP A 1 448  ? 67.852 65.316  -10.989 1.00 14.13 ? 448  TRP A CZ2 1 
ATOM   3527 C  CZ3 . TRP A 1 448  ? 69.319 66.972  -9.963  1.00 14.81 ? 448  TRP A CZ3 1 
ATOM   3528 C  CH2 . TRP A 1 448  ? 68.549 66.489  -11.055 1.00 16.98 ? 448  TRP A CH2 1 
ATOM   3529 N  N   . ASP A 1 449  ? 72.113 64.171  -4.943  1.00 19.73 ? 449  ASP A N   1 
ATOM   3530 C  CA  . ASP A 1 449  ? 72.863 64.583  -3.759  1.00 22.42 ? 449  ASP A CA  1 
ATOM   3531 C  C   . ASP A 1 449  ? 71.854 65.214  -2.804  1.00 22.01 ? 449  ASP A C   1 
ATOM   3532 O  O   . ASP A 1 449  ? 70.938 65.888  -3.230  1.00 20.68 ? 449  ASP A O   1 
ATOM   3533 C  CB  . ASP A 1 449  ? 73.910 65.637  -4.181  1.00 24.35 ? 449  ASP A CB  1 
ATOM   3534 C  CG  . ASP A 1 449  ? 74.810 66.099  -3.024  1.00 28.19 ? 449  ASP A CG  1 
ATOM   3535 O  OD1 . ASP A 1 449  ? 74.400 66.949  -2.211  1.00 28.34 ? 449  ASP A OD1 1 
ATOM   3536 O  OD2 . ASP A 1 449  ? 75.957 65.597  -2.923  1.00 30.66 ? 449  ASP A OD2 1 
ATOM   3537 N  N   . GLY A 1 450  ? 72.042 65.024  -1.504  1.00 22.44 ? 450  GLY A N   1 
ATOM   3538 C  CA  . GLY A 1 450  ? 71.121 65.596  -0.535  1.00 22.48 ? 450  GLY A CA  1 
ATOM   3539 C  C   . GLY A 1 450  ? 70.984 67.084  -0.675  1.00 23.53 ? 450  GLY A C   1 
ATOM   3540 O  O   . GLY A 1 450  ? 69.912 67.672  -0.446  1.00 22.68 ? 450  GLY A O   1 
ATOM   3541 N  N   . MET A 1 451  ? 72.068 67.726  -1.062  1.00 22.04 ? 451  MET A N   1 
ATOM   3542 C  CA  . MET A 1 451  ? 72.010 69.164  -1.220  1.00 25.17 ? 451  MET A CA  1 
ATOM   3543 C  C   . MET A 1 451  ? 71.016 69.595  -2.300  1.00 22.48 ? 451  MET A C   1 
ATOM   3544 O  O   . MET A 1 451  ? 70.663 70.756  -2.356  1.00 24.76 ? 451  MET A O   1 
ATOM   3545 C  CB  . MET A 1 451  ? 73.413 69.700  -1.548  1.00 27.16 ? 451  MET A CB  1 
ATOM   3546 C  CG  . MET A 1 451  ? 74.461 69.325  -0.506  1.00 33.76 ? 451  MET A CG  1 
ATOM   3547 S  SD  . MET A 1 451  ? 74.997 70.694  0.613   1.00 41.42 ? 451  MET A SD  1 
ATOM   3548 C  CE  . MET A 1 451  ? 73.534 70.889  1.743   1.00 37.41 ? 451  MET A CE  1 
ATOM   3549 N  N   . ALA A 1 452  ? 70.579 68.685  -3.163  1.00 20.96 ? 452  ALA A N   1 
ATOM   3550 C  CA  . ALA A 1 452  ? 69.622 69.091  -4.222  1.00 18.09 ? 452  ALA A CA  1 
ATOM   3551 C  C   . ALA A 1 452  ? 68.186 69.202  -3.702  1.00 20.25 ? 452  ALA A C   1 
ATOM   3552 O  O   . ALA A 1 452  ? 67.285 69.697  -4.415  1.00 20.43 ? 452  ALA A O   1 
ATOM   3553 C  CB  . ALA A 1 452  ? 69.673 68.153  -5.342  1.00 19.46 ? 452  ALA A CB  1 
ATOM   3554 N  N   . ARG A 1 453  ? 67.992 68.761  -2.462  1.00 18.86 ? 453  ARG A N   1 
ATOM   3555 C  CA  . ARG A 1 453  ? 66.705 68.748  -1.763  1.00 18.79 ? 453  ARG A CA  1 
ATOM   3556 C  C   . ARG A 1 453  ? 65.532 68.202  -2.618  1.00 15.48 ? 453  ARG A C   1 
ATOM   3557 O  O   . ARG A 1 453  ? 64.381 68.696  -2.527  1.00 16.60 ? 453  ARG A O   1 
ATOM   3558 C  CB  . ARG A 1 453  ? 66.389 70.140  -1.279  1.00 19.07 ? 453  ARG A CB  1 
ATOM   3559 C  CG  . ARG A 1 453  ? 67.527 70.693  -0.438  1.00 22.22 ? 453  ARG A CG  1 
ATOM   3560 C  CD  . ARG A 1 453  ? 67.377 72.174  -0.298  1.00 24.63 ? 453  ARG A CD  1 
ATOM   3561 N  NE  . ARG A 1 453  ? 66.226 72.535  0.517   1.00 26.61 ? 453  ARG A NE  1 
ATOM   3562 C  CZ  . ARG A 1 453  ? 65.740 73.776  0.607   1.00 28.72 ? 453  ARG A CZ  1 
ATOM   3563 N  NH1 . ARG A 1 453  ? 66.313 74.781  -0.079  1.00 29.69 ? 453  ARG A NH1 1 
ATOM   3564 N  NH2 . ARG A 1 453  ? 64.692 74.008  1.386   1.00 29.34 ? 453  ARG A NH2 1 
ATOM   3565 N  N   . ILE A 1 454  ? 65.847 67.251  -3.480  1.00 14.87 ? 454  ILE A N   1 
ATOM   3566 C  CA  . ILE A 1 454  ? 64.837 66.658  -4.331  1.00 13.33 ? 454  ILE A CA  1 
ATOM   3567 C  C   . ILE A 1 454  ? 63.803 65.903  -3.433  1.00 14.09 ? 454  ILE A C   1 
ATOM   3568 O  O   . ILE A 1 454  ? 62.571 66.098  -3.584  1.00 12.00 ? 454  ILE A O   1 
ATOM   3569 C  CB  . ILE A 1 454  ? 65.469 65.688  -5.322  1.00 15.41 ? 454  ILE A CB  1 
ATOM   3570 C  CG1 . ILE A 1 454  ? 66.442 66.454  -6.240  1.00 15.27 ? 454  ILE A CG1 1 
ATOM   3571 C  CG2 . ILE A 1 454  ? 64.398 64.912  -6.131  1.00 14.25 ? 454  ILE A CG2 1 
ATOM   3572 C  CD1 . ILE A 1 454  ? 65.756 67.459  -7.180  1.00 14.19 ? 454  ILE A CD1 1 
ATOM   3573 N  N   . GLU A 1 455  ? 64.270 65.005  -2.570  1.00 11.39 ? 455  GLU A N   1 
ATOM   3574 C  CA  . GLU A 1 455  ? 63.358 64.239  -1.707  1.00 11.14 ? 455  GLU A CA  1 
ATOM   3575 C  C   . GLU A 1 455  ? 62.458 65.129  -0.874  1.00 11.17 ? 455  GLU A C   1 
ATOM   3576 O  O   . GLU A 1 455  ? 61.244 64.868  -0.717  1.00 11.27 ? 455  GLU A O   1 
ATOM   3577 C  CB  . GLU A 1 455  ? 64.148 63.274  -0.818  1.00 13.38 ? 455  GLU A CB  1 
ATOM   3578 C  CG  . GLU A 1 455  ? 64.677 62.072  -1.565  1.00 14.20 ? 455  GLU A CG  1 
ATOM   3579 C  CD  . GLU A 1 455  ? 66.076 62.336  -2.168  1.00 13.85 ? 455  GLU A CD  1 
ATOM   3580 O  OE1 . GLU A 1 455  ? 66.567 63.468  -2.023  1.00 14.73 ? 455  GLU A OE1 1 
ATOM   3581 O  OE2 . GLU A 1 455  ? 66.663 61.381  -2.746  1.00 15.20 ? 455  GLU A OE2 1 
ATOM   3582 N  N   . GLU A 1 456  ? 63.002 66.190  -0.308  1.00 11.64 ? 456  GLU A N   1 
ATOM   3583 C  CA  . GLU A 1 456  ? 62.301 67.133  0.513   1.00 13.08 ? 456  GLU A CA  1 
ATOM   3584 C  C   . GLU A 1 456  ? 61.135 67.791  -0.287  1.00 12.54 ? 456  GLU A C   1 
ATOM   3585 O  O   . GLU A 1 456  ? 59.958 67.815  0.135   1.00 13.46 ? 456  GLU A O   1 
ATOM   3586 C  CB  . GLU A 1 456  ? 63.333 68.179  0.927   1.00 16.35 ? 456  GLU A CB  1 
ATOM   3587 C  CG  . GLU A 1 456  ? 62.793 69.232  1.767   1.00 21.82 ? 456  GLU A CG  1 
ATOM   3588 C  CD  . GLU A 1 456  ? 63.724 70.450  1.877   1.00 25.26 ? 456  GLU A CD  1 
ATOM   3589 O  OE1 . GLU A 1 456  ? 64.958 70.319  1.667   1.00 27.52 ? 456  GLU A OE1 1 
ATOM   3590 O  OE2 . GLU A 1 456  ? 63.214 71.550  2.193   1.00 27.38 ? 456  GLU A OE2 1 
ATOM   3591 N  N   . ARG A 1 457  ? 61.472 68.303  -1.458  1.00 12.90 ? 457  ARG A N   1 
ATOM   3592 C  CA  . ARG A 1 457  ? 60.427 68.975  -2.271  1.00 12.97 ? 457  ARG A CA  1 
ATOM   3593 C  C   . ARG A 1 457  ? 59.310 67.988  -2.708  1.00 11.67 ? 457  ARG A C   1 
ATOM   3594 O  O   . ARG A 1 457  ? 58.121 68.346  -2.715  1.00 12.82 ? 457  ARG A O   1 
ATOM   3595 C  CB  . ARG A 1 457  ? 61.033 69.635  -3.506  1.00 13.73 ? 457  ARG A CB  1 
ATOM   3596 C  CG  . ARG A 1 457  ? 61.365 71.101  -3.314  1.00 16.90 ? 457  ARG A CG  1 
ATOM   3597 C  CD  . ARG A 1 457  ? 62.354 71.283  -2.245  1.00 19.01 ? 457  ARG A CD  1 
ATOM   3598 N  NE  . ARG A 1 457  ? 62.740 72.688  -2.109  1.00 21.29 ? 457  ARG A NE  1 
ATOM   3599 C  CZ  . ARG A 1 457  ? 63.737 73.280  -2.789  1.00 23.03 ? 457  ARG A CZ  1 
ATOM   3600 N  NH1 . ARG A 1 457  ? 64.461 72.620  -3.682  1.00 21.47 ? 457  ARG A NH1 1 
ATOM   3601 N  NH2 . ARG A 1 457  ? 64.057 74.535  -2.523  1.00 23.71 ? 457  ARG A NH2 1 
ATOM   3602 N  N   . LEU A 1 458  ? 59.708 66.782  -3.114  1.00 11.71 ? 458  LEU A N   1 
ATOM   3603 C  CA  . LEU A 1 458  ? 58.725 65.771  -3.540  1.00 10.11 ? 458  LEU A CA  1 
ATOM   3604 C  C   . LEU A 1 458  ? 57.863 65.320  -2.387  1.00 10.87 ? 458  LEU A C   1 
ATOM   3605 O  O   . LEU A 1 458  ? 56.677 65.085  -2.616  1.00 9.80  ? 458  LEU A O   1 
ATOM   3606 C  CB  . LEU A 1 458  ? 59.378 64.562  -4.172  1.00 10.23 ? 458  LEU A CB  1 
ATOM   3607 C  CG  . LEU A 1 458  ? 60.083 64.964  -5.497  1.00 11.72 ? 458  LEU A CG  1 
ATOM   3608 C  CD1 . LEU A 1 458  ? 60.896 63.735  -5.977  1.00 11.00 ? 458  LEU A CD1 1 
ATOM   3609 C  CD2 . LEU A 1 458  ? 59.048 65.454  -6.645  1.00 11.06 ? 458  LEU A CD2 1 
ATOM   3610 N  N   . GLU A 1 459  ? 58.385 65.236  -1.157  1.00 8.92  ? 459  GLU A N   1 
ATOM   3611 C  CA  . GLU A 1 459  ? 57.591 64.797  -0.020  1.00 11.23 ? 459  GLU A CA  1 
ATOM   3612 C  C   . GLU A 1 459  ? 56.571 65.835  0.239   1.00 11.66 ? 459  GLU A C   1 
ATOM   3613 O  O   . GLU A 1 459  ? 55.404 65.506  0.476   1.00 10.49 ? 459  GLU A O   1 
ATOM   3614 C  CB  . GLU A 1 459  ? 58.464 64.567  1.244   1.00 13.46 ? 459  GLU A CB  1 
ATOM   3615 C  CG  . GLU A 1 459  ? 57.671 64.052  2.456   1.00 15.82 ? 459  GLU A CG  1 
ATOM   3616 C  CD  . GLU A 1 459  ? 58.588 63.442  3.518   1.00 18.64 ? 459  GLU A CD  1 
ATOM   3617 O  OE1 . GLU A 1 459  ? 59.197 64.254  4.260   1.00 20.72 ? 459  GLU A OE1 1 
ATOM   3618 O  OE2 . GLU A 1 459  ? 58.706 62.173  3.594   1.00 21.85 ? 459  GLU A OE2 1 
ATOM   3619 N  N   . GLN A 1 460  ? 56.950 67.102  0.185   1.00 10.96 ? 460  GLN A N   1 
ATOM   3620 C  CA  . GLN A 1 460  ? 56.011 68.206  0.429   1.00 11.69 ? 460  GLN A CA  1 
ATOM   3621 C  C   . GLN A 1 460  ? 54.910 68.162  -0.643  1.00 8.33  ? 460  GLN A C   1 
ATOM   3622 O  O   . GLN A 1 460  ? 53.711 68.273  -0.316  1.00 10.80 ? 460  GLN A O   1 
ATOM   3623 C  CB  . GLN A 1 460  ? 56.785 69.544  0.358   1.00 14.34 ? 460  GLN A CB  1 
ATOM   3624 C  CG  . GLN A 1 460  ? 55.867 70.745  0.494   1.00 20.03 ? 460  GLN A CG  1 
ATOM   3625 C  CD  . GLN A 1 460  ? 56.593 72.072  0.287   1.00 23.78 ? 460  GLN A CD  1 
ATOM   3626 O  OE1 . GLN A 1 460  ? 57.673 72.112  -0.308  1.00 27.43 ? 460  GLN A OE1 1 
ATOM   3627 N  NE2 . GLN A 1 460  ? 55.989 73.159  0.748   1.00 28.56 ? 460  GLN A NE2 1 
ATOM   3628 N  N   . ALA A 1 461  ? 55.291 67.933  -1.895  1.00 10.61 ? 461  ALA A N   1 
ATOM   3629 C  CA  . ALA A 1 461  ? 54.276 67.954  -2.978  1.00 9.67  ? 461  ALA A CA  1 
ATOM   3630 C  C   . ALA A 1 461  ? 53.279 66.819  -2.795  1.00 10.50 ? 461  ALA A C   1 
ATOM   3631 O  O   . ALA A 1 461  ? 52.064 67.047  -2.844  1.00 9.71  ? 461  ALA A O   1 
ATOM   3632 C  CB  . ALA A 1 461  ? 54.931 67.893  -4.405  1.00 10.97 ? 461  ALA A CB  1 
ATOM   3633 N  N   . ARG A 1 462  ? 53.773 65.616  -2.551  1.00 9.13  ? 462  ARG A N   1 
ATOM   3634 C  CA  . ARG A 1 462  ? 52.920 64.476  -2.306  1.00 6.91  ? 462  ARG A CA  1 
ATOM   3635 C  C   . ARG A 1 462  ? 52.021 64.722  -1.083  1.00 8.26  ? 462  ARG A C   1 
ATOM   3636 O  O   . ARG A 1 462  ? 50.839 64.366  -1.108  1.00 8.34  ? 462  ARG A O   1 
ATOM   3637 C  CB  . ARG A 1 462  ? 53.739 63.196  -2.061  1.00 8.30  ? 462  ARG A CB  1 
ATOM   3638 C  CG  . ARG A 1 462  ? 54.536 62.713  -3.264  1.00 7.09  ? 462  ARG A CG  1 
ATOM   3639 C  CD  . ARG A 1 462  ? 54.899 61.247  -2.982  1.00 8.90  ? 462  ARG A CD  1 
ATOM   3640 N  NE  . ARG A 1 462  ? 55.820 61.091  -1.824  1.00 9.58  ? 462  ARG A NE  1 
ATOM   3641 C  CZ  . ARG A 1 462  ? 57.154 61.276  -1.883  1.00 11.70 ? 462  ARG A CZ  1 
ATOM   3642 N  NH1 . ARG A 1 462  ? 57.773 61.589  -3.038  1.00 10.61 ? 462  ARG A NH1 1 
ATOM   3643 N  NH2 . ARG A 1 462  ? 57.857 61.224  -0.764  1.00 12.80 ? 462  ARG A NH2 1 
ATOM   3644 N  N   . ARG A 1 463  ? 52.532 65.270  0.015   1.00 7.07  ? 463  ARG A N   1 
ATOM   3645 C  CA  . ARG A 1 463  ? 51.717 65.477  1.200   1.00 8.09  ? 463  ARG A CA  1 
ATOM   3646 C  C   . ARG A 1 463  ? 50.666 66.548  1.005   1.00 8.62  ? 463  ARG A C   1 
ATOM   3647 O  O   . ARG A 1 463  ? 49.522 66.380  1.491   1.00 9.76  ? 463  ARG A O   1 
ATOM   3648 C  CB  . ARG A 1 463  ? 52.565 65.697  2.456   1.00 10.90 ? 463  ARG A CB  1 
ATOM   3649 C  CG  . ARG A 1 463  ? 53.318 64.405  2.780   1.00 10.58 ? 463  ARG A CG  1 
ATOM   3650 C  CD  . ARG A 1 463  ? 54.333 64.603  3.931   1.00 10.68 ? 463  ARG A CD  1 
ATOM   3651 N  NE  . ARG A 1 463  ? 54.832 63.254  4.268   1.00 12.58 ? 463  ARG A NE  1 
ATOM   3652 C  CZ  . ARG A 1 463  ? 55.550 62.975  5.352   1.00 15.88 ? 463  ARG A CZ  1 
ATOM   3653 N  NH1 . ARG A 1 463  ? 55.859 63.940  6.179   1.00 16.31 ? 463  ARG A NH1 1 
ATOM   3654 N  NH2 . ARG A 1 463  ? 55.930 61.710  5.589   1.00 13.42 ? 463  ARG A NH2 1 
ATOM   3655 N  N   . GLU A 1 464  ? 50.933 67.603  0.237   1.00 9.36  ? 464  GLU A N   1 
ATOM   3656 C  CA  . GLU A 1 464  ? 49.881 68.595  0.133   1.00 9.94  ? 464  GLU A CA  1 
ATOM   3657 C  C   . GLU A 1 464  ? 48.801 68.088  -0.812  1.00 7.64  ? 464  GLU A C   1 
ATOM   3658 O  O   . GLU A 1 464  ? 47.608 68.338  -0.563  1.00 8.72  ? 464  GLU A O   1 
ATOM   3659 C  CB  . GLU A 1 464  ? 50.406 69.948  -0.372  1.00 10.17 ? 464  GLU A CB  1 
ATOM   3660 C  CG  . GLU A 1 464  ? 51.611 70.465  0.383   1.00 13.22 ? 464  GLU A CG  1 
ATOM   3661 C  CD  . GLU A 1 464  ? 51.287 70.999  1.740   1.00 15.69 ? 464  GLU A CD  1 
ATOM   3662 O  OE1 . GLU A 1 464  ? 50.272 70.640  2.328   1.00 16.07 ? 464  GLU A OE1 1 
ATOM   3663 O  OE2 . GLU A 1 464  ? 52.087 71.815  2.254   1.00 21.86 ? 464  GLU A OE2 1 
ATOM   3664 N  N   . LEU A 1 465  ? 49.154 67.325  -1.832  1.00 9.25  ? 465  LEU A N   1 
ATOM   3665 C  CA  . LEU A 1 465  ? 48.137 66.774  -2.734  1.00 7.83  ? 465  LEU A CA  1 
ATOM   3666 C  C   . LEU A 1 465  ? 47.338 65.701  -1.986  1.00 8.87  ? 465  LEU A C   1 
ATOM   3667 O  O   . LEU A 1 465  ? 46.121 65.627  -2.150  1.00 8.19  ? 465  LEU A O   1 
ATOM   3668 C  CB  . LEU A 1 465  ? 48.758 66.145  -3.943  1.00 8.97  ? 465  LEU A CB  1 
ATOM   3669 C  CG  . LEU A 1 465  ? 47.810 65.528  -4.986  1.00 9.18  ? 465  LEU A CG  1 
ATOM   3670 C  CD1 . LEU A 1 465  ? 46.754 66.617  -5.522  1.00 8.92  ? 465  LEU A CD1 1 
ATOM   3671 C  CD2 . LEU A 1 465  ? 48.659 64.998  -6.202  1.00 7.51  ? 465  LEU A CD2 1 
ATOM   3672 N  N   . SER A 1 466  ? 48.026 64.876  -1.172  1.00 9.48  ? 466  SER A N   1 
ATOM   3673 C  CA  . SER A 1 466  ? 47.378 63.827  -0.363  1.00 9.02  ? 466  SER A CA  1 
ATOM   3674 C  C   . SER A 1 466  ? 46.400 64.447  0.594   1.00 7.37  ? 466  SER A C   1 
ATOM   3675 O  O   . SER A 1 466  ? 45.263 63.946  0.717   1.00 8.10  ? 466  SER A O   1 
ATOM   3676 C  CB  . SER A 1 466  ? 48.438 63.017  0.421   1.00 8.55  ? 466  SER A CB  1 
ATOM   3677 O  OG  . SER A 1 466  ? 49.197 62.323  -0.562  1.00 9.50  ? 466  SER A OG  1 
ATOM   3678 N  N   . LEU A 1 467  ? 46.781 65.558  1.224   1.00 5.73  ? 467  LEU A N   1 
ATOM   3679 C  CA  . LEU A 1 467  ? 45.915 66.209  2.203   1.00 6.99  ? 467  LEU A CA  1 
ATOM   3680 C  C   . LEU A 1 467  ? 44.625 66.667  1.516   1.00 6.85  ? 467  LEU A C   1 
ATOM   3681 O  O   . LEU A 1 467  ? 43.518 66.505  2.056   1.00 6.86  ? 467  LEU A O   1 
ATOM   3682 C  CB  . LEU A 1 467  ? 46.617 67.434  2.840   1.00 9.48  ? 467  LEU A CB  1 
ATOM   3683 C  CG  . LEU A 1 467  ? 45.785 68.095  3.928   1.00 11.68 ? 467  LEU A CG  1 
ATOM   3684 C  CD1 . LEU A 1 467  ? 45.898 67.307  5.213   1.00 13.31 ? 467  LEU A CD1 1 
ATOM   3685 C  CD2 . LEU A 1 467  ? 46.345 69.557  4.204   1.00 13.49 ? 467  LEU A CD2 1 
ATOM   3686 N  N   . PHE A 1 468  ? 44.736 67.118  0.257   1.00 7.28  ? 468  PHE A N   1 
ATOM   3687 C  CA  . PHE A 1 468  ? 43.562 67.673  -0.458  1.00 7.64  ? 468  PHE A CA  1 
ATOM   3688 C  C   . PHE A 1 468  ? 42.581 66.558  -0.868  1.00 7.74  ? 468  PHE A C   1 
ATOM   3689 O  O   . PHE A 1 468  ? 41.428 66.857  -1.200  1.00 7.52  ? 468  PHE A O   1 
ATOM   3690 C  CB  . PHE A 1 468  ? 43.967 68.482  -1.699  1.00 8.17  ? 468  PHE A CB  1 
ATOM   3691 C  CG  . PHE A 1 468  ? 42.835 69.311  -2.268  1.00 6.22  ? 468  PHE A CG  1 
ATOM   3692 C  CD1 . PHE A 1 468  ? 42.199 70.259  -1.480  1.00 8.29  ? 468  PHE A CD1 1 
ATOM   3693 C  CD2 . PHE A 1 468  ? 42.399 69.107  -3.555  1.00 8.04  ? 468  PHE A CD2 1 
ATOM   3694 C  CE1 . PHE A 1 468  ? 41.066 70.992  -2.041  1.00 6.21  ? 468  PHE A CE1 1 
ATOM   3695 C  CE2 . PHE A 1 468  ? 41.299 69.850  -4.092  1.00 6.86  ? 468  PHE A CE2 1 
ATOM   3696 C  CZ  . PHE A 1 468  ? 40.643 70.769  -3.313  1.00 9.55  ? 468  PHE A CZ  1 
ATOM   3697 N  N   . GLN A 1 469  ? 43.003 65.288  -0.860  1.00 6.64  ? 469  GLN A N   1 
ATOM   3698 C  CA  . GLN A 1 469  ? 42.037 64.219  -1.095  1.00 6.72  ? 469  GLN A CA  1 
ATOM   3699 C  C   . GLN A 1 469  ? 41.017 64.027  0.041   1.00 7.77  ? 469  GLN A C   1 
ATOM   3700 O  O   . GLN A 1 469  ? 40.062 63.269  -0.174  1.00 6.86  ? 469  GLN A O   1 
ATOM   3701 C  CB  . GLN A 1 469  ? 42.738 62.883  -1.277  1.00 7.60  ? 469  GLN A CB  1 
ATOM   3702 C  CG  . GLN A 1 469  ? 43.848 62.925  -2.390  1.00 5.95  ? 469  GLN A CG  1 
ATOM   3703 C  CD  . GLN A 1 469  ? 43.366 63.547  -3.672  1.00 9.05  ? 469  GLN A CD  1 
ATOM   3704 O  OE1 . GLN A 1 469  ? 42.391 63.065  -4.243  1.00 7.61  ? 469  GLN A OE1 1 
ATOM   3705 N  NE2 . GLN A 1 469  ? 44.008 64.633  -4.131  1.00 7.43  ? 469  GLN A NE2 1 
ATOM   3706 N  N   . HIS A 1 470  ? 41.206 64.666  1.212   1.00 5.58  ? 470  HIS A N   1 
ATOM   3707 C  CA  . HIS A 1 470  ? 40.284 64.595  2.362   1.00 5.10  ? 470  HIS A CA  1 
ATOM   3708 C  C   . HIS A 1 470  ? 38.859 64.871  1.848   1.00 5.74  ? 470  HIS A C   1 
ATOM   3709 O  O   . HIS A 1 470  ? 38.659 65.627  0.903   1.00 5.99  ? 470  HIS A O   1 
ATOM   3710 C  CB  . HIS A 1 470  ? 40.707 65.655  3.400   1.00 6.97  ? 470  HIS A CB  1 
ATOM   3711 C  CG  . HIS A 1 470  ? 39.739 65.824  4.507   1.00 7.46  ? 470  HIS A CG  1 
ATOM   3712 N  ND1 . HIS A 1 470  ? 39.140 64.755  5.153   1.00 6.33  ? 470  HIS A ND1 1 
ATOM   3713 C  CD2 . HIS A 1 470  ? 39.228 66.946  5.063   1.00 9.17  ? 470  HIS A CD2 1 
ATOM   3714 C  CE1 . HIS A 1 470  ? 38.291 65.231  6.047   1.00 7.08  ? 470  HIS A CE1 1 
ATOM   3715 N  NE2 . HIS A 1 470  ? 38.312 66.554  5.993   1.00 7.93  ? 470  HIS A NE2 1 
ATOM   3716 N  N   . HIS A 1 471  ? 37.880 64.222  2.499   1.00 5.60  ? 471  HIS A N   1 
ATOM   3717 C  CA  . HIS A 1 471  ? 36.464 64.369  2.168   1.00 6.97  ? 471  HIS A CA  1 
ATOM   3718 C  C   . HIS A 1 471  ? 35.874 65.763  2.412   1.00 9.35  ? 471  HIS A C   1 
ATOM   3719 O  O   . HIS A 1 471  ? 34.659 65.918  2.273   1.00 9.41  ? 471  HIS A O   1 
ATOM   3720 C  CB  . HIS A 1 471  ? 35.580 63.245  2.783   1.00 7.72  ? 471  HIS A CB  1 
ATOM   3721 C  CG  . HIS A 1 471  ? 35.659 63.146  4.270   1.00 4.99  ? 471  HIS A CG  1 
ATOM   3722 N  ND1 . HIS A 1 471  ? 36.656 62.429  4.921   1.00 5.27  ? 471  HIS A ND1 1 
ATOM   3723 C  CD2 . HIS A 1 471  ? 34.879 63.682  5.242   1.00 6.96  ? 471  HIS A CD2 1 
ATOM   3724 C  CE1 . HIS A 1 471  ? 36.498 62.554  6.221   1.00 6.21  ? 471  HIS A CE1 1 
ATOM   3725 N  NE2 . HIS A 1 471  ? 35.421 63.301  6.434   1.00 5.20  ? 471  HIS A NE2 1 
ATOM   3726 N  N   . ASP A 1 472  ? 36.712 66.760  2.818   1.00 8.82  ? 472  ASP A N   1 
ATOM   3727 C  CA  . ASP A 1 472  ? 36.255 68.158  2.870   1.00 8.07  ? 472  ASP A CA  1 
ATOM   3728 C  C   . ASP A 1 472  ? 37.209 69.011  2.054   1.00 7.84  ? 472  ASP A C   1 
ATOM   3729 O  O   . ASP A 1 472  ? 37.056 70.220  2.054   1.00 8.96  ? 472  ASP A O   1 
ATOM   3730 C  CB  . ASP A 1 472  ? 36.160 68.725  4.305   1.00 7.28  ? 472  ASP A CB  1 
ATOM   3731 C  CG  . ASP A 1 472  ? 35.125 67.970  5.154   1.00 8.98  ? 472  ASP A CG  1 
ATOM   3732 O  OD1 . ASP A 1 472  ? 33.929 68.027  4.713   1.00 9.30  ? 472  ASP A OD1 1 
ATOM   3733 O  OD2 . ASP A 1 472  ? 35.500 67.344  6.134   1.00 7.76  ? 472  ASP A OD2 1 
ATOM   3734 N  N   . GLY A 1 473  ? 38.166 68.381  1.354   1.00 6.82  ? 473  GLY A N   1 
ATOM   3735 C  CA  . GLY A 1 473  ? 39.084 69.117  0.520   1.00 7.05  ? 473  GLY A CA  1 
ATOM   3736 C  C   . GLY A 1 473  ? 38.581 69.199  -0.883  1.00 8.41  ? 473  GLY A C   1 
ATOM   3737 O  O   . GLY A 1 473  ? 37.836 70.141  -1.250  1.00 6.72  ? 473  GLY A O   1 
ATOM   3738 N  N   . ILE A 1 474  ? 38.931 68.210  -1.689  1.00 7.24  ? 474  ILE A N   1 
ATOM   3739 C  CA  . ILE A 1 474  ? 38.485 68.230  -3.079  1.00 6.86  ? 474  ILE A CA  1 
ATOM   3740 C  C   . ILE A 1 474  ? 36.951 68.367  -3.213  1.00 7.21  ? 474  ILE A C   1 
ATOM   3741 O  O   . ILE A 1 474  ? 36.448 68.833  -4.209  1.00 9.36  ? 474  ILE A O   1 
ATOM   3742 C  CB  . ILE A 1 474  ? 39.075 66.938  -3.791  1.00 5.33  ? 474  ILE A CB  1 
ATOM   3743 C  CG1 . ILE A 1 474  ? 38.908 67.015  -5.322  1.00 7.60  ? 474  ILE A CG1 1 
ATOM   3744 C  CG2 . ILE A 1 474  ? 38.486 65.636  -3.164  1.00 6.21  ? 474  ILE A CG2 1 
ATOM   3745 C  CD1 . ILE A 1 474  ? 39.581 65.823  -6.098  1.00 8.43  ? 474  ILE A CD1 1 
ATOM   3746 N  N   . THR A 1 475  ? 36.236 67.926  -2.222  1.00 7.56  ? 475  THR A N   1 
ATOM   3747 C  CA  . THR A 1 475  ? 34.772 68.006  -2.229  1.00 6.50  ? 475  THR A CA  1 
ATOM   3748 C  C   . THR A 1 475  ? 34.228 69.454  -2.226  1.00 8.47  ? 475  THR A C   1 
ATOM   3749 O  O   . THR A 1 475  ? 33.054 69.650  -2.539  1.00 8.71  ? 475  THR A O   1 
ATOM   3750 C  CB  . THR A 1 475  ? 34.164 67.359  -0.919  1.00 7.64  ? 475  THR A CB  1 
ATOM   3751 O  OG1 . THR A 1 475  ? 34.718 68.038  0.211   1.00 8.14  ? 475  THR A OG1 1 
ATOM   3752 C  CG2 . THR A 1 475  ? 34.534 65.830  -0.853  1.00 6.03  ? 475  THR A CG2 1 
ATOM   3753 N  N   . GLY A 1 476  ? 35.018 70.416  -1.788  1.00 7.70  ? 476  GLY A N   1 
ATOM   3754 C  CA  . GLY A 1 476  ? 34.493 71.806  -1.750  1.00 7.60  ? 476  GLY A CA  1 
ATOM   3755 C  C   . GLY A 1 476  ? 33.514 71.969  -0.605  1.00 9.01  ? 476  GLY A C   1 
ATOM   3756 O  O   . GLY A 1 476  ? 32.624 72.823  -0.717  1.00 8.31  ? 476  GLY A O   1 
ATOM   3757 N  N   . THR A 1 477  ? 33.670 71.199  0.487   1.00 8.33  ? 477  THR A N   1 
ATOM   3758 C  CA  . THR A 1 477  ? 32.753 71.328  1.597   1.00 7.14  ? 477  THR A CA  1 
ATOM   3759 C  C   . THR A 1 477  ? 33.382 71.954  2.862   1.00 9.28  ? 477  THR A C   1 
ATOM   3760 O  O   . THR A 1 477  ? 32.906 71.826  3.967   1.00 8.80  ? 477  THR A O   1 
ATOM   3761 C  CB  . THR A 1 477  ? 32.096 69.946  1.937   1.00 5.80  ? 477  THR A CB  1 
ATOM   3762 O  OG1 . THR A 1 477  ? 33.153 69.000  2.222   1.00 9.17  ? 477  THR A OG1 1 
ATOM   3763 C  CG2 . THR A 1 477  ? 31.250 69.493  0.789   1.00 6.25  ? 477  THR A CG2 1 
ATOM   3764 N  N   . ALA A 1 478  ? 34.503 72.674  2.689   1.00 9.18  ? 478  ALA A N   1 
ATOM   3765 C  CA  . ALA A 1 478  ? 35.107 73.307  3.846   1.00 9.61  ? 478  ALA A CA  1 
ATOM   3766 C  C   . ALA A 1 478  ? 34.753 74.787  3.954   1.00 11.27 ? 478  ALA A C   1 
ATOM   3767 O  O   . ALA A 1 478  ? 34.246 75.400  3.039   1.00 8.98  ? 478  ALA A O   1 
ATOM   3768 C  CB  . ALA A 1 478  ? 36.688 73.154  3.860   1.00 9.48  ? 478  ALA A CB  1 
ATOM   3769 N  N   . LYS A 1 479  ? 35.090 75.392  5.088   1.00 9.90  ? 479  LYS A N   1 
ATOM   3770 C  CA  . LYS A 1 479  ? 34.834 76.819  5.193   1.00 12.46 ? 479  LYS A CA  1 
ATOM   3771 C  C   . LYS A 1 479  ? 35.808 77.604  4.305   1.00 12.74 ? 479  LYS A C   1 
ATOM   3772 O  O   . LYS A 1 479  ? 36.910 77.146  3.989   1.00 11.65 ? 479  LYS A O   1 
ATOM   3773 C  CB  . LYS A 1 479  ? 34.976 77.254  6.639   1.00 13.38 ? 479  LYS A CB  1 
ATOM   3774 C  CG  . LYS A 1 479  ? 33.724 76.851  7.451   1.00 18.16 ? 479  LYS A CG  1 
ATOM   3775 C  CD  . LYS A 1 479  ? 33.750 77.316  8.890   1.00 21.22 ? 479  LYS A CD  1 
ATOM   3776 C  CE  . LYS A 1 479  ? 32.950 78.579  9.075   1.00 26.06 ? 479  LYS A CE  1 
ATOM   3777 N  NZ  . LYS A 1 479  ? 31.457 78.414  9.138   1.00 25.96 ? 479  LYS A NZ  1 
ATOM   3778 N  N   . THR A 1 480  ? 35.391 78.798  3.932   1.00 14.71 ? 480  THR A N   1 
ATOM   3779 C  CA  . THR A 1 480  ? 36.197 79.648  3.084   1.00 15.82 ? 480  THR A CA  1 
ATOM   3780 C  C   . THR A 1 480  ? 37.679 79.757  3.437   1.00 12.39 ? 480  THR A C   1 
ATOM   3781 O  O   . THR A 1 480  ? 38.530 79.623  2.590   1.00 12.06 ? 480  THR A O   1 
ATOM   3782 C  CB  . THR A 1 480  ? 35.615 81.097  3.076   1.00 17.80 ? 480  THR A CB  1 
ATOM   3783 O  OG1 . THR A 1 480  ? 34.239 81.055  2.676   1.00 20.07 ? 480  THR A OG1 1 
ATOM   3784 C  CG2 . THR A 1 480  ? 36.394 81.979  2.100   1.00 18.37 ? 480  THR A CG2 1 
ATOM   3785 N  N   . HIS A 1 481  ? 37.991 80.022  4.684   1.00 12.29 ? 481  HIS A N   1 
ATOM   3786 C  CA  . HIS A 1 481  ? 39.411 80.171  5.022   1.00 12.29 ? 481  HIS A CA  1 
ATOM   3787 C  C   . HIS A 1 481  ? 40.147 78.870  4.955   1.00 12.52 ? 481  HIS A C   1 
ATOM   3788 O  O   . HIS A 1 481  ? 41.355 78.844  4.902   1.00 13.23 ? 481  HIS A O   1 
ATOM   3789 C  CB  . HIS A 1 481  ? 39.575 80.869  6.402   1.00 13.98 ? 481  HIS A CB  1 
ATOM   3790 C  CG  . HIS A 1 481  ? 39.519 79.980  7.603   1.00 15.18 ? 481  HIS A CG  1 
ATOM   3791 N  ND1 . HIS A 1 481  ? 38.334 79.601  8.208   1.00 16.38 ? 481  HIS A ND1 1 
ATOM   3792 C  CD2 . HIS A 1 481  ? 40.516 79.472  8.370   1.00 13.72 ? 481  HIS A CD2 1 
ATOM   3793 C  CE1 . HIS A 1 481  ? 38.600 78.915  9.312   1.00 17.41 ? 481  HIS A CE1 1 
ATOM   3794 N  NE2 . HIS A 1 481  ? 39.920 78.828  9.433   1.00 14.64 ? 481  HIS A NE2 1 
ATOM   3795 N  N   . VAL A 1 482  ? 39.411 77.758  5.022   1.00 13.32 ? 482  VAL A N   1 
ATOM   3796 C  CA  . VAL A 1 482  ? 40.088 76.441  4.908   1.00 10.81 ? 482  VAL A CA  1 
ATOM   3797 C  C   . VAL A 1 482  ? 40.355 76.152  3.461   1.00 11.29 ? 482  VAL A C   1 
ATOM   3798 O  O   . VAL A 1 482  ? 41.397 75.643  3.164   1.00 8.41  ? 482  VAL A O   1 
ATOM   3799 C  CB  . VAL A 1 482  ? 39.214 75.319  5.508   1.00 10.84 ? 482  VAL A CB  1 
ATOM   3800 C  CG1 . VAL A 1 482  ? 39.966 73.948  5.516   1.00 8.13  ? 482  VAL A CG1 1 
ATOM   3801 C  CG2 . VAL A 1 482  ? 38.944 75.684  6.991   1.00 9.46  ? 482  VAL A CG2 1 
ATOM   3802 N  N   . VAL A 1 483  ? 39.437 76.470  2.557   1.00 8.36  ? 483  VAL A N   1 
ATOM   3803 C  CA  . VAL A 1 483  ? 39.703 76.281  1.120   1.00 9.85  ? 483  VAL A CA  1 
ATOM   3804 C  C   . VAL A 1 483  ? 40.950 77.124  0.808   1.00 11.93 ? 483  VAL A C   1 
ATOM   3805 O  O   . VAL A 1 483  ? 41.789 76.682  0.041   1.00 11.10 ? 483  VAL A O   1 
ATOM   3806 C  CB  . VAL A 1 483  ? 38.463 76.787  0.274   1.00 10.08 ? 483  VAL A CB  1 
ATOM   3807 C  CG1 . VAL A 1 483  ? 38.751 76.713  -1.207  1.00 12.34 ? 483  VAL A CG1 1 
ATOM   3808 C  CG2 . VAL A 1 483  ? 37.213 75.950  0.619   1.00 9.75  ? 483  VAL A CG2 1 
ATOM   3809 N  N   . VAL A 1 484  ? 41.073 78.324  1.397   1.00 11.77 ? 484  VAL A N   1 
ATOM   3810 C  CA  . VAL A 1 484  ? 42.246 79.160  1.152   1.00 11.62 ? 484  VAL A CA  1 
ATOM   3811 C  C   . VAL A 1 484  ? 43.514 78.439  1.584   1.00 11.02 ? 484  VAL A C   1 
ATOM   3812 O  O   . VAL A 1 484  ? 44.524 78.432  0.869   1.00 10.54 ? 484  VAL A O   1 
ATOM   3813 C  CB  . VAL A 1 484  ? 42.119 80.514  1.857   1.00 12.92 ? 484  VAL A CB  1 
ATOM   3814 C  CG1 . VAL A 1 484  ? 43.497 81.285  1.775   1.00 14.82 ? 484  VAL A CG1 1 
ATOM   3815 C  CG2 . VAL A 1 484  ? 41.029 81.330  1.152   1.00 14.83 ? 484  VAL A CG2 1 
ATOM   3816 N  N   . ASP A 1 485  ? 43.448 77.809  2.740   1.00 10.17 ? 485  ASP A N   1 
ATOM   3817 C  CA  . ASP A 1 485  ? 44.629 77.039  3.181   1.00 12.02 ? 485  ASP A CA  1 
ATOM   3818 C  C   . ASP A 1 485  ? 44.974 75.891  2.231   1.00 11.70 ? 485  ASP A C   1 
ATOM   3819 O  O   . ASP A 1 485  ? 46.123 75.711  1.857   1.00 11.37 ? 485  ASP A O   1 
ATOM   3820 C  CB  . ASP A 1 485  ? 44.384 76.484  4.561   1.00 11.71 ? 485  ASP A CB  1 
ATOM   3821 C  CG  . ASP A 1 485  ? 45.649 75.855  5.156   1.00 12.89 ? 485  ASP A CG  1 
ATOM   3822 O  OD1 . ASP A 1 485  ? 46.663 76.603  5.236   1.00 16.64 ? 485  ASP A OD1 1 
ATOM   3823 O  OD2 . ASP A 1 485  ? 45.634 74.676  5.542   1.00 12.93 ? 485  ASP A OD2 1 
ATOM   3824 N  N   . TYR A 1 486  ? 44.008 75.099  1.780   1.00 9.44  ? 486  TYR A N   1 
ATOM   3825 C  CA  . TYR A 1 486  ? 44.328 74.028  0.832   1.00 10.32 ? 486  TYR A CA  1 
ATOM   3826 C  C   . TYR A 1 486  ? 44.908 74.587  -0.471  1.00 10.00 ? 486  TYR A C   1 
ATOM   3827 O  O   . TYR A 1 486  ? 45.824 74.019  -1.051  1.00 9.36  ? 486  TYR A O   1 
ATOM   3828 C  CB  . TYR A 1 486  ? 43.077 73.251  0.440   1.00 11.92 ? 486  TYR A CB  1 
ATOM   3829 C  CG  . TYR A 1 486  ? 42.465 72.475  1.587   1.00 9.79  ? 486  TYR A CG  1 
ATOM   3830 C  CD1 . TYR A 1 486  ? 43.254 71.609  2.334   1.00 12.08 ? 486  TYR A CD1 1 
ATOM   3831 C  CD2 . TYR A 1 486  ? 41.067 72.526  1.872   1.00 10.96 ? 486  TYR A CD2 1 
ATOM   3832 C  CE1 . TYR A 1 486  ? 42.719 70.798  3.298   1.00 12.34 ? 486  TYR A CE1 1 
ATOM   3833 C  CE2 . TYR A 1 486  ? 40.489 71.690  2.852   1.00 10.44 ? 486  TYR A CE2 1 
ATOM   3834 C  CZ  . TYR A 1 486  ? 41.333 70.831  3.541   1.00 10.90 ? 486  TYR A CZ  1 
ATOM   3835 O  OH  . TYR A 1 486  ? 40.685 69.974  4.420   1.00 9.20  ? 486  TYR A OH  1 
ATOM   3836 N  N   . GLU A 1 487  ? 44.384 75.737  -0.902  1.00 11.21 ? 487  GLU A N   1 
ATOM   3837 C  CA  . GLU A 1 487  ? 44.902 76.308  -2.156  1.00 9.89  ? 487  GLU A CA  1 
ATOM   3838 C  C   . GLU A 1 487  ? 46.348 76.744  -1.998  1.00 11.18 ? 487  GLU A C   1 
ATOM   3839 O  O   . GLU A 1 487  ? 47.186 76.515  -2.886  1.00 10.10 ? 487  GLU A O   1 
ATOM   3840 C  CB  . GLU A 1 487  ? 44.037 77.509  -2.621  1.00 10.38 ? 487  GLU A CB  1 
ATOM   3841 C  CG  . GLU A 1 487  ? 44.481 78.120  -3.946  1.00 13.05 ? 487  GLU A CG  1 
ATOM   3842 C  CD  . GLU A 1 487  ? 43.613 79.301  -4.344  1.00 16.82 ? 487  GLU A CD  1 
ATOM   3843 O  OE1 . GLU A 1 487  ? 42.476 79.432  -3.848  1.00 16.12 ? 487  GLU A OE1 1 
ATOM   3844 O  OE2 . GLU A 1 487  ? 44.103 80.115  -5.184  1.00 21.64 ? 487  GLU A OE2 1 
ATOM   3845 N  N   . GLN A 1 488  ? 46.618 77.405  -0.876  1.00 10.64 ? 488  GLN A N   1 
ATOM   3846 C  CA  . GLN A 1 488  ? 48.010 77.883  -0.678  1.00 13.47 ? 488  GLN A CA  1 
ATOM   3847 C  C   . GLN A 1 488  ? 48.955 76.723  -0.631  1.00 13.31 ? 488  GLN A C   1 
ATOM   3848 O  O   . GLN A 1 488  ? 50.059 76.793  -1.146  1.00 11.20 ? 488  GLN A O   1 
ATOM   3849 C  CB  . GLN A 1 488  ? 48.131 78.602  0.670   1.00 15.60 ? 488  GLN A CB  1 
ATOM   3850 C  CG  . GLN A 1 488  ? 47.484 79.955  0.713   1.00 23.45 ? 488  GLN A CG  1 
ATOM   3851 C  CD  . GLN A 1 488  ? 47.581 80.559  2.155   1.00 28.36 ? 488  GLN A CD  1 
ATOM   3852 O  OE1 . GLN A 1 488  ? 46.989 80.021  3.119   1.00 33.50 ? 488  GLN A OE1 1 
ATOM   3853 N  NE2 . GLN A 1 488  ? 48.333 81.651  2.300   1.00 32.04 ? 488  GLN A NE2 1 
ATOM   3854 N  N   . ARG A 1 489  ? 48.548 75.629  0.029   1.00 12.76 ? 489  ARG A N   1 
ATOM   3855 C  CA  . ARG A 1 489  ? 49.385 74.427  0.091   1.00 8.84  ? 489  ARG A CA  1 
ATOM   3856 C  C   . ARG A 1 489  ? 49.594 73.860  -1.277  1.00 10.60 ? 489  ARG A C   1 
ATOM   3857 O  O   . ARG A 1 489  ? 50.703 73.523  -1.621  1.00 10.64 ? 489  ARG A O   1 
ATOM   3858 C  CB  . ARG A 1 489  ? 48.704 73.391  0.990   1.00 10.77 ? 489  ARG A CB  1 
ATOM   3859 C  CG  . ARG A 1 489  ? 48.805 73.749  2.426   1.00 7.81  ? 489  ARG A CG  1 
ATOM   3860 C  CD  . ARG A 1 489  ? 47.813 72.832  3.241   1.00 11.25 ? 489  ARG A CD  1 
ATOM   3861 N  NE  . ARG A 1 489  ? 47.933 72.969  4.693   1.00 11.44 ? 489  ARG A NE  1 
ATOM   3862 C  CZ  . ARG A 1 489  ? 48.780 72.288  5.480   1.00 16.16 ? 489  ARG A CZ  1 
ATOM   3863 N  NH1 . ARG A 1 489  ? 49.608 71.395  4.974   1.00 14.53 ? 489  ARG A NH1 1 
ATOM   3864 N  NH2 . ARG A 1 489  ? 48.746 72.470  6.813   1.00 14.22 ? 489  ARG A NH2 1 
ATOM   3865 N  N   . MET A 1 490  ? 48.543 73.715  -2.070  1.00 9.45  ? 490  MET A N   1 
ATOM   3866 C  CA  . MET A 1 490  ? 48.757 73.201  -3.382  1.00 9.83  ? 490  MET A CA  1 
ATOM   3867 C  C   . MET A 1 490  ? 49.628 74.128  -4.219  1.00 8.95  ? 490  MET A C   1 
ATOM   3868 O  O   . MET A 1 490  ? 50.328 73.634  -5.085  1.00 10.13 ? 490  MET A O   1 
ATOM   3869 C  CB  . MET A 1 490  ? 47.449 72.938  -4.122  1.00 9.05  ? 490  MET A CB  1 
ATOM   3870 C  CG  . MET A 1 490  ? 46.671 71.789  -3.399  1.00 13.45 ? 490  MET A CG  1 
ATOM   3871 S  SD  . MET A 1 490  ? 45.328 71.049  -4.513  1.00 13.62 ? 490  MET A SD  1 
ATOM   3872 C  CE  . MET A 1 490  ? 43.998 72.255  -4.366  1.00 14.40 ? 490  MET A CE  1 
ATOM   3873 N  N   . GLN A 1 491  ? 49.494 75.449  -4.036  1.00 11.41 ? 491  GLN A N   1 
ATOM   3874 C  CA  . GLN A 1 491  ? 50.364 76.358  -4.793  1.00 12.58 ? 491  GLN A CA  1 
ATOM   3875 C  C   . GLN A 1 491  ? 51.827 76.044  -4.488  1.00 13.37 ? 491  GLN A C   1 
ATOM   3876 O  O   . GLN A 1 491  ? 52.677 75.973  -5.381  1.00 12.50 ? 491  GLN A O   1 
ATOM   3877 C  CB  . GLN A 1 491  ? 50.074 77.814  -4.429  1.00 16.14 ? 491  GLN A CB  1 
ATOM   3878 C  CG  . GLN A 1 491  ? 50.847 78.781  -5.340  1.00 22.81 ? 491  GLN A CG  1 
ATOM   3879 C  CD  . GLN A 1 491  ? 50.548 78.520  -6.823  1.00 26.27 ? 491  GLN A CD  1 
ATOM   3880 O  OE1 . GLN A 1 491  ? 49.387 78.610  -7.243  1.00 31.43 ? 491  GLN A OE1 1 
ATOM   3881 N  NE2 . GLN A 1 491  ? 51.578 78.177  -7.607  1.00 27.70 ? 491  GLN A NE2 1 
ATOM   3882 N  N   . GLU A 1 492  ? 52.128 75.841  -3.222  1.00 11.80 ? 492  GLU A N   1 
ATOM   3883 C  CA  . GLU A 1 492  ? 53.529 75.533  -2.910  1.00 12.75 ? 492  GLU A CA  1 
ATOM   3884 C  C   . GLU A 1 492  ? 53.961 74.182  -3.498  1.00 12.62 ? 492  GLU A C   1 
ATOM   3885 O  O   . GLU A 1 492  ? 55.088 73.973  -3.915  1.00 12.43 ? 492  GLU A O   1 
ATOM   3886 C  CB  . GLU A 1 492  ? 53.662 75.512  -1.415  1.00 13.65 ? 492  GLU A CB  1 
ATOM   3887 C  CG  . GLU A 1 492  ? 53.411 76.885  -0.761  1.00 19.88 ? 492  GLU A CG  1 
ATOM   3888 C  CD  . GLU A 1 492  ? 54.437 77.965  -1.200  1.00 25.18 ? 492  GLU A CD  1 
ATOM   3889 O  OE1 . GLU A 1 492  ? 55.621 77.628  -1.478  1.00 27.13 ? 492  GLU A OE1 1 
ATOM   3890 O  OE2 . GLU A 1 492  ? 54.070 79.159  -1.266  1.00 28.49 ? 492  GLU A OE2 1 
ATOM   3891 N  N   . ALA A 1 493  ? 53.020 73.240  -3.506  1.00 9.73  ? 493  ALA A N   1 
ATOM   3892 C  CA  . ALA A 1 493  ? 53.307 71.950  -4.084  1.00 7.95  ? 493  ALA A CA  1 
ATOM   3893 C  C   . ALA A 1 493  ? 53.659 72.086  -5.583  1.00 10.31 ? 493  ALA A C   1 
ATOM   3894 O  O   . ALA A 1 493  ? 54.585 71.494  -6.043  1.00 9.41  ? 493  ALA A O   1 
ATOM   3895 C  CB  . ALA A 1 493  ? 52.050 71.010  -3.846  1.00 9.23  ? 493  ALA A CB  1 
ATOM   3896 N  N   . LEU A 1 494  ? 52.880 72.856  -6.349  1.00 8.85  ? 494  LEU A N   1 
ATOM   3897 C  CA  . LEU A 1 494  ? 53.207 73.083  -7.742  1.00 10.23 ? 494  LEU A CA  1 
ATOM   3898 C  C   . LEU A 1 494  ? 54.623 73.725  -7.837  1.00 9.68  ? 494  LEU A C   1 
ATOM   3899 O  O   . LEU A 1 494  ? 55.384 73.340  -8.699  1.00 11.35 ? 494  LEU A O   1 
ATOM   3900 C  CB  . LEU A 1 494  ? 52.151 74.010  -8.326  1.00 10.27 ? 494  LEU A CB  1 
ATOM   3901 C  CG  . LEU A 1 494  ? 50.767 73.386  -8.459  1.00 10.94 ? 494  LEU A CG  1 
ATOM   3902 C  CD1 . LEU A 1 494  ? 49.723 74.484  -8.807  1.00 12.39 ? 494  LEU A CD1 1 
ATOM   3903 C  CD2 . LEU A 1 494  ? 50.799 72.381  -9.588  1.00 10.61 ? 494  LEU A CD2 1 
ATOM   3904 N  N   . LYS A 1 495  ? 54.931 74.706  -7.008  1.00 12.49 ? 495  LYS A N   1 
ATOM   3905 C  CA  . LYS A 1 495  ? 56.288 75.314  -7.080  1.00 12.50 ? 495  LYS A CA  1 
ATOM   3906 C  C   . LYS A 1 495  ? 57.398 74.257  -6.807  1.00 13.60 ? 495  LYS A C   1 
ATOM   3907 O  O   . LYS A 1 495  ? 58.466 74.212  -7.443  1.00 12.69 ? 495  LYS A O   1 
ATOM   3908 C  CB  . LYS A 1 495  ? 56.418 76.444  -6.048  1.00 12.25 ? 495  LYS A CB  1 
ATOM   3909 C  CG  . LYS A 1 495  ? 55.565 77.739  -6.205  1.00 16.16 ? 495  LYS A CG  1 
ATOM   3910 C  CD  . LYS A 1 495  ? 56.066 78.867  -5.254  1.00 20.15 ? 495  LYS A CD  1 
ATOM   3911 C  CE  . LYS A 1 495  ? 54.958 79.381  -4.346  1.00 24.22 ? 495  LYS A CE  1 
ATOM   3912 N  NZ  . LYS A 1 495  ? 55.350 80.387  -3.288  1.00 24.40 ? 495  LYS A NZ  1 
ATOM   3913 N  N   . ALA A 1 496  ? 57.107 73.339  -5.905  1.00 11.48 ? 496  ALA A N   1 
ATOM   3914 C  CA  . ALA A 1 496  ? 58.092 72.316  -5.563  1.00 11.92 ? 496  ALA A CA  1 
ATOM   3915 C  C   . ALA A 1 496  ? 58.245 71.379  -6.757  1.00 12.61 ? 496  ALA A C   1 
ATOM   3916 O  O   . ALA A 1 496  ? 59.334 71.012  -7.145  1.00 10.49 ? 496  ALA A O   1 
ATOM   3917 C  CB  . ALA A 1 496  ? 57.621 71.587  -4.256  1.00 12.49 ? 496  ALA A CB  1 
ATOM   3918 N  N   . CYS A 1 497  ? 57.160 70.967  -7.401  1.00 9.33  ? 497  CYS A N   1 
ATOM   3919 C  CA  . CYS A 1 497  ? 57.247 70.136  -8.575  1.00 11.54 ? 497  CYS A CA  1 
ATOM   3920 C  C   . CYS A 1 497  ? 58.058 70.832  -9.699  1.00 9.73  ? 497  CYS A C   1 
ATOM   3921 O  O   . CYS A 1 497  ? 58.875 70.216  -10.348 1.00 10.60 ? 497  CYS A O   1 
ATOM   3922 C  CB  . CYS A 1 497  ? 55.805 69.838  -9.037  1.00 7.50  ? 497  CYS A CB  1 
ATOM   3923 S  SG  . CYS A 1 497  ? 54.905 68.626  -7.985  1.00 10.95 ? 497  CYS A SG  1 
ATOM   3924 N  N   . GLN A 1 498  ? 57.740 72.094  -9.945  1.00 10.51 ? 498  GLN A N   1 
ATOM   3925 C  CA  . GLN A 1 498  ? 58.449 72.841  -10.991 1.00 11.63 ? 498  GLN A CA  1 
ATOM   3926 C  C   . GLN A 1 498  ? 59.935 72.825  -10.756 1.00 11.59 ? 498  GLN A C   1 
ATOM   3927 O  O   . GLN A 1 498  ? 60.690 72.542  -11.707 1.00 10.08 ? 498  GLN A O   1 
ATOM   3928 C  CB  . GLN A 1 498  ? 57.938 74.288  -11.054 1.00 11.98 ? 498  GLN A CB  1 
ATOM   3929 C  CG  . GLN A 1 498  ? 58.738 75.128  -12.099 1.00 17.68 ? 498  GLN A CG  1 
ATOM   3930 C  CD  . GLN A 1 498  ? 58.199 76.554  -12.250 1.00 21.08 ? 498  GLN A CD  1 
ATOM   3931 O  OE1 . GLN A 1 498  ? 57.922 77.013  -13.361 1.00 21.67 ? 498  GLN A OE1 1 
ATOM   3932 N  NE2 . GLN A 1 498  ? 58.071 77.260  -11.129 1.00 23.00 ? 498  GLN A NE2 1 
ATOM   3933 N  N   . MET A 1 499  ? 60.323 73.061  -9.530  1.00 10.87 ? 499  MET A N   1 
ATOM   3934 C  CA  . MET A 1 499  ? 61.763 73.055  -9.197  1.00 11.25 ? 499  MET A CA  1 
ATOM   3935 C  C   . MET A 1 499  ? 62.395 71.715  -9.504  1.00 13.26 ? 499  MET A C   1 
ATOM   3936 O  O   . MET A 1 499  ? 63.406 71.657  -10.190 1.00 12.58 ? 499  MET A O   1 
ATOM   3937 C  CB  . MET A 1 499  ? 61.940 73.395  -7.741  1.00 10.63 ? 499  MET A CB  1 
ATOM   3938 C  CG  . MET A 1 499  ? 63.368 73.215  -7.176  1.00 14.43 ? 499  MET A CG  1 
ATOM   3939 S  SD  . MET A 1 499  ? 64.653 74.138  -8.090  1.00 22.31 ? 499  MET A SD  1 
ATOM   3940 C  CE  . MET A 1 499  ? 64.066 75.690  -7.747  1.00 17.55 ? 499  MET A CE  1 
ATOM   3941 N  N   . VAL A 1 500  ? 61.791 70.611  -9.025  1.00 11.55 ? 500  VAL A N   1 
ATOM   3942 C  CA  . VAL A 1 500  ? 62.337 69.302  -9.322  1.00 10.18 ? 500  VAL A CA  1 
ATOM   3943 C  C   . VAL A 1 500  ? 62.357 69.002  -10.798 1.00 12.09 ? 500  VAL A C   1 
ATOM   3944 O  O   . VAL A 1 500  ? 63.348 68.549  -11.331 1.00 10.87 ? 500  VAL A O   1 
ATOM   3945 C  CB  . VAL A 1 500  ? 61.529 68.189  -8.534  1.00 11.66 ? 500  VAL A CB  1 
ATOM   3946 C  CG1 . VAL A 1 500  ? 62.032 66.803  -8.922  1.00 10.61 ? 500  VAL A CG1 1 
ATOM   3947 C  CG2 . VAL A 1 500  ? 61.606 68.448  -7.048  1.00 11.89 ? 500  VAL A CG2 1 
ATOM   3948 N  N   . MET A 1 501  ? 61.252 69.263  -11.500 1.00 10.97 ? 501  MET A N   1 
ATOM   3949 C  CA  . MET A 1 501  ? 61.192 68.998  -12.958 1.00 12.61 ? 501  MET A CA  1 
ATOM   3950 C  C   . MET A 1 501  ? 62.284 69.757  -13.707 1.00 12.22 ? 501  MET A C   1 
ATOM   3951 O  O   . MET A 1 501  ? 62.963 69.177  -14.522 1.00 11.47 ? 501  MET A O   1 
ATOM   3952 C  CB  . MET A 1 501  ? 59.827 69.412  -13.557 1.00 11.22 ? 501  MET A CB  1 
ATOM   3953 C  CG  . MET A 1 501  ? 58.714 68.562  -12.950 1.00 11.32 ? 501  MET A CG  1 
ATOM   3954 S  SD  . MET A 1 501  ? 57.039 69.116  -13.306 1.00 14.04 ? 501  MET A SD  1 
ATOM   3955 C  CE  . MET A 1 501  ? 56.906 68.774  -14.984 1.00 15.44 ? 501  MET A CE  1 
ATOM   3956 N  N   . GLN A 1 502  ? 62.425 71.043  -13.423 1.00 13.95 ? 502  GLN A N   1 
ATOM   3957 C  CA  . GLN A 1 502  ? 63.387 71.843  -14.209 1.00 14.35 ? 502  GLN A CA  1 
ATOM   3958 C  C   . GLN A 1 502  ? 64.843 71.463  -13.897 1.00 14.38 ? 502  GLN A C   1 
ATOM   3959 O  O   . GLN A 1 502  ? 65.668 71.359  -14.825 1.00 11.34 ? 502  GLN A O   1 
ATOM   3960 C  CB  . GLN A 1 502  ? 63.106 73.335  -14.029 1.00 15.21 ? 502  GLN A CB  1 
ATOM   3961 C  CG  . GLN A 1 502  ? 63.318 73.955  -12.669 1.00 15.57 ? 502  GLN A CG  1 
ATOM   3962 C  CD  . GLN A 1 502  ? 64.751 74.404  -12.465 1.00 18.02 ? 502  GLN A CD  1 
ATOM   3963 O  OE1 . GLN A 1 502  ? 65.537 74.489  -13.472 1.00 16.30 ? 502  GLN A OE1 1 
ATOM   3964 N  NE2 . GLN A 1 502  ? 65.116 74.706  -11.216 1.00 17.40 ? 502  GLN A NE2 1 
ATOM   3965 N  N   . GLN A 1 503  ? 65.145 71.168  -12.641 1.00 12.89 ? 503  GLN A N   1 
ATOM   3966 C  CA  . GLN A 1 503  ? 66.515 70.666  -12.322 1.00 13.13 ? 503  GLN A CA  1 
ATOM   3967 C  C   . GLN A 1 503  ? 66.754 69.335  -13.060 1.00 13.29 ? 503  GLN A C   1 
ATOM   3968 O  O   . GLN A 1 503  ? 67.855 69.085  -13.521 1.00 13.72 ? 503  GLN A O   1 
ATOM   3969 C  CB  . GLN A 1 503  ? 66.688 70.416  -10.799 1.00 13.93 ? 503  GLN A CB  1 
ATOM   3970 C  CG  . GLN A 1 503  ? 66.835 71.668  -9.916  1.00 14.77 ? 503  GLN A CG  1 
ATOM   3971 C  CD  . GLN A 1 503  ? 68.187 72.412  -10.091 1.00 14.72 ? 503  GLN A CD  1 
ATOM   3972 O  OE1 . GLN A 1 503  ? 69.174 71.781  -10.458 1.00 16.88 ? 503  GLN A OE1 1 
ATOM   3973 N  NE2 . GLN A 1 503  ? 68.221 73.730  -9.794  1.00 17.86 ? 503  GLN A NE2 1 
ATOM   3974 N  N   . SER A 1 504  ? 65.743 68.442  -13.159 1.00 11.16 ? 504  SER A N   1 
ATOM   3975 C  CA  . SER A 1 504  ? 65.877 67.152  -13.833 1.00 12.79 ? 504  SER A CA  1 
ATOM   3976 C  C   . SER A 1 504  ? 66.108 67.257  -15.364 1.00 12.77 ? 504  SER A C   1 
ATOM   3977 O  O   . SER A 1 504  ? 66.913 66.511  -15.970 1.00 11.15 ? 504  SER A O   1 
ATOM   3978 C  CB  . SER A 1 504  ? 64.655 66.247  -13.585 1.00 13.44 ? 504  SER A CB  1 
ATOM   3979 O  OG  . SER A 1 504  ? 64.398 66.014  -12.204 1.00 11.07 ? 504  SER A OG  1 
ATOM   3980 N  N   . VAL A 1 505  ? 65.338 68.154  -15.999 1.00 13.18 ? 505  VAL A N   1 
ATOM   3981 C  CA  . VAL A 1 505  ? 65.495 68.392  -17.455 1.00 12.28 ? 505  VAL A CA  1 
ATOM   3982 C  C   . VAL A 1 505  ? 66.941 68.876  -17.736 1.00 11.86 ? 505  VAL A C   1 
ATOM   3983 O  O   . VAL A 1 505  ? 67.595 68.412  -18.681 1.00 12.72 ? 505  VAL A O   1 
ATOM   3984 C  CB  . VAL A 1 505  ? 64.470 69.434  -17.946 1.00 13.37 ? 505  VAL A CB  1 
ATOM   3985 C  CG1 . VAL A 1 505  ? 64.737 69.795  -19.459 1.00 14.31 ? 505  VAL A CG1 1 
ATOM   3986 C  CG2 . VAL A 1 505  ? 63.040 68.828  -17.860 1.00 13.52 ? 505  VAL A CG2 1 
ATOM   3987 N  N   . TYR A 1 506  ? 67.404 69.818  -16.961 1.00 13.92 ? 506  TYR A N   1 
ATOM   3988 C  CA  . TYR A 1 506  ? 68.779 70.309  -17.184 1.00 15.32 ? 506  TYR A CA  1 
ATOM   3989 C  C   . TYR A 1 506  ? 69.813 69.203  -17.041 1.00 16.61 ? 506  TYR A C   1 
ATOM   3990 O  O   . TYR A 1 506  ? 70.762 69.121  -17.802 1.00 16.08 ? 506  TYR A O   1 
ATOM   3991 C  CB  . TYR A 1 506  ? 69.087 71.426  -16.217 1.00 15.66 ? 506  TYR A CB  1 
ATOM   3992 C  CG  . TYR A 1 506  ? 70.493 71.974  -16.310 1.00 19.14 ? 506  TYR A CG  1 
ATOM   3993 C  CD1 . TYR A 1 506  ? 71.009 72.528  -17.511 1.00 21.90 ? 506  TYR A CD1 1 
ATOM   3994 C  CD2 . TYR A 1 506  ? 71.328 71.893  -15.220 1.00 20.78 ? 506  TYR A CD2 1 
ATOM   3995 C  CE1 . TYR A 1 506  ? 72.360 72.966  -17.575 1.00 21.37 ? 506  TYR A CE1 1 
ATOM   3996 C  CE2 . TYR A 1 506  ? 72.656 72.321  -15.277 1.00 23.51 ? 506  TYR A CE2 1 
ATOM   3997 C  CZ  . TYR A 1 506  ? 73.175 72.838  -16.428 1.00 23.42 ? 506  TYR A CZ  1 
ATOM   3998 O  OH  . TYR A 1 506  ? 74.549 73.162  -16.368 1.00 24.25 ? 506  TYR A OH  1 
ATOM   3999 N  N   . ARG A 1 507  ? 69.643 68.323  -16.073 1.00 14.66 ? 507  ARG A N   1 
ATOM   4000 C  CA  . ARG A 1 507  ? 70.590 67.217  -15.912 1.00 12.77 ? 507  ARG A CA  1 
ATOM   4001 C  C   . ARG A 1 507  ? 70.398 66.150  -17.027 1.00 14.46 ? 507  ARG A C   1 
ATOM   4002 O  O   . ARG A 1 507  ? 71.356 65.565  -17.534 1.00 13.75 ? 507  ARG A O   1 
ATOM   4003 C  CB  . ARG A 1 507  ? 70.362 66.591  -14.517 1.00 12.15 ? 507  ARG A CB  1 
ATOM   4004 C  CG  . ARG A 1 507  ? 71.407 65.526  -14.153 1.00 15.16 ? 507  ARG A CG  1 
ATOM   4005 C  CD  . ARG A 1 507  ? 71.189 65.033  -12.727 1.00 14.88 ? 507  ARG A CD  1 
ATOM   4006 N  NE  . ARG A 1 507  ? 72.218 64.048  -12.374 1.00 18.93 ? 507  ARG A NE  1 
ATOM   4007 C  CZ  . ARG A 1 507  ? 72.300 63.428  -11.191 1.00 17.27 ? 507  ARG A CZ  1 
ATOM   4008 N  NH1 . ARG A 1 507  ? 71.432 63.683  -10.226 1.00 20.32 ? 507  ARG A NH1 1 
ATOM   4009 N  NH2 . ARG A 1 507  ? 73.219 62.483  -11.020 1.00 19.75 ? 507  ARG A NH2 1 
ATOM   4010 N  N   . LEU A 1 508  ? 69.151 65.900  -17.450 1.00 10.98 ? 508  LEU A N   1 
ATOM   4011 C  CA  . LEU A 1 508  ? 68.907 64.894  -18.455 1.00 12.12 ? 508  LEU A CA  1 
ATOM   4012 C  C   . LEU A 1 508  ? 69.351 65.310  -19.859 1.00 11.22 ? 508  LEU A C   1 
ATOM   4013 O  O   . LEU A 1 508  ? 69.625 64.462  -20.714 1.00 13.58 ? 508  LEU A O   1 
ATOM   4014 C  CB  . LEU A 1 508  ? 67.427 64.503  -18.436 1.00 11.48 ? 508  LEU A CB  1 
ATOM   4015 C  CG  . LEU A 1 508  ? 66.958 63.635  -17.213 1.00 10.84 ? 508  LEU A CG  1 
ATOM   4016 C  CD1 . LEU A 1 508  ? 65.398 63.684  -17.134 1.00 7.39  ? 508  LEU A CD1 1 
ATOM   4017 C  CD2 . LEU A 1 508  ? 67.376 62.160  -17.387 1.00 11.91 ? 508  LEU A CD2 1 
ATOM   4018 N  N   . LEU A 1 509  ? 69.418 66.641  -20.091 1.00 13.32 ? 509  LEU A N   1 
ATOM   4019 C  CA  . LEU A 1 509  ? 69.775 67.132  -21.429 1.00 14.72 ? 509  LEU A CA  1 
ATOM   4020 C  C   . LEU A 1 509  ? 71.030 67.967  -21.507 1.00 16.16 ? 509  LEU A C   1 
ATOM   4021 O  O   . LEU A 1 509  ? 71.185 68.777  -22.433 1.00 15.11 ? 509  LEU A O   1 
ATOM   4022 C  CB  . LEU A 1 509  ? 68.587 67.916  -22.048 1.00 13.06 ? 509  LEU A CB  1 
ATOM   4023 C  CG  . LEU A 1 509  ? 67.357 67.047  -22.376 1.00 12.39 ? 509  LEU A CG  1 
ATOM   4024 C  CD1 . LEU A 1 509  ? 66.185 68.008  -22.736 1.00 10.63 ? 509  LEU A CD1 1 
ATOM   4025 C  CD2 . LEU A 1 509  ? 67.573 66.065  -23.527 1.00 12.95 ? 509  LEU A CD2 1 
ATOM   4026 N  N   . THR A 1 510  ? 71.938 67.802  -20.560 1.00 14.14 ? 510  THR A N   1 
ATOM   4027 C  CA  . THR A 1 510  ? 73.192 68.579  -20.639 1.00 14.09 ? 510  THR A CA  1 
ATOM   4028 C  C   . THR A 1 510  ? 74.349 67.594  -20.649 1.00 15.96 ? 510  THR A C   1 
ATOM   4029 O  O   . THR A 1 510  ? 74.345 66.609  -19.884 1.00 15.66 ? 510  THR A O   1 
ATOM   4030 C  CB  . THR A 1 510  ? 73.357 69.544  -19.483 1.00 13.33 ? 510  THR A CB  1 
ATOM   4031 O  OG1 . THR A 1 510  ? 72.243 70.489  -19.450 1.00 15.45 ? 510  THR A OG1 1 
ATOM   4032 C  CG2 . THR A 1 510  ? 74.680 70.350  -19.649 1.00 14.58 ? 510  THR A CG2 1 
ATOM   4033 N  N   . LYS A 1 511  ? 75.330 67.840  -21.524 1.00 15.23 ? 511  LYS A N   1 
ATOM   4034 C  CA  . LYS A 1 511  ? 76.500 66.963  -21.667 1.00 17.17 ? 511  LYS A CA  1 
ATOM   4035 C  C   . LYS A 1 511  ? 77.027 66.730  -20.258 1.00 15.44 ? 511  LYS A C   1 
ATOM   4036 O  O   . LYS A 1 511  ? 77.326 67.699  -19.569 1.00 16.64 ? 511  LYS A O   1 
ATOM   4037 C  CB  . LYS A 1 511  ? 77.561 67.663  -22.520 1.00 18.35 ? 511  LYS A CB  1 
ATOM   4038 C  CG  . LYS A 1 511  ? 78.747 66.776  -22.765 1.00 23.92 ? 511  LYS A CG  1 
ATOM   4039 C  CD  . LYS A 1 511  ? 79.807 67.395  -23.642 1.00 26.16 ? 511  LYS A CD  1 
ATOM   4040 C  CE  . LYS A 1 511  ? 80.920 66.367  -23.825 1.00 29.38 ? 511  LYS A CE  1 
ATOM   4041 N  NZ  . LYS A 1 511  ? 82.230 66.937  -24.201 1.00 31.01 ? 511  LYS A NZ  1 
ATOM   4042 N  N   . PRO A 1 512  ? 77.196 65.434  -19.820 1.00 16.28 ? 512  PRO A N   1 
ATOM   4043 C  CA  . PRO A 1 512  ? 77.683 65.204  -18.446 1.00 16.57 ? 512  PRO A CA  1 
ATOM   4044 C  C   . PRO A 1 512  ? 78.920 65.947  -17.972 1.00 15.45 ? 512  PRO A C   1 
ATOM   4045 O  O   . PRO A 1 512  ? 78.938 66.402  -16.832 1.00 17.81 ? 512  PRO A O   1 
ATOM   4046 C  CB  . PRO A 1 512  ? 77.884 63.687  -18.386 1.00 16.84 ? 512  PRO A CB  1 
ATOM   4047 C  CG  . PRO A 1 512  ? 76.828 63.192  -19.278 1.00 17.42 ? 512  PRO A CG  1 
ATOM   4048 C  CD  . PRO A 1 512  ? 76.964 64.149  -20.490 1.00 16.76 ? 512  PRO A CD  1 
ATOM   4049 N  N   . SER A 1 513  ? 79.920 66.111  -18.837 1.00 17.09 ? 513  SER A N   1 
ATOM   4050 C  CA  . SER A 1 513  ? 81.154 66.819  -18.477 1.00 17.60 ? 513  SER A CA  1 
ATOM   4051 C  C   . SER A 1 513  ? 81.016 68.323  -18.394 1.00 18.10 ? 513  SER A C   1 
ATOM   4052 O  O   . SER A 1 513  ? 81.940 69.006  -17.943 1.00 19.01 ? 513  SER A O   1 
ATOM   4053 C  CB  . SER A 1 513  ? 82.294 66.468  -19.446 1.00 16.66 ? 513  SER A CB  1 
ATOM   4054 O  OG  . SER A 1 513  ? 81.919 66.586  -20.788 1.00 20.35 ? 513  SER A OG  1 
ATOM   4055 N  N   . ILE A 1 514  ? 79.864 68.844  -18.832 1.00 18.36 ? 514  ILE A N   1 
ATOM   4056 C  CA  . ILE A 1 514  ? 79.572 70.277  -18.778 1.00 18.98 ? 514  ILE A CA  1 
ATOM   4057 C  C   . ILE A 1 514  ? 78.564 70.552  -17.662 1.00 17.14 ? 514  ILE A C   1 
ATOM   4058 O  O   . ILE A 1 514  ? 78.592 71.582  -17.041 1.00 17.23 ? 514  ILE A O   1 
ATOM   4059 C  CB  . ILE A 1 514  ? 79.008 70.763  -20.140 1.00 22.08 ? 514  ILE A CB  1 
ATOM   4060 C  CG1 . ILE A 1 514  ? 80.115 70.723  -21.205 1.00 23.57 ? 514  ILE A CG1 1 
ATOM   4061 C  CG2 . ILE A 1 514  ? 78.476 72.191  -19.999 1.00 20.84 ? 514  ILE A CG2 1 
ATOM   4062 C  CD1 . ILE A 1 514  ? 79.618 70.742  -22.631 1.00 27.12 ? 514  ILE A CD1 1 
ATOM   4063 N  N   . TYR A 1 515  ? 77.706 69.575  -17.360 1.00 16.44 ? 515  TYR A N   1 
ATOM   4064 C  CA  . TYR A 1 515  ? 76.675 69.777  -16.304 1.00 14.48 ? 515  TYR A CA  1 
ATOM   4065 C  C   . TYR A 1 515  ? 77.235 70.416  -15.021 1.00 14.90 ? 515  TYR A C   1 
ATOM   4066 O  O   . TYR A 1 515  ? 78.113 69.814  -14.389 1.00 15.52 ? 515  TYR A O   1 
ATOM   4067 C  CB  . TYR A 1 515  ? 76.043 68.411  -15.992 1.00 15.90 ? 515  TYR A CB  1 
ATOM   4068 C  CG  . TYR A 1 515  ? 75.005 68.422  -14.914 1.00 16.60 ? 515  TYR A CG  1 
ATOM   4069 C  CD1 . TYR A 1 515  ? 73.801 69.087  -15.077 1.00 14.51 ? 515  TYR A CD1 1 
ATOM   4070 C  CD2 . TYR A 1 515  ? 75.230 67.737  -13.723 1.00 15.76 ? 515  TYR A CD2 1 
ATOM   4071 C  CE1 . TYR A 1 515  ? 72.828 69.068  -14.046 1.00 17.68 ? 515  TYR A CE1 1 
ATOM   4072 C  CE2 . TYR A 1 515  ? 74.279 67.696  -12.715 1.00 17.56 ? 515  TYR A CE2 1 
ATOM   4073 C  CZ  . TYR A 1 515  ? 73.088 68.359  -12.891 1.00 17.09 ? 515  TYR A CZ  1 
ATOM   4074 O  OH  . TYR A 1 515  ? 72.153 68.258  -11.930 1.00 17.42 ? 515  TYR A OH  1 
ATOM   4075 N  N   . SER A 1 516  ? 76.776 71.598  -14.608 1.00 16.36 ? 516  SER A N   1 
ATOM   4076 C  CA  . SER A 1 516  ? 77.302 72.255  -13.395 1.00 16.46 ? 516  SER A CA  1 
ATOM   4077 C  C   . SER A 1 516  ? 76.134 72.929  -12.724 1.00 18.35 ? 516  SER A C   1 
ATOM   4078 O  O   . SER A 1 516  ? 75.940 74.132  -12.903 1.00 19.30 ? 516  SER A O   1 
ATOM   4079 C  CB  . SER A 1 516  ? 78.349 73.352  -13.740 1.00 16.70 ? 516  SER A CB  1 
ATOM   4080 O  OG  . SER A 1 516  ? 78.898 73.948  -12.546 1.00 20.97 ? 516  SER A OG  1 
ATOM   4081 N  N   . PRO A 1 517  ? 75.376 72.178  -11.908 1.00 16.78 ? 517  PRO A N   1 
ATOM   4082 C  CA  . PRO A 1 517  ? 74.204 72.731  -11.240 1.00 19.04 ? 517  PRO A CA  1 
ATOM   4083 C  C   . PRO A 1 517  ? 74.357 73.503  -9.971  1.00 19.81 ? 517  PRO A C   1 
ATOM   4084 O  O   . PRO A 1 517  ? 75.256 73.237  -9.179  1.00 22.47 ? 517  PRO A O   1 
ATOM   4085 C  CB  . PRO A 1 517  ? 73.318 71.500  -11.018 1.00 17.78 ? 517  PRO A CB  1 
ATOM   4086 C  CG  . PRO A 1 517  ? 74.359 70.407  -10.720 1.00 16.33 ? 517  PRO A CG  1 
ATOM   4087 C  CD  . PRO A 1 517  ? 75.483 70.729  -11.692 1.00 16.94 ? 517  PRO A CD  1 
ATOM   4088 N  N   . ASP A 1 518  ? 73.482 74.494  -9.830  1.00 20.72 ? 518  ASP A N   1 
ATOM   4089 C  CA  . ASP A 1 518  ? 73.295 75.284  -8.636  1.00 20.84 ? 518  ASP A CA  1 
ATOM   4090 C  C   . ASP A 1 518  ? 71.852 74.858  -8.318  1.00 21.57 ? 518  ASP A C   1 
ATOM   4091 O  O   . ASP A 1 518  ? 70.920 75.273  -8.990  1.00 20.41 ? 518  ASP A O   1 
ATOM   4092 C  CB  . ASP A 1 518  ? 73.297 76.785  -8.915  1.00 22.62 ? 518  ASP A CB  1 
ATOM   4093 C  CG  . ASP A 1 518  ? 72.899 77.578  -7.700  1.00 23.62 ? 518  ASP A CG  1 
ATOM   4094 O  OD1 . ASP A 1 518  ? 72.086 77.095  -6.882  1.00 26.02 ? 518  ASP A OD1 1 
ATOM   4095 O  OD2 . ASP A 1 518  ? 73.360 78.711  -7.556  1.00 27.69 ? 518  ASP A OD2 1 
ATOM   4096 N  N   . PHE A 1 519  ? 71.686 74.004  -7.318  1.00 22.12 ? 519  PHE A N   1 
ATOM   4097 C  CA  . PHE A 1 519  ? 70.367 73.487  -6.975  1.00 22.51 ? 519  PHE A CA  1 
ATOM   4098 C  C   . PHE A 1 519  ? 69.288 74.483  -6.587  1.00 24.20 ? 519  PHE A C   1 
ATOM   4099 O  O   . PHE A 1 519  ? 68.127 74.115  -6.388  1.00 23.31 ? 519  PHE A O   1 
ATOM   4100 C  CB  . PHE A 1 519  ? 70.540 72.416  -5.889  1.00 21.45 ? 519  PHE A CB  1 
ATOM   4101 C  CG  . PHE A 1 519  ? 71.375 71.281  -6.344  1.00 19.85 ? 519  PHE A CG  1 
ATOM   4102 C  CD1 . PHE A 1 519  ? 71.118 70.687  -7.554  1.00 19.74 ? 519  PHE A CD1 1 
ATOM   4103 C  CD2 . PHE A 1 519  ? 72.434 70.818  -5.589  1.00 20.02 ? 519  PHE A CD2 1 
ATOM   4104 C  CE1 . PHE A 1 519  ? 71.878 69.653  -8.037  1.00 18.89 ? 519  PHE A CE1 1 
ATOM   4105 C  CE2 . PHE A 1 519  ? 73.211 69.763  -6.068  1.00 19.19 ? 519  PHE A CE2 1 
ATOM   4106 C  CZ  . PHE A 1 519  ? 72.935 69.197  -7.273  1.00 20.47 ? 519  PHE A CZ  1 
ATOM   4107 N  N   . SER A 1 520  ? 69.640 75.753  -6.479  1.00 24.95 ? 520  SER A N   1 
ATOM   4108 C  CA  . SER A 1 520  ? 68.658 76.764  -6.122  1.00 27.02 ? 520  SER A CA  1 
ATOM   4109 C  C   . SER A 1 520  ? 68.343 77.643  -7.332  1.00 27.25 ? 520  SER A C   1 
ATOM   4110 O  O   . SER A 1 520  ? 67.500 78.528  -7.260  1.00 28.93 ? 520  SER A O   1 
ATOM   4111 C  CB  . SER A 1 520  ? 69.228 77.658  -5.060  1.00 28.34 ? 520  SER A CB  1 
ATOM   4112 O  OG  . SER A 1 520  ? 70.331 78.367  -5.621  1.00 29.65 ? 520  SER A OG  1 
ATOM   4113 N  N   . PHE A 1 521  ? 69.014 77.394  -8.436  1.00 26.87 ? 521  PHE A N   1 
ATOM   4114 C  CA  . PHE A 1 521  ? 68.810 78.250  -9.599  1.00 26.41 ? 521  PHE A CA  1 
ATOM   4115 C  C   . PHE A 1 521  ? 67.718 77.735  -10.535 1.00 24.82 ? 521  PHE A C   1 
ATOM   4116 O  O   . PHE A 1 521  ? 67.464 76.536  -10.604 1.00 24.69 ? 521  PHE A O   1 
ATOM   4117 C  CB  . PHE A 1 521  ? 70.138 78.376  -10.360 1.00 26.82 ? 521  PHE A CB  1 
ATOM   4118 C  CG  . PHE A 1 521  ? 70.146 79.457  -11.372 1.00 28.50 ? 521  PHE A CG  1 
ATOM   4119 C  CD1 . PHE A 1 521  ? 70.278 80.785  -10.974 1.00 29.52 ? 521  PHE A CD1 1 
ATOM   4120 C  CD2 . PHE A 1 521  ? 69.971 79.164  -12.719 1.00 29.97 ? 521  PHE A CD2 1 
ATOM   4121 C  CE1 . PHE A 1 521  ? 70.227 81.810  -11.905 1.00 31.67 ? 521  PHE A CE1 1 
ATOM   4122 C  CE2 . PHE A 1 521  ? 69.918 80.196  -13.673 1.00 31.26 ? 521  PHE A CE2 1 
ATOM   4123 C  CZ  . PHE A 1 521  ? 70.045 81.516  -13.252 1.00 30.28 ? 521  PHE A CZ  1 
ATOM   4124 N  N   . SER A 1 522  ? 67.076 78.647  -11.257 1.00 24.12 ? 522  SER A N   1 
ATOM   4125 C  CA  . SER A 1 522  ? 66.052 78.234  -12.204 1.00 22.32 ? 522  SER A CA  1 
ATOM   4126 C  C   . SER A 1 522  ? 66.551 78.183  -13.649 1.00 20.09 ? 522  SER A C   1 
ATOM   4127 O  O   . SER A 1 522  ? 66.609 79.225  -14.311 1.00 21.04 ? 522  SER A O   1 
ATOM   4128 C  CB  . SER A 1 522  ? 64.838 79.153  -12.089 1.00 24.59 ? 522  SER A CB  1 
ATOM   4129 O  OG  . SER A 1 522  ? 64.030 78.709  -10.992 1.00 30.76 ? 522  SER A OG  1 
ATOM   4130 N  N   . TYR A 1 523  ? 66.929 76.991  -14.115 1.00 15.79 ? 523  TYR A N   1 
ATOM   4131 C  CA  . TYR A 1 523  ? 67.397 76.773  -15.473 1.00 15.82 ? 523  TYR A CA  1 
ATOM   4132 C  C   . TYR A 1 523  ? 66.271 76.839  -16.474 1.00 16.36 ? 523  TYR A C   1 
ATOM   4133 O  O   . TYR A 1 523  ? 66.494 77.240  -17.610 1.00 15.43 ? 523  TYR A O   1 
ATOM   4134 C  CB  . TYR A 1 523  ? 68.094 75.433  -15.640 1.00 16.15 ? 523  TYR A CB  1 
ATOM   4135 C  CG  . TYR A 1 523  ? 69.358 75.412  -14.849 1.00 19.13 ? 523  TYR A CG  1 
ATOM   4136 C  CD1 . TYR A 1 523  ? 70.538 76.006  -15.340 1.00 15.32 ? 523  TYR A CD1 1 
ATOM   4137 C  CD2 . TYR A 1 523  ? 69.366 74.915  -13.535 1.00 15.88 ? 523  TYR A CD2 1 
ATOM   4138 C  CE1 . TYR A 1 523  ? 71.683 76.104  -14.509 1.00 18.72 ? 523  TYR A CE1 1 
ATOM   4139 C  CE2 . TYR A 1 523  ? 70.482 75.001  -12.751 1.00 19.58 ? 523  TYR A CE2 1 
ATOM   4140 C  CZ  . TYR A 1 523  ? 71.640 75.601  -13.234 1.00 17.11 ? 523  TYR A CZ  1 
ATOM   4141 O  OH  . TYR A 1 523  ? 72.746 75.707  -12.387 1.00 18.94 ? 523  TYR A OH  1 
ATOM   4142 N  N   . PHE A 1 524  ? 65.078 76.395  -16.089 1.00 15.23 ? 524  PHE A N   1 
ATOM   4143 C  CA  . PHE A 1 524  ? 63.912 76.451  -16.961 1.00 15.44 ? 524  PHE A CA  1 
ATOM   4144 C  C   . PHE A 1 524  ? 62.722 76.948  -16.154 1.00 17.03 ? 524  PHE A C   1 
ATOM   4145 O  O   . PHE A 1 524  ? 62.685 76.730  -14.942 1.00 15.37 ? 524  PHE A O   1 
ATOM   4146 C  CB  . PHE A 1 524  ? 63.522 75.056  -17.477 1.00 14.59 ? 524  PHE A CB  1 
ATOM   4147 C  CG  . PHE A 1 524  ? 64.543 74.407  -18.356 1.00 13.71 ? 524  PHE A CG  1 
ATOM   4148 C  CD1 . PHE A 1 524  ? 65.574 73.641  -17.820 1.00 15.28 ? 524  PHE A CD1 1 
ATOM   4149 C  CD2 . PHE A 1 524  ? 64.495 74.564  -19.744 1.00 15.02 ? 524  PHE A CD2 1 
ATOM   4150 C  CE1 . PHE A 1 524  ? 66.555 73.048  -18.688 1.00 14.79 ? 524  PHE A CE1 1 
ATOM   4151 C  CE2 . PHE A 1 524  ? 65.438 73.996  -20.610 1.00 13.02 ? 524  PHE A CE2 1 
ATOM   4152 C  CZ  . PHE A 1 524  ? 66.481 73.233  -20.073 1.00 14.76 ? 524  PHE A CZ  1 
ATOM   4153 N  N   . THR A 1 525  ? 61.754 77.603  -16.814 1.00 16.09 ? 525  THR A N   1 
ATOM   4154 C  CA  . THR A 1 525  ? 60.501 77.959  -16.155 1.00 18.97 ? 525  THR A CA  1 
ATOM   4155 C  C   . THR A 1 525  ? 59.436 77.139  -16.897 1.00 16.48 ? 525  THR A C   1 
ATOM   4156 O  O   . THR A 1 525  ? 59.513 76.887  -18.115 1.00 17.35 ? 525  THR A O   1 
ATOM   4157 C  CB  . THR A 1 525  ? 60.152 79.413  -16.279 1.00 20.95 ? 525  THR A CB  1 
ATOM   4158 O  OG1 . THR A 1 525  ? 59.857 79.673  -17.641 1.00 25.78 ? 525  THR A OG1 1 
ATOM   4159 C  CG2 . THR A 1 525  ? 61.307 80.287  -15.798 1.00 22.19 ? 525  THR A CG2 1 
ATOM   4160 N  N   . LEU A 1 526  ? 58.435 76.663  -16.163 1.00 16.47 ? 526  LEU A N   1 
ATOM   4161 C  CA  . LEU A 1 526  ? 57.398 75.856  -16.838 1.00 15.74 ? 526  LEU A CA  1 
ATOM   4162 C  C   . LEU A 1 526  ? 56.373 76.812  -17.453 1.00 15.85 ? 526  LEU A C   1 
ATOM   4163 O  O   . LEU A 1 526  ? 56.111 77.870  -16.901 1.00 18.68 ? 526  LEU A O   1 
ATOM   4164 C  CB  . LEU A 1 526  ? 56.643 74.958  -15.845 1.00 17.13 ? 526  LEU A CB  1 
ATOM   4165 C  CG  . LEU A 1 526  ? 57.074 73.521  -15.531 1.00 18.95 ? 526  LEU A CG  1 
ATOM   4166 C  CD1 . LEU A 1 526  ? 56.121 73.066  -14.430 1.00 19.58 ? 526  LEU A CD1 1 
ATOM   4167 C  CD2 . LEU A 1 526  ? 56.975 72.560  -16.676 1.00 19.88 ? 526  LEU A CD2 1 
ATOM   4168 N  N   . ASP A 1 527  ? 55.835 76.428  -18.605 1.00 14.33 ? 527  ASP A N   1 
ATOM   4169 C  CA  . ASP A 1 527  ? 54.821 77.234  -19.295 1.00 14.01 ? 527  ASP A CA  1 
ATOM   4170 C  C   . ASP A 1 527  ? 53.577 76.328  -19.381 1.00 13.38 ? 527  ASP A C   1 
ATOM   4171 O  O   . ASP A 1 527  ? 53.660 75.246  -19.866 1.00 15.38 ? 527  ASP A O   1 
ATOM   4172 C  CB  . ASP A 1 527  ? 55.298 77.587  -20.715 1.00 15.49 ? 527  ASP A CB  1 
ATOM   4173 C  CG  . ASP A 1 527  ? 54.246 78.403  -21.488 1.00 16.00 ? 527  ASP A CG  1 
ATOM   4174 O  OD1 . ASP A 1 527  ? 53.943 79.538  -21.051 1.00 18.42 ? 527  ASP A OD1 1 
ATOM   4175 O  OD2 . ASP A 1 527  ? 53.711 77.862  -22.476 1.00 18.86 ? 527  ASP A OD2 1 
ATOM   4176 N  N   . ASP A 1 528  ? 52.448 76.764  -18.849 1.00 14.24 ? 528  ASP A N   1 
ATOM   4177 C  CA  . ASP A 1 528  ? 51.268 75.914  -18.858 1.00 13.19 ? 528  ASP A CA  1 
ATOM   4178 C  C   . ASP A 1 528  ? 50.135 76.746  -19.459 1.00 10.30 ? 528  ASP A C   1 
ATOM   4179 O  O   . ASP A 1 528  ? 49.779 77.792  -18.911 1.00 12.35 ? 528  ASP A O   1 
ATOM   4180 C  CB  . ASP A 1 528  ? 50.974 75.520  -17.388 1.00 13.64 ? 528  ASP A CB  1 
ATOM   4181 C  CG  . ASP A 1 528  ? 49.902 74.448  -17.254 1.00 15.78 ? 528  ASP A CG  1 
ATOM   4182 O  OD1 . ASP A 1 528  ? 48.905 74.514  -17.993 1.00 14.35 ? 528  ASP A OD1 1 
ATOM   4183 O  OD2 . ASP A 1 528  ? 50.065 73.541  -16.356 1.00 15.99 ? 528  ASP A OD2 1 
ATOM   4184 N  N   . SER A 1 529  ? 49.612 76.261  -20.575 1.00 12.01 ? 529  SER A N   1 
ATOM   4185 C  CA  . SER A 1 529  ? 48.534 76.907  -21.340 1.00 12.46 ? 529  SER A CA  1 
ATOM   4186 C  C   . SER A 1 529  ? 47.172 76.880  -20.706 1.00 14.51 ? 529  SER A C   1 
ATOM   4187 O  O   . SER A 1 529  ? 46.341 77.787  -20.963 1.00 14.16 ? 529  SER A O   1 
ATOM   4188 C  CB  . SER A 1 529  ? 48.423 76.223  -22.686 1.00 14.29 ? 529  SER A CB  1 
ATOM   4189 O  OG  . SER A 1 529  ? 49.601 76.515  -23.406 1.00 16.40 ? 529  SER A OG  1 
ATOM   4190 N  N   . ARG A 1 530  ? 46.948 75.901  -19.823 1.00 13.09 ? 530  ARG A N   1 
ATOM   4191 C  CA  . ARG A 1 530  ? 45.613 75.719  -19.267 1.00 13.29 ? 530  ARG A CA  1 
ATOM   4192 C  C   . ARG A 1 530  ? 45.491 75.824  -17.756 1.00 12.51 ? 530  ARG A C   1 
ATOM   4193 O  O   . ARG A 1 530  ? 44.460 75.498  -17.201 1.00 15.96 ? 530  ARG A O   1 
ATOM   4194 C  CB  . ARG A 1 530  ? 45.020 74.389  -19.760 1.00 9.77  ? 530  ARG A CB  1 
ATOM   4195 C  CG  . ARG A 1 530  ? 44.991 74.300  -21.315 1.00 9.97  ? 530  ARG A CG  1 
ATOM   4196 C  CD  . ARG A 1 530  ? 44.370 73.065  -21.902 1.00 11.14 ? 530  ARG A CD  1 
ATOM   4197 N  NE  . ARG A 1 530  ? 45.105 71.849  -21.530 1.00 12.35 ? 530  ARG A NE  1 
ATOM   4198 C  CZ  . ARG A 1 530  ? 44.956 70.678  -22.114 1.00 13.69 ? 530  ARG A CZ  1 
ATOM   4199 N  NH1 . ARG A 1 530  ? 44.088 70.526  -23.106 1.00 15.08 ? 530  ARG A NH1 1 
ATOM   4200 N  NH2 . ARG A 1 530  ? 45.742 69.663  -21.759 1.00 15.55 ? 530  ARG A NH2 1 
ATOM   4201 N  N   . TRP A 1 531  ? 46.500 76.297  -17.064 1.00 12.72 ? 531  TRP A N   1 
ATOM   4202 C  CA  . TRP A 1 531  ? 46.356 76.481  -15.609 1.00 12.73 ? 531  TRP A CA  1 
ATOM   4203 C  C   . TRP A 1 531  ? 47.319 77.571  -15.179 1.00 15.28 ? 531  TRP A C   1 
ATOM   4204 O  O   . TRP A 1 531  ? 48.498 77.473  -15.500 1.00 15.73 ? 531  TRP A O   1 
ATOM   4205 C  CB  . TRP A 1 531  ? 46.694 75.195  -14.832 1.00 14.31 ? 531  TRP A CB  1 
ATOM   4206 C  CG  . TRP A 1 531  ? 46.617 75.494  -13.367 1.00 14.33 ? 531  TRP A CG  1 
ATOM   4207 C  CD1 . TRP A 1 531  ? 47.652 75.917  -12.568 1.00 15.91 ? 531  TRP A CD1 1 
ATOM   4208 C  CD2 . TRP A 1 531  ? 45.437 75.611  -12.577 1.00 16.47 ? 531  TRP A CD2 1 
ATOM   4209 N  NE1 . TRP A 1 531  ? 47.186 76.289  -11.341 1.00 17.42 ? 531  TRP A NE1 1 
ATOM   4210 C  CE2 . TRP A 1 531  ? 45.828 76.110  -11.311 1.00 15.85 ? 531  TRP A CE2 1 
ATOM   4211 C  CE3 . TRP A 1 531  ? 44.102 75.349  -12.813 1.00 16.23 ? 531  TRP A CE3 1 
ATOM   4212 C  CZ2 . TRP A 1 531  ? 44.912 76.347  -10.287 1.00 17.98 ? 531  TRP A CZ2 1 
ATOM   4213 C  CZ3 . TRP A 1 531  ? 43.171 75.583  -11.792 1.00 18.03 ? 531  TRP A CZ3 1 
ATOM   4214 C  CH2 . TRP A 1 531  ? 43.581 76.075  -10.554 1.00 17.97 ? 531  TRP A CH2 1 
ATOM   4215 N  N   . PRO A 1 532  ? 46.846 78.585  -14.417 1.00 16.34 ? 532  PRO A N   1 
ATOM   4216 C  CA  . PRO A 1 532  ? 45.441 78.730  -13.979 1.00 18.61 ? 532  PRO A CA  1 
ATOM   4217 C  C   . PRO A 1 532  ? 44.510 79.040  -15.166 1.00 19.18 ? 532  PRO A C   1 
ATOM   4218 O  O   . PRO A 1 532  ? 43.282 78.959  -15.052 1.00 19.05 ? 532  PRO A O   1 
ATOM   4219 C  CB  . PRO A 1 532  ? 45.504 79.899  -12.998 1.00 18.63 ? 532  PRO A CB  1 
ATOM   4220 C  CG  . PRO A 1 532  ? 46.905 79.825  -12.420 1.00 19.14 ? 532  PRO A CG  1 
ATOM   4221 C  CD  . PRO A 1 532  ? 47.701 79.556  -13.701 1.00 17.61 ? 532  PRO A CD  1 
ATOM   4222 N  N   . GLY A 1 533  ? 45.117 79.357  -16.307 1.00 21.21 ? 533  GLY A N   1 
ATOM   4223 C  CA  . GLY A 1 533  ? 44.365 79.638  -17.519 1.00 23.78 ? 533  GLY A CA  1 
ATOM   4224 C  C   . GLY A 1 533  ? 44.195 81.114  -17.829 1.00 25.96 ? 533  GLY A C   1 
ATOM   4225 O  O   . GLY A 1 533  ? 44.216 81.976  -16.939 1.00 26.05 ? 533  GLY A O   1 
ATOM   4226 N  N   . SER A 1 534  ? 44.026 81.394  -19.117 1.00 29.32 ? 534  SER A N   1 
ATOM   4227 C  CA  . SER A 1 534  ? 43.842 82.759  -19.632 1.00 31.88 ? 534  SER A CA  1 
ATOM   4228 C  C   . SER A 1 534  ? 42.564 83.316  -19.029 1.00 32.68 ? 534  SER A C   1 
ATOM   4229 O  O   . SER A 1 534  ? 41.526 82.655  -19.078 1.00 33.61 ? 534  SER A O   1 
ATOM   4230 C  CB  . SER A 1 534  ? 43.741 82.730  -21.169 1.00 33.62 ? 534  SER A CB  1 
ATOM   4231 O  OG  . SER A 1 534  ? 43.455 84.023  -21.727 1.00 37.48 ? 534  SER A OG  1 
ATOM   4232 N  N   . GLY A 1 535  ? 42.626 84.521  -18.467 1.00 33.64 ? 535  GLY A N   1 
ATOM   4233 C  CA  . GLY A 1 535  ? 41.436 85.099  -17.859 1.00 33.78 ? 535  GLY A CA  1 
ATOM   4234 C  C   . GLY A 1 535  ? 41.295 84.736  -16.385 1.00 34.97 ? 535  GLY A C   1 
ATOM   4235 O  O   . GLY A 1 535  ? 40.453 85.295  -15.647 1.00 34.36 ? 535  GLY A O   1 
ATOM   4236 N  N   . VAL A 1 536  ? 42.108 83.775  -15.947 1.00 35.43 ? 536  VAL A N   1 
ATOM   4237 C  CA  . VAL A 1 536  ? 42.103 83.367  -14.555 1.00 35.88 ? 536  VAL A CA  1 
ATOM   4238 C  C   . VAL A 1 536  ? 43.290 84.093  -13.933 1.00 37.24 ? 536  VAL A C   1 
ATOM   4239 O  O   . VAL A 1 536  ? 43.157 84.833  -12.950 1.00 37.04 ? 536  VAL A O   1 
ATOM   4240 C  CB  . VAL A 1 536  ? 42.249 81.828  -14.416 1.00 36.07 ? 536  VAL A CB  1 
ATOM   4241 C  CG1 . VAL A 1 536  ? 42.231 81.421  -12.961 1.00 34.38 ? 536  VAL A CG1 1 
ATOM   4242 C  CG2 . VAL A 1 536  ? 41.091 81.150  -15.113 1.00 34.99 ? 536  VAL A CG2 1 
ATOM   4243 N  N   . GLU A 1 537  ? 44.450 83.941  -14.550 1.00 37.97 ? 537  GLU A N   1 
ATOM   4244 C  CA  . GLU A 1 537  ? 45.630 84.604  -14.038 1.00 39.85 ? 537  GLU A CA  1 
ATOM   4245 C  C   . GLU A 1 537  ? 46.617 84.812  -15.192 1.00 40.21 ? 537  GLU A C   1 
ATOM   4246 O  O   . GLU A 1 537  ? 46.866 83.887  -15.972 1.00 40.41 ? 537  GLU A O   1 
ATOM   4247 C  CB  . GLU A 1 537  ? 46.203 83.725  -12.912 1.00 40.92 ? 537  GLU A CB  1 
ATOM   4248 C  CG  . GLU A 1 537  ? 47.588 84.065  -12.368 1.00 43.20 ? 537  GLU A CG  1 
ATOM   4249 C  CD  . GLU A 1 537  ? 47.922 83.207  -11.140 1.00 44.59 ? 537  GLU A CD  1 
ATOM   4250 O  OE1 . GLU A 1 537  ? 46.969 82.875  -10.390 1.00 45.77 ? 537  GLU A OE1 1 
ATOM   4251 O  OE2 . GLU A 1 537  ? 49.116 82.870  -10.927 1.00 44.66 ? 537  GLU A OE2 1 
ATOM   4252 N  N   . ASP A 1 538  ? 47.130 86.035  -15.360 1.00 40.69 ? 538  ASP A N   1 
ATOM   4253 C  CA  . ASP A 1 538  ? 48.115 86.218  -16.428 1.00 41.00 ? 538  ASP A CA  1 
ATOM   4254 C  C   . ASP A 1 538  ? 49.457 85.871  -15.793 1.00 39.17 ? 538  ASP A C   1 
ATOM   4255 O  O   . ASP A 1 538  ? 50.177 86.733  -15.261 1.00 39.65 ? 538  ASP A O   1 
ATOM   4256 C  CB  . ASP A 1 538  ? 48.139 87.643  -16.981 1.00 43.28 ? 538  ASP A CB  1 
ATOM   4257 C  CG  . ASP A 1 538  ? 49.058 87.761  -18.188 1.00 45.41 ? 538  ASP A CG  1 
ATOM   4258 O  OD1 . ASP A 1 538  ? 50.296 87.547  -18.024 1.00 45.89 ? 538  ASP A OD1 1 
ATOM   4259 O  OD2 . ASP A 1 538  ? 48.542 88.049  -19.299 1.00 46.95 ? 538  ASP A OD2 1 
ATOM   4260 N  N   . SER A 1 539  ? 49.784 84.589  -15.849 1.00 36.41 ? 539  SER A N   1 
ATOM   4261 C  CA  . SER A 1 539  ? 51.003 84.089  -15.217 1.00 33.86 ? 539  SER A CA  1 
ATOM   4262 C  C   . SER A 1 539  ? 52.091 83.636  -16.188 1.00 31.11 ? 539  SER A C   1 
ATOM   4263 O  O   . SER A 1 539  ? 53.241 83.466  -15.784 1.00 31.00 ? 539  SER A O   1 
ATOM   4264 C  CB  . SER A 1 539  ? 50.636 82.912  -14.309 1.00 33.34 ? 539  SER A CB  1 
ATOM   4265 O  OG  . SER A 1 539  ? 50.175 81.845  -15.117 1.00 35.44 ? 539  SER A OG  1 
ATOM   4266 N  N   . ARG A 1 540  ? 51.717 83.453  -17.451 1.00 29.10 ? 540  ARG A N   1 
ATOM   4267 C  CA  . ARG A 1 540  ? 52.627 82.977  -18.505 1.00 27.02 ? 540  ARG A CA  1 
ATOM   4268 C  C   . ARG A 1 540  ? 53.680 83.980  -18.948 1.00 26.51 ? 540  ARG A C   1 
ATOM   4269 O  O   . ARG A 1 540  ? 53.359 85.137  -19.233 1.00 26.84 ? 540  ARG A O   1 
ATOM   4270 C  CB  . ARG A 1 540  ? 51.834 82.581  -19.731 1.00 24.55 ? 540  ARG A CB  1 
ATOM   4271 C  CG  . ARG A 1 540  ? 51.035 81.314  -19.547 1.00 22.84 ? 540  ARG A CG  1 
ATOM   4272 C  CD  . ARG A 1 540  ? 50.305 80.856  -20.834 1.00 19.01 ? 540  ARG A CD  1 
ATOM   4273 N  NE  . ARG A 1 540  ? 51.160 80.222  -21.859 1.00 16.99 ? 540  ARG A NE  1 
ATOM   4274 C  CZ  . ARG A 1 540  ? 50.748 79.754  -23.050 1.00 16.52 ? 540  ARG A CZ  1 
ATOM   4275 N  NH1 . ARG A 1 540  ? 49.468 79.808  -23.474 1.00 16.52 ? 540  ARG A NH1 1 
ATOM   4276 N  NH2 . ARG A 1 540  ? 51.644 79.232  -23.872 1.00 14.95 ? 540  ARG A NH2 1 
ATOM   4277 N  N   . THR A 1 541  ? 54.921 83.527  -19.031 1.00 25.17 ? 541  THR A N   1 
ATOM   4278 C  CA  . THR A 1 541  ? 55.981 84.420  -19.475 1.00 24.90 ? 541  THR A CA  1 
ATOM   4279 C  C   . THR A 1 541  ? 56.027 84.451  -20.990 1.00 23.70 ? 541  THR A C   1 
ATOM   4280 O  O   . THR A 1 541  ? 55.613 83.503  -21.666 1.00 24.18 ? 541  THR A O   1 
ATOM   4281 C  CB  . THR A 1 541  ? 57.342 83.978  -18.954 1.00 25.27 ? 541  THR A CB  1 
ATOM   4282 O  OG1 . THR A 1 541  ? 57.709 82.775  -19.607 1.00 27.17 ? 541  THR A OG1 1 
ATOM   4283 C  CG2 . THR A 1 541  ? 57.280 83.704  -17.423 1.00 26.87 ? 541  THR A CG2 1 
ATOM   4284 N  N   . THR A 1 542  ? 56.458 85.587  -21.521 1.00 21.37 ? 542  THR A N   1 
ATOM   4285 C  CA  . THR A 1 542  ? 56.590 85.741  -22.964 1.00 18.35 ? 542  THR A CA  1 
ATOM   4286 C  C   . THR A 1 542  ? 58.055 85.518  -23.296 1.00 15.08 ? 542  THR A C   1 
ATOM   4287 O  O   . THR A 1 542  ? 58.909 86.049  -22.625 1.00 17.45 ? 542  THR A O   1 
ATOM   4288 C  CB  . THR A 1 542  ? 56.225 87.199  -23.398 1.00 19.24 ? 542  THR A CB  1 
ATOM   4289 O  OG1 . THR A 1 542  ? 54.837 87.418  -23.119 1.00 20.26 ? 542  THR A OG1 1 
ATOM   4290 C  CG2 . THR A 1 542  ? 56.482 87.426  -24.902 1.00 17.64 ? 542  THR A CG2 1 
ATOM   4291 N  N   . ILE A 1 543  ? 58.332 84.712  -24.301 1.00 13.72 ? 543  ILE A N   1 
ATOM   4292 C  CA  . ILE A 1 543  ? 59.717 84.527  -24.733 1.00 12.44 ? 543  ILE A CA  1 
ATOM   4293 C  C   . ILE A 1 543  ? 60.052 85.811  -25.542 1.00 13.94 ? 543  ILE A C   1 
ATOM   4294 O  O   . ILE A 1 543  ? 59.443 86.071  -26.583 1.00 14.05 ? 543  ILE A O   1 
ATOM   4295 C  CB  . ILE A 1 543  ? 59.834 83.279  -25.597 1.00 13.07 ? 543  ILE A CB  1 
ATOM   4296 C  CG1 . ILE A 1 543  ? 59.500 82.026  -24.739 1.00 13.47 ? 543  ILE A CG1 1 
ATOM   4297 C  CG2 . ILE A 1 543  ? 61.292 83.187  -26.189 1.00 13.63 ? 543  ILE A CG2 1 
ATOM   4298 C  CD1 . ILE A 1 543  ? 59.305 80.782  -25.575 1.00 15.34 ? 543  ILE A CD1 1 
ATOM   4299 N  N   . ILE A 1 544  ? 61.029 86.545  -25.056 1.00 13.82 ? 544  ILE A N   1 
ATOM   4300 C  CA  . ILE A 1 544  ? 61.398 87.825  -25.665 1.00 15.20 ? 544  ILE A CA  1 
ATOM   4301 C  C   . ILE A 1 544  ? 62.611 87.664  -26.555 1.00 16.18 ? 544  ILE A C   1 
ATOM   4302 O  O   . ILE A 1 544  ? 63.718 87.361  -26.073 1.00 18.38 ? 544  ILE A O   1 
ATOM   4303 C  CB  . ILE A 1 544  ? 61.699 88.825  -24.566 1.00 16.19 ? 544  ILE A CB  1 
ATOM   4304 C  CG1 . ILE A 1 544  ? 60.428 89.036  -23.732 1.00 18.96 ? 544  ILE A CG1 1 
ATOM   4305 C  CG2 . ILE A 1 544  ? 62.195 90.146  -25.168 1.00 17.77 ? 544  ILE A CG2 1 
ATOM   4306 C  CD1 . ILE A 1 544  ? 60.633 90.001  -22.591 1.00 20.93 ? 544  ILE A CD1 1 
ATOM   4307 N  N   . LEU A 1 545  ? 62.399 87.863  -27.852 1.00 15.89 ? 545  LEU A N   1 
ATOM   4308 C  CA  . LEU A 1 545  ? 63.436 87.692  -28.861 1.00 15.85 ? 545  LEU A CA  1 
ATOM   4309 C  C   . LEU A 1 545  ? 63.606 89.014  -29.558 1.00 15.86 ? 545  LEU A C   1 
ATOM   4310 O  O   . LEU A 1 545  ? 62.747 89.873  -29.504 1.00 17.62 ? 545  LEU A O   1 
ATOM   4311 C  CB  . LEU A 1 545  ? 63.027 86.618  -29.873 1.00 15.61 ? 545  LEU A CB  1 
ATOM   4312 C  CG  . LEU A 1 545  ? 62.741 85.188  -29.341 1.00 16.46 ? 545  LEU A CG  1 
ATOM   4313 C  CD1 . LEU A 1 545  ? 62.155 84.332  -30.413 1.00 16.97 ? 545  LEU A CD1 1 
ATOM   4314 C  CD2 . LEU A 1 545  ? 64.059 84.565  -28.783 1.00 15.23 ? 545  LEU A CD2 1 
ATOM   4315 N  N   . GLY A 1 546  ? 64.744 89.190  -30.188 1.00 14.68 ? 546  GLY A N   1 
ATOM   4316 C  CA  . GLY A 1 546  ? 64.915 90.423  -30.924 1.00 14.40 ? 546  GLY A CA  1 
ATOM   4317 C  C   . GLY A 1 546  ? 66.281 90.433  -31.527 1.00 14.47 ? 546  GLY A C   1 
ATOM   4318 O  O   . GLY A 1 546  ? 67.222 89.905  -30.988 1.00 12.32 ? 546  GLY A O   1 
ATOM   4319 N  N   . GLU A 1 547  ? 66.387 91.028  -32.692 1.00 15.39 ? 547  GLU A N   1 
ATOM   4320 C  CA  . GLU A 1 547  ? 67.679 91.075  -33.343 1.00 18.48 ? 547  GLU A CA  1 
ATOM   4321 C  C   . GLU A 1 547  ? 68.781 91.730  -32.520 1.00 19.63 ? 547  GLU A C   1 
ATOM   4322 O  O   . GLU A 1 547  ? 69.962 91.368  -32.627 1.00 20.19 ? 547  GLU A O   1 
ATOM   4323 C  CB  . GLU A 1 547  ? 67.501 91.798  -34.667 1.00 21.19 ? 547  GLU A CB  1 
ATOM   4324 C  CG  . GLU A 1 547  ? 66.495 91.109  -35.620 1.00 26.60 ? 547  GLU A CG  1 
ATOM   4325 C  CD  . GLU A 1 547  ? 64.985 91.200  -35.253 1.00 30.13 ? 547  GLU A CD  1 
ATOM   4326 O  OE1 . GLU A 1 547  ? 64.512 91.965  -34.345 1.00 26.54 ? 547  GLU A OE1 1 
ATOM   4327 O  OE2 . GLU A 1 547  ? 64.225 90.473  -35.956 1.00 34.20 ? 547  GLU A OE2 1 
ATOM   4328 N  N   . ASP A 1 548  ? 68.384 92.689  -31.681 1.00 20.29 ? 548  ASP A N   1 
ATOM   4329 C  CA  . ASP A 1 548  ? 69.302 93.446  -30.815 1.00 22.13 ? 548  ASP A CA  1 
ATOM   4330 C  C   . ASP A 1 548  ? 69.294 92.930  -29.385 1.00 22.59 ? 548  ASP A C   1 
ATOM   4331 O  O   . ASP A 1 548  ? 69.662 93.661  -28.437 1.00 24.99 ? 548  ASP A O   1 
ATOM   4332 C  CB  . ASP A 1 548  ? 68.842 94.908  -30.762 1.00 22.22 ? 548  ASP A CB  1 
ATOM   4333 C  CG  . ASP A 1 548  ? 69.106 95.640  -32.038 1.00 22.63 ? 548  ASP A CG  1 
ATOM   4334 O  OD1 . ASP A 1 548  ? 70.308 95.721  -32.386 1.00 25.56 ? 548  ASP A OD1 1 
ATOM   4335 O  OD2 . ASP A 1 548  ? 68.147 96.113  -32.680 1.00 24.47 ? 548  ASP A OD2 1 
ATOM   4336 N  N   . ILE A 1 549  ? 68.858 91.698  -29.163 1.00 21.47 ? 549  ILE A N   1 
ATOM   4337 C  CA  . ILE A 1 549  ? 68.837 91.231  -27.773 1.00 21.50 ? 549  ILE A CA  1 
ATOM   4338 C  C   . ILE A 1 549  ? 69.064 89.719  -27.634 1.00 21.90 ? 549  ILE A C   1 
ATOM   4339 O  O   . ILE A 1 549  ? 69.931 89.290  -26.909 1.00 23.97 ? 549  ILE A O   1 
ATOM   4340 C  CB  . ILE A 1 549  ? 67.501 91.644  -27.004 1.00 22.58 ? 549  ILE A CB  1 
ATOM   4341 C  CG1 . ILE A 1 549  ? 67.526 91.061  -25.569 1.00 24.20 ? 549  ILE A CG1 1 
ATOM   4342 C  CG2 . ILE A 1 549  ? 66.236 91.117  -27.693 1.00 21.20 ? 549  ILE A CG2 1 
ATOM   4343 C  CD1 . ILE A 1 549  ? 67.811 92.066  -24.473 1.00 25.36 ? 549  ILE A CD1 1 
ATOM   4344 N  N   . LEU A 1 550  ? 68.304 88.918  -28.356 1.00 21.25 ? 550  LEU A N   1 
ATOM   4345 C  CA  . LEU A 1 550  ? 68.464 87.486  -28.224 1.00 19.35 ? 550  LEU A CA  1 
ATOM   4346 C  C   . LEU A 1 550  ? 67.741 86.985  -29.437 1.00 17.95 ? 550  LEU A C   1 
ATOM   4347 O  O   . LEU A 1 550  ? 66.538 87.187  -29.594 1.00 18.68 ? 550  LEU A O   1 
ATOM   4348 C  CB  . LEU A 1 550  ? 67.809 86.993  -26.895 1.00 20.46 ? 550  LEU A CB  1 
ATOM   4349 C  CG  . LEU A 1 550  ? 67.865 85.479  -26.627 1.00 20.41 ? 550  LEU A CG  1 
ATOM   4350 C  CD1 . LEU A 1 550  ? 69.307 85.033  -26.411 1.00 17.94 ? 550  LEU A CD1 1 
ATOM   4351 C  CD2 . LEU A 1 550  ? 66.981 85.108  -25.413 1.00 17.93 ? 550  LEU A CD2 1 
ATOM   4352 N  N   . PRO A 1 551  ? 68.466 86.324  -30.333 1.00 15.73 ? 551  PRO A N   1 
ATOM   4353 C  CA  . PRO A 1 551  ? 67.791 85.838  -31.532 1.00 15.03 ? 551  PRO A CA  1 
ATOM   4354 C  C   . PRO A 1 551  ? 67.010 84.522  -31.405 1.00 15.44 ? 551  PRO A C   1 
ATOM   4355 O  O   . PRO A 1 551  ? 66.140 84.214  -32.252 1.00 15.28 ? 551  PRO A O   1 
ATOM   4356 C  CB  . PRO A 1 551  ? 68.918 85.754  -32.560 1.00 18.24 ? 551  PRO A CB  1 
ATOM   4357 C  CG  . PRO A 1 551  ? 70.142 85.655  -31.807 1.00 18.82 ? 551  PRO A CG  1 
ATOM   4358 C  CD  . PRO A 1 551  ? 69.935 86.367  -30.506 1.00 17.33 ? 551  PRO A CD  1 
ATOM   4359 N  N   . SER A 1 552  ? 67.343 83.703  -30.409 1.00 14.52 ? 552  SER A N   1 
ATOM   4360 C  CA  . SER A 1 552  ? 66.614 82.452  -30.342 1.00 15.03 ? 552  SER A CA  1 
ATOM   4361 C  C   . SER A 1 552  ? 66.479 81.919  -28.917 1.00 12.94 ? 552  SER A C   1 
ATOM   4362 O  O   . SER A 1 552  ? 67.149 82.399  -28.008 1.00 13.05 ? 552  SER A O   1 
ATOM   4363 C  CB  . SER A 1 552  ? 67.283 81.413  -31.224 1.00 13.38 ? 552  SER A CB  1 
ATOM   4364 O  OG  . SER A 1 552  ? 68.438 80.840  -30.678 1.00 16.88 ? 552  SER A OG  1 
ATOM   4365 N  N   . LYS A 1 553  ? 65.613 80.910  -28.753 1.00 13.23 ? 553  LYS A N   1 
ATOM   4366 C  CA  . LYS A 1 553  ? 65.364 80.328  -27.440 1.00 12.71 ? 553  LYS A CA  1 
ATOM   4367 C  C   . LYS A 1 553  ? 65.070 78.832  -27.502 1.00 11.20 ? 553  LYS A C   1 
ATOM   4368 O  O   . LYS A 1 553  ? 64.324 78.352  -28.371 1.00 11.84 ? 553  LYS A O   1 
ATOM   4369 C  CB  . LYS A 1 553  ? 64.164 81.046  -26.803 1.00 14.29 ? 553  LYS A CB  1 
ATOM   4370 C  CG  . LYS A 1 553  ? 63.632 80.333  -25.542 1.00 14.19 ? 553  LYS A CG  1 
ATOM   4371 C  CD  . LYS A 1 553  ? 64.642 80.445  -24.442 1.00 14.99 ? 553  LYS A CD  1 
ATOM   4372 C  CE  . LYS A 1 553  ? 64.710 81.899  -23.873 1.00 14.80 ? 553  LYS A CE  1 
ATOM   4373 N  NZ  . LYS A 1 553  ? 65.937 82.163  -23.057 1.00 17.30 ? 553  LYS A NZ  1 
ATOM   4374 N  N   . HIS A 1 554  ? 65.733 78.094  -26.620 1.00 11.56 ? 554  HIS A N   1 
ATOM   4375 C  CA  . HIS A 1 554  ? 65.507 76.647  -26.517 1.00 11.42 ? 554  HIS A CA  1 
ATOM   4376 C  C   . HIS A 1 554  ? 64.306 76.363  -25.604 1.00 11.94 ? 554  HIS A C   1 
ATOM   4377 O  O   . HIS A 1 554  ? 64.169 76.994  -24.562 1.00 13.13 ? 554  HIS A O   1 
ATOM   4378 C  CB  . HIS A 1 554  ? 66.735 75.931  -25.926 1.00 13.88 ? 554  HIS A CB  1 
ATOM   4379 C  CG  . HIS A 1 554  ? 67.828 75.677  -26.911 1.00 16.32 ? 554  HIS A CG  1 
ATOM   4380 N  ND1 . HIS A 1 554  ? 68.493 76.702  -27.554 1.00 18.71 ? 554  HIS A ND1 1 
ATOM   4381 C  CD2 . HIS A 1 554  ? 68.425 74.522  -27.307 1.00 19.14 ? 554  HIS A CD2 1 
ATOM   4382 C  CE1 . HIS A 1 554  ? 69.469 76.188  -28.284 1.00 18.96 ? 554  HIS A CE1 1 
ATOM   4383 N  NE2 . HIS A 1 554  ? 69.452 74.869  -28.150 1.00 15.65 ? 554  HIS A NE2 1 
ATOM   4384 N  N   . VAL A 1 555  ? 63.468 75.424  -26.061 1.00 10.10 ? 555  VAL A N   1 
ATOM   4385 C  CA  . VAL A 1 555  ? 62.320 74.959  -25.296 1.00 10.86 ? 555  VAL A CA  1 
ATOM   4386 C  C   . VAL A 1 555  ? 62.393 73.433  -25.266 1.00 10.36 ? 555  VAL A C   1 
ATOM   4387 O  O   . VAL A 1 555  ? 62.889 72.810  -26.188 1.00 10.70 ? 555  VAL A O   1 
ATOM   4388 C  CB  . VAL A 1 555  ? 60.937 75.446  -25.878 1.00 9.62  ? 555  VAL A CB  1 
ATOM   4389 C  CG1 . VAL A 1 555  ? 60.880 76.967  -25.759 1.00 13.38 ? 555  VAL A CG1 1 
ATOM   4390 C  CG2 . VAL A 1 555  ? 60.693 74.955  -27.277 1.00 11.34 ? 555  VAL A CG2 1 
ATOM   4391 N  N   . VAL A 1 556  ? 61.775 72.811  -24.259 1.00 10.86 ? 556  VAL A N   1 
ATOM   4392 C  CA  . VAL A 1 556  ? 61.844 71.358  -24.115 1.00 10.45 ? 556  VAL A CA  1 
ATOM   4393 C  C   . VAL A 1 556  ? 60.453 70.834  -23.667 1.00 9.24  ? 556  VAL A C   1 
ATOM   4394 O  O   . VAL A 1 556  ? 59.824 71.447  -22.770 1.00 10.50 ? 556  VAL A O   1 
ATOM   4395 C  CB  . VAL A 1 556  ? 62.860 70.952  -22.982 1.00 10.56 ? 556  VAL A CB  1 
ATOM   4396 C  CG1 . VAL A 1 556  ? 62.814 69.406  -22.751 1.00 11.44 ? 556  VAL A CG1 1 
ATOM   4397 C  CG2 . VAL A 1 556  ? 64.342 71.363  -23.315 1.00 11.38 ? 556  VAL A CG2 1 
ATOM   4398 N  N   . MET A 1 557  ? 60.038 69.757  -24.282 1.00 8.59  ? 557  MET A N   1 
ATOM   4399 C  CA  . MET A 1 557  ? 58.771 69.107  -23.919 1.00 10.67 ? 557  MET A CA  1 
ATOM   4400 C  C   . MET A 1 557  ? 59.067 67.737  -23.301 1.00 11.02 ? 557  MET A C   1 
ATOM   4401 O  O   . MET A 1 557  ? 59.940 66.990  -23.762 1.00 9.69  ? 557  MET A O   1 
ATOM   4402 C  CB  . MET A 1 557  ? 57.857 68.877  -25.133 1.00 11.97 ? 557  MET A CB  1 
ATOM   4403 C  CG  . MET A 1 557  ? 56.824 69.998  -25.455 1.00 11.13 ? 557  MET A CG  1 
ATOM   4404 S  SD  . MET A 1 557  ? 57.555 71.624  -25.644 1.00 11.37 ? 557  MET A SD  1 
ATOM   4405 C  CE  . MET A 1 557  ? 58.678 71.532  -26.951 1.00 13.01 ? 557  MET A CE  1 
ATOM   4406 N  N   . HIS A 1 558  ? 58.262 67.400  -22.300 1.00 10.51 ? 558  HIS A N   1 
ATOM   4407 C  CA  . HIS A 1 558  ? 58.364 66.119  -21.634 1.00 10.62 ? 558  HIS A CA  1 
ATOM   4408 C  C   . HIS A 1 558  ? 57.081 65.381  -21.878 1.00 8.79  ? 558  HIS A C   1 
ATOM   4409 O  O   . HIS A 1 558  ? 56.004 65.972  -21.832 1.00 9.71  ? 558  HIS A O   1 
ATOM   4410 C  CB  . HIS A 1 558  ? 58.488 66.353  -20.137 1.00 9.28  ? 558  HIS A CB  1 
ATOM   4411 C  CG  . HIS A 1 558  ? 58.432 65.097  -19.323 1.00 9.82  ? 558  HIS A CG  1 
ATOM   4412 N  ND1 . HIS A 1 558  ? 57.506 64.910  -18.297 1.00 10.70 ? 558  HIS A ND1 1 
ATOM   4413 C  CD2 . HIS A 1 558  ? 59.189 63.976  -19.371 1.00 9.09  ? 558  HIS A CD2 1 
ATOM   4414 C  CE1 . HIS A 1 558  ? 57.699 63.705  -17.774 1.00 9.71  ? 558  HIS A CE1 1 
ATOM   4415 N  NE2 . HIS A 1 558  ? 58.706 63.117  -18.406 1.00 11.09 ? 558  HIS A NE2 1 
ATOM   4416 N  N   . ASN A 1 559  ? 57.179 64.092  -22.046 1.00 9.09  ? 559  ASN A N   1 
ATOM   4417 C  CA  . ASN A 1 559  ? 56.028 63.243  -22.269 1.00 9.05  ? 559  ASN A CA  1 
ATOM   4418 C  C   . ASN A 1 559  ? 56.046 62.166  -21.195 1.00 8.16  ? 559  ASN A C   1 
ATOM   4419 O  O   . ASN A 1 559  ? 56.763 61.208  -21.324 1.00 8.05  ? 559  ASN A O   1 
ATOM   4420 C  CB  . ASN A 1 559  ? 56.115 62.618  -23.655 1.00 9.31  ? 559  ASN A CB  1 
ATOM   4421 C  CG  . ASN A 1 559  ? 55.142 61.496  -23.878 1.00 8.32  ? 559  ASN A CG  1 
ATOM   4422 O  OD1 . ASN A 1 559  ? 53.990 61.490  -23.354 1.00 10.54 ? 559  ASN A OD1 1 
ATOM   4423 N  ND2 . ASN A 1 559  ? 55.537 60.562  -24.742 1.00 10.61 ? 559  ASN A ND2 1 
ATOM   4424 N  N   . THR A 1 560  ? 55.201 62.301  -20.179 1.00 8.34  ? 560  THR A N   1 
ATOM   4425 C  CA  . THR A 1 560  ? 55.171 61.313  -19.065 1.00 9.18  ? 560  THR A CA  1 
ATOM   4426 C  C   . THR A 1 560  ? 54.586 59.943  -19.465 1.00 9.14  ? 560  THR A C   1 
ATOM   4427 O  O   . THR A 1 560  ? 54.839 58.943  -18.783 1.00 11.08 ? 560  THR A O   1 
ATOM   4428 C  CB  . THR A 1 560  ? 54.410 61.931  -17.893 1.00 9.57  ? 560  THR A CB  1 
ATOM   4429 O  OG1 . THR A 1 560  ? 54.723 61.199  -16.671 1.00 9.82  ? 560  THR A OG1 1 
ATOM   4430 C  CG2 . THR A 1 560  ? 52.911 61.823  -18.126 1.00 8.17  ? 560  THR A CG2 1 
ATOM   4431 N  N   . LEU A 1 561  ? 53.840 59.861  -20.559 1.00 9.19  ? 561  LEU A N   1 
ATOM   4432 C  CA  . LEU A 1 561  ? 53.254 58.592  -20.998 1.00 8.78  ? 561  LEU A CA  1 
ATOM   4433 C  C   . LEU A 1 561  ? 54.300 57.647  -21.672 1.00 10.41 ? 561  LEU A C   1 
ATOM   4434 O  O   . LEU A 1 561  ? 55.206 58.107  -22.386 1.00 9.17  ? 561  LEU A O   1 
ATOM   4435 C  CB  . LEU A 1 561  ? 52.109 58.830  -22.029 1.00 9.27  ? 561  LEU A CB  1 
ATOM   4436 C  CG  . LEU A 1 561  ? 51.017 59.778  -21.512 1.00 9.78  ? 561  LEU A CG  1 
ATOM   4437 C  CD1 . LEU A 1 561  ? 50.004 60.004  -22.651 1.00 11.42 ? 561  LEU A CD1 1 
ATOM   4438 C  CD2 . LEU A 1 561  ? 50.299 59.181  -20.248 1.00 9.91  ? 561  LEU A CD2 1 
ATOM   4439 N  N   . PRO A 1 562  ? 54.131 56.337  -21.536 1.00 9.53  ? 562  PRO A N   1 
ATOM   4440 C  CA  . PRO A 1 562  ? 55.067 55.391  -22.118 1.00 9.96  ? 562  PRO A CA  1 
ATOM   4441 C  C   . PRO A 1 562  ? 54.917 55.056  -23.575 1.00 11.87 ? 562  PRO A C   1 
ATOM   4442 O  O   . PRO A 1 562  ? 55.104 53.891  -23.960 1.00 11.12 ? 562  PRO A O   1 
ATOM   4443 C  CB  . PRO A 1 562  ? 54.928 54.151  -21.238 1.00 9.43  ? 562  PRO A CB  1 
ATOM   4444 C  CG  . PRO A 1 562  ? 53.387 54.220  -20.902 1.00 10.93 ? 562  PRO A CG  1 
ATOM   4445 C  CD  . PRO A 1 562  ? 53.214 55.673  -20.581 1.00 8.93  ? 562  PRO A CD  1 
ATOM   4446 N  N   . HIS A 1 563  ? 54.562 56.037  -24.415 1.00 9.50  ? 563  HIS A N   1 
ATOM   4447 C  CA  . HIS A 1 563  ? 54.537 55.735  -25.858 1.00 11.68 ? 563  HIS A CA  1 
ATOM   4448 C  C   . HIS A 1 563  ? 54.946 57.049  -26.544 1.00 10.44 ? 563  HIS A C   1 
ATOM   4449 O  O   . HIS A 1 563  ? 54.803 58.122  -25.991 1.00 10.93 ? 563  HIS A O   1 
ATOM   4450 C  CB  . HIS A 1 563  ? 53.149 55.252  -26.343 1.00 11.43 ? 563  HIS A CB  1 
ATOM   4451 C  CG  . HIS A 1 563  ? 52.002 56.124  -25.912 1.00 13.74 ? 563  HIS A CG  1 
ATOM   4452 N  ND1 . HIS A 1 563  ? 51.185 55.797  -24.839 1.00 10.72 ? 563  HIS A ND1 1 
ATOM   4453 C  CD2 . HIS A 1 563  ? 51.517 57.289  -26.418 1.00 11.18 ? 563  HIS A CD2 1 
ATOM   4454 C  CE1 . HIS A 1 563  ? 50.250 56.723  -24.711 1.00 12.47 ? 563  HIS A CE1 1 
ATOM   4455 N  NE2 . HIS A 1 563  ? 50.428 57.648  -25.645 1.00 11.89 ? 563  HIS A NE2 1 
ATOM   4456 N  N   . TRP A 1 564  ? 55.461 56.932  -27.767 1.00 11.05 ? 564  TRP A N   1 
ATOM   4457 C  CA  . TRP A 1 564  ? 55.806 58.156  -28.529 1.00 11.47 ? 564  TRP A CA  1 
ATOM   4458 C  C   . TRP A 1 564  ? 54.540 59.006  -28.641 1.00 12.04 ? 564  TRP A C   1 
ATOM   4459 O  O   . TRP A 1 564  ? 53.427 58.495  -28.845 1.00 12.21 ? 564  TRP A O   1 
ATOM   4460 C  CB  . TRP A 1 564  ? 56.280 57.782  -29.936 1.00 11.91 ? 564  TRP A CB  1 
ATOM   4461 C  CG  . TRP A 1 564  ? 57.692 57.358  -30.013 1.00 11.09 ? 564  TRP A CG  1 
ATOM   4462 C  CD1 . TRP A 1 564  ? 58.161 56.085  -29.891 1.00 12.12 ? 564  TRP A CD1 1 
ATOM   4463 C  CD2 . TRP A 1 564  ? 58.847 58.211  -30.168 1.00 13.39 ? 564  TRP A CD2 1 
ATOM   4464 N  NE1 . TRP A 1 564  ? 59.534 56.084  -29.962 1.00 15.16 ? 564  TRP A NE1 1 
ATOM   4465 C  CE2 . TRP A 1 564  ? 59.981 57.368  -30.125 1.00 13.77 ? 564  TRP A CE2 1 
ATOM   4466 C  CE3 . TRP A 1 564  ? 59.037 59.615  -30.336 1.00 14.62 ? 564  TRP A CE3 1 
ATOM   4467 C  CZ2 . TRP A 1 564  ? 61.303 57.868  -30.242 1.00 14.42 ? 564  TRP A CZ2 1 
ATOM   4468 C  CZ3 . TRP A 1 564  ? 60.371 60.118  -30.451 1.00 14.30 ? 564  TRP A CZ3 1 
ATOM   4469 C  CH2 . TRP A 1 564  ? 61.471 59.243  -30.401 1.00 14.60 ? 564  TRP A CH2 1 
ATOM   4470 N  N   . ARG A 1 565  ? 54.689 60.313  -28.525 1.00 9.69  ? 565  ARG A N   1 
ATOM   4471 C  CA  . ARG A 1 565  ? 53.474 61.119  -28.585 1.00 11.94 ? 565  ARG A CA  1 
ATOM   4472 C  C   . ARG A 1 565  ? 53.685 62.430  -29.339 1.00 11.22 ? 565  ARG A C   1 
ATOM   4473 O  O   . ARG A 1 565  ? 54.728 63.045  -29.204 1.00 12.39 ? 565  ARG A O   1 
ATOM   4474 C  CB  . ARG A 1 565  ? 53.001 61.422  -27.135 1.00 11.46 ? 565  ARG A CB  1 
ATOM   4475 C  CG  . ARG A 1 565  ? 51.717 62.302  -27.123 1.00 13.00 ? 565  ARG A CG  1 
ATOM   4476 C  CD  . ARG A 1 565  ? 50.785 62.224  -25.869 1.00 14.76 ? 565  ARG A CD  1 
ATOM   4477 N  NE  . ARG A 1 565  ? 51.555 62.529  -24.687 1.00 15.33 ? 565  ARG A NE  1 
ATOM   4478 C  CZ  . ARG A 1 565  ? 51.056 63.073  -23.593 1.00 14.34 ? 565  ARG A CZ  1 
ATOM   4479 N  NH1 . ARG A 1 565  ? 49.762 63.422  -23.524 1.00 14.67 ? 565  ARG A NH1 1 
ATOM   4480 N  NH2 . ARG A 1 565  ? 51.851 63.185  -22.558 1.00 12.81 ? 565  ARG A NH2 1 
ATOM   4481 N  N   . GLU A 1 566  ? 52.723 62.783  -30.196 1.00 12.15 ? 566  GLU A N   1 
ATOM   4482 C  CA  . GLU A 1 566  ? 52.766 64.115  -30.860 1.00 13.72 ? 566  GLU A CA  1 
ATOM   4483 C  C   . GLU A 1 566  ? 51.628 64.927  -30.257 1.00 13.21 ? 566  GLU A C   1 
ATOM   4484 O  O   . GLU A 1 566  ? 50.534 64.370  -30.001 1.00 14.74 ? 566  GLU A O   1 
ATOM   4485 C  CB  . GLU A 1 566  ? 52.515 64.034  -32.381 1.00 13.17 ? 566  GLU A CB  1 
ATOM   4486 C  CG  . GLU A 1 566  ? 53.607 63.359  -33.091 1.00 15.92 ? 566  GLU A CG  1 
ATOM   4487 C  CD  . GLU A 1 566  ? 53.323 63.258  -34.576 1.00 19.69 ? 566  GLU A CD  1 
ATOM   4488 O  OE1 . GLU A 1 566  ? 52.181 62.932  -34.995 1.00 19.72 ? 566  GLU A OE1 1 
ATOM   4489 O  OE2 . GLU A 1 566  ? 54.279 63.534  -35.292 1.00 21.52 ? 566  GLU A OE2 1 
ATOM   4490 N  N   . GLN A 1 567  ? 51.857 66.220  -30.000 1.00 11.84 ? 567  GLN A N   1 
ATOM   4491 C  CA  . GLN A 1 567  ? 50.789 67.090  -29.489 1.00 11.37 ? 567  GLN A CA  1 
ATOM   4492 C  C   . GLN A 1 567  ? 51.137 68.507  -29.905 1.00 13.03 ? 567  GLN A C   1 
ATOM   4493 O  O   . GLN A 1 567  ? 52.325 68.885  -29.891 1.00 11.74 ? 567  GLN A O   1 
ATOM   4494 C  CB  . GLN A 1 567  ? 50.725 66.979  -27.958 1.00 13.27 ? 567  GLN A CB  1 
ATOM   4495 C  CG  . GLN A 1 567  ? 49.629 67.849  -27.392 1.00 14.15 ? 567  GLN A CG  1 
ATOM   4496 C  CD  . GLN A 1 567  ? 49.962 68.336  -25.981 1.00 19.11 ? 567  GLN A CD  1 
ATOM   4497 O  OE1 . GLN A 1 567  ? 50.012 67.541  -25.032 1.00 17.09 ? 567  GLN A OE1 1 
ATOM   4498 N  NE2 . GLN A 1 567  ? 50.243 69.656  -25.838 1.00 21.10 ? 567  GLN A NE2 1 
ATOM   4499 N  N   . LEU A 1 568  ? 50.136 69.271  -30.334 1.00 12.76 ? 568  LEU A N   1 
ATOM   4500 C  CA  . LEU A 1 568  ? 50.453 70.662  -30.625 1.00 12.11 ? 568  LEU A CA  1 
ATOM   4501 C  C   . LEU A 1 568  ? 50.766 71.364  -29.302 1.00 12.25 ? 568  LEU A C   1 
ATOM   4502 O  O   . LEU A 1 568  ? 50.092 71.120  -28.260 1.00 13.87 ? 568  LEU A O   1 
ATOM   4503 C  CB  . LEU A 1 568  ? 49.313 71.416  -31.293 1.00 12.75 ? 568  LEU A CB  1 
ATOM   4504 C  CG  . LEU A 1 568  ? 48.929 70.960  -32.706 1.00 15.62 ? 568  LEU A CG  1 
ATOM   4505 C  CD1 . LEU A 1 568  ? 47.918 71.944  -33.250 1.00 17.02 ? 568  LEU A CD1 1 
ATOM   4506 C  CD2 . LEU A 1 568  ? 50.138 70.869  -33.598 1.00 14.25 ? 568  LEU A CD2 1 
ATOM   4507 N  N   . VAL A 1 569  ? 51.805 72.177  -29.325 1.00 13.10 ? 569  VAL A N   1 
ATOM   4508 C  CA  . VAL A 1 569  ? 52.163 72.963  -28.157 1.00 12.17 ? 569  VAL A CA  1 
ATOM   4509 C  C   . VAL A 1 569  ? 52.270 74.455  -28.526 1.00 13.64 ? 569  VAL A C   1 
ATOM   4510 O  O   . VAL A 1 569  ? 52.570 74.797  -29.692 1.00 13.50 ? 569  VAL A O   1 
ATOM   4511 C  CB  . VAL A 1 569  ? 53.523 72.568  -27.473 1.00 10.69 ? 569  VAL A CB  1 
ATOM   4512 C  CG1 . VAL A 1 569  ? 53.384 71.188  -26.763 1.00 11.62 ? 569  VAL A CG1 1 
ATOM   4513 C  CG2 . VAL A 1 569  ? 54.707 72.586  -28.494 1.00 12.77 ? 569  VAL A CG2 1 
ATOM   4514 N  N   . ASP A 1 570  ? 51.984 75.334  -27.583 1.00 12.94 ? 570  ASP A N   1 
ATOM   4515 C  CA  . ASP A 1 570  ? 52.053 76.778  -27.837 1.00 13.67 ? 570  ASP A CA  1 
ATOM   4516 C  C   . ASP A 1 570  ? 52.869 77.563  -26.819 1.00 15.22 ? 570  ASP A C   1 
ATOM   4517 O  O   . ASP A 1 570  ? 52.931 77.208  -25.636 1.00 13.67 ? 570  ASP A O   1 
ATOM   4518 C  CB  . ASP A 1 570  ? 50.640 77.425  -27.938 1.00 15.87 ? 570  ASP A CB  1 
ATOM   4519 C  CG  . ASP A 1 570  ? 49.848 77.355  -26.659 1.00 19.61 ? 570  ASP A CG  1 
ATOM   4520 O  OD1 . ASP A 1 570  ? 49.653 76.236  -26.157 1.00 23.32 ? 570  ASP A OD1 1 
ATOM   4521 O  OD2 . ASP A 1 570  ? 49.403 78.392  -26.167 1.00 24.28 ? 570  ASP A OD2 1 
ATOM   4522 N  N   . PHE A 1 571  ? 53.513 78.638  -27.284 1.00 12.13 ? 571  PHE A N   1 
ATOM   4523 C  CA  . PHE A 1 571  ? 54.280 79.515  -26.446 1.00 12.76 ? 571  PHE A CA  1 
ATOM   4524 C  C   . PHE A 1 571  ? 53.942 80.979  -26.808 1.00 13.14 ? 571  PHE A C   1 
ATOM   4525 O  O   . PHE A 1 571  ? 53.580 81.237  -27.970 1.00 15.02 ? 571  PHE A O   1 
ATOM   4526 C  CB  . PHE A 1 571  ? 55.793 79.331  -26.676 1.00 10.81 ? 571  PHE A CB  1 
ATOM   4527 C  CG  . PHE A 1 571  ? 56.305 77.996  -26.265 1.00 11.25 ? 571  PHE A CG  1 
ATOM   4528 C  CD1 . PHE A 1 571  ? 56.309 76.924  -27.117 1.00 11.45 ? 571  PHE A CD1 1 
ATOM   4529 C  CD2 . PHE A 1 571  ? 56.732 77.825  -24.964 1.00 11.05 ? 571  PHE A CD2 1 
ATOM   4530 C  CE1 . PHE A 1 571  ? 56.724 75.655  -26.691 1.00 11.02 ? 571  PHE A CE1 1 
ATOM   4531 C  CE2 . PHE A 1 571  ? 57.150 76.573  -24.513 1.00 10.37 ? 571  PHE A CE2 1 
ATOM   4532 C  CZ  . PHE A 1 571  ? 57.145 75.503  -25.352 1.00 12.88 ? 571  PHE A CZ  1 
ATOM   4533 N  N   . TYR A 1 572  ? 54.085 81.887  -25.843 1.00 12.91 ? 572  TYR A N   1 
ATOM   4534 C  CA  . TYR A 1 572  ? 53.889 83.329  -26.123 1.00 13.40 ? 572  TYR A CA  1 
ATOM   4535 C  C   . TYR A 1 572  ? 55.257 83.845  -26.577 1.00 14.91 ? 572  TYR A C   1 
ATOM   4536 O  O   . TYR A 1 572  ? 56.263 83.512  -25.966 1.00 15.06 ? 572  TYR A O   1 
ATOM   4537 C  CB  . TYR A 1 572  ? 53.505 84.113  -24.902 1.00 15.23 ? 572  TYR A CB  1 
ATOM   4538 C  CG  . TYR A 1 572  ? 52.075 83.925  -24.456 1.00 17.74 ? 572  TYR A CG  1 
ATOM   4539 C  CD1 . TYR A 1 572  ? 51.149 83.256  -25.239 1.00 17.57 ? 572  TYR A CD1 1 
ATOM   4540 C  CD2 . TYR A 1 572  ? 51.642 84.502  -23.268 1.00 20.25 ? 572  TYR A CD2 1 
ATOM   4541 C  CE1 . TYR A 1 572  ? 49.780 83.169  -24.843 1.00 21.22 ? 572  TYR A CE1 1 
ATOM   4542 C  CE2 . TYR A 1 572  ? 50.305 84.437  -22.869 1.00 22.56 ? 572  TYR A CE2 1 
ATOM   4543 C  CZ  . TYR A 1 572  ? 49.389 83.769  -23.666 1.00 21.70 ? 572  TYR A CZ  1 
ATOM   4544 O  OH  . TYR A 1 572  ? 48.073 83.715  -23.204 1.00 22.02 ? 572  TYR A OH  1 
ATOM   4545 N  N   . VAL A 1 573  ? 55.317 84.690  -27.623 1.00 14.57 ? 573  VAL A N   1 
ATOM   4546 C  CA  . VAL A 1 573  ? 56.600 85.214  -28.147 1.00 14.57 ? 573  VAL A CA  1 
ATOM   4547 C  C   . VAL A 1 573  ? 56.401 86.679  -28.417 1.00 15.95 ? 573  VAL A C   1 
ATOM   4548 O  O   . VAL A 1 573  ? 55.261 87.088  -28.708 1.00 16.60 ? 573  VAL A O   1 
ATOM   4549 C  CB  . VAL A 1 573  ? 57.046 84.504  -29.430 1.00 13.65 ? 573  VAL A CB  1 
ATOM   4550 C  CG1 . VAL A 1 573  ? 57.536 83.111  -29.118 1.00 15.40 ? 573  VAL A CG1 1 
ATOM   4551 C  CG2 . VAL A 1 573  ? 55.906 84.445  -30.438 1.00 14.43 ? 573  VAL A CG2 1 
ATOM   4552 N  N   . SER A 1 574  ? 57.481 87.474  -28.365 1.00 15.54 ? 574  SER A N   1 
ATOM   4553 C  CA  . SER A 1 574  ? 57.382 88.939  -28.505 1.00 14.53 ? 574  SER A CA  1 
ATOM   4554 C  C   . SER A 1 574  ? 57.317 89.447  -29.960 1.00 14.92 ? 574  SER A C   1 
ATOM   4555 O  O   . SER A 1 574  ? 57.193 90.651  -30.162 1.00 16.44 ? 574  SER A O   1 
ATOM   4556 C  CB  . SER A 1 574  ? 58.531 89.621  -27.768 1.00 16.78 ? 574  SER A CB  1 
ATOM   4557 O  OG  . SER A 1 574  ? 59.758 89.270  -28.405 1.00 16.24 ? 574  SER A OG  1 
ATOM   4558 N  N   . SER A 1 575  ? 57.350 88.532  -30.922 1.00 14.95 ? 575  SER A N   1 
ATOM   4559 C  CA  . SER A 1 575  ? 57.264 88.865  -32.370 1.00 17.17 ? 575  SER A CA  1 
ATOM   4560 C  C   . SER A 1 575  ? 56.483 87.805  -33.123 1.00 15.88 ? 575  SER A C   1 
ATOM   4561 O  O   . SER A 1 575  ? 56.476 86.633  -32.750 1.00 16.63 ? 575  SER A O   1 
ATOM   4562 C  CB  . SER A 1 575  ? 58.693 88.950  -32.992 1.00 18.41 ? 575  SER A CB  1 
ATOM   4563 O  OG  . SER A 1 575  ? 58.650 89.087  -34.412 1.00 18.93 ? 575  SER A OG  1 
ATOM   4564 N  N   . PRO A 1 576  ? 55.760 88.201  -34.164 1.00 16.31 ? 576  PRO A N   1 
ATOM   4565 C  CA  . PRO A 1 576  ? 55.022 87.189  -34.927 1.00 15.26 ? 576  PRO A CA  1 
ATOM   4566 C  C   . PRO A 1 576  ? 55.928 86.486  -35.909 1.00 14.61 ? 576  PRO A C   1 
ATOM   4567 O  O   . PRO A 1 576  ? 55.567 85.500  -36.556 1.00 14.73 ? 576  PRO A O   1 
ATOM   4568 C  CB  . PRO A 1 576  ? 53.944 87.993  -35.672 1.00 15.52 ? 576  PRO A CB  1 
ATOM   4569 C  CG  . PRO A 1 576  ? 54.596 89.372  -35.844 1.00 17.41 ? 576  PRO A CG  1 
ATOM   4570 C  CD  . PRO A 1 576  ? 55.383 89.587  -34.542 1.00 16.06 ? 576  PRO A CD  1 
ATOM   4571 N  N   . PHE A 1 577  ? 57.129 87.023  -36.066 1.00 14.64 ? 577  PHE A N   1 
ATOM   4572 C  CA  . PHE A 1 577  ? 58.033 86.466  -37.018 1.00 17.24 ? 577  PHE A CA  1 
ATOM   4573 C  C   . PHE A 1 577  ? 58.990 85.512  -36.374 1.00 17.15 ? 577  PHE A C   1 
ATOM   4574 O  O   . PHE A 1 577  ? 60.171 85.829  -36.180 1.00 18.06 ? 577  PHE A O   1 
ATOM   4575 C  CB  . PHE A 1 577  ? 58.750 87.629  -37.710 1.00 18.85 ? 577  PHE A CB  1 
ATOM   4576 C  CG  . PHE A 1 577  ? 57.786 88.630  -38.316 1.00 21.89 ? 577  PHE A CG  1 
ATOM   4577 C  CD1 . PHE A 1 577  ? 56.782 88.205  -39.176 1.00 22.58 ? 577  PHE A CD1 1 
ATOM   4578 C  CD2 . PHE A 1 577  ? 57.861 89.967  -37.980 1.00 23.34 ? 577  PHE A CD2 1 
ATOM   4579 C  CE1 . PHE A 1 577  ? 55.858 89.095  -39.703 1.00 23.11 ? 577  PHE A CE1 1 
ATOM   4580 C  CE2 . PHE A 1 577  ? 56.924 90.897  -38.500 1.00 26.02 ? 577  PHE A CE2 1 
ATOM   4581 C  CZ  . PHE A 1 577  ? 55.923 90.440  -39.366 1.00 26.03 ? 577  PHE A CZ  1 
ATOM   4582 N  N   . VAL A 1 578  ? 58.478 84.312  -36.108 1.00 16.63 ? 578  VAL A N   1 
ATOM   4583 C  CA  . VAL A 1 578  ? 59.280 83.323  -35.395 1.00 15.86 ? 578  VAL A CA  1 
ATOM   4584 C  C   . VAL A 1 578  ? 59.160 81.987  -36.071 1.00 14.92 ? 578  VAL A C   1 
ATOM   4585 O  O   . VAL A 1 578  ? 58.085 81.631  -36.550 1.00 16.45 ? 578  VAL A O   1 
ATOM   4586 C  CB  . VAL A 1 578  ? 58.805 83.176  -33.903 1.00 14.60 ? 578  VAL A CB  1 
ATOM   4587 C  CG1 . VAL A 1 578  ? 59.643 82.088  -33.188 1.00 12.51 ? 578  VAL A CG1 1 
ATOM   4588 C  CG2 . VAL A 1 578  ? 58.936 84.398  -33.209 1.00 14.34 ? 578  VAL A CG2 1 
ATOM   4589 N  N   . SER A 1 579  ? 60.278 81.288  -36.185 1.00 14.49 ? 579  SER A N   1 
ATOM   4590 C  CA  . SER A 1 579  ? 60.204 79.948  -36.761 1.00 15.67 ? 579  SER A CA  1 
ATOM   4591 C  C   . SER A 1 579  ? 60.804 78.910  -35.786 1.00 14.28 ? 579  SER A C   1 
ATOM   4592 O  O   . SER A 1 579  ? 61.584 79.242  -34.882 1.00 16.18 ? 579  SER A O   1 
ATOM   4593 C  CB  . SER A 1 579  ? 60.863 79.852  -38.141 1.00 18.83 ? 579  SER A CB  1 
ATOM   4594 O  OG  . SER A 1 579  ? 62.073 80.540  -38.151 1.00 22.71 ? 579  SER A OG  1 
ATOM   4595 N  N   . VAL A 1 580  ? 60.448 77.659  -36.043 1.00 15.30 ? 580  VAL A N   1 
ATOM   4596 C  CA  . VAL A 1 580  ? 60.834 76.571  -35.154 1.00 13.68 ? 580  VAL A CA  1 
ATOM   4597 C  C   . VAL A 1 580  ? 61.681 75.521  -35.871 1.00 13.27 ? 580  VAL A C   1 
ATOM   4598 O  O   . VAL A 1 580  ? 61.441 75.198  -37.017 1.00 14.46 ? 580  VAL A O   1 
ATOM   4599 C  CB  . VAL A 1 580  ? 59.522 75.878  -34.631 1.00 13.00 ? 580  VAL A CB  1 
ATOM   4600 C  CG1 . VAL A 1 580  ? 59.861 74.691  -33.656 1.00 12.13 ? 580  VAL A CG1 1 
ATOM   4601 C  CG2 . VAL A 1 580  ? 58.587 76.932  -34.003 1.00 13.69 ? 580  VAL A CG2 1 
ATOM   4602 N  N   . THR A 1 581  ? 62.704 75.060  -35.149 1.00 13.61 ? 581  THR A N   1 
ATOM   4603 C  CA  . THR A 1 581  ? 63.561 73.979  -35.614 1.00 13.73 ? 581  THR A CA  1 
ATOM   4604 C  C   . THR A 1 581  ? 63.738 72.944  -34.497 1.00 14.25 ? 581  THR A C   1 
ATOM   4605 O  O   . THR A 1 581  ? 63.552 73.287  -33.315 1.00 14.99 ? 581  THR A O   1 
ATOM   4606 C  CB  . THR A 1 581  ? 64.978 74.451  -36.018 1.00 13.29 ? 581  THR A CB  1 
ATOM   4607 O  OG1 . THR A 1 581  ? 65.528 75.332  -35.040 1.00 15.83 ? 581  THR A OG1 1 
ATOM   4608 C  CG2 . THR A 1 581  ? 64.893 75.196  -37.372 1.00 13.42 ? 581  THR A CG2 1 
ATOM   4609 N  N   . ASP A 1 582  ? 64.113 71.712  -34.849 1.00 15.76 ? 582  ASP A N   1 
ATOM   4610 C  CA  . ASP A 1 582  ? 64.368 70.668  -33.817 1.00 17.89 ? 582  ASP A CA  1 
ATOM   4611 C  C   . ASP A 1 582  ? 65.868 70.714  -33.553 1.00 18.39 ? 582  ASP A C   1 
ATOM   4612 O  O   . ASP A 1 582  ? 66.549 71.589  -34.083 1.00 18.08 ? 582  ASP A O   1 
ATOM   4613 C  CB  . ASP A 1 582  ? 63.941 69.270  -34.278 1.00 18.48 ? 582  ASP A CB  1 
ATOM   4614 C  CG  . ASP A 1 582  ? 64.664 68.796  -35.527 1.00 21.20 ? 582  ASP A CG  1 
ATOM   4615 O  OD1 . ASP A 1 582  ? 65.709 69.368  -35.843 1.00 20.52 ? 582  ASP A OD1 1 
ATOM   4616 O  OD2 . ASP A 1 582  ? 64.161 67.832  -36.156 1.00 22.06 ? 582  ASP A OD2 1 
ATOM   4617 N  N   . LEU A 1 583  ? 66.440 69.802  -32.766 1.00 21.27 ? 583  LEU A N   1 
ATOM   4618 C  CA  . LEU A 1 583  ? 67.866 70.007  -32.570 1.00 23.55 ? 583  LEU A CA  1 
ATOM   4619 C  C   . LEU A 1 583  ? 68.770 69.486  -33.669 1.00 23.51 ? 583  LEU A C   1 
ATOM   4620 O  O   . LEU A 1 583  ? 69.987 69.548  -33.542 1.00 25.29 ? 583  LEU A O   1 
ATOM   4621 C  CB  . LEU A 1 583  ? 68.364 69.588  -31.159 1.00 24.93 ? 583  LEU A CB  1 
ATOM   4622 C  CG  . LEU A 1 583  ? 69.293 70.662  -30.515 1.00 24.06 ? 583  LEU A CG  1 
ATOM   4623 C  CD1 . LEU A 1 583  ? 68.497 71.965  -30.405 1.00 24.35 ? 583  LEU A CD1 1 
ATOM   4624 C  CD2 . LEU A 1 583  ? 69.822 70.339  -29.113 1.00 25.50 ? 583  LEU A CD2 1 
ATOM   4625 N  N   . ALA A 1 584  ? 68.175 68.956  -34.751 1.00 22.03 ? 584  ALA A N   1 
ATOM   4626 C  CA  . ALA A 1 584  ? 69.005 68.587  -35.909 1.00 19.11 ? 584  ALA A CA  1 
ATOM   4627 C  C   . ALA A 1 584  ? 68.879 69.814  -36.874 1.00 18.49 ? 584  ALA A C   1 
ATOM   4628 O  O   . ALA A 1 584  ? 69.326 69.786  -38.021 1.00 16.67 ? 584  ALA A O   1 
ATOM   4629 C  CB  . ALA A 1 584  ? 68.492 67.330  -36.585 1.00 20.47 ? 584  ALA A CB  1 
ATOM   4630 N  N   . ASN A 1 585  ? 68.241 70.873  -36.401 1.00 17.36 ? 585  ASN A N   1 
ATOM   4631 C  CA  . ASN A 1 585  ? 68.075 72.092  -37.184 1.00 16.99 ? 585  ASN A CA  1 
ATOM   4632 C  C   . ASN A 1 585  ? 67.106 71.875  -38.330 1.00 18.08 ? 585  ASN A C   1 
ATOM   4633 O  O   . ASN A 1 585  ? 67.176 72.570  -39.347 1.00 19.10 ? 585  ASN A O   1 
ATOM   4634 C  CB  . ASN A 1 585  ? 69.410 72.571  -37.752 1.00 20.26 ? 585  ASN A CB  1 
ATOM   4635 C  CG  . ASN A 1 585  ? 69.407 74.055  -38.036 1.00 23.11 ? 585  ASN A CG  1 
ATOM   4636 O  OD1 . ASN A 1 585  ? 68.765 74.829  -37.334 1.00 25.40 ? 585  ASN A OD1 1 
ATOM   4637 N  ND2 . ASN A 1 585  ? 70.147 74.464  -39.065 1.00 25.55 ? 585  ASN A ND2 1 
ATOM   4638 N  N   . ASN A 1 586  ? 66.245 70.879  -38.193 1.00 15.95 ? 586  ASN A N   1 
ATOM   4639 C  CA  . ASN A 1 586  ? 65.235 70.586  -39.194 1.00 18.16 ? 586  ASN A CA  1 
ATOM   4640 C  C   . ASN A 1 586  ? 64.048 71.533  -38.999 1.00 18.44 ? 586  ASN A C   1 
ATOM   4641 O  O   . ASN A 1 586  ? 63.509 71.637  -37.909 1.00 18.34 ? 586  ASN A O   1 
ATOM   4642 C  CB  . ASN A 1 586  ? 64.680 69.169  -39.041 1.00 18.87 ? 586  ASN A CB  1 
ATOM   4643 C  CG  . ASN A 1 586  ? 65.732 68.102  -39.208 1.00 22.01 ? 586  ASN A CG  1 
ATOM   4644 O  OD1 . ASN A 1 586  ? 66.519 68.141  -40.166 1.00 21.71 ? 586  ASN A OD1 1 
ATOM   4645 N  ND2 . ASN A 1 586  ? 65.750 67.110  -38.267 1.00 21.30 ? 586  ASN A ND2 1 
ATOM   4646 N  N   . PRO A 1 587  ? 63.625 72.253  -40.048 1.00 17.30 ? 587  PRO A N   1 
ATOM   4647 C  CA  . PRO A 1 587  ? 62.474 73.130  -39.808 1.00 17.74 ? 587  PRO A CA  1 
ATOM   4648 C  C   . PRO A 1 587  ? 61.251 72.370  -39.310 1.00 17.17 ? 587  PRO A C   1 
ATOM   4649 O  O   . PRO A 1 587  ? 61.026 71.196  -39.644 1.00 18.23 ? 587  PRO A O   1 
ATOM   4650 C  CB  . PRO A 1 587  ? 62.191 73.751  -41.180 1.00 18.87 ? 587  PRO A CB  1 
ATOM   4651 C  CG  . PRO A 1 587  ? 63.571 73.849  -41.777 1.00 20.38 ? 587  PRO A CG  1 
ATOM   4652 C  CD  . PRO A 1 587  ? 64.201 72.480  -41.391 1.00 18.87 ? 587  PRO A CD  1 
ATOM   4653 N  N   . VAL A 1 588  ? 60.461 73.058  -38.506 1.00 14.07 ? 588  VAL A N   1 
ATOM   4654 C  CA  . VAL A 1 588  ? 59.224 72.513  -38.002 1.00 15.92 ? 588  VAL A CA  1 
ATOM   4655 C  C   . VAL A 1 588  ? 58.059 73.445  -38.347 1.00 15.99 ? 588  VAL A C   1 
ATOM   4656 O  O   . VAL A 1 588  ? 58.121 74.627  -38.088 1.00 15.23 ? 588  VAL A O   1 
ATOM   4657 C  CB  . VAL A 1 588  ? 59.303 72.340  -36.478 1.00 15.76 ? 588  VAL A CB  1 
ATOM   4658 C  CG1 . VAL A 1 588  ? 57.919 71.889  -35.914 1.00 15.58 ? 588  VAL A CG1 1 
ATOM   4659 C  CG2 . VAL A 1 588  ? 60.428 71.341  -36.177 1.00 14.60 ? 588  VAL A CG2 1 
ATOM   4660 N  N   . GLU A 1 589  ? 57.028 72.915  -38.982 1.00 16.53 ? 589  GLU A N   1 
ATOM   4661 C  CA  . GLU A 1 589  ? 55.903 73.741  -39.355 1.00 17.78 ? 589  GLU A CA  1 
ATOM   4662 C  C   . GLU A 1 589  ? 55.230 74.359  -38.120 1.00 16.52 ? 589  GLU A C   1 
ATOM   4663 O  O   . GLU A 1 589  ? 54.961 73.660  -37.125 1.00 16.99 ? 589  GLU A O   1 
ATOM   4664 C  CB  . GLU A 1 589  ? 54.884 72.927  -40.159 1.00 19.24 ? 589  GLU A CB  1 
ATOM   4665 C  CG  . GLU A 1 589  ? 53.667 73.786  -40.518 1.00 23.82 ? 589  GLU A CG  1 
ATOM   4666 C  CD  . GLU A 1 589  ? 52.554 73.055  -41.262 1.00 27.79 ? 589  GLU A CD  1 
ATOM   4667 O  OE1 . GLU A 1 589  ? 52.449 71.791  -41.228 1.00 32.10 ? 589  GLU A OE1 1 
ATOM   4668 O  OE2 . GLU A 1 589  ? 51.728 73.772  -41.879 1.00 30.70 ? 589  GLU A OE2 1 
ATOM   4669 N  N   . ALA A 1 590  ? 54.929 75.648  -38.183 1.00 15.02 ? 590  ALA A N   1 
ATOM   4670 C  CA  . ALA A 1 590  ? 54.345 76.362  -37.067 1.00 16.51 ? 590  ALA A CA  1 
ATOM   4671 C  C   . ALA A 1 590  ? 53.264 77.257  -37.579 1.00 16.81 ? 590  ALA A C   1 
ATOM   4672 O  O   . ALA A 1 590  ? 53.196 77.545  -38.812 1.00 15.67 ? 590  ALA A O   1 
ATOM   4673 C  CB  . ALA A 1 590  ? 55.383 77.223  -36.385 1.00 14.13 ? 590  ALA A CB  1 
ATOM   4674 N  N   . GLN A 1 591  ? 52.426 77.690  -36.638 1.00 16.38 ? 591  GLN A N   1 
ATOM   4675 C  CA  . GLN A 1 591  ? 51.321 78.626  -36.928 1.00 16.43 ? 591  GLN A CA  1 
ATOM   4676 C  C   . GLN A 1 591  ? 51.352 79.705  -35.859 1.00 16.33 ? 591  GLN A C   1 
ATOM   4677 O  O   . GLN A 1 591  ? 51.497 79.403  -34.653 1.00 15.23 ? 591  GLN A O   1 
ATOM   4678 C  CB  . GLN A 1 591  ? 49.968 77.907  -36.879 1.00 14.79 ? 591  GLN A CB  1 
ATOM   4679 C  CG  . GLN A 1 591  ? 48.742 78.891  -36.857 1.00 14.92 ? 591  GLN A CG  1 
ATOM   4680 C  CD  . GLN A 1 591  ? 47.389 78.168  -36.671 1.00 11.83 ? 591  GLN A CD  1 
ATOM   4681 O  OE1 . GLN A 1 591  ? 47.122 77.119  -37.265 1.00 14.93 ? 591  GLN A OE1 1 
ATOM   4682 N  NE2 . GLN A 1 591  ? 46.546 78.734  -35.829 1.00 15.71 ? 591  GLN A NE2 1 
ATOM   4683 N  N   . VAL A 1 592  ? 51.215 80.969  -36.256 1.00 14.00 ? 592  VAL A N   1 
ATOM   4684 C  CA  . VAL A 1 592  ? 51.192 82.044  -35.328 1.00 14.82 ? 592  VAL A CA  1 
ATOM   4685 C  C   . VAL A 1 592  ? 49.777 82.647  -35.262 1.00 14.95 ? 592  VAL A C   1 
ATOM   4686 O  O   . VAL A 1 592  ? 49.122 82.760  -36.264 1.00 15.22 ? 592  VAL A O   1 
ATOM   4687 C  CB  . VAL A 1 592  ? 52.281 83.087  -35.663 1.00 13.74 ? 592  VAL A CB  1 
ATOM   4688 C  CG1 . VAL A 1 592  ? 52.082 84.283  -34.833 1.00 13.74 ? 592  VAL A CG1 1 
ATOM   4689 C  CG2 . VAL A 1 592  ? 53.638 82.514  -35.286 1.00 14.06 ? 592  VAL A CG2 1 
ATOM   4690 N  N   . SER A 1 593  ? 49.295 82.947  -34.064 1.00 13.64 ? 593  SER A N   1 
ATOM   4691 C  CA  . SER A 1 593  ? 47.960 83.496  -33.886 1.00 15.27 ? 593  SER A CA  1 
ATOM   4692 C  C   . SER A 1 593  ? 48.062 84.611  -32.892 1.00 15.79 ? 593  SER A C   1 
ATOM   4693 O  O   . SER A 1 593  ? 49.074 84.744  -32.144 1.00 16.90 ? 593  SER A O   1 
ATOM   4694 C  CB  . SER A 1 593  ? 46.967 82.476  -33.278 1.00 17.25 ? 593  SER A CB  1 
ATOM   4695 O  OG  . SER A 1 593  ? 46.720 81.329  -34.066 1.00 21.25 ? 593  SER A OG  1 
ATOM   4696 N  N   . PRO A 1 594  ? 47.042 85.471  -32.830 1.00 16.15 ? 594  PRO A N   1 
ATOM   4697 C  CA  . PRO A 1 594  ? 47.107 86.557  -31.844 1.00 15.57 ? 594  PRO A CA  1 
ATOM   4698 C  C   . PRO A 1 594  ? 46.861 86.045  -30.385 1.00 14.72 ? 594  PRO A C   1 
ATOM   4699 O  O   . PRO A 1 594  ? 46.353 84.907  -30.173 1.00 14.69 ? 594  PRO A O   1 
ATOM   4700 C  CB  . PRO A 1 594  ? 45.940 87.472  -32.243 1.00 15.23 ? 594  PRO A CB  1 
ATOM   4701 C  CG  . PRO A 1 594  ? 45.644 87.088  -33.672 1.00 17.76 ? 594  PRO A CG  1 
ATOM   4702 C  CD  . PRO A 1 594  ? 45.888 85.633  -33.750 1.00 14.89 ? 594  PRO A CD  1 
ATOM   4703 N  N   . VAL A 1 595  ? 47.196 86.874  -29.391 1.00 13.88 ? 595  VAL A N   1 
ATOM   4704 C  CA  . VAL A 1 595  ? 46.888 86.536  -27.999 1.00 14.48 ? 595  VAL A CA  1 
ATOM   4705 C  C   . VAL A 1 595  ? 45.580 87.281  -27.733 1.00 14.29 ? 595  VAL A C   1 
ATOM   4706 O  O   . VAL A 1 595  ? 45.561 88.497  -27.632 1.00 14.27 ? 595  VAL A O   1 
ATOM   4707 C  CB  . VAL A 1 595  ? 47.977 87.021  -26.967 1.00 14.44 ? 595  VAL A CB  1 
ATOM   4708 C  CG1 . VAL A 1 595  ? 47.504 86.725  -25.564 1.00 15.05 ? 595  VAL A CG1 1 
ATOM   4709 C  CG2 . VAL A 1 595  ? 49.293 86.243  -27.169 1.00 13.64 ? 595  VAL A CG2 1 
ATOM   4710 N  N   . TRP A 1 596  ? 44.467 86.555  -27.638 1.00 15.06 ? 596  TRP A N   1 
ATOM   4711 C  CA  . TRP A 1 596  ? 43.152 87.144  -27.381 1.00 16.54 ? 596  TRP A CA  1 
ATOM   4712 C  C   . TRP A 1 596  ? 42.730 87.064  -25.900 1.00 17.53 ? 596  TRP A C   1 
ATOM   4713 O  O   . TRP A 1 596  ? 42.837 86.000  -25.267 1.00 18.12 ? 596  TRP A O   1 
ATOM   4714 C  CB  . TRP A 1 596  ? 42.072 86.408  -28.233 1.00 15.29 ? 596  TRP A CB  1 
ATOM   4715 C  CG  . TRP A 1 596  ? 42.196 86.637  -29.734 1.00 15.73 ? 596  TRP A CG  1 
ATOM   4716 C  CD1 . TRP A 1 596  ? 42.674 85.758  -30.670 1.00 14.99 ? 596  TRP A CD1 1 
ATOM   4717 C  CD2 . TRP A 1 596  ? 41.866 87.841  -30.451 1.00 16.41 ? 596  TRP A CD2 1 
ATOM   4718 N  NE1 . TRP A 1 596  ? 42.653 86.325  -31.920 1.00 17.00 ? 596  TRP A NE1 1 
ATOM   4719 C  CE2 . TRP A 1 596  ? 42.174 87.606  -31.812 1.00 16.74 ? 596  TRP A CE2 1 
ATOM   4720 C  CE3 . TRP A 1 596  ? 41.350 89.079  -30.074 1.00 19.01 ? 596  TRP A CE3 1 
ATOM   4721 C  CZ2 . TRP A 1 596  ? 41.987 88.576  -32.798 1.00 18.37 ? 596  TRP A CZ2 1 
ATOM   4722 C  CZ3 . TRP A 1 596  ? 41.159 90.059  -31.074 1.00 18.04 ? 596  TRP A CZ3 1 
ATOM   4723 C  CH2 . TRP A 1 596  ? 41.484 89.784  -32.396 1.00 18.24 ? 596  TRP A CH2 1 
ATOM   4724 N  N   . SER A 1 597  ? 42.241 88.160  -25.348 1.00 18.48 ? 597  SER A N   1 
ATOM   4725 C  CA  . SER A 1 597  ? 41.738 88.136  -23.986 1.00 20.01 ? 597  SER A CA  1 
ATOM   4726 C  C   . SER A 1 597  ? 40.336 88.720  -23.953 1.00 21.36 ? 597  SER A C   1 
ATOM   4727 O  O   . SER A 1 597  ? 40.001 89.676  -24.663 1.00 21.70 ? 597  SER A O   1 
ATOM   4728 C  CB  . SER A 1 597  ? 42.660 88.858  -23.006 1.00 22.20 ? 597  SER A CB  1 
ATOM   4729 O  OG  . SER A 1 597  ? 42.746 90.235  -23.239 1.00 26.87 ? 597  SER A OG  1 
ATOM   4730 N  N   . TRP A 1 598  ? 39.493 88.144  -23.119 1.00 21.50 ? 598  TRP A N   1 
ATOM   4731 C  CA  . TRP A 1 598  ? 38.140 88.649  -23.046 1.00 23.00 ? 598  TRP A CA  1 
ATOM   4732 C  C   . TRP A 1 598  ? 37.926 89.560  -21.843 1.00 25.41 ? 598  TRP A C   1 
ATOM   4733 O  O   . TRP A 1 598  ? 38.483 89.364  -20.773 1.00 25.55 ? 598  TRP A O   1 
ATOM   4734 C  CB  . TRP A 1 598  ? 37.167 87.471  -23.046 1.00 20.50 ? 598  TRP A CB  1 
ATOM   4735 C  CG  . TRP A 1 598  ? 37.104 86.727  -24.335 1.00 19.20 ? 598  TRP A CG  1 
ATOM   4736 C  CD1 . TRP A 1 598  ? 38.036 85.860  -24.860 1.00 18.11 ? 598  TRP A CD1 1 
ATOM   4737 C  CD2 . TRP A 1 598  ? 36.061 86.809  -25.287 1.00 18.33 ? 598  TRP A CD2 1 
ATOM   4738 N  NE1 . TRP A 1 598  ? 37.629 85.390  -26.099 1.00 18.30 ? 598  TRP A NE1 1 
ATOM   4739 C  CE2 . TRP A 1 598  ? 36.415 85.966  -26.381 1.00 18.10 ? 598  TRP A CE2 1 
ATOM   4740 C  CE3 . TRP A 1 598  ? 34.850 87.519  -25.335 1.00 18.48 ? 598  TRP A CE3 1 
ATOM   4741 C  CZ2 . TRP A 1 598  ? 35.612 85.820  -27.491 1.00 18.45 ? 598  TRP A CZ2 1 
ATOM   4742 C  CZ3 . TRP A 1 598  ? 34.054 87.367  -26.455 1.00 18.64 ? 598  TRP A CZ3 1 
ATOM   4743 C  CH2 . TRP A 1 598  ? 34.442 86.522  -27.518 1.00 18.56 ? 598  TRP A CH2 1 
ATOM   4744 N  N   . HIS A 1 599  ? 37.116 90.591  -22.031 1.00 29.77 ? 599  HIS A N   1 
ATOM   4745 C  CA  . HIS A 1 599  ? 36.864 91.536  -20.956 1.00 35.16 ? 599  HIS A CA  1 
ATOM   4746 C  C   . HIS A 1 599  ? 35.408 91.899  -20.894 1.00 37.96 ? 599  HIS A C   1 
ATOM   4747 O  O   . HIS A 1 599  ? 34.729 91.895  -21.931 1.00 37.98 ? 599  HIS A O   1 
ATOM   4748 C  CB  . HIS A 1 599  ? 37.672 92.818  -21.179 1.00 36.81 ? 599  HIS A CB  1 
ATOM   4749 C  CG  . HIS A 1 599  ? 39.151 92.594  -21.192 1.00 39.35 ? 599  HIS A CG  1 
ATOM   4750 N  ND1 . HIS A 1 599  ? 39.875 92.339  -20.045 1.00 39.95 ? 599  HIS A ND1 1 
ATOM   4751 C  CD2 . HIS A 1 599  ? 40.030 92.500  -22.222 1.00 39.85 ? 599  HIS A CD2 1 
ATOM   4752 C  CE1 . HIS A 1 599  ? 41.133 92.090  -20.367 1.00 40.00 ? 599  HIS A CE1 1 
ATOM   4753 N  NE2 . HIS A 1 599  ? 41.255 92.179  -21.681 1.00 40.07 ? 599  HIS A NE2 1 
ATOM   4754 N  N   . HIS A 1 600  ? 34.909 92.153  -19.685 1.00 41.92 ? 600  HIS A N   1 
ATOM   4755 C  CA  . HIS A 1 600  ? 33.534 92.604  -19.587 1.00 45.50 ? 600  HIS A CA  1 
ATOM   4756 C  C   . HIS A 1 600  ? 33.711 94.095  -19.673 1.00 46.70 ? 600  HIS A C   1 
ATOM   4757 O  O   . HIS A 1 600  ? 34.339 94.714  -18.804 1.00 46.47 ? 600  HIS A O   1 
ATOM   4758 C  CB  . HIS A 1 600  ? 32.818 92.284  -18.275 1.00 47.63 ? 600  HIS A CB  1 
ATOM   4759 C  CG  . HIS A 1 600  ? 31.473 92.951  -18.186 1.00 51.12 ? 600  HIS A CG  1 
ATOM   4760 N  ND1 . HIS A 1 600  ? 30.588 92.975  -19.248 1.00 52.74 ? 600  HIS A ND1 1 
ATOM   4761 C  CD2 . HIS A 1 600  ? 30.892 93.682  -17.202 1.00 52.87 ? 600  HIS A CD2 1 
ATOM   4762 C  CE1 . HIS A 1 600  ? 29.525 93.691  -18.925 1.00 53.21 ? 600  HIS A CE1 1 
ATOM   4763 N  NE2 . HIS A 1 600  ? 29.683 94.134  -17.689 1.00 53.49 ? 600  HIS A NE2 1 
ATOM   4764 N  N   . ASP A 1 601  ? 33.186 94.660  -20.747 1.00 47.62 ? 601  ASP A N   1 
ATOM   4765 C  CA  . ASP A 1 601  ? 33.293 96.078  -20.973 1.00 49.25 ? 601  ASP A CA  1 
ATOM   4766 C  C   . ASP A 1 601  ? 32.161 96.750  -20.193 1.00 49.69 ? 601  ASP A C   1 
ATOM   4767 O  O   . ASP A 1 601  ? 31.025 96.785  -20.662 1.00 49.92 ? 601  ASP A O   1 
ATOM   4768 C  CB  . ASP A 1 601  ? 33.151 96.352  -22.469 1.00 50.24 ? 601  ASP A CB  1 
ATOM   4769 C  CG  . ASP A 1 601  ? 33.719 97.696  -22.875 1.00 51.24 ? 601  ASP A CG  1 
ATOM   4770 O  OD1 . ASP A 1 601  ? 33.639 98.651  -22.067 1.00 52.59 ? 601  ASP A OD1 1 
ATOM   4771 O  OD2 . ASP A 1 601  ? 34.230 97.796  -24.014 1.00 51.47 ? 601  ASP A OD2 1 
ATOM   4772 N  N   . THR A 1 602  ? 32.469 97.268  -19.004 1.00 50.16 ? 602  THR A N   1 
ATOM   4773 C  CA  . THR A 1 602  ? 31.454 97.930  -18.174 1.00 50.45 ? 602  THR A CA  1 
ATOM   4774 C  C   . THR A 1 602  ? 30.923 99.194  -18.834 1.00 49.79 ? 602  THR A C   1 
ATOM   4775 O  O   . THR A 1 602  ? 29.917 99.748  -18.393 1.00 50.60 ? 602  THR A O   1 
ATOM   4776 C  CB  . THR A 1 602  ? 31.998 98.301  -16.765 1.00 51.31 ? 602  THR A CB  1 
ATOM   4777 O  OG1 . THR A 1 602  ? 33.285 98.934  -16.891 1.00 52.00 ? 602  THR A OG1 1 
ATOM   4778 C  CG2 . THR A 1 602  ? 32.095 97.061  -15.885 1.00 51.31 ? 602  THR A CG2 1 
ATOM   4779 N  N   . LEU A 1 603  ? 31.608 99.648  -19.882 1.00 48.62 ? 603  LEU A N   1 
ATOM   4780 C  CA  . LEU A 1 603  ? 31.198 100.841 -20.622 1.00 46.92 ? 603  LEU A CA  1 
ATOM   4781 C  C   . LEU A 1 603  ? 30.179 100.483 -21.704 1.00 44.79 ? 603  LEU A C   1 
ATOM   4782 O  O   . LEU A 1 603  ? 29.102 101.068 -21.762 1.00 44.84 ? 603  LEU A O   1 
ATOM   4783 C  CB  . LEU A 1 603  ? 32.408 101.533 -21.270 1.00 48.24 ? 603  LEU A CB  1 
ATOM   4784 C  CG  . LEU A 1 603  ? 33.351 102.343 -20.374 1.00 49.50 ? 603  LEU A CG  1 
ATOM   4785 C  CD1 . LEU A 1 603  ? 32.555 103.441 -19.669 1.00 50.46 ? 603  LEU A CD1 1 
ATOM   4786 C  CD2 . LEU A 1 603  ? 34.027 101.430 -19.350 1.00 50.76 ? 603  LEU A CD2 1 
ATOM   4787 N  N   . THR A 1 604  ? 30.515 99.513  -22.554 1.00 41.83 ? 604  THR A N   1 
ATOM   4788 C  CA  . THR A 1 604  ? 29.607 99.094  -23.622 1.00 38.07 ? 604  THR A CA  1 
ATOM   4789 C  C   . THR A 1 604  ? 28.615 98.001  -23.226 1.00 35.28 ? 604  THR A C   1 
ATOM   4790 O  O   . THR A 1 604  ? 27.664 97.750  -23.962 1.00 33.38 ? 604  THR A O   1 
ATOM   4791 C  CB  . THR A 1 604  ? 30.381 98.571  -24.848 1.00 38.84 ? 604  THR A CB  1 
ATOM   4792 O  OG1 . THR A 1 604  ? 31.136 97.398  -24.480 1.00 38.47 ? 604  THR A OG1 1 
ATOM   4793 C  CG2 . THR A 1 604  ? 31.320 99.650  -25.382 1.00 38.73 ? 604  THR A CG2 1 
ATOM   4794 N  N   . LYS A 1 605  ? 28.852 97.348  -22.087 1.00 33.18 ? 605  LYS A N   1 
ATOM   4795 C  CA  . LYS A 1 605  ? 28.006 96.247  -21.601 1.00 32.10 ? 605  LYS A CA  1 
ATOM   4796 C  C   . LYS A 1 605  ? 28.017 95.053  -22.554 1.00 31.09 ? 605  LYS A C   1 
ATOM   4797 O  O   . LYS A 1 605  ? 26.978 94.457  -22.887 1.00 30.23 ? 605  LYS A O   1 
ATOM   4798 C  CB  . LYS A 1 605  ? 26.570 96.711  -21.354 1.00 33.71 ? 605  LYS A CB  1 
ATOM   4799 C  CG  . LYS A 1 605  ? 26.446 97.753  -20.257 1.00 36.39 ? 605  LYS A CG  1 
ATOM   4800 C  CD  . LYS A 1 605  ? 27.086 97.266  -18.937 1.00 37.91 ? 605  LYS A CD  1 
ATOM   4801 C  CE  . LYS A 1 605  ? 26.907 98.274  -17.813 1.00 39.25 ? 605  LYS A CE  1 
ATOM   4802 N  NZ  . LYS A 1 605  ? 27.378 99.626  -18.217 1.00 40.21 ? 605  LYS A NZ  1 
ATOM   4803 N  N   . THR A 1 606  ? 29.215 94.719  -23.013 1.00 28.43 ? 606  THR A N   1 
ATOM   4804 C  CA  . THR A 1 606  ? 29.396 93.570  -23.895 1.00 26.66 ? 606  THR A CA  1 
ATOM   4805 C  C   . THR A 1 606  ? 30.642 92.854  -23.401 1.00 24.86 ? 606  THR A C   1 
ATOM   4806 O  O   . THR A 1 606  ? 31.456 93.434  -22.705 1.00 24.67 ? 606  THR A O   1 
ATOM   4807 C  CB  . THR A 1 606  ? 29.623 93.983  -25.394 1.00 26.69 ? 606  THR A CB  1 
ATOM   4808 O  OG1 . THR A 1 606  ? 30.840 94.740  -25.507 1.00 25.80 ? 606  THR A OG1 1 
ATOM   4809 C  CG2 . THR A 1 606  ? 28.445 94.796  -25.921 1.00 26.25 ? 606  THR A CG2 1 
ATOM   4810 N  N   . ILE A 1 607  ? 30.730 91.572  -23.720 1.00 24.35 ? 607  ILE A N   1 
ATOM   4811 C  CA  . ILE A 1 607  ? 31.870 90.718  -23.383 1.00 22.22 ? 607  ILE A CA  1 
ATOM   4812 C  C   . ILE A 1 607  ? 32.508 90.521  -24.760 1.00 22.36 ? 607  ILE A C   1 
ATOM   4813 O  O   . ILE A 1 607  ? 31.934 89.879  -25.672 1.00 21.71 ? 607  ILE A O   1 
ATOM   4814 C  CB  . ILE A 1 607  ? 31.362 89.386  -22.780 1.00 22.54 ? 607  ILE A CB  1 
ATOM   4815 C  CG1 . ILE A 1 607  ? 30.514 89.676  -21.515 1.00 22.40 ? 607  ILE A CG1 1 
ATOM   4816 C  CG2 . ILE A 1 607  ? 32.535 88.465  -22.450 1.00 22.30 ? 607  ILE A CG2 1 
ATOM   4817 C  CD1 . ILE A 1 607  ? 29.510 88.527  -21.173 1.00 23.37 ? 607  ILE A CD1 1 
ATOM   4818 N  N   . HIS A 1 608  ? 33.698 91.087  -24.941 1.00 21.60 ? 608  HIS A N   1 
ATOM   4819 C  CA  . HIS A 1 608  ? 34.315 91.006  -26.253 1.00 23.25 ? 608  HIS A CA  1 
ATOM   4820 C  C   . HIS A 1 608  ? 35.795 90.836  -26.104 1.00 21.89 ? 608  HIS A C   1 
ATOM   4821 O  O   . HIS A 1 608  ? 36.355 91.168  -25.079 1.00 22.25 ? 608  HIS A O   1 
ATOM   4822 C  CB  . HIS A 1 608  ? 34.026 92.261  -27.042 1.00 26.18 ? 608  HIS A CB  1 
ATOM   4823 C  CG  . HIS A 1 608  ? 34.633 93.469  -26.439 1.00 28.37 ? 608  HIS A CG  1 
ATOM   4824 N  ND1 . HIS A 1 608  ? 35.645 94.267  -26.860 1.00 30.31 ? 608  HIS A ND1 1 
ATOM   4825 C  CD2 . HIS A 1 608  ? 34.251 93.945  -25.204 1.00 30.35 ? 608  HIS A CD2 1 
ATOM   4826 C  CE1 . HIS A 1 608  ? 35.854 95.204  -25.871 1.00 31.43 ? 608  HIS A CE1 1 
ATOM   4827 N  NE2 . HIS A 1 608  ? 35.000 94.988  -24.884 1.00 31.69 ? 608  HIS A NE2 1 
ATOM   4828 N  N   . PRO A 1 609  ? 36.434 90.328  -27.139 1.00 20.58 ? 609  PRO A N   1 
ATOM   4829 C  CA  . PRO A 1 609  ? 37.874 90.087  -27.109 1.00 20.53 ? 609  PRO A CA  1 
ATOM   4830 C  C   . PRO A 1 609  ? 38.754 91.265  -27.476 1.00 22.66 ? 609  PRO A C   1 
ATOM   4831 O  O   . PRO A 1 609  ? 38.392 92.093  -28.352 1.00 24.07 ? 609  PRO A O   1 
ATOM   4832 C  CB  . PRO A 1 609  ? 38.042 88.952  -28.096 1.00 21.54 ? 609  PRO A CB  1 
ATOM   4833 C  CG  . PRO A 1 609  ? 37.040 89.324  -29.167 1.00 20.88 ? 609  PRO A CG  1 
ATOM   4834 C  CD  . PRO A 1 609  ? 35.861 89.996  -28.457 1.00 20.77 ? 609  PRO A CD  1 
ATOM   4835 N  N   . GLN A 1 610  ? 39.904 91.340  -26.813 1.00 20.94 ? 610  GLN A N   1 
ATOM   4836 C  CA  . GLN A 1 610  ? 40.892 92.403  -27.099 1.00 20.88 ? 610  GLN A CA  1 
ATOM   4837 C  C   . GLN A 1 610  ? 42.109 91.624  -27.536 1.00 18.98 ? 610  GLN A C   1 
ATOM   4838 O  O   . GLN A 1 610  ? 42.392 90.579  -26.961 1.00 17.83 ? 610  GLN A O   1 
ATOM   4839 C  CB  . GLN A 1 610  ? 41.259 93.199  -25.834 1.00 24.07 ? 610  GLN A CB  1 
ATOM   4840 C  CG  . GLN A 1 610  ? 40.289 94.321  -25.468 1.00 31.24 ? 610  GLN A CG  1 
ATOM   4841 C  CD  . GLN A 1 610  ? 40.714 95.089  -24.196 1.00 35.15 ? 610  GLN A CD  1 
ATOM   4842 O  OE1 . GLN A 1 610  ? 41.732 94.575  -23.492 1.00 38.22 ? 610  GLN A OE1 1 
ATOM   4843 N  NE2 . GLN A 1 610  ? 40.128 96.129  -23.855 1.00 36.57 ? 610  GLN A NE2 1 
ATOM   4844 N  N   . GLY A 1 611  ? 42.798 92.094  -28.558 1.00 18.00 ? 611  GLY A N   1 
ATOM   4845 C  CA  . GLY A 1 611  ? 43.985 91.428  -29.057 1.00 18.68 ? 611  GLY A CA  1 
ATOM   4846 C  C   . GLY A 1 611  ? 45.237 92.118  -28.554 1.00 19.25 ? 611  GLY A C   1 
ATOM   4847 O  O   . GLY A 1 611  ? 45.307 93.365  -28.511 1.00 19.78 ? 611  GLY A O   1 
ATOM   4848 N  N   . SER A 1 612  ? 46.222 91.331  -28.139 1.00 18.72 ? 612  SER A N   1 
ATOM   4849 C  CA  . SER A 1 612  ? 47.476 91.911  -27.652 1.00 18.92 ? 612  SER A CA  1 
ATOM   4850 C  C   . SER A 1 612  ? 48.225 92.632  -28.747 1.00 18.87 ? 612  SER A C   1 
ATOM   4851 O  O   . SER A 1 612  ? 48.278 92.171  -29.876 1.00 18.70 ? 612  SER A O   1 
ATOM   4852 C  CB  . SER A 1 612  ? 48.426 90.824  -27.152 1.00 16.14 ? 612  SER A CB  1 
ATOM   4853 O  OG  . SER A 1 612  ? 49.670 91.430  -26.791 1.00 18.47 ? 612  SER A OG  1 
ATOM   4854 N  N   . THR A 1 613  ? 48.824 93.781  -28.401 1.00 20.71 ? 613  THR A N   1 
ATOM   4855 C  CA  . THR A 1 613  ? 49.635 94.523  -29.390 1.00 22.51 ? 613  THR A CA  1 
ATOM   4856 C  C   . THR A 1 613  ? 51.093 94.410  -28.930 1.00 23.40 ? 613  THR A C   1 
ATOM   4857 O  O   . THR A 1 613  ? 51.967 95.167  -29.409 1.00 24.27 ? 613  THR A O   1 
ATOM   4858 C  CB  . THR A 1 613  ? 49.358 96.044  -29.425 1.00 22.64 ? 613  THR A CB  1 
ATOM   4859 O  OG1 . THR A 1 613  ? 49.807 96.644  -28.185 1.00 24.97 ? 613  THR A OG1 1 
ATOM   4860 C  CG2 . THR A 1 613  ? 47.846 96.314  -29.594 1.00 21.92 ? 613  THR A CG2 1 
ATOM   4861 N  N   . THR A 1 614  ? 51.375 93.503  -27.998 1.00 24.56 ? 614  THR A N   1 
ATOM   4862 C  CA  . THR A 1 614  ? 52.759 93.375  -27.524 1.00 24.38 ? 614  THR A CA  1 
ATOM   4863 C  C   . THR A 1 614  ? 53.265 91.938  -27.429 1.00 24.91 ? 614  THR A C   1 
ATOM   4864 O  O   . THR A 1 614  ? 54.433 91.731  -27.075 1.00 25.60 ? 614  THR A O   1 
ATOM   4865 C  CB  . THR A 1 614  ? 52.924 94.069  -26.186 1.00 26.08 ? 614  THR A CB  1 
ATOM   4866 O  OG1 . THR A 1 614  ? 52.187 93.361  -25.170 1.00 26.77 ? 614  THR A OG1 1 
ATOM   4867 C  CG2 . THR A 1 614  ? 52.381 95.484  -26.296 1.00 26.76 ? 614  THR A CG2 1 
ATOM   4868 N  N   . LYS A 1 615  ? 52.415 90.956  -27.751 1.00 22.79 ? 615  LYS A N   1 
ATOM   4869 C  CA  . LYS A 1 615  ? 52.823 89.551  -27.706 1.00 20.81 ? 615  LYS A CA  1 
ATOM   4870 C  C   . LYS A 1 615  ? 51.901 88.669  -28.582 1.00 20.44 ? 615  LYS A C   1 
ATOM   4871 O  O   . LYS A 1 615  ? 50.774 89.067  -28.892 1.00 18.88 ? 615  LYS A O   1 
ATOM   4872 C  CB  . LYS A 1 615  ? 52.941 89.089  -26.222 1.00 21.28 ? 615  LYS A CB  1 
ATOM   4873 C  CG  . LYS A 1 615  ? 51.659 88.782  -25.484 1.00 21.36 ? 615  LYS A CG  1 
ATOM   4874 C  CD  . LYS A 1 615  ? 51.940 88.540  -23.979 1.00 21.75 ? 615  LYS A CD  1 
ATOM   4875 C  CE  . LYS A 1 615  ? 50.691 88.008  -23.300 1.00 22.77 ? 615  LYS A CE  1 
ATOM   4876 N  NZ  . LYS A 1 615  ? 50.663 88.140  -21.801 1.00 21.69 ? 615  LYS A NZ  1 
ATOM   4877 N  N   . TYR A 1 616  ? 52.409 87.511  -29.020 1.00 18.08 ? 616  TYR A N   1 
ATOM   4878 C  CA  . TYR A 1 616  ? 51.730 86.580  -29.945 1.00 16.64 ? 616  TYR A CA  1 
ATOM   4879 C  C   . TYR A 1 616  ? 51.906 85.116  -29.544 1.00 17.97 ? 616  TYR A C   1 
ATOM   4880 O  O   . TYR A 1 616  ? 52.796 84.835  -28.736 1.00 18.99 ? 616  TYR A O   1 
ATOM   4881 C  CB  . TYR A 1 616  ? 52.329 86.747  -31.370 1.00 19.60 ? 616  TYR A CB  1 
ATOM   4882 C  CG  . TYR A 1 616  ? 52.486 88.212  -31.765 1.00 22.33 ? 616  TYR A CG  1 
ATOM   4883 C  CD1 . TYR A 1 616  ? 53.613 88.926  -31.399 1.00 21.93 ? 616  TYR A CD1 1 
ATOM   4884 C  CD2 . TYR A 1 616  ? 51.416 88.911  -32.353 1.00 23.66 ? 616  TYR A CD2 1 
ATOM   4885 C  CE1 . TYR A 1 616  ? 53.687 90.332  -31.586 1.00 25.11 ? 616  TYR A CE1 1 
ATOM   4886 C  CE2 . TYR A 1 616  ? 51.471 90.297  -32.541 1.00 24.89 ? 616  TYR A CE2 1 
ATOM   4887 C  CZ  . TYR A 1 616  ? 52.603 90.994  -32.154 1.00 26.26 ? 616  TYR A CZ  1 
ATOM   4888 O  OH  . TYR A 1 616  ? 52.660 92.370  -32.325 1.00 30.83 ? 616  TYR A OH  1 
ATOM   4889 N  N   . ARG A 1 617  ? 51.112 84.208  -30.121 1.00 14.58 ? 617  ARG A N   1 
ATOM   4890 C  CA  . ARG A 1 617  ? 51.193 82.749  -29.835 1.00 15.88 ? 617  ARG A CA  1 
ATOM   4891 C  C   . ARG A 1 617  ? 51.770 81.949  -31.005 1.00 15.61 ? 617  ARG A C   1 
ATOM   4892 O  O   . ARG A 1 617  ? 51.263 82.075  -32.119 1.00 16.37 ? 617  ARG A O   1 
ATOM   4893 C  CB  . ARG A 1 617  ? 49.805 82.125  -29.577 1.00 16.57 ? 617  ARG A CB  1 
ATOM   4894 C  CG  . ARG A 1 617  ? 49.074 82.389  -28.288 1.00 20.05 ? 617  ARG A CG  1 
ATOM   4895 C  CD  . ARG A 1 617  ? 47.650 81.673  -28.288 1.00 20.22 ? 617  ARG A CD  1 
ATOM   4896 N  NE  . ARG A 1 617  ? 47.680 80.203  -28.291 1.00 20.46 ? 617  ARG A NE  1 
ATOM   4897 C  CZ  . ARG A 1 617  ? 47.039 79.450  -29.189 1.00 20.91 ? 617  ARG A CZ  1 
ATOM   4898 N  NH1 . ARG A 1 617  ? 46.313 80.026  -30.151 1.00 20.77 ? 617  ARG A NH1 1 
ATOM   4899 N  NH2 . ARG A 1 617  ? 47.136 78.127  -29.172 1.00 19.03 ? 617  ARG A NH2 1 
ATOM   4900 N  N   . ILE A 1 618  ? 52.805 81.125  -30.784 1.00 13.77 ? 618  ILE A N   1 
ATOM   4901 C  CA  . ILE A 1 618  ? 53.305 80.253  -31.823 1.00 15.08 ? 618  ILE A CA  1 
ATOM   4902 C  C   . ILE A 1 618  ? 52.919 78.854  -31.408 1.00 15.97 ? 618  ILE A C   1 
ATOM   4903 O  O   . ILE A 1 618  ? 52.994 78.524  -30.216 1.00 17.19 ? 618  ILE A O   1 
ATOM   4904 C  CB  . ILE A 1 618  ? 54.824 80.432  -32.065 1.00 14.63 ? 618  ILE A CB  1 
ATOM   4905 C  CG1 . ILE A 1 618  ? 55.215 79.617  -33.271 1.00 17.99 ? 618  ILE A CG1 1 
ATOM   4906 C  CG2 . ILE A 1 618  ? 55.662 80.092  -30.830 1.00 17.22 ? 618  ILE A CG2 1 
ATOM   4907 C  CD1 . ILE A 1 618  ? 56.442 80.066  -33.909 1.00 17.04 ? 618  ILE A CD1 1 
ATOM   4908 N  N   . ILE A 1 619  ? 52.473 78.071  -32.382 1.00 14.58 ? 619  ILE A N   1 
ATOM   4909 C  CA  . ILE A 1 619  ? 51.980 76.708  -32.188 1.00 14.42 ? 619  ILE A CA  1 
ATOM   4910 C  C   . ILE A 1 619  ? 52.724 75.759  -33.105 1.00 12.96 ? 619  ILE A C   1 
ATOM   4911 O  O   . ILE A 1 619  ? 52.886 76.060  -34.287 1.00 14.73 ? 619  ILE A O   1 
ATOM   4912 C  CB  . ILE A 1 619  ? 50.441 76.649  -32.597 1.00 16.19 ? 619  ILE A CB  1 
ATOM   4913 C  CG1 . ILE A 1 619  ? 49.658 77.616  -31.747 1.00 18.89 ? 619  ILE A CG1 1 
ATOM   4914 C  CG2 . ILE A 1 619  ? 49.841 75.249  -32.491 1.00 16.74 ? 619  ILE A CG2 1 
ATOM   4915 C  CD1 . ILE A 1 619  ? 48.318 78.137  -32.427 1.00 18.90 ? 619  ILE A CD1 1 
ATOM   4916 N  N   . PHE A 1 620  ? 53.169 74.606  -32.629 1.00 12.12 ? 620  PHE A N   1 
ATOM   4917 C  CA  . PHE A 1 620  ? 53.779 73.632  -33.509 1.00 11.00 ? 620  PHE A CA  1 
ATOM   4918 C  C   . PHE A 1 620  ? 53.615 72.257  -32.926 1.00 13.42 ? 620  PHE A C   1 
ATOM   4919 O  O   . PHE A 1 620  ? 53.321 72.132  -31.732 1.00 12.89 ? 620  PHE A O   1 
ATOM   4920 C  CB  . PHE A 1 620  ? 55.258 73.872  -33.763 1.00 11.96 ? 620  PHE A CB  1 
ATOM   4921 C  CG  . PHE A 1 620  ? 56.094 73.821  -32.558 1.00 10.94 ? 620  PHE A CG  1 
ATOM   4922 C  CD1 . PHE A 1 620  ? 56.206 74.916  -31.734 1.00 9.47  ? 620  PHE A CD1 1 
ATOM   4923 C  CD2 . PHE A 1 620  ? 56.803 72.645  -32.234 1.00 12.00 ? 620  PHE A CD2 1 
ATOM   4924 C  CE1 . PHE A 1 620  ? 57.036 74.893  -30.555 1.00 13.25 ? 620  PHE A CE1 1 
ATOM   4925 C  CE2 . PHE A 1 620  ? 57.640 72.623  -31.044 1.00 11.62 ? 620  PHE A CE2 1 
ATOM   4926 C  CZ  . PHE A 1 620  ? 57.740 73.731  -30.247 1.00 11.89 ? 620  PHE A CZ  1 
ATOM   4927 N  N   . LYS A 1 621  ? 53.790 71.235  -33.743 1.00 13.04 ? 621  LYS A N   1 
ATOM   4928 C  CA  . LYS A 1 621  ? 53.651 69.883  -33.262 1.00 14.30 ? 621  LYS A CA  1 
ATOM   4929 C  C   . LYS A 1 621  ? 54.951 69.353  -32.682 1.00 14.03 ? 621  LYS A C   1 
ATOM   4930 O  O   . LYS A 1 621  ? 55.973 69.244  -33.371 1.00 14.47 ? 621  LYS A O   1 
ATOM   4931 C  CB  . LYS A 1 621  ? 53.153 69.012  -34.406 1.00 15.64 ? 621  LYS A CB  1 
ATOM   4932 C  CG  . LYS A 1 621  ? 52.765 67.594  -33.992 1.00 18.25 ? 621  LYS A CG  1 
ATOM   4933 C  CD  . LYS A 1 621  ? 51.865 67.014  -35.051 1.00 21.44 ? 621  LYS A CD  1 
ATOM   4934 C  CE  . LYS A 1 621  ? 52.645 66.731  -36.326 1.00 21.96 ? 621  LYS A CE  1 
ATOM   4935 N  NZ  . LYS A 1 621  ? 51.793 66.156  -37.493 1.00 25.01 ? 621  LYS A NZ  1 
ATOM   4936 N  N   . ALA A 1 622  ? 54.923 69.048  -31.399 1.00 12.06 ? 622  ALA A N   1 
ATOM   4937 C  CA  . ALA A 1 622  ? 56.105 68.452  -30.747 1.00 11.42 ? 622  ALA A CA  1 
ATOM   4938 C  C   . ALA A 1 622  ? 55.962 66.945  -30.799 1.00 12.09 ? 622  ALA A C   1 
ATOM   4939 O  O   . ALA A 1 622  ? 54.856 66.431  -30.620 1.00 13.11 ? 622  ALA A O   1 
ATOM   4940 C  CB  . ALA A 1 622  ? 56.176 68.908  -29.304 1.00 12.00 ? 622  ALA A CB  1 
ATOM   4941 N  N   . ARG A 1 623  ? 57.071 66.243  -30.999 1.00 11.50 ? 623  ARG A N   1 
ATOM   4942 C  CA  . ARG A 1 623  ? 57.087 64.763  -31.059 1.00 12.25 ? 623  ARG A CA  1 
ATOM   4943 C  C   . ARG A 1 623  ? 58.075 64.383  -29.934 1.00 13.67 ? 623  ARG A C   1 
ATOM   4944 O  O   . ARG A 1 623  ? 59.266 64.762  -29.972 1.00 15.35 ? 623  ARG A O   1 
ATOM   4945 C  CB  . ARG A 1 623  ? 57.591 64.241  -32.419 1.00 12.87 ? 623  ARG A CB  1 
ATOM   4946 C  CG  . ARG A 1 623  ? 57.601 62.703  -32.523 1.00 16.02 ? 623  ARG A CG  1 
ATOM   4947 C  CD  . ARG A 1 623  ? 57.561 62.135  -33.987 1.00 19.17 ? 623  ARG A CD  1 
ATOM   4948 N  NE  . ARG A 1 623  ? 57.576 60.676  -33.992 1.00 19.36 ? 623  ARG A NE  1 
ATOM   4949 C  CZ  . ARG A 1 623  ? 58.677 59.949  -33.910 1.00 20.10 ? 623  ARG A CZ  1 
ATOM   4950 N  NH1 . ARG A 1 623  ? 59.857 60.551  -33.855 1.00 22.88 ? 623  ARG A NH1 1 
ATOM   4951 N  NH2 . ARG A 1 623  ? 58.596 58.626  -33.774 1.00 18.51 ? 623  ARG A NH2 1 
ATOM   4952 N  N   . VAL A 1 624  ? 57.586 63.631  -28.953 1.00 10.65 ? 624  VAL A N   1 
ATOM   4953 C  CA  . VAL A 1 624  ? 58.412 63.319  -27.788 1.00 12.21 ? 624  VAL A CA  1 
ATOM   4954 C  C   . VAL A 1 624  ? 58.459 61.839  -27.513 1.00 12.23 ? 624  VAL A C   1 
ATOM   4955 O  O   . VAL A 1 624  ? 57.430 61.195  -27.575 1.00 11.02 ? 624  VAL A O   1 
ATOM   4956 C  CB  . VAL A 1 624  ? 57.813 64.059  -26.570 1.00 11.37 ? 624  VAL A CB  1 
ATOM   4957 C  CG1 . VAL A 1 624  ? 58.837 64.042  -25.425 1.00 10.67 ? 624  VAL A CG1 1 
ATOM   4958 C  CG2 . VAL A 1 624  ? 57.486 65.549  -26.970 1.00 12.70 ? 624  VAL A CG2 1 
ATOM   4959 N  N   . PRO A 1 625  ? 59.655 61.283  -27.207 1.00 11.79 ? 625  PRO A N   1 
ATOM   4960 C  CA  . PRO A 1 625  ? 59.761 59.836  -26.937 1.00 10.97 ? 625  PRO A CA  1 
ATOM   4961 C  C   . PRO A 1 625  ? 58.949 59.378  -25.717 1.00 11.57 ? 625  PRO A C   1 
ATOM   4962 O  O   . PRO A 1 625  ? 58.519 60.204  -24.895 1.00 11.86 ? 625  PRO A O   1 
ATOM   4963 C  CB  . PRO A 1 625  ? 61.281 59.604  -26.652 1.00 13.75 ? 625  PRO A CB  1 
ATOM   4964 C  CG  . PRO A 1 625  ? 61.932 60.803  -27.225 1.00 12.79 ? 625  PRO A CG  1 
ATOM   4965 C  CD  . PRO A 1 625  ? 60.946 61.950  -27.037 1.00 11.03 ? 625  PRO A CD  1 
ATOM   4966 N  N   . PRO A 1 626  ? 58.782 58.062  -25.595 1.00 12.12 ? 626  PRO A N   1 
ATOM   4967 C  CA  . PRO A 1 626  ? 58.024 57.553  -24.416 1.00 11.29 ? 626  PRO A CA  1 
ATOM   4968 C  C   . PRO A 1 626  ? 58.789 57.956  -23.153 1.00 10.51 ? 626  PRO A C   1 
ATOM   4969 O  O   . PRO A 1 626  ? 60.039 57.794  -23.046 1.00 12.27 ? 626  PRO A O   1 
ATOM   4970 C  CB  . PRO A 1 626  ? 58.067 56.024  -24.589 1.00 11.01 ? 626  PRO A CB  1 
ATOM   4971 C  CG  . PRO A 1 626  ? 58.476 55.792  -26.087 1.00 11.75 ? 626  PRO A CG  1 
ATOM   4972 C  CD  . PRO A 1 626  ? 59.448 56.952  -26.286 1.00 12.80 ? 626  PRO A CD  1 
ATOM   4973 N  N   . MET A 1 627  ? 58.087 58.519  -22.169 1.00 11.58 ? 627  MET A N   1 
ATOM   4974 C  CA  . MET A 1 627  ? 58.695 58.913  -20.869 1.00 8.98  ? 627  MET A CA  1 
ATOM   4975 C  C   . MET A 1 627  ? 59.977 59.680  -21.076 1.00 9.66  ? 627  MET A C   1 
ATOM   4976 O  O   . MET A 1 627  ? 61.003 59.508  -20.350 1.00 10.21 ? 627  MET A O   1 
ATOM   4977 C  CB  . MET A 1 627  ? 59.011 57.640  -20.042 1.00 10.15 ? 627  MET A CB  1 
ATOM   4978 C  CG  . MET A 1 627  ? 57.706 56.959  -19.618 1.00 10.95 ? 627  MET A CG  1 
ATOM   4979 S  SD  . MET A 1 627  ? 57.938 55.294  -18.905 1.00 13.70 ? 627  MET A SD  1 
ATOM   4980 C  CE  . MET A 1 627  ? 58.628 55.651  -17.421 1.00 13.76 ? 627  MET A CE  1 
ATOM   4981 N  N   . GLY A 1 628  ? 59.896 60.575  -22.066 1.00 8.25  ? 628  GLY A N   1 
ATOM   4982 C  CA  . GLY A 1 628  ? 61.102 61.314  -22.442 1.00 9.19  ? 628  GLY A CA  1 
ATOM   4983 C  C   . GLY A 1 628  ? 60.998 62.788  -22.716 1.00 9.28  ? 628  GLY A C   1 
ATOM   4984 O  O   . GLY A 1 628  ? 59.978 63.394  -22.424 1.00 11.92 ? 628  GLY A O   1 
ATOM   4985 N  N   . LEU A 1 629  ? 62.037 63.340  -23.359 1.00 11.25 ? 629  LEU A N   1 
ATOM   4986 C  CA  . LEU A 1 629  ? 62.192 64.797  -23.608 1.00 11.44 ? 629  LEU A CA  1 
ATOM   4987 C  C   . LEU A 1 629  ? 62.586 65.080  -25.054 1.00 12.23 ? 629  LEU A C   1 
ATOM   4988 O  O   . LEU A 1 629  ? 63.270 64.245  -25.696 1.00 11.11 ? 629  LEU A O   1 
ATOM   4989 C  CB  . LEU A 1 629  ? 63.298 65.301  -22.721 1.00 10.57 ? 629  LEU A CB  1 
ATOM   4990 C  CG  . LEU A 1 629  ? 63.036 65.214  -21.197 1.00 8.30  ? 629  LEU A CG  1 
ATOM   4991 C  CD1 . LEU A 1 629  ? 64.363 65.444  -20.403 1.00 10.39 ? 629  LEU A CD1 1 
ATOM   4992 C  CD2 . LEU A 1 629  ? 61.899 66.212  -20.869 1.00 11.83 ? 629  LEU A CD2 1 
ATOM   4993 N  N   . ALA A 1 630  ? 62.128 66.232  -25.557 1.00 10.84 ? 630  ALA A N   1 
ATOM   4994 C  CA  . ALA A 1 630  ? 62.508 66.651  -26.923 1.00 12.37 ? 630  ALA A CA  1 
ATOM   4995 C  C   . ALA A 1 630  ? 62.769 68.180  -26.850 1.00 11.16 ? 630  ALA A C   1 
ATOM   4996 O  O   . ALA A 1 630  ? 61.986 68.938  -26.288 1.00 11.99 ? 630  ALA A O   1 
ATOM   4997 C  CB  . ALA A 1 630  ? 61.412 66.371  -27.935 1.00 11.67 ? 630  ALA A CB  1 
ATOM   4998 N  N   . THR A 1 631  ? 63.865 68.633  -27.481 1.00 10.96 ? 631  THR A N   1 
ATOM   4999 C  CA  . THR A 1 631  ? 64.277 70.021  -27.489 1.00 13.69 ? 631  THR A CA  1 
ATOM   5000 C  C   . THR A 1 631  ? 64.001 70.673  -28.836 1.00 11.96 ? 631  THR A C   1 
ATOM   5001 O  O   . THR A 1 631  ? 64.263 70.056  -29.896 1.00 12.07 ? 631  THR A O   1 
ATOM   5002 C  CB  . THR A 1 631  ? 65.788 70.086  -27.216 1.00 14.10 ? 631  THR A CB  1 
ATOM   5003 O  OG1 . THR A 1 631  ? 66.041 69.437  -25.966 1.00 14.76 ? 631  THR A OG1 1 
ATOM   5004 C  CG2 . THR A 1 631  ? 66.250 71.521  -27.135 1.00 14.24 ? 631  THR A CG2 1 
ATOM   5005 N  N   . TYR A 1 632  ? 63.427 71.880  -28.776 1.00 10.36 ? 632  TYR A N   1 
ATOM   5006 C  CA  . TYR A 1 632  ? 63.165 72.618  -30.023 1.00 12.41 ? 632  TYR A CA  1 
ATOM   5007 C  C   . TYR A 1 632  ? 63.722 74.023  -29.836 1.00 10.92 ? 632  TYR A C   1 
ATOM   5008 O  O   . TYR A 1 632  ? 64.026 74.453  -28.742 1.00 12.21 ? 632  TYR A O   1 
ATOM   5009 C  CB  . TYR A 1 632  ? 61.670 72.731  -30.373 1.00 12.00 ? 632  TYR A CB  1 
ATOM   5010 C  CG  . TYR A 1 632  ? 61.040 71.416  -30.791 1.00 12.14 ? 632  TYR A CG  1 
ATOM   5011 C  CD1 . TYR A 1 632  ? 60.660 70.482  -29.819 1.00 14.68 ? 632  TYR A CD1 1 
ATOM   5012 C  CD2 . TYR A 1 632  ? 60.839 71.081  -32.122 1.00 13.26 ? 632  TYR A CD2 1 
ATOM   5013 C  CE1 . TYR A 1 632  ? 60.124 69.268  -30.153 1.00 11.73 ? 632  TYR A CE1 1 
ATOM   5014 C  CE2 . TYR A 1 632  ? 60.268 69.856  -32.489 1.00 12.76 ? 632  TYR A CE2 1 
ATOM   5015 C  CZ  . TYR A 1 632  ? 59.917 68.925  -31.482 1.00 13.83 ? 632  TYR A CZ  1 
ATOM   5016 O  OH  . TYR A 1 632  ? 59.425 67.701  -31.792 1.00 16.31 ? 632  TYR A OH  1 
ATOM   5017 N  N   . VAL A 1 633  ? 63.904 74.744  -30.966 1.00 11.61 ? 633  VAL A N   1 
ATOM   5018 C  CA  . VAL A 1 633  ? 64.439 76.120  -30.915 1.00 11.67 ? 633  VAL A CA  1 
ATOM   5019 C  C   . VAL A 1 633  ? 63.510 77.152  -31.618 1.00 10.26 ? 633  VAL A C   1 
ATOM   5020 O  O   . VAL A 1 633  ? 63.013 76.824  -32.698 1.00 11.78 ? 633  VAL A O   1 
ATOM   5021 C  CB  . VAL A 1 633  ? 65.802 76.159  -31.622 1.00 12.33 ? 633  VAL A CB  1 
ATOM   5022 C  CG1 . VAL A 1 633  ? 66.372 77.516  -31.630 1.00 12.44 ? 633  VAL A CG1 1 
ATOM   5023 C  CG2 . VAL A 1 633  ? 66.764 75.167  -30.973 1.00 12.66 ? 633  VAL A CG2 1 
ATOM   5024 N  N   . LEU A 1 634  ? 63.234 78.282  -30.976 1.00 12.29 ? 634  LEU A N   1 
ATOM   5025 C  CA  . LEU A 1 634  ? 62.391 79.366  -31.560 1.00 13.25 ? 634  LEU A CA  1 
ATOM   5026 C  C   . LEU A 1 634  ? 63.371 80.458  -31.947 1.00 13.07 ? 634  LEU A C   1 
ATOM   5027 O  O   . LEU A 1 634  ? 64.154 80.921  -31.086 1.00 13.65 ? 634  LEU A O   1 
ATOM   5028 C  CB  . LEU A 1 634  ? 61.411 79.927  -30.505 1.00 13.45 ? 634  LEU A CB  1 
ATOM   5029 C  CG  . LEU A 1 634  ? 60.470 78.870  -29.845 1.00 18.76 ? 634  LEU A CG  1 
ATOM   5030 C  CD1 . LEU A 1 634  ? 59.253 79.618  -29.352 1.00 19.66 ? 634  LEU A CD1 1 
ATOM   5031 C  CD2 . LEU A 1 634  ? 60.065 77.730  -30.766 1.00 18.63 ? 634  LEU A CD2 1 
ATOM   5032 N  N   . THR A 1 635  ? 63.350 80.850  -33.242 1.00 13.72 ? 635  THR A N   1 
ATOM   5033 C  CA  . THR A 1 635  ? 64.300 81.840  -33.763 1.00 14.12 ? 635  THR A CA  1 
ATOM   5034 C  C   . THR A 1 635  ? 63.537 83.015  -34.401 1.00 14.58 ? 635  THR A C   1 
ATOM   5035 O  O   . THR A 1 635  ? 62.589 82.789  -35.160 1.00 16.27 ? 635  THR A O   1 
ATOM   5036 C  CB  . THR A 1 635  ? 65.176 81.162  -34.809 1.00 13.80 ? 635  THR A CB  1 
ATOM   5037 O  OG1 . THR A 1 635  ? 65.850 80.017  -34.235 1.00 14.55 ? 635  THR A OG1 1 
ATOM   5038 C  CG2 . THR A 1 635  ? 66.217 82.127  -35.326 1.00 15.20 ? 635  THR A CG2 1 
ATOM   5039 N  N   . ILE A 1 636  ? 63.967 84.242  -34.106 1.00 15.81 ? 636  ILE A N   1 
ATOM   5040 C  CA  . ILE A 1 636  ? 63.247 85.370  -34.678 1.00 17.67 ? 636  ILE A CA  1 
ATOM   5041 C  C   . ILE A 1 636  ? 63.832 85.766  -36.021 1.00 19.85 ? 636  ILE A C   1 
ATOM   5042 O  O   . ILE A 1 636  ? 64.940 85.410  -36.328 1.00 18.84 ? 636  ILE A O   1 
ATOM   5043 C  CB  . ILE A 1 636  ? 63.272 86.564  -33.743 1.00 18.06 ? 636  ILE A CB  1 
ATOM   5044 C  CG1 . ILE A 1 636  ? 62.235 87.595  -34.190 1.00 19.73 ? 636  ILE A CG1 1 
ATOM   5045 C  CG2 . ILE A 1 636  ? 64.684 87.206  -33.738 1.00 18.89 ? 636  ILE A CG2 1 
ATOM   5046 C  CD1 . ILE A 1 636  ? 62.230 88.847  -33.352 1.00 18.79 ? 636  ILE A CD1 1 
ATOM   5047 N  N   . SER A 1 637  ? 63.031 86.448  -36.833 1.00 22.31 ? 637  SER A N   1 
ATOM   5048 C  CA  . SER A 1 637  ? 63.490 86.932  -38.144 1.00 25.33 ? 637  SER A CA  1 
ATOM   5049 C  C   . SER A 1 637  ? 62.854 88.295  -38.385 1.00 27.18 ? 637  SER A C   1 
ATOM   5050 O  O   . SER A 1 637  ? 62.067 88.782  -37.587 1.00 25.15 ? 637  SER A O   1 
ATOM   5051 C  CB  . SER A 1 637  ? 63.128 85.962  -39.267 1.00 26.31 ? 637  SER A CB  1 
ATOM   5052 O  OG  . SER A 1 637  ? 61.743 85.728  -39.244 1.00 30.60 ? 637  SER A OG  1 
ATOM   5053 N  N   . ASP A 1 638  ? 63.224 88.950  -39.478 1.00 29.64 ? 638  ASP A N   1 
ATOM   5054 C  CA  . ASP A 1 638  ? 62.674 90.273  -39.730 1.00 31.95 ? 638  ASP A CA  1 
ATOM   5055 C  C   . ASP A 1 638  ? 61.319 90.234  -40.465 1.00 31.99 ? 638  ASP A C   1 
ATOM   5056 O  O   . ASP A 1 638  ? 60.529 91.185  -40.372 1.00 33.42 ? 638  ASP A O   1 
ATOM   5057 C  CB  . ASP A 1 638  ? 63.700 91.063  -40.531 1.00 35.07 ? 638  ASP A CB  1 
ATOM   5058 C  CG  . ASP A 1 638  ? 64.117 90.316  -41.768 1.00 37.77 ? 638  ASP A CG  1 
ATOM   5059 O  OD1 . ASP A 1 638  ? 63.252 90.149  -42.664 1.00 40.12 ? 638  ASP A OD1 1 
ATOM   5060 O  OD2 . ASP A 1 638  ? 65.283 89.863  -41.837 1.00 40.79 ? 638  ASP A OD2 1 
ATOM   5061 N  N   . SER A 1 639  ? 61.036 89.139  -41.165 1.00 30.80 ? 639  SER A N   1 
ATOM   5062 C  CA  . SER A 1 639  ? 59.785 89.042  -41.900 1.00 30.49 ? 639  SER A CA  1 
ATOM   5063 C  C   . SER A 1 639  ? 59.178 87.630  -41.811 1.00 30.66 ? 639  SER A C   1 
ATOM   5064 O  O   . SER A 1 639  ? 59.737 86.764  -41.136 1.00 29.36 ? 639  SER A O   1 
ATOM   5065 C  CB  . SER A 1 639  ? 60.059 89.446  -43.357 1.00 30.02 ? 639  SER A CB  1 
ATOM   5066 O  OG  . SER A 1 639  ? 61.130 88.676  -43.887 1.00 31.09 ? 639  SER A OG  1 
ATOM   5067 N  N   . LYS A 1 640  ? 58.041 87.387  -42.473 1.00 30.21 ? 640  LYS A N   1 
ATOM   5068 C  CA  . LYS A 1 640  ? 57.435 86.056  -42.418 1.00 29.63 ? 640  LYS A CA  1 
ATOM   5069 C  C   . LYS A 1 640  ? 58.429 84.954  -42.715 1.00 28.76 ? 640  LYS A C   1 
ATOM   5070 O  O   . LYS A 1 640  ? 59.153 84.992  -43.705 1.00 28.77 ? 640  LYS A O   1 
ATOM   5071 C  CB  . LYS A 1 640  ? 56.250 85.919  -43.374 1.00 30.60 ? 640  LYS A CB  1 
ATOM   5072 C  CG  . LYS A 1 640  ? 55.039 86.741  -42.960 1.00 33.53 ? 640  LYS A CG  1 
ATOM   5073 C  CD  . LYS A 1 640  ? 53.806 86.455  -43.831 1.00 33.87 ? 640  LYS A CD  1 
ATOM   5074 C  CE  . LYS A 1 640  ? 52.710 87.491  -43.535 1.00 36.14 ? 640  LYS A CE  1 
ATOM   5075 N  NZ  . LYS A 1 640  ? 51.328 87.016  -43.888 1.00 38.09 ? 640  LYS A NZ  1 
ATOM   5076 N  N   . PRO A 1 641  ? 58.514 83.963  -41.822 1.00 27.42 ? 641  PRO A N   1 
ATOM   5077 C  CA  . PRO A 1 641  ? 59.443 82.845  -42.038 1.00 25.29 ? 641  PRO A CA  1 
ATOM   5078 C  C   . PRO A 1 641  ? 58.788 81.855  -42.993 1.00 23.50 ? 641  PRO A C   1 
ATOM   5079 O  O   . PRO A 1 641  ? 57.561 81.767  -43.054 1.00 23.16 ? 641  PRO A O   1 
ATOM   5080 C  CB  . PRO A 1 641  ? 59.588 82.238  -40.633 1.00 27.01 ? 641  PRO A CB  1 
ATOM   5081 C  CG  . PRO A 1 641  ? 59.252 83.376  -39.735 1.00 28.04 ? 641  PRO A CG  1 
ATOM   5082 C  CD  . PRO A 1 641  ? 58.073 84.002  -40.426 1.00 27.28 ? 641  PRO A CD  1 
ATOM   5083 N  N   . GLU A 1 642  ? 59.584 81.090  -43.712 1.00 23.03 ? 642  GLU A N   1 
ATOM   5084 C  CA  . GLU A 1 642  ? 59.031 80.109  -44.665 1.00 23.29 ? 642  GLU A CA  1 
ATOM   5085 C  C   . GLU A 1 642  ? 58.079 79.051  -44.094 1.00 23.73 ? 642  GLU A C   1 
ATOM   5086 O  O   . GLU A 1 642  ? 57.057 78.716  -44.690 1.00 23.96 ? 642  GLU A O   1 
ATOM   5087 C  CB  . GLU A 1 642  ? 60.169 79.379  -45.364 1.00 26.51 ? 642  GLU A CB  1 
ATOM   5088 C  CG  . GLU A 1 642  ? 59.675 78.398  -46.400 1.00 30.28 ? 642  GLU A CG  1 
ATOM   5089 C  CD  . GLU A 1 642  ? 60.790 77.616  -47.090 1.00 33.24 ? 642  GLU A CD  1 
ATOM   5090 O  OE1 . GLU A 1 642  ? 61.975 78.057  -47.045 1.00 34.71 ? 642  GLU A OE1 1 
ATOM   5091 O  OE2 . GLU A 1 642  ? 60.452 76.550  -47.681 1.00 35.81 ? 642  GLU A OE2 1 
ATOM   5092 N  N   . HIS A 1 643  ? 58.404 78.550  -42.909 1.00 22.74 ? 643  HIS A N   1 
ATOM   5093 C  CA  . HIS A 1 643  ? 57.623 77.478  -42.296 1.00 22.08 ? 643  HIS A CA  1 
ATOM   5094 C  C   . HIS A 1 643  ? 56.629 77.872  -41.222 1.00 21.40 ? 643  HIS A C   1 
ATOM   5095 O  O   . HIS A 1 643  ? 56.165 77.006  -40.457 1.00 19.75 ? 643  HIS A O   1 
ATOM   5096 C  CB  . HIS A 1 643  ? 58.585 76.401  -41.781 1.00 22.56 ? 643  HIS A CB  1 
ATOM   5097 C  CG  . HIS A 1 643  ? 59.437 75.813  -42.857 1.00 22.71 ? 643  HIS A CG  1 
ATOM   5098 N  ND1 . HIS A 1 643  ? 58.989 74.806  -43.680 1.00 22.21 ? 643  HIS A ND1 1 
ATOM   5099 C  CD2 . HIS A 1 643  ? 60.687 76.122  -43.282 1.00 22.66 ? 643  HIS A CD2 1 
ATOM   5100 C  CE1 . HIS A 1 643  ? 59.927 74.514  -44.564 1.00 23.68 ? 643  HIS A CE1 1 
ATOM   5101 N  NE2 . HIS A 1 643  ? 60.967 75.296  -44.341 1.00 22.03 ? 643  HIS A NE2 1 
ATOM   5102 N  N   . THR A 1 644  ? 56.295 79.152  -41.184 1.00 18.14 ? 644  THR A N   1 
ATOM   5103 C  CA  . THR A 1 644  ? 55.316 79.676  -40.249 1.00 17.37 ? 644  THR A CA  1 
ATOM   5104 C  C   . THR A 1 644  ? 54.141 80.319  -40.950 1.00 19.23 ? 644  THR A C   1 
ATOM   5105 O  O   . THR A 1 644  ? 54.316 81.186  -41.814 1.00 19.76 ? 644  THR A O   1 
ATOM   5106 C  CB  . THR A 1 644  ? 55.925 80.646  -39.281 1.00 17.27 ? 644  THR A CB  1 
ATOM   5107 O  OG1 . THR A 1 644  ? 56.904 79.918  -38.539 1.00 16.78 ? 644  THR A OG1 1 
ATOM   5108 C  CG2 . THR A 1 644  ? 54.864 81.188  -38.320 1.00 17.47 ? 644  THR A CG2 1 
ATOM   5109 N  N   . SER A 1 645  ? 52.940 79.895  -40.586 1.00 17.01 ? 645  SER A N   1 
ATOM   5110 C  CA  . SER A 1 645  ? 51.736 80.450  -41.203 1.00 17.84 ? 645  SER A CA  1 
ATOM   5111 C  C   . SER A 1 645  ? 51.043 81.327  -40.182 1.00 18.66 ? 645  SER A C   1 
ATOM   5112 O  O   . SER A 1 645  ? 51.369 81.308  -38.983 1.00 18.00 ? 645  SER A O   1 
ATOM   5113 C  CB  . SER A 1 645  ? 50.790 79.348  -41.676 1.00 18.73 ? 645  SER A CB  1 
ATOM   5114 O  OG  . SER A 1 645  ? 50.329 78.559  -40.577 1.00 17.36 ? 645  SER A OG  1 
ATOM   5115 N  N   . TYR A 1 646  ? 50.092 82.130  -40.666 1.00 17.40 ? 646  TYR A N   1 
ATOM   5116 C  CA  . TYR A 1 646  ? 49.350 83.031  -39.803 1.00 16.45 ? 646  TYR A CA  1 
ATOM   5117 C  C   . TYR A 1 646  ? 47.858 82.766  -39.860 1.00 16.66 ? 646  TYR A C   1 
ATOM   5118 O  O   . TYR A 1 646  ? 47.296 82.500  -40.924 1.00 18.41 ? 646  TYR A O   1 
ATOM   5119 C  CB  . TYR A 1 646  ? 49.671 84.490  -40.156 1.00 18.09 ? 646  TYR A CB  1 
ATOM   5120 C  CG  . TYR A 1 646  ? 51.129 84.776  -39.923 1.00 17.11 ? 646  TYR A CG  1 
ATOM   5121 C  CD1 . TYR A 1 646  ? 52.060 84.463  -40.893 1.00 17.58 ? 646  TYR A CD1 1 
ATOM   5122 C  CD2 . TYR A 1 646  ? 51.580 85.207  -38.674 1.00 16.77 ? 646  TYR A CD2 1 
ATOM   5123 C  CE1 . TYR A 1 646  ? 53.429 84.555  -40.637 1.00 19.93 ? 646  TYR A CE1 1 
ATOM   5124 C  CE2 . TYR A 1 646  ? 52.968 85.295  -38.381 1.00 18.00 ? 646  TYR A CE2 1 
ATOM   5125 C  CZ  . TYR A 1 646  ? 53.875 84.965  -39.371 1.00 20.18 ? 646  TYR A CZ  1 
ATOM   5126 O  OH  . TYR A 1 646  ? 55.239 85.012  -39.098 1.00 19.68 ? 646  TYR A OH  1 
ATOM   5127 N  N   . ALA A 1 647  ? 47.220 82.776  -38.682 1.00 15.79 ? 647  ALA A N   1 
ATOM   5128 C  CA  . ALA A 1 647  ? 45.805 82.498  -38.642 1.00 16.23 ? 647  ALA A CA  1 
ATOM   5129 C  C   . ALA A 1 647  ? 44.996 83.693  -39.104 1.00 14.81 ? 647  ALA A C   1 
ATOM   5130 O  O   . ALA A 1 647  ? 45.411 84.807  -38.946 1.00 16.94 ? 647  ALA A O   1 
ATOM   5131 C  CB  . ALA A 1 647  ? 45.397 82.189  -37.212 1.00 15.12 ? 647  ALA A CB  1 
ATOM   5132 N  N   . SER A 1 648  ? 43.850 83.433  -39.708 1.00 16.02 ? 648  SER A N   1 
ATOM   5133 C  CA  . SER A 1 648  ? 42.965 84.550  -40.016 1.00 16.53 ? 648  SER A CA  1 
ATOM   5134 C  C   . SER A 1 648  ? 42.027 84.678  -38.807 1.00 16.17 ? 648  SER A C   1 
ATOM   5135 O  O   . SER A 1 648  ? 41.799 83.670  -38.077 1.00 17.41 ? 648  SER A O   1 
ATOM   5136 C  CB  . SER A 1 648  ? 42.121 84.285  -41.269 1.00 17.28 ? 648  SER A CB  1 
ATOM   5137 O  OG  . SER A 1 648  ? 41.440 83.052  -41.173 1.00 23.47 ? 648  SER A OG  1 
ATOM   5138 N  N   . ASN A 1 649  ? 41.504 85.872  -38.575 1.00 14.75 ? 649  ASN A N   1 
ATOM   5139 C  CA  . ASN A 1 649  ? 40.586 86.164  -37.472 1.00 14.70 ? 649  ASN A CA  1 
ATOM   5140 C  C   . ASN A 1 649  ? 39.351 86.923  -37.964 1.00 15.44 ? 649  ASN A C   1 
ATOM   5141 O  O   . ASN A 1 649  ? 39.480 87.888  -38.731 1.00 14.89 ? 649  ASN A O   1 
ATOM   5142 C  CB  . ASN A 1 649  ? 41.287 86.973  -36.418 1.00 15.62 ? 649  ASN A CB  1 
ATOM   5143 C  CG  . ASN A 1 649  ? 42.470 86.217  -35.795 1.00 17.66 ? 649  ASN A CG  1 
ATOM   5144 O  OD1 . ASN A 1 649  ? 42.303 85.255  -35.006 1.00 17.80 ? 649  ASN A OD1 1 
ATOM   5145 N  ND2 . ASN A 1 649  ? 43.666 86.651  -36.153 1.00 17.25 ? 649  ASN A ND2 1 
ATOM   5146 N  N   . LEU A 1 650  ? 38.187 86.505  -37.484 1.00 14.64 ? 650  LEU A N   1 
ATOM   5147 C  CA  . LEU A 1 650  ? 36.880 87.084  -37.837 1.00 16.18 ? 650  LEU A CA  1 
ATOM   5148 C  C   . LEU A 1 650  ? 36.066 87.359  -36.560 1.00 18.13 ? 650  LEU A C   1 
ATOM   5149 O  O   . LEU A 1 650  ? 35.796 86.438  -35.739 1.00 19.55 ? 650  LEU A O   1 
ATOM   5150 C  CB  . LEU A 1 650  ? 36.130 86.104  -38.790 1.00 15.07 ? 650  LEU A CB  1 
ATOM   5151 C  CG  . LEU A 1 650  ? 34.676 86.434  -39.165 1.00 15.73 ? 650  LEU A CG  1 
ATOM   5152 C  CD1 . LEU A 1 650  ? 34.624 87.726  -40.064 1.00 14.22 ? 650  LEU A CD1 1 
ATOM   5153 C  CD2 . LEU A 1 650  ? 34.084 85.298  -39.907 1.00 15.78 ? 650  LEU A CD2 1 
ATOM   5154 N  N   . LEU A 1 651  ? 35.727 88.625  -36.335 1.00 18.22 ? 651  LEU A N   1 
ATOM   5155 C  CA  . LEU A 1 651  ? 34.911 89.009  -35.205 1.00 18.73 ? 651  LEU A CA  1 
ATOM   5156 C  C   . LEU A 1 651  ? 33.466 89.221  -35.676 1.00 19.24 ? 651  LEU A C   1 
ATOM   5157 O  O   . LEU A 1 651  ? 33.188 90.086  -36.523 1.00 20.35 ? 651  LEU A O   1 
ATOM   5158 C  CB  . LEU A 1 651  ? 35.454 90.274  -34.557 1.00 20.90 ? 651  LEU A CB  1 
ATOM   5159 C  CG  . LEU A 1 651  ? 35.171 90.613  -33.074 1.00 22.78 ? 651  LEU A CG  1 
ATOM   5160 C  CD1 . LEU A 1 651  ? 33.814 91.192  -32.883 1.00 25.77 ? 651  LEU A CD1 1 
ATOM   5161 C  CD2 . LEU A 1 651  ? 35.322 89.364  -32.210 1.00 23.08 ? 651  LEU A CD2 1 
ATOM   5162 N  N   . LEU A 1 652  ? 32.552 88.386  -35.173 1.00 18.80 ? 652  LEU A N   1 
ATOM   5163 C  CA  . LEU A 1 652  ? 31.156 88.481  -35.570 1.00 18.25 ? 652  LEU A CA  1 
ATOM   5164 C  C   . LEU A 1 652  ? 30.348 89.160  -34.460 1.00 20.54 ? 652  LEU A C   1 
ATOM   5165 O  O   . LEU A 1 652  ? 30.224 88.648  -33.340 1.00 17.60 ? 652  LEU A O   1 
ATOM   5166 C  CB  . LEU A 1 652  ? 30.614 87.088  -35.865 1.00 17.69 ? 652  LEU A CB  1 
ATOM   5167 C  CG  . LEU A 1 652  ? 31.362 86.356  -36.986 1.00 17.95 ? 652  LEU A CG  1 
ATOM   5168 C  CD1 . LEU A 1 652  ? 30.782 84.942  -37.137 1.00 17.41 ? 652  LEU A CD1 1 
ATOM   5169 C  CD2 . LEU A 1 652  ? 31.265 87.126  -38.353 1.00 20.10 ? 652  LEU A CD2 1 
ATOM   5170 N  N   . ARG A 1 653  ? 29.826 90.349  -34.770 1.00 19.89 ? 653  ARG A N   1 
ATOM   5171 C  CA  . ARG A 1 653  ? 29.021 91.088  -33.823 1.00 21.60 ? 653  ARG A CA  1 
ATOM   5172 C  C   . ARG A 1 653  ? 28.439 92.275  -34.552 1.00 23.20 ? 653  ARG A C   1 
ATOM   5173 O  O   . ARG A 1 653  ? 29.066 92.794  -35.504 1.00 20.47 ? 653  ARG A O   1 
ATOM   5174 C  CB  . ARG A 1 653  ? 29.893 91.588  -32.696 1.00 22.30 ? 653  ARG A CB  1 
ATOM   5175 C  CG  . ARG A 1 653  ? 30.955 92.553  -33.185 1.00 27.53 ? 653  ARG A CG  1 
ATOM   5176 C  CD  . ARG A 1 653  ? 31.519 93.348  -32.046 1.00 28.82 ? 653  ARG A CD  1 
ATOM   5177 N  NE  . ARG A 1 653  ? 30.434 93.781  -31.185 1.00 34.50 ? 653  ARG A NE  1 
ATOM   5178 C  CZ  . ARG A 1 653  ? 30.597 94.471  -30.066 1.00 35.83 ? 653  ARG A CZ  1 
ATOM   5179 N  NH1 . ARG A 1 653  ? 31.812 94.831  -29.677 1.00 37.82 ? 653  ARG A NH1 1 
ATOM   5180 N  NH2 . ARG A 1 653  ? 29.552 94.731  -29.299 1.00 38.36 ? 653  ARG A NH2 1 
ATOM   5181 N  N   . LYS A 1 654  ? 27.270 92.741  -34.134 1.00 24.16 ? 654  LYS A N   1 
ATOM   5182 C  CA  . LYS A 1 654  ? 26.757 93.933  -34.805 1.00 27.57 ? 654  LYS A CA  1 
ATOM   5183 C  C   . LYS A 1 654  ? 27.549 95.132  -34.232 1.00 28.38 ? 654  LYS A C   1 
ATOM   5184 O  O   . LYS A 1 654  ? 28.117 95.056  -33.123 1.00 29.96 ? 654  LYS A O   1 
ATOM   5185 C  CB  . LYS A 1 654  ? 25.248 94.070  -34.594 1.00 29.22 ? 654  LYS A CB  1 
ATOM   5186 C  CG  . LYS A 1 654  ? 24.410 93.118  -35.469 1.00 30.19 ? 654  LYS A CG  1 
ATOM   5187 C  CD  . LYS A 1 654  ? 23.122 93.801  -35.909 1.00 32.89 ? 654  LYS A CD  1 
ATOM   5188 C  CE  . LYS A 1 654  ? 21.990 92.811  -36.287 1.00 34.16 ? 654  LYS A CE  1 
ATOM   5189 N  NZ  . LYS A 1 654  ? 22.352 91.955  -37.473 1.00 36.26 ? 654  LYS A NZ  1 
ATOM   5190 N  N   . ASN A 1 655  ? 27.617 96.207  -35.005 1.00 30.70 ? 655  ASN A N   1 
ATOM   5191 C  CA  . ASN A 1 655  ? 28.356 97.402  -34.624 1.00 31.82 ? 655  ASN A CA  1 
ATOM   5192 C  C   . ASN A 1 655  ? 29.767 97.095  -34.111 1.00 31.26 ? 655  ASN A C   1 
ATOM   5193 O  O   . ASN A 1 655  ? 30.109 97.311  -32.950 1.00 31.15 ? 655  ASN A O   1 
ATOM   5194 C  CB  . ASN A 1 655  ? 27.533 98.213  -33.627 1.00 34.68 ? 655  ASN A CB  1 
ATOM   5195 C  CG  . ASN A 1 655  ? 26.269 98.791  -34.282 1.00 37.75 ? 655  ASN A CG  1 
ATOM   5196 O  OD1 . ASN A 1 655  ? 26.361 99.567  -35.259 1.00 39.50 ? 655  ASN A OD1 1 
ATOM   5197 N  ND2 . ASN A 1 655  ? 25.081 98.392  -33.779 1.00 38.55 ? 655  ASN A ND2 1 
ATOM   5198 N  N   . PRO A 1 656  ? 30.620 96.590  -35.016 1.00 30.27 ? 656  PRO A N   1 
ATOM   5199 C  CA  . PRO A 1 656  ? 31.993 96.256  -34.652 1.00 29.65 ? 656  PRO A CA  1 
ATOM   5200 C  C   . PRO A 1 656  ? 32.873 97.474  -34.604 1.00 28.75 ? 656  PRO A C   1 
ATOM   5201 O  O   . PRO A 1 656  ? 32.552 98.525  -35.152 1.00 28.59 ? 656  PRO A O   1 
ATOM   5202 C  CB  . PRO A 1 656  ? 32.418 95.291  -35.737 1.00 29.37 ? 656  PRO A CB  1 
ATOM   5203 C  CG  . PRO A 1 656  ? 31.673 95.847  -36.946 1.00 29.44 ? 656  PRO A CG  1 
ATOM   5204 C  CD  . PRO A 1 656  ? 30.315 96.192  -36.404 1.00 29.98 ? 656  PRO A CD  1 
ATOM   5205 N  N   . THR A 1 657  ? 33.985 97.308  -33.922 1.00 28.71 ? 657  THR A N   1 
ATOM   5206 C  CA  . THR A 1 657  ? 34.966 98.355  -33.764 1.00 29.11 ? 657  THR A CA  1 
ATOM   5207 C  C   . THR A 1 657  ? 36.319 97.715  -34.140 1.00 29.12 ? 657  THR A C   1 
ATOM   5208 O  O   . THR A 1 657  ? 36.463 96.499  -34.056 1.00 28.22 ? 657  THR A O   1 
ATOM   5209 C  CB  . THR A 1 657  ? 34.953 98.831  -32.311 1.00 29.82 ? 657  THR A CB  1 
ATOM   5210 O  OG1 . THR A 1 657  ? 35.431 100.162 -32.272 1.00 34.42 ? 657  THR A OG1 1 
ATOM   5211 C  CG2 . THR A 1 657  ? 35.839 97.984  -31.443 1.00 31.10 ? 657  THR A CG2 1 
ATOM   5212 N  N   . SER A 1 658  ? 37.293 98.508  -34.570 1.00 28.73 ? 658  SER A N   1 
ATOM   5213 C  CA  . SER A 1 658  ? 38.592 97.977  -34.971 1.00 29.74 ? 658  SER A CA  1 
ATOM   5214 C  C   . SER A 1 658  ? 39.318 97.219  -33.842 1.00 29.66 ? 658  SER A C   1 
ATOM   5215 O  O   . SER A 1 658  ? 39.117 97.496  -32.660 1.00 29.99 ? 658  SER A O   1 
ATOM   5216 C  CB  . SER A 1 658  ? 39.508 99.117  -35.436 1.00 30.36 ? 658  SER A CB  1 
ATOM   5217 O  OG  . SER A 1 658  ? 39.904 99.891  -34.306 1.00 31.94 ? 658  SER A OG  1 
ATOM   5218 N  N   . LEU A 1 659  ? 40.163 96.273  -34.243 1.00 29.62 ? 659  LEU A N   1 
ATOM   5219 C  CA  . LEU A 1 659  ? 40.980 95.491  -33.318 1.00 29.59 ? 659  LEU A CA  1 
ATOM   5220 C  C   . LEU A 1 659  ? 42.368 95.363  -33.956 1.00 28.86 ? 659  LEU A C   1 
ATOM   5221 O  O   . LEU A 1 659  ? 42.642 94.472  -34.760 1.00 28.63 ? 659  LEU A O   1 
ATOM   5222 C  CB  . LEU A 1 659  ? 40.357 94.105  -33.075 1.00 31.81 ? 659  LEU A CB  1 
ATOM   5223 C  CG  . LEU A 1 659  ? 39.241 94.027  -32.022 1.00 32.41 ? 659  LEU A CG  1 
ATOM   5224 C  CD1 . LEU A 1 659  ? 38.521 92.713  -32.163 1.00 35.15 ? 659  LEU A CD1 1 
ATOM   5225 C  CD2 . LEU A 1 659  ? 39.807 94.193  -30.630 1.00 34.13 ? 659  LEU A CD2 1 
ATOM   5226 N  N   . PRO A 1 660  ? 43.253 96.306  -33.638 1.00 28.59 ? 660  PRO A N   1 
ATOM   5227 C  CA  . PRO A 1 660  ? 44.612 96.257  -34.199 1.00 28.30 ? 660  PRO A CA  1 
ATOM   5228 C  C   . PRO A 1 660  ? 45.444 95.235  -33.412 1.00 27.03 ? 660  PRO A C   1 
ATOM   5229 O  O   . PRO A 1 660  ? 45.215 95.043  -32.224 1.00 27.56 ? 660  PRO A O   1 
ATOM   5230 C  CB  . PRO A 1 660  ? 45.113 97.684  -34.014 1.00 27.86 ? 660  PRO A CB  1 
ATOM   5231 C  CG  . PRO A 1 660  ? 44.477 98.105  -32.730 1.00 28.25 ? 660  PRO A CG  1 
ATOM   5232 C  CD  . PRO A 1 660  ? 43.075 97.453  -32.737 1.00 29.68 ? 660  PRO A CD  1 
ATOM   5233 N  N   . LEU A 1 661  ? 46.404 94.608  -34.064 1.00 26.54 ? 661  LEU A N   1 
ATOM   5234 C  CA  . LEU A 1 661  ? 47.197 93.578  -33.384 1.00 25.89 ? 661  LEU A CA  1 
ATOM   5235 C  C   . LEU A 1 661  ? 48.712 93.864  -33.427 1.00 25.71 ? 661  LEU A C   1 
ATOM   5236 O  O   . LEU A 1 661  ? 49.497 93.036  -33.918 1.00 26.43 ? 661  LEU A O   1 
ATOM   5237 C  CB  . LEU A 1 661  ? 46.894 92.245  -34.063 1.00 24.80 ? 661  LEU A CB  1 
ATOM   5238 C  CG  . LEU A 1 661  ? 45.410 91.848  -34.099 1.00 24.92 ? 661  LEU A CG  1 
ATOM   5239 C  CD1 . LEU A 1 661  ? 45.147 90.647  -35.036 1.00 25.11 ? 661  LEU A CD1 1 
ATOM   5240 C  CD2 . LEU A 1 661  ? 44.989 91.597  -32.681 1.00 25.15 ? 661  LEU A CD2 1 
ATOM   5241 N  N   . GLY A 1 662  ? 49.103 95.047  -32.939 1.00 25.69 ? 662  GLY A N   1 
ATOM   5242 C  CA  . GLY A 1 662  ? 50.509 95.432  -32.981 1.00 25.86 ? 662  GLY A CA  1 
ATOM   5243 C  C   . GLY A 1 662  ? 51.114 95.056  -34.327 1.00 24.05 ? 662  GLY A C   1 
ATOM   5244 O  O   . GLY A 1 662  ? 50.665 95.517  -35.352 1.00 24.68 ? 662  GLY A O   1 
ATOM   5245 N  N   . GLN A 1 663  ? 52.141 94.211  -34.302 1.00 24.97 ? 663  GLN A N   1 
ATOM   5246 C  CA  . GLN A 1 663  ? 52.831 93.729  -35.505 1.00 24.78 ? 663  GLN A CA  1 
ATOM   5247 C  C   . GLN A 1 663  ? 52.188 92.561  -36.273 1.00 25.19 ? 663  GLN A C   1 
ATOM   5248 O  O   . GLN A 1 663  ? 52.701 92.124  -37.295 1.00 24.87 ? 663  GLN A O   1 
ATOM   5249 C  CB  . GLN A 1 663  ? 54.237 93.233  -35.124 1.00 27.36 ? 663  GLN A CB  1 
ATOM   5250 C  CG  . GLN A 1 663  ? 55.291 94.251  -34.655 1.00 28.98 ? 663  GLN A CG  1 
ATOM   5251 C  CD  . GLN A 1 663  ? 56.601 93.534  -34.342 1.00 30.76 ? 663  GLN A CD  1 
ATOM   5252 O  OE1 . GLN A 1 663  ? 57.259 92.991  -35.251 1.00 33.14 ? 663  GLN A OE1 1 
ATOM   5253 N  NE2 . GLN A 1 663  ? 56.972 93.495  -33.068 1.00 30.36 ? 663  GLN A NE2 1 
ATOM   5254 N  N   . TYR A 1 664  ? 51.090 92.012  -35.780 1.00 25.36 ? 664  TYR A N   1 
ATOM   5255 C  CA  . TYR A 1 664  ? 50.501 90.853  -36.452 1.00 26.51 ? 664  TYR A CA  1 
ATOM   5256 C  C   . TYR A 1 664  ? 50.261 91.148  -37.914 1.00 28.41 ? 664  TYR A C   1 
ATOM   5257 O  O   . TYR A 1 664  ? 49.687 92.186  -38.230 1.00 29.52 ? 664  TYR A O   1 
ATOM   5258 C  CB  . TYR A 1 664  ? 49.197 90.470  -35.758 1.00 23.12 ? 664  TYR A CB  1 
ATOM   5259 C  CG  . TYR A 1 664  ? 48.703 89.085  -36.107 1.00 20.14 ? 664  TYR A CG  1 
ATOM   5260 C  CD1 . TYR A 1 664  ? 49.303 87.943  -35.560 1.00 19.30 ? 664  TYR A CD1 1 
ATOM   5261 C  CD2 . TYR A 1 664  ? 47.612 88.920  -36.974 1.00 18.79 ? 664  TYR A CD2 1 
ATOM   5262 C  CE1 . TYR A 1 664  ? 48.815 86.678  -35.856 1.00 18.10 ? 664  TYR A CE1 1 
ATOM   5263 C  CE2 . TYR A 1 664  ? 47.120 87.661  -37.287 1.00 16.30 ? 664  TYR A CE2 1 
ATOM   5264 C  CZ  . TYR A 1 664  ? 47.718 86.523  -36.721 1.00 18.32 ? 664  TYR A CZ  1 
ATOM   5265 O  OH  . TYR A 1 664  ? 47.175 85.268  -37.019 1.00 16.03 ? 664  TYR A OH  1 
ATOM   5266 N  N   . PRO A 1 665  ? 50.662 90.249  -38.824 1.00 29.59 ? 665  PRO A N   1 
ATOM   5267 C  CA  . PRO A 1 665  ? 50.464 90.503  -40.268 1.00 31.38 ? 665  PRO A CA  1 
ATOM   5268 C  C   . PRO A 1 665  ? 49.036 90.721  -40.792 1.00 32.06 ? 665  PRO A C   1 
ATOM   5269 O  O   . PRO A 1 665  ? 48.658 91.843  -41.143 1.00 33.86 ? 665  PRO A O   1 
ATOM   5270 C  CB  . PRO A 1 665  ? 51.117 89.301  -40.952 1.00 31.57 ? 665  PRO A CB  1 
ATOM   5271 C  CG  . PRO A 1 665  ? 51.981 88.658  -39.883 1.00 30.24 ? 665  PRO A CG  1 
ATOM   5272 C  CD  . PRO A 1 665  ? 51.278 88.925  -38.592 1.00 29.98 ? 665  PRO A CD  1 
ATOM   5273 N  N   . GLU A 1 666  ? 48.252 89.648  -40.845 1.00 31.49 ? 666  GLU A N   1 
ATOM   5274 C  CA  . GLU A 1 666  ? 46.887 89.691  -41.357 1.00 31.14 ? 666  GLU A CA  1 
ATOM   5275 C  C   . GLU A 1 666  ? 45.886 90.510  -40.564 1.00 29.66 ? 666  GLU A C   1 
ATOM   5276 O  O   . GLU A 1 666  ? 45.855 90.442  -39.334 1.00 28.62 ? 666  GLU A O   1 
ATOM   5277 C  CB  . GLU A 1 666  ? 46.347 88.275  -41.509 1.00 33.77 ? 666  GLU A CB  1 
ATOM   5278 C  CG  . GLU A 1 666  ? 44.890 88.300  -41.895 1.00 37.41 ? 666  GLU A CG  1 
ATOM   5279 C  CD  . GLU A 1 666  ? 44.561 87.286  -42.959 1.00 38.38 ? 666  GLU A CD  1 
ATOM   5280 O  OE1 . GLU A 1 666  ? 45.479 86.964  -43.771 1.00 40.24 ? 666  GLU A OE1 1 
ATOM   5281 O  OE2 . GLU A 1 666  ? 43.387 86.828  -42.994 1.00 39.40 ? 666  GLU A OE2 1 
ATOM   5282 N  N   . ASP A 1 667  ? 45.045 91.276  -41.279 1.00 26.71 ? 667  ASP A N   1 
ATOM   5283 C  CA  . ASP A 1 667  ? 44.042 92.134  -40.627 1.00 25.50 ? 667  ASP A CA  1 
ATOM   5284 C  C   . ASP A 1 667  ? 42.799 91.365  -40.154 1.00 21.52 ? 667  ASP A C   1 
ATOM   5285 O  O   . ASP A 1 667  ? 42.305 90.477  -40.842 1.00 21.38 ? 667  ASP A O   1 
ATOM   5286 C  CB  . ASP A 1 667  ? 43.540 93.239  -41.577 1.00 28.62 ? 667  ASP A CB  1 
ATOM   5287 C  CG  . ASP A 1 667  ? 44.642 94.161  -42.051 1.00 30.89 ? 667  ASP A CG  1 
ATOM   5288 O  OD1 . ASP A 1 667  ? 45.564 94.450  -41.258 1.00 32.11 ? 667  ASP A OD1 1 
ATOM   5289 O  OD2 . ASP A 1 667  ? 44.566 94.610  -43.211 1.00 33.02 ? 667  ASP A OD2 1 
ATOM   5290 N  N   . VAL A 1 668  ? 42.284 91.739  -39.000 1.00 20.96 ? 668  VAL A N   1 
ATOM   5291 C  CA  . VAL A 1 668  ? 41.089 91.062  -38.497 1.00 19.02 ? 668  VAL A CA  1 
ATOM   5292 C  C   . VAL A 1 668  ? 39.929 91.470  -39.379 1.00 19.22 ? 668  VAL A C   1 
ATOM   5293 O  O   . VAL A 1 668  ? 39.895 92.602  -39.832 1.00 18.54 ? 668  VAL A O   1 
ATOM   5294 C  CB  . VAL A 1 668  ? 40.795 91.496  -37.077 1.00 17.44 ? 668  VAL A CB  1 
ATOM   5295 C  CG1 . VAL A 1 668  ? 39.461 90.944  -36.596 1.00 17.48 ? 668  VAL A CG1 1 
ATOM   5296 C  CG2 . VAL A 1 668  ? 41.907 90.908  -36.196 1.00 18.87 ? 668  VAL A CG2 1 
ATOM   5297 N  N   . LYS A 1 669  ? 39.016 90.539  -39.621 1.00 18.37 ? 669  LYS A N   1 
ATOM   5298 C  CA  . LYS A 1 669  ? 37.811 90.806  -40.410 1.00 18.31 ? 669  LYS A CA  1 
ATOM   5299 C  C   . LYS A 1 669  ? 36.615 90.869  -39.486 1.00 18.88 ? 669  LYS A C   1 
ATOM   5300 O  O   . LYS A 1 669  ? 36.649 90.299  -38.368 1.00 17.55 ? 669  LYS A O   1 
ATOM   5301 C  CB  . LYS A 1 669  ? 37.592 89.730  -41.449 1.00 19.28 ? 669  LYS A CB  1 
ATOM   5302 C  CG  . LYS A 1 669  ? 38.401 90.006  -42.695 1.00 25.21 ? 669  LYS A CG  1 
ATOM   5303 C  CD  . LYS A 1 669  ? 37.838 89.253  -43.921 1.00 27.20 ? 669  LYS A CD  1 
ATOM   5304 C  CE  . LYS A 1 669  ? 38.452 89.821  -45.193 1.00 27.50 ? 669  LYS A CE  1 
ATOM   5305 N  NZ  . LYS A 1 669  ? 39.807 90.365  -44.836 1.00 28.46 ? 669  LYS A NZ  1 
ATOM   5306 N  N   . PHE A 1 670  ? 35.564 91.574  -39.922 1.00 17.85 ? 670  PHE A N   1 
ATOM   5307 C  CA  . PHE A 1 670  ? 34.341 91.722  -39.125 1.00 18.08 ? 670  PHE A CA  1 
ATOM   5308 C  C   . PHE A 1 670  ? 33.118 91.302  -39.927 1.00 18.36 ? 670  PHE A C   1 
ATOM   5309 O  O   . PHE A 1 670  ? 33.194 91.172  -41.141 1.00 18.42 ? 670  PHE A O   1 
ATOM   5310 C  CB  . PHE A 1 670  ? 34.182 93.167  -38.655 1.00 18.21 ? 670  PHE A CB  1 
ATOM   5311 C  CG  . PHE A 1 670  ? 35.356 93.650  -37.885 1.00 18.92 ? 670  PHE A CG  1 
ATOM   5312 C  CD1 . PHE A 1 670  ? 36.507 94.143  -38.539 1.00 20.03 ? 670  PHE A CD1 1 
ATOM   5313 C  CD2 . PHE A 1 670  ? 35.349 93.543  -36.515 1.00 19.10 ? 670  PHE A CD2 1 
ATOM   5314 C  CE1 . PHE A 1 670  ? 37.640 94.533  -37.762 1.00 19.54 ? 670  PHE A CE1 1 
ATOM   5315 C  CE2 . PHE A 1 670  ? 36.459 93.921  -35.737 1.00 19.71 ? 670  PHE A CE2 1 
ATOM   5316 C  CZ  . PHE A 1 670  ? 37.598 94.421  -36.377 1.00 18.72 ? 670  PHE A CZ  1 
ATOM   5317 N  N   . GLY A 1 671  ? 32.016 91.018  -39.230 1.00 19.02 ? 671  GLY A N   1 
ATOM   5318 C  CA  . GLY A 1 671  ? 30.808 90.587  -39.920 1.00 17.13 ? 671  GLY A CA  1 
ATOM   5319 C  C   . GLY A 1 671  ? 29.659 90.499  -38.930 1.00 17.97 ? 671  GLY A C   1 
ATOM   5320 O  O   . GLY A 1 671  ? 29.889 90.481  -37.724 1.00 17.25 ? 671  GLY A O   1 
ATOM   5321 N  N   . ASP A 1 672  ? 28.420 90.505  -39.417 1.00 16.46 ? 672  ASP A N   1 
ATOM   5322 C  CA  . ASP A 1 672  ? 27.312 90.365  -38.482 1.00 17.30 ? 672  ASP A CA  1 
ATOM   5323 C  C   . ASP A 1 672  ? 27.266 88.898  -38.071 1.00 16.13 ? 672  ASP A C   1 
ATOM   5324 O  O   . ASP A 1 672  ? 27.727 88.007  -38.782 1.00 16.25 ? 672  ASP A O   1 
ATOM   5325 C  CB  . ASP A 1 672  ? 25.963 90.643  -39.145 1.00 19.03 ? 672  ASP A CB  1 
ATOM   5326 C  CG  . ASP A 1 672  ? 25.742 92.098  -39.447 1.00 21.11 ? 672  ASP A CG  1 
ATOM   5327 O  OD1 . ASP A 1 672  ? 26.291 92.990  -38.750 1.00 24.62 ? 672  ASP A OD1 1 
ATOM   5328 O  OD2 . ASP A 1 672  ? 24.969 92.355  -40.408 1.00 25.61 ? 672  ASP A OD2 1 
ATOM   5329 N  N   . PRO A 1 673  ? 26.648 88.630  -36.922 1.00 17.54 ? 673  PRO A N   1 
ATOM   5330 C  CA  . PRO A 1 673  ? 26.548 87.218  -36.483 1.00 17.22 ? 673  PRO A CA  1 
ATOM   5331 C  C   . PRO A 1 673  ? 25.952 86.327  -37.620 1.00 17.21 ? 673  PRO A C   1 
ATOM   5332 O  O   . PRO A 1 673  ? 25.031 86.731  -38.342 1.00 19.04 ? 673  PRO A O   1 
ATOM   5333 C  CB  . PRO A 1 673  ? 25.588 87.302  -35.310 1.00 17.53 ? 673  PRO A CB  1 
ATOM   5334 C  CG  . PRO A 1 673  ? 25.925 88.641  -34.715 1.00 19.72 ? 673  PRO A CG  1 
ATOM   5335 C  CD  . PRO A 1 673  ? 26.035 89.545  -35.945 1.00 18.35 ? 673  PRO A CD  1 
ATOM   5336 N  N   . ARG A 1 674  ? 26.458 85.121  -37.764 1.00 17.31 ? 674  ARG A N   1 
ATOM   5337 C  CA  . ARG A 1 674  ? 25.990 84.206  -38.789 1.00 18.81 ? 674  ARG A CA  1 
ATOM   5338 C  C   . ARG A 1 674  ? 26.494 82.810  -38.479 1.00 18.74 ? 674  ARG A C   1 
ATOM   5339 O  O   . ARG A 1 674  ? 27.459 82.652  -37.744 1.00 18.00 ? 674  ARG A O   1 
ATOM   5340 C  CB  . ARG A 1 674  ? 26.526 84.622  -40.170 1.00 19.74 ? 674  ARG A CB  1 
ATOM   5341 C  CG  . ARG A 1 674  ? 28.044 84.555  -40.343 1.00 20.49 ? 674  ARG A CG  1 
ATOM   5342 C  CD  . ARG A 1 674  ? 28.420 84.745  -41.810 1.00 22.79 ? 674  ARG A CD  1 
ATOM   5343 N  NE  . ARG A 1 674  ? 29.819 84.427  -42.089 1.00 25.31 ? 674  ARG A NE  1 
ATOM   5344 C  CZ  . ARG A 1 674  ? 30.778 85.333  -42.297 1.00 26.15 ? 674  ARG A CZ  1 
ATOM   5345 N  NH1 . ARG A 1 674  ? 30.527 86.659  -42.251 1.00 27.37 ? 674  ARG A NH1 1 
ATOM   5346 N  NH2 . ARG A 1 674  ? 31.997 84.904  -42.623 1.00 26.58 ? 674  ARG A NH2 1 
ATOM   5347 N  N   . GLU A 1 675  ? 25.887 81.798  -39.074 1.00 18.55 ? 675  GLU A N   1 
ATOM   5348 C  CA  . GLU A 1 675  ? 26.357 80.446  -38.825 1.00 18.95 ? 675  GLU A CA  1 
ATOM   5349 C  C   . GLU A 1 675  ? 27.699 80.233  -39.546 1.00 20.43 ? 675  GLU A C   1 
ATOM   5350 O  O   . GLU A 1 675  ? 27.973 80.829  -40.602 1.00 22.55 ? 675  GLU A O   1 
ATOM   5351 C  CB  . GLU A 1 675  ? 25.301 79.450  -39.274 1.00 19.86 ? 675  GLU A CB  1 
ATOM   5352 C  CG  . GLU A 1 675  ? 24.005 79.632  -38.534 1.00 22.36 ? 675  GLU A CG  1 
ATOM   5353 C  CD  . GLU A 1 675  ? 23.202 78.349  -38.454 1.00 26.32 ? 675  GLU A CD  1 
ATOM   5354 O  OE1 . GLU A 1 675  ? 23.261 77.552  -39.433 1.00 27.54 ? 675  GLU A OE1 1 
ATOM   5355 O  OE2 . GLU A 1 675  ? 22.505 78.148  -37.417 1.00 27.75 ? 675  GLU A OE2 1 
ATOM   5356 N  N   . ILE A 1 676  ? 28.579 79.427  -38.963 1.00 21.37 ? 676  ILE A N   1 
ATOM   5357 C  CA  . ILE A 1 676  ? 29.883 79.170  -39.567 1.00 21.83 ? 676  ILE A CA  1 
ATOM   5358 C  C   . ILE A 1 676  ? 30.311 77.691  -39.483 1.00 22.01 ? 676  ILE A C   1 
ATOM   5359 O  O   . ILE A 1 676  ? 29.848 76.946  -38.635 1.00 21.20 ? 676  ILE A O   1 
ATOM   5360 C  CB  . ILE A 1 676  ? 30.985 80.021  -38.903 1.00 25.60 ? 676  ILE A CB  1 
ATOM   5361 C  CG1 . ILE A 1 676  ? 31.376 79.434  -37.565 1.00 25.03 ? 676  ILE A CG1 1 
ATOM   5362 C  CG2 . ILE A 1 676  ? 30.507 81.448  -38.675 1.00 26.33 ? 676  ILE A CG2 1 
ATOM   5363 C  CD1 . ILE A 1 676  ? 32.321 80.319  -36.824 1.00 28.45 ? 676  ILE A CD1 1 
ATOM   5364 N  N   . SER A 1 677  ? 31.162 77.263  -40.405 1.00 20.27 ? 677  SER A N   1 
ATOM   5365 C  CA  . SER A 1 677  ? 31.682 75.910  -40.416 1.00 21.55 ? 677  SER A CA  1 
ATOM   5366 C  C   . SER A 1 677  ? 33.191 75.945  -40.520 1.00 20.28 ? 677  SER A C   1 
ATOM   5367 O  O   . SER A 1 677  ? 33.771 76.802  -41.206 1.00 19.32 ? 677  SER A O   1 
ATOM   5368 C  CB  . SER A 1 677  ? 31.095 75.105  -41.587 1.00 23.50 ? 677  SER A CB  1 
ATOM   5369 O  OG  . SER A 1 677  ? 29.804 74.671  -41.200 1.00 28.50 ? 677  SER A OG  1 
ATOM   5370 N  N   . LEU A 1 678  ? 33.822 74.975  -39.859 1.00 20.54 ? 678  LEU A N   1 
ATOM   5371 C  CA  . LEU A 1 678  ? 35.276 74.865  -39.831 1.00 19.18 ? 678  LEU A CA  1 
ATOM   5372 C  C   . LEU A 1 678  ? 35.698 73.442  -39.946 1.00 18.70 ? 678  LEU A C   1 
ATOM   5373 O  O   . LEU A 1 678  ? 35.004 72.550  -39.453 1.00 19.24 ? 678  LEU A O   1 
ATOM   5374 C  CB  . LEU A 1 678  ? 35.821 75.365  -38.487 1.00 18.09 ? 678  LEU A CB  1 
ATOM   5375 C  CG  . LEU A 1 678  ? 35.725 76.848  -38.173 1.00 20.61 ? 678  LEU A CG  1 
ATOM   5376 C  CD1 . LEU A 1 678  ? 36.194 77.125  -36.754 1.00 20.17 ? 678  LEU A CD1 1 
ATOM   5377 C  CD2 . LEU A 1 678  ? 36.632 77.606  -39.180 1.00 22.01 ? 678  LEU A CD2 1 
ATOM   5378 N  N   . ARG A 1 679  ? 36.847 73.247  -40.572 1.00 19.69 ? 679  ARG A N   1 
ATOM   5379 C  CA  . ARG A 1 679  ? 37.444 71.944  -40.724 1.00 20.69 ? 679  ARG A CA  1 
ATOM   5380 C  C   . ARG A 1 679  ? 38.960 72.137  -40.660 1.00 21.61 ? 679  ARG A C   1 
ATOM   5381 O  O   . ARG A 1 679  ? 39.529 72.944  -41.391 1.00 20.99 ? 679  ARG A O   1 
ATOM   5382 C  CB  . ARG A 1 679  ? 37.068 71.314  -42.064 1.00 21.02 ? 679  ARG A CB  1 
ATOM   5383 C  CG  . ARG A 1 679  ? 37.416 69.863  -42.127 1.00 24.06 ? 679  ARG A CG  1 
ATOM   5384 C  CD  . ARG A 1 679  ? 37.116 69.265  -43.490 1.00 28.07 ? 679  ARG A CD  1 
ATOM   5385 N  NE  . ARG A 1 679  ? 37.415 67.845  -43.435 1.00 30.90 ? 679  ARG A NE  1 
ATOM   5386 C  CZ  . ARG A 1 679  ? 37.526 67.070  -44.497 1.00 33.40 ? 679  ARG A CZ  1 
ATOM   5387 N  NH1 . ARG A 1 679  ? 37.363 67.591  -45.717 1.00 34.66 ? 679  ARG A NH1 1 
ATOM   5388 N  NH2 . ARG A 1 679  ? 37.796 65.779  -44.339 1.00 34.82 ? 679  ARG A NH2 1 
ATOM   5389 N  N   . VAL A 1 680  ? 39.626 71.421  -39.748 1.00 20.20 ? 680  VAL A N   1 
ATOM   5390 C  CA  . VAL A 1 680  ? 41.085 71.484  -39.679 1.00 20.26 ? 680  VAL A CA  1 
ATOM   5391 C  C   . VAL A 1 680  ? 41.568 70.147  -40.182 1.00 22.00 ? 680  VAL A C   1 
ATOM   5392 O  O   . VAL A 1 680  ? 41.049 69.111  -39.745 1.00 22.68 ? 680  VAL A O   1 
ATOM   5393 C  CB  . VAL A 1 680  ? 41.587 71.709  -38.242 1.00 17.91 ? 680  VAL A CB  1 
ATOM   5394 C  CG1 . VAL A 1 680  ? 43.105 71.621  -38.164 1.00 19.19 ? 680  VAL A CG1 1 
ATOM   5395 C  CG2 . VAL A 1 680  ? 41.195 73.060  -37.822 1.00 15.03 ? 680  VAL A CG2 1 
ATOM   5396 N  N   . GLY A 1 681  ? 42.543 70.191  -41.107 1.00 23.55 ? 681  GLY A N   1 
ATOM   5397 C  CA  . GLY A 1 681  ? 43.110 68.985  -41.711 1.00 25.86 ? 681  GLY A CA  1 
ATOM   5398 C  C   . GLY A 1 681  ? 42.065 68.060  -42.328 1.00 26.57 ? 681  GLY A C   1 
ATOM   5399 O  O   . GLY A 1 681  ? 41.103 68.529  -42.939 1.00 26.75 ? 681  GLY A O   1 
ATOM   5400 N  N   . ASN A 1 682  ? 42.256 66.749  -42.140 1.00 29.06 ? 682  ASN A N   1 
ATOM   5401 C  CA  . ASN A 1 682  ? 41.350 65.708  -42.636 1.00 30.94 ? 682  ASN A CA  1 
ATOM   5402 C  C   . ASN A 1 682  ? 40.209 65.566  -41.640 1.00 30.75 ? 682  ASN A C   1 
ATOM   5403 O  O   . ASN A 1 682  ? 39.232 64.845  -41.885 1.00 32.40 ? 682  ASN A O   1 
ATOM   5404 C  CB  . ASN A 1 682  ? 42.059 64.353  -42.663 1.00 33.16 ? 682  ASN A CB  1 
ATOM   5405 C  CG  . ASN A 1 682  ? 43.074 64.238  -43.761 1.00 36.26 ? 682  ASN A CG  1 
ATOM   5406 O  OD1 . ASN A 1 682  ? 42.826 63.579  -44.778 1.00 39.46 ? 682  ASN A OD1 1 
ATOM   5407 N  ND2 . ASN A 1 682  ? 44.236 64.868  -43.574 1.00 38.23 ? 682  ASN A ND2 1 
ATOM   5408 N  N   . GLY A 1 683  ? 40.358 66.242  -40.514 1.00 29.36 ? 683  GLY A N   1 
ATOM   5409 C  CA  . GLY A 1 683  ? 39.400 66.130  -39.426 1.00 27.98 ? 683  GLY A CA  1 
ATOM   5410 C  C   . GLY A 1 683  ? 37.922 66.348  -39.661 1.00 25.03 ? 683  GLY A C   1 
ATOM   5411 O  O   . GLY A 1 683  ? 37.491 66.543  -40.761 1.00 26.60 ? 683  GLY A O   1 
ATOM   5412 N  N   . PRO A 1 684  ? 37.121 66.297  -38.599 1.00 23.26 ? 684  PRO A N   1 
ATOM   5413 C  CA  . PRO A 1 684  ? 35.677 66.502  -38.683 1.00 21.48 ? 684  PRO A CA  1 
ATOM   5414 C  C   . PRO A 1 684  ? 35.378 67.957  -39.048 1.00 19.97 ? 684  PRO A C   1 
ATOM   5415 O  O   . PRO A 1 684  ? 36.206 68.852  -38.919 1.00 20.28 ? 684  PRO A O   1 
ATOM   5416 C  CB  . PRO A 1 684  ? 35.205 66.175  -37.268 1.00 21.18 ? 684  PRO A CB  1 
ATOM   5417 C  CG  . PRO A 1 684  ? 36.386 66.636  -36.438 1.00 20.81 ? 684  PRO A CG  1 
ATOM   5418 C  CD  . PRO A 1 684  ? 37.527 66.023  -37.205 1.00 22.75 ? 684  PRO A CD  1 
ATOM   5419 N  N   . THR A 1 685  ? 34.178 68.170  -39.544 1.00 19.83 ? 685  THR A N   1 
ATOM   5420 C  CA  . THR A 1 685  ? 33.726 69.493  -39.905 1.00 18.51 ? 685  THR A CA  1 
ATOM   5421 C  C   . THR A 1 685  ? 32.675 69.888  -38.865 1.00 18.02 ? 685  THR A C   1 
ATOM   5422 O  O   . THR A 1 685  ? 31.697 69.180  -38.669 1.00 18.57 ? 685  THR A O   1 
ATOM   5423 C  CB  . THR A 1 685  ? 33.104 69.496  -41.314 1.00 19.63 ? 685  THR A CB  1 
ATOM   5424 O  OG1 . THR A 1 685  ? 34.128 69.190  -42.266 1.00 20.72 ? 685  THR A OG1 1 
ATOM   5425 C  CG2 . THR A 1 685  ? 32.520 70.859  -41.590 1.00 19.38 ? 685  THR A CG2 1 
ATOM   5426 N  N   . LEU A 1 686  ? 32.900 71.011  -38.192 1.00 16.63 ? 686  LEU A N   1 
ATOM   5427 C  CA  . LEU A 1 686  ? 31.994 71.456  -37.159 1.00 17.41 ? 686  LEU A CA  1 
ATOM   5428 C  C   . LEU A 1 686  ? 31.210 72.655  -37.617 1.00 17.55 ? 686  LEU A C   1 
ATOM   5429 O  O   . LEU A 1 686  ? 31.767 73.600  -38.193 1.00 17.20 ? 686  LEU A O   1 
ATOM   5430 C  CB  . LEU A 1 686  ? 32.750 71.784  -35.838 1.00 20.33 ? 686  LEU A CB  1 
ATOM   5431 C  CG  . LEU A 1 686  ? 33.751 70.743  -35.289 1.00 21.68 ? 686  LEU A CG  1 
ATOM   5432 C  CD1 . LEU A 1 686  ? 34.111 71.094  -33.848 1.00 23.66 ? 686  LEU A CD1 1 
ATOM   5433 C  CD2 . LEU A 1 686  ? 33.202 69.375  -35.365 1.00 22.43 ? 686  LEU A CD2 1 
ATOM   5434 N  N   . ALA A 1 687  ? 29.917 72.623  -37.357 1.00 16.94 ? 687  ALA A N   1 
ATOM   5435 C  CA  . ALA A 1 687  ? 29.061 73.748  -37.722 1.00 17.42 ? 687  ALA A CA  1 
ATOM   5436 C  C   . ALA A 1 687  ? 28.621 74.433  -36.405 1.00 18.27 ? 687  ALA A C   1 
ATOM   5437 O  O   . ALA A 1 687  ? 28.269 73.773  -35.397 1.00 17.60 ? 687  ALA A O   1 
ATOM   5438 C  CB  . ALA A 1 687  ? 27.835 73.256  -38.499 1.00 18.65 ? 687  ALA A CB  1 
ATOM   5439 N  N   . PHE A 1 688  ? 28.596 75.753  -36.432 1.00 16.06 ? 688  PHE A N   1 
ATOM   5440 C  CA  . PHE A 1 688  ? 28.229 76.562  -35.271 1.00 13.96 ? 688  PHE A CA  1 
ATOM   5441 C  C   . PHE A 1 688  ? 27.068 77.517  -35.557 1.00 16.50 ? 688  PHE A C   1 
ATOM   5442 O  O   . PHE A 1 688  ? 26.954 78.060  -36.682 1.00 18.21 ? 688  PHE A O   1 
ATOM   5443 C  CB  . PHE A 1 688  ? 29.410 77.431  -34.830 1.00 14.41 ? 688  PHE A CB  1 
ATOM   5444 C  CG  . PHE A 1 688  ? 30.651 76.641  -34.465 1.00 13.52 ? 688  PHE A CG  1 
ATOM   5445 C  CD1 . PHE A 1 688  ? 31.483 76.157  -35.458 1.00 13.36 ? 688  PHE A CD1 1 
ATOM   5446 C  CD2 . PHE A 1 688  ? 30.932 76.341  -33.127 1.00 13.76 ? 688  PHE A CD2 1 
ATOM   5447 C  CE1 . PHE A 1 688  ? 32.593 75.356  -35.175 1.00 14.56 ? 688  PHE A CE1 1 
ATOM   5448 C  CE2 . PHE A 1 688  ? 32.062 75.526  -32.803 1.00 13.13 ? 688  PHE A CE2 1 
ATOM   5449 C  CZ  . PHE A 1 688  ? 32.894 75.028  -33.818 1.00 12.82 ? 688  PHE A CZ  1 
ATOM   5450 N  N   . SER A 1 689  ? 26.230 77.732  -34.547 1.00 14.72 ? 689  SER A N   1 
ATOM   5451 C  CA  . SER A 1 689  ? 25.094 78.662  -34.613 1.00 15.80 ? 689  SER A CA  1 
ATOM   5452 C  C   . SER A 1 689  ? 25.629 80.081  -34.668 1.00 15.84 ? 689  SER A C   1 
ATOM   5453 O  O   . SER A 1 689  ? 26.802 80.322  -34.445 1.00 16.02 ? 689  SER A O   1 
ATOM   5454 C  CB  . SER A 1 689  ? 24.180 78.526  -33.370 1.00 16.22 ? 689  SER A CB  1 
ATOM   5455 O  OG  . SER A 1 689  ? 24.717 79.118  -32.189 1.00 16.35 ? 689  SER A OG  1 
ATOM   5456 N  N   . GLU A 1 690  ? 24.755 81.025  -34.996 1.00 17.00 ? 690  GLU A N   1 
ATOM   5457 C  CA  . GLU A 1 690  ? 25.159 82.435  -35.027 1.00 18.11 ? 690  GLU A CA  1 
ATOM   5458 C  C   . GLU A 1 690  ? 25.496 82.908  -33.595 1.00 18.11 ? 690  GLU A C   1 
ATOM   5459 O  O   . GLU A 1 690  ? 26.079 83.973  -33.401 1.00 16.60 ? 690  GLU A O   1 
ATOM   5460 C  CB  . GLU A 1 690  ? 24.034 83.304  -35.668 1.00 21.12 ? 690  GLU A CB  1 
ATOM   5461 C  CG  . GLU A 1 690  ? 22.807 83.623  -34.801 1.00 26.23 ? 690  GLU A CG  1 
ATOM   5462 C  CD  . GLU A 1 690  ? 21.907 84.704  -35.483 1.00 29.45 ? 690  GLU A CD  1 
ATOM   5463 O  OE1 . GLU A 1 690  ? 21.225 84.365  -36.480 1.00 31.69 ? 690  GLU A OE1 1 
ATOM   5464 O  OE2 . GLU A 1 690  ? 21.886 85.889  -35.036 1.00 32.34 ? 690  GLU A OE2 1 
ATOM   5465 N  N   . GLN A 1 691  ? 25.162 82.087  -32.584 1.00 17.87 ? 691  GLN A N   1 
ATOM   5466 C  CA  . GLN A 1 691  ? 25.489 82.406  -31.191 1.00 17.30 ? 691  GLN A CA  1 
ATOM   5467 C  C   . GLN A 1 691  ? 26.888 81.824  -30.794 1.00 16.04 ? 691  GLN A C   1 
ATOM   5468 O  O   . GLN A 1 691  ? 27.307 81.990  -29.679 1.00 16.63 ? 691  GLN A O   1 
ATOM   5469 C  CB  . GLN A 1 691  ? 24.435 81.850  -30.230 1.00 20.27 ? 691  GLN A CB  1 
ATOM   5470 C  CG  . GLN A 1 691  ? 23.157 82.686  -30.138 1.00 24.14 ? 691  GLN A CG  1 
ATOM   5471 C  CD  . GLN A 1 691  ? 21.934 81.807  -30.016 1.00 28.79 ? 691  GLN A CD  1 
ATOM   5472 O  OE1 . GLN A 1 691  ? 21.900 80.841  -29.248 1.00 29.16 ? 691  GLN A OE1 1 
ATOM   5473 N  NE2 . GLN A 1 691  ? 20.915 82.122  -30.812 1.00 32.46 ? 691  GLN A NE2 1 
ATOM   5474 N  N   . GLY A 1 692  ? 27.546 81.129  -31.706 1.00 13.31 ? 692  GLY A N   1 
ATOM   5475 C  CA  . GLY A 1 692  ? 28.902 80.628  -31.495 1.00 14.39 ? 692  GLY A CA  1 
ATOM   5476 C  C   . GLY A 1 692  ? 28.967 79.278  -30.823 1.00 13.94 ? 692  GLY A C   1 
ATOM   5477 O  O   . GLY A 1 692  ? 30.020 78.860  -30.392 1.00 15.58 ? 692  GLY A O   1 
ATOM   5478 N  N   . LEU A 1 693  ? 27.837 78.606  -30.760 1.00 14.43 ? 693  LEU A N   1 
ATOM   5479 C  CA  . LEU A 1 693  ? 27.744 77.290  -30.123 1.00 14.71 ? 693  LEU A CA  1 
ATOM   5480 C  C   . LEU A 1 693  ? 27.624 76.191  -31.160 1.00 16.01 ? 693  LEU A C   1 
ATOM   5481 O  O   . LEU A 1 693  ? 26.970 76.340  -32.224 1.00 13.89 ? 693  LEU A O   1 
ATOM   5482 C  CB  . LEU A 1 693  ? 26.516 77.265  -29.221 1.00 15.45 ? 693  LEU A CB  1 
ATOM   5483 C  CG  . LEU A 1 693  ? 26.464 78.253  -28.056 1.00 17.49 ? 693  LEU A CG  1 
ATOM   5484 C  CD1 . LEU A 1 693  ? 25.027 78.471  -27.583 1.00 17.50 ? 693  LEU A CD1 1 
ATOM   5485 C  CD2 . LEU A 1 693  ? 27.310 77.720  -26.919 1.00 19.01 ? 693  LEU A CD2 1 
ATOM   5486 N  N   . LEU A 1 694  ? 28.267 75.072  -30.874 1.00 14.83 ? 694  LEU A N   1 
ATOM   5487 C  CA  . LEU A 1 694  ? 28.245 73.941  -31.765 1.00 15.40 ? 694  LEU A CA  1 
ATOM   5488 C  C   . LEU A 1 694  ? 26.793 73.528  -32.076 1.00 13.45 ? 694  LEU A C   1 
ATOM   5489 O  O   . LEU A 1 694  ? 25.916 73.559  -31.177 1.00 15.02 ? 694  LEU A O   1 
ATOM   5490 C  CB  . LEU A 1 694  ? 29.000 72.772  -31.111 1.00 15.36 ? 694  LEU A CB  1 
ATOM   5491 C  CG  . LEU A 1 694  ? 29.119 71.508  -31.950 1.00 16.02 ? 694  LEU A CG  1 
ATOM   5492 C  CD1 . LEU A 1 694  ? 30.034 71.752  -33.159 1.00 16.02 ? 694  LEU A CD1 1 
ATOM   5493 C  CD2 . LEU A 1 694  ? 29.729 70.381  -31.061 1.00 15.54 ? 694  LEU A CD2 1 
ATOM   5494 N  N   . LYS A 1 695  ? 26.566 73.171  -33.344 1.00 14.39 ? 695  LYS A N   1 
ATOM   5495 C  CA  . LYS A 1 695  ? 25.238 72.737  -33.833 1.00 16.26 ? 695  LYS A CA  1 
ATOM   5496 C  C   . LYS A 1 695  ? 25.270 71.341  -34.431 1.00 15.21 ? 695  LYS A C   1 
ATOM   5497 O  O   . LYS A 1 695  ? 24.309 70.581  -34.307 1.00 16.60 ? 695  LYS A O   1 
ATOM   5498 C  CB  . LYS A 1 695  ? 24.779 73.723  -34.914 1.00 19.00 ? 695  LYS A CB  1 
ATOM   5499 C  CG  . LYS A 1 695  ? 23.385 73.649  -35.379 1.00 26.19 ? 695  LYS A CG  1 
ATOM   5500 C  CD  . LYS A 1 695  ? 23.255 74.725  -36.530 1.00 26.49 ? 695  LYS A CD  1 
ATOM   5501 C  CE  . LYS A 1 695  ? 21.889 74.699  -37.239 1.00 31.18 ? 695  LYS A CE  1 
ATOM   5502 N  NZ  . LYS A 1 695  ? 21.694 75.852  -38.214 1.00 31.60 ? 695  LYS A NZ  1 
ATOM   5503 N  N   . SER A 1 696  ? 26.374 71.008  -35.087 1.00 15.74 ? 696  SER A N   1 
ATOM   5504 C  CA  . SER A 1 696  ? 26.528 69.709  -35.694 1.00 16.33 ? 696  SER A CA  1 
ATOM   5505 C  C   . SER A 1 696  ? 27.970 69.351  -35.932 1.00 16.12 ? 696  SER A C   1 
ATOM   5506 O  O   . SER A 1 696  ? 28.876 70.224  -35.966 1.00 15.79 ? 696  SER A O   1 
ATOM   5507 C  CB  . SER A 1 696  ? 25.751 69.597  -37.034 1.00 17.53 ? 696  SER A CB  1 
ATOM   5508 O  OG  . SER A 1 696  ? 26.316 70.453  -38.013 1.00 18.75 ? 696  SER A OG  1 
ATOM   5509 N  N   . ILE A 1 697  ? 28.192 68.050  -36.108 1.00 17.56 ? 697  ILE A N   1 
ATOM   5510 C  CA  . ILE A 1 697  ? 29.514 67.513  -36.366 1.00 18.37 ? 697  ILE A CA  1 
ATOM   5511 C  C   . ILE A 1 697  ? 29.397 66.550  -37.531 1.00 20.70 ? 697  ILE A C   1 
ATOM   5512 O  O   . ILE A 1 697  ? 28.531 65.655  -37.537 1.00 21.91 ? 697  ILE A O   1 
ATOM   5513 C  CB  . ILE A 1 697  ? 30.107 66.694  -35.144 1.00 16.76 ? 697  ILE A CB  1 
ATOM   5514 C  CG1 . ILE A 1 697  ? 30.194 67.572  -33.890 1.00 15.40 ? 697  ILE A CG1 1 
ATOM   5515 C  CG2 . ILE A 1 697  ? 31.470 66.085  -35.543 1.00 18.65 ? 697  ILE A CG2 1 
ATOM   5516 C  CD1 . ILE A 1 697  ? 30.732 66.815  -32.603 1.00 17.15 ? 697  ILE A CD1 1 
ATOM   5517 N  N   . GLN A 1 698  ? 30.255 66.733  -38.520 1.00 21.77 ? 698  GLN A N   1 
ATOM   5518 C  CA  . GLN A 1 698  ? 30.262 65.869  -39.684 1.00 24.11 ? 698  GLN A CA  1 
ATOM   5519 C  C   . GLN A 1 698  ? 31.609 65.206  -39.669 1.00 24.72 ? 698  GLN A C   1 
ATOM   5520 O  O   . GLN A 1 698  ? 32.638 65.868  -39.852 1.00 24.94 ? 698  GLN A O   1 
ATOM   5521 C  CB  . GLN A 1 698  ? 30.074 66.663  -40.985 1.00 25.26 ? 698  GLN A CB  1 
ATOM   5522 C  CG  . GLN A 1 698  ? 30.226 65.788  -42.219 1.00 28.56 ? 698  GLN A CG  1 
ATOM   5523 C  CD  . GLN A 1 698  ? 30.166 66.596  -43.518 1.00 31.15 ? 698  GLN A CD  1 
ATOM   5524 O  OE1 . GLN A 1 698  ? 30.846 67.739  -43.537 1.00 32.90 ? 698  GLN A OE1 1 
ATOM   5525 N  NE2 . GLN A 1 698  ? 29.519 66.183  -44.494 1.00 30.59 ? 698  GLN A NE2 1 
ATOM   5526 N  N   . LEU A 1 699  ? 31.591 63.901  -39.432 1.00 27.54 ? 699  LEU A N   1 
ATOM   5527 C  CA  . LEU A 1 699  ? 32.813 63.124  -39.324 1.00 30.78 ? 699  LEU A CA  1 
ATOM   5528 C  C   . LEU A 1 699  ? 33.676 63.060  -40.575 1.00 33.78 ? 699  LEU A C   1 
ATOM   5529 O  O   . LEU A 1 699  ? 34.885 63.198  -40.490 1.00 33.68 ? 699  LEU A O   1 
ATOM   5530 C  CB  . LEU A 1 699  ? 32.488 61.708  -38.832 1.00 29.76 ? 699  LEU A CB  1 
ATOM   5531 C  CG  . LEU A 1 699  ? 31.952 61.541  -37.400 1.00 31.10 ? 699  LEU A CG  1 
ATOM   5532 C  CD1 . LEU A 1 699  ? 32.226 60.106  -37.005 1.00 30.14 ? 699  LEU A CD1 1 
ATOM   5533 C  CD2 . LEU A 1 699  ? 32.649 62.469  -36.402 1.00 30.91 ? 699  LEU A CD2 1 
ATOM   5534 N  N   . THR A 1 700  ? 33.067 62.830  -41.730 1.00 37.18 ? 700  THR A N   1 
ATOM   5535 C  CA  . THR A 1 700  ? 33.830 62.757  -42.973 1.00 40.66 ? 700  THR A CA  1 
ATOM   5536 C  C   . THR A 1 700  ? 33.151 63.681  -43.952 1.00 42.76 ? 700  THR A C   1 
ATOM   5537 O  O   . THR A 1 700  ? 31.981 64.015  -43.786 1.00 43.17 ? 700  THR A O   1 
ATOM   5538 C  CB  . THR A 1 700  ? 33.849 61.339  -43.539 1.00 41.20 ? 700  THR A CB  1 
ATOM   5539 O  OG1 . THR A 1 700  ? 32.524 60.789  -43.483 1.00 42.46 ? 700  THR A OG1 1 
ATOM   5540 C  CG2 . THR A 1 700  ? 34.792 60.466  -42.742 1.00 41.09 ? 700  THR A CG2 1 
ATOM   5541 N  N   . GLN A 1 701  ? 33.872 64.092  -44.979 1.00 45.39 ? 701  GLN A N   1 
ATOM   5542 C  CA  . GLN A 1 701  ? 33.312 65.032  -45.936 1.00 48.01 ? 701  GLN A CA  1 
ATOM   5543 C  C   . GLN A 1 701  ? 31.968 64.644  -46.584 1.00 48.32 ? 701  GLN A C   1 
ATOM   5544 O  O   . GLN A 1 701  ? 31.210 65.525  -47.011 1.00 48.61 ? 701  GLN A O   1 
ATOM   5545 C  CB  . GLN A 1 701  ? 34.343 65.323  -47.018 1.00 50.31 ? 701  GLN A CB  1 
ATOM   5546 C  CG  . GLN A 1 701  ? 33.987 66.524  -47.853 1.00 53.62 ? 701  GLN A CG  1 
ATOM   5547 C  CD  . GLN A 1 701  ? 34.830 66.602  -49.092 1.00 55.49 ? 701  GLN A CD  1 
ATOM   5548 O  OE1 . GLN A 1 701  ? 36.061 66.722  -49.012 1.00 56.54 ? 701  GLN A OE1 1 
ATOM   5549 N  NE2 . GLN A 1 701  ? 34.177 66.523  -50.261 1.00 56.22 ? 701  GLN A NE2 1 
ATOM   5550 N  N   . ASP A 1 702  ? 31.661 63.345  -46.641 1.00 48.25 ? 702  ASP A N   1 
ATOM   5551 C  CA  . ASP A 1 702  ? 30.404 62.882  -47.250 1.00 48.29 ? 702  ASP A CA  1 
ATOM   5552 C  C   . ASP A 1 702  ? 29.281 62.413  -46.283 1.00 46.53 ? 702  ASP A C   1 
ATOM   5553 O  O   . ASP A 1 702  ? 28.118 62.246  -46.700 1.00 45.94 ? 702  ASP A O   1 
ATOM   5554 C  CB  . ASP A 1 702  ? 30.715 61.749  -48.232 1.00 51.23 ? 702  ASP A CB  1 
ATOM   5555 C  CG  . ASP A 1 702  ? 31.403 60.575  -47.555 1.00 53.66 ? 702  ASP A CG  1 
ATOM   5556 O  OD1 . ASP A 1 702  ? 32.454 60.817  -46.910 1.00 55.03 ? 702  ASP A OD1 1 
ATOM   5557 O  OD2 . ASP A 1 702  ? 30.900 59.425  -47.660 1.00 54.80 ? 702  ASP A OD2 1 
ATOM   5558 N  N   . SER A 1 703  ? 29.638 62.198  -45.015 1.00 43.66 ? 703  SER A N   1 
ATOM   5559 C  CA  . SER A 1 703  ? 28.705 61.748  -43.976 1.00 40.55 ? 703  SER A CA  1 
ATOM   5560 C  C   . SER A 1 703  ? 27.736 62.831  -43.528 1.00 38.56 ? 703  SER A C   1 
ATOM   5561 O  O   . SER A 1 703  ? 27.919 64.009  -43.824 1.00 37.73 ? 703  SER A O   1 
ATOM   5562 C  CB  . SER A 1 703  ? 29.487 61.243  -42.759 1.00 40.59 ? 703  SER A CB  1 
ATOM   5563 O  OG  . SER A 1 703  ? 30.314 62.251  -42.201 1.00 39.94 ? 703  SER A OG  1 
ATOM   5564 N  N   . PRO A 1 704  ? 26.689 62.441  -42.788 1.00 36.94 ? 704  PRO A N   1 
ATOM   5565 C  CA  . PRO A 1 704  ? 25.698 63.393  -42.309 1.00 35.40 ? 704  PRO A CA  1 
ATOM   5566 C  C   . PRO A 1 704  ? 26.194 64.315  -41.220 1.00 33.78 ? 704  PRO A C   1 
ATOM   5567 O  O   . PRO A 1 704  ? 27.172 64.027  -40.536 1.00 34.00 ? 704  PRO A O   1 
ATOM   5568 C  CB  . PRO A 1 704  ? 24.551 62.507  -41.846 1.00 35.98 ? 704  PRO A CB  1 
ATOM   5569 C  CG  . PRO A 1 704  ? 25.204 61.271  -41.452 1.00 37.19 ? 704  PRO A CG  1 
ATOM   5570 C  CD  . PRO A 1 704  ? 26.295 61.061  -42.456 1.00 36.85 ? 704  PRO A CD  1 
ATOM   5571 N  N   . HIS A 1 705  ? 25.511 65.447  -41.097 1.00 31.30 ? 705  HIS A N   1 
ATOM   5572 C  CA  . HIS A 1 705  ? 25.828 66.439  -40.094 1.00 29.12 ? 705  HIS A CA  1 
ATOM   5573 C  C   . HIS A 1 705  ? 25.001 66.028  -38.901 1.00 26.61 ? 705  HIS A C   1 
ATOM   5574 O  O   . HIS A 1 705  ? 23.811 66.334  -38.798 1.00 26.12 ? 705  HIS A O   1 
ATOM   5575 C  CB  . HIS A 1 705  ? 25.422 67.826  -40.571 1.00 30.14 ? 705  HIS A CB  1 
ATOM   5576 C  CG  . HIS A 1 705  ? 26.242 68.321  -41.721 1.00 32.70 ? 705  HIS A CG  1 
ATOM   5577 N  ND1 . HIS A 1 705  ? 27.444 68.976  -41.557 1.00 33.34 ? 705  HIS A ND1 1 
ATOM   5578 C  CD2 . HIS A 1 705  ? 26.033 68.250  -43.057 1.00 32.98 ? 705  HIS A CD2 1 
ATOM   5579 C  CE1 . HIS A 1 705  ? 27.937 69.294  -42.740 1.00 35.17 ? 705  HIS A CE1 1 
ATOM   5580 N  NE2 . HIS A 1 705  ? 27.097 68.865  -43.668 1.00 34.57 ? 705  HIS A NE2 1 
ATOM   5581 N  N   . VAL A 1 706  ? 25.649 65.311  -37.995 1.00 23.51 ? 706  VAL A N   1 
ATOM   5582 C  CA  . VAL A 1 706  ? 24.994 64.807  -36.810 1.00 21.27 ? 706  VAL A CA  1 
ATOM   5583 C  C   . VAL A 1 706  ? 24.698 65.948  -35.852 1.00 19.63 ? 706  VAL A C   1 
ATOM   5584 O  O   . VAL A 1 706  ? 25.623 66.640  -35.445 1.00 18.46 ? 706  VAL A O   1 
ATOM   5585 C  CB  . VAL A 1 706  ? 25.938 63.821  -36.099 1.00 21.18 ? 706  VAL A CB  1 
ATOM   5586 C  CG1 . VAL A 1 706  ? 25.252 63.229  -34.891 1.00 20.28 ? 706  VAL A CG1 1 
ATOM   5587 C  CG2 . VAL A 1 706  ? 26.384 62.743  -37.060 1.00 21.28 ? 706  VAL A CG2 1 
ATOM   5588 N  N   . PRO A 1 707  ? 23.419 66.161  -35.477 1.00 18.52 ? 707  PRO A N   1 
ATOM   5589 C  CA  . PRO A 1 707  ? 23.013 67.225  -34.546 1.00 17.97 ? 707  PRO A CA  1 
ATOM   5590 C  C   . PRO A 1 707  ? 23.720 66.993  -33.196 1.00 18.43 ? 707  PRO A C   1 
ATOM   5591 O  O   . PRO A 1 707  ? 23.646 65.907  -32.634 1.00 19.00 ? 707  PRO A O   1 
ATOM   5592 C  CB  . PRO A 1 707  ? 21.509 67.048  -34.422 1.00 16.00 ? 707  PRO A CB  1 
ATOM   5593 C  CG  . PRO A 1 707  ? 21.103 66.427  -35.741 1.00 20.26 ? 707  PRO A CG  1 
ATOM   5594 C  CD  . PRO A 1 707  ? 22.241 65.495  -36.094 1.00 18.00 ? 707  PRO A CD  1 
ATOM   5595 N  N   . VAL A 1 708  ? 24.461 67.997  -32.750 1.00 17.27 ? 708  VAL A N   1 
ATOM   5596 C  CA  . VAL A 1 708  ? 25.208 67.985  -31.477 1.00 16.72 ? 708  VAL A CA  1 
ATOM   5597 C  C   . VAL A 1 708  ? 25.212 69.463  -31.080 1.00 16.74 ? 708  VAL A C   1 
ATOM   5598 O  O   . VAL A 1 708  ? 25.988 70.316  -31.597 1.00 15.71 ? 708  VAL A O   1 
ATOM   5599 C  CB  . VAL A 1 708  ? 26.671 67.464  -31.620 1.00 15.13 ? 708  VAL A CB  1 
ATOM   5600 C  CG1 . VAL A 1 708  ? 27.346 67.507  -30.180 1.00 16.04 ? 708  VAL A CG1 1 
ATOM   5601 C  CG2 . VAL A 1 708  ? 26.687 66.023  -32.151 1.00 15.80 ? 708  VAL A CG2 1 
ATOM   5602 N  N   . HIS A 1 709  ? 24.327 69.792  -30.148 1.00 16.05 ? 709  HIS A N   1 
ATOM   5603 C  CA  . HIS A 1 709  ? 24.143 71.187  -29.732 1.00 17.43 ? 709  HIS A CA  1 
ATOM   5604 C  C   . HIS A 1 709  ? 24.558 71.529  -28.292 1.00 17.17 ? 709  HIS A C   1 
ATOM   5605 O  O   . HIS A 1 709  ? 24.039 70.925  -27.348 1.00 16.12 ? 709  HIS A O   1 
ATOM   5606 C  CB  A HIS A 1 709  ? 22.656 71.567  -29.888 0.50 19.73 ? 709  HIS A CB  1 
ATOM   5607 C  CB  B HIS A 1 709  ? 22.811 71.697  -30.027 0.50 18.93 ? 709  HIS A CB  1 
ATOM   5608 C  CG  A HIS A 1 709  ? 22.112 71.420  -31.278 0.50 21.64 ? 709  HIS A CG  1 
ATOM   5609 C  CG  B HIS A 1 709  ? 22.581 73.131  -29.650 0.50 20.53 ? 709  HIS A CG  1 
ATOM   5610 N  ND1 A HIS A 1 709  ? 21.998 72.480  -32.150 0.50 23.75 ? 709  HIS A ND1 1 
ATOM   5611 N  ND1 B HIS A 1 709  ? 23.336 74.167  -30.162 0.50 19.72 ? 709  HIS A ND1 1 
ATOM   5612 C  CD2 A HIS A 1 709  ? 21.634 70.341  -31.939 0.50 23.16 ? 709  HIS A CD2 1 
ATOM   5613 C  CD2 B HIS A 1 709  ? 21.681 73.700  -28.813 0.50 21.61 ? 709  HIS A CD2 1 
ATOM   5614 C  CE1 A HIS A 1 709  ? 21.475 72.061  -33.286 0.50 22.91 ? 709  HIS A CE1 1 
ATOM   5615 C  CE1 B HIS A 1 709  ? 22.914 75.310  -29.653 0.50 22.23 ? 709  HIS A CE1 1 
ATOM   5616 N  NE2 A HIS A 1 709  ? 21.247 70.765  -33.185 0.50 22.95 ? 709  HIS A NE2 1 
ATOM   5617 N  NE2 B HIS A 1 709  ? 21.911 75.056  -28.831 0.50 22.41 ? 709  HIS A NE2 1 
ATOM   5618 N  N   . PHE A 1 710  ? 25.462 72.499  -28.120 1.00 16.30 ? 710  PHE A N   1 
ATOM   5619 C  CA  . PHE A 1 710  ? 25.861 72.937  -26.785 1.00 15.38 ? 710  PHE A CA  1 
ATOM   5620 C  C   . PHE A 1 710  ? 24.846 73.997  -26.400 1.00 17.01 ? 710  PHE A C   1 
ATOM   5621 O  O   . PHE A 1 710  ? 24.411 74.823  -27.253 1.00 15.94 ? 710  PHE A O   1 
ATOM   5622 C  CB  . PHE A 1 710  ? 27.261 73.577  -26.739 1.00 15.76 ? 710  PHE A CB  1 
ATOM   5623 C  CG  . PHE A 1 710  ? 28.377 72.611  -26.383 1.00 16.32 ? 710  PHE A CG  1 
ATOM   5624 C  CD1 . PHE A 1 710  ? 28.385 71.909  -25.182 1.00 18.38 ? 710  PHE A CD1 1 
ATOM   5625 C  CD2 . PHE A 1 710  ? 29.433 72.417  -27.260 1.00 17.57 ? 710  PHE A CD2 1 
ATOM   5626 C  CE1 . PHE A 1 710  ? 29.451 71.034  -24.882 1.00 18.65 ? 710  PHE A CE1 1 
ATOM   5627 C  CE2 . PHE A 1 710  ? 30.471 71.557  -26.950 1.00 17.17 ? 710  PHE A CE2 1 
ATOM   5628 C  CZ  . PHE A 1 710  ? 30.484 70.880  -25.778 1.00 16.69 ? 710  PHE A CZ  1 
ATOM   5629 N  N   . LYS A 1 711  ? 24.462 73.985  -25.124 1.00 14.45 ? 711  LYS A N   1 
ATOM   5630 C  CA  . LYS A 1 711  ? 23.503 74.942  -24.584 1.00 15.21 ? 711  LYS A CA  1 
ATOM   5631 C  C   . LYS A 1 711  ? 23.849 75.171  -23.124 1.00 15.07 ? 711  LYS A C   1 
ATOM   5632 O  O   . LYS A 1 711  ? 24.229 74.224  -22.396 1.00 18.23 ? 711  LYS A O   1 
ATOM   5633 C  CB  . LYS A 1 711  ? 22.059 74.398  -24.689 1.00 16.03 ? 711  LYS A CB  1 
ATOM   5634 C  CG  . LYS A 1 711  ? 20.977 75.393  -24.362 1.00 17.97 ? 711  LYS A CG  1 
ATOM   5635 C  CD  . LYS A 1 711  ? 19.560 74.741  -24.439 1.00 22.21 ? 711  LYS A CD  1 
ATOM   5636 C  CE  . LYS A 1 711  ? 19.033 74.663  -25.877 1.00 24.20 ? 711  LYS A CE  1 
ATOM   5637 N  NZ  . LYS A 1 711  ? 17.646 74.050  -25.970 1.00 27.31 ? 711  LYS A NZ  1 
ATOM   5638 N  N   . PHE A 1 712  ? 23.727 76.396  -22.653 1.00 14.17 ? 712  PHE A N   1 
ATOM   5639 C  CA  . PHE A 1 712  ? 23.999 76.689  -21.255 1.00 12.78 ? 712  PHE A CA  1 
ATOM   5640 C  C   . PHE A 1 712  ? 22.710 77.045  -20.554 1.00 14.26 ? 712  PHE A C   1 
ATOM   5641 O  O   . PHE A 1 712  ? 21.890 77.827  -21.093 1.00 14.07 ? 712  PHE A O   1 
ATOM   5642 C  CB  . PHE A 1 712  ? 25.012 77.831  -21.108 1.00 14.20 ? 712  PHE A CB  1 
ATOM   5643 C  CG  . PHE A 1 712  ? 26.425 77.410  -21.428 1.00 12.34 ? 712  PHE A CG  1 
ATOM   5644 C  CD1 . PHE A 1 712  ? 26.892 77.449  -22.764 1.00 13.43 ? 712  PHE A CD1 1 
ATOM   5645 C  CD2 . PHE A 1 712  ? 27.265 76.941  -20.433 1.00 13.62 ? 712  PHE A CD2 1 
ATOM   5646 C  CE1 . PHE A 1 712  ? 28.183 77.036  -23.085 1.00 10.21 ? 712  PHE A CE1 1 
ATOM   5647 C  CE2 . PHE A 1 712  ? 28.557 76.523  -20.729 1.00 11.37 ? 712  PHE A CE2 1 
ATOM   5648 C  CZ  . PHE A 1 712  ? 29.041 76.564  -22.038 1.00 12.81 ? 712  PHE A CZ  1 
ATOM   5649 N  N   . LEU A 1 713  ? 22.469 76.432  -19.398 1.00 12.13 ? 713  LEU A N   1 
ATOM   5650 C  CA  . LEU A 1 713  ? 21.229 76.678  -18.640 1.00 13.77 ? 713  LEU A CA  1 
ATOM   5651 C  C   . LEU A 1 713  ? 21.564 76.920  -17.186 1.00 12.43 ? 713  LEU A C   1 
ATOM   5652 O  O   . LEU A 1 713  ? 22.758 76.840  -16.780 1.00 13.20 ? 713  LEU A O   1 
ATOM   5653 C  CB  . LEU A 1 713  ? 20.259 75.503  -18.757 1.00 11.24 ? 713  LEU A CB  1 
ATOM   5654 C  CG  . LEU A 1 713  ? 19.971 74.997  -20.174 1.00 13.39 ? 713  LEU A CG  1 
ATOM   5655 C  CD1 . LEU A 1 713  ? 20.914 73.881  -20.521 1.00 15.50 ? 713  LEU A CD1 1 
ATOM   5656 C  CD2 . LEU A 1 713  ? 18.477 74.490  -20.270 1.00 14.44 ? 713  LEU A CD2 1 
ATOM   5657 N  N   . LYS A 1 714  ? 20.564 77.290  -16.408 1.00 13.70 ? 714  LYS A N   1 
ATOM   5658 C  CA  . LYS A 1 714  ? 20.793 77.510  -14.997 1.00 14.28 ? 714  LYS A CA  1 
ATOM   5659 C  C   . LYS A 1 714  ? 19.732 76.890  -14.141 1.00 15.21 ? 714  LYS A C   1 
ATOM   5660 O  O   . LYS A 1 714  ? 18.567 76.815  -14.551 1.00 14.94 ? 714  LYS A O   1 
ATOM   5661 C  CB  . LYS A 1 714  ? 20.895 78.978  -14.646 1.00 20.83 ? 714  LYS A CB  1 
ATOM   5662 C  CG  . LYS A 1 714  ? 19.690 79.765  -14.914 1.00 25.32 ? 714  LYS A CG  1 
ATOM   5663 C  CD  . LYS A 1 714  ? 20.033 81.224  -14.603 1.00 29.68 ? 714  LYS A CD  1 
ATOM   5664 C  CE  . LYS A 1 714  ? 21.197 81.705  -15.496 1.00 32.19 ? 714  LYS A CE  1 
ATOM   5665 N  NZ  . LYS A 1 714  ? 21.657 83.099  -15.177 1.00 34.64 ? 714  LYS A NZ  1 
ATOM   5666 N  N   . TYR A 1 715  ? 20.176 76.389  -12.983 1.00 12.72 ? 715  TYR A N   1 
ATOM   5667 C  CA  . TYR A 1 715  ? 19.326 75.814  -11.961 1.00 12.71 ? 715  TYR A CA  1 
ATOM   5668 C  C   . TYR A 1 715  ? 19.249 76.838  -10.845 1.00 12.86 ? 715  TYR A C   1 
ATOM   5669 O  O   . TYR A 1 715  ? 20.209 77.560  -10.572 1.00 13.71 ? 715  TYR A O   1 
ATOM   5670 C  CB  . TYR A 1 715  ? 19.916 74.506  -11.352 1.00 12.85 ? 715  TYR A CB  1 
ATOM   5671 C  CG  . TYR A 1 715  ? 19.836 73.362  -12.289 1.00 11.65 ? 715  TYR A CG  1 
ATOM   5672 C  CD1 . TYR A 1 715  ? 18.637 72.610  -12.374 1.00 8.48  ? 715  TYR A CD1 1 
ATOM   5673 C  CD2 . TYR A 1 715  ? 20.958 72.948  -13.042 1.00 9.42  ? 715  TYR A CD2 1 
ATOM   5674 C  CE1 . TYR A 1 715  ? 18.562 71.504  -13.139 1.00 10.86 ? 715  TYR A CE1 1 
ATOM   5675 C  CE2 . TYR A 1 715  ? 20.882 71.816  -13.849 1.00 11.09 ? 715  TYR A CE2 1 
ATOM   5676 C  CZ  . TYR A 1 715  ? 19.675 71.090  -13.887 1.00 10.32 ? 715  TYR A CZ  1 
ATOM   5677 O  OH  . TYR A 1 715  ? 19.548 69.940  -14.576 1.00 13.20 ? 715  TYR A OH  1 
ATOM   5678 N  N   . GLY A 1 716  ? 18.116 76.904  -10.172 1.00 15.00 ? 716  GLY A N   1 
ATOM   5679 C  CA  . GLY A 1 716  ? 17.976 77.794  -9.060  1.00 14.66 ? 716  GLY A CA  1 
ATOM   5680 C  C   . GLY A 1 716  ? 17.890 77.024  -7.755  1.00 15.59 ? 716  GLY A C   1 
ATOM   5681 O  O   . GLY A 1 716  ? 18.241 75.811  -7.622  1.00 16.05 ? 716  GLY A O   1 
ATOM   5682 N  N   . VAL A 1 717  ? 17.413 77.735  -6.753  1.00 16.12 ? 717  VAL A N   1 
ATOM   5683 C  CA  . VAL A 1 717  ? 17.251 77.204  -5.417  1.00 16.74 ? 717  VAL A CA  1 
ATOM   5684 C  C   . VAL A 1 717  ? 15.839 77.343  -4.862  1.00 19.91 ? 717  VAL A C   1 
ATOM   5685 O  O   . VAL A 1 717  ? 15.129 78.272  -5.230  1.00 21.49 ? 717  VAL A O   1 
ATOM   5686 C  CB  . VAL A 1 717  ? 18.211 77.889  -4.483  1.00 17.55 ? 717  VAL A CB  1 
ATOM   5687 C  CG1 . VAL A 1 717  ? 18.019 77.407  -3.124  1.00 19.95 ? 717  VAL A CG1 1 
ATOM   5688 C  CG2 . VAL A 1 717  ? 19.659 77.634  -4.936  1.00 15.70 ? 717  VAL A CG2 1 
ATOM   5689 N  N   . ARG A 1 718  ? 15.412 76.433  -3.987  1.00 19.49 ? 718  ARG A N   1 
ATOM   5690 C  CA  . ARG A 1 718  ? 14.047 76.517  -3.409  1.00 21.46 ? 718  ARG A CA  1 
ATOM   5691 C  C   . ARG A 1 718  ? 13.860 77.696  -2.445  1.00 23.39 ? 718  ARG A C   1 
ATOM   5692 O  O   . ARG A 1 718  ? 14.710 77.994  -1.623  1.00 23.18 ? 718  ARG A O   1 
ATOM   5693 C  CB  . ARG A 1 718  ? 13.677 75.196  -2.704  1.00 20.03 ? 718  ARG A CB  1 
ATOM   5694 C  CG  . ARG A 1 718  ? 13.585 74.061  -3.678  1.00 17.40 ? 718  ARG A CG  1 
ATOM   5695 C  CD  . ARG A 1 718  ? 13.602 72.691  -2.980  1.00 16.81 ? 718  ARG A CD  1 
ATOM   5696 N  NE  . ARG A 1 718  ? 13.906 71.687  -3.975  1.00 15.05 ? 718  ARG A NE  1 
ATOM   5697 C  CZ  . ARG A 1 718  ? 13.836 70.358  -3.835  1.00 13.99 ? 718  ARG A CZ  1 
ATOM   5698 N  NH1 . ARG A 1 718  ? 13.436 69.805  -2.697  1.00 13.27 ? 718  ARG A NH1 1 
ATOM   5699 N  NH2 . ARG A 1 718  ? 14.219 69.609  -4.832  1.00 17.47 ? 718  ARG A NH2 1 
ATOM   5700 N  N   . SER A 1 719  ? 12.720 78.376  -2.557  1.00 27.09 ? 719  SER A N   1 
ATOM   5701 C  CA  . SER A 1 719  ? 12.428 79.518  -1.682  1.00 30.90 ? 719  SER A CA  1 
ATOM   5702 C  C   . SER A 1 719  ? 11.868 79.108  -0.309  1.00 32.55 ? 719  SER A C   1 
ATOM   5703 O  O   . SER A 1 719  ? 12.053 79.819  0.684   1.00 32.61 ? 719  SER A O   1 
ATOM   5704 C  CB  . SER A 1 719  ? 11.456 80.475  -2.390  1.00 32.24 ? 719  SER A CB  1 
ATOM   5705 O  OG  . SER A 1 719  ? 10.549 79.760  -3.236  1.00 34.64 ? 719  SER A OG  1 
ATOM   5706 N  N   . HIS A 1 720  ? 11.181 77.966  -0.286  1.00 33.79 ? 720  HIS A N   1 
ATOM   5707 C  CA  . HIS A 1 720  ? 10.604 77.374  0.918   1.00 35.36 ? 720  HIS A CA  1 
ATOM   5708 C  C   . HIS A 1 720  ? 11.033 75.904  0.873   1.00 34.69 ? 720  HIS A C   1 
ATOM   5709 O  O   . HIS A 1 720  ? 11.052 75.266  -0.202  1.00 36.78 ? 720  HIS A O   1 
ATOM   5710 C  CB  . HIS A 1 720  ? 9.079  77.463  0.882   1.00 38.51 ? 720  HIS A CB  1 
ATOM   5711 C  CG  . HIS A 1 720  ? 8.473  76.806  -0.318  1.00 42.04 ? 720  HIS A CG  1 
ATOM   5712 N  ND1 . HIS A 1 720  ? 8.740  77.225  -1.609  1.00 43.73 ? 720  HIS A ND1 1 
ATOM   5713 C  CD2 . HIS A 1 720  ? 7.628  75.751  -0.429  1.00 43.30 ? 720  HIS A CD2 1 
ATOM   5714 C  CE1 . HIS A 1 720  ? 8.082  76.456  -2.461  1.00 44.24 ? 720  HIS A CE1 1 
ATOM   5715 N  NE2 . HIS A 1 720  ? 7.402  75.554  -1.772  1.00 44.32 ? 720  HIS A NE2 1 
ATOM   5716 N  N   . GLY A 1 721  ? 11.381 75.361  2.025   1.00 32.32 ? 721  GLY A N   1 
ATOM   5717 C  CA  . GLY A 1 721  ? 11.824 73.980  2.041   1.00 27.97 ? 721  GLY A CA  1 
ATOM   5718 C  C   . GLY A 1 721  ? 13.347 73.973  2.159   1.00 24.21 ? 721  GLY A C   1 
ATOM   5719 O  O   . GLY A 1 721  ? 13.969 75.026  2.335   1.00 22.68 ? 721  GLY A O   1 
ATOM   5720 N  N   . ASP A 1 722  ? 13.953 72.802  2.012   1.00 20.75 ? 722  ASP A N   1 
ATOM   5721 C  CA  . ASP A 1 722  ? 15.398 72.674  2.167   1.00 20.26 ? 722  ASP A CA  1 
ATOM   5722 C  C   . ASP A 1 722  ? 16.175 73.349  1.043   1.00 17.40 ? 722  ASP A C   1 
ATOM   5723 O  O   . ASP A 1 722  ? 15.806 73.273  -0.117  1.00 18.01 ? 722  ASP A O   1 
ATOM   5724 C  CB  . ASP A 1 722  ? 15.771 71.198  2.200   1.00 18.40 ? 722  ASP A CB  1 
ATOM   5725 C  CG  . ASP A 1 722  ? 15.157 70.466  3.383   1.00 19.93 ? 722  ASP A CG  1 
ATOM   5726 O  OD1 . ASP A 1 722  ? 14.927 71.099  4.457   1.00 18.38 ? 722  ASP A OD1 1 
ATOM   5727 O  OD2 . ASP A 1 722  ? 14.928 69.235  3.213   1.00 18.22 ? 722  ASP A OD2 1 
ATOM   5728 N  N   . ARG A 1 723  ? 17.256 74.035  1.398   1.00 17.16 ? 723  ARG A N   1 
ATOM   5729 C  CA  . ARG A 1 723  ? 18.079 74.709  0.395   1.00 17.08 ? 723  ARG A CA  1 
ATOM   5730 C  C   . ARG A 1 723  ? 19.385 73.992  0.018   1.00 13.92 ? 723  ARG A C   1 
ATOM   5731 O  O   . ARG A 1 723  ? 20.031 73.353  0.850   1.00 14.12 ? 723  ARG A O   1 
ATOM   5732 C  CB  . ARG A 1 723  ? 18.497 76.081  0.894   1.00 17.69 ? 723  ARG A CB  1 
ATOM   5733 C  CG  . ARG A 1 723  ? 17.473 77.184  0.716   1.00 26.07 ? 723  ARG A CG  1 
ATOM   5734 C  CD  . ARG A 1 723  ? 16.237 76.957  1.553   1.00 29.58 ? 723  ARG A CD  1 
ATOM   5735 N  NE  . ARG A 1 723  ? 15.379 78.155  1.594   1.00 34.02 ? 723  ARG A NE  1 
ATOM   5736 C  CZ  . ARG A 1 723  ? 15.838 79.398  1.750   1.00 35.11 ? 723  ARG A CZ  1 
ATOM   5737 N  NH1 . ARG A 1 723  ? 17.150 79.620  1.874   1.00 35.86 ? 723  ARG A NH1 1 
ATOM   5738 N  NH2 . ARG A 1 723  ? 14.985 80.418  1.806   1.00 35.73 ? 723  ARG A NH2 1 
ATOM   5739 N  N   . SER A 1 724  ? 19.754 74.140  -1.239  1.00 14.73 ? 724  SER A N   1 
ATOM   5740 C  CA  . SER A 1 724  ? 21.023 73.631  -1.713  1.00 12.84 ? 724  SER A CA  1 
ATOM   5741 C  C   . SER A 1 724  ? 22.123 74.322  -0.921  1.00 14.00 ? 724  SER A C   1 
ATOM   5742 O  O   . SER A 1 724  ? 21.994 75.461  -0.508  1.00 15.59 ? 724  SER A O   1 
ATOM   5743 C  CB  . SER A 1 724  ? 21.199 73.995  -3.157  1.00 12.81 ? 724  SER A CB  1 
ATOM   5744 O  OG  . SER A 1 724  ? 20.143 73.417  -3.919  1.00 13.22 ? 724  SER A OG  1 
ATOM   5745 N  N   . GLY A 1 725  ? 23.216 73.607  -0.695  1.00 13.96 ? 725  GLY A N   1 
ATOM   5746 C  CA  . GLY A 1 725  ? 24.373 74.156  -0.015  1.00 12.99 ? 725  GLY A CA  1 
ATOM   5747 C  C   . GLY A 1 725  ? 25.585 73.447  -0.652  1.00 9.42  ? 725  GLY A C   1 
ATOM   5748 O  O   . GLY A 1 725  ? 25.482 72.842  -1.762  1.00 11.32 ? 725  GLY A O   1 
ATOM   5749 N  N   . ALA A 1 726  ? 26.719 73.473  0.062   1.00 11.43 ? 726  ALA A N   1 
ATOM   5750 C  CA  . ALA A 1 726  ? 27.943 72.866  -0.442  1.00 9.44  ? 726  ALA A CA  1 
ATOM   5751 C  C   . ALA A 1 726  ? 27.837 71.343  -0.702  1.00 10.07 ? 726  ALA A C   1 
ATOM   5752 O  O   . ALA A 1 726  ? 28.514 70.817  -1.609  1.00 9.53  ? 726  ALA A O   1 
ATOM   5753 C  CB  . ALA A 1 726  ? 29.122 73.156  0.559   1.00 10.11 ? 726  ALA A CB  1 
ATOM   5754 N  N   . TYR A 1 727  ? 26.972 70.690  0.068   1.00 8.91  ? 727  TYR A N   1 
ATOM   5755 C  CA  . TYR A 1 727  ? 26.783 69.247  -0.085  1.00 9.44  ? 727  TYR A CA  1 
ATOM   5756 C  C   . TYR A 1 727  ? 25.610 68.910  -0.982  1.00 7.24  ? 727  TYR A C   1 
ATOM   5757 O  O   . TYR A 1 727  ? 25.712 68.103  -1.898  1.00 8.91  ? 727  TYR A O   1 
ATOM   5758 C  CB  . TYR A 1 727  ? 26.497 68.580  1.273   1.00 9.58  ? 727  TYR A CB  1 
ATOM   5759 C  CG  . TYR A 1 727  ? 27.505 68.859  2.387   1.00 8.64  ? 727  TYR A CG  1 
ATOM   5760 C  CD1 . TYR A 1 727  ? 27.396 70.005  3.214   1.00 8.88  ? 727  TYR A CD1 1 
ATOM   5761 C  CD2 . TYR A 1 727  ? 28.583 67.958  2.594   1.00 7.91  ? 727  TYR A CD2 1 
ATOM   5762 C  CE1 . TYR A 1 727  ? 28.348 70.258  4.263   1.00 8.51  ? 727  TYR A CE1 1 
ATOM   5763 C  CE2 . TYR A 1 727  ? 29.532 68.207  3.615   1.00 8.60  ? 727  TYR A CE2 1 
ATOM   5764 C  CZ  . TYR A 1 727  ? 29.403 69.353  4.437   1.00 8.39  ? 727  TYR A CZ  1 
ATOM   5765 O  OH  . TYR A 1 727  ? 30.279 69.520  5.462   1.00 9.37  ? 727  TYR A OH  1 
ATOM   5766 N  N   . LEU A 1 728  ? 24.470 69.527  -0.665  1.00 10.77 ? 728  LEU A N   1 
ATOM   5767 C  CA  . LEU A 1 728  ? 23.203 69.183  -1.311  1.00 10.20 ? 728  LEU A CA  1 
ATOM   5768 C  C   . LEU A 1 728  ? 22.818 69.939  -2.563  1.00 10.04 ? 728  LEU A C   1 
ATOM   5769 O  O   . LEU A 1 728  ? 22.991 71.186  -2.577  1.00 10.48 ? 728  LEU A O   1 
ATOM   5770 C  CB  . LEU A 1 728  ? 22.046 69.359  -0.306  1.00 12.03 ? 728  LEU A CB  1 
ATOM   5771 C  CG  . LEU A 1 728  ? 22.147 68.731  1.098   1.00 10.59 ? 728  LEU A CG  1 
ATOM   5772 C  CD1 . LEU A 1 728  ? 20.758 68.897  1.899   1.00 9.91  ? 728  LEU A CD1 1 
ATOM   5773 C  CD2 . LEU A 1 728  ? 22.463 67.192  0.997   1.00 10.99 ? 728  LEU A CD2 1 
ATOM   5774 N  N   . PHE A 1 729  ? 22.277 69.244  -3.559  1.00 9.83  ? 729  PHE A N   1 
ATOM   5775 C  CA  . PHE A 1 729  ? 21.787 69.872  -4.792  1.00 11.02 ? 729  PHE A CA  1 
ATOM   5776 C  C   . PHE A 1 729  ? 20.234 69.676  -4.714  1.00 12.07 ? 729  PHE A C   1 
ATOM   5777 O  O   . PHE A 1 729  ? 19.734 68.544  -4.833  1.00 10.12 ? 729  PHE A O   1 
ATOM   5778 C  CB  . PHE A 1 729  ? 22.355 69.137  -6.027  1.00 10.83 ? 729  PHE A CB  1 
ATOM   5779 C  CG  . PHE A 1 729  ? 21.798 69.608  -7.371  1.00 10.70 ? 729  PHE A CG  1 
ATOM   5780 C  CD1 . PHE A 1 729  ? 21.431 70.954  -7.600  1.00 10.44 ? 729  PHE A CD1 1 
ATOM   5781 C  CD2 . PHE A 1 729  ? 21.698 68.725  -8.404  1.00 8.58  ? 729  PHE A CD2 1 
ATOM   5782 C  CE1 . PHE A 1 729  ? 20.972 71.349  -8.881  1.00 11.79 ? 729  PHE A CE1 1 
ATOM   5783 C  CE2 . PHE A 1 729  ? 21.257 69.101  -9.683  1.00 10.04 ? 729  PHE A CE2 1 
ATOM   5784 C  CZ  . PHE A 1 729  ? 20.894 70.459  -9.888  1.00 10.56 ? 729  PHE A CZ  1 
ATOM   5785 N  N   . LEU A 1 730  ? 19.477 70.773  -4.513  1.00 12.81 ? 730  LEU A N   1 
ATOM   5786 C  CA  . LEU A 1 730  ? 18.006 70.684  -4.369  1.00 13.80 ? 730  LEU A CA  1 
ATOM   5787 C  C   . LEU A 1 730  ? 17.431 71.752  -5.296  1.00 12.34 ? 730  LEU A C   1 
ATOM   5788 O  O   . LEU A 1 730  ? 16.985 72.836  -4.849  1.00 12.90 ? 730  LEU A O   1 
ATOM   5789 C  CB  . LEU A 1 730  ? 17.620 70.941  -2.921  1.00 13.04 ? 730  LEU A CB  1 
ATOM   5790 C  CG  . LEU A 1 730  ? 18.061 69.916  -1.859  1.00 12.72 ? 730  LEU A CG  1 
ATOM   5791 C  CD1 . LEU A 1 730  ? 18.145 70.507  -0.450  1.00 13.55 ? 730  LEU A CD1 1 
ATOM   5792 C  CD2 . LEU A 1 730  ? 17.052 68.790  -1.845  1.00 12.42 ? 730  LEU A CD2 1 
ATOM   5793 N  N   . PRO A 1 731  ? 17.468 71.453  -6.585  1.00 13.59 ? 731  PRO A N   1 
ATOM   5794 C  CA  . PRO A 1 731  ? 16.961 72.414  -7.579  1.00 14.01 ? 731  PRO A CA  1 
ATOM   5795 C  C   . PRO A 1 731  ? 15.477 72.688  -7.471  1.00 15.47 ? 731  PRO A C   1 
ATOM   5796 O  O   . PRO A 1 731  ? 14.690 71.840  -7.007  1.00 14.53 ? 731  PRO A O   1 
ATOM   5797 C  CB  . PRO A 1 731  ? 17.287 71.765  -8.906  1.00 14.42 ? 731  PRO A CB  1 
ATOM   5798 C  CG  . PRO A 1 731  ? 17.217 70.244  -8.592  1.00 13.37 ? 731  PRO A CG  1 
ATOM   5799 C  CD  . PRO A 1 731  ? 17.826 70.159  -7.198  1.00 13.98 ? 731  PRO A CD  1 
ATOM   5800 N  N   . ASN A 1 732  ? 15.104 73.888  -7.916  1.00 16.34 ? 732  ASN A N   1 
ATOM   5801 C  CA  . ASN A 1 732  ? 13.699 74.262  -7.993  1.00 18.51 ? 732  ASN A CA  1 
ATOM   5802 C  C   . ASN A 1 732  ? 13.208 73.996  -9.390  1.00 17.45 ? 732  ASN A C   1 
ATOM   5803 O  O   . ASN A 1 732  ? 12.775 74.921  -10.101 1.00 20.01 ? 732  ASN A O   1 
ATOM   5804 C  CB  . ASN A 1 732  ? 13.521 75.731  -7.634  1.00 20.70 ? 732  ASN A CB  1 
ATOM   5805 C  CG  . ASN A 1 732  ? 14.191 76.670  -8.606  1.00 23.89 ? 732  ASN A CG  1 
ATOM   5806 O  OD1 . ASN A 1 732  ? 15.200 76.357  -9.256  1.00 23.42 ? 732  ASN A OD1 1 
ATOM   5807 N  ND2 . ASN A 1 732  ? 13.625 77.869  -8.706  1.00 27.31 ? 732  ASN A ND2 1 
ATOM   5808 N  N   . GLY A 1 733  ? 13.272 72.741  -9.806  1.00 16.42 ? 733  GLY A N   1 
ATOM   5809 C  CA  . GLY A 1 733  ? 12.814 72.342  -11.124 1.00 16.61 ? 733  GLY A CA  1 
ATOM   5810 C  C   . GLY A 1 733  ? 13.924 72.211  -12.144 1.00 16.30 ? 733  GLY A C   1 
ATOM   5811 O  O   . GLY A 1 733  ? 15.114 72.492  -11.851 1.00 17.66 ? 733  GLY A O   1 
ATOM   5812 N  N   . PRO A 1 734  ? 13.589 71.758  -13.344 1.00 16.48 ? 734  PRO A N   1 
ATOM   5813 C  CA  . PRO A 1 734  ? 14.531 71.587  -14.439 1.00 15.53 ? 734  PRO A CA  1 
ATOM   5814 C  C   . PRO A 1 734  ? 15.171 72.944  -14.716 1.00 14.91 ? 734  PRO A C   1 
ATOM   5815 O  O   . PRO A 1 734  ? 14.589 74.000  -14.474 1.00 15.96 ? 734  PRO A O   1 
ATOM   5816 C  CB  . PRO A 1 734  ? 13.657 71.143  -15.601 1.00 17.17 ? 734  PRO A CB  1 
ATOM   5817 C  CG  . PRO A 1 734  ? 12.546 70.399  -14.913 1.00 19.80 ? 734  PRO A CG  1 
ATOM   5818 C  CD  . PRO A 1 734  ? 12.243 71.311  -13.748 1.00 16.58 ? 734  PRO A CD  1 
ATOM   5819 N  N   . ALA A 1 735  ? 16.376 72.918  -15.232 1.00 12.41 ? 735  ALA A N   1 
ATOM   5820 C  CA  . ALA A 1 735  ? 17.093 74.171  -15.519 1.00 14.43 ? 735  ALA A CA  1 
ATOM   5821 C  C   . ALA A 1 735  ? 16.399 75.043  -16.591 1.00 15.58 ? 735  ALA A C   1 
ATOM   5822 O  O   . ALA A 1 735  ? 15.687 74.551  -17.430 1.00 16.12 ? 735  ALA A O   1 
ATOM   5823 C  CB  . ALA A 1 735  ? 18.529 73.824  -15.916 1.00 12.98 ? 735  ALA A CB  1 
ATOM   5824 N  N   . SER A 1 736  ? 16.647 76.346  -16.524 1.00 17.25 ? 736  SER A N   1 
ATOM   5825 C  CA  . SER A 1 736  ? 16.062 77.293  -17.494 1.00 18.99 ? 736  SER A CA  1 
ATOM   5826 C  C   . SER A 1 736  ? 17.199 77.799  -18.387 1.00 19.96 ? 736  SER A C   1 
ATOM   5827 O  O   . SER A 1 736  ? 18.312 77.965  -17.911 1.00 19.66 ? 736  SER A O   1 
ATOM   5828 C  CB  . SER A 1 736  ? 15.473 78.466  -16.724 1.00 19.36 ? 736  SER A CB  1 
ATOM   5829 O  OG  . SER A 1 736  ? 14.628 78.006  -15.664 1.00 24.71 ? 736  SER A OG  1 
ATOM   5830 N  N   . PRO A 1 737  ? 16.932 78.079  -19.673 1.00 21.81 ? 737  PRO A N   1 
ATOM   5831 C  CA  . PRO A 1 737  ? 17.973 78.570  -20.600 1.00 22.76 ? 737  PRO A CA  1 
ATOM   5832 C  C   . PRO A 1 737  ? 18.606 79.882  -20.163 1.00 22.81 ? 737  PRO A C   1 
ATOM   5833 O  O   . PRO A 1 737  ? 17.914 80.769  -19.677 1.00 24.03 ? 737  PRO A O   1 
ATOM   5834 C  CB  . PRO A 1 737  ? 17.226 78.744  -21.928 1.00 24.17 ? 737  PRO A CB  1 
ATOM   5835 C  CG  . PRO A 1 737  ? 16.142 77.711  -21.858 1.00 23.57 ? 737  PRO A CG  1 
ATOM   5836 C  CD  . PRO A 1 737  ? 15.664 77.832  -20.390 1.00 23.65 ? 737  PRO A CD  1 
ATOM   5837 N  N   . VAL A 1 738  ? 19.934 79.976  -20.249 1.00 23.66 ? 738  VAL A N   1 
ATOM   5838 C  CA  . VAL A 1 738  ? 20.622 81.237  -19.936 1.00 24.46 ? 738  VAL A CA  1 
ATOM   5839 C  C   . VAL A 1 738  ? 20.254 82.199  -21.096 1.00 24.88 ? 738  VAL A C   1 
ATOM   5840 O  O   . VAL A 1 738  ? 20.355 81.833  -22.270 1.00 24.78 ? 738  VAL A O   1 
ATOM   5841 C  CB  . VAL A 1 738  ? 22.171 81.054  -19.910 1.00 24.02 ? 738  VAL A CB  1 
ATOM   5842 C  CG1 . VAL A 1 738  ? 22.873 82.440  -19.952 1.00 23.62 ? 738  VAL A CG1 1 
ATOM   5843 C  CG2 . VAL A 1 738  ? 22.606 80.273  -18.611 1.00 23.26 ? 738  VAL A CG2 1 
ATOM   5844 N  N   . GLU A 1 739  ? 19.758 83.391  -20.792 1.00 25.83 ? 739  GLU A N   1 
ATOM   5845 C  CA  . GLU A 1 739  ? 19.426 84.330  -21.864 1.00 27.47 ? 739  GLU A CA  1 
ATOM   5846 C  C   . GLU A 1 739  ? 20.762 84.855  -22.402 1.00 26.35 ? 739  GLU A C   1 
ATOM   5847 O  O   . GLU A 1 739  ? 21.502 85.519  -21.684 1.00 23.90 ? 739  GLU A O   1 
ATOM   5848 C  CB  . GLU A 1 739  ? 18.547 85.459  -21.326 1.00 30.53 ? 739  GLU A CB  1 
ATOM   5849 C  CG  . GLU A 1 739  ? 18.640 86.782  -22.109 1.00 35.11 ? 739  GLU A CG  1 
ATOM   5850 C  CD  . GLU A 1 739  ? 17.387 87.657  -22.007 1.00 37.58 ? 739  GLU A CD  1 
ATOM   5851 O  OE1 . GLU A 1 739  ? 16.255 87.103  -21.856 1.00 38.04 ? 739  GLU A OE1 1 
ATOM   5852 O  OE2 . GLU A 1 739  ? 17.540 88.902  -22.106 1.00 38.57 ? 739  GLU A OE2 1 
ATOM   5853 N  N   . LEU A 1 740  ? 21.034 84.551  -23.673 1.00 26.43 ? 740  LEU A N   1 
ATOM   5854 C  CA  . LEU A 1 740  ? 22.308 84.898  -24.331 1.00 27.00 ? 740  LEU A CA  1 
ATOM   5855 C  C   . LEU A 1 740  ? 22.478 86.250  -25.010 1.00 27.59 ? 740  LEU A C   1 
ATOM   5856 O  O   . LEU A 1 740  ? 23.605 86.617  -25.329 1.00 27.20 ? 740  LEU A O   1 
ATOM   5857 C  CB  . LEU A 1 740  ? 22.672 83.817  -25.354 1.00 26.26 ? 740  LEU A CB  1 
ATOM   5858 C  CG  . LEU A 1 740  ? 22.653 82.377  -24.821 1.00 25.75 ? 740  LEU A CG  1 
ATOM   5859 C  CD1 . LEU A 1 740  ? 23.220 81.447  -25.885 1.00 26.51 ? 740  LEU A CD1 1 
ATOM   5860 C  CD2 . LEU A 1 740  ? 23.489 82.271  -23.547 1.00 25.88 ? 740  LEU A CD2 1 
ATOM   5861 N  N   . GLY A 1 741  ? 21.382 86.971  -25.245 1.00 26.93 ? 741  GLY A N   1 
ATOM   5862 C  CA  . GLY A 1 741  ? 21.474 88.266  -25.905 1.00 27.32 ? 741  GLY A CA  1 
ATOM   5863 C  C   . GLY A 1 741  ? 22.038 88.047  -27.301 1.00 26.93 ? 741  GLY A C   1 
ATOM   5864 O  O   . GLY A 1 741  ? 21.699 87.054  -27.940 1.00 26.59 ? 741  GLY A O   1 
ATOM   5865 N  N   . GLN A 1 742  ? 22.869 88.969  -27.784 1.00 27.60 ? 742  GLN A N   1 
ATOM   5866 C  CA  . GLN A 1 742  ? 23.503 88.823  -29.108 1.00 28.36 ? 742  GLN A CA  1 
ATOM   5867 C  C   . GLN A 1 742  ? 24.992 88.759  -28.764 1.00 25.80 ? 742  GLN A C   1 
ATOM   5868 O  O   . GLN A 1 742  ? 25.677 89.762  -28.695 1.00 26.71 ? 742  GLN A O   1 
ATOM   5869 C  CB  . GLN A 1 742  ? 23.211 90.029  -29.999 1.00 30.84 ? 742  GLN A CB  1 
ATOM   5870 C  CG  . GLN A 1 742  ? 23.441 89.722  -31.473 1.00 36.35 ? 742  GLN A CG  1 
ATOM   5871 C  CD  . GLN A 1 742  ? 22.521 90.517  -32.422 1.00 40.00 ? 742  GLN A CD  1 
ATOM   5872 O  OE1 . GLN A 1 742  ? 22.626 90.378  -33.655 1.00 41.89 ? 742  GLN A OE1 1 
ATOM   5873 N  NE2 . GLN A 1 742  ? 21.613 91.344  -31.854 1.00 40.02 ? 742  GLN A NE2 1 
ATOM   5874 N  N   . PRO A 1 743  ? 25.499 87.558  -28.497 1.00 23.83 ? 743  PRO A N   1 
ATOM   5875 C  CA  . PRO A 1 743  ? 26.920 87.471  -28.137 1.00 22.28 ? 743  PRO A CA  1 
ATOM   5876 C  C   . PRO A 1 743  ? 27.984 87.754  -29.176 1.00 20.27 ? 743  PRO A C   1 
ATOM   5877 O  O   . PRO A 1 743  ? 27.776 87.561  -30.345 1.00 21.29 ? 743  PRO A O   1 
ATOM   5878 C  CB  . PRO A 1 743  ? 27.044 86.047  -27.591 1.00 20.64 ? 743  PRO A CB  1 
ATOM   5879 C  CG  . PRO A 1 743  ? 26.032 85.284  -28.405 1.00 23.05 ? 743  PRO A CG  1 
ATOM   5880 C  CD  . PRO A 1 743  ? 24.843 86.231  -28.463 1.00 23.49 ? 743  PRO A CD  1 
ATOM   5881 N  N   . VAL A 1 744  ? 29.146 88.194  -28.712 1.00 18.60 ? 744  VAL A N   1 
ATOM   5882 C  CA  . VAL A 1 744  ? 30.269 88.437  -29.581 1.00 15.35 ? 744  VAL A CA  1 
ATOM   5883 C  C   . VAL A 1 744  ? 30.995 87.094  -29.841 1.00 14.49 ? 744  VAL A C   1 
ATOM   5884 O  O   . VAL A 1 744  ? 31.319 86.352  -28.890 1.00 15.22 ? 744  VAL A O   1 
ATOM   5885 C  CB  . VAL A 1 744  ? 31.201 89.431  -28.960 1.00 15.78 ? 744  VAL A CB  1 
ATOM   5886 C  CG1 . VAL A 1 744  ? 32.474 89.532  -29.781 1.00 15.57 ? 744  VAL A CG1 1 
ATOM   5887 C  CG2 . VAL A 1 744  ? 30.475 90.787  -28.857 1.00 14.66 ? 744  VAL A CG2 1 
ATOM   5888 N  N   . VAL A 1 745  ? 31.209 86.768  -31.110 1.00 12.62 ? 745  VAL A N   1 
ATOM   5889 C  CA  . VAL A 1 745  ? 31.832 85.503  -31.513 1.00 12.35 ? 745  VAL A CA  1 
ATOM   5890 C  C   . VAL A 1 745  ? 33.122 85.750  -32.253 1.00 13.78 ? 745  VAL A C   1 
ATOM   5891 O  O   . VAL A 1 745  ? 33.170 86.590  -33.145 1.00 14.43 ? 745  VAL A O   1 
ATOM   5892 C  CB  . VAL A 1 745  ? 30.862 84.634  -32.479 1.00 11.38 ? 745  VAL A CB  1 
ATOM   5893 C  CG1 . VAL A 1 745  ? 31.524 83.320  -32.887 1.00 12.80 ? 745  VAL A CG1 1 
ATOM   5894 C  CG2 . VAL A 1 745  ? 29.505 84.424  -31.835 1.00 10.29 ? 745  VAL A CG2 1 
ATOM   5895 N  N   . LEU A 1 746  ? 34.199 85.073  -31.854 1.00 12.99 ? 746  LEU A N   1 
ATOM   5896 C  CA  . LEU A 1 746  ? 35.499 85.195  -32.480 1.00 12.04 ? 746  LEU A CA  1 
ATOM   5897 C  C   . LEU A 1 746  ? 35.928 83.871  -33.134 1.00 14.27 ? 746  LEU A C   1 
ATOM   5898 O  O   . LEU A 1 746  ? 36.022 82.823  -32.450 1.00 14.19 ? 746  LEU A O   1 
ATOM   5899 C  CB  . LEU A 1 746  ? 36.501 85.654  -31.389 1.00 13.69 ? 746  LEU A CB  1 
ATOM   5900 C  CG  . LEU A 1 746  ? 37.975 85.693  -31.828 1.00 14.60 ? 746  LEU A CG  1 
ATOM   5901 C  CD1 . LEU A 1 746  ? 38.230 86.695  -32.992 1.00 19.48 ? 746  LEU A CD1 1 
ATOM   5902 C  CD2 . LEU A 1 746  ? 38.811 86.163  -30.623 1.00 18.79 ? 746  LEU A CD2 1 
ATOM   5903 N  N   . VAL A 1 747  ? 36.208 83.899  -34.442 1.00 13.15 ? 747  VAL A N   1 
ATOM   5904 C  CA  . VAL A 1 747  ? 36.612 82.732  -35.200 1.00 13.27 ? 747  VAL A CA  1 
ATOM   5905 C  C   . VAL A 1 747  ? 38.037 82.918  -35.629 1.00 13.85 ? 747  VAL A C   1 
ATOM   5906 O  O   . VAL A 1 747  ? 38.389 83.953  -36.241 1.00 15.37 ? 747  VAL A O   1 
ATOM   5907 C  CB  . VAL A 1 747  ? 35.732 82.520  -36.484 1.00 12.19 ? 747  VAL A CB  1 
ATOM   5908 C  CG1 . VAL A 1 747  ? 36.086 81.237  -37.108 1.00 15.51 ? 747  VAL A CG1 1 
ATOM   5909 C  CG2 . VAL A 1 747  ? 34.239 82.576  -36.083 1.00 14.05 ? 747  VAL A CG2 1 
ATOM   5910 N  N   . THR A 1 748  ? 38.900 81.972  -35.301 1.00 13.49 ? 748  THR A N   1 
ATOM   5911 C  CA  . THR A 1 748  ? 40.316 82.065  -35.651 1.00 13.85 ? 748  THR A CA  1 
ATOM   5912 C  C   . THR A 1 748  ? 40.539 80.834  -36.462 1.00 14.00 ? 748  THR A C   1 
ATOM   5913 O  O   . THR A 1 748  ? 40.281 79.731  -35.984 1.00 16.22 ? 748  THR A O   1 
ATOM   5914 C  CB  . THR A 1 748  ? 41.187 82.042  -34.375 1.00 14.41 ? 748  THR A CB  1 
ATOM   5915 O  OG1 . THR A 1 748  ? 40.978 83.257  -33.688 1.00 13.84 ? 748  THR A OG1 1 
ATOM   5916 C  CG2 . THR A 1 748  ? 42.681 81.957  -34.704 1.00 17.89 ? 748  THR A CG2 1 
ATOM   5917 N  N   . LYS A 1 749  ? 40.974 80.985  -37.716 1.00 14.96 ? 749  LYS A N   1 
ATOM   5918 C  CA  . LYS A 1 749  ? 41.172 79.850  -38.600 1.00 16.03 ? 749  LYS A CA  1 
ATOM   5919 C  C   . LYS A 1 749  ? 42.608 79.726  -38.993 1.00 16.86 ? 749  LYS A C   1 
ATOM   5920 O  O   . LYS A 1 749  ? 43.211 80.643  -39.580 1.00 15.75 ? 749  LYS A O   1 
ATOM   5921 C  CB  . LYS A 1 749  ? 40.292 79.988  -39.862 1.00 15.96 ? 749  LYS A CB  1 
ATOM   5922 C  CG  . LYS A 1 749  ? 40.479 78.888  -40.869 1.00 21.89 ? 749  LYS A CG  1 
ATOM   5923 C  CD  . LYS A 1 749  ? 39.367 78.985  -41.922 1.00 24.45 ? 749  LYS A CD  1 
ATOM   5924 C  CE  . LYS A 1 749  ? 39.648 78.051  -43.045 1.00 26.17 ? 749  LYS A CE  1 
ATOM   5925 N  NZ  . LYS A 1 749  ? 41.012 78.416  -43.560 1.00 27.95 ? 749  LYS A NZ  1 
ATOM   5926 N  N   . GLY A 1 750  ? 43.160 78.565  -38.655 1.00 15.66 ? 750  GLY A N   1 
ATOM   5927 C  CA  . GLY A 1 750  ? 44.542 78.287  -38.952 1.00 15.91 ? 750  GLY A CA  1 
ATOM   5928 C  C   . GLY A 1 750  ? 44.748 76.941  -39.582 1.00 16.18 ? 750  GLY A C   1 
ATOM   5929 O  O   . GLY A 1 750  ? 43.879 76.053  -39.584 1.00 15.95 ? 750  GLY A O   1 
ATOM   5930 N  N   . LYS A 1 751  ? 45.954 76.764  -40.082 1.00 14.27 ? 751  LYS A N   1 
ATOM   5931 C  CA  . LYS A 1 751  ? 46.294 75.531  -40.681 1.00 16.65 ? 751  LYS A CA  1 
ATOM   5932 C  C   . LYS A 1 751  ? 46.372 74.383  -39.650 1.00 15.50 ? 751  LYS A C   1 
ATOM   5933 O  O   . LYS A 1 751  ? 45.970 73.256  -39.913 1.00 16.82 ? 751  LYS A O   1 
ATOM   5934 C  CB  . LYS A 1 751  ? 47.646 75.681  -41.356 1.00 18.45 ? 751  LYS A CB  1 
ATOM   5935 C  CG  . LYS A 1 751  ? 48.021 74.471  -42.180 1.00 23.82 ? 751  LYS A CG  1 
ATOM   5936 C  CD  . LYS A 1 751  ? 49.140 74.849  -43.133 1.00 28.13 ? 751  LYS A CD  1 
ATOM   5937 C  CE  . LYS A 1 751  ? 49.507 73.686  -44.051 1.00 29.22 ? 751  LYS A CE  1 
ATOM   5938 N  NZ  . LYS A 1 751  ? 49.756 72.434  -43.257 1.00 30.94 ? 751  LYS A NZ  1 
ATOM   5939 N  N   . LEU A 1 752  ? 46.929 74.708  -38.492 1.00 16.42 ? 752  LEU A N   1 
ATOM   5940 C  CA  . LEU A 1 752  ? 47.173 73.715  -37.417 1.00 16.11 ? 752  LEU A CA  1 
ATOM   5941 C  C   . LEU A 1 752  ? 46.119 73.710  -36.346 1.00 15.70 ? 752  LEU A C   1 
ATOM   5942 O  O   . LEU A 1 752  ? 45.799 72.667  -35.803 1.00 14.75 ? 752  LEU A O   1 
ATOM   5943 C  CB  . LEU A 1 752  ? 48.506 73.990  -36.723 1.00 16.87 ? 752  LEU A CB  1 
ATOM   5944 C  CG  . LEU A 1 752  ? 49.764 74.014  -37.609 1.00 18.97 ? 752  LEU A CG  1 
ATOM   5945 C  CD1 . LEU A 1 752  ? 51.051 74.202  -36.776 1.00 20.28 ? 752  LEU A CD1 1 
ATOM   5946 C  CD2 . LEU A 1 752  ? 49.805 72.716  -38.350 1.00 18.34 ? 752  LEU A CD2 1 
ATOM   5947 N  N   . GLU A 1 753  ? 45.502 74.853  -36.111 1.00 14.37 ? 753  GLU A N   1 
ATOM   5948 C  CA  . GLU A 1 753  ? 44.511 74.985  -35.056 1.00 15.34 ? 753  GLU A CA  1 
ATOM   5949 C  C   . GLU A 1 753  ? 43.522 76.092  -35.394 1.00 14.30 ? 753  GLU A C   1 
ATOM   5950 O  O   . GLU A 1 753  ? 43.931 77.186  -35.803 1.00 15.78 ? 753  GLU A O   1 
ATOM   5951 C  CB  . GLU A 1 753  ? 45.221 75.374  -33.730 1.00 14.79 ? 753  GLU A CB  1 
ATOM   5952 C  CG  . GLU A 1 753  ? 44.224 75.564  -32.527 1.00 20.13 ? 753  GLU A CG  1 
ATOM   5953 C  CD  . GLU A 1 753  ? 44.864 75.922  -31.166 1.00 23.23 ? 753  GLU A CD  1 
ATOM   5954 O  OE1 . GLU A 1 753  ? 45.268 77.069  -30.973 1.00 25.05 ? 753  GLU A OE1 1 
ATOM   5955 O  OE2 . GLU A 1 753  ? 44.944 75.042  -30.282 1.00 26.80 ? 753  GLU A OE2 1 
ATOM   5956 N  N   . SER A 1 754  ? 42.235 75.844  -35.166 1.00 13.60 ? 754  SER A N   1 
ATOM   5957 C  CA  . SER A 1 754  ? 41.233 76.887  -35.367 1.00 13.55 ? 754  SER A CA  1 
ATOM   5958 C  C   . SER A 1 754  ? 40.339 76.880  -34.152 1.00 14.37 ? 754  SER A C   1 
ATOM   5959 O  O   . SER A 1 754  ? 40.337 75.898  -33.392 1.00 13.27 ? 754  SER A O   1 
ATOM   5960 C  CB  . SER A 1 754  ? 40.368 76.604  -36.602 1.00 13.10 ? 754  SER A CB  1 
ATOM   5961 O  OG  . SER A 1 754  ? 41.157 76.583  -37.778 1.00 13.21 ? 754  SER A OG  1 
ATOM   5962 N  N   . SER A 1 755  ? 39.510 77.895  -34.003 1.00 12.63 ? 755  SER A N   1 
ATOM   5963 C  CA  . SER A 1 755  ? 38.619 77.914  -32.843 1.00 13.64 ? 755  SER A CA  1 
ATOM   5964 C  C   . SER A 1 755  ? 37.529 78.944  -32.985 1.00 14.35 ? 755  SER A C   1 
ATOM   5965 O  O   . SER A 1 755  ? 37.639 79.888  -33.782 1.00 15.14 ? 755  SER A O   1 
ATOM   5966 C  CB  . SER A 1 755  ? 39.388 78.252  -31.562 1.00 16.54 ? 755  SER A CB  1 
ATOM   5967 O  OG  . SER A 1 755  ? 39.848 79.579  -31.649 1.00 17.27 ? 755  SER A OG  1 
ATOM   5968 N  N   . VAL A 1 756  ? 36.457 78.707  -32.276 1.00 11.74 ? 756  VAL A N   1 
ATOM   5969 C  CA  . VAL A 1 756  ? 35.332 79.622  -32.230 1.00 11.89 ? 756  VAL A CA  1 
ATOM   5970 C  C   . VAL A 1 756  ? 35.172 79.875  -30.717 1.00 13.15 ? 756  VAL A C   1 
ATOM   5971 O  O   . VAL A 1 756  ? 35.029 78.936  -29.909 1.00 13.42 ? 756  VAL A O   1 
ATOM   5972 C  CB  . VAL A 1 756  ? 34.019 78.972  -32.769 1.00 11.85 ? 756  VAL A CB  1 
ATOM   5973 C  CG1 . VAL A 1 756  ? 32.832 79.913  -32.468 1.00 10.49 ? 756  VAL A CG1 1 
ATOM   5974 C  CG2 . VAL A 1 756  ? 34.136 78.582  -34.245 1.00 14.15 ? 756  VAL A CG2 1 
ATOM   5975 N  N   . SER A 1 757  ? 35.170 81.131  -30.330 1.00 11.63 ? 757  SER A N   1 
ATOM   5976 C  CA  . SER A 1 757  ? 35.026 81.537  -28.959 1.00 12.32 ? 757  SER A CA  1 
ATOM   5977 C  C   . SER A 1 757  ? 33.890 82.487  -28.812 1.00 13.48 ? 757  SER A C   1 
ATOM   5978 O  O   . SER A 1 757  ? 33.754 83.397  -29.619 1.00 13.57 ? 757  SER A O   1 
ATOM   5979 C  CB  . SER A 1 757  ? 36.318 82.228  -28.452 1.00 13.19 ? 757  SER A CB  1 
ATOM   5980 O  OG  . SER A 1 757  ? 37.414 81.289  -28.610 1.00 15.57 ? 757  SER A OG  1 
ATOM   5981 N  N   . VAL A 1 758  ? 33.076 82.340  -27.792 1.00 13.25 ? 758  VAL A N   1 
ATOM   5982 C  CA  . VAL A 1 758  ? 31.940 83.265  -27.636 1.00 12.45 ? 758  VAL A CA  1 
ATOM   5983 C  C   . VAL A 1 758  ? 31.843 83.766  -26.221 1.00 13.91 ? 758  VAL A C   1 
ATOM   5984 O  O   . VAL A 1 758  ? 32.014 83.000  -25.245 1.00 14.40 ? 758  VAL A O   1 
ATOM   5985 C  CB  . VAL A 1 758  ? 30.578 82.635  -28.021 1.00 14.16 ? 758  VAL A CB  1 
ATOM   5986 C  CG1 . VAL A 1 758  ? 30.314 81.320  -27.223 1.00 15.48 ? 758  VAL A CG1 1 
ATOM   5987 C  CG2 . VAL A 1 758  ? 29.449 83.657  -27.743 1.00 14.96 ? 758  VAL A CG2 1 
ATOM   5988 N  N   . GLY A 1 759  ? 31.560 85.049  -26.076 1.00 14.58 ? 759  GLY A N   1 
ATOM   5989 C  CA  . GLY A 1 759  ? 31.416 85.648  -24.760 1.00 12.46 ? 759  GLY A CA  1 
ATOM   5990 C  C   . GLY A 1 759  ? 29.971 85.573  -24.312 1.00 13.98 ? 759  GLY A C   1 
ATOM   5991 O  O   . GLY A 1 759  ? 29.123 86.304  -24.776 1.00 12.90 ? 759  GLY A O   1 
ATOM   5992 N  N   . LEU A 1 760  ? 29.662 84.639  -23.424 1.00 13.58 ? 760  LEU A N   1 
ATOM   5993 C  CA  . LEU A 1 760  ? 28.294 84.433  -22.910 1.00 13.97 ? 760  LEU A CA  1 
ATOM   5994 C  C   . LEU A 1 760  ? 28.237 84.958  -21.500 1.00 13.92 ? 760  LEU A C   1 
ATOM   5995 O  O   . LEU A 1 760  ? 29.280 85.194  -20.873 1.00 16.65 ? 760  LEU A O   1 
ATOM   5996 C  CB  . LEU A 1 760  ? 27.938 82.922  -22.872 1.00 14.06 ? 760  LEU A CB  1 
ATOM   5997 C  CG  . LEU A 1 760  ? 28.050 82.110  -24.189 1.00 12.67 ? 760  LEU A CG  1 
ATOM   5998 C  CD1 . LEU A 1 760  ? 27.662 80.655  -24.010 1.00 17.35 ? 760  LEU A CD1 1 
ATOM   5999 C  CD2 . LEU A 1 760  ? 27.154 82.773  -25.282 1.00 16.30 ? 760  LEU A CD2 1 
ATOM   6000 N  N   . PRO A 1 761  ? 27.029 85.169  -20.955 1.00 15.09 ? 761  PRO A N   1 
ATOM   6001 C  CA  . PRO A 1 761  ? 26.982 85.667  -19.562 1.00 15.56 ? 761  PRO A CA  1 
ATOM   6002 C  C   . PRO A 1 761  ? 27.553 84.536  -18.644 1.00 17.49 ? 761  PRO A C   1 
ATOM   6003 O  O   . PRO A 1 761  ? 27.105 83.361  -18.726 1.00 18.78 ? 761  PRO A O   1 
ATOM   6004 C  CB  . PRO A 1 761  ? 25.493 85.894  -19.316 1.00 16.36 ? 761  PRO A CB  1 
ATOM   6005 C  CG  . PRO A 1 761  ? 24.905 86.062  -20.698 1.00 15.94 ? 761  PRO A CG  1 
ATOM   6006 C  CD  . PRO A 1 761  ? 25.693 85.148  -21.595 1.00 13.39 ? 761  PRO A CD  1 
ATOM   6007 N  N   . SER A 1 762  ? 28.551 84.880  -17.841 1.00 15.52 ? 762  SER A N   1 
ATOM   6008 C  CA  . SER A 1 762  ? 29.241 83.909  -16.937 1.00 15.60 ? 762  SER A CA  1 
ATOM   6009 C  C   . SER A 1 762  ? 30.185 82.922  -17.559 1.00 13.31 ? 762  SER A C   1 
ATOM   6010 O  O   . SER A 1 762  ? 30.827 82.157  -16.834 1.00 14.43 ? 762  SER A O   1 
ATOM   6011 C  CB  . SER A 1 762  ? 28.251 83.073  -16.148 1.00 14.18 ? 762  SER A CB  1 
ATOM   6012 O  OG  . SER A 1 762  ? 27.458 83.878  -15.333 1.00 17.83 ? 762  SER A OG  1 
ATOM   6013 N  N   . VAL A 1 763  ? 30.302 82.884  -18.883 1.00 12.43 ? 763  VAL A N   1 
ATOM   6014 C  CA  . VAL A 1 763  ? 31.188 81.907  -19.517 1.00 12.27 ? 763  VAL A CA  1 
ATOM   6015 C  C   . VAL A 1 763  ? 31.746 82.305  -20.858 1.00 12.94 ? 763  VAL A C   1 
ATOM   6016 O  O   . VAL A 1 763  ? 30.960 82.582  -21.756 1.00 13.81 ? 763  VAL A O   1 
ATOM   6017 C  CB  . VAL A 1 763  ? 30.417 80.569  -19.779 1.00 13.27 ? 763  VAL A CB  1 
ATOM   6018 C  CG1 . VAL A 1 763  ? 31.347 79.473  -20.296 1.00 12.79 ? 763  VAL A CG1 1 
ATOM   6019 C  CG2 . VAL A 1 763  ? 29.735 80.105  -18.489 1.00 14.79 ? 763  VAL A CG2 1 
ATOM   6020 N  N   . VAL A 1 764  ? 33.066 82.291  -21.010 1.00 10.74 ? 764  VAL A N   1 
ATOM   6021 C  CA  . VAL A 1 764  ? 33.671 82.477  -22.328 1.00 11.53 ? 764  VAL A CA  1 
ATOM   6022 C  C   . VAL A 1 764  ? 33.841 81.021  -22.737 1.00 12.02 ? 764  VAL A C   1 
ATOM   6023 O  O   . VAL A 1 764  ? 34.678 80.248  -22.165 1.00 10.68 ? 764  VAL A O   1 
ATOM   6024 C  CB  . VAL A 1 764  ? 35.030 83.267  -22.313 1.00 11.52 ? 764  VAL A CB  1 
ATOM   6025 C  CG1 . VAL A 1 764  ? 35.617 83.279  -23.730 1.00 11.91 ? 764  VAL A CG1 1 
ATOM   6026 C  CG2 . VAL A 1 764  ? 34.827 84.673  -21.793 1.00 11.76 ? 764  VAL A CG2 1 
ATOM   6027 N  N   . HIS A 1 765  ? 33.034 80.590  -23.719 1.00 13.24 ? 765  HIS A N   1 
ATOM   6028 C  CA  . HIS A 1 765  ? 32.988 79.210  -24.230 1.00 12.14 ? 765  HIS A CA  1 
ATOM   6029 C  C   . HIS A 1 765  ? 33.818 79.107  -25.499 1.00 14.33 ? 765  HIS A C   1 
ATOM   6030 O  O   . HIS A 1 765  ? 33.560 79.868  -26.448 1.00 13.21 ? 765  HIS A O   1 
ATOM   6031 C  CB  . HIS A 1 765  ? 31.509 78.874  -24.520 1.00 12.90 ? 765  HIS A CB  1 
ATOM   6032 C  CG  . HIS A 1 765  ? 31.261 77.578  -25.207 1.00 12.92 ? 765  HIS A CG  1 
ATOM   6033 N  ND1 . HIS A 1 765  ? 31.419 76.353  -24.583 1.00 12.78 ? 765  HIS A ND1 1 
ATOM   6034 C  CD2 . HIS A 1 765  ? 30.761 77.316  -26.445 1.00 12.32 ? 765  HIS A CD2 1 
ATOM   6035 C  CE1 . HIS A 1 765  ? 31.022 75.396  -25.413 1.00 13.88 ? 765  HIS A CE1 1 
ATOM   6036 N  NE2 . HIS A 1 765  ? 30.616 75.954  -26.549 1.00 13.00 ? 765  HIS A NE2 1 
ATOM   6037 N  N   . GLN A 1 766  ? 34.731 78.148  -25.573 1.00 13.40 ? 766  GLN A N   1 
ATOM   6038 C  CA  . GLN A 1 766  ? 35.607 78.055  -26.719 1.00 13.53 ? 766  GLN A CA  1 
ATOM   6039 C  C   . GLN A 1 766  ? 35.655 76.632  -27.238 1.00 13.57 ? 766  GLN A C   1 
ATOM   6040 O  O   . GLN A 1 766  ? 35.744 75.664  -26.416 1.00 10.96 ? 766  GLN A O   1 
ATOM   6041 C  CB  . GLN A 1 766  ? 37.010 78.482  -26.294 1.00 16.00 ? 766  GLN A CB  1 
ATOM   6042 C  CG  . GLN A 1 766  ? 37.009 79.718  -25.428 1.00 21.13 ? 766  GLN A CG  1 
ATOM   6043 C  CD  . GLN A 1 766  ? 38.214 79.819  -24.475 1.00 24.68 ? 766  GLN A CD  1 
ATOM   6044 O  OE1 . GLN A 1 766  ? 39.356 79.448  -24.841 1.00 26.76 ? 766  GLN A OE1 1 
ATOM   6045 N  NE2 . GLN A 1 766  ? 37.960 80.339  -23.231 1.00 25.62 ? 766  GLN A NE2 1 
ATOM   6046 N  N   . THR A 1 767  ? 35.547 76.459  -28.565 1.00 12.39 ? 767  THR A N   1 
ATOM   6047 C  CA  . THR A 1 767  ? 35.651 75.162  -29.173 1.00 12.54 ? 767  THR A CA  1 
ATOM   6048 C  C   . THR A 1 767  ? 36.918 75.198  -30.045 1.00 13.48 ? 767  THR A C   1 
ATOM   6049 O  O   . THR A 1 767  ? 36.988 75.996  -30.996 1.00 14.01 ? 767  THR A O   1 
ATOM   6050 C  CB  . THR A 1 767  ? 34.431 74.835  -30.078 1.00 11.15 ? 767  THR A CB  1 
ATOM   6051 O  OG1 . THR A 1 767  ? 33.234 74.882  -29.302 1.00 13.94 ? 767  THR A OG1 1 
ATOM   6052 C  CG2 . THR A 1 767  ? 34.590 73.522  -30.714 1.00 12.22 ? 767  THR A CG2 1 
ATOM   6053 N  N   . ILE A 1 768  ? 37.911 74.359  -29.746 1.00 11.99 ? 768  ILE A N   1 
ATOM   6054 C  CA  . ILE A 1 768  ? 39.188 74.314  -30.483 1.00 12.96 ? 768  ILE A CA  1 
ATOM   6055 C  C   . ILE A 1 768  ? 39.312 73.082  -31.320 1.00 12.79 ? 768  ILE A C   1 
ATOM   6056 O  O   . ILE A 1 768  ? 38.936 71.987  -30.843 1.00 13.80 ? 768  ILE A O   1 
ATOM   6057 C  CB  . ILE A 1 768  ? 40.326 74.389  -29.502 1.00 11.92 ? 768  ILE A CB  1 
ATOM   6058 C  CG1 . ILE A 1 768  ? 40.057 75.566  -28.593 1.00 11.67 ? 768  ILE A CG1 1 
ATOM   6059 C  CG2 . ILE A 1 768  ? 41.628 74.640  -30.216 1.00 12.83 ? 768  ILE A CG2 1 
ATOM   6060 C  CD1 . ILE A 1 768  ? 40.983 75.671  -27.346 1.00 16.23 ? 768  ILE A CD1 1 
ATOM   6061 N  N   . MET A 1 769  ? 39.804 73.225  -32.559 1.00 12.97 ? 769  MET A N   1 
ATOM   6062 C  CA  . MET A 1 769  ? 39.953 72.135  -33.520 1.00 14.84 ? 769  MET A CA  1 
ATOM   6063 C  C   . MET A 1 769  ? 41.394 72.013  -33.962 1.00 14.77 ? 769  MET A C   1 
ATOM   6064 O  O   . MET A 1 769  ? 42.035 72.998  -34.375 1.00 14.75 ? 769  MET A O   1 
ATOM   6065 C  CB  . MET A 1 769  ? 39.066 72.386  -34.743 1.00 14.35 ? 769  MET A CB  1 
ATOM   6066 C  CG  . MET A 1 769  ? 37.594 72.302  -34.429 1.00 14.58 ? 769  MET A CG  1 
ATOM   6067 S  SD  A MET A 1 769  ? 36.600 73.424  -35.465 0.50 15.48 ? 769  MET A SD  1 
ATOM   6068 S  SD  B MET A 1 769  ? 36.617 72.839  -35.725 0.50 15.43 ? 769  MET A SD  1 
ATOM   6069 C  CE  A MET A 1 769  ? 36.486 74.838  -34.431 0.50 13.12 ? 769  MET A CE  1 
ATOM   6070 C  CE  B MET A 1 769  ? 36.919 71.422  -36.737 0.50 11.26 ? 769  MET A CE  1 
ATOM   6071 N  N   . ARG A 1 770  ? 41.923 70.801  -33.841 1.00 14.59 ? 770  ARG A N   1 
ATOM   6072 C  CA  . ARG A 1 770  ? 43.292 70.571  -34.233 1.00 15.18 ? 770  ARG A CA  1 
ATOM   6073 C  C   . ARG A 1 770  ? 43.421 69.382  -35.160 1.00 15.47 ? 770  ARG A C   1 
ATOM   6074 O  O   . ARG A 1 770  ? 44.519 68.899  -35.387 1.00 15.71 ? 770  ARG A O   1 
ATOM   6075 C  CB  . ARG A 1 770  ? 44.196 70.447  -32.979 1.00 17.26 ? 770  ARG A CB  1 
ATOM   6076 C  CG  . ARG A 1 770  ? 44.268 71.768  -32.159 1.00 19.71 ? 770  ARG A CG  1 
ATOM   6077 C  CD  . ARG A 1 770  ? 45.124 71.742  -30.865 1.00 22.76 ? 770  ARG A CD  1 
ATOM   6078 N  NE  . ARG A 1 770  ? 44.314 71.607  -29.655 1.00 27.48 ? 770  ARG A NE  1 
ATOM   6079 C  CZ  . ARG A 1 770  ? 44.389 70.548  -28.861 1.00 29.31 ? 770  ARG A CZ  1 
ATOM   6080 N  NH1 . ARG A 1 770  ? 45.239 69.579  -29.178 1.00 30.37 ? 770  ARG A NH1 1 
ATOM   6081 N  NH2 . ARG A 1 770  ? 43.627 70.441  -27.775 1.00 30.82 ? 770  ARG A NH2 1 
ATOM   6082 N  N   . GLY A 1 771  ? 42.293 68.943  -35.735 1.00 15.39 ? 771  GLY A N   1 
ATOM   6083 C  CA  . GLY A 1 771  ? 42.312 67.830  -36.647 1.00 17.89 ? 771  GLY A CA  1 
ATOM   6084 C  C   . GLY A 1 771  ? 41.603 66.575  -36.225 1.00 18.34 ? 771  GLY A C   1 
ATOM   6085 O  O   . GLY A 1 771  ? 41.391 65.695  -37.077 1.00 19.42 ? 771  GLY A O   1 
ATOM   6086 N  N   . GLY A 1 772  ? 41.259 66.482  -34.936 1.00 17.90 ? 772  GLY A N   1 
ATOM   6087 C  CA  . GLY A 1 772  ? 40.533 65.332  -34.398 1.00 16.75 ? 772  GLY A CA  1 
ATOM   6088 C  C   . GLY A 1 772  ? 39.383 65.832  -33.521 1.00 17.24 ? 772  GLY A C   1 
ATOM   6089 O  O   . GLY A 1 772  ? 38.709 66.825  -33.875 1.00 16.80 ? 772  GLY A O   1 
ATOM   6090 N  N   . ALA A 1 773  ? 39.109 65.163  -32.397 1.00 16.76 ? 773  ALA A N   1 
ATOM   6091 C  CA  . ALA A 1 773  ? 38.011 65.591  -31.519 1.00 15.74 ? 773  ALA A CA  1 
ATOM   6092 C  C   . ALA A 1 773  ? 38.262 66.977  -31.056 1.00 13.97 ? 773  ALA A C   1 
ATOM   6093 O  O   . ALA A 1 773  ? 39.366 67.309  -30.721 1.00 13.20 ? 773  ALA A O   1 
ATOM   6094 C  CB  . ALA A 1 773  ? 37.906 64.685  -30.322 1.00 17.37 ? 773  ALA A CB  1 
ATOM   6095 N  N   . PRO A 1 774  ? 37.235 67.825  -31.025 1.00 13.75 ? 774  PRO A N   1 
ATOM   6096 C  CA  . PRO A 1 774  ? 37.524 69.163  -30.556 1.00 13.48 ? 774  PRO A CA  1 
ATOM   6097 C  C   . PRO A 1 774  ? 37.825 69.234  -29.044 1.00 13.01 ? 774  PRO A C   1 
ATOM   6098 O  O   . PRO A 1 774  ? 37.493 68.297  -28.271 1.00 13.17 ? 774  PRO A O   1 
ATOM   6099 C  CB  . PRO A 1 774  ? 36.259 69.957  -30.899 1.00 13.60 ? 774  PRO A CB  1 
ATOM   6100 C  CG  . PRO A 1 774  ? 35.236 68.949  -30.848 1.00 15.17 ? 774  PRO A CG  1 
ATOM   6101 C  CD  . PRO A 1 774  ? 35.864 67.747  -31.558 1.00 13.28 ? 774  PRO A CD  1 
ATOM   6102 N  N   . GLU A 1 775  ? 38.439 70.325  -28.658 1.00 13.70 ? 775  GLU A N   1 
ATOM   6103 C  CA  . GLU A 1 775  ? 38.665 70.583  -27.266 1.00 11.86 ? 775  GLU A CA  1 
ATOM   6104 C  C   . GLU A 1 775  ? 37.713 71.699  -26.903 1.00 13.01 ? 775  GLU A C   1 
ATOM   6105 O  O   . GLU A 1 775  ? 37.472 72.603  -27.725 1.00 14.05 ? 775  GLU A O   1 
ATOM   6106 C  CB  . GLU A 1 775  ? 40.119 71.003  -27.003 1.00 13.22 ? 775  GLU A CB  1 
ATOM   6107 C  CG  . GLU A 1 775  ? 40.351 71.482  -25.562 1.00 10.24 ? 775  GLU A CG  1 
ATOM   6108 C  CD  . GLU A 1 775  ? 41.760 71.918  -25.238 1.00 15.94 ? 775  GLU A CD  1 
ATOM   6109 O  OE1 . GLU A 1 775  ? 42.608 71.912  -26.151 1.00 17.15 ? 775  GLU A OE1 1 
ATOM   6110 O  OE2 . GLU A 1 775  ? 42.038 72.273  -24.077 1.00 15.05 ? 775  GLU A OE2 1 
ATOM   6111 N  N   . ILE A 1 776  ? 37.109 71.632  -25.715 1.00 11.47 ? 776  ILE A N   1 
ATOM   6112 C  CA  . ILE A 1 776  ? 36.251 72.693  -25.228 1.00 11.93 ? 776  ILE A CA  1 
ATOM   6113 C  C   . ILE A 1 776  ? 36.880 73.341  -24.040 1.00 12.85 ? 776  ILE A C   1 
ATOM   6114 O  O   . ILE A 1 776  ? 37.380 72.644  -23.139 1.00 12.09 ? 776  ILE A O   1 
ATOM   6115 C  CB  . ILE A 1 776  ? 34.869 72.192  -24.762 1.00 11.73 ? 776  ILE A CB  1 
ATOM   6116 C  CG1 . ILE A 1 776  ? 34.257 71.263  -25.847 1.00 14.45 ? 776  ILE A CG1 1 
ATOM   6117 C  CG2 . ILE A 1 776  ? 34.005 73.342  -24.385 1.00 12.68 ? 776  ILE A CG2 1 
ATOM   6118 C  CD1 . ILE A 1 776  ? 34.206 71.814  -27.326 1.00 16.16 ? 776  ILE A CD1 1 
ATOM   6119 N  N   . ARG A 1 777  ? 36.891 74.658  -24.011 1.00 10.85 ? 777  ARG A N   1 
ATOM   6120 C  CA  . ARG A 1 777  ? 37.376 75.365  -22.849 1.00 10.47 ? 777  ARG A CA  1 
ATOM   6121 C  C   . ARG A 1 777  ? 36.353 76.356  -22.377 1.00 12.51 ? 777  ARG A C   1 
ATOM   6122 O  O   . ARG A 1 777  ? 35.834 77.144  -23.234 1.00 11.37 ? 777  ARG A O   1 
ATOM   6123 C  CB  . ARG A 1 777  ? 38.691 76.121  -23.075 1.00 12.92 ? 777  ARG A CB  1 
ATOM   6124 C  CG  . ARG A 1 777  ? 39.858 75.271  -23.489 1.00 12.08 ? 777  ARG A CG  1 
ATOM   6125 C  CD  . ARG A 1 777  ? 41.204 76.041  -23.506 1.00 14.51 ? 777  ARG A CD  1 
ATOM   6126 N  NE  . ARG A 1 777  ? 42.252 75.150  -24.021 1.00 14.28 ? 777  ARG A NE  1 
ATOM   6127 C  CZ  . ARG A 1 777  ? 43.414 75.549  -24.541 1.00 16.95 ? 777  ARG A CZ  1 
ATOM   6128 N  NH1 . ARG A 1 777  ? 43.714 76.836  -24.599 1.00 18.21 ? 777  ARG A NH1 1 
ATOM   6129 N  NH2 . ARG A 1 777  ? 44.231 74.663  -25.093 1.00 18.99 ? 777  ARG A NH2 1 
ATOM   6130 N  N   . ASN A 1 778  ? 36.002 76.350  -21.077 1.00 9.44  ? 778  ASN A N   1 
ATOM   6131 C  CA  . ASN A 1 778  ? 35.035 77.319  -20.532 1.00 10.80 ? 778  ASN A CA  1 
ATOM   6132 C  C   . ASN A 1 778  ? 35.674 78.140  -19.426 1.00 11.66 ? 778  ASN A C   1 
ATOM   6133 O  O   . ASN A 1 778  ? 36.172 77.572  -18.406 1.00 11.87 ? 778  ASN A O   1 
ATOM   6134 C  CB  . ASN A 1 778  ? 33.730 76.707  -19.888 1.00 11.01 ? 778  ASN A CB  1 
ATOM   6135 C  CG  . ASN A 1 778  ? 32.837 75.957  -20.867 1.00 12.32 ? 778  ASN A CG  1 
ATOM   6136 O  OD1 . ASN A 1 778  ? 32.849 76.188  -22.085 1.00 11.88 ? 778  ASN A OD1 1 
ATOM   6137 N  ND2 . ASN A 1 778  ? 32.064 75.009  -20.328 1.00 10.21 ? 778  ASN A ND2 1 
ATOM   6138 N  N   . LEU A 1 779  ? 35.737 79.459  -19.609 1.00 11.88 ? 779  LEU A N   1 
ATOM   6139 C  CA  . LEU A 1 779  ? 36.243 80.353  -18.557 1.00 11.50 ? 779  LEU A CA  1 
ATOM   6140 C  C   . LEU A 1 779  ? 34.989 80.760  -17.852 1.00 12.94 ? 779  LEU A C   1 
ATOM   6141 O  O   . LEU A 1 779  ? 34.194 81.593  -18.329 1.00 11.77 ? 779  LEU A O   1 
ATOM   6142 C  CB  . LEU A 1 779  ? 36.988 81.591  -19.139 1.00 12.89 ? 779  LEU A CB  1 
ATOM   6143 C  CG  . LEU A 1 779  ? 37.423 82.555  -18.007 1.00 14.75 ? 779  LEU A CG  1 
ATOM   6144 C  CD1 . LEU A 1 779  ? 38.435 81.959  -17.029 1.00 19.20 ? 779  LEU A CD1 1 
ATOM   6145 C  CD2 . LEU A 1 779  ? 37.923 83.887  -18.709 1.00 17.09 ? 779  LEU A CD2 1 
ATOM   6146 N  N   . VAL A 1 780  ? 34.795 80.111  -16.705 1.00 10.86 ? 780  VAL A N   1 
ATOM   6147 C  CA  . VAL A 1 780  ? 33.589 80.249  -15.894 1.00 11.50 ? 780  VAL A CA  1 
ATOM   6148 C  C   . VAL A 1 780  ? 33.718 81.232  -14.755 1.00 11.18 ? 780  VAL A C   1 
ATOM   6149 O  O   . VAL A 1 780  ? 34.515 81.084  -13.786 1.00 10.67 ? 780  VAL A O   1 
ATOM   6150 C  CB  . VAL A 1 780  ? 33.039 78.818  -15.360 1.00 9.63  ? 780  VAL A CB  1 
ATOM   6151 C  CG1 . VAL A 1 780  ? 31.631 79.007  -14.754 1.00 12.36 ? 780  VAL A CG1 1 
ATOM   6152 C  CG2 . VAL A 1 780  ? 32.932 77.804  -16.517 1.00 10.90 ? 780  VAL A CG2 1 
ATOM   6153 N  N   . ASP A 1 781  ? 32.960 82.336  -14.892 1.00 11.80 ? 781  ASP A N   1 
ATOM   6154 C  CA  . ASP A 1 781  ? 32.929 83.312  -13.823 1.00 12.69 ? 781  ASP A CA  1 
ATOM   6155 C  C   . ASP A 1 781  ? 31.503 83.598  -13.487 1.00 14.67 ? 781  ASP A C   1 
ATOM   6156 O  O   . ASP A 1 781  ? 30.847 84.415  -14.184 1.00 14.65 ? 781  ASP A O   1 
ATOM   6157 C  CB  . ASP A 1 781  ? 33.628 84.627  -14.207 1.00 14.80 ? 781  ASP A CB  1 
ATOM   6158 C  CG  . ASP A 1 781  ? 33.713 85.630  -13.058 1.00 16.60 ? 781  ASP A CG  1 
ATOM   6159 O  OD1 . ASP A 1 781  ? 33.228 85.425  -11.938 1.00 17.02 ? 781  ASP A OD1 1 
ATOM   6160 O  OD2 . ASP A 1 781  ? 34.287 86.729  -13.279 1.00 20.61 ? 781  ASP A OD2 1 
ATOM   6161 N  N   . ILE A 1 782  ? 31.012 82.963  -12.404 1.00 14.33 ? 782  ILE A N   1 
ATOM   6162 C  CA  . ILE A 1 782  ? 29.605 83.090  -11.993 1.00 15.90 ? 782  ILE A CA  1 
ATOM   6163 C  C   . ILE A 1 782  ? 29.331 84.412  -11.318 1.00 16.12 ? 782  ILE A C   1 
ATOM   6164 O  O   . ILE A 1 782  ? 28.170 84.740  -11.089 1.00 17.30 ? 782  ILE A O   1 
ATOM   6165 C  CB  . ILE A 1 782  ? 29.236 81.852  -11.120 1.00 15.22 ? 782  ILE A CB  1 
ATOM   6166 C  CG1 . ILE A 1 782  ? 27.724 81.611  -11.045 1.00 17.36 ? 782  ILE A CG1 1 
ATOM   6167 C  CG2 . ILE A 1 782  ? 29.857 81.990  -9.744  1.00 14.33 ? 782  ILE A CG2 1 
ATOM   6168 C  CD1 . ILE A 1 782  ? 27.434 80.200  -10.562 1.00 17.15 ? 782  ILE A CD1 1 
ATOM   6169 N  N   . GLY A 1 783  ? 30.379 85.192  -11.065 1.00 16.92 ? 783  GLY A N   1 
ATOM   6170 C  CA  . GLY A 1 783  ? 30.254 86.528  -10.490 1.00 18.26 ? 783  GLY A CA  1 
ATOM   6171 C  C   . GLY A 1 783  ? 29.418 86.640  -9.254  1.00 19.54 ? 783  GLY A C   1 
ATOM   6172 O  O   . GLY A 1 783  ? 29.680 85.951  -8.281  1.00 21.07 ? 783  GLY A O   1 
ATOM   6173 N  N   . SER A 1 784  ? 28.422 87.520  -9.248  1.00 20.94 ? 784  SER A N   1 
ATOM   6174 C  CA  . SER A 1 784  ? 27.591 87.666  -8.065  1.00 22.10 ? 784  SER A CA  1 
ATOM   6175 C  C   . SER A 1 784  ? 26.209 87.061  -8.227  1.00 20.98 ? 784  SER A C   1 
ATOM   6176 O  O   . SER A 1 784  ? 25.242 87.491  -7.585  1.00 20.83 ? 784  SER A O   1 
ATOM   6177 C  CB  . SER A 1 784  ? 27.435 89.158  -7.697  1.00 24.28 ? 784  SER A CB  1 
ATOM   6178 O  OG  . SER A 1 784  ? 26.846 89.899  -8.779  1.00 27.55 ? 784  SER A OG  1 
ATOM   6179 N  N   . LEU A 1 785  ? 26.075 86.072  -9.094  1.00 21.17 ? 785  LEU A N   1 
ATOM   6180 C  CA  . LEU A 1 785  ? 24.745 85.473  -9.279  1.00 21.67 ? 785  LEU A CA  1 
ATOM   6181 C  C   . LEU A 1 785  ? 24.398 84.498  -8.167  1.00 21.56 ? 785  LEU A C   1 
ATOM   6182 O  O   . LEU A 1 785  ? 24.590 83.268  -8.319  1.00 20.39 ? 785  LEU A O   1 
ATOM   6183 C  CB  . LEU A 1 785  ? 24.706 84.735  -10.595 1.00 22.13 ? 785  LEU A CB  1 
ATOM   6184 C  CG  . LEU A 1 785  ? 24.926 85.599  -11.827 1.00 24.68 ? 785  LEU A CG  1 
ATOM   6185 C  CD1 . LEU A 1 785  ? 25.114 84.694  -12.934 1.00 23.46 ? 785  LEU A CD1 1 
ATOM   6186 C  CD2 . LEU A 1 785  ? 23.759 86.524  -12.088 1.00 23.37 ? 785  LEU A CD2 1 
ATOM   6187 N  N   . ASP A 1 786  ? 23.896 84.992  -7.044  1.00 21.62 ? 786  ASP A N   1 
ATOM   6188 C  CA  . ASP A 1 786  ? 23.520 84.112  -5.920  1.00 21.94 ? 786  ASP A CA  1 
ATOM   6189 C  C   . ASP A 1 786  ? 22.430 83.079  -6.272  1.00 20.13 ? 786  ASP A C   1 
ATOM   6190 O  O   . ASP A 1 786  ? 21.559 83.331  -7.096  1.00 20.82 ? 786  ASP A O   1 
ATOM   6191 C  CB  . ASP A 1 786  ? 23.017 84.949  -4.751  1.00 24.87 ? 786  ASP A CB  1 
ATOM   6192 C  CG  . ASP A 1 786  ? 24.111 85.779  -4.117  1.00 28.25 ? 786  ASP A CG  1 
ATOM   6193 O  OD1 . ASP A 1 786  ? 25.254 85.775  -4.646  1.00 28.10 ? 786  ASP A OD1 1 
ATOM   6194 O  OD2 . ASP A 1 786  ? 23.819 86.449  -3.099  1.00 29.33 ? 786  ASP A OD2 1 
ATOM   6195 N  N   . ASN A 1 787  ? 22.509 81.891  -5.679  1.00 18.63 ? 787  ASN A N   1 
ATOM   6196 C  CA  . ASN A 1 787  ? 21.493 80.848  -5.895  1.00 17.34 ? 787  ASN A CA  1 
ATOM   6197 C  C   . ASN A 1 787  ? 21.315 80.424  -7.323  1.00 17.14 ? 787  ASN A C   1 
ATOM   6198 O  O   . ASN A 1 787  ? 20.205 80.268  -7.854  1.00 15.74 ? 787  ASN A O   1 
ATOM   6199 C  CB  . ASN A 1 787  ? 20.171 81.306  -5.276  1.00 19.60 ? 787  ASN A CB  1 
ATOM   6200 C  CG  . ASN A 1 787  ? 20.317 81.565  -3.786  1.00 21.61 ? 787  ASN A CG  1 
ATOM   6201 O  OD1 . ASN A 1 787  ? 21.019 80.825  -3.057  1.00 22.67 ? 787  ASN A OD1 1 
ATOM   6202 N  ND2 . ASN A 1 787  ? 19.661 82.632  -3.308  1.00 23.13 ? 787  ASN A ND2 1 
ATOM   6203 N  N   . THR A 1 788  ? 22.447 80.198  -7.958  1.00 14.19 ? 788  THR A N   1 
ATOM   6204 C  CA  . THR A 1 788  ? 22.472 79.830  -9.343  1.00 14.33 ? 788  THR A CA  1 
ATOM   6205 C  C   . THR A 1 788  ? 23.482 78.730  -9.545  1.00 12.42 ? 788  THR A C   1 
ATOM   6206 O  O   . THR A 1 788  ? 24.569 78.771  -8.943  1.00 14.61 ? 788  THR A O   1 
ATOM   6207 C  CB  . THR A 1 788  ? 22.899 81.053  -10.271 1.00 13.67 ? 788  THR A CB  1 
ATOM   6208 O  OG1 . THR A 1 788  ? 21.895 82.095  -10.128 1.00 16.54 ? 788  THR A OG1 1 
ATOM   6209 C  CG2 . THR A 1 788  ? 23.018 80.619  -11.754 1.00 17.86 ? 788  THR A CG2 1 
ATOM   6210 N  N   . GLU A 1 789  ? 23.107 77.759  -10.363 1.00 11.13 ? 789  GLU A N   1 
ATOM   6211 C  CA  . GLU A 1 789  ? 24.088 76.709  -10.741 1.00 10.92 ? 789  GLU A CA  1 
ATOM   6212 C  C   . GLU A 1 789  ? 24.092 76.711  -12.278 1.00 11.85 ? 789  GLU A C   1 
ATOM   6213 O  O   . GLU A 1 789  ? 23.037 76.585  -12.914 1.00 13.93 ? 789  GLU A O   1 
ATOM   6214 C  CB  . GLU A 1 789  ? 23.676 75.314  -10.172 1.00 12.97 ? 789  GLU A CB  1 
ATOM   6215 C  CG  . GLU A 1 789  ? 23.347 75.398  -8.684  1.00 11.10 ? 789  GLU A CG  1 
ATOM   6216 C  CD  . GLU A 1 789  ? 23.565 74.090  -7.924  1.00 13.05 ? 789  GLU A CD  1 
ATOM   6217 O  OE1 . GLU A 1 789  ? 24.381 73.279  -8.419  1.00 9.71  ? 789  GLU A OE1 1 
ATOM   6218 O  OE2 . GLU A 1 789  ? 22.946 73.898  -6.849  1.00 12.07 ? 789  GLU A OE2 1 
ATOM   6219 N  N   . ILE A 1 790  ? 25.249 76.913  -12.886 1.00 9.83  ? 790  ILE A N   1 
ATOM   6220 C  CA  . ILE A 1 790  ? 25.364 76.971  -14.322 1.00 11.38 ? 790  ILE A CA  1 
ATOM   6221 C  C   . ILE A 1 790  ? 25.720 75.599  -14.848 1.00 10.65 ? 790  ILE A C   1 
ATOM   6222 O  O   . ILE A 1 790  ? 26.702 75.009  -14.375 1.00 11.13 ? 790  ILE A O   1 
ATOM   6223 C  CB  . ILE A 1 790  ? 26.477 77.940  -14.682 1.00 11.81 ? 790  ILE A CB  1 
ATOM   6224 C  CG1 . ILE A 1 790  ? 26.138 79.307  -14.041 1.00 14.33 ? 790  ILE A CG1 1 
ATOM   6225 C  CG2 . ILE A 1 790  ? 26.694 78.006  -16.218 1.00 11.99 ? 790  ILE A CG2 1 
ATOM   6226 C  CD1 . ILE A 1 790  ? 27.179 80.396  -14.283 1.00 18.20 ? 790  ILE A CD1 1 
ATOM   6227 N  N   . VAL A 1 791  ? 24.948 75.085  -15.788 1.00 10.72 ? 791  VAL A N   1 
ATOM   6228 C  CA  . VAL A 1 791  ? 25.169 73.804  -16.402 1.00 10.72 ? 791  VAL A CA  1 
ATOM   6229 C  C   . VAL A 1 791  ? 25.394 73.927  -17.887 1.00 11.96 ? 791  VAL A C   1 
ATOM   6230 O  O   . VAL A 1 791  ? 24.814 74.811  -18.583 1.00 11.65 ? 791  VAL A O   1 
ATOM   6231 C  CB  . VAL A 1 791  ? 23.929 72.850  -16.129 1.00 11.42 ? 791  VAL A CB  1 
ATOM   6232 C  CG1 . VAL A 1 791  ? 22.610 73.422  -16.810 1.00 12.19 ? 791  VAL A CG1 1 
ATOM   6233 C  CG2 . VAL A 1 791  ? 24.251 71.393  -16.641 1.00 11.16 ? 791  VAL A CG2 1 
ATOM   6234 N  N   . MET A 1 792  ? 26.273 73.095  -18.403 1.00 9.65  ? 792  MET A N   1 
ATOM   6235 C  CA  . MET A 1 792  ? 26.531 72.982  -19.835 1.00 10.38 ? 792  MET A CA  1 
ATOM   6236 C  C   . MET A 1 792  ? 25.911 71.646  -20.255 1.00 11.60 ? 792  MET A C   1 
ATOM   6237 O  O   . MET A 1 792  ? 26.216 70.589  -19.685 1.00 10.98 ? 792  MET A O   1 
ATOM   6238 C  CB  . MET A 1 792  ? 28.035 72.986  -20.142 1.00 8.85  ? 792  MET A CB  1 
ATOM   6239 C  CG  . MET A 1 792  ? 28.385 72.700  -21.571 1.00 10.96 ? 792  MET A CG  1 
ATOM   6240 S  SD  . MET A 1 792  ? 30.150 72.821  -21.999 1.00 12.04 ? 792  MET A SD  1 
ATOM   6241 C  CE  . MET A 1 792  ? 30.731 71.206  -21.172 1.00 9.79  ? 792  MET A CE  1 
ATOM   6242 N  N   . ARG A 1 793  ? 24.993 71.708  -21.227 1.00 10.81 ? 793  ARG A N   1 
ATOM   6243 C  CA  . ARG A 1 793  ? 24.245 70.584  -21.801 1.00 11.03 ? 793  ARG A CA  1 
ATOM   6244 C  C   . ARG A 1 793  ? 24.582 70.335  -23.285 1.00 12.26 ? 793  ARG A C   1 
ATOM   6245 O  O   . ARG A 1 793  ? 24.794 71.264  -24.082 1.00 14.80 ? 793  ARG A O   1 
ATOM   6246 C  CB  . ARG A 1 793  ? 22.703 70.786  -21.633 1.00 12.16 ? 793  ARG A CB  1 
ATOM   6247 C  CG  . ARG A 1 793  ? 21.884 69.550  -22.059 1.00 12.35 ? 793  ARG A CG  1 
ATOM   6248 C  CD  . ARG A 1 793  ? 20.371 69.838  -21.781 1.00 11.55 ? 793  ARG A CD  1 
ATOM   6249 N  NE  . ARG A 1 793  ? 20.149 69.898  -20.342 1.00 12.76 ? 793  ARG A NE  1 
ATOM   6250 C  CZ  . ARG A 1 793  ? 19.098 70.455  -19.786 1.00 14.05 ? 793  ARG A CZ  1 
ATOM   6251 N  NH1 . ARG A 1 793  ? 18.160 71.009  -20.585 1.00 12.56 ? 793  ARG A NH1 1 
ATOM   6252 N  NH2 . ARG A 1 793  ? 18.988 70.506  -18.473 1.00 11.60 ? 793  ARG A NH2 1 
ATOM   6253 N  N   . LEU A 1 794  ? 24.552 69.081  -23.666 1.00 12.90 ? 794  LEU A N   1 
ATOM   6254 C  CA  . LEU A 1 794  ? 24.725 68.681  -25.027 1.00 12.84 ? 794  LEU A CA  1 
ATOM   6255 C  C   . LEU A 1 794  ? 23.419 68.017  -25.428 1.00 13.16 ? 794  LEU A C   1 
ATOM   6256 O  O   . LEU A 1 794  ? 22.951 67.080  -24.775 1.00 12.27 ? 794  LEU A O   1 
ATOM   6257 C  CB  . LEU A 1 794  ? 25.850 67.673  -25.185 1.00 14.65 ? 794  LEU A CB  1 
ATOM   6258 C  CG  . LEU A 1 794  ? 27.196 68.374  -25.217 1.00 13.75 ? 794  LEU A CG  1 
ATOM   6259 C  CD1 . LEU A 1 794  ? 28.266 67.437  -24.834 1.00 15.94 ? 794  LEU A CD1 1 
ATOM   6260 C  CD2 . LEU A 1 794  ? 27.450 68.914  -26.606 1.00 16.20 ? 794  LEU A CD2 1 
ATOM   6261 N  N   . GLU A 1 795  ? 22.816 68.510  -26.512 1.00 14.65 ? 795  GLU A N   1 
ATOM   6262 C  CA  . GLU A 1 795  ? 21.588 67.924  -27.032 1.00 15.02 ? 795  GLU A CA  1 
ATOM   6263 C  C   . GLU A 1 795  ? 21.866 67.184  -28.331 1.00 15.37 ? 795  GLU A C   1 
ATOM   6264 O  O   . GLU A 1 795  ? 22.487 67.732  -29.268 1.00 16.62 ? 795  GLU A O   1 
ATOM   6265 C  CB  . GLU A 1 795  ? 20.515 69.000  -27.238 1.00 15.58 ? 795  GLU A CB  1 
ATOM   6266 C  CG  . GLU A 1 795  ? 20.169 69.734  -25.926 1.00 17.17 ? 795  GLU A CG  1 
ATOM   6267 C  CD  . GLU A 1 795  ? 19.254 70.962  -26.136 1.00 20.23 ? 795  GLU A CD  1 
ATOM   6268 O  OE1 . GLU A 1 795  ? 19.360 71.638  -27.168 1.00 22.95 ? 795  GLU A OE1 1 
ATOM   6269 O  OE2 . GLU A 1 795  ? 18.437 71.288  -25.272 1.00 23.24 ? 795  GLU A OE2 1 
ATOM   6270 N  N   . THR A 1 796  ? 21.486 65.910  -28.384 1.00 14.03 ? 796  THR A N   1 
ATOM   6271 C  CA  . THR A 1 796  ? 21.698 65.127  -29.592 1.00 14.05 ? 796  THR A CA  1 
ATOM   6272 C  C   . THR A 1 796  ? 20.421 64.322  -29.823 1.00 13.95 ? 796  THR A C   1 
ATOM   6273 O  O   . THR A 1 796  ? 19.434 64.368  -29.023 1.00 16.80 ? 796  THR A O   1 
ATOM   6274 C  CB  . THR A 1 796  ? 22.888 64.150  -29.483 1.00 12.92 ? 796  THR A CB  1 
ATOM   6275 O  OG1 . THR A 1 796  ? 22.494 62.983  -28.757 1.00 14.09 ? 796  THR A OG1 1 
ATOM   6276 C  CG2 . THR A 1 796  ? 24.040 64.833  -28.694 1.00 14.26 ? 796  THR A CG2 1 
ATOM   6277 N  N   . HIS A 1 797  ? 20.424 63.598  -30.915 1.00 16.25 ? 797  HIS A N   1 
ATOM   6278 C  CA  . HIS A 1 797  ? 19.274 62.771  -31.246 1.00 18.06 ? 797  HIS A CA  1 
ATOM   6279 C  C   . HIS A 1 797  ? 19.672 61.304  -31.052 1.00 18.07 ? 797  HIS A C   1 
ATOM   6280 O  O   . HIS A 1 797  ? 19.024 60.391  -31.600 1.00 20.06 ? 797  HIS A O   1 
ATOM   6281 C  CB  . HIS A 1 797  ? 18.814 63.119  -32.683 1.00 18.32 ? 797  HIS A CB  1 
ATOM   6282 C  CG  . HIS A 1 797  ? 18.270 64.503  -32.798 1.00 16.77 ? 797  HIS A CG  1 
ATOM   6283 N  ND1 . HIS A 1 797  ? 17.964 65.089  -34.005 1.00 16.71 ? 797  HIS A ND1 1 
ATOM   6284 C  CD2 . HIS A 1 797  ? 17.926 65.406  -31.851 1.00 17.58 ? 797  HIS A CD2 1 
ATOM   6285 C  CE1 . HIS A 1 797  ? 17.439 66.279  -33.795 1.00 19.29 ? 797  HIS A CE1 1 
ATOM   6286 N  NE2 . HIS A 1 797  ? 17.403 66.500  -32.498 1.00 20.25 ? 797  HIS A NE2 1 
ATOM   6287 N  N   . ILE A 1 798  ? 20.735 61.054  -30.265 1.00 15.53 ? 798  ILE A N   1 
ATOM   6288 C  CA  . ILE A 1 798  ? 21.184 59.664  -29.987 1.00 12.95 ? 798  ILE A CA  1 
ATOM   6289 C  C   . ILE A 1 798  ? 20.062 59.051  -29.135 1.00 12.91 ? 798  ILE A C   1 
ATOM   6290 O  O   . ILE A 1 798  ? 19.576 59.651  -28.194 1.00 14.08 ? 798  ILE A O   1 
ATOM   6291 C  CB  . ILE A 1 798  ? 22.550 59.681  -29.231 1.00 13.89 ? 798  ILE A CB  1 
ATOM   6292 C  CG1 . ILE A 1 798  ? 23.595 60.269  -30.145 1.00 13.46 ? 798  ILE A CG1 1 
ATOM   6293 C  CG2 . ILE A 1 798  ? 22.981 58.292  -28.783 1.00 15.45 ? 798  ILE A CG2 1 
ATOM   6294 C  CD1 . ILE A 1 798  ? 24.839 60.814  -29.324 1.00 15.12 ? 798  ILE A CD1 1 
ATOM   6295 N  N   . ASP A 1 799  ? 19.647 57.848  -29.521 1.00 14.97 ? 799  ASP A N   1 
ATOM   6296 C  CA  . ASP A 1 799  ? 18.533 57.155  -28.856 1.00 14.19 ? 799  ASP A CA  1 
ATOM   6297 C  C   . ASP A 1 799  ? 19.091 56.359  -27.645 1.00 15.32 ? 799  ASP A C   1 
ATOM   6298 O  O   . ASP A 1 799  ? 19.099 55.139  -27.653 1.00 13.98 ? 799  ASP A O   1 
ATOM   6299 C  CB  . ASP A 1 799  ? 17.884 56.247  -29.907 1.00 18.02 ? 799  ASP A CB  1 
ATOM   6300 C  CG  . ASP A 1 799  ? 16.639 55.593  -29.427 1.00 19.56 ? 799  ASP A CG  1 
ATOM   6301 O  OD1 . ASP A 1 799  ? 16.015 56.062  -28.469 1.00 23.47 ? 799  ASP A OD1 1 
ATOM   6302 O  OD2 . ASP A 1 799  ? 16.285 54.581  -30.038 1.00 24.21 ? 799  ASP A OD2 1 
ATOM   6303 N  N   . SER A 1 800  ? 19.557 57.097  -26.645 1.00 14.82 ? 800  SER A N   1 
ATOM   6304 C  CA  . SER A 1 800  ? 20.147 56.509  -25.460 1.00 14.25 ? 800  SER A CA  1 
ATOM   6305 C  C   . SER A 1 800  ? 19.083 56.088  -24.465 1.00 13.96 ? 800  SER A C   1 
ATOM   6306 O  O   . SER A 1 800  ? 19.375 55.274  -23.587 1.00 14.38 ? 800  SER A O   1 
ATOM   6307 C  CB  . SER A 1 800  ? 21.085 57.510  -24.769 1.00 12.32 ? 800  SER A CB  1 
ATOM   6308 O  OG  . SER A 1 800  ? 20.423 58.724  -24.488 1.00 12.54 ? 800  SER A OG  1 
ATOM   6309 N  N   . GLY A 1 801  ? 17.878 56.648  -24.559 1.00 12.94 ? 801  GLY A N   1 
ATOM   6310 C  CA  . GLY A 1 801  ? 16.793 56.269  -23.668 1.00 12.28 ? 801  GLY A CA  1 
ATOM   6311 C  C   . GLY A 1 801  ? 17.028 56.753  -22.266 1.00 13.12 ? 801  GLY A C   1 
ATOM   6312 O  O   . GLY A 1 801  ? 17.061 57.965  -22.055 1.00 13.95 ? 801  GLY A O   1 
ATOM   6313 N  N   . ASP A 1 802  ? 17.186 55.818  -21.318 1.00 12.46 ? 802  ASP A N   1 
ATOM   6314 C  CA  . ASP A 1 802  ? 17.421 56.207  -19.918 1.00 13.45 ? 802  ASP A CA  1 
ATOM   6315 C  C   . ASP A 1 802  ? 18.841 55.773  -19.446 1.00 13.07 ? 802  ASP A C   1 
ATOM   6316 O  O   . ASP A 1 802  ? 19.178 55.837  -18.254 1.00 11.54 ? 802  ASP A O   1 
ATOM   6317 C  CB  . ASP A 1 802  ? 16.285 55.620  -19.023 1.00 13.58 ? 802  ASP A CB  1 
ATOM   6318 C  CG  . ASP A 1 802  ? 16.187 54.108  -19.085 1.00 16.68 ? 802  ASP A CG  1 
ATOM   6319 O  OD1 . ASP A 1 802  ? 17.038 53.487  -19.732 1.00 18.02 ? 802  ASP A OD1 1 
ATOM   6320 O  OD2 . ASP A 1 802  ? 15.218 53.543  -18.458 1.00 18.55 ? 802  ASP A OD2 1 
ATOM   6321 N  N   . ILE A 1 803  ? 19.666 55.359  -20.404 1.00 11.13 ? 803  ILE A N   1 
ATOM   6322 C  CA  . ILE A 1 803  ? 21.024 54.891  -20.074 1.00 11.34 ? 803  ILE A CA  1 
ATOM   6323 C  C   . ILE A 1 803  ? 22.120 55.908  -20.412 1.00 10.19 ? 803  ILE A C   1 
ATOM   6324 O  O   . ILE A 1 803  ? 22.122 56.555  -21.466 1.00 10.77 ? 803  ILE A O   1 
ATOM   6325 C  CB  . ILE A 1 803  ? 21.372 53.595  -20.875 1.00 10.84 ? 803  ILE A CB  1 
ATOM   6326 C  CG1 . ILE A 1 803  ? 20.322 52.529  -20.582 1.00 13.18 ? 803  ILE A CG1 1 
ATOM   6327 C  CG2 . ILE A 1 803  ? 22.815 53.143  -20.634 1.00 12.43 ? 803  ILE A CG2 1 
ATOM   6328 C  CD1 . ILE A 1 803  ? 20.195 52.173  -19.091 1.00 12.63 ? 803  ILE A CD1 1 
ATOM   6329 N  N   . PHE A 1 804  ? 23.124 55.973  -19.534 1.00 9.93  ? 804  PHE A N   1 
ATOM   6330 C  CA  . PHE A 1 804  ? 24.320 56.801  -19.783 1.00 9.00  ? 804  PHE A CA  1 
ATOM   6331 C  C   . PHE A 1 804  ? 25.459 56.193  -18.956 1.00 8.63  ? 804  PHE A C   1 
ATOM   6332 O  O   . PHE A 1 804  ? 25.256 55.248  -18.162 1.00 9.60  ? 804  PHE A O   1 
ATOM   6333 C  CB  . PHE A 1 804  ? 24.112 58.296  -19.457 1.00 8.65  ? 804  PHE A CB  1 
ATOM   6334 C  CG  . PHE A 1 804  ? 23.716 58.605  -18.028 1.00 6.65  ? 804  PHE A CG  1 
ATOM   6335 C  CD1 . PHE A 1 804  ? 22.405 58.356  -17.561 1.00 8.35  ? 804  PHE A CD1 1 
ATOM   6336 C  CD2 . PHE A 1 804  ? 24.637 59.225  -17.131 1.00 10.32 ? 804  PHE A CD2 1 
ATOM   6337 C  CE1 . PHE A 1 804  ? 22.051 58.734  -16.275 1.00 9.41  ? 804  PHE A CE1 1 
ATOM   6338 C  CE2 . PHE A 1 804  ? 24.267 59.586  -15.863 1.00 7.94  ? 804  PHE A CE2 1 
ATOM   6339 C  CZ  . PHE A 1 804  ? 22.970 59.363  -15.411 1.00 10.46 ? 804  PHE A CZ  1 
ATOM   6340 N  N   . TYR A 1 805  ? 26.655 56.683  -19.176 1.00 8.27  ? 805  TYR A N   1 
ATOM   6341 C  CA  . TYR A 1 805  ? 27.790 56.132  -18.482 1.00 7.80  ? 805  TYR A CA  1 
ATOM   6342 C  C   . TYR A 1 805  ? 28.631 57.243  -17.899 1.00 9.71  ? 805  TYR A C   1 
ATOM   6343 O  O   . TYR A 1 805  ? 28.802 58.304  -18.495 1.00 9.90  ? 805  TYR A O   1 
ATOM   6344 C  CB  . TYR A 1 805  ? 28.658 55.313  -19.466 1.00 9.75  ? 805  TYR A CB  1 
ATOM   6345 C  CG  . TYR A 1 805  ? 27.984 54.088  -20.065 1.00 7.77  ? 805  TYR A CG  1 
ATOM   6346 C  CD1 . TYR A 1 805  ? 27.024 54.218  -21.093 1.00 9.38  ? 805  TYR A CD1 1 
ATOM   6347 C  CD2 . TYR A 1 805  ? 28.272 52.809  -19.577 1.00 10.34 ? 805  TYR A CD2 1 
ATOM   6348 C  CE1 . TYR A 1 805  ? 26.373 53.076  -21.584 1.00 11.65 ? 805  TYR A CE1 1 
ATOM   6349 C  CE2 . TYR A 1 805  ? 27.633 51.662  -20.073 1.00 8.84  ? 805  TYR A CE2 1 
ATOM   6350 C  CZ  . TYR A 1 805  ? 26.685 51.824  -21.076 1.00 10.83 ? 805  TYR A CZ  1 
ATOM   6351 O  OH  . TYR A 1 805  ? 26.081 50.674  -21.535 1.00 12.02 ? 805  TYR A OH  1 
ATOM   6352 N  N   . THR A 1 806  ? 29.103 57.004  -16.678 1.00 9.70  ? 806  THR A N   1 
ATOM   6353 C  CA  . THR A 1 806  ? 30.012 57.940  -16.026 1.00 8.18  ? 806  THR A CA  1 
ATOM   6354 C  C   . THR A 1 806  ? 31.200 57.150  -15.472 1.00 9.27  ? 806  THR A C   1 
ATOM   6355 O  O   . THR A 1 806  ? 31.099 55.951  -15.276 1.00 10.03 ? 806  THR A O   1 
ATOM   6356 C  CB  . THR A 1 806  ? 29.317 58.721  -14.896 1.00 8.27  ? 806  THR A CB  1 
ATOM   6357 O  OG1 . THR A 1 806  ? 28.875 57.850  -13.849 1.00 7.63  ? 806  THR A OG1 1 
ATOM   6358 C  CG2 . THR A 1 806  ? 28.032 59.403  -15.419 1.00 8.49  ? 806  THR A CG2 1 
ATOM   6359 N  N   . ASP A 1 807  ? 32.307 57.829  -15.193 1.00 9.18  ? 807  ASP A N   1 
ATOM   6360 C  CA  . ASP A 1 807  ? 33.435 57.094  -14.598 1.00 7.28  ? 807  ASP A CA  1 
ATOM   6361 C  C   . ASP A 1 807  ? 33.516 57.189  -13.095 1.00 6.16  ? 807  ASP A C   1 
ATOM   6362 O  O   . ASP A 1 807  ? 32.900 58.026  -12.413 1.00 8.71  ? 807  ASP A O   1 
ATOM   6363 C  CB  . ASP A 1 807  ? 34.776 57.524  -15.207 1.00 8.93  ? 807  ASP A CB  1 
ATOM   6364 C  CG  . ASP A 1 807  ? 35.224 58.880  -14.754 1.00 8.94  ? 807  ASP A CG  1 
ATOM   6365 O  OD1 . ASP A 1 807  ? 34.455 59.880  -14.840 1.00 9.40  ? 807  ASP A OD1 1 
ATOM   6366 O  OD2 . ASP A 1 807  ? 36.391 58.951  -14.248 1.00 9.10  ? 807  ASP A OD2 1 
ATOM   6367 N  N   . LEU A 1 808  ? 34.265 56.232  -12.567 1.00 7.28  ? 808  LEU A N   1 
ATOM   6368 C  CA  . LEU A 1 808  ? 34.576 56.214  -11.137 1.00 6.64  ? 808  LEU A CA  1 
ATOM   6369 C  C   . LEU A 1 808  ? 36.072 56.444  -10.941 1.00 7.22  ? 808  LEU A C   1 
ATOM   6370 O  O   . LEU A 1 808  ? 36.895 55.634  -11.399 1.00 6.21  ? 808  LEU A O   1 
ATOM   6371 C  CB  . LEU A 1 808  ? 34.195 54.867  -10.486 1.00 6.74  ? 808  LEU A CB  1 
ATOM   6372 C  CG  . LEU A 1 808  ? 32.662 54.688  -10.446 1.00 6.11  ? 808  LEU A CG  1 
ATOM   6373 C  CD1 . LEU A 1 808  ? 32.277 53.231  -10.284 1.00 6.30  ? 808  LEU A CD1 1 
ATOM   6374 C  CD2 . LEU A 1 808  ? 32.024 55.529  -9.306  1.00 7.94  ? 808  LEU A CD2 1 
ATOM   6375 N  N   . ASN A 1 809  ? 36.417 57.580  -10.337 1.00 7.33  ? 809  ASN A N   1 
ATOM   6376 C  CA  . ASN A 1 809  ? 37.826 57.909  -10.029 1.00 7.66  ? 809  ASN A CA  1 
ATOM   6377 C  C   . ASN A 1 809  ? 38.795 57.813  -11.231 1.00 6.86  ? 809  ASN A C   1 
ATOM   6378 O  O   . ASN A 1 809  ? 39.977 57.552  -11.060 1.00 7.01  ? 809  ASN A O   1 
ATOM   6379 C  CB  . ASN A 1 809  ? 38.312 57.023  -8.829  1.00 6.60  ? 809  ASN A CB  1 
ATOM   6380 C  CG  . ASN A 1 809  ? 37.264 56.907  -7.796  1.00 6.33  ? 809  ASN A CG  1 
ATOM   6381 O  OD1 . ASN A 1 809  ? 36.393 55.990  -7.885  1.00 6.55  ? 809  ASN A OD1 1 
ATOM   6382 N  ND2 . ASN A 1 809  ? 37.258 57.863  -6.851  1.00 7.21  ? 809  ASN A ND2 1 
ATOM   6383 N  N   . GLY A 1 810  ? 38.336 58.042  -12.450 1.00 8.67  ? 810  GLY A N   1 
ATOM   6384 C  CA  . GLY A 1 810  ? 39.263 57.986  -13.573 1.00 8.15  ? 810  GLY A CA  1 
ATOM   6385 C  C   . GLY A 1 810  ? 39.727 56.567  -13.842 1.00 8.58  ? 810  GLY A C   1 
ATOM   6386 O  O   . GLY A 1 810  ? 40.676 56.366  -14.610 1.00 8.30  ? 810  GLY A O   1 
ATOM   6387 N  N   . LEU A 1 811  ? 39.047 55.582  -13.270 1.00 7.76  ? 811  LEU A N   1 
ATOM   6388 C  CA  . LEU A 1 811  ? 39.510 54.189  -13.402 1.00 7.13  ? 811  LEU A CA  1 
ATOM   6389 C  C   . LEU A 1 811  ? 38.681 53.263  -14.257 1.00 9.31  ? 811  LEU A C   1 
ATOM   6390 O  O   . LEU A 1 811  ? 39.226 52.398  -14.946 1.00 10.27 ? 811  LEU A O   1 
ATOM   6391 C  CB  . LEU A 1 811  ? 39.579 53.579  -11.992 1.00 10.03 ? 811  LEU A CB  1 
ATOM   6392 C  CG  . LEU A 1 811  ? 40.027 52.137  -11.863 1.00 10.05 ? 811  LEU A CG  1 
ATOM   6393 C  CD1 . LEU A 1 811  ? 41.457 52.046  -12.265 1.00 11.42 ? 811  LEU A CD1 1 
ATOM   6394 C  CD2 . LEU A 1 811  ? 39.883 51.637  -10.426 1.00 10.85 ? 811  LEU A CD2 1 
ATOM   6395 N  N   . GLN A 1 812  ? 37.371 53.462  -14.217 1.00 8.17  ? 812  GLN A N   1 
ATOM   6396 C  CA  . GLN A 1 812  ? 36.408 52.584  -14.863 1.00 8.36  ? 812  GLN A CA  1 
ATOM   6397 C  C   . GLN A 1 812  ? 35.158 53.332  -15.183 1.00 7.55  ? 812  GLN A C   1 
ATOM   6398 O  O   . GLN A 1 812  ? 34.845 54.314  -14.532 1.00 8.36  ? 812  GLN A O   1 
ATOM   6399 C  CB  . GLN A 1 812  ? 36.082 51.452  -13.916 1.00 9.62  ? 812  GLN A CB  1 
ATOM   6400 C  CG  . GLN A 1 812  ? 35.416 51.918  -12.583 1.00 10.00 ? 812  GLN A CG  1 
ATOM   6401 C  CD  . GLN A 1 812  ? 35.190 50.785  -11.619 1.00 13.37 ? 812  GLN A CD  1 
ATOM   6402 O  OE1 . GLN A 1 812  ? 34.272 49.980  -11.783 1.00 13.00 ? 812  GLN A OE1 1 
ATOM   6403 N  NE2 . GLN A 1 812  ? 36.044 50.710  -10.605 1.00 14.81 ? 812  GLN A NE2 1 
ATOM   6404 N  N   . PHE A 1 813  ? 34.401 52.847  -16.173 1.00 9.03  ? 813  PHE A N   1 
ATOM   6405 C  CA  . PHE A 1 813  ? 33.141 53.486  -16.525 1.00 8.14  ? 813  PHE A CA  1 
ATOM   6406 C  C   . PHE A 1 813  ? 32.017 52.571  -16.095 1.00 8.12  ? 813  PHE A C   1 
ATOM   6407 O  O   . PHE A 1 813  ? 32.039 51.406  -16.388 1.00 9.42  ? 813  PHE A O   1 
ATOM   6408 C  CB  . PHE A 1 813  ? 33.098 53.754  -18.044 1.00 8.71  ? 813  PHE A CB  1 
ATOM   6409 C  CG  . PHE A 1 813  ? 33.856 54.993  -18.417 1.00 6.52  ? 813  PHE A CG  1 
ATOM   6410 C  CD1 . PHE A 1 813  ? 35.239 54.967  -18.462 1.00 8.25  ? 813  PHE A CD1 1 
ATOM   6411 C  CD2 . PHE A 1 813  ? 33.188 56.190  -18.627 1.00 8.67  ? 813  PHE A CD2 1 
ATOM   6412 C  CE1 . PHE A 1 813  ? 35.975 56.147  -18.709 1.00 10.11 ? 813  PHE A CE1 1 
ATOM   6413 C  CE2 . PHE A 1 813  ? 33.891 57.369  -18.882 1.00 10.24 ? 813  PHE A CE2 1 
ATOM   6414 C  CZ  . PHE A 1 813  ? 35.308 57.336  -18.925 1.00 10.18 ? 813  PHE A CZ  1 
ATOM   6415 N  N   . ILE A 1 814  ? 31.022 53.117  -15.444 1.00 7.58  ? 814  ILE A N   1 
ATOM   6416 C  CA  . ILE A 1 814  ? 29.891 52.343  -14.945 1.00 6.39  ? 814  ILE A CA  1 
ATOM   6417 C  C   . ILE A 1 814  ? 28.606 52.798  -15.580 1.00 7.72  ? 814  ILE A C   1 
ATOM   6418 O  O   . ILE A 1 814  ? 28.399 53.977  -15.824 1.00 7.21  ? 814  ILE A O   1 
ATOM   6419 C  CB  . ILE A 1 814  ? 29.855 52.470  -13.369 1.00 6.93  ? 814  ILE A CB  1 
ATOM   6420 C  CG1 . ILE A 1 814  ? 28.781 51.505  -12.772 1.00 7.54  ? 814  ILE A CG1 1 
ATOM   6421 C  CG2 . ILE A 1 814  ? 29.625 53.954  -12.880 1.00 7.78  ? 814  ILE A CG2 1 
ATOM   6422 C  CD1 . ILE A 1 814  ? 28.951 51.323  -11.188 1.00 7.90  ? 814  ILE A CD1 1 
ATOM   6423 N  N   . LYS A 1 815  ? 27.763 51.825  -15.955 1.00 7.59  ? 815  LYS A N   1 
ATOM   6424 C  CA  . LYS A 1 815  ? 26.439 52.088  -16.536 1.00 8.53  ? 815  LYS A CA  1 
ATOM   6425 C  C   . LYS A 1 815  ? 25.504 52.697  -15.502 1.00 7.88  ? 815  LYS A C   1 
ATOM   6426 O  O   . LYS A 1 815  ? 25.399 52.197  -14.340 1.00 7.67  ? 815  LYS A O   1 
ATOM   6427 C  CB  . LYS A 1 815  ? 25.825 50.783  -16.955 1.00 10.52 ? 815  LYS A CB  1 
ATOM   6428 C  CG  . LYS A 1 815  ? 24.513 50.935  -17.851 1.00 7.96  ? 815  LYS A CG  1 
ATOM   6429 C  CD  . LYS A 1 815  ? 24.176 49.506  -18.348 1.00 11.18 ? 815  LYS A CD  1 
ATOM   6430 C  CE  . LYS A 1 815  ? 23.128 49.465  -19.446 1.00 14.78 ? 815  LYS A CE  1 
ATOM   6431 N  NZ  . LYS A 1 815  ? 23.123 47.991  -19.892 1.00 18.17 ? 815  LYS A NZ  1 
ATOM   6432 N  N   . ARG A 1 816  ? 24.853 53.790  -15.914 1.00 8.99  ? 816  ARG A N   1 
ATOM   6433 C  CA  . ARG A 1 816  ? 23.876 54.478  -15.067 1.00 7.61  ? 816  ARG A CA  1 
ATOM   6434 C  C   . ARG A 1 816  ? 22.515 54.350  -15.782 1.00 5.73  ? 816  ARG A C   1 
ATOM   6435 O  O   . ARG A 1 816  ? 22.434 54.287  -16.999 1.00 9.63  ? 816  ARG A O   1 
ATOM   6436 C  CB  . ARG A 1 816  ? 24.162 56.022  -14.859 1.00 7.74  ? 816  ARG A CB  1 
ATOM   6437 C  CG  . ARG A 1 816  ? 25.527 56.329  -14.314 1.00 8.92  ? 816  ARG A CG  1 
ATOM   6438 C  CD  . ARG A 1 816  ? 25.710 55.639  -12.981 1.00 7.44  ? 816  ARG A CD  1 
ATOM   6439 N  NE  . ARG A 1 816  ? 26.914 56.219  -12.363 1.00 8.03  ? 816  ARG A NE  1 
ATOM   6440 C  CZ  . ARG A 1 816  ? 27.339 55.841  -11.163 1.00 7.46  ? 816  ARG A CZ  1 
ATOM   6441 N  NH1 . ARG A 1 816  ? 26.685 54.882  -10.501 1.00 8.37  ? 816  ARG A NH1 1 
ATOM   6442 N  NH2 . ARG A 1 816  ? 28.379 56.435  -10.584 1.00 7.18  ? 816  ARG A NH2 1 
ATOM   6443 N  N   . ARG A 1 817  ? 21.445 54.309  -14.989 1.00 9.33  ? 817  ARG A N   1 
ATOM   6444 C  CA  . ARG A 1 817  ? 20.102 54.320  -15.563 1.00 8.19  ? 817  ARG A CA  1 
ATOM   6445 C  C   . ARG A 1 817  ? 19.367 55.448  -14.812 1.00 9.07  ? 817  ARG A C   1 
ATOM   6446 O  O   . ARG A 1 817  ? 19.254 55.462  -13.557 1.00 9.18  ? 817  ARG A O   1 
ATOM   6447 C  CB  . ARG A 1 817  ? 19.366 52.947  -15.379 1.00 9.75  ? 817  ARG A CB  1 
ATOM   6448 C  CG  . ARG A 1 817  ? 17.872 53.065  -15.708 1.00 10.42 ? 817  ARG A CG  1 
ATOM   6449 C  CD  . ARG A 1 817  ? 17.139 51.688  -15.546 1.00 14.14 ? 817  ARG A CD  1 
ATOM   6450 N  NE  . ARG A 1 817  ? 17.722 50.685  -16.435 1.00 13.92 ? 817  ARG A NE  1 
ATOM   6451 C  CZ  . ARG A 1 817  ? 18.500 49.680  -16.067 1.00 15.43 ? 817  ARG A CZ  1 
ATOM   6452 N  NH1 . ARG A 1 817  ? 18.817 49.496  -14.786 1.00 13.92 ? 817  ARG A NH1 1 
ATOM   6453 N  NH2 . ARG A 1 817  ? 18.936 48.825  -16.979 1.00 18.31 ? 817  ARG A NH2 1 
ATOM   6454 N  N   . ARG A 1 818  ? 18.911 56.400  -15.645 1.00 9.37  ? 818  ARG A N   1 
ATOM   6455 C  CA  . ARG A 1 818  ? 18.103 57.498  -15.176 1.00 11.68 ? 818  ARG A CA  1 
ATOM   6456 C  C   . ARG A 1 818  ? 16.784 56.908  -14.642 1.00 11.54 ? 818  ARG A C   1 
ATOM   6457 O  O   . ARG A 1 818  ? 16.148 56.135  -15.329 1.00 13.07 ? 818  ARG A O   1 
ATOM   6458 C  CB  . ARG A 1 818  ? 17.753 58.416  -16.362 1.00 11.75 ? 818  ARG A CB  1 
ATOM   6459 C  CG  . ARG A 1 818  ? 17.120 59.684  -15.859 1.00 12.54 ? 818  ARG A CG  1 
ATOM   6460 C  CD  . ARG A 1 818  ? 16.423 60.500  -16.967 1.00 15.58 ? 818  ARG A CD  1 
ATOM   6461 N  NE  . ARG A 1 818  ? 15.131 59.897  -17.269 1.00 16.40 ? 818  ARG A NE  1 
ATOM   6462 C  CZ  . ARG A 1 818  ? 14.806 59.289  -18.417 1.00 18.99 ? 818  ARG A CZ  1 
ATOM   6463 N  NH1 . ARG A 1 818  ? 15.668 59.172  -19.438 1.00 19.12 ? 818  ARG A NH1 1 
ATOM   6464 N  NH2 . ARG A 1 818  ? 13.575 58.794  -18.511 1.00 19.87 ? 818  ARG A NH2 1 
ATOM   6465 N  N   . LEU A 1 819  ? 16.394 57.301  -13.429 1.00 10.69 ? 819  LEU A N   1 
ATOM   6466 C  CA  . LEU A 1 819  ? 15.156 56.785  -12.808 1.00 11.32 ? 819  LEU A CA  1 
ATOM   6467 C  C   . LEU A 1 819  ? 14.179 57.925  -12.508 1.00 13.93 ? 819  LEU A C   1 
ATOM   6468 O  O   . LEU A 1 819  ? 14.440 58.802  -11.699 1.00 11.98 ? 819  LEU A O   1 
ATOM   6469 C  CB  . LEU A 1 819  ? 15.488 56.016  -11.515 1.00 13.05 ? 819  LEU A CB  1 
ATOM   6470 C  CG  . LEU A 1 819  ? 16.442 54.793  -11.645 1.00 13.27 ? 819  LEU A CG  1 
ATOM   6471 C  CD1 . LEU A 1 819  ? 16.842 54.339  -10.179 1.00 12.89 ? 819  LEU A CD1 1 
ATOM   6472 C  CD2 . LEU A 1 819  ? 15.860 53.658  -12.466 1.00 14.27 ? 819  LEU A CD2 1 
ATOM   6473 N  N   . ASP A 1 820  ? 13.021 57.891  -13.179 1.00 14.82 ? 820  ASP A N   1 
ATOM   6474 C  CA  . ASP A 1 820  ? 12.061 58.956  -12.920 1.00 15.05 ? 820  ASP A CA  1 
ATOM   6475 C  C   . ASP A 1 820  ? 11.365 58.769  -11.558 1.00 13.06 ? 820  ASP A C   1 
ATOM   6476 O  O   . ASP A 1 820  ? 10.705 59.672  -11.094 1.00 13.12 ? 820  ASP A O   1 
ATOM   6477 C  CB  . ASP A 1 820  ? 11.077 59.107  -14.076 1.00 15.90 ? 820  ASP A CB  1 
ATOM   6478 C  CG  . ASP A 1 820  ? 11.798 59.386  -15.426 1.00 17.21 ? 820  ASP A CG  1 
ATOM   6479 O  OD1 . ASP A 1 820  ? 12.925 59.964  -15.456 1.00 19.82 ? 820  ASP A OD1 1 
ATOM   6480 O  OD2 . ASP A 1 820  ? 11.237 59.019  -16.465 1.00 20.60 ? 820  ASP A OD2 1 
ATOM   6481 N  N   . LYS A 1 821  ? 11.609 57.645  -10.865 1.00 12.80 ? 821  LYS A N   1 
ATOM   6482 C  CA  . LYS A 1 821  ? 11.044 57.487  -9.520  1.00 12.78 ? 821  LYS A CA  1 
ATOM   6483 C  C   . LYS A 1 821  ? 11.897 58.245  -8.506  1.00 14.42 ? 821  LYS A C   1 
ATOM   6484 O  O   . LYS A 1 821  ? 11.492 58.438  -7.360  1.00 15.25 ? 821  LYS A O   1 
ATOM   6485 C  CB  . LYS A 1 821  ? 10.958 56.007  -9.089  1.00 11.21 ? 821  LYS A CB  1 
ATOM   6486 C  CG  . LYS A 1 821  ? 12.305 55.289  -9.015  1.00 10.74 ? 821  LYS A CG  1 
ATOM   6487 C  CD  . LYS A 1 821  ? 12.059 53.791  -8.878  1.00 13.13 ? 821  LYS A CD  1 
ATOM   6488 C  CE  . LYS A 1 821  ? 13.376 53.064  -8.905  1.00 13.52 ? 821  LYS A CE  1 
ATOM   6489 N  NZ  . LYS A 1 821  ? 13.247 51.606  -8.948  1.00 13.43 ? 821  LYS A NZ  1 
ATOM   6490 N  N   . LEU A 1 822  ? 13.075 58.705  -8.935  1.00 12.35 ? 822  LEU A N   1 
ATOM   6491 C  CA  . LEU A 1 822  ? 13.919 59.490  -8.039  1.00 13.75 ? 822  LEU A CA  1 
ATOM   6492 C  C   . LEU A 1 822  ? 13.923 60.934  -8.570  1.00 13.05 ? 822  LEU A C   1 
ATOM   6493 O  O   . LEU A 1 822  ? 13.699 61.159  -9.763  1.00 11.72 ? 822  LEU A O   1 
ATOM   6494 C  CB  . LEU A 1 822  ? 15.347 58.937  -7.978  1.00 14.82 ? 822  LEU A CB  1 
ATOM   6495 C  CG  . LEU A 1 822  ? 15.496 57.502  -7.457  1.00 13.75 ? 822  LEU A CG  1 
ATOM   6496 C  CD1 . LEU A 1 822  ? 16.954 57.197  -7.432  1.00 16.60 ? 822  LEU A CD1 1 
ATOM   6497 C  CD2 . LEU A 1 822  ? 14.852 57.297  -6.117  1.00 15.03 ? 822  LEU A CD2 1 
ATOM   6498 N  N   . PRO A 1 823  ? 14.147 61.915  -7.678  1.00 13.97 ? 823  PRO A N   1 
ATOM   6499 C  CA  . PRO A 1 823  ? 14.179 63.323  -8.040  1.00 13.52 ? 823  PRO A CA  1 
ATOM   6500 C  C   . PRO A 1 823  ? 15.390 63.636  -8.917  1.00 13.35 ? 823  PRO A C   1 
ATOM   6501 O  O   . PRO A 1 823  ? 16.350 62.854  -9.010  1.00 14.70 ? 823  PRO A O   1 
ATOM   6502 C  CB  . PRO A 1 823  ? 14.156 64.051  -6.687  1.00 14.97 ? 823  PRO A CB  1 
ATOM   6503 C  CG  . PRO A 1 823  ? 14.764 63.087  -5.698  1.00 15.94 ? 823  PRO A CG  1 
ATOM   6504 C  CD  . PRO A 1 823  ? 14.349 61.711  -6.222  1.00 13.76 ? 823  PRO A CD  1 
ATOM   6505 N  N   . LEU A 1 824  ? 15.353 64.778  -9.618  1.00 12.67 ? 824  LEU A N   1 
ATOM   6506 C  CA  . LEU A 1 824  ? 16.437 65.139  -10.539 1.00 10.71 ? 824  LEU A CA  1 
ATOM   6507 C  C   . LEU A 1 824  ? 17.833 65.050  -9.875  1.00 11.22 ? 824  LEU A C   1 
ATOM   6508 O  O   . LEU A 1 824  ? 18.763 64.501  -10.464 1.00 10.30 ? 824  LEU A O   1 
ATOM   6509 C  CB  . LEU A 1 824  ? 16.155 66.581  -10.979 1.00 12.91 ? 824  LEU A CB  1 
ATOM   6510 C  CG  . LEU A 1 824  ? 16.953 67.237  -12.120 1.00 11.75 ? 824  LEU A CG  1 
ATOM   6511 C  CD1 . LEU A 1 824  ? 16.199 68.497  -12.560 1.00 13.85 ? 824  LEU A CD1 1 
ATOM   6512 C  CD2 . LEU A 1 824  ? 18.377 67.644  -11.663 1.00 13.41 ? 824  LEU A CD2 1 
ATOM   6513 N  N   . GLN A 1 825  ? 17.948 65.587  -8.671  1.00 9.94  ? 825  GLN A N   1 
ATOM   6514 C  CA  . GLN A 1 825  ? 19.274 65.600  -8.041  1.00 10.35 ? 825  GLN A CA  1 
ATOM   6515 C  C   . GLN A 1 825  ? 19.860 64.191  -7.783  1.00 10.66 ? 825  GLN A C   1 
ATOM   6516 O  O   . GLN A 1 825  ? 21.107 64.035  -7.578  1.00 8.06  ? 825  GLN A O   1 
ATOM   6517 C  CB  . GLN A 1 825  ? 19.267 66.454  -6.783  1.00 9.94  ? 825  GLN A CB  1 
ATOM   6518 C  CG  . GLN A 1 825  ? 18.312 65.945  -5.688  1.00 8.88  ? 825  GLN A CG  1 
ATOM   6519 C  CD  . GLN A 1 825  ? 16.844 66.423  -5.819  1.00 8.92  ? 825  GLN A CD  1 
ATOM   6520 O  OE1 . GLN A 1 825  ? 16.397 66.861  -6.872  1.00 13.03 ? 825  GLN A OE1 1 
ATOM   6521 N  NE2 . GLN A 1 825  ? 16.113 66.308  -4.757  1.00 11.99 ? 825  GLN A NE2 1 
ATOM   6522 N  N   . ALA A 1 826  ? 18.970 63.190  -7.717  1.00 9.54  ? 826  ALA A N   1 
ATOM   6523 C  CA  . ALA A 1 826  ? 19.409 61.808  -7.467  1.00 9.87  ? 826  ALA A CA  1 
ATOM   6524 C  C   . ALA A 1 826  ? 19.994 61.219  -8.713  1.00 9.69  ? 826  ALA A C   1 
ATOM   6525 O  O   . ALA A 1 826  ? 20.743 60.257  -8.609  1.00 10.27 ? 826  ALA A O   1 
ATOM   6526 C  CB  . ALA A 1 826  ? 18.181 60.971  -6.983  1.00 10.69 ? 826  ALA A CB  1 
ATOM   6527 N  N   . ASN A 1 827  ? 19.626 61.751  -9.901  1.00 8.81  ? 827  ASN A N   1 
ATOM   6528 C  CA  . ASN A 1 827  ? 20.130 61.268  -11.182 1.00 8.19  ? 827  ASN A CA  1 
ATOM   6529 C  C   . ASN A 1 827  ? 21.438 61.936  -11.594 1.00 7.20  ? 827  ASN A C   1 
ATOM   6530 O  O   . ASN A 1 827  ? 21.927 61.604  -12.664 1.00 8.63  ? 827  ASN A O   1 
ATOM   6531 C  CB  . ASN A 1 827  ? 19.032 61.383  -12.283 1.00 10.06 ? 827  ASN A CB  1 
ATOM   6532 C  CG  . ASN A 1 827  ? 17.904 60.454  -12.002 1.00 13.12 ? 827  ASN A CG  1 
ATOM   6533 O  OD1 . ASN A 1 827  ? 18.073 59.240  -12.057 1.00 10.54 ? 827  ASN A OD1 1 
ATOM   6534 N  ND2 . ASN A 1 827  ? 16.742 61.011  -11.668 1.00 13.80 ? 827  ASN A ND2 1 
ATOM   6535 N  N   . TYR A 1 828  ? 21.927 62.819  -10.716 1.00 9.49  ? 828  TYR A N   1 
ATOM   6536 C  CA  . TYR A 1 828  ? 23.242 63.407  -10.895 1.00 8.17  ? 828  TYR A CA  1 
ATOM   6537 C  C   . TYR A 1 828  ? 24.264 62.456  -10.306 1.00 10.27 ? 828  TYR A C   1 
ATOM   6538 O  O   . TYR A 1 828  ? 24.037 61.930  -9.200  1.00 11.49 ? 828  TYR A O   1 
ATOM   6539 C  CB  . TYR A 1 828  ? 23.352 64.730  -10.145 1.00 7.33  ? 828  TYR A CB  1 
ATOM   6540 C  CG  . TYR A 1 828  ? 23.397 65.894  -11.139 1.00 10.74 ? 828  TYR A CG  1 
ATOM   6541 C  CD1 . TYR A 1 828  ? 22.343 66.108  -12.033 1.00 8.09  ? 828  TYR A CD1 1 
ATOM   6542 C  CD2 . TYR A 1 828  ? 24.484 66.755  -11.179 1.00 10.42 ? 828  TYR A CD2 1 
ATOM   6543 C  CE1 . TYR A 1 828  ? 22.366 67.158  -12.949 1.00 12.68 ? 828  TYR A CE1 1 
ATOM   6544 C  CE2 . TYR A 1 828  ? 24.541 67.783  -12.078 1.00 10.40 ? 828  TYR A CE2 1 
ATOM   6545 C  CZ  . TYR A 1 828  ? 23.477 68.002  -12.978 1.00 9.93  ? 828  TYR A CZ  1 
ATOM   6546 O  OH  . TYR A 1 828  ? 23.526 69.008  -13.923 1.00 11.83 ? 828  TYR A OH  1 
ATOM   6547 N  N   . TYR A 1 829  ? 25.362 62.273  -11.040 1.00 8.14  ? 829  TYR A N   1 
ATOM   6548 C  CA  . TYR A 1 829  ? 26.509 61.395  -10.638 1.00 7.47  ? 829  TYR A CA  1 
ATOM   6549 C  C   . TYR A 1 829  ? 27.841 62.127  -10.771 1.00 8.96  ? 829  TYR A C   1 
ATOM   6550 O  O   . TYR A 1 829  ? 27.936 63.226  -11.373 1.00 9.07  ? 829  TYR A O   1 
ATOM   6551 C  CB  . TYR A 1 829  ? 26.543 60.120  -11.488 1.00 7.32  ? 829  TYR A CB  1 
ATOM   6552 C  CG  . TYR A 1 829  ? 25.346 59.240  -11.213 1.00 8.70  ? 829  TYR A CG  1 
ATOM   6553 C  CD1 . TYR A 1 829  ? 25.412 58.345  -10.152 1.00 9.20  ? 829  TYR A CD1 1 
ATOM   6554 C  CD2 . TYR A 1 829  ? 24.177 59.319  -11.992 1.00 9.91  ? 829  TYR A CD2 1 
ATOM   6555 C  CE1 . TYR A 1 829  ? 24.316 57.504  -9.806  1.00 10.60 ? 829  TYR A CE1 1 
ATOM   6556 C  CE2 . TYR A 1 829  ? 23.071 58.497  -11.692 1.00 9.27  ? 829  TYR A CE2 1 
ATOM   6557 C  CZ  . TYR A 1 829  ? 23.163 57.586  -10.570 1.00 8.79  ? 829  TYR A CZ  1 
ATOM   6558 O  OH  . TYR A 1 829  ? 22.103 56.773  -10.252 1.00 10.55 ? 829  TYR A OH  1 
ATOM   6559 N  N   . PRO A 1 830  ? 28.881 61.599  -10.079 1.00 8.81  ? 830  PRO A N   1 
ATOM   6560 C  CA  . PRO A 1 830  ? 30.188 62.276  -10.238 1.00 6.01  ? 830  PRO A CA  1 
ATOM   6561 C  C   . PRO A 1 830  ? 30.675 62.012  -11.677 1.00 7.18  ? 830  PRO A C   1 
ATOM   6562 O  O   . PRO A 1 830  ? 30.454 60.942  -12.230 1.00 6.86  ? 830  PRO A O   1 
ATOM   6563 C  CB  . PRO A 1 830  ? 31.097 61.534  -9.229  1.00 8.95  ? 830  PRO A CB  1 
ATOM   6564 C  CG  . PRO A 1 830  ? 30.160 60.801  -8.305  1.00 10.10 ? 830  PRO A CG  1 
ATOM   6565 C  CD  . PRO A 1 830  ? 28.842 60.590  -8.992  1.00 8.95  ? 830  PRO A CD  1 
ATOM   6566 N  N   . ILE A 1 831  ? 31.295 63.018  -12.255 1.00 6.57  ? 831  ILE A N   1 
ATOM   6567 C  CA  . ILE A 1 831  ? 31.951 62.921  -13.549 1.00 6.58  ? 831  ILE A CA  1 
ATOM   6568 C  C   . ILE A 1 831  ? 33.380 63.235  -13.234 1.00 8.24  ? 831  ILE A C   1 
ATOM   6569 O  O   . ILE A 1 831  ? 33.913 64.275  -13.622 1.00 10.10 ? 831  ILE A O   1 
ATOM   6570 C  CB  . ILE A 1 831  ? 31.349 63.898  -14.600 1.00 7.12  ? 831  ILE A CB  1 
ATOM   6571 C  CG1 . ILE A 1 831  ? 29.802 63.961  -14.586 1.00 6.65  ? 831  ILE A CG1 1 
ATOM   6572 C  CG2 . ILE A 1 831  ? 31.869 63.464  -15.969 1.00 9.09  ? 831  ILE A CG2 1 
ATOM   6573 C  CD1 . ILE A 1 831  ? 29.101 62.583  -14.928 1.00 9.49  ? 831  ILE A CD1 1 
ATOM   6574 N  N   . PRO A 1 832  ? 34.125 62.236  -12.648 1.00 7.01  ? 832  PRO A N   1 
ATOM   6575 C  CA  . PRO A 1 832  ? 35.512 62.584  -12.322 1.00 7.66  ? 832  PRO A CA  1 
ATOM   6576 C  C   . PRO A 1 832  ? 36.425 62.776  -13.499 1.00 6.98  ? 832  PRO A C   1 
ATOM   6577 O  O   . PRO A 1 832  ? 37.339 63.583  -13.392 1.00 9.25  ? 832  PRO A O   1 
ATOM   6578 C  CB  . PRO A 1 832  ? 35.940 61.512  -11.266 1.00 6.13  ? 832  PRO A CB  1 
ATOM   6579 C  CG  . PRO A 1 832  ? 34.966 60.370  -11.467 1.00 9.00  ? 832  PRO A CG  1 
ATOM   6580 C  CD  . PRO A 1 832  ? 33.668 61.010  -11.962 1.00 6.82  ? 832  PRO A CD  1 
ATOM   6581 N  N   . SER A 1 833  ? 36.128 62.108  -14.613 1.00 9.47  ? 833  SER A N   1 
ATOM   6582 C  CA  . SER A 1 833  ? 36.947 62.202  -15.842 1.00 8.12  ? 833  SER A CA  1 
ATOM   6583 C  C   . SER A 1 833  ? 36.158 62.070  -17.130 1.00 8.71  ? 833  SER A C   1 
ATOM   6584 O  O   . SER A 1 833  ? 36.699 62.404  -18.168 1.00 8.01  ? 833  SER A O   1 
ATOM   6585 C  CB  . SER A 1 833  ? 37.981 61.067  -15.951 1.00 11.39 ? 833  SER A CB  1 
ATOM   6586 O  OG  . SER A 1 833  ? 38.632 60.983  -14.733 1.00 22.84 ? 833  SER A OG  1 
ATOM   6587 N  N   . GLY A 1 834  ? 34.925 61.548  -17.111 1.00 7.41  ? 834  GLY A N   1 
ATOM   6588 C  CA  . GLY A 1 834  ? 34.248 61.449  -18.390 1.00 8.44  ? 834  GLY A CA  1 
ATOM   6589 C  C   . GLY A 1 834  ? 32.888 60.831  -18.300 1.00 7.76  ? 834  GLY A C   1 
ATOM   6590 O  O   . GLY A 1 834  ? 32.509 60.206  -17.289 1.00 9.54  ? 834  GLY A O   1 
ATOM   6591 N  N   . MET A 1 835  ? 32.151 60.923  -19.425 1.00 7.28  ? 835  MET A N   1 
ATOM   6592 C  CA  . MET A 1 835  ? 30.778 60.401  -19.451 1.00 7.30  ? 835  MET A CA  1 
ATOM   6593 C  C   . MET A 1 835  ? 30.389 60.222  -20.892 1.00 8.34  ? 835  MET A C   1 
ATOM   6594 O  O   . MET A 1 835  ? 31.012 60.859  -21.793 1.00 9.04  ? 835  MET A O   1 
ATOM   6595 C  CB  . MET A 1 835  ? 29.792 61.409  -18.761 1.00 9.03  ? 835  MET A CB  1 
ATOM   6596 C  CG  . MET A 1 835  ? 29.686 62.769  -19.499 1.00 11.36 ? 835  MET A CG  1 
ATOM   6597 S  SD  . MET A 1 835  ? 28.748 64.070  -18.635 1.00 13.31 ? 835  MET A SD  1 
ATOM   6598 C  CE  . MET A 1 835  ? 27.262 63.300  -18.324 1.00 14.95 ? 835  MET A CE  1 
ATOM   6599 N  N   . PHE A 1 836  ? 29.435 59.319  -21.153 1.00 8.56  ? 836  PHE A N   1 
ATOM   6600 C  CA  . PHE A 1 836  ? 28.976 59.154  -22.544 1.00 9.96  ? 836  PHE A CA  1 
ATOM   6601 C  C   . PHE A 1 836  ? 27.608 58.567  -22.608 1.00 11.53 ? 836  PHE A C   1 
ATOM   6602 O  O   . PHE A 1 836  ? 27.056 58.078  -21.615 1.00 10.28 ? 836  PHE A O   1 
ATOM   6603 C  CB  . PHE A 1 836  ? 29.961 58.330  -23.413 1.00 8.56  ? 836  PHE A CB  1 
ATOM   6604 C  CG  . PHE A 1 836  ? 30.180 56.844  -22.966 1.00 9.39  ? 836  PHE A CG  1 
ATOM   6605 C  CD1 . PHE A 1 836  ? 29.350 55.792  -23.447 1.00 8.76  ? 836  PHE A CD1 1 
ATOM   6606 C  CD2 . PHE A 1 836  ? 31.279 56.469  -22.162 1.00 7.69  ? 836  PHE A CD2 1 
ATOM   6607 C  CE1 . PHE A 1 836  ? 29.619 54.424  -23.148 1.00 12.50 ? 836  PHE A CE1 1 
ATOM   6608 C  CE2 . PHE A 1 836  ? 31.546 55.070  -21.868 1.00 10.02 ? 836  PHE A CE2 1 
ATOM   6609 C  CZ  . PHE A 1 836  ? 30.720 54.055  -22.360 1.00 11.99 ? 836  PHE A CZ  1 
ATOM   6610 N  N   . ILE A 1 837  ? 27.031 58.704  -23.802 1.00 9.86  ? 837  ILE A N   1 
ATOM   6611 C  CA  . ILE A 1 837  ? 25.728 58.109  -24.154 1.00 9.92  ? 837  ILE A CA  1 
ATOM   6612 C  C   . ILE A 1 837  ? 25.923 57.487  -25.505 1.00 11.42 ? 837  ILE A C   1 
ATOM   6613 O  O   . ILE A 1 837  ? 26.804 57.928  -26.319 1.00 11.06 ? 837  ILE A O   1 
ATOM   6614 C  CB  . ILE A 1 837  ? 24.605 59.121  -24.252 1.00 11.81 ? 837  ILE A CB  1 
ATOM   6615 C  CG1 . ILE A 1 837  ? 25.042 60.360  -25.029 1.00 11.27 ? 837  ILE A CG1 1 
ATOM   6616 C  CG2 . ILE A 1 837  ? 24.100 59.443  -22.876 1.00 11.26 ? 837  ILE A CG2 1 
ATOM   6617 C  CD1 . ILE A 1 837  ? 23.811 61.218  -25.600 1.00 12.96 ? 837  ILE A CD1 1 
ATOM   6618 N  N   . GLU A 1 838  ? 25.114 56.456  -25.794 1.00 10.33 ? 838  GLU A N   1 
ATOM   6619 C  CA  . GLU A 1 838  ? 25.223 55.798  -27.082 1.00 11.88 ? 838  GLU A CA  1 
ATOM   6620 C  C   . GLU A 1 838  ? 23.910 55.070  -27.408 1.00 9.58  ? 838  GLU A C   1 
ATOM   6621 O  O   . GLU A 1 838  ? 23.031 54.860  -26.580 1.00 11.06 ? 838  GLU A O   1 
ATOM   6622 C  CB  . GLU A 1 838  ? 26.379 54.766  -27.058 1.00 11.84 ? 838  GLU A CB  1 
ATOM   6623 C  CG  . GLU A 1 838  ? 26.137 53.616  -26.057 1.00 13.07 ? 838  GLU A CG  1 
ATOM   6624 C  CD  . GLU A 1 838  ? 27.264 52.663  -25.978 1.00 13.93 ? 838  GLU A CD  1 
ATOM   6625 O  OE1 . GLU A 1 838  ? 28.300 52.877  -26.611 1.00 17.08 ? 838  GLU A OE1 1 
ATOM   6626 O  OE2 . GLU A 1 838  ? 27.134 51.628  -25.293 1.00 17.08 ? 838  GLU A OE2 1 
ATOM   6627 N  N   . ASP A 1 839  ? 23.784 54.752  -28.692 1.00 13.23 ? 839  ASP A N   1 
ATOM   6628 C  CA  . ASP A 1 839  ? 22.686 53.901  -29.088 1.00 12.96 ? 839  ASP A CA  1 
ATOM   6629 C  C   . ASP A 1 839  ? 23.387 52.843  -29.920 1.00 15.08 ? 839  ASP A C   1 
ATOM   6630 O  O   . ASP A 1 839  ? 24.578 52.645  -29.793 1.00 17.66 ? 839  ASP A O   1 
ATOM   6631 C  CB  . ASP A 1 839  ? 21.565 54.641  -29.862 1.00 13.72 ? 839  ASP A CB  1 
ATOM   6632 C  CG  . ASP A 1 839  ? 22.049 55.371  -31.129 1.00 14.15 ? 839  ASP A CG  1 
ATOM   6633 O  OD1 . ASP A 1 839  ? 23.076 54.983  -31.736 1.00 15.84 ? 839  ASP A OD1 1 
ATOM   6634 O  OD2 . ASP A 1 839  ? 21.346 56.357  -31.493 1.00 16.25 ? 839  ASP A OD2 1 
ATOM   6635 N  N   . ALA A 1 840  ? 22.672 52.121  -30.772 1.00 16.26 ? 840  ALA A N   1 
ATOM   6636 C  CA  . ALA A 1 840  ? 23.333 51.069  -31.516 1.00 14.30 ? 840  ALA A CA  1 
ATOM   6637 C  C   . ALA A 1 840  ? 24.406 51.540  -32.466 1.00 15.22 ? 840  ALA A C   1 
ATOM   6638 O  O   . ALA A 1 840  ? 25.378 50.853  -32.679 1.00 17.11 ? 840  ALA A O   1 
ATOM   6639 C  CB  . ALA A 1 840  ? 22.278 50.233  -32.275 1.00 17.50 ? 840  ALA A CB  1 
ATOM   6640 N  N   . ASN A 1 841  ? 24.300 52.762  -32.968 1.00 15.01 ? 841  ASN A N   1 
ATOM   6641 C  CA  . ASN A 1 841  ? 25.257 53.203  -33.978 1.00 15.19 ? 841  ASN A CA  1 
ATOM   6642 C  C   . ASN A 1 841  ? 26.175 54.344  -33.629 1.00 16.04 ? 841  ASN A C   1 
ATOM   6643 O  O   . ASN A 1 841  ? 27.278 54.447  -34.190 1.00 14.58 ? 841  ASN A O   1 
ATOM   6644 C  CB  . ASN A 1 841  ? 24.516 53.600  -35.275 1.00 16.35 ? 841  ASN A CB  1 
ATOM   6645 C  CG  . ASN A 1 841  ? 23.710 52.452  -35.862 1.00 17.90 ? 841  ASN A CG  1 
ATOM   6646 O  OD1 . ASN A 1 841  ? 24.238 51.366  -36.106 1.00 16.84 ? 841  ASN A OD1 1 
ATOM   6647 N  ND2 . ASN A 1 841  ? 22.433 52.694  -36.101 1.00 20.48 ? 841  ASN A ND2 1 
ATOM   6648 N  N   . THR A 1 842  ? 25.750 55.163  -32.671 1.00 15.22 ? 842  THR A N   1 
ATOM   6649 C  CA  . THR A 1 842  ? 26.479 56.386  -32.387 1.00 15.07 ? 842  THR A CA  1 
ATOM   6650 C  C   . THR A 1 842  ? 26.767 56.617  -30.909 1.00 14.02 ? 842  THR A C   1 
ATOM   6651 O  O   . THR A 1 842  ? 25.914 56.296  -30.064 1.00 14.23 ? 842  THR A O   1 
ATOM   6652 C  CB  . THR A 1 842  ? 25.662 57.587  -32.885 1.00 14.75 ? 842  THR A CB  1 
ATOM   6653 O  OG1 . THR A 1 842  ? 25.196 57.337  -34.246 1.00 15.83 ? 842  THR A OG1 1 
ATOM   6654 C  CG2 . THR A 1 842  ? 26.500 58.862  -32.828 1.00 13.80 ? 842  THR A CG2 1 
ATOM   6655 N  N   . ARG A 1 843  ? 27.938 57.170  -30.594 1.00 13.42 ? 843  ARG A N   1 
ATOM   6656 C  CA  . ARG A 1 843  ? 28.278 57.473  -29.213 1.00 12.83 ? 843  ARG A CA  1 
ATOM   6657 C  C   . ARG A 1 843  ? 28.850 58.884  -29.117 1.00 12.55 ? 843  ARG A C   1 
ATOM   6658 O  O   . ARG A 1 843  ? 29.586 59.376  -30.032 1.00 12.95 ? 843  ARG A O   1 
ATOM   6659 C  CB  . ARG A 1 843  ? 29.330 56.480  -28.703 1.00 12.61 ? 843  ARG A CB  1 
ATOM   6660 C  CG  . ARG A 1 843  ? 29.816 56.783  -27.242 1.00 12.84 ? 843  ARG A CG  1 
ATOM   6661 C  CD  . ARG A 1 843  ? 30.996 55.877  -26.825 1.00 10.58 ? 843  ARG A CD  1 
ATOM   6662 N  NE  . ARG A 1 843  ? 30.565 54.527  -26.499 1.00 12.26 ? 843  ARG A NE  1 
ATOM   6663 C  CZ  . ARG A 1 843  ? 31.356 53.626  -25.892 1.00 11.04 ? 843  ARG A CZ  1 
ATOM   6664 N  NH1 . ARG A 1 843  ? 32.612 53.951  -25.568 1.00 12.47 ? 843  ARG A NH1 1 
ATOM   6665 N  NH2 . ARG A 1 843  ? 30.902 52.421  -25.633 1.00 13.02 ? 843  ARG A NH2 1 
ATOM   6666 N  N   . LEU A 1 844  ? 28.504 59.571  -28.023 1.00 11.81 ? 844  LEU A N   1 
ATOM   6667 C  CA  . LEU A 1 844  ? 29.062 60.892  -27.798 1.00 10.61 ? 844  LEU A CA  1 
ATOM   6668 C  C   . LEU A 1 844  ? 29.706 60.789  -26.410 1.00 10.42 ? 844  LEU A C   1 
ATOM   6669 O  O   . LEU A 1 844  ? 29.055 60.471  -25.423 1.00 11.57 ? 844  LEU A O   1 
ATOM   6670 C  CB  . LEU A 1 844  ? 27.996 61.978  -27.787 1.00 11.49 ? 844  LEU A CB  1 
ATOM   6671 C  CG  . LEU A 1 844  ? 28.589 63.405  -27.625 1.00 9.02  ? 844  LEU A CG  1 
ATOM   6672 C  CD1 . LEU A 1 844  ? 29.464 63.734  -28.891 1.00 12.60 ? 844  LEU A CD1 1 
ATOM   6673 C  CD2 . LEU A 1 844  ? 27.506 64.433  -27.354 1.00 12.68 ? 844  LEU A CD2 1 
ATOM   6674 N  N   . THR A 1 845  ? 30.995 61.082  -26.354 1.00 10.55 ? 845  THR A N   1 
ATOM   6675 C  CA  . THR A 1 845  ? 31.725 61.007  -25.092 1.00 10.74 ? 845  THR A CA  1 
ATOM   6676 C  C   . THR A 1 845  ? 32.302 62.379  -24.776 1.00 9.91  ? 845  THR A C   1 
ATOM   6677 O  O   . THR A 1 845  ? 32.911 63.003  -25.652 1.00 10.46 ? 845  THR A O   1 
ATOM   6678 C  CB  . THR A 1 845  ? 32.924 60.024  -25.182 1.00 10.80 ? 845  THR A CB  1 
ATOM   6679 O  OG1 . THR A 1 845  ? 32.512 58.713  -25.594 1.00 11.73 ? 845  THR A OG1 1 
ATOM   6680 C  CG2 . THR A 1 845  ? 33.621 59.943  -23.797 1.00 9.12  ? 845  THR A CG2 1 
ATOM   6681 N  N   . LEU A 1 846  ? 32.124 62.829  -23.548 1.00 9.09  ? 846  LEU A N   1 
ATOM   6682 C  CA  . LEU A 1 846  ? 32.681 64.113  -23.057 1.00 10.36 ? 846  LEU A CA  1 
ATOM   6683 C  C   . LEU A 1 846  ? 33.731 63.778  -22.011 1.00 10.38 ? 846  LEU A C   1 
ATOM   6684 O  O   . LEU A 1 846  ? 33.376 63.174  -20.997 1.00 9.81  ? 846  LEU A O   1 
ATOM   6685 C  CB  . LEU A 1 846  ? 31.603 64.978  -22.434 1.00 10.70 ? 846  LEU A CB  1 
ATOM   6686 C  CG  . LEU A 1 846  ? 32.002 66.345  -21.888 1.00 10.92 ? 846  LEU A CG  1 
ATOM   6687 C  CD1 . LEU A 1 846  ? 32.403 67.275  -23.053 1.00 12.75 ? 846  LEU A CD1 1 
ATOM   6688 C  CD2 . LEU A 1 846  ? 30.889 66.957  -21.115 1.00 13.03 ? 846  LEU A CD2 1 
ATOM   6689 N  N   . LEU A 1 847  ? 35.000 64.103  -22.277 1.00 9.50  ? 847  LEU A N   1 
ATOM   6690 C  CA  . LEU A 1 847  ? 36.110 63.824  -21.300 1.00 9.01  ? 847  LEU A CA  1 
ATOM   6691 C  C   . LEU A 1 847  ? 36.358 65.150  -20.591 1.00 9.20  ? 847  LEU A C   1 
ATOM   6692 O  O   . LEU A 1 847  ? 36.236 66.208  -21.197 1.00 8.58  ? 847  LEU A O   1 
ATOM   6693 C  CB  . LEU A 1 847  ? 37.382 63.348  -22.027 1.00 9.20  ? 847  LEU A CB  1 
ATOM   6694 C  CG  . LEU A 1 847  ? 37.388 62.027  -22.788 1.00 8.86  ? 847  LEU A CG  1 
ATOM   6695 C  CD1 . LEU A 1 847  ? 36.731 60.953  -21.944 1.00 9.53  ? 847  LEU A CD1 1 
ATOM   6696 C  CD2 . LEU A 1 847  ? 36.723 62.145  -24.178 1.00 9.35  ? 847  LEU A CD2 1 
ATOM   6697 N  N   . THR A 1 848  ? 36.731 65.120  -19.299 1.00 8.05  ? 848  THR A N   1 
ATOM   6698 C  CA  . THR A 1 848  ? 36.941 66.330  -18.467 1.00 9.18  ? 848  THR A CA  1 
ATOM   6699 C  C   . THR A 1 848  ? 38.351 66.403  -17.882 1.00 10.72 ? 848  THR A C   1 
ATOM   6700 O  O   . THR A 1 848  ? 39.034 65.336  -17.687 1.00 10.43 ? 848  THR A O   1 
ATOM   6701 C  CB  . THR A 1 848  ? 35.947 66.407  -17.253 1.00 11.06 ? 848  THR A CB  1 
ATOM   6702 O  OG1 . THR A 1 848  ? 36.365 65.411  -16.271 1.00 12.38 ? 848  THR A OG1 1 
ATOM   6703 C  CG2 . THR A 1 848  ? 34.517 66.136  -17.688 1.00 10.43 ? 848  THR A CG2 1 
ATOM   6704 N  N   . GLY A 1 849  ? 38.793 67.624  -17.622 1.00 10.28 ? 849  GLY A N   1 
ATOM   6705 C  CA  . GLY A 1 849  ? 40.105 67.834  -17.054 1.00 10.23 ? 849  GLY A CA  1 
ATOM   6706 C  C   . GLY A 1 849  ? 39.936 68.201  -15.588 1.00 6.98  ? 849  GLY A C   1 
ATOM   6707 O  O   . GLY A 1 849  ? 40.850 68.616  -14.896 1.00 7.17  ? 849  GLY A O   1 
ATOM   6708 N  N   . GLN A 1 850  ? 38.740 67.942  -15.063 1.00 7.85  ? 850  GLN A N   1 
ATOM   6709 C  CA  . GLN A 1 850  ? 38.377 68.258  -13.675 1.00 6.89  ? 850  GLN A CA  1 
ATOM   6710 C  C   . GLN A 1 850  ? 37.085 67.519  -13.281 1.00 7.18  ? 850  GLN A C   1 
ATOM   6711 O  O   . GLN A 1 850  ? 36.236 67.298  -14.121 1.00 6.85  ? 850  GLN A O   1 
ATOM   6712 C  CB  . GLN A 1 850  ? 38.103 69.769  -13.502 1.00 8.19  ? 850  GLN A CB  1 
ATOM   6713 C  CG  . GLN A 1 850  ? 36.981 70.370  -14.422 1.00 7.57  ? 850  GLN A CG  1 
ATOM   6714 C  CD  . GLN A 1 850  ? 37.361 70.466  -15.885 1.00 10.10 ? 850  GLN A CD  1 
ATOM   6715 O  OE1 . GLN A 1 850  ? 38.470 70.902  -16.227 1.00 9.01  ? 850  GLN A OE1 1 
ATOM   6716 N  NE2 . GLN A 1 850  ? 36.421 70.113  -16.774 1.00 9.34  ? 850  GLN A NE2 1 
ATOM   6717 N  N   . PRO A 1 851  ? 36.962 67.131  -12.018 1.00 6.57  ? 851  PRO A N   1 
ATOM   6718 C  CA  . PRO A 1 851  ? 35.704 66.419  -11.624 1.00 6.01  ? 851  PRO A CA  1 
ATOM   6719 C  C   . PRO A 1 851  ? 34.570 67.414  -11.425 1.00 7.26  ? 851  PRO A C   1 
ATOM   6720 O  O   . PRO A 1 851  ? 34.762 68.462  -10.799 1.00 7.32  ? 851  PRO A O   1 
ATOM   6721 C  CB  . PRO A 1 851  ? 36.123 65.693  -10.312 1.00 7.77  ? 851  PRO A CB  1 
ATOM   6722 C  CG  . PRO A 1 851  ? 37.185 66.689  -9.679  1.00 6.08  ? 851  PRO A CG  1 
ATOM   6723 C  CD  . PRO A 1 851  ? 37.977 67.183  -10.944 1.00 6.45  ? 851  PRO A CD  1 
ATOM   6724 N  N   . LEU A 1 852  ? 33.412 67.071  -12.002 1.00 6.95  ? 852  LEU A N   1 
ATOM   6725 C  CA  . LEU A 1 852  ? 32.216 67.927  -11.864 1.00 9.09  ? 852  LEU A CA  1 
ATOM   6726 C  C   . LEU A 1 852  ? 31.009 66.974  -11.786 1.00 8.80  ? 852  LEU A C   1 
ATOM   6727 O  O   . LEU A 1 852  ? 31.137 65.767  -12.027 1.00 11.79 ? 852  LEU A O   1 
ATOM   6728 C  CB  . LEU A 1 852  ? 32.108 68.839  -13.119 1.00 8.80  ? 852  LEU A CB  1 
ATOM   6729 C  CG  . LEU A 1 852  ? 33.254 69.884  -13.287 1.00 6.57  ? 852  LEU A CG  1 
ATOM   6730 C  CD1 . LEU A 1 852  ? 33.221 70.523  -14.719 1.00 10.43 ? 852  LEU A CD1 1 
ATOM   6731 C  CD2 . LEU A 1 852  ? 33.126 70.899  -12.172 1.00 7.66  ? 852  LEU A CD2 1 
ATOM   6732 N  N   . GLY A 1 853  ? 29.827 67.506  -11.455 1.00 8.07  ? 853  GLY A N   1 
ATOM   6733 C  CA  . GLY A 1 853  ? 28.638 66.683  -11.400 1.00 8.53  ? 853  GLY A CA  1 
ATOM   6734 C  C   . GLY A 1 853  ? 27.882 66.696  -12.705 1.00 8.18  ? 853  GLY A C   1 
ATOM   6735 O  O   . GLY A 1 853  ? 27.915 67.664  -13.439 1.00 8.24  ? 853  GLY A O   1 
ATOM   6736 N  N   . GLY A 1 854  ? 27.183 65.627  -13.034 1.00 7.57  ? 854  GLY A N   1 
ATOM   6737 C  CA  . GLY A 1 854  ? 26.492 65.620  -14.328 1.00 8.45  ? 854  GLY A CA  1 
ATOM   6738 C  C   . GLY A 1 854  ? 25.464 64.508  -14.442 1.00 9.49  ? 854  GLY A C   1 
ATOM   6739 O  O   . GLY A 1 854  ? 25.351 63.635  -13.545 1.00 10.72 ? 854  GLY A O   1 
ATOM   6740 N  N   . SER A 1 855  ? 24.756 64.491  -15.567 1.00 11.59 ? 855  SER A N   1 
ATOM   6741 C  CA  . SER A 1 855  ? 23.745 63.470  -15.778 1.00 10.70 ? 855  SER A CA  1 
ATOM   6742 C  C   . SER A 1 855  ? 23.336 63.421  -17.245 1.00 12.39 ? 855  SER A C   1 
ATOM   6743 O  O   . SER A 1 855  ? 23.973 64.048  -18.117 1.00 11.62 ? 855  SER A O   1 
ATOM   6744 C  CB  . SER A 1 855  ? 22.541 63.813  -14.914 1.00 12.54 ? 855  SER A CB  1 
ATOM   6745 O  OG  . SER A 1 855  ? 21.505 62.844  -15.089 1.00 9.27  ? 855  SER A OG  1 
ATOM   6746 N  N   . SER A 1 856  ? 22.296 62.640  -17.506 1.00 11.95 ? 856  SER A N   1 
ATOM   6747 C  CA  . SER A 1 856  ? 21.662 62.563  -18.834 1.00 11.52 ? 856  SER A CA  1 
ATOM   6748 C  C   . SER A 1 856  ? 20.201 62.569  -18.401 1.00 9.84  ? 856  SER A C   1 
ATOM   6749 O  O   . SER A 1 856  ? 19.652 61.516  -18.021 1.00 10.95 ? 856  SER A O   1 
ATOM   6750 C  CB  . SER A 1 856  ? 21.949 61.253  -19.559 1.00 10.96 ? 856  SER A CB  1 
ATOM   6751 O  OG  . SER A 1 856  ? 21.174 61.239  -20.777 1.00 10.31 ? 856  SER A OG  1 
ATOM   6752 N  N   . LEU A 1 857  ? 19.548 63.721  -18.428 1.00 12.03 ? 857  LEU A N   1 
ATOM   6753 C  CA  . LEU A 1 857  ? 18.182 63.767  -17.895 1.00 12.24 ? 857  LEU A CA  1 
ATOM   6754 C  C   . LEU A 1 857  ? 17.068 63.474  -18.884 1.00 12.45 ? 857  LEU A C   1 
ATOM   6755 O  O   . LEU A 1 857  ? 15.909 63.413  -18.498 1.00 13.27 ? 857  LEU A O   1 
ATOM   6756 C  CB  . LEU A 1 857  ? 17.955 65.109  -17.187 1.00 11.38 ? 857  LEU A CB  1 
ATOM   6757 C  CG  . LEU A 1 857  ? 18.802 65.436  -15.946 1.00 13.06 ? 857  LEU A CG  1 
ATOM   6758 C  CD1 . LEU A 1 857  ? 18.553 66.872  -15.613 1.00 13.48 ? 857  LEU A CD1 1 
ATOM   6759 C  CD2 . LEU A 1 857  ? 18.450 64.547  -14.741 1.00 12.30 ? 857  LEU A CD2 1 
ATOM   6760 N  N   . ALA A 1 858  ? 17.450 63.195  -20.118 1.00 12.34 ? 858  ALA A N   1 
ATOM   6761 C  CA  . ALA A 1 858  ? 16.531 62.833  -21.220 1.00 13.49 ? 858  ALA A CA  1 
ATOM   6762 C  C   . ALA A 1 858  ? 17.361 62.146  -22.271 1.00 13.23 ? 858  ALA A C   1 
ATOM   6763 O  O   . ALA A 1 858  ? 18.572 62.426  -22.438 1.00 13.29 ? 858  ALA A O   1 
ATOM   6764 C  CB  . ALA A 1 858  ? 15.868 64.098  -21.889 1.00 13.21 ? 858  ALA A CB  1 
ATOM   6765 N  N   . SER A 1 859  ? 16.749 61.251  -23.026 1.00 14.39 ? 859  SER A N   1 
ATOM   6766 C  CA  . SER A 1 859  ? 17.407 60.552  -24.099 1.00 13.30 ? 859  SER A CA  1 
ATOM   6767 C  C   . SER A 1 859  ? 18.155 61.532  -25.025 1.00 13.42 ? 859  SER A C   1 
ATOM   6768 O  O   . SER A 1 859  ? 17.618 62.612  -25.313 1.00 14.56 ? 859  SER A O   1 
ATOM   6769 C  CB  . SER A 1 859  ? 16.327 59.808  -24.912 1.00 13.41 ? 859  SER A CB  1 
ATOM   6770 O  OG  . SER A 1 859  ? 16.883 58.998  -25.921 1.00 16.56 ? 859  SER A OG  1 
ATOM   6771 N  N   . GLY A 1 860  ? 19.390 61.194  -25.389 1.00 12.30 ? 860  GLY A N   1 
ATOM   6772 C  CA  . GLY A 1 860  ? 20.195 62.022  -26.272 1.00 12.18 ? 860  GLY A CA  1 
ATOM   6773 C  C   . GLY A 1 860  ? 20.913 63.215  -25.631 1.00 12.52 ? 860  GLY A C   1 
ATOM   6774 O  O   . GLY A 1 860  ? 21.652 63.948  -26.326 1.00 12.36 ? 860  GLY A O   1 
ATOM   6775 N  N   . GLU A 1 861  ? 20.727 63.412  -24.326 1.00 10.75 ? 861  GLU A N   1 
ATOM   6776 C  CA  . GLU A 1 861  ? 21.383 64.509  -23.598 1.00 11.43 ? 861  GLU A CA  1 
ATOM   6777 C  C   . GLU A 1 861  ? 22.548 64.125  -22.663 1.00 11.63 ? 861  GLU A C   1 
ATOM   6778 O  O   . GLU A 1 861  ? 22.640 62.973  -22.122 1.00 11.90 ? 861  GLU A O   1 
ATOM   6779 C  CB  . GLU A 1 861  ? 20.409 65.280  -22.717 1.00 13.84 ? 861  GLU A CB  1 
ATOM   6780 C  CG  . GLU A 1 861  ? 19.241 65.865  -23.490 1.00 15.49 ? 861  GLU A CG  1 
ATOM   6781 C  CD  . GLU A 1 861  ? 18.361 66.713  -22.624 1.00 18.40 ? 861  GLU A CD  1 
ATOM   6782 O  OE1 . GLU A 1 861  ? 18.568 66.751  -21.391 1.00 16.64 ? 861  GLU A OE1 1 
ATOM   6783 O  OE2 . GLU A 1 861  ? 17.402 67.363  -23.142 1.00 17.90 ? 861  GLU A OE2 1 
ATOM   6784 N  N   . LEU A 1 862  ? 23.453 65.080  -22.537 1.00 13.37 ? 862  LEU A N   1 
ATOM   6785 C  CA  . LEU A 1 862  ? 24.536 64.946  -21.545 1.00 13.13 ? 862  LEU A CA  1 
ATOM   6786 C  C   . LEU A 1 862  ? 24.598 66.318  -20.915 1.00 10.42 ? 862  LEU A C   1 
ATOM   6787 O  O   . LEU A 1 862  ? 24.392 67.341  -21.614 1.00 11.48 ? 862  LEU A O   1 
ATOM   6788 C  CB  . LEU A 1 862  ? 25.888 64.717  -22.219 1.00 13.35 ? 862  LEU A CB  1 
ATOM   6789 C  CG  . LEU A 1 862  ? 26.182 63.331  -22.749 1.00 15.06 ? 862  LEU A CG  1 
ATOM   6790 C  CD1 . LEU A 1 862  ? 27.539 63.331  -23.487 1.00 17.57 ? 862  LEU A CD1 1 
ATOM   6791 C  CD2 . LEU A 1 862  ? 26.235 62.325  -21.582 1.00 15.15 ? 862  LEU A CD2 1 
ATOM   6792 N  N   . GLU A 1 863  ? 24.827 66.414  -19.601 1.00 9.75  ? 863  GLU A N   1 
ATOM   6793 C  CA  . GLU A 1 863  ? 25.001 67.728  -18.997 1.00 10.30 ? 863  GLU A CA  1 
ATOM   6794 C  C   . GLU A 1 863  ? 25.958 67.649  -17.835 1.00 11.48 ? 863  GLU A C   1 
ATOM   6795 O  O   . GLU A 1 863  ? 26.123 66.555  -17.254 1.00 9.99  ? 863  GLU A O   1 
ATOM   6796 C  CB  . GLU A 1 863  ? 23.696 68.340  -18.555 1.00 10.08 ? 863  GLU A CB  1 
ATOM   6797 C  CG  . GLU A 1 863  ? 23.121 67.800  -17.268 1.00 10.68 ? 863  GLU A CG  1 
ATOM   6798 C  CD  . GLU A 1 863  ? 21.797 68.487  -16.947 1.00 13.07 ? 863  GLU A CD  1 
ATOM   6799 O  OE1 . GLU A 1 863  ? 20.906 68.468  -17.873 1.00 13.76 ? 863  GLU A OE1 1 
ATOM   6800 O  OE2 . GLU A 1 863  ? 21.677 69.035  -15.821 1.00 11.31 ? 863  GLU A OE2 1 
ATOM   6801 N  N   . ILE A 1 864  ? 26.665 68.749  -17.596 1.00 9.41  ? 864  ILE A N   1 
ATOM   6802 C  CA  . ILE A 1 864  ? 27.708 68.775  -16.549 1.00 10.92 ? 864  ILE A CA  1 
ATOM   6803 C  C   . ILE A 1 864  ? 27.739 70.161  -16.006 1.00 10.06 ? 864  ILE A C   1 
ATOM   6804 O  O   . ILE A 1 864  ? 27.816 71.188  -16.740 1.00 10.27 ? 864  ILE A O   1 
ATOM   6805 C  CB  . ILE A 1 864  ? 29.080 68.368  -17.172 1.00 10.50 ? 864  ILE A CB  1 
ATOM   6806 C  CG1 . ILE A 1 864  ? 30.189 68.352  -16.121 1.00 12.05 ? 864  ILE A CG1 1 
ATOM   6807 C  CG2 . ILE A 1 864  ? 29.467 69.277  -18.319 1.00 14.00 ? 864  ILE A CG2 1 
ATOM   6808 C  CD1 . ILE A 1 864  ? 31.292 67.348  -16.640 1.00 12.79 ? 864  ILE A CD1 1 
ATOM   6809 N  N   . MET A 1 865  ? 27.682 70.211  -14.702 1.00 8.56  ? 865  MET A N   1 
ATOM   6810 C  CA  . MET A 1 865  ? 27.667 71.465  -13.974 1.00 8.68  ? 865  MET A CA  1 
ATOM   6811 C  C   . MET A 1 865  ? 29.028 72.143  -14.005 1.00 8.61  ? 865  MET A C   1 
ATOM   6812 O  O   . MET A 1 865  ? 30.075 71.492  -13.890 1.00 8.83  ? 865  MET A O   1 
ATOM   6813 C  CB  . MET A 1 865  ? 27.221 71.245  -12.538 1.00 8.93  ? 865  MET A CB  1 
ATOM   6814 C  CG  . MET A 1 865  ? 26.597 72.439  -11.860 1.00 7.83  ? 865  MET A CG  1 
ATOM   6815 S  SD  . MET A 1 865  ? 24.970 72.851  -12.558 1.00 12.02 ? 865  MET A SD  1 
ATOM   6816 C  CE  . MET A 1 865  ? 23.930 71.617  -11.572 1.00 10.41 ? 865  MET A CE  1 
ATOM   6817 N  N   . GLN A 1 866  ? 29.018 73.455  -14.167 1.00 8.96  ? 866  GLN A N   1 
ATOM   6818 C  CA  . GLN A 1 866  ? 30.241 74.285  -14.297 1.00 8.43  ? 866  GLN A CA  1 
ATOM   6819 C  C   . GLN A 1 866  ? 30.643 74.936  -12.975 1.00 8.07  ? 866  GLN A C   1 
ATOM   6820 O  O   . GLN A 1 866  ? 31.818 74.903  -12.580 1.00 10.61 ? 866  GLN A O   1 
ATOM   6821 C  CB  . GLN A 1 866  ? 29.992 75.331  -15.382 1.00 9.46  ? 866  GLN A CB  1 
ATOM   6822 C  CG  . GLN A 1 866  ? 29.652 74.702  -16.736 1.00 10.22 ? 866  GLN A CG  1 
ATOM   6823 C  CD  . GLN A 1 866  ? 30.716 73.726  -17.220 1.00 9.46  ? 866  GLN A CD  1 
ATOM   6824 O  OE1 . GLN A 1 866  ? 31.824 74.149  -17.595 1.00 10.01 ? 866  GLN A OE1 1 
ATOM   6825 N  NE2 . GLN A 1 866  ? 30.410 72.442  -17.218 1.00 10.31 ? 866  GLN A NE2 1 
ATOM   6826 N  N   . ASP A 1 867  ? 29.681 75.569  -12.257 1.00 9.03  ? 867  ASP A N   1 
ATOM   6827 C  CA  . ASP A 1 867  ? 29.895 76.189  -10.966 1.00 9.11  ? 867  ASP A CA  1 
ATOM   6828 C  C   . ASP A 1 867  ? 28.541 76.438  -10.333 1.00 9.86  ? 867  ASP A C   1 
ATOM   6829 O  O   . ASP A 1 867  ? 27.494 76.316  -11.012 1.00 9.71  ? 867  ASP A O   1 
ATOM   6830 C  CB  . ASP A 1 867  ? 30.741 77.530  -11.070 1.00 9.14  ? 867  ASP A CB  1 
ATOM   6831 C  CG  . ASP A 1 867  ? 31.387 77.944  -9.722  1.00 13.08 ? 867  ASP A CG  1 
ATOM   6832 O  OD1 . ASP A 1 867  ? 31.259 77.227  -8.709  1.00 11.03 ? 867  ASP A OD1 1 
ATOM   6833 O  OD2 . ASP A 1 867  ? 32.094 78.978  -9.674  1.00 13.55 ? 867  ASP A OD2 1 
ATOM   6834 N  N   . ARG A 1 868  ? 28.549 76.673  -9.024  1.00 7.99  ? 868  ARG A N   1 
ATOM   6835 C  CA  . ARG A 1 868  ? 27.329 76.883  -8.276  1.00 10.43 ? 868  ARG A CA  1 
ATOM   6836 C  C   . ARG A 1 868  ? 27.640 77.894  -7.196  1.00 10.97 ? 868  ARG A C   1 
ATOM   6837 O  O   . ARG A 1 868  ? 28.726 77.874  -6.581  1.00 12.86 ? 868  ARG A O   1 
ATOM   6838 C  CB  . ARG A 1 868  ? 26.857 75.526  -7.686  1.00 9.76  ? 868  ARG A CB  1 
ATOM   6839 C  CG  . ARG A 1 868  ? 27.861 74.776  -6.762  1.00 11.64 ? 868  ARG A CG  1 
ATOM   6840 C  CD  . ARG A 1 868  ? 27.590 73.274  -6.863  1.00 8.63  ? 868  ARG A CD  1 
ATOM   6841 N  NE  . ARG A 1 868  ? 26.229 72.990  -6.436  1.00 9.37  ? 868  ARG A NE  1 
ATOM   6842 C  CZ  . ARG A 1 868  ? 25.865 72.672  -5.183  1.00 7.47  ? 868  ARG A CZ  1 
ATOM   6843 N  NH1 . ARG A 1 868  ? 26.727 72.530  -4.189  1.00 9.12  ? 868  ARG A NH1 1 
ATOM   6844 N  NH2 . ARG A 1 868  ? 24.545 72.557  -4.888  1.00 10.47 ? 868  ARG A NH2 1 
ATOM   6845 N  N   . ARG A 1 869  ? 26.713 78.856  -7.003  1.00 12.71 ? 869  ARG A N   1 
ATOM   6846 C  CA  . ARG A 1 869  ? 26.911 79.883  -5.961  1.00 13.34 ? 869  ARG A CA  1 
ATOM   6847 C  C   . ARG A 1 869  ? 25.646 79.870  -5.109  1.00 14.45 ? 869  ARG A C   1 
ATOM   6848 O  O   . ARG A 1 869  ? 24.573 80.069  -5.667  1.00 13.17 ? 869  ARG A O   1 
ATOM   6849 C  CB  . ARG A 1 869  ? 27.153 81.232  -6.627  1.00 14.85 ? 869  ARG A CB  1 
ATOM   6850 C  CG  . ARG A 1 869  ? 27.371 82.351  -5.622  1.00 15.74 ? 869  ARG A CG  1 
ATOM   6851 C  CD  . ARG A 1 869  ? 27.630 83.670  -6.395  1.00 18.10 ? 869  ARG A CD  1 
ATOM   6852 N  NE  . ARG A 1 869  ? 27.779 84.831  -5.497  1.00 18.62 ? 869  ARG A NE  1 
ATOM   6853 C  CZ  . ARG A 1 869  ? 28.924 85.181  -4.918  1.00 20.67 ? 869  ARG A CZ  1 
ATOM   6854 N  NH1 . ARG A 1 869  ? 30.034 84.465  -5.156  1.00 18.83 ? 869  ARG A NH1 1 
ATOM   6855 N  NH2 . ARG A 1 869  ? 28.973 86.214  -4.065  1.00 21.58 ? 869  ARG A NH2 1 
ATOM   6856 N  N   . LEU A 1 870  ? 25.789 79.619  -3.806  1.00 14.33 ? 870  LEU A N   1 
ATOM   6857 C  CA  . LEU A 1 870  ? 24.627 79.380  -2.935  1.00 15.77 ? 870  LEU A CA  1 
ATOM   6858 C  C   . LEU A 1 870  ? 24.646 80.247  -1.702  1.00 14.17 ? 870  LEU A C   1 
ATOM   6859 O  O   . LEU A 1 870  ? 25.592 80.199  -0.939  1.00 14.21 ? 870  LEU A O   1 
ATOM   6860 C  CB  . LEU A 1 870  ? 24.632 77.893  -2.529  1.00 16.45 ? 870  LEU A CB  1 
ATOM   6861 C  CG  . LEU A 1 870  ? 24.713 77.037  -3.812  1.00 20.29 ? 870  LEU A CG  1 
ATOM   6862 C  CD1 . LEU A 1 870  ? 25.241 75.683  -3.452  1.00 20.40 ? 870  LEU A CD1 1 
ATOM   6863 C  CD2 . LEU A 1 870  ? 23.385 76.931  -4.517  1.00 18.61 ? 870  LEU A CD2 1 
ATOM   6864 N  N   . ALA A 1 871  ? 23.572 81.021  -1.479  1.00 15.39 ? 871  ALA A N   1 
ATOM   6865 C  CA  . ALA A 1 871  ? 23.577 81.930  -0.323  1.00 16.76 ? 871  ALA A CA  1 
ATOM   6866 C  C   . ALA A 1 871  ? 23.198 81.315  1.018   1.00 18.08 ? 871  ALA A C   1 
ATOM   6867 O  O   . ALA A 1 871  ? 23.353 81.953  2.059   1.00 18.49 ? 871  ALA A O   1 
ATOM   6868 C  CB  . ALA A 1 871  ? 22.674 83.137  -0.599  1.00 17.53 ? 871  ALA A CB  1 
ATOM   6869 N  N   . SER A 1 872  ? 22.705 80.081  1.008   1.00 16.52 ? 872  SER A N   1 
ATOM   6870 C  CA  . SER A 1 872  ? 22.340 79.444  2.260   1.00 17.01 ? 872  SER A CA  1 
ATOM   6871 C  C   . SER A 1 872  ? 23.165 78.240  2.593   1.00 16.64 ? 872  SER A C   1 
ATOM   6872 O  O   . SER A 1 872  ? 23.788 77.624  1.715   1.00 17.03 ? 872  SER A O   1 
ATOM   6873 C  CB  . SER A 1 872  ? 20.886 78.981  2.250   1.00 18.00 ? 872  SER A CB  1 
ATOM   6874 O  OG  . SER A 1 872  ? 19.999 80.089  2.220   1.00 23.38 ? 872  SER A OG  1 
ATOM   6875 N  N   . ASP A 1 873  ? 23.098 77.893  3.867   1.00 16.55 ? 873  ASP A N   1 
ATOM   6876 C  CA  . ASP A 1 873  ? 23.771 76.714  4.438   1.00 17.74 ? 873  ASP A CA  1 
ATOM   6877 C  C   . ASP A 1 873  ? 22.776 75.582  4.261   1.00 16.98 ? 873  ASP A C   1 
ATOM   6878 O  O   . ASP A 1 873  ? 21.553 75.825  4.267   1.00 17.20 ? 873  ASP A O   1 
ATOM   6879 C  CB  . ASP A 1 873  ? 24.028 76.935  5.922   1.00 15.61 ? 873  ASP A CB  1 
ATOM   6880 C  CG  . ASP A 1 873  ? 24.534 75.696  6.616   1.00 17.82 ? 873  ASP A CG  1 
ATOM   6881 O  OD1 . ASP A 1 873  ? 25.624 75.199  6.239   1.00 19.12 ? 873  ASP A OD1 1 
ATOM   6882 O  OD2 . ASP A 1 873  ? 23.845 75.222  7.530   1.00 18.56 ? 873  ASP A OD2 1 
ATOM   6883 N  N   . ASP A 1 874  ? 23.291 74.352  4.083   1.00 15.85 ? 874  ASP A N   1 
ATOM   6884 C  CA  . ASP A 1 874  ? 22.413 73.183  3.876   1.00 14.21 ? 874  ASP A CA  1 
ATOM   6885 C  C   . ASP A 1 874  ? 22.276 72.257  5.089   1.00 14.57 ? 874  ASP A C   1 
ATOM   6886 O  O   . ASP A 1 874  ? 22.018 71.020  4.944   1.00 17.28 ? 874  ASP A O   1 
ATOM   6887 C  CB  . ASP A 1 874  ? 22.812 72.374  2.653   1.00 12.28 ? 874  ASP A CB  1 
ATOM   6888 C  CG  . ASP A 1 874  ? 24.319 72.028  2.590   1.00 13.27 ? 874  ASP A CG  1 
ATOM   6889 O  OD1 . ASP A 1 874  ? 25.117 72.366  3.505   1.00 15.68 ? 874  ASP A OD1 1 
ATOM   6890 O  OD2 . ASP A 1 874  ? 24.672 71.455  1.524   1.00 12.66 ? 874  ASP A OD2 1 
ATOM   6891 N  N   . GLU A 1 875  ? 22.519 72.825  6.276   1.00 14.66 ? 875  GLU A N   1 
ATOM   6892 C  CA  . GLU A 1 875  ? 22.294 72.156  7.553   1.00 16.35 ? 875  GLU A CA  1 
ATOM   6893 C  C   . GLU A 1 875  ? 23.018 70.863  7.874   1.00 16.87 ? 875  GLU A C   1 
ATOM   6894 O  O   . GLU A 1 875  ? 22.476 69.981  8.546   1.00 16.04 ? 875  GLU A O   1 
ATOM   6895 C  CB  . GLU A 1 875  ? 20.804 71.900  7.742   1.00 21.42 ? 875  GLU A CB  1 
ATOM   6896 C  CG  . GLU A 1 875  ? 19.980 73.083  7.355   1.00 26.83 ? 875  GLU A CG  1 
ATOM   6897 C  CD  . GLU A 1 875  ? 18.888 73.353  8.336   1.00 31.70 ? 875  GLU A CD  1 
ATOM   6898 O  OE1 . GLU A 1 875  ? 19.164 73.348  9.568   1.00 34.80 ? 875  GLU A OE1 1 
ATOM   6899 O  OE2 . GLU A 1 875  ? 17.753 73.598  7.875   1.00 34.35 ? 875  GLU A OE2 1 
ATOM   6900 N  N   . ARG A 1 876  ? 24.255 70.745  7.419   1.00 15.23 ? 876  ARG A N   1 
ATOM   6901 C  CA  . ARG A 1 876  ? 25.027 69.577  7.697   1.00 16.81 ? 876  ARG A CA  1 
ATOM   6902 C  C   . ARG A 1 876  ? 26.179 69.953  8.598   1.00 17.43 ? 876  ARG A C   1 
ATOM   6903 O  O   . ARG A 1 876  ? 27.061 69.125  8.832   1.00 18.15 ? 876  ARG A O   1 
ATOM   6904 C  CB  . ARG A 1 876  ? 25.515 68.938  6.379   1.00 14.27 ? 876  ARG A CB  1 
ATOM   6905 C  CG  . ARG A 1 876  ? 24.365 68.337  5.463   1.00 13.42 ? 876  ARG A CG  1 
ATOM   6906 C  CD  . ARG A 1 876  ? 23.479 67.328  6.268   1.00 14.48 ? 876  ARG A CD  1 
ATOM   6907 N  NE  . ARG A 1 876  ? 22.452 66.621  5.491   1.00 16.03 ? 876  ARG A NE  1 
ATOM   6908 C  CZ  . ARG A 1 876  ? 21.277 67.136  5.121   1.00 15.28 ? 876  ARG A CZ  1 
ATOM   6909 N  NH1 . ARG A 1 876  ? 20.980 68.390  5.392   1.00 12.91 ? 876  ARG A NH1 1 
ATOM   6910 N  NH2 . ARG A 1 876  ? 20.315 66.335  4.657   1.00 10.68 ? 876  ARG A NH2 1 
ATOM   6911 N  N   . GLY A 1 877  ? 26.225 71.211  9.052   1.00 17.20 ? 877  GLY A N   1 
ATOM   6912 C  CA  . GLY A 1 877  ? 27.277 71.621  9.966   1.00 16.99 ? 877  GLY A CA  1 
ATOM   6913 C  C   . GLY A 1 877  ? 28.341 72.575  9.442   1.00 14.81 ? 877  GLY A C   1 
ATOM   6914 O  O   . GLY A 1 877  ? 29.116 73.133  10.270  1.00 15.74 ? 877  GLY A O   1 
ATOM   6915 N  N   . LEU A 1 878  ? 28.363 72.804  8.115   1.00 13.16 ? 878  LEU A N   1 
ATOM   6916 C  CA  . LEU A 1 878  ? 29.353 73.692  7.501   1.00 13.72 ? 878  LEU A CA  1 
ATOM   6917 C  C   . LEU A 1 878  ? 29.085 75.130  7.936   1.00 14.96 ? 878  LEU A C   1 
ATOM   6918 O  O   . LEU A 1 878  ? 30.026 75.914  8.109   1.00 15.27 ? 878  LEU A O   1 
ATOM   6919 C  CB  . LEU A 1 878  ? 29.361 73.589  5.972   1.00 14.09 ? 878  LEU A CB  1 
ATOM   6920 C  CG  . LEU A 1 878  ? 30.268 74.607  5.244   1.00 13.32 ? 878  LEU A CG  1 
ATOM   6921 C  CD1 . LEU A 1 878  ? 31.787 74.555  5.691   1.00 15.88 ? 878  LEU A CD1 1 
ATOM   6922 C  CD2 . LEU A 1 878  ? 30.096 74.332  3.796   1.00 15.43 ? 878  LEU A CD2 1 
ATOM   6923 N  N   . GLY A 1 879  ? 27.806 75.446  8.171   1.00 14.73 ? 879  GLY A N   1 
ATOM   6924 C  CA  . GLY A 1 879  ? 27.438 76.769  8.655   1.00 19.07 ? 879  GLY A CA  1 
ATOM   6925 C  C   . GLY A 1 879  ? 27.754 77.942  7.746   1.00 18.53 ? 879  GLY A C   1 
ATOM   6926 O  O   . GLY A 1 879  ? 28.081 79.031  8.224   1.00 20.95 ? 879  GLY A O   1 
ATOM   6927 N  N   . GLN A 1 880  ? 27.671 77.723  6.440   1.00 18.87 ? 880  GLN A N   1 
ATOM   6928 C  CA  . GLN A 1 880  ? 27.866 78.757  5.450   1.00 16.90 ? 880  GLN A CA  1 
ATOM   6929 C  C   . GLN A 1 880  ? 27.403 78.260  4.076   1.00 16.39 ? 880  GLN A C   1 
ATOM   6930 O  O   . GLN A 1 880  ? 27.280 77.052  3.845   1.00 17.00 ? 880  GLN A O   1 
ATOM   6931 C  CB  . GLN A 1 880  ? 29.367 79.232  5.400   1.00 17.15 ? 880  GLN A CB  1 
ATOM   6932 C  CG  . GLN A 1 880  ? 30.390 78.233  4.767   1.00 16.63 ? 880  GLN A CG  1 
ATOM   6933 C  CD  . GLN A 1 880  ? 31.692 78.911  4.250   1.00 13.42 ? 880  GLN A CD  1 
ATOM   6934 O  OE1 . GLN A 1 880  ? 32.639 79.163  4.997   1.00 16.96 ? 880  GLN A OE1 1 
ATOM   6935 N  NE2 . GLN A 1 880  ? 31.715 79.183  2.979   1.00 17.54 ? 880  GLN A NE2 1 
ATOM   6936 N  N   . GLY A 1 881  ? 27.091 79.188  3.185   1.00 15.38 ? 881  GLY A N   1 
ATOM   6937 C  CA  . GLY A 1 881  ? 26.762 78.810  1.828   1.00 15.29 ? 881  GLY A CA  1 
ATOM   6938 C  C   . GLY A 1 881  ? 28.070 78.761  1.006   1.00 13.79 ? 881  GLY A C   1 
ATOM   6939 O  O   . GLY A 1 881  ? 29.166 78.586  1.543   1.00 18.14 ? 881  GLY A O   1 
ATOM   6940 N  N   . VAL A 1 882  ? 27.933 78.886  -0.298  1.00 13.83 ? 882  VAL A N   1 
ATOM   6941 C  CA  . VAL A 1 882  ? 29.110 78.867  -1.162  1.00 12.94 ? 882  VAL A CA  1 
ATOM   6942 C  C   . VAL A 1 882  ? 29.068 80.223  -1.912  1.00 13.34 ? 882  VAL A C   1 
ATOM   6943 O  O   . VAL A 1 882  ? 28.349 80.376  -2.906  1.00 14.98 ? 882  VAL A O   1 
ATOM   6944 C  CB  . VAL A 1 882  ? 29.042 77.667  -2.152  1.00 13.80 ? 882  VAL A CB  1 
ATOM   6945 C  CG1 . VAL A 1 882  ? 30.230 77.710  -3.135  1.00 14.11 ? 882  VAL A CG1 1 
ATOM   6946 C  CG2 . VAL A 1 882  ? 29.123 76.366  -1.381  1.00 15.63 ? 882  VAL A CG2 1 
ATOM   6947 N  N   . LEU A 1 883  ? 29.860 81.188  -1.440  1.00 16.95 ? 883  LEU A N   1 
ATOM   6948 C  CA  . LEU A 1 883  ? 29.881 82.530  -2.053  1.00 17.42 ? 883  LEU A CA  1 
ATOM   6949 C  C   . LEU A 1 883  ? 31.315 83.009  -2.229  1.00 17.66 ? 883  LEU A C   1 
ATOM   6950 O  O   . LEU A 1 883  ? 31.588 84.218  -2.146  1.00 18.17 ? 883  LEU A O   1 
ATOM   6951 C  CB  . LEU A 1 883  ? 29.128 83.498  -1.143  1.00 18.69 ? 883  LEU A CB  1 
ATOM   6952 C  CG  . LEU A 1 883  ? 27.644 83.138  -0.900  1.00 18.61 ? 883  LEU A CG  1 
ATOM   6953 C  CD1 . LEU A 1 883  ? 27.084 84.053  0.106   1.00 20.76 ? 883  LEU A CD1 1 
ATOM   6954 C  CD2 . LEU A 1 883  ? 26.833 83.268  -2.145  1.00 18.57 ? 883  LEU A CD2 1 
ATOM   6955 N  N   . ASP A 1 884  ? 32.228 82.060  -2.436  1.00 15.72 ? 884  ASP A N   1 
ATOM   6956 C  CA  . ASP A 1 884  ? 33.663 82.307  -2.668  1.00 13.91 ? 884  ASP A CA  1 
ATOM   6957 C  C   . ASP A 1 884  ? 34.162 81.913  -4.036  1.00 12.87 ? 884  ASP A C   1 
ATOM   6958 O  O   . ASP A 1 884  ? 35.372 81.701  -4.254  1.00 12.17 ? 884  ASP A O   1 
ATOM   6959 C  CB  . ASP A 1 884  ? 34.535 81.680  -1.566  1.00 15.31 ? 884  ASP A CB  1 
ATOM   6960 C  CG  . ASP A 1 884  ? 34.277 80.188  -1.369  1.00 15.87 ? 884  ASP A CG  1 
ATOM   6961 O  OD1 . ASP A 1 884  ? 33.460 79.583  -2.103  1.00 14.19 ? 884  ASP A OD1 1 
ATOM   6962 O  OD2 . ASP A 1 884  ? 34.918 79.647  -0.446  1.00 15.59 ? 884  ASP A OD2 1 
ATOM   6963 N  N   . ASN A 1 885  ? 33.243 81.815  -4.974  1.00 12.20 ? 885  ASN A N   1 
ATOM   6964 C  CA  . ASN A 1 885  ? 33.545 81.495  -6.376  1.00 13.09 ? 885  ASN A CA  1 
ATOM   6965 C  C   . ASN A 1 885  ? 34.625 82.377  -6.962  1.00 14.19 ? 885  ASN A C   1 
ATOM   6966 O  O   . ASN A 1 885  ? 34.786 83.539  -6.555  1.00 14.44 ? 885  ASN A O   1 
ATOM   6967 C  CB  . ASN A 1 885  ? 32.276 81.658  -7.217  1.00 13.59 ? 885  ASN A CB  1 
ATOM   6968 C  CG  . ASN A 1 885  ? 31.119 81.010  -6.582  1.00 13.28 ? 885  ASN A CG  1 
ATOM   6969 O  OD1 . ASN A 1 885  ? 30.484 81.579  -5.694  1.00 14.81 ? 885  ASN A OD1 1 
ATOM   6970 N  ND2 . ASN A 1 885  ? 30.850 79.779  -6.992  1.00 12.68 ? 885  ASN A ND2 1 
ATOM   6971 N  N   . LYS A 1 886  ? 35.404 81.808  -7.863  1.00 13.61 ? 886  LYS A N   1 
ATOM   6972 C  CA  . LYS A 1 886  ? 36.466 82.561  -8.582  1.00 14.27 ? 886  LYS A CA  1 
ATOM   6973 C  C   . LYS A 1 886  ? 36.496 81.988  -9.960  1.00 12.70 ? 886  LYS A C   1 
ATOM   6974 O  O   . LYS A 1 886  ? 36.077 80.816  -10.154 1.00 11.71 ? 886  LYS A O   1 
ATOM   6975 C  CB  . LYS A 1 886  ? 37.852 82.413  -7.945  1.00 17.20 ? 886  LYS A CB  1 
ATOM   6976 C  CG  . LYS A 1 886  ? 38.363 80.982  -7.684  1.00 18.88 ? 886  LYS A CG  1 
ATOM   6977 C  CD  . LYS A 1 886  ? 39.412 80.990  -6.536  1.00 20.09 ? 886  LYS A CD  1 
ATOM   6978 C  CE  . LYS A 1 886  ? 40.725 81.429  -7.062  1.00 17.02 ? 886  LYS A CE  1 
ATOM   6979 N  NZ  . LYS A 1 886  ? 41.816 81.662  -6.051  1.00 19.38 ? 886  LYS A NZ  1 
ATOM   6980 N  N   . PRO A 1 887  ? 37.021 82.748  -10.941 1.00 11.18 ? 887  PRO A N   1 
ATOM   6981 C  CA  . PRO A 1 887  ? 37.107 82.319  -12.326 1.00 12.90 ? 887  PRO A CA  1 
ATOM   6982 C  C   . PRO A 1 887  ? 37.876 81.009  -12.430 1.00 10.98 ? 887  PRO A C   1 
ATOM   6983 O  O   . PRO A 1 887  ? 38.948 80.891  -11.828 1.00 12.57 ? 887  PRO A O   1 
ATOM   6984 C  CB  . PRO A 1 887  ? 37.895 83.475  -12.995 1.00 13.21 ? 887  PRO A CB  1 
ATOM   6985 C  CG  . PRO A 1 887  ? 37.400 84.685  -12.234 1.00 14.89 ? 887  PRO A CG  1 
ATOM   6986 C  CD  . PRO A 1 887  ? 37.381 84.178  -10.793 1.00 14.51 ? 887  PRO A CD  1 
ATOM   6987 N  N   . VAL A 1 888  ? 37.384 80.062  -13.188 1.00 10.34 ? 888  VAL A N   1 
ATOM   6988 C  CA  . VAL A 1 888  ? 38.082 78.805  -13.386 1.00 9.55  ? 888  VAL A CA  1 
ATOM   6989 C  C   . VAL A 1 888  ? 37.984 78.454  -14.848 1.00 11.21 ? 888  VAL A C   1 
ATOM   6990 O  O   . VAL A 1 888  ? 36.937 78.698  -15.460 1.00 12.98 ? 888  VAL A O   1 
ATOM   6991 C  CB  . VAL A 1 888  ? 37.428 77.645  -12.497 1.00 9.77  ? 888  VAL A CB  1 
ATOM   6992 C  CG1 . VAL A 1 888  ? 35.883 77.536  -12.705 1.00 11.46 ? 888  VAL A CG1 1 
ATOM   6993 C  CG2 . VAL A 1 888  ? 38.117 76.314  -12.748 1.00 10.25 ? 888  VAL A CG2 1 
ATOM   6994 N  N   . LEU A 1 889  ? 39.045 77.871  -15.426 1.00 8.17  ? 889  LEU A N   1 
ATOM   6995 C  CA  . LEU A 1 889  ? 39.047 77.403  -16.770 1.00 9.77  ? 889  LEU A CA  1 
ATOM   6996 C  C   . LEU A 1 889  ? 38.841 75.870  -16.789 1.00 9.61  ? 889  LEU A C   1 
ATOM   6997 O  O   . LEU A 1 889  ? 39.728 75.051  -16.479 1.00 10.85 ? 889  LEU A O   1 
ATOM   6998 C  CB  . LEU A 1 889  ? 40.399 77.763  -17.471 1.00 9.37  ? 889  LEU A CB  1 
ATOM   6999 C  CG  . LEU A 1 889  ? 40.457 77.334  -18.954 1.00 11.09 ? 889  LEU A CG  1 
ATOM   7000 C  CD1 . LEU A 1 889  ? 39.584 78.256  -19.775 1.00 12.48 ? 889  LEU A CD1 1 
ATOM   7001 C  CD2 . LEU A 1 889  ? 41.868 77.298  -19.450 1.00 12.64 ? 889  LEU A CD2 1 
ATOM   7002 N  N   . HIS A 1 890  ? 37.633 75.444  -17.123 1.00 7.26  ? 890  HIS A N   1 
ATOM   7003 C  CA  . HIS A 1 890  ? 37.348 74.022  -17.304 1.00 9.66  ? 890  HIS A CA  1 
ATOM   7004 C  C   . HIS A 1 890  ? 37.730 73.567  -18.695 1.00 9.12  ? 890  HIS A C   1 
ATOM   7005 O  O   . HIS A 1 890  ? 37.464 74.307  -19.667 1.00 9.05  ? 890  HIS A O   1 
ATOM   7006 C  CB  . HIS A 1 890  ? 35.850 73.744  -17.092 1.00 9.24  ? 890  HIS A CB  1 
ATOM   7007 C  CG  . HIS A 1 890  ? 35.404 73.973  -15.678 1.00 9.63  ? 890  HIS A CG  1 
ATOM   7008 N  ND1 . HIS A 1 890  ? 36.192 73.601  -14.596 1.00 11.74 ? 890  HIS A ND1 1 
ATOM   7009 C  CD2 . HIS A 1 890  ? 34.245 74.452  -15.156 1.00 10.59 ? 890  HIS A CD2 1 
ATOM   7010 C  CE1 . HIS A 1 890  ? 35.539 73.832  -13.473 1.00 8.93  ? 890  HIS A CE1 1 
ATOM   7011 N  NE2 . HIS A 1 890  ? 34.350 74.354  -13.777 1.00 8.54  ? 890  HIS A NE2 1 
ATOM   7012 N  N   . ILE A 1 891  ? 38.294 72.371  -18.855 1.00 8.26  ? 891  ILE A N   1 
ATOM   7013 C  CA  . ILE A 1 891  ? 38.680 71.841  -20.159 1.00 8.84  ? 891  ILE A CA  1 
ATOM   7014 C  C   . ILE A 1 891  ? 38.024 70.498  -20.432 1.00 8.66  ? 891  ILE A C   1 
ATOM   7015 O  O   . ILE A 1 891  ? 37.750 69.733  -19.496 1.00 9.65  ? 891  ILE A O   1 
ATOM   7016 C  CB  . ILE A 1 891  ? 40.237 71.781  -20.298 1.00 9.54  ? 891  ILE A CB  1 
ATOM   7017 C  CG1 . ILE A 1 891  ? 40.863 70.743  -19.324 1.00 9.61  ? 891  ILE A CG1 1 
ATOM   7018 C  CG2 . ILE A 1 891  ? 40.774 73.213  -20.006 1.00 10.37 ? 891  ILE A CG2 1 
ATOM   7019 C  CD1 . ILE A 1 891  ? 42.393 70.559  -19.492 1.00 9.17  ? 891  ILE A CD1 1 
ATOM   7020 N  N   . TYR A 1 892  ? 37.803 70.191  -21.705 1.00 10.18 ? 892  TYR A N   1 
ATOM   7021 C  CA  . TYR A 1 892  ? 37.122 68.986  -22.138 1.00 8.12  ? 892  TYR A CA  1 
ATOM   7022 C  C   . TYR A 1 892  ? 37.546 68.555  -23.530 1.00 9.11  ? 892  TYR A C   1 
ATOM   7023 O  O   . TYR A 1 892  ? 38.170 69.340  -24.269 1.00 9.97  ? 892  TYR A O   1 
ATOM   7024 C  CB  . TYR A 1 892  ? 35.606 69.253  -22.269 1.00 7.70  ? 892  TYR A CB  1 
ATOM   7025 C  CG  . TYR A 1 892  ? 34.948 69.909  -21.091 1.00 6.74  ? 892  TYR A CG  1 
ATOM   7026 C  CD1 . TYR A 1 892  ? 34.933 71.264  -20.937 1.00 8.83  ? 892  TYR A CD1 1 
ATOM   7027 C  CD2 . TYR A 1 892  ? 34.368 69.116  -20.072 1.00 10.81 ? 892  TYR A CD2 1 
ATOM   7028 C  CE1 . TYR A 1 892  ? 34.374 71.870  -19.842 1.00 9.21  ? 892  TYR A CE1 1 
ATOM   7029 C  CE2 . TYR A 1 892  ? 33.820 69.666  -18.977 1.00 8.15  ? 892  TYR A CE2 1 
ATOM   7030 C  CZ  . TYR A 1 892  ? 33.786 71.058  -18.798 1.00 7.60  ? 892  TYR A CZ  1 
ATOM   7031 O  OH  . TYR A 1 892  ? 33.165 71.662  -17.712 1.00 9.87  ? 892  TYR A OH  1 
ATOM   7032 N  N   . ARG A 1 893  ? 37.208 67.313  -23.886 1.00 8.99  ? 893  ARG A N   1 
ATOM   7033 C  CA  . ARG A 1 893  ? 37.363 66.818  -25.251 1.00 10.85 ? 893  ARG A CA  1 
ATOM   7034 C  C   . ARG A 1 893  ? 35.985 66.245  -25.537 1.00 8.64  ? 893  ARG A C   1 
ATOM   7035 O  O   . ARG A 1 893  ? 35.383 65.556  -24.702 1.00 10.86 ? 893  ARG A O   1 
ATOM   7036 C  CB  . ARG A 1 893  ? 38.426 65.727  -25.454 1.00 9.53  ? 893  ARG A CB  1 
ATOM   7037 C  CG  . ARG A 1 893  ? 39.846 66.270  -25.175 1.00 10.66 ? 893  ARG A CG  1 
ATOM   7038 C  CD  . ARG A 1 893  ? 40.316 67.338  -26.238 1.00 11.29 ? 893  ARG A CD  1 
ATOM   7039 N  NE  . ARG A 1 893  ? 40.390 66.855  -27.625 1.00 11.98 ? 893  ARG A NE  1 
ATOM   7040 C  CZ  . ARG A 1 893  ? 41.366 66.110  -28.111 1.00 11.03 ? 893  ARG A CZ  1 
ATOM   7041 N  NH1 . ARG A 1 893  ? 42.364 65.720  -27.322 1.00 12.46 ? 893  ARG A NH1 1 
ATOM   7042 N  NH2 . ARG A 1 893  ? 41.414 65.763  -29.393 1.00 13.49 ? 893  ARG A NH2 1 
ATOM   7043 N  N   . LEU A 1 894  ? 35.487 66.507  -26.751 1.00 11.10 ? 894  LEU A N   1 
ATOM   7044 C  CA  . LEU A 1 894  ? 34.181 66.025  -27.188 1.00 11.58 ? 894  LEU A CA  1 
ATOM   7045 C  C   . LEU A 1 894  ? 34.416 65.072  -28.347 1.00 12.09 ? 894  LEU A C   1 
ATOM   7046 O  O   . LEU A 1 894  ? 34.857 65.496  -29.454 1.00 13.41 ? 894  LEU A O   1 
ATOM   7047 C  CB  . LEU A 1 894  ? 33.348 67.212  -27.620 1.00 12.40 ? 894  LEU A CB  1 
ATOM   7048 C  CG  . LEU A 1 894  ? 31.871 66.838  -27.854 1.00 11.86 ? 894  LEU A CG  1 
ATOM   7049 C  CD1 . LEU A 1 894  ? 31.139 66.382  -26.540 1.00 12.79 ? 894  LEU A CD1 1 
ATOM   7050 C  CD2 . LEU A 1 894  ? 31.141 68.053  -28.399 1.00 13.95 ? 894  LEU A CD2 1 
ATOM   7051 N  N   . VAL A 1 895  ? 34.058 63.803  -28.140 1.00 12.77 ? 895  VAL A N   1 
ATOM   7052 C  CA  . VAL A 1 895  ? 34.319 62.777  -29.114 1.00 12.04 ? 895  VAL A CA  1 
ATOM   7053 C  C   . VAL A 1 895  ? 33.033 62.154  -29.652 1.00 13.12 ? 895  VAL A C   1 
ATOM   7054 O  O   . VAL A 1 895  ? 32.338 61.440  -28.937 1.00 12.51 ? 895  VAL A O   1 
ATOM   7055 C  CB  . VAL A 1 895  ? 35.162 61.631  -28.512 1.00 11.52 ? 895  VAL A CB  1 
ATOM   7056 C  CG1 . VAL A 1 895  ? 35.503 60.595  -29.616 1.00 13.50 ? 895  VAL A CG1 1 
ATOM   7057 C  CG2 . VAL A 1 895  ? 36.400 62.259  -27.804 1.00 13.73 ? 895  VAL A CG2 1 
ATOM   7058 N  N   . LEU A 1 896  ? 32.733 62.397  -30.926 1.00 14.68 ? 896  LEU A N   1 
ATOM   7059 C  CA  . LEU A 1 896  ? 31.568 61.773  -31.497 1.00 14.55 ? 896  LEU A CA  1 
ATOM   7060 C  C   . LEU A 1 896  ? 32.126 60.679  -32.358 1.00 14.07 ? 896  LEU A C   1 
ATOM   7061 O  O   . LEU A 1 896  ? 33.096 60.885  -33.116 1.00 14.40 ? 896  LEU A O   1 
ATOM   7062 C  CB  . LEU A 1 896  ? 30.766 62.795  -32.347 1.00 14.77 ? 896  LEU A CB  1 
ATOM   7063 C  CG  . LEU A 1 896  ? 29.629 62.221  -33.226 1.00 16.36 ? 896  LEU A CG  1 
ATOM   7064 C  CD1 . LEU A 1 896  ? 28.390 62.076  -32.439 1.00 17.63 ? 896  LEU A CD1 1 
ATOM   7065 C  CD2 . LEU A 1 896  ? 29.336 63.212  -34.384 1.00 18.04 ? 896  LEU A CD2 1 
ATOM   7066 N  N   . GLU A 1 897  ? 31.555 59.481  -32.258 1.00 14.01 ? 897  GLU A N   1 
ATOM   7067 C  CA  . GLU A 1 897  ? 32.067 58.383  -33.027 1.00 14.63 ? 897  GLU A CA  1 
ATOM   7068 C  C   . GLU A 1 897  ? 30.992 57.344  -33.361 1.00 15.26 ? 897  GLU A C   1 
ATOM   7069 O  O   . GLU A 1 897  ? 29.984 57.257  -32.679 1.00 15.13 ? 897  GLU A O   1 
ATOM   7070 C  CB  . GLU A 1 897  ? 33.267 57.758  -32.263 1.00 18.37 ? 897  GLU A CB  1 
ATOM   7071 C  CG  . GLU A 1 897  ? 32.942 57.184  -30.925 1.00 20.52 ? 897  GLU A CG  1 
ATOM   7072 C  CD  . GLU A 1 897  ? 34.197 57.163  -29.955 1.00 20.74 ? 897  GLU A CD  1 
ATOM   7073 O  OE1 . GLU A 1 897  ? 35.369 57.115  -30.393 1.00 20.19 ? 897  GLU A OE1 1 
ATOM   7074 O  OE2 . GLU A 1 897  ? 33.946 57.207  -28.754 1.00 23.73 ? 897  GLU A OE2 1 
ATOM   7075 N  N   . LYS A 1 898  ? 31.208 56.592  -34.437 1.00 18.60 ? 898  LYS A N   1 
ATOM   7076 C  CA  . LYS A 1 898  ? 30.310 55.519  -34.831 1.00 19.22 ? 898  LYS A CA  1 
ATOM   7077 C  C   . LYS A 1 898  ? 30.751 54.292  -34.056 1.00 20.28 ? 898  LYS A C   1 
ATOM   7078 O  O   . LYS A 1 898  ? 31.951 53.995  -34.028 1.00 20.14 ? 898  LYS A O   1 
ATOM   7079 C  CB  . LYS A 1 898  ? 30.430 55.270  -36.344 1.00 22.37 ? 898  LYS A CB  1 
ATOM   7080 C  CG  . LYS A 1 898  ? 29.942 56.435  -37.144 1.00 23.82 ? 898  LYS A CG  1 
ATOM   7081 C  CD  . LYS A 1 898  ? 28.819 57.185  -36.378 1.00 26.99 ? 898  LYS A CD  1 
ATOM   7082 C  CE  . LYS A 1 898  ? 27.401 56.840  -36.877 1.00 28.76 ? 898  LYS A CE  1 
ATOM   7083 N  NZ  . LYS A 1 898  ? 27.144 55.362  -37.004 1.00 31.38 ? 898  LYS A NZ  1 
ATOM   7084 N  N   . VAL A 1 899  ? 29.808 53.580  -33.441 1.00 19.04 ? 899  VAL A N   1 
ATOM   7085 C  CA  . VAL A 1 899  ? 30.153 52.412  -32.642 1.00 19.57 ? 899  VAL A CA  1 
ATOM   7086 C  C   . VAL A 1 899  ? 29.368 51.132  -33.045 1.00 19.28 ? 899  VAL A C   1 
ATOM   7087 O  O   . VAL A 1 899  ? 29.319 50.125  -32.318 1.00 17.28 ? 899  VAL A O   1 
ATOM   7088 C  CB  . VAL A 1 899  ? 29.941 52.755  -31.142 1.00 19.01 ? 899  VAL A CB  1 
ATOM   7089 C  CG1 . VAL A 1 899  ? 30.869 53.893  -30.742 1.00 19.85 ? 899  VAL A CG1 1 
ATOM   7090 C  CG2 . VAL A 1 899  ? 28.516 53.152  -30.928 1.00 19.92 ? 899  VAL A CG2 1 
ATOM   7091 N  N   . ASN A 1 900  ? 28.782 51.150  -34.242 1.00 19.15 ? 900  ASN A N   1 
ATOM   7092 C  CA  . ASN A 1 900  ? 28.042 49.982  -34.698 1.00 19.36 ? 900  ASN A CA  1 
ATOM   7093 C  C   . ASN A 1 900  ? 28.991 48.829  -34.941 1.00 18.24 ? 900  ASN A C   1 
ATOM   7094 O  O   . ASN A 1 900  ? 28.576 47.689  -34.865 1.00 21.05 ? 900  ASN A O   1 
ATOM   7095 C  CB  . ASN A 1 900  ? 27.246 50.306  -35.982 1.00 19.98 ? 900  ASN A CB  1 
ATOM   7096 C  CG  . ASN A 1 900  ? 28.120 50.866  -37.081 1.00 21.76 ? 900  ASN A CG  1 
ATOM   7097 O  OD1 . ASN A 1 900  ? 28.712 51.954  -36.956 1.00 23.49 ? 900  ASN A OD1 1 
ATOM   7098 N  ND2 . ASN A 1 900  ? 28.217 50.119  -38.185 1.00 24.37 ? 900  ASN A ND2 1 
ATOM   7099 N  N   . ASN A 1 901  ? 30.269 49.097  -35.174 1.00 18.72 ? 901  ASN A N   1 
ATOM   7100 C  CA  . ASN A 1 901  ? 31.207 48.000  -35.378 1.00 19.49 ? 901  ASN A CA  1 
ATOM   7101 C  C   . ASN A 1 901  ? 31.991 47.575  -34.162 1.00 18.34 ? 901  ASN A C   1 
ATOM   7102 O  O   . ASN A 1 901  ? 32.762 46.587  -34.226 1.00 19.04 ? 901  ASN A O   1 
ATOM   7103 C  CB  . ASN A 1 901  ? 32.182 48.333  -36.490 1.00 22.02 ? 901  ASN A CB  1 
ATOM   7104 C  CG  . ASN A 1 901  ? 31.515 48.353  -37.847 1.00 24.57 ? 901  ASN A CG  1 
ATOM   7105 O  OD1 . ASN A 1 901  ? 31.735 49.287  -38.607 1.00 28.59 ? 901  ASN A OD1 1 
ATOM   7106 N  ND2 . ASN A 1 901  ? 30.712 47.329  -38.162 1.00 26.26 ? 901  ASN A ND2 1 
ATOM   7107 N  N   . CYS A 1 902  ? 31.810 48.285  -33.051 1.00 17.78 ? 902  CYS A N   1 
ATOM   7108 C  CA  . CYS A 1 902  ? 32.540 47.899  -31.830 1.00 17.42 ? 902  CYS A CA  1 
ATOM   7109 C  C   . CYS A 1 902  ? 31.962 46.696  -31.080 1.00 15.94 ? 902  CYS A C   1 
ATOM   7110 O  O   . CYS A 1 902  ? 30.737 46.539  -30.986 1.00 17.30 ? 902  CYS A O   1 
ATOM   7111 C  CB  . CYS A 1 902  ? 32.547 49.038  -30.838 1.00 16.71 ? 902  CYS A CB  1 
ATOM   7112 S  SG  . CYS A 1 902  ? 33.208 50.626  -31.432 1.00 19.12 ? 902  CYS A SG  1 
ATOM   7113 N  N   . VAL A 1 903  ? 32.851 45.882  -30.522 1.00 16.05 ? 903  VAL A N   1 
ATOM   7114 C  CA  . VAL A 1 903  ? 32.449 44.743  -29.700 1.00 17.34 ? 903  VAL A CA  1 
ATOM   7115 C  C   . VAL A 1 903  ? 32.183 45.305  -28.296 1.00 17.23 ? 903  VAL A C   1 
ATOM   7116 O  O   . VAL A 1 903  ? 33.110 45.650  -27.545 1.00 17.96 ? 903  VAL A O   1 
ATOM   7117 C  CB  . VAL A 1 903  ? 33.569 43.699  -29.695 1.00 15.74 ? 903  VAL A CB  1 
ATOM   7118 C  CG1 . VAL A 1 903  ? 33.219 42.591  -28.729 1.00 17.04 ? 903  VAL A CG1 1 
ATOM   7119 C  CG2 . VAL A 1 903  ? 33.792 43.200  -31.165 1.00 14.67 ? 903  VAL A CG2 1 
ATOM   7120 N  N   . ARG A 1 904  ? 30.905 45.443  -27.976 1.00 17.40 ? 904  ARG A N   1 
ATOM   7121 C  CA  . ARG A 1 904  ? 30.488 46.026  -26.709 1.00 16.34 ? 904  ARG A CA  1 
ATOM   7122 C  C   . ARG A 1 904  ? 29.935 44.967  -25.775 1.00 15.76 ? 904  ARG A C   1 
ATOM   7123 O  O   . ARG A 1 904  ? 29.553 43.857  -26.192 1.00 14.07 ? 904  ARG A O   1 
ATOM   7124 C  CB  . ARG A 1 904  ? 29.421 47.104  -26.980 1.00 17.54 ? 904  ARG A CB  1 
ATOM   7125 C  CG  . ARG A 1 904  ? 30.037 48.396  -27.544 1.00 18.14 ? 904  ARG A CG  1 
ATOM   7126 C  CD  . ARG A 1 904  ? 29.029 49.474  -27.859 1.00 20.95 ? 904  ARG A CD  1 
ATOM   7127 N  NE  . ARG A 1 904  ? 28.231 49.074  -29.020 1.00 21.90 ? 904  ARG A NE  1 
ATOM   7128 C  CZ  . ARG A 1 904  ? 27.218 49.773  -29.534 1.00 21.30 ? 904  ARG A CZ  1 
ATOM   7129 N  NH1 . ARG A 1 904  ? 26.838 50.914  -29.021 1.00 22.63 ? 904  ARG A NH1 1 
ATOM   7130 N  NH2 . ARG A 1 904  ? 26.569 49.297  -30.586 1.00 21.14 ? 904  ARG A NH2 1 
ATOM   7131 N  N   . PRO A 1 905  ? 29.892 45.289  -24.472 1.00 13.37 ? 905  PRO A N   1 
ATOM   7132 C  CA  . PRO A 1 905  ? 29.355 44.332  -23.493 1.00 14.36 ? 905  PRO A CA  1 
ATOM   7133 C  C   . PRO A 1 905  ? 27.874 44.117  -23.796 1.00 14.20 ? 905  PRO A C   1 
ATOM   7134 O  O   . PRO A 1 905  ? 27.267 44.986  -24.415 1.00 14.91 ? 905  PRO A O   1 
ATOM   7135 C  CB  . PRO A 1 905  ? 29.531 45.083  -22.163 1.00 13.86 ? 905  PRO A CB  1 
ATOM   7136 C  CG  . PRO A 1 905  ? 30.593 46.100  -22.419 1.00 13.16 ? 905  PRO A CG  1 
ATOM   7137 C  CD  . PRO A 1 905  ? 30.340 46.544  -23.829 1.00 14.67 ? 905  PRO A CD  1 
ATOM   7138 N  N   . SER A 1 906  ? 27.272 43.022  -23.311 1.00 13.92 ? 906  SER A N   1 
ATOM   7139 C  CA  . SER A 1 906  ? 25.859 42.761  -23.529 1.00 17.51 ? 906  SER A CA  1 
ATOM   7140 C  C   . SER A 1 906  ? 24.989 43.715  -22.720 1.00 17.97 ? 906  SER A C   1 
ATOM   7141 O  O   . SER A 1 906  ? 25.485 44.467  -21.894 1.00 17.17 ? 906  SER A O   1 
ATOM   7142 C  CB  . SER A 1 906  ? 25.528 41.305  -23.179 1.00 18.93 ? 906  SER A CB  1 
ATOM   7143 O  OG  . SER A 1 906  ? 25.466 41.155  -21.790 1.00 23.96 ? 906  SER A OG  1 
ATOM   7144 N  N   . LYS A 1 907  ? 23.683 43.699  -22.982 1.00 18.82 ? 907  LYS A N   1 
ATOM   7145 C  CA  . LYS A 1 907  ? 22.731 44.585  -22.311 1.00 21.42 ? 907  LYS A CA  1 
ATOM   7146 C  C   . LYS A 1 907  ? 22.715 44.457  -20.797 1.00 20.03 ? 907  LYS A C   1 
ATOM   7147 O  O   . LYS A 1 907  ? 22.353 45.389  -20.092 1.00 20.91 ? 907  LYS A O   1 
ATOM   7148 C  CB  . LYS A 1 907  ? 21.321 44.334  -22.877 1.00 24.32 ? 907  LYS A CB  1 
ATOM   7149 C  CG  . LYS A 1 907  ? 21.211 44.765  -24.316 1.00 29.07 ? 907  LYS A CG  1 
ATOM   7150 C  CD  . LYS A 1 907  ? 19.867 44.361  -24.941 1.00 31.56 ? 907  LYS A CD  1 
ATOM   7151 C  CE  . LYS A 1 907  ? 19.734 45.012  -26.333 1.00 32.82 ? 907  LYS A CE  1 
ATOM   7152 N  NZ  . LYS A 1 907  ? 19.873 46.529  -26.250 1.00 35.21 ? 907  LYS A NZ  1 
ATOM   7153 N  N   . LEU A 1 908  ? 23.119 43.300  -20.307 1.00 19.36 ? 908  LEU A N   1 
ATOM   7154 C  CA  . LEU A 1 908  ? 23.120 43.074  -18.852 1.00 18.70 ? 908  LEU A CA  1 
ATOM   7155 C  C   . LEU A 1 908  ? 24.418 43.410  -18.106 1.00 17.23 ? 908  LEU A C   1 
ATOM   7156 O  O   . LEU A 1 908  ? 24.477 43.385  -16.869 1.00 17.60 ? 908  LEU A O   1 
ATOM   7157 C  CB  . LEU A 1 908  ? 22.738 41.619  -18.574 1.00 21.89 ? 908  LEU A CB  1 
ATOM   7158 C  CG  . LEU A 1 908  ? 21.336 41.310  -19.105 1.00 23.76 ? 908  LEU A CG  1 
ATOM   7159 C  CD1 . LEU A 1 908  ? 20.951 39.925  -18.581 1.00 25.69 ? 908  LEU A CD1 1 
ATOM   7160 C  CD2 . LEU A 1 908  ? 20.325 42.360  -18.656 1.00 25.20 ? 908  LEU A CD2 1 
ATOM   7161 N  N   . HIS A 1 909  ? 25.468 43.698  -18.857 1.00 16.30 ? 909  HIS A N   1 
ATOM   7162 C  CA  . HIS A 1 909  ? 26.756 44.013  -18.272 1.00 13.42 ? 909  HIS A CA  1 
ATOM   7163 C  C   . HIS A 1 909  ? 26.712 45.413  -17.627 1.00 12.50 ? 909  HIS A C   1 
ATOM   7164 O  O   . HIS A 1 909  ? 26.257 46.369  -18.230 1.00 13.09 ? 909  HIS A O   1 
ATOM   7165 C  CB  . HIS A 1 909  ? 27.830 43.923  -19.344 1.00 13.04 ? 909  HIS A CB  1 
ATOM   7166 C  CG  . HIS A 1 909  ? 29.195 43.749  -18.800 1.00 12.84 ? 909  HIS A CG  1 
ATOM   7167 N  ND1 . HIS A 1 909  ? 29.843 44.711  -18.048 1.00 13.01 ? 909  HIS A ND1 1 
ATOM   7168 C  CD2 . HIS A 1 909  ? 30.053 42.717  -18.924 1.00 12.17 ? 909  HIS A CD2 1 
ATOM   7169 C  CE1 . HIS A 1 909  ? 31.047 44.267  -17.733 1.00 12.88 ? 909  HIS A CE1 1 
ATOM   7170 N  NE2 . HIS A 1 909  ? 31.202 43.061  -18.255 1.00 13.43 ? 909  HIS A NE2 1 
ATOM   7171 N  N   . PRO A 1 910  ? 27.183 45.521  -16.361 1.00 11.19 ? 910  PRO A N   1 
ATOM   7172 C  CA  . PRO A 1 910  ? 27.167 46.809  -15.657 1.00 10.77 ? 910  PRO A CA  1 
ATOM   7173 C  C   . PRO A 1 910  ? 28.257 47.819  -16.016 1.00 10.30 ? 910  PRO A C   1 
ATOM   7174 O  O   . PRO A 1 910  ? 28.189 48.924  -15.527 1.00 10.11 ? 910  PRO A O   1 
ATOM   7175 C  CB  . PRO A 1 910  ? 27.196 46.401  -14.195 1.00 13.66 ? 910  PRO A CB  1 
ATOM   7176 C  CG  . PRO A 1 910  ? 27.949 45.105  -14.187 1.00 14.34 ? 910  PRO A CG  1 
ATOM   7177 C  CD  . PRO A 1 910  ? 27.618 44.404  -15.520 1.00 13.21 ? 910  PRO A CD  1 
ATOM   7178 N  N   . ALA A 1 911  ? 29.214 47.428  -16.869 1.00 11.27 ? 911  ALA A N   1 
ATOM   7179 C  CA  . ALA A 1 911  ? 30.308 48.362  -17.256 1.00 9.30  ? 911  ALA A CA  1 
ATOM   7180 C  C   . ALA A 1 911  ? 30.209 48.845  -18.694 1.00 9.72  ? 911  ALA A C   1 
ATOM   7181 O  O   . ALA A 1 911  ? 29.455 48.297  -19.523 1.00 10.81 ? 911  ALA A O   1 
ATOM   7182 C  CB  . ALA A 1 911  ? 31.687 47.653  -17.059 1.00 8.79  ? 911  ALA A CB  1 
ATOM   7183 N  N   . GLY A 1 912  ? 31.015 49.873  -18.969 1.00 9.88  ? 912  GLY A N   1 
ATOM   7184 C  CA  . GLY A 1 912  ? 31.173 50.421  -20.303 1.00 9.02  ? 912  GLY A CA  1 
ATOM   7185 C  C   . GLY A 1 912  ? 32.671 50.657  -20.510 1.00 10.23 ? 912  GLY A C   1 
ATOM   7186 O  O   . GLY A 1 912  ? 33.407 50.704  -19.527 1.00 10.99 ? 912  GLY A O   1 
ATOM   7187 N  N   . TYR A 1 913  ? 33.145 50.822  -21.756 1.00 10.51 ? 913  TYR A N   1 
ATOM   7188 C  CA  . TYR A 1 913  ? 34.561 51.036  -22.013 1.00 10.63 ? 913  TYR A CA  1 
ATOM   7189 C  C   . TYR A 1 913  ? 34.725 52.068  -23.105 1.00 10.89 ? 913  TYR A C   1 
ATOM   7190 O  O   . TYR A 1 913  ? 33.922 52.136  -24.106 1.00 10.15 ? 913  TYR A O   1 
ATOM   7191 C  CB  . TYR A 1 913  ? 35.260 49.749  -22.475 1.00 10.72 ? 913  TYR A CB  1 
ATOM   7192 C  CG  . TYR A 1 913  ? 35.192 48.686  -21.447 1.00 10.47 ? 913  TYR A CG  1 
ATOM   7193 C  CD1 . TYR A 1 913  ? 36.038 48.711  -20.370 1.00 9.69  ? 913  TYR A CD1 1 
ATOM   7194 C  CD2 . TYR A 1 913  ? 34.208 47.717  -21.502 1.00 10.63 ? 913  TYR A CD2 1 
ATOM   7195 C  CE1 . TYR A 1 913  ? 35.931 47.849  -19.347 1.00 9.72  ? 913  TYR A CE1 1 
ATOM   7196 C  CE2 . TYR A 1 913  ? 34.059 46.779  -20.430 1.00 9.38  ? 913  TYR A CE2 1 
ATOM   7197 C  CZ  . TYR A 1 913  ? 34.948 46.872  -19.353 1.00 10.13 ? 913  TYR A CZ  1 
ATOM   7198 O  OH  . TYR A 1 913  ? 34.836 45.993  -18.285 1.00 12.78 ? 913  TYR A OH  1 
ATOM   7199 N  N   . LEU A 1 914  ? 35.794 52.817  -22.969 1.00 11.71 ? 914  LEU A N   1 
ATOM   7200 C  CA  . LEU A 1 914  ? 36.155 53.843  -23.965 1.00 11.53 ? 914  LEU A CA  1 
ATOM   7201 C  C   . LEU A 1 914  ? 36.791 53.228  -25.239 1.00 12.29 ? 914  LEU A C   1 
ATOM   7202 O  O   . LEU A 1 914  ? 37.235 52.082  -25.252 1.00 10.88 ? 914  LEU A O   1 
ATOM   7203 C  CB  . LEU A 1 914  ? 37.173 54.818  -23.357 1.00 10.26 ? 914  LEU A CB  1 
ATOM   7204 C  CG  . LEU A 1 914  ? 36.772 55.705  -22.199 1.00 8.72  ? 914  LEU A CG  1 
ATOM   7205 C  CD1 . LEU A 1 914  ? 37.864 56.758  -21.982 1.00 9.58  ? 914  LEU A CD1 1 
ATOM   7206 C  CD2 . LEU A 1 914  ? 35.482 56.449  -22.559 1.00 10.79 ? 914  LEU A CD2 1 
ATOM   7207 N  N   . THR A 1 915  ? 36.771 54.027  -26.318 1.00 13.06 ? 915  THR A N   1 
ATOM   7208 C  CA  . THR A 1 915  ? 37.414 53.665  -27.550 1.00 11.99 ? 915  THR A CA  1 
ATOM   7209 C  C   . THR A 1 915  ? 38.814 54.259  -27.427 1.00 13.52 ? 915  THR A C   1 
ATOM   7210 O  O   . THR A 1 915  ? 39.104 55.070  -26.498 1.00 12.15 ? 915  THR A O   1 
ATOM   7211 C  CB  . THR A 1 915  ? 36.729 54.364  -28.742 1.00 13.02 ? 915  THR A CB  1 
ATOM   7212 O  OG1 . THR A 1 915  ? 36.739 55.772  -28.516 1.00 15.30 ? 915  THR A OG1 1 
ATOM   7213 C  CG2 . THR A 1 915  ? 35.303 53.875  -28.939 1.00 13.17 ? 915  THR A CG2 1 
ATOM   7214 N  N   . SER A 1 916  ? 39.681 53.876  -28.366 1.00 13.55 ? 916  SER A N   1 
ATOM   7215 C  CA  . SER A 1 916  ? 41.038 54.404  -28.409 1.00 13.28 ? 916  SER A CA  1 
ATOM   7216 C  C   . SER A 1 916  ? 41.032 55.934  -28.471 1.00 12.16 ? 916  SER A C   1 
ATOM   7217 O  O   . SER A 1 916  ? 41.753 56.605  -27.743 1.00 12.78 ? 916  SER A O   1 
ATOM   7218 C  CB  . SER A 1 916  ? 41.766 53.845  -29.648 1.00 14.19 ? 916  SER A CB  1 
ATOM   7219 O  OG  . SER A 1 916  ? 43.018 54.506  -29.778 1.00 19.10 ? 916  SER A OG  1 
ATOM   7220 N  N   . ALA A 1 917  ? 40.189 56.486  -29.343 1.00 10.01 ? 917  ALA A N   1 
ATOM   7221 C  CA  . ALA A 1 917  ? 40.199 57.936  -29.481 1.00 10.50 ? 917  ALA A CA  1 
ATOM   7222 C  C   . ALA A 1 917  ? 39.767 58.671  -28.185 1.00 9.89  ? 917  ALA A C   1 
ATOM   7223 O  O   . ALA A 1 917  ? 40.318 59.692  -27.795 1.00 10.20 ? 917  ALA A O   1 
ATOM   7224 C  CB  . ALA A 1 917  ? 39.298 58.341  -30.653 1.00 12.11 ? 917  ALA A CB  1 
ATOM   7225 N  N   . ALA A 1 918  ? 38.777 58.112  -27.504 1.00 11.24 ? 918  ALA A N   1 
ATOM   7226 C  CA  . ALA A 1 918  ? 38.303 58.734  -26.296 1.00 9.79  ? 918  ALA A CA  1 
ATOM   7227 C  C   . ALA A 1 918  ? 39.289 58.632  -25.134 1.00 10.41 ? 918  ALA A C   1 
ATOM   7228 O  O   . ALA A 1 918  ? 39.478 59.591  -24.408 1.00 11.29 ? 918  ALA A O   1 
ATOM   7229 C  CB  . ALA A 1 918  ? 36.920 58.163  -25.934 1.00 9.99  ? 918  ALA A CB  1 
ATOM   7230 N  N   . HIS A 1 919  ? 39.972 57.495  -25.041 1.00 9.06  ? 919  HIS A N   1 
ATOM   7231 C  CA  . HIS A 1 919  ? 40.982 57.324  -23.990 1.00 11.02 ? 919  HIS A CA  1 
ATOM   7232 C  C   . HIS A 1 919  ? 42.167 58.286  -24.289 1.00 9.72  ? 919  HIS A C   1 
ATOM   7233 O  O   . HIS A 1 919  ? 42.654 58.944  -23.395 1.00 10.29 ? 919  HIS A O   1 
ATOM   7234 C  CB  . HIS A 1 919  ? 41.438 55.878  -24.033 1.00 9.84  ? 919  HIS A CB  1 
ATOM   7235 C  CG  . HIS A 1 919  ? 42.562 55.583  -23.114 1.00 13.34 ? 919  HIS A CG  1 
ATOM   7236 N  ND1 . HIS A 1 919  ? 43.805 55.213  -23.586 1.00 13.89 ? 919  HIS A ND1 1 
ATOM   7237 C  CD2 . HIS A 1 919  ? 42.669 55.693  -21.773 1.00 12.32 ? 919  HIS A CD2 1 
ATOM   7238 C  CE1 . HIS A 1 919  ? 44.637 55.108  -22.561 1.00 14.33 ? 919  HIS A CE1 1 
ATOM   7239 N  NE2 . HIS A 1 919  ? 43.980 55.391  -21.458 1.00 14.37 ? 919  HIS A NE2 1 
ATOM   7240 N  N   . LYS A 1 920  ? 42.606 58.386  -25.539 1.00 11.35 ? 920  LYS A N   1 
ATOM   7241 C  CA  . LYS A 1 920  ? 43.715 59.298  -25.770 1.00 10.51 ? 920  LYS A CA  1 
ATOM   7242 C  C   . LYS A 1 920  ? 43.265 60.720  -25.490 1.00 9.33  ? 920  LYS A C   1 
ATOM   7243 O  O   . LYS A 1 920  ? 44.057 61.551  -25.052 1.00 10.90 ? 920  LYS A O   1 
ATOM   7244 C  CB  . LYS A 1 920  ? 44.236 59.213  -27.192 1.00 12.98 ? 920  LYS A CB  1 
ATOM   7245 C  CG  . LYS A 1 920  ? 45.162 57.970  -27.346 1.00 15.11 ? 920  LYS A CG  1 
ATOM   7246 C  CD  . LYS A 1 920  ? 45.792 57.808  -28.741 1.00 17.79 ? 920  LYS A CD  1 
ATOM   7247 C  CE  . LYS A 1 920  ? 46.870 56.733  -28.755 1.00 18.45 ? 920  LYS A CE  1 
ATOM   7248 N  NZ  . LYS A 1 920  ? 48.010 56.941  -27.853 1.00 15.20 ? 920  LYS A NZ  1 
ATOM   7249 N  N   . ALA A 1 921  ? 42.016 61.036  -25.804 1.00 8.47  ? 921  ALA A N   1 
ATOM   7250 C  CA  . ALA A 1 921  ? 41.509 62.356  -25.558 1.00 9.46  ? 921  ALA A CA  1 
ATOM   7251 C  C   . ALA A 1 921  ? 41.551 62.634  -24.032 1.00 10.58 ? 921  ALA A C   1 
ATOM   7252 O  O   . ALA A 1 921  ? 41.873 63.725  -23.600 1.00 9.88  ? 921  ALA A O   1 
ATOM   7253 C  CB  . ALA A 1 921  ? 40.061 62.473  -26.141 1.00 8.76  ? 921  ALA A CB  1 
ATOM   7254 N  N   . SER A 1 922  ? 41.137 61.632  -23.236 1.00 9.26  ? 922  SER A N   1 
ATOM   7255 C  CA  . SER A 1 922  ? 41.258 61.826  -21.769 1.00 7.10  ? 922  SER A CA  1 
ATOM   7256 C  C   . SER A 1 922  ? 42.737 62.066  -21.287 1.00 9.89  ? 922  SER A C   1 
ATOM   7257 O  O   . SER A 1 922  ? 42.997 62.969  -20.459 1.00 8.53  ? 922  SER A O   1 
ATOM   7258 C  CB  . SER A 1 922  ? 40.662 60.600  -21.041 1.00 8.87  ? 922  SER A CB  1 
ATOM   7259 O  OG  . SER A 1 922  ? 40.844 60.756  -19.643 1.00 7.33  ? 922  SER A OG  1 
ATOM   7260 N  N   . GLN A 1 923  ? 43.682 61.325  -21.875 1.00 8.42  ? 923  GLN A N   1 
ATOM   7261 C  CA  . GLN A 1 923  ? 45.102 61.478  -21.507 1.00 10.04 ? 923  GLN A CA  1 
ATOM   7262 C  C   . GLN A 1 923  ? 45.592 62.873  -21.896 1.00 9.86  ? 923  GLN A C   1 
ATOM   7263 O  O   . GLN A 1 923  ? 46.387 63.499  -21.162 1.00 11.05 ? 923  GLN A O   1 
ATOM   7264 C  CB  . GLN A 1 923  ? 45.950 60.395  -22.183 1.00 9.68  ? 923  GLN A CB  1 
ATOM   7265 C  CG  . GLN A 1 923  ? 45.634 58.938  -21.708 1.00 9.72  ? 923  GLN A CG  1 
ATOM   7266 C  CD  . GLN A 1 923  ? 46.590 57.950  -22.317 1.00 9.63  ? 923  GLN A CD  1 
ATOM   7267 O  OE1 . GLN A 1 923  ? 46.758 57.979  -23.533 1.00 13.39 ? 923  GLN A OE1 1 
ATOM   7268 N  NE2 . GLN A 1 923  ? 47.220 57.074  -21.501 1.00 10.14 ? 923  GLN A NE2 1 
ATOM   7269 N  N   . SER A 1 924  ? 45.061 63.423  -23.015 1.00 9.58  ? 924  SER A N   1 
ATOM   7270 C  CA  . SER A 1 924  ? 45.496 64.765  -23.433 1.00 8.47  ? 924  SER A CA  1 
ATOM   7271 C  C   . SER A 1 924  ? 45.129 65.862  -22.458 1.00 9.12  ? 924  SER A C   1 
ATOM   7272 O  O   . SER A 1 924  ? 45.782 66.885  -22.468 1.00 10.54 ? 924  SER A O   1 
ATOM   7273 C  CB  . SER A 1 924  ? 44.888 65.129  -24.818 1.00 11.52 ? 924  SER A CB  1 
ATOM   7274 O  OG  . SER A 1 924  ? 43.525 65.539  -24.703 1.00 12.74 ? 924  SER A OG  1 
ATOM   7275 N  N   . LEU A 1 925  ? 44.085 65.660  -21.641 1.00 10.18 ? 925  LEU A N   1 
ATOM   7276 C  CA  . LEU A 1 925  ? 43.596 66.627  -20.679 1.00 9.39  ? 925  LEU A CA  1 
ATOM   7277 C  C   . LEU A 1 925  ? 44.284 66.395  -19.336 1.00 10.12 ? 925  LEU A C   1 
ATOM   7278 O  O   . LEU A 1 925  ? 44.685 67.315  -18.677 1.00 10.77 ? 925  LEU A O   1 
ATOM   7279 C  CB  . LEU A 1 925  ? 42.072 66.480  -20.462 1.00 10.65 ? 925  LEU A CB  1 
ATOM   7280 C  CG  . LEU A 1 925  ? 41.190 66.636  -21.689 1.00 10.66 ? 925  LEU A CG  1 
ATOM   7281 C  CD1 . LEU A 1 925  ? 39.803 66.325  -21.276 1.00 10.85 ? 925  LEU A CD1 1 
ATOM   7282 C  CD2 . LEU A 1 925  ? 41.288 68.126  -22.222 1.00 8.90  ? 925  LEU A CD2 1 
ATOM   7283 N  N   . LEU A 1 926  ? 44.419 65.117  -18.987 1.00 9.88  ? 926  LEU A N   1 
ATOM   7284 C  CA  . LEU A 1 926  ? 45.042 64.849  -17.705 1.00 8.18  ? 926  LEU A CA  1 
ATOM   7285 C  C   . LEU A 1 926  ? 46.559 64.810  -17.655 1.00 8.59  ? 926  LEU A C   1 
ATOM   7286 O  O   . LEU A 1 926  ? 47.107 65.224  -16.650 1.00 10.65 ? 926  LEU A O   1 
ATOM   7287 C  CB  . LEU A 1 926  ? 44.447 63.544  -17.124 1.00 9.64  ? 926  LEU A CB  1 
ATOM   7288 C  CG  . LEU A 1 926  ? 42.922 63.626  -16.811 1.00 10.20 ? 926  LEU A CG  1 
ATOM   7289 C  CD1 . LEU A 1 926  ? 42.500 62.223  -16.301 1.00 11.42 ? 926  LEU A CD1 1 
ATOM   7290 C  CD2 . LEU A 1 926  ? 42.564 64.699  -15.773 1.00 11.60 ? 926  LEU A CD2 1 
ATOM   7291 N  N   . ASP A 1 927  ? 47.222 64.326  -18.709 1.00 10.09 ? 927  ASP A N   1 
ATOM   7292 C  CA  . ASP A 1 927  ? 48.681 64.242  -18.748 1.00 9.88  ? 927  ASP A CA  1 
ATOM   7293 C  C   . ASP A 1 927  ? 49.263 64.770  -20.060 1.00 9.64  ? 927  ASP A C   1 
ATOM   7294 O  O   . ASP A 1 927  ? 49.808 64.059  -20.837 1.00 9.11  ? 927  ASP A O   1 
ATOM   7295 C  CB  . ASP A 1 927  ? 49.097 62.807  -18.480 1.00 11.25 ? 927  ASP A CB  1 
ATOM   7296 C  CG  . ASP A 1 927  ? 48.748 62.378  -17.032 1.00 9.94  ? 927  ASP A CG  1 
ATOM   7297 O  OD1 . ASP A 1 927  ? 49.481 62.758  -16.069 1.00 8.80  ? 927  ASP A OD1 1 
ATOM   7298 O  OD2 . ASP A 1 927  ? 47.722 61.639  -16.872 1.00 10.52 ? 927  ASP A OD2 1 
ATOM   7299 N  N   . PRO A 1 928  ? 49.089 66.078  -20.280 1.00 11.92 ? 928  PRO A N   1 
ATOM   7300 C  CA  . PRO A 1 928  ? 49.599 66.709  -21.502 1.00 10.80 ? 928  PRO A CA  1 
ATOM   7301 C  C   . PRO A 1 928  ? 51.092 66.730  -21.472 1.00 12.63 ? 928  PRO A C   1 
ATOM   7302 O  O   . PRO A 1 928  ? 51.721 66.434  -20.453 1.00 11.57 ? 928  PRO A O   1 
ATOM   7303 C  CB  . PRO A 1 928  ? 49.057 68.154  -21.428 1.00 10.75 ? 928  PRO A CB  1 
ATOM   7304 C  CG  . PRO A 1 928  ? 48.971 68.440  -19.938 1.00 11.47 ? 928  PRO A CG  1 
ATOM   7305 C  CD  . PRO A 1 928  ? 48.513 67.064  -19.350 1.00 11.51 ? 928  PRO A CD  1 
ATOM   7306 N  N   . LEU A 1 929  ? 51.678 67.158  -22.582 1.00 10.64 ? 929  LEU A N   1 
ATOM   7307 C  CA  . LEU A 1 929  ? 53.128 67.319  -22.545 1.00 9.90  ? 929  LEU A CA  1 
ATOM   7308 C  C   . LEU A 1 929  ? 53.443 68.493  -21.632 1.00 9.61  ? 929  LEU A C   1 
ATOM   7309 O  O   . LEU A 1 929  ? 52.678 69.438  -21.482 1.00 11.69 ? 929  LEU A O   1 
ATOM   7310 C  CB  . LEU A 1 929  ? 53.648 67.721  -23.933 1.00 10.42 ? 929  LEU A CB  1 
ATOM   7311 C  CG  . LEU A 1 929  ? 53.500 66.697  -25.045 1.00 9.68  ? 929  LEU A CG  1 
ATOM   7312 C  CD1 . LEU A 1 929  ? 54.144 67.365  -26.307 1.00 10.19 ? 929  LEU A CD1 1 
ATOM   7313 C  CD2 . LEU A 1 929  ? 54.207 65.346  -24.805 1.00 9.50  ? 929  LEU A CD2 1 
ATOM   7314 N  N   . ASP A 1 930  ? 54.563 68.415  -20.912 1.00 9.56  ? 930  ASP A N   1 
ATOM   7315 C  CA  . ASP A 1 930  ? 55.010 69.526  -20.084 1.00 8.49  ? 930  ASP A CA  1 
ATOM   7316 C  C   . ASP A 1 930  ? 55.969 70.398  -20.928 1.00 9.29  ? 930  ASP A C   1 
ATOM   7317 O  O   . ASP A 1 930  ? 56.699 69.839  -21.780 1.00 11.56 ? 930  ASP A O   1 
ATOM   7318 C  CB  . ASP A 1 930  ? 55.773 68.975  -18.851 1.00 9.38  ? 930  ASP A CB  1 
ATOM   7319 C  CG  . ASP A 1 930  ? 54.951 67.926  -18.137 1.00 10.81 ? 930  ASP A CG  1 
ATOM   7320 O  OD1 . ASP A 1 930  ? 53.866 68.369  -17.649 1.00 13.20 ? 930  ASP A OD1 1 
ATOM   7321 O  OD2 . ASP A 1 930  ? 55.354 66.716  -18.108 1.00 11.51 ? 930  ASP A OD2 1 
ATOM   7322 N  N   . LYS A 1 931  ? 55.948 71.696  -20.690 1.00 10.63 ? 931  LYS A N   1 
ATOM   7323 C  CA  . LYS A 1 931  ? 56.718 72.644  -21.468 1.00 10.17 ? 931  LYS A CA  1 
ATOM   7324 C  C   . LYS A 1 931  ? 57.641 73.449  -20.610 1.00 10.69 ? 931  LYS A C   1 
ATOM   7325 O  O   . LYS A 1 931  ? 57.247 74.100  -19.625 1.00 11.70 ? 931  LYS A O   1 
ATOM   7326 C  CB  . LYS A 1 931  ? 55.762 73.594  -22.216 1.00 11.06 ? 931  LYS A CB  1 
ATOM   7327 C  CG  . LYS A 1 931  ? 54.933 72.927  -23.304 1.00 11.20 ? 931  LYS A CG  1 
ATOM   7328 C  CD  . LYS A 1 931  ? 54.013 73.946  -23.995 1.00 14.41 ? 931  LYS A CD  1 
ATOM   7329 C  CE  . LYS A 1 931  ? 53.178 74.713  -22.968 1.00 15.94 ? 931  LYS A CE  1 
ATOM   7330 N  NZ  . LYS A 1 931  ? 52.199 75.697  -23.501 1.00 16.77 ? 931  LYS A NZ  1 
ATOM   7331 N  N   . PHE A 1 932  ? 58.913 73.452  -21.055 1.00 10.09 ? 932  PHE A N   1 
ATOM   7332 C  CA  . PHE A 1 932  ? 59.955 74.166  -20.337 1.00 9.84  ? 932  PHE A CA  1 
ATOM   7333 C  C   . PHE A 1 932  ? 60.666 75.203  -21.222 1.00 8.14  ? 932  PHE A C   1 
ATOM   7334 O  O   . PHE A 1 932  ? 61.046 74.880  -22.337 1.00 10.01 ? 932  PHE A O   1 
ATOM   7335 C  CB  . PHE A 1 932  ? 61.035 73.169  -19.876 1.00 9.20  ? 932  PHE A CB  1 
ATOM   7336 C  CG  . PHE A 1 932  ? 60.509 72.078  -18.947 1.00 9.45  ? 932  PHE A CG  1 
ATOM   7337 C  CD1 . PHE A 1 932  ? 59.964 70.902  -19.449 1.00 9.87  ? 932  PHE A CD1 1 
ATOM   7338 C  CD2 . PHE A 1 932  ? 60.615 72.251  -17.572 1.00 12.38 ? 932  PHE A CD2 1 
ATOM   7339 C  CE1 . PHE A 1 932  ? 59.523 69.864  -18.550 1.00 10.44 ? 932  PHE A CE1 1 
ATOM   7340 C  CE2 . PHE A 1 932  ? 60.178 71.235  -16.673 1.00 14.30 ? 932  PHE A CE2 1 
ATOM   7341 C  CZ  . PHE A 1 932  ? 59.647 70.082  -17.172 1.00 12.08 ? 932  PHE A CZ  1 
ATOM   7342 N  N   . ILE A 1 933  ? 60.859 76.405  -20.732 1.00 8.43  ? 933  ILE A N   1 
ATOM   7343 C  CA  . ILE A 1 933  ? 61.564 77.480  -21.510 1.00 9.90  ? 933  ILE A CA  1 
ATOM   7344 C  C   . ILE A 1 933  ? 62.892 77.726  -20.810 1.00 11.44 ? 933  ILE A C   1 
ATOM   7345 O  O   . ILE A 1 933  ? 62.919 78.038  -19.586 1.00 9.84  ? 933  ILE A O   1 
ATOM   7346 C  CB  . ILE A 1 933  ? 60.774 78.806  -21.461 1.00 10.67 ? 933  ILE A CB  1 
ATOM   7347 C  CG1 . ILE A 1 933  ? 59.343 78.565  -21.946 1.00 10.86 ? 933  ILE A CG1 1 
ATOM   7348 C  CG2 . ILE A 1 933  ? 61.437 79.852  -22.378 1.00 11.72 ? 933  ILE A CG2 1 
ATOM   7349 C  CD1 . ILE A 1 933  ? 58.379 79.737  -21.697 1.00 10.12 ? 933  ILE A CD1 1 
ATOM   7350 N  N   . PHE A 1 934  ? 64.007 77.584  -21.542 1.00 10.77 ? 934  PHE A N   1 
ATOM   7351 C  CA  . PHE A 1 934  ? 65.305 77.827  -20.938 1.00 12.75 ? 934  PHE A CA  1 
ATOM   7352 C  C   . PHE A 1 934  ? 65.352 79.283  -20.459 1.00 14.10 ? 934  PHE A C   1 
ATOM   7353 O  O   . PHE A 1 934  ? 65.031 80.245  -21.206 1.00 13.52 ? 934  PHE A O   1 
ATOM   7354 C  CB  . PHE A 1 934  ? 66.410 77.581  -21.931 1.00 12.41 ? 934  PHE A CB  1 
ATOM   7355 C  CG  . PHE A 1 934  ? 67.774 77.620  -21.300 1.00 14.57 ? 934  PHE A CG  1 
ATOM   7356 C  CD1 . PHE A 1 934  ? 68.167 76.640  -20.398 1.00 13.88 ? 934  PHE A CD1 1 
ATOM   7357 C  CD2 . PHE A 1 934  ? 68.650 78.669  -21.572 1.00 15.97 ? 934  PHE A CD2 1 
ATOM   7358 C  CE1 . PHE A 1 934  ? 69.430 76.722  -19.770 1.00 16.80 ? 934  PHE A CE1 1 
ATOM   7359 C  CE2 . PHE A 1 934  ? 69.921 78.772  -20.959 1.00 16.24 ? 934  PHE A CE2 1 
ATOM   7360 C  CZ  . PHE A 1 934  ? 70.303 77.802  -20.062 1.00 17.68 ? 934  PHE A CZ  1 
ATOM   7361 N  N   . ALA A 1 935  ? 65.772 79.488  -19.224 1.00 13.83 ? 935  ALA A N   1 
ATOM   7362 C  CA  . ALA A 1 935  ? 65.715 80.826  -18.685 1.00 17.68 ? 935  ALA A CA  1 
ATOM   7363 C  C   . ALA A 1 935  ? 66.842 81.839  -18.942 1.00 21.62 ? 935  ALA A C   1 
ATOM   7364 O  O   . ALA A 1 935  ? 66.586 83.037  -18.874 1.00 23.36 ? 935  ALA A O   1 
ATOM   7365 C  CB  . ALA A 1 935  ? 65.420 80.779  -17.168 1.00 18.60 ? 935  ALA A CB  1 
ATOM   7366 N  N   . GLU A 1 936  ? 68.059 81.358  -19.215 1.00 21.06 ? 936  GLU A N   1 
ATOM   7367 C  CA  . GLU A 1 936  ? 69.215 82.228  -19.491 1.00 21.37 ? 936  GLU A CA  1 
ATOM   7368 C  C   . GLU A 1 936  ? 69.319 82.411  -21.014 1.00 20.63 ? 936  GLU A C   1 
ATOM   7369 O  O   . GLU A 1 936  ? 68.527 81.843  -21.793 1.00 21.05 ? 936  GLU A O   1 
ATOM   7370 C  CB  . GLU A 1 936  ? 70.496 81.544  -19.004 1.00 23.79 ? 936  GLU A CB  1 
ATOM   7371 C  CG  . GLU A 1 936  ? 70.699 81.519  -17.526 1.00 29.57 ? 936  GLU A CG  1 
ATOM   7372 C  CD  . GLU A 1 936  ? 69.697 82.356  -16.815 1.00 32.53 ? 936  GLU A CD  1 
ATOM   7373 O  OE1 . GLU A 1 936  ? 68.501 81.940  -16.783 1.00 37.81 ? 936  GLU A OE1 1 
ATOM   7374 O  OE2 . GLU A 1 936  ? 70.076 83.426  -16.290 1.00 34.97 ? 936  GLU A OE2 1 
ATOM   7375 N  N   . ASN A 1 937  ? 70.315 83.187  -21.460 1.00 20.81 ? 937  ASN A N   1 
ATOM   7376 C  CA  . ASN A 1 937  ? 70.476 83.403  -22.903 1.00 21.28 ? 937  ASN A CA  1 
ATOM   7377 C  C   . ASN A 1 937  ? 71.016 82.222  -23.643 1.00 21.08 ? 937  ASN A C   1 
ATOM   7378 O  O   . ASN A 1 937  ? 70.605 81.917  -24.761 1.00 22.05 ? 937  ASN A O   1 
ATOM   7379 C  CB  . ASN A 1 937  ? 71.422 84.567  -23.169 1.00 22.47 ? 937  ASN A CB  1 
ATOM   7380 C  CG  . ASN A 1 937  ? 70.799 85.896  -22.826 1.00 24.46 ? 937  ASN A CG  1 
ATOM   7381 O  OD1 . ASN A 1 937  ? 69.572 86.000  -22.640 1.00 26.44 ? 937  ASN A OD1 1 
ATOM   7382 N  ND2 . ASN A 1 937  ? 71.624 86.926  -22.735 1.00 27.37 ? 937  ASN A ND2 1 
ATOM   7383 N  N   . GLU A 1 938  ? 71.967 81.555  -23.015 1.00 20.43 ? 938  GLU A N   1 
ATOM   7384 C  CA  . GLU A 1 938  ? 72.600 80.431  -23.666 1.00 21.81 ? 938  GLU A CA  1 
ATOM   7385 C  C   . GLU A 1 938  ? 72.720 79.156  -22.814 1.00 19.36 ? 938  GLU A C   1 
ATOM   7386 O  O   . GLU A 1 938  ? 73.252 79.228  -21.709 1.00 20.35 ? 938  GLU A O   1 
ATOM   7387 C  CB  . GLU A 1 938  ? 73.989 80.860  -24.128 1.00 23.19 ? 938  GLU A CB  1 
ATOM   7388 C  CG  . GLU A 1 938  ? 74.659 79.771  -24.901 1.00 29.08 ? 938  GLU A CG  1 
ATOM   7389 C  CD  . GLU A 1 938  ? 76.080 80.124  -25.218 1.00 32.34 ? 938  GLU A CD  1 
ATOM   7390 O  OE1 . GLU A 1 938  ? 76.624 81.058  -24.561 1.00 33.91 ? 938  GLU A OE1 1 
ATOM   7391 O  OE2 . GLU A 1 938  ? 76.647 79.445  -26.107 1.00 33.79 ? 938  GLU A OE2 1 
ATOM   7392 N  N   . TRP A 1 939  ? 72.291 78.018  -23.381 1.00 18.48 ? 939  TRP A N   1 
ATOM   7393 C  CA  . TRP A 1 939  ? 72.334 76.715  -22.696 1.00 18.19 ? 939  TRP A CA  1 
ATOM   7394 C  C   . TRP A 1 939  ? 73.517 75.964  -23.267 1.00 17.58 ? 939  TRP A C   1 
ATOM   7395 O  O   . TRP A 1 939  ? 73.424 75.406  -24.335 1.00 19.79 ? 939  TRP A O   1 
ATOM   7396 C  CB  . TRP A 1 939  ? 71.014 75.952  -22.954 1.00 17.07 ? 939  TRP A CB  1 
ATOM   7397 C  CG  . TRP A 1 939  ? 70.914 74.529  -22.392 1.00 14.13 ? 939  TRP A CG  1 
ATOM   7398 C  CD1 . TRP A 1 939  ? 71.826 73.861  -21.586 1.00 14.47 ? 939  TRP A CD1 1 
ATOM   7399 C  CD2 . TRP A 1 939  ? 69.848 73.608  -22.633 1.00 15.67 ? 939  TRP A CD2 1 
ATOM   7400 N  NE1 . TRP A 1 939  ? 71.369 72.583  -21.325 1.00 17.18 ? 939  TRP A NE1 1 
ATOM   7401 C  CE2 . TRP A 1 939  ? 70.161 72.398  -21.946 1.00 14.44 ? 939  TRP A CE2 1 
ATOM   7402 C  CE3 . TRP A 1 939  ? 68.651 73.688  -23.368 1.00 13.77 ? 939  TRP A CE3 1 
ATOM   7403 C  CZ2 . TRP A 1 939  ? 69.324 71.272  -21.966 1.00 15.34 ? 939  TRP A CZ2 1 
ATOM   7404 C  CZ3 . TRP A 1 939  ? 67.801 72.560  -23.397 1.00 13.63 ? 939  TRP A CZ3 1 
ATOM   7405 C  CH2 . TRP A 1 939  ? 68.145 71.369  -22.698 1.00 12.55 ? 939  TRP A CH2 1 
ATOM   7406 N  N   . ILE A 1 940  ? 74.635 75.954  -22.551 1.00 19.34 ? 940  ILE A N   1 
ATOM   7407 C  CA  . ILE A 1 940  ? 75.839 75.266  -23.065 1.00 21.13 ? 940  ILE A CA  1 
ATOM   7408 C  C   . ILE A 1 940  ? 75.727 73.777  -22.761 1.00 20.15 ? 940  ILE A C   1 
ATOM   7409 O  O   . ILE A 1 940  ? 75.314 73.416  -21.666 1.00 21.97 ? 940  ILE A O   1 
ATOM   7410 C  CB  . ILE A 1 940  ? 77.117 75.841  -22.398 1.00 22.31 ? 940  ILE A CB  1 
ATOM   7411 C  CG1 . ILE A 1 940  ? 77.324 77.291  -22.830 1.00 24.01 ? 940  ILE A CG1 1 
ATOM   7412 C  CG2 . ILE A 1 940  ? 78.365 75.056  -22.765 1.00 23.79 ? 940  ILE A CG2 1 
ATOM   7413 C  CD1 . ILE A 1 940  ? 76.975 78.321  -21.690 1.00 25.02 ? 940  ILE A CD1 1 
ATOM   7414 N  N   . GLY A 1 941  ? 76.016 72.942  -23.755 1.00 20.89 ? 941  GLY A N   1 
ATOM   7415 C  CA  . GLY A 1 941  ? 75.952 71.500  -23.564 1.00 19.85 ? 941  GLY A CA  1 
ATOM   7416 C  C   . GLY A 1 941  ? 74.581 70.892  -23.856 1.00 20.13 ? 941  GLY A C   1 
ATOM   7417 O  O   . GLY A 1 941  ? 74.358 69.688  -23.661 1.00 19.78 ? 941  GLY A O   1 
ATOM   7418 N  N   . ALA A 1 942  ? 73.675 71.699  -24.406 1.00 18.59 ? 942  ALA A N   1 
ATOM   7419 C  CA  . ALA A 1 942  ? 72.336 71.218  -24.732 1.00 17.94 ? 942  ALA A CA  1 
ATOM   7420 C  C   . ALA A 1 942  ? 72.273 70.011  -25.610 1.00 18.96 ? 942  ALA A C   1 
ATOM   7421 O  O   . ALA A 1 942  ? 73.026 69.906  -26.584 1.00 19.32 ? 942  ALA A O   1 
ATOM   7422 C  CB  . ALA A 1 942  ? 71.534 72.368  -25.367 1.00 17.56 ? 942  ALA A CB  1 
ATOM   7423 N  N   . GLN A 1 943  ? 71.335 69.120  -25.320 1.00 19.31 ? 943  GLN A N   1 
ATOM   7424 C  CA  . GLN A 1 943  ? 71.129 67.904  -26.073 1.00 19.43 ? 943  GLN A CA  1 
ATOM   7425 C  C   . GLN A 1 943  ? 69.723 67.877  -26.654 1.00 17.50 ? 943  GLN A C   1 
ATOM   7426 O  O   . GLN A 1 943  ? 68.828 68.521  -26.118 1.00 19.21 ? 943  GLN A O   1 
ATOM   7427 C  CB  . GLN A 1 943  ? 71.380 66.720  -25.150 1.00 22.41 ? 943  GLN A CB  1 
ATOM   7428 C  CG  . GLN A 1 943  ? 72.718 66.845  -24.448 1.00 26.01 ? 943  GLN A CG  1 
ATOM   7429 C  CD  . GLN A 1 943  ? 73.092 65.543  -23.796 1.00 28.09 ? 943  GLN A CD  1 
ATOM   7430 O  OE1 . GLN A 1 943  ? 72.280 64.971  -23.027 1.00 30.84 ? 943  GLN A OE1 1 
ATOM   7431 N  NE2 . GLN A 1 943  ? 74.300 65.046  -24.087 1.00 29.15 ? 943  GLN A NE2 1 
ATOM   7432 N  N   . GLY A 1 944  ? 69.518 67.140  -27.744 1.00 18.19 ? 944  GLY A N   1 
ATOM   7433 C  CA  . GLY A 1 944  ? 68.231 67.197  -28.419 1.00 18.61 ? 944  GLY A CA  1 
ATOM   7434 C  C   . GLY A 1 944  ? 67.102 66.335  -27.955 1.00 18.48 ? 944  GLY A C   1 
ATOM   7435 O  O   . GLY A 1 944  ? 65.959 66.685  -28.160 1.00 19.52 ? 944  GLY A O   1 
ATOM   7436 N  N   . GLN A 1 945  ? 67.411 65.231  -27.294 1.00 18.33 ? 945  GLN A N   1 
ATOM   7437 C  CA  . GLN A 1 945  ? 66.347 64.296  -26.920 1.00 17.23 ? 945  GLN A CA  1 
ATOM   7438 C  C   . GLN A 1 945  ? 66.809 63.394  -25.772 1.00 17.44 ? 945  GLN A C   1 
ATOM   7439 O  O   . GLN A 1 945  ? 67.999 63.172  -25.578 1.00 17.99 ? 945  GLN A O   1 
ATOM   7440 C  CB  . GLN A 1 945  ? 66.050 63.449  -28.154 1.00 19.30 ? 945  GLN A CB  1 
ATOM   7441 C  CG  . GLN A 1 945  ? 64.866 62.487  -28.123 1.00 22.29 ? 945  GLN A CG  1 
ATOM   7442 C  CD  . GLN A 1 945  ? 64.764 61.638  -29.413 1.00 23.16 ? 945  GLN A CD  1 
ATOM   7443 O  OE1 . GLN A 1 945  ? 63.984 61.964  -30.314 1.00 25.50 ? 945  GLN A OE1 1 
ATOM   7444 N  NE2 . GLN A 1 945  ? 65.549 60.553  -29.499 1.00 23.57 ? 945  GLN A NE2 1 
ATOM   7445 N  N   . PHE A 1 946  ? 65.848 62.878  -25.019 1.00 14.81 ? 946  PHE A N   1 
ATOM   7446 C  CA  . PHE A 1 946  ? 66.140 61.930  -23.949 1.00 14.38 ? 946  PHE A CA  1 
ATOM   7447 C  C   . PHE A 1 946  ? 65.057 60.883  -24.072 1.00 13.88 ? 946  PHE A C   1 
ATOM   7448 O  O   . PHE A 1 946  ? 63.879 61.228  -24.296 1.00 13.03 ? 946  PHE A O   1 
ATOM   7449 C  CB  . PHE A 1 946  ? 66.117 62.593  -22.554 1.00 14.46 ? 946  PHE A CB  1 
ATOM   7450 C  CG  . PHE A 1 946  ? 66.022 61.588  -21.407 1.00 15.58 ? 946  PHE A CG  1 
ATOM   7451 C  CD1 . PHE A 1 946  ? 67.088 60.746  -21.114 1.00 16.01 ? 946  PHE A CD1 1 
ATOM   7452 C  CD2 . PHE A 1 946  ? 64.819 61.433  -20.708 1.00 16.98 ? 946  PHE A CD2 1 
ATOM   7453 C  CE1 . PHE A 1 946  ? 66.955 59.734  -20.120 1.00 17.65 ? 946  PHE A CE1 1 
ATOM   7454 C  CE2 . PHE A 1 946  ? 64.669 60.445  -19.735 1.00 16.22 ? 946  PHE A CE2 1 
ATOM   7455 C  CZ  . PHE A 1 946  ? 65.730 59.589  -19.433 1.00 15.26 ? 946  PHE A CZ  1 
ATOM   7456 N  N   . GLY A 1 947  ? 65.421 59.609  -23.990 1.00 13.96 ? 947  GLY A N   1 
ATOM   7457 C  CA  . GLY A 1 947  ? 64.405 58.581  -24.002 1.00 13.71 ? 947  GLY A CA  1 
ATOM   7458 C  C   . GLY A 1 947  ? 64.085 57.965  -25.350 1.00 15.81 ? 947  GLY A C   1 
ATOM   7459 O  O   . GLY A 1 947  ? 63.165 57.140  -25.475 1.00 14.46 ? 947  GLY A O   1 
ATOM   7460 N  N   . GLY A 1 948  ? 64.859 58.320  -26.370 1.00 16.03 ? 948  GLY A N   1 
ATOM   7461 C  CA  . GLY A 1 948  ? 64.605 57.729  -27.667 1.00 17.86 ? 948  GLY A CA  1 
ATOM   7462 C  C   . GLY A 1 948  ? 64.648 56.212  -27.663 1.00 17.24 ? 948  GLY A C   1 
ATOM   7463 O  O   . GLY A 1 948  ? 64.013 55.586  -28.495 1.00 19.61 ? 948  GLY A O   1 
ATOM   7464 N  N   . ASP A 1 949  ? 65.375 55.607  -26.724 1.00 18.26 ? 949  ASP A N   1 
ATOM   7465 C  CA  . ASP A 1 949  ? 65.430 54.165  -26.676 1.00 19.46 ? 949  ASP A CA  1 
ATOM   7466 C  C   . ASP A 1 949  ? 64.419 53.531  -25.707 1.00 18.77 ? 949  ASP A C   1 
ATOM   7467 O  O   . ASP A 1 949  ? 64.421 52.316  -25.484 1.00 17.79 ? 949  ASP A O   1 
ATOM   7468 C  CB  . ASP A 1 949  ? 66.856 53.677  -26.376 1.00 21.89 ? 949  ASP A CB  1 
ATOM   7469 C  CG  . ASP A 1 949  ? 67.375 54.155  -25.029 1.00 23.39 ? 949  ASP A CG  1 
ATOM   7470 O  OD1 . ASP A 1 949  ? 66.721 54.970  -24.340 1.00 25.23 ? 949  ASP A OD1 1 
ATOM   7471 O  OD2 . ASP A 1 949  ? 68.465 53.697  -24.633 1.00 29.03 ? 949  ASP A OD2 1 
ATOM   7472 N  N   . HIS A 1 950  ? 63.544 54.347  -25.122 1.00 17.45 ? 950  HIS A N   1 
ATOM   7473 C  CA  . HIS A 1 950  ? 62.513 53.782  -24.249 1.00 16.75 ? 950  HIS A CA  1 
ATOM   7474 C  C   . HIS A 1 950  ? 61.464 53.026  -25.061 1.00 17.28 ? 950  HIS A C   1 
ATOM   7475 O  O   . HIS A 1 950  ? 61.064 53.453  -26.143 1.00 16.83 ? 950  HIS A O   1 
ATOM   7476 C  CB  . HIS A 1 950  ? 61.812 54.886  -23.473 1.00 14.78 ? 950  HIS A CB  1 
ATOM   7477 C  CG  . HIS A 1 950  ? 62.685 55.591  -22.492 1.00 13.24 ? 950  HIS A CG  1 
ATOM   7478 N  ND1 . HIS A 1 950  ? 62.314 56.772  -21.883 1.00 12.23 ? 950  HIS A ND1 1 
ATOM   7479 C  CD2 . HIS A 1 950  ? 63.927 55.293  -22.012 1.00 13.42 ? 950  HIS A CD2 1 
ATOM   7480 C  CE1 . HIS A 1 950  ? 63.274 57.166  -21.070 1.00 15.28 ? 950  HIS A CE1 1 
ATOM   7481 N  NE2 . HIS A 1 950  ? 64.263 56.286  -21.127 1.00 13.55 ? 950  HIS A NE2 1 
ATOM   7482 N  N   . PRO A 1 951  ? 60.987 51.878  -24.555 1.00 16.55 ? 951  PRO A N   1 
ATOM   7483 C  CA  . PRO A 1 951  ? 59.987 51.180  -25.348 1.00 15.50 ? 951  PRO A CA  1 
ATOM   7484 C  C   . PRO A 1 951  ? 58.684 51.971  -25.442 1.00 14.24 ? 951  PRO A C   1 
ATOM   7485 O  O   . PRO A 1 951  ? 58.282 52.634  -24.470 1.00 15.47 ? 951  PRO A O   1 
ATOM   7486 C  CB  . PRO A 1 951  ? 59.762 49.841  -24.603 1.00 17.98 ? 951  PRO A CB  1 
ATOM   7487 C  CG  . PRO A 1 951  ? 60.977 49.682  -23.749 1.00 17.99 ? 951  PRO A CG  1 
ATOM   7488 C  CD  . PRO A 1 951  ? 61.376 51.103  -23.357 1.00 16.43 ? 951  PRO A CD  1 
ATOM   7489 N  N   . SER A 1 952  ? 58.039 51.862  -26.600 1.00 14.25 ? 952  SER A N   1 
ATOM   7490 C  CA  . SER A 1 952  ? 56.762 52.535  -26.836 1.00 13.70 ? 952  SER A CA  1 
ATOM   7491 C  C   . SER A 1 952  ? 55.713 51.445  -26.672 1.00 12.26 ? 952  SER A C   1 
ATOM   7492 O  O   . SER A 1 952  ? 55.453 50.639  -27.556 1.00 15.39 ? 952  SER A O   1 
ATOM   7493 C  CB  . SER A 1 952  ? 56.750 53.108  -28.239 1.00 13.42 ? 952  SER A CB  1 
ATOM   7494 O  OG  . SER A 1 952  ? 55.695 54.027  -28.396 1.00 13.43 ? 952  SER A OG  1 
ATOM   7495 N  N   . ALA A 1 953  ? 55.113 51.448  -25.482 1.00 14.38 ? 953  ALA A N   1 
ATOM   7496 C  CA  . ALA A 1 953  ? 54.151 50.437  -25.071 1.00 13.42 ? 953  ALA A CA  1 
ATOM   7497 C  C   . ALA A 1 953  ? 52.784 50.572  -25.707 1.00 12.97 ? 953  ALA A C   1 
ATOM   7498 O  O   . ALA A 1 953  ? 52.403 51.667  -26.185 1.00 12.77 ? 953  ALA A O   1 
ATOM   7499 C  CB  . ALA A 1 953  ? 54.053 50.511  -23.530 1.00 14.54 ? 953  ALA A CB  1 
ATOM   7500 N  N   . ARG A 1 954  ? 52.028 49.481  -25.685 1.00 12.75 ? 954  ARG A N   1 
ATOM   7501 C  CA  . ARG A 1 954  ? 50.691 49.446  -26.268 1.00 13.32 ? 954  ARG A CA  1 
ATOM   7502 C  C   . ARG A 1 954  ? 49.870 50.573  -25.664 1.00 12.60 ? 954  ARG A C   1 
ATOM   7503 O  O   . ARG A 1 954  ? 49.971 50.893  -24.480 1.00 12.29 ? 954  ARG A O   1 
ATOM   7504 C  CB  . ARG A 1 954  ? 50.001 48.079  -26.088 1.00 14.64 ? 954  ARG A CB  1 
ATOM   7505 C  CG  . ARG A 1 954  ? 48.720 47.974  -26.928 1.00 19.80 ? 954  ARG A CG  1 
ATOM   7506 C  CD  . ARG A 1 954  ? 48.341 46.536  -27.261 1.00 24.24 ? 954  ARG A CD  1 
ATOM   7507 N  NE  . ARG A 1 954  ? 47.708 45.819  -26.162 1.00 28.24 ? 954  ARG A NE  1 
ATOM   7508 C  CZ  . ARG A 1 954  ? 46.403 45.608  -26.052 1.00 29.57 ? 954  ARG A CZ  1 
ATOM   7509 N  NH1 . ARG A 1 954  ? 45.570 46.086  -26.981 1.00 32.01 ? 954  ARG A NH1 1 
ATOM   7510 N  NH2 . ARG A 1 954  ? 45.923 44.858  -25.056 1.00 29.45 ? 954  ARG A NH2 1 
ATOM   7511 N  N   . GLU A 1 955  ? 49.001 51.158  -26.478 1.00 12.37 ? 955  GLU A N   1 
ATOM   7512 C  CA  . GLU A 1 955  ? 48.281 52.366  -26.078 1.00 11.23 ? 955  GLU A CA  1 
ATOM   7513 C  C   . GLU A 1 955  ? 47.391 52.285  -24.822 1.00 11.06 ? 955  GLU A C   1 
ATOM   7514 O  O   . GLU A 1 955  ? 47.127 53.324  -24.218 1.00 12.29 ? 955  GLU A O   1 
ATOM   7515 C  CB  . GLU A 1 955  ? 47.413 52.849  -27.233 1.00 15.26 ? 955  GLU A CB  1 
ATOM   7516 C  CG  . GLU A 1 955  ? 46.254 51.907  -27.571 1.00 18.16 ? 955  GLU A CG  1 
ATOM   7517 C  CD  . GLU A 1 955  ? 45.315 52.445  -28.649 1.00 20.85 ? 955  GLU A CD  1 
ATOM   7518 O  OE1 . GLU A 1 955  ? 45.125 53.678  -28.752 1.00 20.42 ? 955  GLU A OE1 1 
ATOM   7519 O  OE2 . GLU A 1 955  ? 44.720 51.613  -29.380 1.00 20.19 ? 955  GLU A OE2 1 
ATOM   7520 N  N   . ASP A 1 956  ? 46.926 51.079  -24.471 1.00 10.92 ? 956  ASP A N   1 
ATOM   7521 C  CA  . ASP A 1 956  ? 46.049 50.945  -23.306 1.00 10.93 ? 956  ASP A CA  1 
ATOM   7522 C  C   . ASP A 1 956  ? 46.884 50.817  -22.017 1.00 11.41 ? 956  ASP A C   1 
ATOM   7523 O  O   . ASP A 1 956  ? 46.331 50.742  -20.898 1.00 11.65 ? 956  ASP A O   1 
ATOM   7524 C  CB  . ASP A 1 956  ? 45.094 49.727  -23.454 1.00 12.34 ? 956  ASP A CB  1 
ATOM   7525 C  CG  . ASP A 1 956  ? 45.786 48.419  -23.768 1.00 14.10 ? 956  ASP A CG  1 
ATOM   7526 O  OD1 . ASP A 1 956  ? 47.003 48.336  -23.947 1.00 15.89 ? 956  ASP A OD1 1 
ATOM   7527 O  OD2 . ASP A 1 956  ? 45.051 47.439  -23.861 1.00 14.57 ? 956  ASP A OD2 1 
ATOM   7528 N  N   . LEU A 1 957  ? 48.216 50.813  -22.150 1.00 11.69 ? 957  LEU A N   1 
ATOM   7529 C  CA  . LEU A 1 957  ? 49.055 50.651  -20.965 1.00 11.74 ? 957  LEU A CA  1 
ATOM   7530 C  C   . LEU A 1 957  ? 49.662 51.967  -20.504 1.00 9.69  ? 957  LEU A C   1 
ATOM   7531 O  O   . LEU A 1 957  ? 50.139 52.789  -21.318 1.00 10.62 ? 957  LEU A O   1 
ATOM   7532 C  CB  . LEU A 1 957  ? 50.188 49.663  -21.251 1.00 11.09 ? 957  LEU A CB  1 
ATOM   7533 C  CG  . LEU A 1 957  ? 51.048 49.111  -20.105 1.00 15.37 ? 957  LEU A CG  1 
ATOM   7534 C  CD1 . LEU A 1 957  ? 50.148 48.140  -19.252 1.00 17.05 ? 957  LEU A CD1 1 
ATOM   7535 C  CD2 . LEU A 1 957  ? 52.289 48.296  -20.670 1.00 16.69 ? 957  LEU A CD2 1 
ATOM   7536 N  N   . ASP A 1 958  ? 49.719 52.175  -19.194 1.00 9.17  ? 958  ASP A N   1 
ATOM   7537 C  CA  . ASP A 1 958  ? 50.327 53.391  -18.665 1.00 8.49  ? 958  ASP A CA  1 
ATOM   7538 C  C   . ASP A 1 958  ? 51.243 53.075  -17.478 1.00 9.68  ? 958  ASP A C   1 
ATOM   7539 O  O   . ASP A 1 958  ? 50.979 52.120  -16.720 1.00 8.83  ? 958  ASP A O   1 
ATOM   7540 C  CB  . ASP A 1 958  ? 49.224 54.403  -18.233 1.00 9.49  ? 958  ASP A CB  1 
ATOM   7541 C  CG  . ASP A 1 958  ? 49.771 55.811  -17.936 1.00 11.16 ? 958  ASP A CG  1 
ATOM   7542 O  OD1 . ASP A 1 958  ? 50.862 56.136  -18.442 1.00 9.92  ? 958  ASP A OD1 1 
ATOM   7543 O  OD2 . ASP A 1 958  ? 49.113 56.623  -17.199 1.00 11.69 ? 958  ASP A OD2 1 
ATOM   7544 N  N   . VAL A 1 959  ? 52.288 53.891  -17.313 1.00 7.35  ? 959  VAL A N   1 
ATOM   7545 C  CA  . VAL A 1 959  ? 53.174 53.817  -16.153 1.00 9.00  ? 959  VAL A CA  1 
ATOM   7546 C  C   . VAL A 1 959  ? 52.629 54.944  -15.266 1.00 9.12  ? 959  VAL A C   1 
ATOM   7547 O  O   . VAL A 1 959  ? 53.021 56.122  -15.362 1.00 9.32  ? 959  VAL A O   1 
ATOM   7548 C  CB  . VAL A 1 959  ? 54.636 54.070  -16.549 1.00 10.07 ? 959  VAL A CB  1 
ATOM   7549 C  CG1 . VAL A 1 959  ? 55.501 54.228  -15.285 1.00 9.76  ? 959  VAL A CG1 1 
ATOM   7550 C  CG2 . VAL A 1 959  ? 55.184 52.898  -17.370 1.00 10.44 ? 959  VAL A CG2 1 
ATOM   7551 N  N   . SER A 1 960  ? 51.634 54.590  -14.450 1.00 9.17  ? 960  SER A N   1 
ATOM   7552 C  CA  . SER A 1 960  ? 50.935 55.568  -13.603 1.00 9.82  ? 960  SER A CA  1 
ATOM   7553 C  C   . SER A 1 960  ? 51.849 56.317  -12.637 1.00 9.01  ? 960  SER A C   1 
ATOM   7554 O  O   . SER A 1 960  ? 51.699 57.512  -12.411 1.00 8.05  ? 960  SER A O   1 
ATOM   7555 C  CB  . SER A 1 960  ? 49.806 54.876  -12.818 1.00 7.95  ? 960  SER A CB  1 
ATOM   7556 O  OG  . SER A 1 960  ? 49.000 54.106  -13.666 1.00 11.09 ? 960  SER A OG  1 
ATOM   7557 N  N   . VAL A 1 961  ? 52.832 55.594  -12.078 1.00 8.09  ? 961  VAL A N   1 
ATOM   7558 C  CA  . VAL A 1 961  ? 53.813 56.098  -11.136 1.00 10.22 ? 961  VAL A CA  1 
ATOM   7559 C  C   . VAL A 1 961  ? 55.183 55.482  -11.458 1.00 8.49  ? 961  VAL A C   1 
ATOM   7560 O  O   . VAL A 1 961  ? 55.311 54.269  -11.777 1.00 9.46  ? 961  VAL A O   1 
ATOM   7561 C  CB  . VAL A 1 961  ? 53.470 55.595  -9.734  1.00 9.43  ? 961  VAL A CB  1 
ATOM   7562 C  CG1 . VAL A 1 961  ? 54.544 56.054  -8.692  1.00 10.71 ? 961  VAL A CG1 1 
ATOM   7563 C  CG2 . VAL A 1 961  ? 52.076 56.109  -9.317  1.00 7.72  ? 961  VAL A CG2 1 
ATOM   7564 N  N   . MET A 1 962  ? 56.202 56.328  -11.392 1.00 9.30  ? 962  MET A N   1 
ATOM   7565 C  CA  . MET A 1 962  ? 57.596 55.903  -11.448 1.00 6.55  ? 962  MET A CA  1 
ATOM   7566 C  C   . MET A 1 962  ? 58.133 56.741  -10.283 1.00 7.81  ? 962  MET A C   1 
ATOM   7567 O  O   . MET A 1 962  ? 58.065 58.004  -10.281 1.00 8.07  ? 962  MET A O   1 
ATOM   7568 C  CB  . MET A 1 962  ? 58.288 56.278  -12.767 1.00 8.46  ? 962  MET A CB  1 
ATOM   7569 C  CG  . MET A 1 962  ? 59.791 56.028  -12.665 1.00 10.06 ? 962  MET A CG  1 
ATOM   7570 S  SD  . MET A 1 962  ? 60.588 56.350  -14.308 1.00 10.52 ? 962  MET A SD  1 
ATOM   7571 C  CE  . MET A 1 962  ? 62.353 55.850  -14.012 1.00 8.79  ? 962  MET A CE  1 
ATOM   7572 N  N   . ARG A 1 963  ? 58.735 56.069  -9.295  1.00 9.48  ? 963  ARG A N   1 
ATOM   7573 C  CA  . ARG A 1 963  ? 59.233 56.716  -8.099  1.00 8.44  ? 963  ARG A CA  1 
ATOM   7574 C  C   . ARG A 1 963  ? 60.499 56.059  -7.555  1.00 8.78  ? 963  ARG A C   1 
ATOM   7575 O  O   . ARG A 1 963  ? 60.465 54.879  -7.230  1.00 9.68  ? 963  ARG A O   1 
ATOM   7576 C  CB  . ARG A 1 963  ? 58.168 56.666  -6.934  1.00 6.66  ? 963  ARG A CB  1 
ATOM   7577 C  CG  . ARG A 1 963  ? 58.661 57.273  -5.627  1.00 11.64 ? 963  ARG A CG  1 
ATOM   7578 C  CD  . ARG A 1 963  ? 57.586 57.216  -4.470  1.00 12.38 ? 963  ARG A CD  1 
ATOM   7579 N  NE  . ARG A 1 963  ? 56.354 57.894  -4.919  1.00 11.08 ? 963  ARG A NE  1 
ATOM   7580 C  CZ  . ARG A 1 963  ? 55.134 57.373  -4.884  1.00 10.28 ? 963  ARG A CZ  1 
ATOM   7581 N  NH1 . ARG A 1 963  ? 54.871 56.164  -4.388  1.00 10.10 ? 963  ARG A NH1 1 
ATOM   7582 N  NH2 . ARG A 1 963  ? 54.181 58.043  -5.511  1.00 9.08  ? 963  ARG A NH2 1 
ATOM   7583 N  N   . ARG A 1 964  ? 61.619 56.813  -7.468  1.00 10.35 ? 964  ARG A N   1 
ATOM   7584 C  CA  . ARG A 1 964  ? 62.842 56.218  -6.834  1.00 9.60  ? 964  ARG A CA  1 
ATOM   7585 C  C   . ARG A 1 964  ? 62.519 56.161  -5.331  1.00 10.42 ? 964  ARG A C   1 
ATOM   7586 O  O   . ARG A 1 964  ? 62.071 57.109  -4.712  1.00 10.09 ? 964  ARG A O   1 
ATOM   7587 C  CB  . ARG A 1 964  ? 64.041 57.134  -7.054  1.00 10.88 ? 964  ARG A CB  1 
ATOM   7588 C  CG  . ARG A 1 964  ? 65.316 56.404  -6.595  1.00 10.06 ? 964  ARG A CG  1 
ATOM   7589 C  CD  . ARG A 1 964  ? 66.641 57.083  -7.013  1.00 8.71  ? 964  ARG A CD  1 
ATOM   7590 N  NE  . ARG A 1 964  ? 66.834 56.909  -8.420  1.00 11.59 ? 964  ARG A NE  1 
ATOM   7591 C  CZ  . ARG A 1 964  ? 67.706 56.108  -9.013  1.00 12.61 ? 964  ARG A CZ  1 
ATOM   7592 N  NH1 . ARG A 1 964  ? 68.559 55.324  -8.316  1.00 15.69 ? 964  ARG A NH1 1 
ATOM   7593 N  NH2 . ARG A 1 964  ? 67.719 56.056  -10.347 1.00 12.35 ? 964  ARG A NH2 1 
ATOM   7594 N  N   . LEU A 1 965  ? 62.739 54.990  -4.749  1.00 10.73 ? 965  LEU A N   1 
ATOM   7595 C  CA  . LEU A 1 965  ? 62.371 54.745  -3.340  1.00 10.09 ? 965  LEU A CA  1 
ATOM   7596 C  C   . LEU A 1 965  ? 63.516 54.860  -2.294  1.00 11.95 ? 965  LEU A C   1 
ATOM   7597 O  O   . LEU A 1 965  ? 63.291 54.837  -1.080  1.00 12.96 ? 965  LEU A O   1 
ATOM   7598 C  CB  . LEU A 1 965  ? 61.763 53.353  -3.207  1.00 11.49 ? 965  LEU A CB  1 
ATOM   7599 C  CG  . LEU A 1 965  ? 60.594 53.078  -4.163  1.00 10.45 ? 965  LEU A CG  1 
ATOM   7600 C  CD1 . LEU A 1 965  ? 60.191 51.593  -4.129  1.00 10.84 ? 965  LEU A CD1 1 
ATOM   7601 C  CD2 . LEU A 1 965  ? 59.398 53.954  -3.763  1.00 13.07 ? 965  LEU A CD2 1 
ATOM   7602 N  N   . THR A 1 966  ? 64.727 55.063  -2.824  1.00 11.50 ? 966  THR A N   1 
ATOM   7603 C  CA  . THR A 1 966  ? 65.939 55.160  -2.024  1.00 11.35 ? 966  THR A CA  1 
ATOM   7604 C  C   . THR A 1 966  ? 66.659 56.457  -2.220  1.00 12.29 ? 966  THR A C   1 
ATOM   7605 O  O   . THR A 1 966  ? 66.690 56.993  -3.326  1.00 13.11 ? 966  THR A O   1 
ATOM   7606 C  CB  . THR A 1 966  ? 66.994 54.041  -2.420  1.00 9.57  ? 966  THR A CB  1 
ATOM   7607 O  OG1 . THR A 1 966  ? 67.064 53.880  -3.851  1.00 11.80 ? 966  THR A OG1 1 
ATOM   7608 C  CG2 . THR A 1 966  ? 66.568 52.667  -1.823  1.00 11.65 ? 966  THR A CG2 1 
ATOM   7609 N  N   . LYS A 1 967  ? 67.291 56.889  -1.140  1.00 12.71 ? 967  LYS A N   1 
ATOM   7610 C  CA  . LYS A 1 967  ? 68.143 58.054  -1.165  1.00 14.97 ? 967  LYS A CA  1 
ATOM   7611 C  C   . LYS A 1 967  ? 69.514 57.644  -1.742  1.00 14.21 ? 967  LYS A C   1 
ATOM   7612 O  O   . LYS A 1 967  ? 69.808 56.458  -1.939  1.00 13.26 ? 967  LYS A O   1 
ATOM   7613 C  CB  . LYS A 1 967  ? 68.290 58.637  0.238   1.00 16.37 ? 967  LYS A CB  1 
ATOM   7614 C  CG  . LYS A 1 967  ? 67.037 59.358  0.711   1.00 21.93 ? 967  LYS A CG  1 
ATOM   7615 C  CD  . LYS A 1 967  ? 67.216 59.832  2.124   1.00 25.34 ? 967  LYS A CD  1 
ATOM   7616 C  CE  . LYS A 1 967  ? 65.911 60.258  2.709   1.00 28.21 ? 967  LYS A CE  1 
ATOM   7617 N  NZ  . LYS A 1 967  ? 65.666 61.708  2.523   1.00 30.47 ? 967  LYS A NZ  1 
ATOM   7618 N  N   . SER A 1 968  ? 70.339 58.648  -2.052  1.00 16.48 ? 968  SER A N   1 
ATOM   7619 C  CA  . SER A 1 968  ? 71.620 58.397  -2.699  1.00 16.91 ? 968  SER A CA  1 
ATOM   7620 C  C   . SER A 1 968  ? 72.639 57.579  -1.884  1.00 18.13 ? 968  SER A C   1 
ATOM   7621 O  O   . SER A 1 968  ? 73.469 56.924  -2.464  1.00 19.43 ? 968  SER A O   1 
ATOM   7622 C  CB  . SER A 1 968  ? 72.247 59.742  -3.132  1.00 19.78 ? 968  SER A CB  1 
ATOM   7623 O  OG  . SER A 1 968  ? 72.610 60.501  -1.979  1.00 23.49 ? 968  SER A OG  1 
ATOM   7624 N  N   . SER A 1 969  ? 72.557 57.577  -0.557  1.00 17.33 ? 969  SER A N   1 
ATOM   7625 C  CA  . SER A 1 969  ? 73.568 56.802  0.200   1.00 19.23 ? 969  SER A CA  1 
ATOM   7626 C  C   . SER A 1 969  ? 73.271 55.283  0.165   1.00 18.92 ? 969  SER A C   1 
ATOM   7627 O  O   . SER A 1 969  ? 74.099 54.482  0.601   1.00 18.55 ? 969  SER A O   1 
ATOM   7628 C  CB  . SER A 1 969  ? 73.571 57.287  1.631   1.00 22.17 ? 969  SER A CB  1 
ATOM   7629 O  OG  . SER A 1 969  ? 72.452 56.703  2.267   1.00 27.65 ? 969  SER A OG  1 
ATOM   7630 N  N   . ALA A 1 970  ? 72.109 54.847  -0.336  1.00 16.96 ? 970  ALA A N   1 
ATOM   7631 C  CA  . ALA A 1 970  ? 71.805 53.424  -0.380  1.00 16.42 ? 970  ALA A CA  1 
ATOM   7632 C  C   . ALA A 1 970  ? 72.656 52.658  -1.406  1.00 17.06 ? 970  ALA A C   1 
ATOM   7633 O  O   . ALA A 1 970  ? 72.661 53.006  -2.588  1.00 17.73 ? 970  ALA A O   1 
ATOM   7634 C  CB  . ALA A 1 970  ? 70.281 53.206  -0.683  1.00 16.14 ? 970  ALA A CB  1 
ATOM   7635 N  N   . LYS A 1 971  ? 73.422 51.647  -0.950  1.00 17.91 ? 971  LYS A N   1 
ATOM   7636 C  CA  . LYS A 1 971  ? 74.201 50.844  -1.864  1.00 18.14 ? 971  LYS A CA  1 
ATOM   7637 C  C   . LYS A 1 971  ? 73.296 50.236  -2.922  1.00 17.65 ? 971  LYS A C   1 
ATOM   7638 O  O   . LYS A 1 971  ? 73.639 50.237  -4.078  1.00 17.67 ? 971  LYS A O   1 
ATOM   7639 C  CB  . LYS A 1 971  ? 74.923 49.735  -1.082  1.00 20.74 ? 971  LYS A CB  1 
ATOM   7640 C  CG  . LYS A 1 971  ? 76.017 49.057  -1.849  1.00 26.23 ? 971  LYS A CG  1 
ATOM   7641 C  CD  . LYS A 1 971  ? 76.837 48.205  -0.854  1.00 28.73 ? 971  LYS A CD  1 
ATOM   7642 C  CE  . LYS A 1 971  ? 78.187 47.725  -1.427  1.00 30.90 ? 971  LYS A CE  1 
ATOM   7643 N  NZ  . LYS A 1 971  ? 79.171 48.812  -1.850  1.00 33.79 ? 971  LYS A NZ  1 
ATOM   7644 N  N   . THR A 1 972  ? 72.147 49.685  -2.520  1.00 17.81 ? 972  THR A N   1 
ATOM   7645 C  CA  . THR A 1 972  ? 71.221 49.111  -3.498  1.00 17.03 ? 972  THR A CA  1 
ATOM   7646 C  C   . THR A 1 972  ? 70.075 50.118  -3.744  1.00 16.58 ? 972  THR A C   1 
ATOM   7647 O  O   . THR A 1 972  ? 69.315 50.444  -2.811  1.00 15.87 ? 972  THR A O   1 
ATOM   7648 C  CB  . THR A 1 972  ? 70.620 47.768  -3.042  1.00 19.65 ? 972  THR A CB  1 
ATOM   7649 O  OG1 . THR A 1 972  ? 71.698 46.853  -2.741  1.00 20.07 ? 972  THR A OG1 1 
ATOM   7650 C  CG2 . THR A 1 972  ? 69.769 47.138  -4.198  1.00 17.89 ? 972  THR A CG2 1 
ATOM   7651 N  N   . GLN A 1 973  ? 70.023 50.674  -4.963  1.00 13.59 ? 973  GLN A N   1 
ATOM   7652 C  CA  . GLN A 1 973  ? 68.982 51.646  -5.307  1.00 13.54 ? 973  GLN A CA  1 
ATOM   7653 C  C   . GLN A 1 973  ? 67.730 50.860  -5.684  1.00 12.49 ? 973  GLN A C   1 
ATOM   7654 O  O   . GLN A 1 973  ? 67.815 49.800  -6.250  1.00 13.06 ? 973  GLN A O   1 
ATOM   7655 C  CB  . GLN A 1 973  ? 69.451 52.552  -6.485  1.00 11.36 ? 973  GLN A CB  1 
ATOM   7656 C  CG  . GLN A 1 973  ? 70.528 53.557  -6.071  1.00 13.92 ? 973  GLN A CG  1 
ATOM   7657 C  CD  . GLN A 1 973  ? 70.006 54.572  -5.065  1.00 14.36 ? 973  GLN A CD  1 
ATOM   7658 O  OE1 . GLN A 1 973  ? 68.983 55.240  -5.343  1.00 14.07 ? 973  GLN A OE1 1 
ATOM   7659 N  NE2 . GLN A 1 973  ? 70.658 54.720  -3.908  1.00 11.81 ? 973  GLN A NE2 1 
ATOM   7660 N  N   . ARG A 1 974  ? 66.560 51.445  -5.365  1.00 13.82 ? 974  ARG A N   1 
ATOM   7661 C  CA  . ARG A 1 974  ? 65.292 50.807  -5.689  1.00 12.51 ? 974  ARG A CA  1 
ATOM   7662 C  C   . ARG A 1 974  ? 64.352 51.805  -6.385  1.00 10.53 ? 974  ARG A C   1 
ATOM   7663 O  O   . ARG A 1 974  ? 64.294 52.973  -5.991  1.00 11.88 ? 974  ARG A O   1 
ATOM   7664 C  CB  . ARG A 1 974  ? 64.611 50.243  -4.405  1.00 12.66 ? 974  ARG A CB  1 
ATOM   7665 C  CG  . ARG A 1 974  ? 65.479 49.216  -3.641  1.00 14.02 ? 974  ARG A CG  1 
ATOM   7666 C  CD  . ARG A 1 974  ? 64.907 48.832  -2.266  1.00 15.35 ? 974  ARG A CD  1 
ATOM   7667 N  NE  . ARG A 1 974  ? 63.641 48.124  -2.410  1.00 18.34 ? 974  ARG A NE  1 
ATOM   7668 C  CZ  . ARG A 1 974  ? 62.471 48.538  -1.916  1.00 18.48 ? 974  ARG A CZ  1 
ATOM   7669 N  NH1 . ARG A 1 974  ? 62.371 49.661  -1.241  1.00 18.42 ? 974  ARG A NH1 1 
ATOM   7670 N  NH2 . ARG A 1 974  ? 61.394 47.783  -2.074  1.00 18.50 ? 974  ARG A NH2 1 
ATOM   7671 N  N   . VAL A 1 975  ? 63.695 51.330  -7.452  1.00 11.95 ? 975  VAL A N   1 
ATOM   7672 C  CA  . VAL A 1 975  ? 62.757 52.236  -8.165  1.00 11.88 ? 975  VAL A CA  1 
ATOM   7673 C  C   . VAL A 1 975  ? 61.442 51.525  -8.281  1.00 10.63 ? 975  VAL A C   1 
ATOM   7674 O  O   . VAL A 1 975  ? 61.414 50.360  -8.720  1.00 10.59 ? 975  VAL A O   1 
ATOM   7675 C  CB  . VAL A 1 975  ? 63.305 52.613  -9.591  1.00 14.17 ? 975  VAL A CB  1 
ATOM   7676 C  CG1 . VAL A 1 975  ? 62.276 53.531  -10.381 1.00 10.11 ? 975  VAL A CG1 1 
ATOM   7677 C  CG2 . VAL A 1 975  ? 64.635 53.363  -9.407  1.00 12.15 ? 975  VAL A CG2 1 
ATOM   7678 N  N   . GLY A 1 976  ? 60.359 52.218  -7.919  1.00 12.37 ? 976  GLY A N   1 
ATOM   7679 C  CA  . GLY A 1 976  ? 59.026 51.621  -8.003  1.00 8.94  ? 976  GLY A CA  1 
ATOM   7680 C  C   . GLY A 1 976  ? 58.155 52.106  -9.140  1.00 8.88  ? 976  GLY A C   1 
ATOM   7681 O  O   . GLY A 1 976  ? 58.231 53.294  -9.513  1.00 9.41  ? 976  GLY A O   1 
ATOM   7682 N  N   . TYR A 1 977  ? 57.426 51.188  -9.710  1.00 8.32  ? 977  TYR A N   1 
ATOM   7683 C  CA  . TYR A 1 977  ? 56.539 51.517  -10.827 1.00 8.22  ? 977  TYR A CA  1 
ATOM   7684 C  C   . TYR A 1 977  ? 55.138 50.975  -10.576 1.00 7.96  ? 977  TYR A C   1 
ATOM   7685 O  O   . TYR A 1 977  ? 55.009 49.879  -10.078 1.00 9.66  ? 977  TYR A O   1 
ATOM   7686 C  CB  . TYR A 1 977  ? 57.012 50.850  -12.139 1.00 9.33  ? 977  TYR A CB  1 
ATOM   7687 C  CG  . TYR A 1 977  ? 58.428 51.202  -12.524 1.00 11.94 ? 977  TYR A CG  1 
ATOM   7688 C  CD1 . TYR A 1 977  ? 59.527 50.519  -12.001 1.00 10.50 ? 977  TYR A CD1 1 
ATOM   7689 C  CD2 . TYR A 1 977  ? 58.664 52.240  -13.414 1.00 10.84 ? 977  TYR A CD2 1 
ATOM   7690 C  CE1 . TYR A 1 977  ? 60.825 50.869  -12.361 1.00 13.93 ? 977  TYR A CE1 1 
ATOM   7691 C  CE2 . TYR A 1 977  ? 59.960 52.592  -13.780 1.00 10.97 ? 977  TYR A CE2 1 
ATOM   7692 C  CZ  . TYR A 1 977  ? 61.028 51.900  -13.240 1.00 11.93 ? 977  TYR A CZ  1 
ATOM   7693 O  OH  . TYR A 1 977  ? 62.292 52.312  -13.584 1.00 13.64 ? 977  TYR A OH  1 
ATOM   7694 N  N   . VAL A 1 978  ? 54.113 51.758  -10.931 1.00 7.98  ? 978  VAL A N   1 
ATOM   7695 C  CA  . VAL A 1 978  ? 52.729 51.288  -10.891 1.00 7.79  ? 978  VAL A CA  1 
ATOM   7696 C  C   . VAL A 1 978  ? 52.339 51.259  -12.363 1.00 9.85  ? 978  VAL A C   1 
ATOM   7697 O  O   . VAL A 1 978  ? 52.467 52.287  -13.062 1.00 10.45 ? 978  VAL A O   1 
ATOM   7698 C  CB  . VAL A 1 978  ? 51.806 52.208  -10.090 1.00 7.44  ? 978  VAL A CB  1 
ATOM   7699 C  CG1 . VAL A 1 978  ? 50.349 51.683  -10.260 1.00 8.43  ? 978  VAL A CG1 1 
ATOM   7700 C  CG2 . VAL A 1 978  ? 52.164 52.146  -8.558  1.00 7.51  ? 978  VAL A CG2 1 
ATOM   7701 N  N   . LEU A 1 979  ? 51.945 50.085  -12.843 1.00 8.96  ? 979  LEU A N   1 
ATOM   7702 C  CA  . LEU A 1 979  ? 51.543 49.881  -14.234 1.00 10.46 ? 979  LEU A CA  1 
ATOM   7703 C  C   . LEU A 1 979  ? 50.064 49.631  -14.222 1.00 10.90 ? 979  LEU A C   1 
ATOM   7704 O  O   A LEU A 1 979  ? 49.551 48.883  -13.389 0.50 11.81 ? 979  LEU A O   1 
ATOM   7705 O  O   B LEU A 1 979  ? 49.597 48.538  -13.710 0.50 10.99 ? 979  LEU A O   1 
ATOM   7706 C  CB  . LEU A 1 979  ? 52.310 48.664  -14.806 1.00 12.14 ? 979  LEU A CB  1 
ATOM   7707 C  CG  A LEU A 1 979  ? 52.238 48.217  -16.280 0.50 14.18 ? 979  LEU A CG  1 
ATOM   7708 C  CG  B LEU A 1 979  ? 52.835 48.557  -16.175 0.50 15.73 ? 979  LEU A CG  1 
ATOM   7709 C  CD1 A LEU A 1 979  ? 52.982 49.234  -17.127 0.50 14.85 ? 979  LEU A CD1 1 
ATOM   7710 C  CD1 B LEU A 1 979  ? 53.726 49.753  -16.371 0.50 12.70 ? 979  LEU A CD1 1 
ATOM   7711 C  CD2 A LEU A 1 979  ? 52.886 46.831  -16.450 0.50 15.41 ? 979  LEU A CD2 1 
ATOM   7712 C  CD2 B LEU A 1 979  ? 53.582 47.233  -16.495 0.50 15.53 ? 979  LEU A CD2 1 
ATOM   7713 N  N   . HIS A 1 980  ? 49.364 50.295  -15.123 1.00 10.12 ? 980  HIS A N   1 
ATOM   7714 C  CA  . HIS A 1 980  ? 47.942 50.136  -15.237 1.00 9.93  ? 980  HIS A CA  1 
ATOM   7715 C  C   . HIS A 1 980  ? 47.544 49.921  -16.692 1.00 12.01 ? 980  HIS A C   1 
ATOM   7716 O  O   . HIS A 1 980  ? 48.021 50.664  -17.578 1.00 13.72 ? 980  HIS A O   1 
ATOM   7717 C  CB  . HIS A 1 980  ? 47.186 51.406  -14.712 1.00 10.49 ? 980  HIS A CB  1 
ATOM   7718 C  CG  . HIS A 1 980  ? 45.709 51.341  -14.906 1.00 11.31 ? 980  HIS A CG  1 
ATOM   7719 N  ND1 . HIS A 1 980  ? 44.932 50.441  -14.213 1.00 12.21 ? 980  HIS A ND1 1 
ATOM   7720 C  CD2 . HIS A 1 980  ? 44.880 51.940  -15.797 1.00 11.55 ? 980  HIS A CD2 1 
ATOM   7721 C  CE1 . HIS A 1 980  ? 43.685 50.486  -14.671 1.00 12.36 ? 980  HIS A CE1 1 
ATOM   7722 N  NE2 . HIS A 1 980  ? 43.624 51.392  -15.631 1.00 12.69 ? 980  HIS A NE2 1 
ATOM   7723 N  N   . ARG A 1 981  ? 46.698 48.930  -16.961 1.00 10.05 ? 981  ARG A N   1 
ATOM   7724 C  CA  . ARG A 1 981  ? 46.211 48.770  -18.292 1.00 11.38 ? 981  ARG A CA  1 
ATOM   7725 C  C   . ARG A 1 981  ? 44.719 48.923  -18.254 1.00 10.76 ? 981  ARG A C   1 
ATOM   7726 O  O   . ARG A 1 981  ? 44.044 48.269  -17.445 1.00 10.01 ? 981  ARG A O   1 
ATOM   7727 C  CB  . ARG A 1 981  ? 46.574 47.411  -18.899 1.00 10.77 ? 981  ARG A CB  1 
ATOM   7728 C  CG  . ARG A 1 981  ? 46.202 47.391  -20.419 1.00 12.60 ? 981  ARG A CG  1 
ATOM   7729 C  CD  . ARG A 1 981  ? 46.254 45.991  -21.066 1.00 17.61 ? 981  ARG A CD  1 
ATOM   7730 N  NE  . ARG A 1 981  ? 47.510 45.331  -20.840 1.00 21.66 ? 981  ARG A NE  1 
ATOM   7731 C  CZ  . ARG A 1 981  ? 48.519 45.310  -21.702 1.00 23.17 ? 981  ARG A CZ  1 
ATOM   7732 N  NH1 . ARG A 1 981  ? 48.420 45.924  -22.877 1.00 23.38 ? 981  ARG A NH1 1 
ATOM   7733 N  NH2 . ARG A 1 981  ? 49.629 44.653  -21.382 1.00 24.28 ? 981  ARG A NH2 1 
ATOM   7734 N  N   . THR A 1 982  ? 44.189 49.801  -19.103 1.00 9.56  ? 982  THR A N   1 
ATOM   7735 C  CA  . THR A 1 982  ? 42.758 50.008  -19.186 1.00 9.74  ? 982  THR A CA  1 
ATOM   7736 C  C   . THR A 1 982  ? 42.259 49.006  -20.205 1.00 12.24 ? 982  THR A C   1 
ATOM   7737 O  O   . THR A 1 982  ? 42.963 48.102  -20.595 1.00 12.87 ? 982  THR A O   1 
ATOM   7738 C  CB  . THR A 1 982  ? 42.455 51.496  -19.590 1.00 9.87  ? 982  THR A CB  1 
ATOM   7739 O  OG1 . THR A 1 982  ? 41.055 51.730  -19.448 1.00 9.84  ? 982  THR A OG1 1 
ATOM   7740 C  CG2 . THR A 1 982  ? 42.951 51.813  -21.025 1.00 12.28 ? 982  THR A CG2 1 
ATOM   7741 N  N   . ASN A 1 983  ? 40.991 49.084  -20.526 1.00 10.68 ? 983  ASN A N   1 
ATOM   7742 C  CA  . ASN A 1 983  ? 40.427 48.212  -21.526 1.00 10.78 ? 983  ASN A CA  1 
ATOM   7743 C  C   . ASN A 1 983  ? 39.745 49.102  -22.539 1.00 9.40  ? 983  ASN A C   1 
ATOM   7744 O  O   . ASN A 1 983  ? 38.808 49.840  -22.226 1.00 10.76 ? 983  ASN A O   1 
ATOM   7745 C  CB  . ASN A 1 983  ? 39.412 47.195  -20.968 1.00 10.61 ? 983  ASN A CB  1 
ATOM   7746 C  CG  . ASN A 1 983  ? 38.952 46.217  -22.016 1.00 11.45 ? 983  ASN A CG  1 
ATOM   7747 O  OD1 . ASN A 1 983  ? 39.696 45.341  -22.438 1.00 11.73 ? 983  ASN A OD1 1 
ATOM   7748 N  ND2 . ASN A 1 983  ? 37.753 46.448  -22.519 1.00 10.36 ? 983  ASN A ND2 1 
ATOM   7749 N  N   . LEU A 1 984  ? 40.178 48.963  -23.793 1.00 10.55 ? 984  LEU A N   1 
ATOM   7750 C  CA  . LEU A 1 984  ? 39.628 49.792  -24.870 1.00 11.62 ? 984  LEU A CA  1 
ATOM   7751 C  C   . LEU A 1 984  ? 38.769 48.988  -25.827 1.00 13.31 ? 984  LEU A C   1 
ATOM   7752 O  O   . LEU A 1 984  ? 39.122 47.852  -26.148 1.00 15.87 ? 984  LEU A O   1 
ATOM   7753 C  CB  . LEU A 1 984  ? 40.781 50.366  -25.668 1.00 12.22 ? 984  LEU A CB  1 
ATOM   7754 C  CG  . LEU A 1 984  ? 41.708 51.246  -24.865 1.00 11.63 ? 984  LEU A CG  1 
ATOM   7755 C  CD1 . LEU A 1 984  ? 42.882 51.651  -25.760 1.00 13.01 ? 984  LEU A CD1 1 
ATOM   7756 C  CD2 . LEU A 1 984  ? 40.956 52.434  -24.286 1.00 11.61 ? 984  LEU A CD2 1 
ATOM   7757 N  N   . MET A 1 985  ? 37.690 49.565  -26.345 1.00 15.35 ? 985  MET A N   1 
ATOM   7758 C  CA  . MET A 1 985  ? 36.832 48.820  -27.266 1.00 17.99 ? 985  MET A CA  1 
ATOM   7759 C  C   . MET A 1 985  ? 37.496 48.427  -28.574 1.00 20.73 ? 985  MET A C   1 
ATOM   7760 O  O   . MET A 1 985  ? 38.269 49.188  -29.189 1.00 19.87 ? 985  MET A O   1 
ATOM   7761 C  CB  . MET A 1 985  ? 35.570 49.594  -27.581 1.00 17.99 ? 985  MET A CB  1 
ATOM   7762 C  CG  . MET A 1 985  ? 34.623 49.644  -26.419 1.00 20.04 ? 985  MET A CG  1 
ATOM   7763 S  SD  . MET A 1 985  ? 32.917 49.587  -26.929 1.00 22.56 ? 985  MET A SD  1 
ATOM   7764 C  CE  . MET A 1 985  ? 32.806 51.157  -27.684 1.00 24.59 ? 985  MET A CE  1 
ATOM   7765 N  N   . GLN A 1 986  ? 37.176 47.219  -29.015 1.00 23.06 ? 986  GLN A N   1 
ATOM   7766 C  CA  . GLN A 1 986  ? 37.735 46.749  -30.272 1.00 23.63 ? 986  GLN A CA  1 
ATOM   7767 C  C   . GLN A 1 986  ? 36.708 47.113  -31.314 1.00 23.83 ? 986  GLN A C   1 
ATOM   7768 O  O   . GLN A 1 986  ? 35.602 46.541  -31.275 1.00 21.55 ? 986  GLN A O   1 
ATOM   7769 C  CB  . GLN A 1 986  ? 37.961 45.247  -30.218 1.00 26.94 ? 986  GLN A CB  1 
ATOM   7770 C  CG  . GLN A 1 986  ? 39.103 44.893  -29.285 1.00 32.14 ? 986  GLN A CG  1 
ATOM   7771 C  CD  . GLN A 1 986  ? 39.653 43.517  -29.535 1.00 35.11 ? 986  GLN A CD  1 
ATOM   7772 O  OE1 . GLN A 1 986  ? 39.114 42.491  -29.038 1.00 38.14 ? 986  GLN A OE1 1 
ATOM   7773 N  NE2 . GLN A 1 986  ? 40.727 43.458  -30.342 1.00 36.81 ? 986  GLN A NE2 1 
ATOM   7774 N  N   . CYS A 1 987  ? 37.070 48.061  -32.202 1.00 22.63 ? 987  CYS A N   1 
ATOM   7775 C  CA  . CYS A 1 987  ? 36.172 48.549  -33.248 1.00 25.05 ? 987  CYS A CA  1 
ATOM   7776 C  C   . CYS A 1 987  ? 36.680 48.405  -34.683 1.00 28.38 ? 987  CYS A C   1 
ATOM   7777 O  O   . CYS A 1 987  ? 36.313 49.215  -35.535 1.00 28.96 ? 987  CYS A O   1 
ATOM   7778 C  CB  . CYS A 1 987  ? 35.854 50.015  -33.010 1.00 22.45 ? 987  CYS A CB  1 
ATOM   7779 S  SG  . CYS A 1 987  ? 35.259 50.471  -31.325 1.00 21.03 ? 987  CYS A SG  1 
ATOM   7780 N  N   . GLY A 1 988  ? 37.524 47.412  -34.943 1.00 30.32 ? 988  GLY A N   1 
ATOM   7781 C  CA  . GLY A 1 988  ? 38.005 47.216  -36.299 1.00 34.92 ? 988  GLY A CA  1 
ATOM   7782 C  C   . GLY A 1 988  ? 39.272 47.919  -36.746 1.00 38.00 ? 988  GLY A C   1 
ATOM   7783 O  O   . GLY A 1 988  ? 39.595 47.909  -37.941 1.00 38.17 ? 988  GLY A O   1 
ATOM   7784 N  N   . THR A 1 989  ? 39.989 48.538  -35.822 1.00 40.26 ? 989  THR A N   1 
ATOM   7785 C  CA  . THR A 1 989  ? 41.235 49.214  -36.161 1.00 43.48 ? 989  THR A CA  1 
ATOM   7786 C  C   . THR A 1 989  ? 42.361 48.232  -35.872 1.00 46.45 ? 989  THR A C   1 
ATOM   7787 O  O   . THR A 1 989  ? 42.537 47.820  -34.725 1.00 46.33 ? 989  THR A O   1 
ATOM   7788 C  CB  . THR A 1 989  ? 41.440 50.449  -35.302 1.00 42.83 ? 989  THR A CB  1 
ATOM   7789 O  OG1 . THR A 1 989  ? 40.253 51.248  -35.324 1.00 43.38 ? 989  THR A OG1 1 
ATOM   7790 C  CG2 . THR A 1 989  ? 42.586 51.267  -35.824 1.00 43.83 ? 989  THR A CG2 1 
ATOM   7791 N  N   . PRO A 1 990  ? 43.127 47.830  -36.907 1.00 49.66 ? 990  PRO A N   1 
ATOM   7792 C  CA  . PRO A 1 990  ? 44.246 46.887  -36.772 1.00 52.60 ? 990  PRO A CA  1 
ATOM   7793 C  C   . PRO A 1 990  ? 45.243 47.183  -35.635 1.00 55.69 ? 990  PRO A C   1 
ATOM   7794 O  O   . PRO A 1 990  ? 45.511 46.307  -34.800 1.00 56.46 ? 990  PRO A O   1 
ATOM   7795 C  CB  . PRO A 1 990  ? 44.906 46.940  -38.149 1.00 52.10 ? 990  PRO A CB  1 
ATOM   7796 C  CG  . PRO A 1 990  ? 43.758 47.161  -39.063 1.00 51.01 ? 990  PRO A CG  1 
ATOM   7797 C  CD  . PRO A 1 990  ? 42.943 48.212  -38.323 1.00 50.45 ? 990  PRO A CD  1 
ATOM   7798 N  N   . GLU A 1 991  ? 45.795 48.398  -35.602 1.00 58.67 ? 991  GLU A N   1 
ATOM   7799 C  CA  . GLU A 1 991  ? 46.770 48.797  -34.568 1.00 62.00 ? 991  GLU A CA  1 
ATOM   7800 C  C   . GLU A 1 991  ? 47.571 47.622  -33.943 1.00 62.76 ? 991  GLU A C   1 
ATOM   7801 O  O   . GLU A 1 991  ? 47.102 46.973  -32.999 1.00 63.10 ? 991  GLU A O   1 
ATOM   7802 C  CB  . GLU A 1 991  ? 46.036 49.591  -33.467 1.00 63.54 ? 991  GLU A CB  1 
ATOM   7803 C  CG  . GLU A 1 991  ? 45.273 50.817  -34.011 1.00 65.82 ? 991  GLU A CG  1 
ATOM   7804 C  CD  . GLU A 1 991  ? 44.367 51.504  -32.980 1.00 67.20 ? 991  GLU A CD  1 
ATOM   7805 O  OE1 . GLU A 1 991  ? 43.406 50.864  -32.488 1.00 67.60 ? 991  GLU A OE1 1 
ATOM   7806 O  OE2 . GLU A 1 991  ? 44.612 52.697  -32.672 1.00 68.04 ? 991  GLU A OE2 1 
ATOM   7807 N  N   . GLU A 1 992  ? 48.774 47.350  -34.454 1.00 63.47 ? 992  GLU A N   1 
ATOM   7808 C  CA  . GLU A 1 992  ? 49.565 46.233  -33.914 1.00 64.11 ? 992  GLU A CA  1 
ATOM   7809 C  C   . GLU A 1 992  ? 51.093 46.403  -33.831 1.00 62.97 ? 992  GLU A C   1 
ATOM   7810 O  O   . GLU A 1 992  ? 51.807 45.400  -33.692 1.00 63.56 ? 992  GLU A O   1 
ATOM   7811 C  CB  . GLU A 1 992  ? 49.286 44.942  -34.719 1.00 66.35 ? 992  GLU A CB  1 
ATOM   7812 C  CG  . GLU A 1 992  ? 47.885 44.827  -35.352 1.00 68.79 ? 992  GLU A CG  1 
ATOM   7813 C  CD  . GLU A 1 992  ? 47.567 43.429  -35.910 1.00 70.31 ? 992  GLU A CD  1 
ATOM   7814 O  OE1 . GLU A 1 992  ? 48.332 42.472  -35.641 1.00 71.05 ? 992  GLU A OE1 1 
ATOM   7815 O  OE2 . GLU A 1 992  ? 46.537 43.287  -36.611 1.00 70.94 ? 992  GLU A OE2 1 
ATOM   7816 N  N   . HIS A 1 993  ? 51.613 47.628  -33.897 1.00 61.00 ? 993  HIS A N   1 
ATOM   7817 C  CA  . HIS A 1 993  ? 53.078 47.798  -33.860 1.00 58.31 ? 993  HIS A CA  1 
ATOM   7818 C  C   . HIS A 1 993  ? 53.674 48.470  -32.617 1.00 54.58 ? 993  HIS A C   1 
ATOM   7819 O  O   . HIS A 1 993  ? 54.058 49.644  -32.671 1.00 54.27 ? 993  HIS A O   1 
ATOM   7820 C  CB  . HIS A 1 993  ? 53.553 48.554  -35.116 1.00 61.05 ? 993  HIS A CB  1 
ATOM   7821 C  CG  . HIS A 1 993  ? 53.309 47.812  -36.400 1.00 64.26 ? 993  HIS A CG  1 
ATOM   7822 N  ND1 . HIS A 1 993  ? 53.863 46.575  -36.666 1.00 65.38 ? 993  HIS A ND1 1 
ATOM   7823 C  CD2 . HIS A 1 993  ? 52.547 48.120  -37.480 1.00 65.03 ? 993  HIS A CD2 1 
ATOM   7824 C  CE1 . HIS A 1 993  ? 53.452 46.153  -37.850 1.00 65.92 ? 993  HIS A CE1 1 
ATOM   7825 N  NE2 . HIS A 1 993  ? 52.652 47.072  -38.364 1.00 65.67 ? 993  HIS A NE2 1 
ATOM   7826 N  N   . THR A 1 994  ? 53.775 47.726  -31.510 1.00 49.18 ? 994  THR A N   1 
ATOM   7827 C  CA  . THR A 1 994  ? 54.343 48.277  -30.270 1.00 43.30 ? 994  THR A CA  1 
ATOM   7828 C  C   . THR A 1 994  ? 55.341 47.346  -29.586 1.00 39.88 ? 994  THR A C   1 
ATOM   7829 O  O   . THR A 1 994  ? 55.403 46.162  -29.890 1.00 39.41 ? 994  THR A O   1 
ATOM   7830 C  CB  . THR A 1 994  ? 53.241 48.620  -29.243 1.00 42.78 ? 994  THR A CB  1 
ATOM   7831 O  OG1 . THR A 1 994  ? 52.497 47.437  -28.926 1.00 41.46 ? 994  THR A OG1 1 
ATOM   7832 C  CG2 . THR A 1 994  ? 52.295 49.656  -29.816 1.00 42.00 ? 994  THR A CG2 1 
ATOM   7833 N  N   . GLN A 1 995  ? 56.105 47.901  -28.648 1.00 34.62 ? 995  GLN A N   1 
ATOM   7834 C  CA  . GLN A 1 995  ? 57.112 47.152  -27.902 1.00 30.23 ? 995  GLN A CA  1 
ATOM   7835 C  C   . GLN A 1 995  ? 56.625 46.728  -26.512 1.00 26.73 ? 995  GLN A C   1 
ATOM   7836 O  O   . GLN A 1 995  ? 55.868 47.440  -25.856 1.00 24.81 ? 995  GLN A O   1 
ATOM   7837 C  CB  . GLN A 1 995  ? 58.368 48.009  -27.718 1.00 30.26 ? 995  GLN A CB  1 
ATOM   7838 C  CG  . GLN A 1 995  ? 59.103 48.316  -29.025 1.00 31.60 ? 995  GLN A CG  1 
ATOM   7839 C  CD  . GLN A 1 995  ? 59.710 49.714  -29.077 1.00 32.31 ? 995  GLN A CD  1 
ATOM   7840 O  OE1 . GLN A 1 995  ? 59.008 50.725  -28.999 1.00 29.16 ? 995  GLN A OE1 1 
ATOM   7841 N  NE2 . GLN A 1 995  ? 61.032 49.773  -29.238 1.00 34.02 ? 995  GLN A NE2 1 
ATOM   7842 N  N   . LYS A 1 996  ? 57.089 45.569  -26.086 1.00 23.58 ? 996  LYS A N   1 
ATOM   7843 C  CA  . LYS A 1 996  ? 56.792 45.062  -24.745 1.00 22.93 ? 996  LYS A CA  1 
ATOM   7844 C  C   . LYS A 1 996  ? 57.524 46.030  -23.800 1.00 20.72 ? 996  LYS A C   1 
ATOM   7845 O  O   . LYS A 1 996  ? 58.679 46.411  -24.046 1.00 18.88 ? 996  LYS A O   1 
ATOM   7846 C  CB  . LYS A 1 996  ? 57.348 43.623  -24.604 1.00 24.98 ? 996  LYS A CB  1 
ATOM   7847 C  CG  . LYS A 1 996  ? 57.264 43.024  -23.218 1.00 28.56 ? 996  LYS A CG  1 
ATOM   7848 C  CD  . LYS A 1 996  ? 57.885 41.573  -23.148 1.00 30.50 ? 996  LYS A CD  1 
ATOM   7849 C  CE  . LYS A 1 996  ? 58.058 41.132  -21.681 1.00 32.36 ? 996  LYS A CE  1 
ATOM   7850 N  NZ  . LYS A 1 996  ? 58.925 39.905  -21.533 1.00 34.59 ? 996  LYS A NZ  1 
ATOM   7851 N  N   . LEU A 1 997  ? 56.848 46.438  -22.723 1.00 18.11 ? 997  LEU A N   1 
ATOM   7852 C  CA  . LEU A 1 997  ? 57.455 47.351  -21.765 1.00 17.96 ? 997  LEU A CA  1 
ATOM   7853 C  C   . LEU A 1 997  ? 57.770 46.511  -20.550 1.00 16.69 ? 997  LEU A C   1 
ATOM   7854 O  O   . LEU A 1 997  ? 56.861 45.929  -19.989 1.00 15.88 ? 997  LEU A O   1 
ATOM   7855 C  CB  . LEU A 1 997  ? 56.480 48.469  -21.334 1.00 18.32 ? 997  LEU A CB  1 
ATOM   7856 C  CG  . LEU A 1 997  ? 56.997 49.393  -20.239 1.00 20.78 ? 997  LEU A CG  1 
ATOM   7857 C  CD1 . LEU A 1 997  ? 58.333 50.061  -20.550 1.00 18.59 ? 997  LEU A CD1 1 
ATOM   7858 C  CD2 . LEU A 1 997  ? 55.925 50.444  -20.021 1.00 21.53 ? 997  LEU A CD2 1 
ATOM   7859 N  N   . ASP A 1 998  ? 59.044 46.451  -20.201 1.00 17.45 ? 998  ASP A N   1 
ATOM   7860 C  CA  . ASP A 1 998  ? 59.532 45.748  -19.021 1.00 17.39 ? 998  ASP A CA  1 
ATOM   7861 C  C   . ASP A 1 998  ? 60.110 46.866  -18.120 1.00 16.52 ? 998  ASP A C   1 
ATOM   7862 O  O   . ASP A 1 998  ? 61.243 47.337  -18.302 1.00 17.25 ? 998  ASP A O   1 
ATOM   7863 C  CB  . ASP A 1 998  ? 60.629 44.751  -19.405 1.00 18.14 ? 998  ASP A CB  1 
ATOM   7864 C  CG  . ASP A 1 998  ? 61.411 44.277  -18.213 1.00 21.23 ? 998  ASP A CG  1 
ATOM   7865 O  OD1 . ASP A 1 998  ? 61.012 44.588  -17.078 1.00 19.04 ? 998  ASP A OD1 1 
ATOM   7866 O  OD2 . ASP A 1 998  ? 62.436 43.577  -18.399 1.00 21.42 ? 998  ASP A OD2 1 
ATOM   7867 N  N   . VAL A 1 999  ? 59.325 47.306  -17.131 1.00 16.09 ? 999  VAL A N   1 
ATOM   7868 C  CA  . VAL A 1 999  ? 59.831 48.401  -16.350 1.00 14.62 ? 999  VAL A CA  1 
ATOM   7869 C  C   . VAL A 1 999  ? 61.111 48.146  -15.581 1.00 14.93 ? 999  VAL A C   1 
ATOM   7870 O  O   . VAL A 1 999  ? 61.881 49.080  -15.372 1.00 16.02 ? 999  VAL A O   1 
ATOM   7871 C  CB  . VAL A 1 999  ? 58.759 49.004  -15.404 1.00 13.84 ? 999  VAL A CB  1 
ATOM   7872 C  CG1 . VAL A 1 999  ? 57.622 49.545  -16.244 1.00 14.06 ? 999  VAL A CG1 1 
ATOM   7873 C  CG2 . VAL A 1 999  ? 58.307 47.981  -14.351 1.00 13.75 ? 999  VAL A CG2 1 
ATOM   7874 N  N   . CYS A 1 1000 ? 61.357 46.884  -15.210 1.00 15.18 ? 1000 CYS A N   1 
ATOM   7875 C  CA  . CYS A 1 1000 ? 62.558 46.572  -14.490 1.00 16.81 ? 1000 CYS A CA  1 
ATOM   7876 C  C   . CYS A 1 1000 ? 63.869 46.809  -15.255 1.00 16.56 ? 1000 CYS A C   1 
ATOM   7877 O  O   . CYS A 1 1000 ? 64.928 46.894  -14.646 1.00 17.62 ? 1000 CYS A O   1 
ATOM   7878 C  CB  . CYS A 1 1000 ? 62.474 45.145  -13.928 1.00 18.31 ? 1000 CYS A CB  1 
ATOM   7879 S  SG  . CYS A 1 1000 ? 61.525 45.148  -12.340 1.00 20.59 ? 1000 CYS A SG  1 
ATOM   7880 N  N   . HIS A 1 1001 ? 63.800 46.890  -16.577 1.00 17.74 ? 1001 HIS A N   1 
ATOM   7881 C  CA  . HIS A 1 1001 ? 65.027 47.176  -17.306 1.00 18.68 ? 1001 HIS A CA  1 
ATOM   7882 C  C   . HIS A 1 1001 ? 65.101 48.660  -17.780 1.00 19.52 ? 1001 HIS A C   1 
ATOM   7883 O  O   . HIS A 1 1001 ? 65.942 48.987  -18.597 1.00 21.22 ? 1001 HIS A O   1 
ATOM   7884 C  CB  . HIS A 1 1001 ? 65.220 46.192  -18.477 1.00 18.67 ? 1001 HIS A CB  1 
ATOM   7885 C  CG  . HIS A 1 1001 ? 65.767 44.856  -18.045 1.00 18.35 ? 1001 HIS A CG  1 
ATOM   7886 N  ND1 . HIS A 1 1001 ? 64.971 43.848  -17.545 1.00 18.29 ? 1001 HIS A ND1 1 
ATOM   7887 C  CD2 . HIS A 1 1001 ? 67.043 44.410  -17.950 1.00 18.35 ? 1001 HIS A CD2 1 
ATOM   7888 C  CE1 . HIS A 1 1001 ? 65.735 42.838  -17.155 1.00 19.43 ? 1001 HIS A CE1 1 
ATOM   7889 N  NE2 . HIS A 1 1001 ? 66.995 43.155  -17.385 1.00 18.65 ? 1001 HIS A NE2 1 
ATOM   7890 N  N   . LEU A 1 1002 ? 64.256 49.570  -17.267 1.00 20.91 ? 1002 LEU A N   1 
ATOM   7891 C  CA  . LEU A 1 1002 ? 64.311 50.984  -17.708 1.00 19.51 ? 1002 LEU A CA  1 
ATOM   7892 C  C   . LEU A 1 1002 ? 65.579 51.634  -17.180 1.00 19.60 ? 1002 LEU A C   1 
ATOM   7893 O  O   . LEU A 1 1002 ? 66.106 52.545  -17.791 1.00 20.94 ? 1002 LEU A O   1 
ATOM   7894 C  CB  . LEU A 1 1002 ? 63.089 51.784  -17.220 1.00 19.28 ? 1002 LEU A CB  1 
ATOM   7895 C  CG  . LEU A 1 1002 ? 61.835 51.538  -18.063 1.00 16.60 ? 1002 LEU A CG  1 
ATOM   7896 C  CD1 . LEU A 1 1002 ? 60.629 52.246  -17.435 1.00 18.15 ? 1002 LEU A CD1 1 
ATOM   7897 C  CD2 . LEU A 1 1002 ? 62.076 52.064  -19.473 1.00 18.72 ? 1002 LEU A CD2 1 
ATOM   7898 N  N   . LEU A 1 1003 ? 66.083 51.163  -16.044 1.00 19.77 ? 1003 LEU A N   1 
ATOM   7899 C  CA  . LEU A 1 1003 ? 67.320 51.681  -15.498 1.00 20.48 ? 1003 LEU A CA  1 
ATOM   7900 C  C   . LEU A 1 1003 ? 68.375 50.568  -15.636 1.00 21.60 ? 1003 LEU A C   1 
ATOM   7901 O  O   . LEU A 1 1003 ? 68.038 49.381  -15.629 1.00 21.25 ? 1003 LEU A O   1 
ATOM   7902 C  CB  . LEU A 1 1003 ? 67.125 52.092  -14.048 1.00 20.90 ? 1003 LEU A CB  1 
ATOM   7903 C  CG  . LEU A 1 1003 ? 66.470 53.489  -13.933 1.00 24.08 ? 1003 LEU A CG  1 
ATOM   7904 C  CD1 . LEU A 1 1003 ? 65.965 53.734  -12.534 1.00 23.88 ? 1003 LEU A CD1 1 
ATOM   7905 C  CD2 . LEU A 1 1003 ? 67.529 54.554  -14.345 1.00 21.83 ? 1003 LEU A CD2 1 
ATOM   7906 N  N   . PRO A 1 1004 ? 69.656 50.948  -15.830 1.00 22.61 ? 1004 PRO A N   1 
ATOM   7907 C  CA  . PRO A 1 1004 ? 70.737 49.975  -15.983 1.00 22.11 ? 1004 PRO A CA  1 
ATOM   7908 C  C   . PRO A 1 1004 ? 71.142 49.273  -14.663 1.00 22.25 ? 1004 PRO A C   1 
ATOM   7909 O  O   . PRO A 1 1004 ? 70.731 49.650  -13.577 1.00 21.27 ? 1004 PRO A O   1 
ATOM   7910 C  CB  . PRO A 1 1004 ? 71.860 50.835  -16.584 1.00 22.19 ? 1004 PRO A CB  1 
ATOM   7911 C  CG  . PRO A 1 1004 ? 71.714 52.116  -15.832 1.00 23.82 ? 1004 PRO A CG  1 
ATOM   7912 C  CD  . PRO A 1 1004 ? 70.183 52.334  -15.838 1.00 22.29 ? 1004 PRO A CD  1 
ATOM   7913 N  N   . ASN A 1 1005 ? 71.964 48.239  -14.797 1.00 21.29 ? 1005 ASN A N   1 
ATOM   7914 C  CA  . ASN A 1 1005 ? 72.459 47.448  -13.675 1.00 21.20 ? 1005 ASN A CA  1 
ATOM   7915 C  C   . ASN A 1 1005 ? 71.366 46.887  -12.745 1.00 20.40 ? 1005 ASN A C   1 
ATOM   7916 O  O   . ASN A 1 1005 ? 71.502 46.945  -11.540 1.00 20.49 ? 1005 ASN A O   1 
ATOM   7917 C  CB  . ASN A 1 1005 ? 73.484 48.250  -12.859 1.00 21.63 ? 1005 ASN A CB  1 
ATOM   7918 C  CG  . ASN A 1 1005 ? 74.487 48.990  -13.756 1.00 25.86 ? 1005 ASN A CG  1 
ATOM   7919 O  OD1 . ASN A 1 1005 ? 74.310 50.180  -14.058 1.00 28.67 ? 1005 ASN A OD1 1 
ATOM   7920 N  ND2 . ASN A 1 1005 ? 75.516 48.298  -14.187 1.00 24.59 ? 1005 ASN A ND2 1 
ATOM   7921 N  N   . VAL A 1 1006 ? 70.307 46.332  -13.324 1.00 20.68 ? 1006 VAL A N   1 
ATOM   7922 C  CA  . VAL A 1 1006 ? 69.251 45.790  -12.489 1.00 21.76 ? 1006 VAL A CA  1 
ATOM   7923 C  C   . VAL A 1 1006 ? 69.797 44.470  -11.891 1.00 22.32 ? 1006 VAL A C   1 
ATOM   7924 O  O   . VAL A 1 1006 ? 70.367 43.655  -12.614 1.00 24.03 ? 1006 VAL A O   1 
ATOM   7925 C  CB  . VAL A 1 1006 ? 67.928 45.536  -13.293 1.00 22.80 ? 1006 VAL A CB  1 
ATOM   7926 C  CG1 . VAL A 1 1006 ? 68.107 44.513  -14.375 1.00 23.61 ? 1006 VAL A CG1 1 
ATOM   7927 C  CG2 . VAL A 1 1006 ? 66.848 45.023  -12.338 1.00 23.15 ? 1006 VAL A CG2 1 
ATOM   7928 N  N   . ALA A 1 1007 ? 69.603 44.307  -10.587 1.00 20.00 ? 1007 ALA A N   1 
ATOM   7929 C  CA  . ALA A 1 1007 ? 70.039 43.142  -9.820  1.00 20.74 ? 1007 ALA A CA  1 
ATOM   7930 C  C   . ALA A 1 1007 ? 68.830 42.333  -9.367  1.00 22.25 ? 1007 ALA A C   1 
ATOM   7931 O  O   . ALA A 1 1007 ? 68.959 41.174  -8.952  1.00 22.66 ? 1007 ALA A O   1 
ATOM   7932 C  CB  . ALA A 1 1007 ? 70.821 43.617  -8.594  1.00 20.82 ? 1007 ALA A CB  1 
ATOM   7933 N  N   . ARG A 1 1008 ? 67.643 42.928  -9.419  1.00 21.78 ? 1008 ARG A N   1 
ATOM   7934 C  CA  . ARG A 1 1008 ? 66.467 42.194  -8.995  1.00 19.74 ? 1008 ARG A CA  1 
ATOM   7935 C  C   . ARG A 1 1008 ? 65.224 42.933  -9.416  1.00 17.84 ? 1008 ARG A C   1 
ATOM   7936 O  O   . ARG A 1 1008 ? 65.234 44.152  -9.468  1.00 16.66 ? 1008 ARG A O   1 
ATOM   7937 C  CB  . ARG A 1 1008 ? 66.431 42.110  -7.477  1.00 21.82 ? 1008 ARG A CB  1 
ATOM   7938 C  CG  . ARG A 1 1008 ? 65.389 41.218  -6.945  1.00 25.24 ? 1008 ARG A CG  1 
ATOM   7939 C  CD  . ARG A 1 1008 ? 65.703 40.898  -5.487  1.00 30.16 ? 1008 ARG A CD  1 
ATOM   7940 N  NE  . ARG A 1 1008 ? 64.622 40.108  -4.909  1.00 34.93 ? 1008 ARG A NE  1 
ATOM   7941 C  CZ  . ARG A 1 1008 ? 64.787 38.925  -4.321  1.00 37.49 ? 1008 ARG A CZ  1 
ATOM   7942 N  NH1 . ARG A 1 1008 ? 66.010 38.390  -4.229  1.00 38.30 ? 1008 ARG A NH1 1 
ATOM   7943 N  NH2 . ARG A 1 1008 ? 63.724 38.274  -3.847  1.00 38.10 ? 1008 ARG A NH2 1 
ATOM   7944 N  N   . CYS A 1 1009 ? 64.154 42.177  -9.601  1.00 15.26 ? 1009 CYS A N   1 
ATOM   7945 C  CA  . CYS A 1 1009 ? 62.864 42.748  -9.958  1.00 16.56 ? 1009 CYS A CA  1 
ATOM   7946 C  C   . CYS A 1 1009 ? 61.827 41.997  -9.127  1.00 15.71 ? 1009 CYS A C   1 
ATOM   7947 O  O   . CYS A 1 1009 ? 61.740 40.753  -9.205  1.00 14.51 ? 1009 CYS A O   1 
ATOM   7948 C  CB  . CYS A 1 1009 ? 62.590 42.531  -11.440 1.00 16.16 ? 1009 CYS A CB  1 
ATOM   7949 S  SG  . CYS A 1 1009 ? 61.016 43.200  -12.116 1.00 22.58 ? 1009 CYS A SG  1 
ATOM   7950 N  N   . GLU A 1 1010 ? 61.015 42.745  -8.364  1.00 15.14 ? 1010 GLU A N   1 
ATOM   7951 C  CA  . GLU A 1 1010 ? 59.967 42.188  -7.544  1.00 13.86 ? 1010 GLU A CA  1 
ATOM   7952 C  C   . GLU A 1 1010 ? 58.596 42.775  -7.819  1.00 13.43 ? 1010 GLU A C   1 
ATOM   7953 O  O   . GLU A 1 1010 ? 58.467 43.987  -8.026  1.00 12.86 ? 1010 GLU A O   1 
ATOM   7954 C  CB  . GLU A 1 1010 ? 60.306 42.470  -6.106  1.00 14.79 ? 1010 GLU A CB  1 
ATOM   7955 C  CG  . GLU A 1 1010 ? 61.540 41.640  -5.712  1.00 20.18 ? 1010 GLU A CG  1 
ATOM   7956 C  CD  . GLU A 1 1010 ? 62.338 42.223  -4.583  1.00 24.44 ? 1010 GLU A CD  1 
ATOM   7957 O  OE1 . GLU A 1 1010 ? 62.608 43.443  -4.552  1.00 27.16 ? 1010 GLU A OE1 1 
ATOM   7958 O  OE2 . GLU A 1 1010 ? 62.738 41.404  -3.712  1.00 24.86 ? 1010 GLU A OE2 1 
ATOM   7959 N  N   . ARG A 1 1011 ? 57.588 41.917  -7.835  1.00 12.86 ? 1011 ARG A N   1 
ATOM   7960 C  CA  . ARG A 1 1011 ? 56.225 42.446  -7.896  1.00 11.21 ? 1011 ARG A CA  1 
ATOM   7961 C  C   . ARG A 1 1011 ? 55.874 42.744  -6.407  1.00 12.16 ? 1011 ARG A C   1 
ATOM   7962 O  O   . ARG A 1 1011 ? 56.158 41.948  -5.506  1.00 12.69 ? 1011 ARG A O   1 
ATOM   7963 C  CB  . ARG A 1 1011 ? 55.240 41.463  -8.480  1.00 11.44 ? 1011 ARG A CB  1 
ATOM   7964 C  CG  . ARG A 1 1011 ? 53.874 42.151  -8.600  1.00 13.74 ? 1011 ARG A CG  1 
ATOM   7965 C  CD  . ARG A 1 1011 ? 52.903 41.351  -9.389  1.00 17.87 ? 1011 ARG A CD  1 
ATOM   7966 N  NE  . ARG A 1 1011 ? 52.575 40.114  -8.682  1.00 19.20 ? 1011 ARG A NE  1 
ATOM   7967 C  CZ  . ARG A 1 1011 ? 51.680 40.048  -7.686  1.00 22.84 ? 1011 ARG A CZ  1 
ATOM   7968 N  NH1 . ARG A 1 1011 ? 51.048 41.163  -7.296  1.00 24.97 ? 1011 ARG A NH1 1 
ATOM   7969 N  NH2 . ARG A 1 1011 ? 51.372 38.869  -7.104  1.00 26.37 ? 1011 ARG A NH2 1 
ATOM   7970 N  N   . THR A 1 1012 ? 55.252 43.896  -6.168  1.00 10.49 ? 1012 THR A N   1 
ATOM   7971 C  CA  . THR A 1 1012 ? 54.885 44.350  -4.850  1.00 10.08 ? 1012 THR A CA  1 
ATOM   7972 C  C   . THR A 1 1012 ? 53.435 44.805  -4.769  1.00 8.14  ? 1012 THR A C   1 
ATOM   7973 O  O   . THR A 1 1012 ? 52.725 44.915  -5.782  1.00 9.41  ? 1012 THR A O   1 
ATOM   7974 C  CB  . THR A 1 1012 ? 55.755 45.567  -4.398  1.00 8.50  ? 1012 THR A CB  1 
ATOM   7975 O  OG1 . THR A 1 1012 ? 55.480 46.700  -5.246  1.00 11.36 ? 1012 THR A OG1 1 
ATOM   7976 C  CG2 . THR A 1 1012 ? 57.261 45.261  -4.457  1.00 10.71 ? 1012 THR A CG2 1 
ATOM   7977 N  N   . THR A 1 1013 ? 53.000 45.059  -3.535  1.00 8.47  ? 1013 THR A N   1 
ATOM   7978 C  CA  . THR A 1 1013 ? 51.688 45.665  -3.312  1.00 9.02  ? 1013 THR A CA  1 
ATOM   7979 C  C   . THR A 1 1013 ? 51.802 47.062  -3.938  1.00 9.31  ? 1013 THR A C   1 
ATOM   7980 O  O   . THR A 1 1013 ? 52.905 47.577  -4.154  1.00 8.97  ? 1013 THR A O   1 
ATOM   7981 C  CB  . THR A 1 1013 ? 51.403 45.802  -1.802  1.00 9.35  ? 1013 THR A CB  1 
ATOM   7982 O  OG1 . THR A 1 1013 ? 52.606 46.224  -1.148  1.00 8.81  ? 1013 THR A OG1 1 
ATOM   7983 C  CG2 . THR A 1 1013 ? 50.904 44.451  -1.204  1.00 9.83  ? 1013 THR A CG2 1 
ATOM   7984 N  N   . LEU A 1 1014 ? 50.674 47.691  -4.171  1.00 7.92  ? 1014 LEU A N   1 
ATOM   7985 C  CA  . LEU A 1 1014 ? 50.676 48.995  -4.877  1.00 7.55  ? 1014 LEU A CA  1 
ATOM   7986 C  C   . LEU A 1 1014 ? 51.327 50.147  -4.145  1.00 7.77  ? 1014 LEU A C   1 
ATOM   7987 O  O   . LEU A 1 1014 ? 51.697 51.136  -4.740  1.00 8.08  ? 1014 LEU A O   1 
ATOM   7988 C  CB  . LEU A 1 1014 ? 49.225 49.416  -5.303  1.00 7.98  ? 1014 LEU A CB  1 
ATOM   7989 C  CG  . LEU A 1 1014 ? 48.454 48.471  -6.193  1.00 8.82  ? 1014 LEU A CG  1 
ATOM   7990 C  CD1 . LEU A 1 1014 ? 47.161 49.146  -6.516  1.00 9.68  ? 1014 LEU A CD1 1 
ATOM   7991 C  CD2 . LEU A 1 1014 ? 49.243 48.112  -7.535  1.00 8.84  ? 1014 LEU A CD2 1 
ATOM   7992 N  N   . THR A 1 1015 ? 51.523 49.997  -2.836  1.00 5.95  ? 1015 THR A N   1 
ATOM   7993 C  CA  . THR A 1 1015 ? 52.147 50.956  -1.983  1.00 6.91  ? 1015 THR A CA  1 
ATOM   7994 C  C   . THR A 1 1015 ? 53.664 50.728  -1.919  1.00 7.24  ? 1015 THR A C   1 
ATOM   7995 O  O   . THR A 1 1015 ? 54.398 51.477  -1.260  1.00 8.45  ? 1015 THR A O   1 
ATOM   7996 C  CB  . THR A 1 1015 ? 51.649 50.815  -0.555  1.00 8.84  ? 1015 THR A CB  1 
ATOM   7997 O  OG1 . THR A 1 1015 ? 51.819 49.434  -0.149  1.00 7.53  ? 1015 THR A OG1 1 
ATOM   7998 C  CG2 . THR A 1 1015 ? 50.149 51.187  -0.465  1.00 9.25  ? 1015 THR A CG2 1 
ATOM   7999 N  N   . PHE A 1 1016 ? 54.123 49.651  -2.575  1.00 8.78  ? 1016 PHE A N   1 
ATOM   8000 C  CA  . PHE A 1 1016 ? 55.537 49.179  -2.648  1.00 8.47  ? 1016 PHE A CA  1 
ATOM   8001 C  C   . PHE A 1 1016 ? 56.012 48.659  -1.284  1.00 9.82  ? 1016 PHE A C   1 
ATOM   8002 O  O   . PHE A 1 1016 ? 57.212 48.443  -1.155  1.00 11.53 ? 1016 PHE A O   1 
ATOM   8003 C  CB  . PHE A 1 1016 ? 56.501 50.307  -3.068  1.00 9.61  ? 1016 PHE A CB  1 
ATOM   8004 C  CG  . PHE A 1 1016 ? 56.137 50.956  -4.397  1.00 8.66  ? 1016 PHE A CG  1 
ATOM   8005 C  CD1 . PHE A 1 1016 ? 55.994 50.215  -5.581  1.00 9.07  ? 1016 PHE A CD1 1 
ATOM   8006 C  CD2 . PHE A 1 1016 ? 55.984 52.339  -4.461  1.00 8.12  ? 1016 PHE A CD2 1 
ATOM   8007 C  CE1 . PHE A 1 1016 ? 55.711 50.934  -6.815  1.00 8.02  ? 1016 PHE A CE1 1 
ATOM   8008 C  CE2 . PHE A 1 1016 ? 55.708 53.006  -5.659  1.00 9.62  ? 1016 PHE A CE2 1 
ATOM   8009 C  CZ  . PHE A 1 1016 ? 55.582 52.347  -6.785  1.00 9.87  ? 1016 PHE A CZ  1 
ATOM   8010 N  N   . LEU A 1 1017 ? 55.117 48.397  -0.334  1.00 9.35  ? 1017 LEU A N   1 
ATOM   8011 C  CA  . LEU A 1 1017 ? 55.574 48.022  1.019   1.00 9.11  ? 1017 LEU A CA  1 
ATOM   8012 C  C   . LEU A 1 1017 ? 55.766 46.547  1.302   1.00 10.89 ? 1017 LEU A C   1 
ATOM   8013 O  O   . LEU A 1 1017 ? 56.383 46.204  2.336   1.00 12.82 ? 1017 LEU A O   1 
ATOM   8014 C  CB  . LEU A 1 1017 ? 54.642 48.632  2.053   1.00 8.75  ? 1017 LEU A CB  1 
ATOM   8015 C  CG  . LEU A 1 1017 ? 54.693 50.154  1.961   1.00 6.72  ? 1017 LEU A CG  1 
ATOM   8016 C  CD1 . LEU A 1 1017 ? 53.550 50.627  2.901   1.00 9.87  ? 1017 LEU A CD1 1 
ATOM   8017 C  CD2 . LEU A 1 1017 ? 56.048 50.721  2.351   1.00 10.61 ? 1017 LEU A CD2 1 
ATOM   8018 N  N   . GLN A 1 1018 ? 55.290 45.651  0.452   1.00 11.09 ? 1018 GLN A N   1 
ATOM   8019 C  CA  . GLN A 1 1018 ? 55.458 44.220  0.635   1.00 12.84 ? 1018 GLN A CA  1 
ATOM   8020 C  C   . GLN A 1 1018 ? 55.822 43.590  -0.700  1.00 13.47 ? 1018 GLN A C   1 
ATOM   8021 O  O   . GLN A 1 1018 ? 55.160 43.879  -1.713  1.00 11.03 ? 1018 GLN A O   1 
ATOM   8022 C  CB  . GLN A 1 1018 ? 54.148 43.587  1.086   1.00 14.13 ? 1018 GLN A CB  1 
ATOM   8023 C  CG  . GLN A 1 1018 ? 54.302 42.059  1.301   1.00 19.31 ? 1018 GLN A CG  1 
ATOM   8024 C  CD  . GLN A 1 1018 ? 53.096 41.468  1.969   1.00 24.15 ? 1018 GLN A CD  1 
ATOM   8025 O  OE1 . GLN A 1 1018 ? 51.966 41.875  1.696   1.00 24.51 ? 1018 GLN A OE1 1 
ATOM   8026 N  NE2 . GLN A 1 1018 ? 53.318 40.475  2.844   1.00 26.89 ? 1018 GLN A NE2 1 
ATOM   8027 N  N   . ASN A 1 1019 ? 56.819 42.687  -0.711  1.00 13.65 ? 1019 ASN A N   1 
ATOM   8028 C  CA  . ASN A 1 1019 ? 57.215 42.006  -1.947  1.00 13.62 ? 1019 ASN A CA  1 
ATOM   8029 C  C   . ASN A 1 1019 ? 56.311 40.786  -2.059  1.00 15.60 ? 1019 ASN A C   1 
ATOM   8030 O  O   . ASN A 1 1019 ? 56.122 40.049  -1.067  1.00 18.17 ? 1019 ASN A O   1 
ATOM   8031 C  CB  . ASN A 1 1019 ? 58.690 41.557  -1.917  1.00 16.41 ? 1019 ASN A CB  1 
ATOM   8032 C  CG  . ASN A 1 1019 ? 59.672 42.714  -1.744  1.00 17.46 ? 1019 ASN A CG  1 
ATOM   8033 O  OD1 . ASN A 1 1019 ? 59.507 43.802  -2.312  1.00 18.64 ? 1019 ASN A OD1 1 
ATOM   8034 N  ND2 . ASN A 1 1019 ? 60.733 42.461  -0.985  1.00 20.48 ? 1019 ASN A ND2 1 
ATOM   8035 N  N   . LEU A 1 1020 ? 55.710 40.594  -3.218  1.00 14.71 ? 1020 LEU A N   1 
ATOM   8036 C  CA  . LEU A 1 1020 ? 54.779 39.513  -3.455  1.00 16.14 ? 1020 LEU A CA  1 
ATOM   8037 C  C   . LEU A 1 1020 ? 55.356 38.426  -4.371  1.00 17.25 ? 1020 LEU A C   1 
ATOM   8038 O  O   . LEU A 1 1020 ? 54.890 37.274  -4.322  1.00 18.64 ? 1020 LEU A O   1 
ATOM   8039 C  CB  . LEU A 1 1020 ? 53.488 40.057  -4.079  1.00 15.28 ? 1020 LEU A CB  1 
ATOM   8040 C  CG  . LEU A 1 1020 ? 52.807 41.146  -3.266  1.00 15.81 ? 1020 LEU A CG  1 
ATOM   8041 C  CD1 . LEU A 1 1020 ? 51.648 41.719  -4.048  1.00 18.30 ? 1020 LEU A CD1 1 
ATOM   8042 C  CD2 . LEU A 1 1020 ? 52.314 40.535  -1.961  1.00 17.94 ? 1020 LEU A CD2 1 
ATOM   8043 N  N   . GLU A 1 1021 ? 56.331 38.777  -5.223  1.00 18.10 ? 1021 GLU A N   1 
ATOM   8044 C  CA  . GLU A 1 1021 ? 56.908 37.792  -6.149  1.00 20.08 ? 1021 GLU A CA  1 
ATOM   8045 C  C   . GLU A 1 1021 ? 58.306 38.177  -6.626  1.00 20.75 ? 1021 GLU A C   1 
ATOM   8046 O  O   . GLU A 1 1021 ? 58.538 39.306  -7.042  1.00 18.57 ? 1021 GLU A O   1 
ATOM   8047 C  CB  . GLU A 1 1021 ? 55.974 37.669  -7.348  1.00 21.52 ? 1021 GLU A CB  1 
ATOM   8048 C  CG  . GLU A 1 1021 ? 56.294 36.584  -8.346  1.00 26.16 ? 1021 GLU A CG  1 
ATOM   8049 C  CD  . GLU A 1 1021 ? 55.427 36.742  -9.606  1.00 28.59 ? 1021 GLU A CD  1 
ATOM   8050 O  OE1 . GLU A 1 1021 ? 54.455 37.560  -9.604  1.00 27.78 ? 1021 GLU A OE1 1 
ATOM   8051 O  OE2 . GLU A 1 1021 ? 55.748 36.059  -10.602 1.00 31.25 ? 1021 GLU A OE2 1 
ATOM   8052 N  N   . HIS A 1 1022 ? 59.262 37.267  -6.517  1.00 21.74 ? 1022 HIS A N   1 
ATOM   8053 C  CA  . HIS A 1 1022 ? 60.616 37.518  -6.992  1.00 24.74 ? 1022 HIS A CA  1 
ATOM   8054 C  C   . HIS A 1 1022 ? 60.513 37.162  -8.474  1.00 23.92 ? 1022 HIS A C   1 
ATOM   8055 O  O   . HIS A 1 1022 ? 60.164 36.039  -8.805  1.00 24.55 ? 1022 HIS A O   1 
ATOM   8056 C  CB  . HIS A 1 1022 ? 61.590 36.570  -6.296  1.00 27.79 ? 1022 HIS A CB  1 
ATOM   8057 C  CG  . HIS A 1 1022 ? 63.017 36.960  -6.454  1.00 33.01 ? 1022 HIS A CG  1 
ATOM   8058 N  ND1 . HIS A 1 1022 ? 64.057 36.170  -6.006  1.00 35.80 ? 1022 HIS A ND1 1 
ATOM   8059 C  CD2 . HIS A 1 1022 ? 63.588 38.062  -7.003  1.00 34.59 ? 1022 HIS A CD2 1 
ATOM   8060 C  CE1 . HIS A 1 1022 ? 65.208 36.767  -6.278  1.00 37.44 ? 1022 HIS A CE1 1 
ATOM   8061 N  NE2 . HIS A 1 1022 ? 64.952 37.917  -6.881  1.00 36.21 ? 1022 HIS A NE2 1 
ATOM   8062 N  N   . LEU A 1 1023 ? 60.815 38.094  -9.374  1.00 22.70 ? 1023 LEU A N   1 
ATOM   8063 C  CA  . LEU A 1 1023 ? 60.599 37.840  -10.791 1.00 22.42 ? 1023 LEU A CA  1 
ATOM   8064 C  C   . LEU A 1 1023 ? 61.750 37.237  -11.571 1.00 22.84 ? 1023 LEU A C   1 
ATOM   8065 O  O   . LEU A 1 1023 ? 62.883 37.718  -11.523 1.00 22.36 ? 1023 LEU A O   1 
ATOM   8066 C  CB  . LEU A 1 1023 ? 60.150 39.155  -11.443 1.00 21.48 ? 1023 LEU A CB  1 
ATOM   8067 C  CG  . LEU A 1 1023 ? 58.782 39.508  -10.866 1.00 20.39 ? 1023 LEU A CG  1 
ATOM   8068 C  CD1 . LEU A 1 1023 ? 58.408 40.944  -11.026 1.00 21.01 ? 1023 LEU A CD1 1 
ATOM   8069 C  CD2 . LEU A 1 1023 ? 57.799 38.633  -11.557 1.00 20.86 ? 1023 LEU A CD2 1 
ATOM   8070 N  N   . ASP A 1 1024 ? 61.442 36.173  -12.294 1.00 24.33 ? 1024 ASP A N   1 
ATOM   8071 C  CA  . ASP A 1 1024 ? 62.476 35.506  -13.078 1.00 26.61 ? 1024 ASP A CA  1 
ATOM   8072 C  C   . ASP A 1 1024 ? 63.017 36.352  -14.227 1.00 25.95 ? 1024 ASP A C   1 
ATOM   8073 O  O   . ASP A 1 1024 ? 62.254 37.001  -14.954 1.00 27.23 ? 1024 ASP A O   1 
ATOM   8074 C  CB  . ASP A 1 1024 ? 61.943 34.165  -13.563 1.00 29.05 ? 1024 ASP A CB  1 
ATOM   8075 C  CG  . ASP A 1 1024 ? 61.856 33.155  -12.420 1.00 33.06 ? 1024 ASP A CG  1 
ATOM   8076 O  OD1 . ASP A 1 1024 ? 62.839 33.097  -11.622 1.00 35.36 ? 1024 ASP A OD1 1 
ATOM   8077 O  OD2 . ASP A 1 1024 ? 60.829 32.438  -12.305 1.00 35.23 ? 1024 ASP A OD2 1 
ATOM   8078 N  N   . GLY A 1 1025 ? 64.339 36.364  -14.368 1.00 25.42 ? 1025 GLY A N   1 
ATOM   8079 C  CA  . GLY A 1 1025 ? 64.970 37.145  -15.421 1.00 24.96 ? 1025 GLY A CA  1 
ATOM   8080 C  C   . GLY A 1 1025 ? 64.989 38.633  -15.128 1.00 24.62 ? 1025 GLY A C   1 
ATOM   8081 O  O   . GLY A 1 1025 ? 65.474 39.432  -15.925 1.00 24.86 ? 1025 GLY A O   1 
ATOM   8082 N  N   . MET A 1 1026 ? 64.486 39.009  -13.961 1.00 24.55 ? 1026 MET A N   1 
ATOM   8083 C  CA  . MET A 1 1026 ? 64.423 40.421  -13.567 1.00 24.81 ? 1026 MET A CA  1 
ATOM   8084 C  C   . MET A 1 1026 ? 63.548 41.186  -14.565 1.00 22.79 ? 1026 MET A C   1 
ATOM   8085 O  O   . MET A 1 1026 ? 63.786 42.353  -14.834 1.00 21.97 ? 1026 MET A O   1 
ATOM   8086 C  CB  . MET A 1 1026 ? 65.831 41.043  -13.474 1.00 26.56 ? 1026 MET A CB  1 
ATOM   8087 C  CG  . MET A 1 1026 ? 66.815 40.144  -12.716 1.00 30.93 ? 1026 MET A CG  1 
ATOM   8088 S  SD  . MET A 1 1026 ? 68.384 40.945  -12.453 1.00 36.03 ? 1026 MET A SD  1 
ATOM   8089 C  CE  . MET A 1 1026 ? 69.116 40.821  -14.073 1.00 35.32 ? 1026 MET A CE  1 
ATOM   8090 N  N   . VAL A 1 1027 ? 62.537 40.492  -15.086 1.00 20.49 ? 1027 VAL A N   1 
ATOM   8091 C  CA  . VAL A 1 1027 ? 61.563 41.031  -16.050 1.00 21.67 ? 1027 VAL A CA  1 
ATOM   8092 C  C   . VAL A 1 1027 ? 60.205 41.248  -15.385 1.00 21.87 ? 1027 VAL A C   1 
ATOM   8093 O  O   . VAL A 1 1027 ? 59.690 40.371  -14.703 1.00 22.75 ? 1027 VAL A O   1 
ATOM   8094 C  CB  . VAL A 1 1027 ? 61.388 40.047  -17.257 1.00 20.20 ? 1027 VAL A CB  1 
ATOM   8095 C  CG1 . VAL A 1 1027 ? 60.217 40.472  -18.173 1.00 20.21 ? 1027 VAL A CG1 1 
ATOM   8096 C  CG2 . VAL A 1 1027 ? 62.665 39.985  -18.037 1.00 20.27 ? 1027 VAL A CG2 1 
ATOM   8097 N  N   . ALA A 1 1028 ? 59.649 42.445  -15.550 1.00 21.35 ? 1028 ALA A N   1 
ATOM   8098 C  CA  . ALA A 1 1028 ? 58.319 42.783  -15.027 1.00 20.99 ? 1028 ALA A CA  1 
ATOM   8099 C  C   . ALA A 1 1028 ? 57.336 42.564  -16.161 1.00 21.11 ? 1028 ALA A C   1 
ATOM   8100 O  O   . ALA A 1 1028 ? 57.404 43.268  -17.184 1.00 23.04 ? 1028 ALA A O   1 
ATOM   8101 C  CB  . ALA A 1 1028 ? 58.263 44.225  -14.615 1.00 20.19 ? 1028 ALA A CB  1 
ATOM   8102 N  N   . PRO A 1 1029 ? 56.439 41.588  -16.029 1.00 20.25 ? 1029 PRO A N   1 
ATOM   8103 C  CA  . PRO A 1 1029 ? 55.431 41.299  -17.053 1.00 20.66 ? 1029 PRO A CA  1 
ATOM   8104 C  C   . PRO A 1 1029 ? 54.516 42.525  -17.244 1.00 21.18 ? 1029 PRO A C   1 
ATOM   8105 O  O   . PRO A 1 1029 ? 54.574 43.456  -16.472 1.00 23.79 ? 1029 PRO A O   1 
ATOM   8106 C  CB  . PRO A 1 1029 ? 54.637 40.139  -16.461 1.00 20.16 ? 1029 PRO A CB  1 
ATOM   8107 C  CG  . PRO A 1 1029 ? 55.622 39.517  -15.401 1.00 18.85 ? 1029 PRO A CG  1 
ATOM   8108 C  CD  . PRO A 1 1029 ? 56.335 40.696  -14.857 1.00 20.17 ? 1029 PRO A CD  1 
ATOM   8109 N  N   . GLU A 1 1030 ? 53.728 42.555  -18.307 1.00 20.88 ? 1030 GLU A N   1 
ATOM   8110 C  CA  . GLU A 1 1030 ? 52.781 43.649  -18.432 1.00 19.89 ? 1030 GLU A CA  1 
ATOM   8111 C  C   . GLU A 1 1030 ? 51.539 43.115  -17.703 1.00 19.97 ? 1030 GLU A C   1 
ATOM   8112 O  O   . GLU A 1 1030 ? 51.498 41.932  -17.352 1.00 22.56 ? 1030 GLU A O   1 
ATOM   8113 C  CB  . GLU A 1 1030 ? 52.469 43.930  -19.898 1.00 20.81 ? 1030 GLU A CB  1 
ATOM   8114 C  CG  . GLU A 1 1030 ? 53.672 44.560  -20.573 1.00 20.23 ? 1030 GLU A CG  1 
ATOM   8115 C  CD  . GLU A 1 1030 ? 53.368 45.020  -21.988 1.00 19.18 ? 1030 GLU A CD  1 
ATOM   8116 O  OE1 . GLU A 1 1030 ? 52.335 44.567  -22.537 1.00 21.37 ? 1030 GLU A OE1 1 
ATOM   8117 O  OE2 . GLU A 1 1030 ? 54.165 45.817  -22.528 1.00 19.00 ? 1030 GLU A OE2 1 
ATOM   8118 N  N   . VAL A 1 1031 ? 50.538 43.967  -17.498 1.00 17.59 ? 1031 VAL A N   1 
ATOM   8119 C  CA  . VAL A 1 1031 ? 49.336 43.550  -16.770 1.00 16.33 ? 1031 VAL A CA  1 
ATOM   8120 C  C   . VAL A 1 1031 ? 48.154 43.313  -17.691 1.00 16.19 ? 1031 VAL A C   1 
ATOM   8121 O  O   . VAL A 1 1031 ? 48.216 43.667  -18.853 1.00 17.27 ? 1031 VAL A O   1 
ATOM   8122 C  CB  . VAL A 1 1031 ? 48.948 44.591  -15.689 1.00 17.53 ? 1031 VAL A CB  1 
ATOM   8123 C  CG1 . VAL A 1 1031 ? 50.108 44.758  -14.661 1.00 17.46 ? 1031 VAL A CG1 1 
ATOM   8124 C  CG2 . VAL A 1 1031 ? 48.615 45.938  -16.335 1.00 15.59 ? 1031 VAL A CG2 1 
ATOM   8125 N  N   . CYS A 1 1032 ? 47.089 42.682  -17.189 1.00 13.95 ? 1032 CYS A N   1 
ATOM   8126 C  CA  . CYS A 1 1032 ? 45.914 42.400  -17.979 1.00 14.71 ? 1032 CYS A CA  1 
ATOM   8127 C  C   . CYS A 1 1032 ? 44.990 43.602  -18.049 1.00 13.76 ? 1032 CYS A C   1 
ATOM   8128 O  O   . CYS A 1 1032 ? 45.142 44.525  -17.298 1.00 10.32 ? 1032 CYS A O   1 
ATOM   8129 C  CB  . CYS A 1 1032 ? 45.104 41.226  -17.377 1.00 16.36 ? 1032 CYS A CB  1 
ATOM   8130 S  SG  . CYS A 1 1032 ? 45.918 39.596  -17.517 1.00 19.55 ? 1032 CYS A SG  1 
ATOM   8131 N  N   . PRO A 1 1033 ? 44.060 43.621  -19.031 1.00 11.83 ? 1033 PRO A N   1 
ATOM   8132 C  CA  . PRO A 1 1033 ? 43.131 44.748  -19.116 1.00 10.30 ? 1033 PRO A CA  1 
ATOM   8133 C  C   . PRO A 1 1033 ? 42.404 44.924  -17.786 1.00 9.75  ? 1033 PRO A C   1 
ATOM   8134 O  O   . PRO A 1 1033 ? 41.891 43.955  -17.225 1.00 11.05 ? 1033 PRO A O   1 
ATOM   8135 C  CB  . PRO A 1 1033 ? 42.130 44.302  -20.194 1.00 11.19 ? 1033 PRO A CB  1 
ATOM   8136 C  CG  . PRO A 1 1033 ? 42.968 43.470  -21.100 1.00 11.06 ? 1033 PRO A CG  1 
ATOM   8137 C  CD  . PRO A 1 1033 ? 43.908 42.706  -20.188 1.00 14.18 ? 1033 PRO A CD  1 
ATOM   8138 N  N   . MET A 1 1034 ? 42.351 46.177  -17.344 1.00 9.89  ? 1034 MET A N   1 
ATOM   8139 C  CA  . MET A 1 1034 ? 41.681 46.572  -16.090 1.00 10.66 ? 1034 MET A CA  1 
ATOM   8140 C  C   . MET A 1 1034 ? 42.480 46.246  -14.830 1.00 13.58 ? 1034 MET A C   1 
ATOM   8141 O  O   . MET A 1 1034 ? 42.037 46.532  -13.716 1.00 13.89 ? 1034 MET A O   1 
ATOM   8142 C  CB  . MET A 1 1034 ? 40.197 46.115  -16.030 1.00 9.66  ? 1034 MET A CB  1 
ATOM   8143 C  CG  . MET A 1 1034 ? 39.351 46.652  -17.182 1.00 11.24 ? 1034 MET A CG  1 
ATOM   8144 S  SD  . MET A 1 1034 ? 39.328 48.453  -17.237 1.00 13.66 ? 1034 MET A SD  1 
ATOM   8145 C  CE  . MET A 1 1034 ? 38.237 48.999  -15.857 1.00 16.06 ? 1034 MET A CE  1 
ATOM   8146 N  N   . GLU A 1 1035 ? 43.656 45.680  -14.983 1.00 12.28 ? 1035 GLU A N   1 
ATOM   8147 C  CA  . GLU A 1 1035 ? 44.478 45.362  -13.821 1.00 12.49 ? 1035 GLU A CA  1 
ATOM   8148 C  C   . GLU A 1 1035 ? 45.524 46.387  -13.617 1.00 13.13 ? 1035 GLU A C   1 
ATOM   8149 O  O   . GLU A 1 1035 ? 45.846 47.099  -14.534 1.00 11.38 ? 1035 GLU A O   1 
ATOM   8150 C  CB  . GLU A 1 1035 ? 45.120 43.983  -13.980 1.00 16.68 ? 1035 GLU A CB  1 
ATOM   8151 C  CG  . GLU A 1 1035 ? 44.066 42.841  -13.825 1.00 21.55 ? 1035 GLU A CG  1 
ATOM   8152 C  CD  . GLU A 1 1035 ? 43.547 42.732  -12.378 1.00 26.78 ? 1035 GLU A CD  1 
ATOM   8153 O  OE1 . GLU A 1 1035 ? 44.275 43.200  -11.461 1.00 30.31 ? 1035 GLU A OE1 1 
ATOM   8154 O  OE2 . GLU A 1 1035 ? 42.436 42.167  -12.160 1.00 29.36 ? 1035 GLU A OE2 1 
ATOM   8155 N  N   . THR A 1 1036 ? 46.026 46.465  -12.380 1.00 9.85  ? 1036 THR A N   1 
ATOM   8156 C  CA  . THR A 1 1036 ? 47.082 47.406  -11.974 1.00 10.20 ? 1036 THR A CA  1 
ATOM   8157 C  C   . THR A 1 1036 ? 48.062 46.564  -11.155 1.00 9.09  ? 1036 THR A C   1 
ATOM   8158 O  O   . THR A 1 1036 ? 47.647 45.775  -10.278 1.00 11.33 ? 1036 THR A O   1 
ATOM   8159 C  CB  . THR A 1 1036 ? 46.525 48.565  -11.096 1.00 9.36  ? 1036 THR A CB  1 
ATOM   8160 O  OG1 . THR A 1 1036 ? 45.429 49.181  -11.808 1.00 10.44 ? 1036 THR A OG1 1 
ATOM   8161 C  CG2 . THR A 1 1036 ? 47.568 49.616  -10.798 1.00 12.38 ? 1036 THR A CG2 1 
ATOM   8162 N  N   . ALA A 1 1037 ? 49.351 46.694  -11.465 1.00 9.62  ? 1037 ALA A N   1 
ATOM   8163 C  CA  . ALA A 1 1037 ? 50.408 46.014  -10.694 1.00 10.35 ? 1037 ALA A CA  1 
ATOM   8164 C  C   . ALA A 1 1037 ? 51.494 47.000  -10.338 1.00 10.24 ? 1037 ALA A C   1 
ATOM   8165 O  O   . ALA A 1 1037 ? 51.580 48.089  -10.922 1.00 12.64 ? 1037 ALA A O   1 
ATOM   8166 C  CB  . ALA A 1 1037 ? 51.008 44.912  -11.508 1.00 11.57 ? 1037 ALA A CB  1 
ATOM   8167 N  N   . ALA A 1 1038 ? 52.319 46.615  -9.370  1.00 8.64  ? 1038 ALA A N   1 
ATOM   8168 C  CA  . ALA A 1 1038 ? 53.446 47.397  -8.955  1.00 8.50  ? 1038 ALA A CA  1 
ATOM   8169 C  C   . ALA A 1 1038 ? 54.710 46.562  -8.998  1.00 9.95  ? 1038 ALA A C   1 
ATOM   8170 O  O   . ALA A 1 1038 ? 54.683 45.388  -8.725  1.00 10.03 ? 1038 ALA A O   1 
ATOM   8171 C  CB  . ALA A 1 1038 ? 53.203 48.002  -7.547  1.00 8.99  ? 1038 ALA A CB  1 
ATOM   8172 N  N   . TYR A 1 1039 ? 55.802 47.208  -9.376  1.00 9.85  ? 1039 TYR A N   1 
ATOM   8173 C  CA  . TYR A 1 1039 ? 57.082 46.528  -9.446  1.00 11.11 ? 1039 TYR A CA  1 
ATOM   8174 C  C   . TYR A 1 1039 ? 58.143 47.397  -8.860  1.00 11.98 ? 1039 TYR A C   1 
ATOM   8175 O  O   . TYR A 1 1039 ? 58.082 48.625  -8.961  1.00 12.47 ? 1039 TYR A O   1 
ATOM   8176 C  CB  . TYR A 1 1039 ? 57.489 46.178  -10.907 1.00 11.39 ? 1039 TYR A CB  1 
ATOM   8177 C  CG  . TYR A 1 1039 ? 56.526 45.287  -11.628 1.00 10.23 ? 1039 TYR A CG  1 
ATOM   8178 C  CD1 . TYR A 1 1039 ? 56.469 43.873  -11.397 1.00 9.59  ? 1039 TYR A CD1 1 
ATOM   8179 C  CD2 . TYR A 1 1039 ? 55.597 45.817  -12.510 1.00 13.36 ? 1039 TYR A CD2 1 
ATOM   8180 C  CE1 . TYR A 1 1039 ? 55.511 43.077  -12.026 1.00 11.54 ? 1039 TYR A CE1 1 
ATOM   8181 C  CE2 . TYR A 1 1039 ? 54.660 45.008  -13.137 1.00 12.77 ? 1039 TYR A CE2 1 
ATOM   8182 C  CZ  . TYR A 1 1039 ? 54.612 43.658  -12.904 1.00 13.85 ? 1039 TYR A CZ  1 
ATOM   8183 O  OH  . TYR A 1 1039 ? 53.693 42.863  -13.574 1.00 15.42 ? 1039 TYR A OH  1 
ATOM   8184 N  N   . VAL A 1 1040 ? 59.147 46.754  -8.254  1.00 10.70 ? 1040 VAL A N   1 
ATOM   8185 C  CA  . VAL A 1 1040 ? 60.278 47.466  -7.701  1.00 12.02 ? 1040 VAL A CA  1 
ATOM   8186 C  C   . VAL A 1 1040 ? 61.545 46.805  -8.235  1.00 12.98 ? 1040 VAL A C   1 
ATOM   8187 O  O   . VAL A 1 1040 ? 61.714 45.555  -8.140  1.00 13.76 ? 1040 VAL A O   1 
ATOM   8188 C  CB  . VAL A 1 1040 ? 60.325 47.418  -6.156  1.00 10.14 ? 1040 VAL A CB  1 
ATOM   8189 C  CG1 . VAL A 1 1040 ? 61.703 48.053  -5.609  1.00 12.65 ? 1040 VAL A CG1 1 
ATOM   8190 C  CG2 . VAL A 1 1040 ? 59.137 48.183  -5.626  1.00 12.50 ? 1040 VAL A CG2 1 
ATOM   8191 N  N   . SER A 1 1041 ? 62.369 47.594  -8.922  1.00 12.20 ? 1041 SER A N   1 
ATOM   8192 C  CA  . SER A 1 1041 ? 63.635 47.099  -9.460  1.00 13.39 ? 1041 SER A CA  1 
ATOM   8193 C  C   . SER A 1 1041 ? 64.741 47.601  -8.518  1.00 13.27 ? 1041 SER A C   1 
ATOM   8194 O  O   . SER A 1 1041 ? 64.677 48.711  -7.995  1.00 13.75 ? 1041 SER A O   1 
ATOM   8195 C  CB  . SER A 1 1041 ? 63.855 47.595  -10.912 1.00 14.71 ? 1041 SER A CB  1 
ATOM   8196 O  OG  . SER A 1 1041 ? 63.916 49.016  -11.054 1.00 14.47 ? 1041 SER A OG  1 
ATOM   8197 N  N   . SER A 1 1042 ? 65.739 46.732  -8.291  1.00 12.71 ? 1042 SER A N   1 
ATOM   8198 C  CA  . SER A 1 1042 ? 66.870 47.037  -7.427  1.00 14.39 ? 1042 SER A CA  1 
ATOM   8199 C  C   . SER A 1 1042 ? 68.100 47.035  -8.347  1.00 12.36 ? 1042 SER A C   1 
ATOM   8200 O  O   . SER A 1 1042 ? 68.227 46.194  -9.264  1.00 16.31 ? 1042 SER A O   1 
ATOM   8201 C  CB  . SER A 1 1042 ? 67.024 45.961  -6.363  1.00 14.18 ? 1042 SER A CB  1 
ATOM   8202 O  OG  . SER A 1 1042 ? 65.855 45.919  -5.552  1.00 15.91 ? 1042 SER A OG  1 
ATOM   8203 N  N   . HIS A 1 1043 ? 68.976 48.010  -8.073  1.00 15.13 ? 1043 HIS A N   1 
ATOM   8204 C  CA  . HIS A 1 1043 ? 70.174 48.277  -8.886  1.00 16.60 ? 1043 HIS A CA  1 
ATOM   8205 C  C   . HIS A 1 1043 ? 71.405 48.425  -7.974  1.00 19.24 ? 1043 HIS A C   1 
ATOM   8206 O  O   . HIS A 1 1043 ? 71.385 49.117  -6.960  1.00 18.48 ? 1043 HIS A O   1 
ATOM   8207 C  CB  . HIS A 1 1043 ? 69.913 49.584  -9.657  1.00 16.92 ? 1043 HIS A CB  1 
ATOM   8208 C  CG  . HIS A 1 1043 ? 68.622 49.569  -10.427 1.00 17.29 ? 1043 HIS A CG  1 
ATOM   8209 N  ND1 . HIS A 1 1043 ? 68.537 49.151  -11.735 1.00 15.42 ? 1043 HIS A ND1 1 
ATOM   8210 C  CD2 . HIS A 1 1043 ? 67.349 49.832  -10.033 1.00 16.08 ? 1043 HIS A CD2 1 
ATOM   8211 C  CE1 . HIS A 1 1043 ? 67.268 49.148  -12.114 1.00 16.92 ? 1043 HIS A CE1 1 
ATOM   8212 N  NE2 . HIS A 1 1043 ? 66.532 49.558  -11.095 1.00 16.12 ? 1043 HIS A NE2 1 
ATOM   8213 N  N   . SER A 1 1044 ? 72.488 47.771  -8.361  1.00 22.56 ? 1044 SER A N   1 
ATOM   8214 C  CA  . SER A 1 1044 ? 73.686 47.808  -7.544  1.00 27.53 ? 1044 SER A CA  1 
ATOM   8215 C  C   . SER A 1 1044 ? 74.707 48.761  -8.077  1.00 29.72 ? 1044 SER A C   1 
ATOM   8216 O  O   . SER A 1 1044 ? 75.880 48.319  -7.972  1.00 31.03 ? 1044 SER A O   1 
ATOM   8217 C  CB  . SER A 1 1044 ? 74.327 46.414  -7.500  1.00 29.45 ? 1044 SER A CB  1 
ATOM   8218 O  OG  . SER A 1 1044 ? 74.288 45.813  -8.793  1.00 32.26 ? 1044 SER A OG  1 
HETATM 8219 C  C1  . NAG B 2 .    ? 58.494 44.695  12.939  1.00 35.35 ? 5004 NAG A C1  1 
HETATM 8220 C  C2  . NAG B 2 .    ? 59.470 44.192  14.018  1.00 38.49 ? 5004 NAG A C2  1 
HETATM 8221 C  C3  . NAG B 2 .    ? 59.888 42.764  13.659  1.00 40.63 ? 5004 NAG A C3  1 
HETATM 8222 C  C4  . NAG B 2 .    ? 58.645 41.914  13.697  1.00 41.18 ? 5004 NAG A C4  1 
HETATM 8223 C  C5  . NAG B 2 .    ? 57.659 42.425  12.643  1.00 41.26 ? 5004 NAG A C5  1 
HETATM 8224 C  C6  . NAG B 2 .    ? 56.354 41.675  12.773  1.00 42.33 ? 5004 NAG A C6  1 
HETATM 8225 C  C7  . NAG B 2 .    ? 61.422 45.302  13.087  1.00 42.28 ? 5004 NAG A C7  1 
HETATM 8226 C  C8  . NAG B 2 .    ? 62.717 44.503  13.000  1.00 43.26 ? 5004 NAG A C8  1 
HETATM 8227 N  N2  . NAG B 2 .    ? 60.622 45.074  14.134  1.00 40.58 ? 5004 NAG A N2  1 
HETATM 8228 O  O3  . NAG B 2 .    ? 60.839 42.265  14.587  1.00 41.95 ? 5004 NAG A O3  1 
HETATM 8229 O  O4  . NAG B 2 .    ? 58.978 40.551  13.464  1.00 43.37 ? 5004 NAG A O4  1 
HETATM 8230 O  O5  . NAG B 2 .    ? 57.346 43.832  12.865  1.00 38.07 ? 5004 NAG A O5  1 
HETATM 8231 O  O6  . NAG B 2 .    ? 55.944 41.626  14.143  1.00 43.41 ? 5004 NAG A O6  1 
HETATM 8232 O  O7  . NAG B 2 .    ? 61.166 46.134  12.211  1.00 43.15 ? 5004 NAG A O7  1 
HETATM 8233 ZN ZN  . ZN  C 3 .    ? 34.587 63.998  8.223   1.00 8.43  ? 5001 ZN  A ZN  1 
HETATM 8234 P  P   . PO4 D 4 .    ? 45.535 66.582  -28.444 1.00 28.67 ? 5005 PO4 A P   1 
HETATM 8235 O  O1  . PO4 D 4 .    ? 44.601 67.377  -29.460 1.00 32.15 ? 5005 PO4 A O1  1 
HETATM 8236 O  O2  . PO4 D 4 .    ? 46.902 66.268  -29.050 1.00 31.93 ? 5005 PO4 A O2  1 
HETATM 8237 O  O3  . PO4 D 4 .    ? 44.798 65.251  -28.088 1.00 29.72 ? 5005 PO4 A O3  1 
HETATM 8238 O  O4  . PO4 D 4 .    ? 45.706 67.534  -27.195 1.00 29.84 ? 5005 PO4 A O4  1 
HETATM 8239 C  C5  . MSN E 5 .    ? 31.319 65.877  9.450   1.00 9.46  ? 5002 MSN A C5  1 
HETATM 8240 N  N5  . MSN E 5 .    ? 31.148 64.508  9.944   1.00 9.35  ? 5002 MSN A N5  1 
HETATM 8241 C  C4  . MSN E 5 .    ? 32.801 66.188  9.512   1.00 8.64  ? 5002 MSN A C4  1 
HETATM 8242 O  O4  . MSN E 5 .    ? 33.622 65.088  9.913   1.00 9.38  ? 5002 MSN A O4  1 
HETATM 8243 C  C3  . MSN E 5 .    ? 33.074 66.715  8.099   1.00 10.63 ? 5002 MSN A C3  1 
HETATM 8244 O  O3  . MSN E 5 .    ? 33.836 65.824  7.291   1.00 8.47  ? 5002 MSN A O3  1 
HETATM 8245 C  C2  . MSN E 5 .    ? 31.799 67.049  7.331   1.00 9.08  ? 5002 MSN A C2  1 
HETATM 8246 O  O2  . MSN E 5 .    ? 31.766 67.289  5.923   1.00 7.80  ? 5002 MSN A O2  1 
HETATM 8247 C  C1  . MSN E 5 .    ? 30.936 65.949  7.979   1.00 8.48  ? 5002 MSN A C1  1 
HETATM 8248 S  S6  . MSN E 5 .    ? 29.232 66.518  8.017   1.00 12.15 ? 5002 MSN A S6  1 
HETATM 8249 C  C7  A MSN E 5 .    ? 28.420 65.373  9.143   0.50 5.26  ? 5002 MSN A C7  1 
HETATM 8250 C  C7  B MSN E 5 .    ? 28.591 66.069  6.397   0.50 6.80  ? 5002 MSN A C7  1 
HETATM 8251 C  C1  . MPD F 6 .    ? 16.492 62.332  10.510  1.00 23.24 ? 5003 MPD A C1  1 
HETATM 8252 C  C2  . MPD F 6 .    ? 16.161 60.865  10.698  1.00 23.18 ? 5003 MPD A C2  1 
HETATM 8253 O  O2  . MPD F 6 .    ? 14.757 60.715  10.334  1.00 21.65 ? 5003 MPD A O2  1 
HETATM 8254 C  CM  . MPD F 6 .    ? 16.974 59.981  9.750   1.00 21.67 ? 5003 MPD A CM  1 
HETATM 8255 C  C3  . MPD F 6 .    ? 16.269 60.422  12.206  1.00 21.42 ? 5003 MPD A C3  1 
HETATM 8256 C  C4  . MPD F 6 .    ? 17.663 60.324  12.886  1.00 21.62 ? 5003 MPD A C4  1 
HETATM 8257 O  O4  . MPD F 6 .    ? 17.636 59.429  13.997  1.00 15.83 ? 5003 MPD A O4  1 
HETATM 8258 C  C5  . MPD F 6 .    ? 18.169 61.680  13.447  1.00 23.04 ? 5003 MPD A C5  1 
HETATM 8259 O  O   . HOH G 7 .    ? 28.098 47.042  -31.468 1.00 28.51 ? 5006 HOH A O   1 
HETATM 8260 O  O   . HOH G 7 .    ? 28.476 44.381  -29.510 1.00 36.08 ? 5007 HOH A O   1 
HETATM 8261 O  O   . HOH G 7 .    ? 26.394 44.243  -27.394 1.00 36.23 ? 5008 HOH A O   1 
HETATM 8262 O  O   . HOH G 7 .    ? 27.022 41.781  -27.468 1.00 29.73 ? 5009 HOH A O   1 
HETATM 8263 O  O   . HOH G 7 .    ? 29.337 41.323  -25.570 1.00 25.13 ? 5010 HOH A O   1 
HETATM 8264 O  O   . HOH G 7 .    ? 28.072 39.243  -24.949 1.00 35.96 ? 5011 HOH A O   1 
HETATM 8265 O  O   . HOH G 7 .    ? 27.837 38.968  -22.627 1.00 29.05 ? 5012 HOH A O   1 
HETATM 8266 O  O   . HOH G 7 .    ? 28.735 41.328  -21.637 1.00 16.09 ? 5013 HOH A O   1 
HETATM 8267 O  O   . HOH G 7 .    ? 27.603 36.652  -19.717 1.00 26.63 ? 5014 HOH A O   1 
HETATM 8268 O  O   . HOH G 7 .    ? 25.974 36.473  -15.612 1.00 29.70 ? 5015 HOH A O   1 
HETATM 8269 O  O   . HOH G 7 .    ? 24.585 39.064  -11.556 1.00 25.94 ? 5016 HOH A O   1 
HETATM 8270 O  O   . HOH G 7 .    ? 22.220 40.472  -11.374 1.00 34.47 ? 5017 HOH A O   1 
HETATM 8271 O  O   . HOH G 7 .    ? 21.954 40.263  -8.867  1.00 27.51 ? 5018 HOH A O   1 
HETATM 8272 O  O   . HOH G 7 .    ? 20.884 42.700  -7.364  1.00 18.30 ? 5019 HOH A O   1 
HETATM 8273 O  O   . HOH G 7 .    ? 19.838 41.777  -5.110  1.00 28.04 ? 5020 HOH A O   1 
HETATM 8274 O  O   . HOH G 7 .    ? 19.260 42.595  -2.404  1.00 25.12 ? 5021 HOH A O   1 
HETATM 8275 O  O   . HOH G 7 .    ? 16.660 42.752  -2.424  1.00 24.35 ? 5022 HOH A O   1 
HETATM 8276 O  O   . HOH G 7 .    ? 20.000 38.953  -3.676  1.00 34.83 ? 5023 HOH A O   1 
HETATM 8277 O  O   . HOH G 7 .    ? 20.888 35.893  -4.507  1.00 37.24 ? 5024 HOH A O   1 
HETATM 8278 O  O   . HOH G 7 .    ? 22.092 36.606  0.145   1.00 21.13 ? 5025 HOH A O   1 
HETATM 8279 O  O   . HOH G 7 .    ? 23.646 34.515  -0.002  1.00 51.50 ? 5026 HOH A O   1 
HETATM 8280 O  O   . HOH G 7 .    ? 23.083 31.930  2.025   1.00 46.01 ? 5027 HOH A O   1 
HETATM 8281 O  O   . HOH G 7 .    ? 24.883 32.705  6.487   1.00 19.91 ? 5028 HOH A O   1 
HETATM 8282 O  O   . HOH G 7 .    ? 24.650 32.786  9.455   1.00 23.43 ? 5029 HOH A O   1 
HETATM 8283 O  O   . HOH G 7 .    ? 25.222 33.374  13.364  1.00 31.28 ? 5030 HOH A O   1 
HETATM 8284 O  O   . HOH G 7 .    ? 24.295 34.035  15.555  1.00 23.13 ? 5031 HOH A O   1 
HETATM 8285 O  O   . HOH G 7 .    ? 23.345 36.445  13.271  1.00 23.38 ? 5032 HOH A O   1 
HETATM 8286 O  O   . HOH G 7 .    ? 22.297 33.997  12.454  1.00 35.69 ? 5033 HOH A O   1 
HETATM 8287 O  O   . HOH G 7 .    ? 20.509 37.658  12.291  1.00 22.95 ? 5034 HOH A O   1 
HETATM 8288 O  O   . HOH G 7 .    ? 21.731 37.742  15.719  1.00 17.75 ? 5035 HOH A O   1 
HETATM 8289 O  O   . HOH G 7 .    ? 19.776 38.785  17.534  1.00 17.54 ? 5036 HOH A O   1 
HETATM 8290 O  O   . HOH G 7 .    ? 18.611 37.286  19.837  1.00 28.23 ? 5037 HOH A O   1 
HETATM 8291 O  O   . HOH G 7 .    ? 19.207 36.248  22.283  1.00 26.47 ? 5038 HOH A O   1 
HETATM 8292 O  O   . HOH G 7 .    ? 19.832 35.271  25.480  1.00 27.37 ? 5039 HOH A O   1 
HETATM 8293 O  O   . HOH G 7 .    ? 17.072 33.447  26.681  1.00 45.82 ? 5040 HOH A O   1 
HETATM 8294 O  O   . HOH G 7 .    ? 18.288 31.768  25.507  1.00 34.98 ? 5041 HOH A O   1 
HETATM 8295 O  O   . HOH G 7 .    ? 14.034 33.556  27.091  1.00 38.41 ? 5042 HOH A O   1 
HETATM 8296 O  O   . HOH G 7 .    ? 18.085 37.985  29.359  1.00 52.00 ? 5043 HOH A O   1 
HETATM 8297 O  O   . HOH G 7 .    ? 19.021 38.953  26.409  1.00 31.03 ? 5044 HOH A O   1 
HETATM 8298 O  O   . HOH G 7 .    ? 17.846 41.550  25.388  1.00 31.49 ? 5045 HOH A O   1 
HETATM 8299 O  O   . HOH G 7 .    ? 14.583 44.316  27.215  1.00 42.06 ? 5046 HOH A O   1 
HETATM 8300 O  O   . HOH G 7 .    ? 12.926 45.380  28.379  1.00 51.51 ? 5047 HOH A O   1 
HETATM 8301 O  O   . HOH G 7 .    ? 14.011 47.199  26.673  1.00 37.40 ? 5048 HOH A O   1 
HETATM 8302 O  O   . HOH G 7 .    ? 16.401 48.758  24.126  1.00 12.53 ? 5049 HOH A O   1 
HETATM 8303 O  O   . HOH G 7 .    ? 13.947 50.156  24.242  1.00 22.66 ? 5050 HOH A O   1 
HETATM 8304 O  O   . HOH G 7 .    ? 12.811 51.843  25.755  1.00 31.27 ? 5051 HOH A O   1 
HETATM 8305 O  O   . HOH G 7 .    ? 12.916 54.639  25.306  1.00 32.13 ? 5052 HOH A O   1 
HETATM 8306 O  O   . HOH G 7 .    ? 14.450 55.146  27.606  1.00 31.06 ? 5053 HOH A O   1 
HETATM 8307 O  O   . HOH G 7 .    ? 14.512 54.253  29.711  1.00 36.33 ? 5054 HOH A O   1 
HETATM 8308 O  O   . HOH G 7 .    ? 18.235 59.033  31.684  1.00 39.76 ? 5055 HOH A O   1 
HETATM 8309 O  O   . HOH G 7 .    ? 23.016 55.699  31.002  1.00 16.56 ? 5056 HOH A O   1 
HETATM 8310 O  O   . HOH G 7 .    ? 24.110 60.547  36.157  1.00 34.49 ? 5057 HOH A O   1 
HETATM 8311 O  O   . HOH G 7 .    ? 22.362 62.677  33.776  1.00 31.27 ? 5058 HOH A O   1 
HETATM 8312 O  O   . HOH G 7 .    ? 22.176 65.156  32.548  1.00 28.06 ? 5059 HOH A O   1 
HETATM 8313 O  O   . HOH G 7 .    ? 22.380 66.076  29.144  1.00 25.32 ? 5060 HOH A O   1 
HETATM 8314 O  O   . HOH G 7 .    ? 20.270 65.308  27.345  1.00 28.96 ? 5061 HOH A O   1 
HETATM 8315 O  O   . HOH G 7 .    ? 17.778 65.765  28.160  1.00 28.90 ? 5062 HOH A O   1 
HETATM 8316 O  O   . HOH G 7 .    ? 18.276 66.307  30.717  1.00 42.39 ? 5063 HOH A O   1 
HETATM 8317 O  O   . HOH G 7 .    ? 16.918 65.114  32.315  1.00 42.93 ? 5064 HOH A O   1 
HETATM 8318 O  O   . HOH G 7 .    ? 13.867 68.935  26.232  1.00 34.12 ? 5065 HOH A O   1 
HETATM 8319 O  O   . HOH G 7 .    ? 15.280 69.106  23.859  1.00 38.31 ? 5066 HOH A O   1 
HETATM 8320 O  O   . HOH G 7 .    ? 13.064 69.383  22.825  1.00 37.74 ? 5067 HOH A O   1 
HETATM 8321 O  O   . HOH G 7 .    ? 15.632 68.100  21.500  1.00 30.16 ? 5068 HOH A O   1 
HETATM 8322 O  O   . HOH G 7 .    ? 20.377 67.922  22.413  1.00 23.09 ? 5069 HOH A O   1 
HETATM 8323 O  O   . HOH G 7 .    ? 22.371 67.881  20.637  1.00 26.51 ? 5070 HOH A O   1 
HETATM 8324 O  O   . HOH G 7 .    ? 24.761 67.979  22.015  1.00 19.87 ? 5071 HOH A O   1 
HETATM 8325 O  O   . HOH G 7 .    ? 25.130 70.773  21.991  1.00 31.02 ? 5072 HOH A O   1 
HETATM 8326 O  O   . HOH G 7 .    ? 29.178 71.851  21.942  1.00 32.73 ? 5073 HOH A O   1 
HETATM 8327 O  O   . HOH G 7 .    ? 32.545 68.966  24.050  1.00 26.70 ? 5074 HOH A O   1 
HETATM 8328 O  O   . HOH G 7 .    ? 35.555 68.507  23.414  1.00 30.27 ? 5075 HOH A O   1 
HETATM 8329 O  O   . HOH G 7 .    ? 36.445 70.716  23.485  1.00 35.15 ? 5076 HOH A O   1 
HETATM 8330 O  O   . HOH G 7 .    ? 35.734 67.574  20.755  1.00 24.74 ? 5077 HOH A O   1 
HETATM 8331 O  O   . HOH G 7 .    ? 33.148 66.500  21.389  1.00 18.07 ? 5078 HOH A O   1 
HETATM 8332 O  O   . HOH G 7 .    ? 31.854 65.127  19.243  1.00 14.58 ? 5079 HOH A O   1 
HETATM 8333 O  O   . HOH G 7 .    ? 29.799 66.615  18.229  1.00 32.56 ? 5080 HOH A O   1 
HETATM 8334 O  O   . HOH G 7 .    ? 29.179 65.446  15.796  1.00 22.21 ? 5081 HOH A O   1 
HETATM 8335 O  O   . HOH G 7 .    ? 30.360 66.948  13.403  1.00 30.41 ? 5082 HOH A O   1 
HETATM 8336 O  O   . HOH G 7 .    ? 28.074 67.607  11.542  1.00 31.95 ? 5083 HOH A O   1 
HETATM 8337 O  O   . HOH G 7 .    ? 26.202 66.951  10.077  1.00 28.19 ? 5084 HOH A O   1 
HETATM 8338 O  O   . HOH G 7 .    ? 25.930 65.113  8.614   1.00 30.84 ? 5085 HOH A O   1 
HETATM 8339 O  O   . HOH G 7 .    ? 24.195 63.236  7.625   1.00 14.96 ? 5086 HOH A O   1 
HETATM 8340 O  O   . HOH G 7 .    ? 24.667 61.190  9.234   1.00 15.98 ? 5087 HOH A O   1 
HETATM 8341 O  O   . HOH G 7 .    ? 27.187 60.848  10.486  1.00 22.83 ? 5088 HOH A O   1 
HETATM 8342 O  O   . HOH G 7 .    ? 27.108 59.075  8.639   1.00 18.58 ? 5089 HOH A O   1 
HETATM 8343 O  O   . HOH G 7 .    ? 23.872 57.917  6.460   1.00 8.50  ? 5090 HOH A O   1 
HETATM 8344 O  O   . HOH G 7 .    ? 21.703 56.929  5.166   1.00 10.23 ? 5091 HOH A O   1 
HETATM 8345 O  O   . HOH G 7 .    ? 20.164 55.808  7.237   1.00 13.37 ? 5092 HOH A O   1 
HETATM 8346 O  O   . HOH G 7 .    ? 19.359 53.350  8.201   1.00 11.04 ? 5093 HOH A O   1 
HETATM 8347 O  O   . HOH G 7 .    ? 17.571 52.484  6.395   1.00 12.26 ? 5094 HOH A O   1 
HETATM 8348 O  O   . HOH G 7 .    ? 13.781 53.881  4.457   1.00 12.34 ? 5095 HOH A O   1 
HETATM 8349 O  O   . HOH G 7 .    ? 13.374 53.474  1.858   1.00 14.66 ? 5096 HOH A O   1 
HETATM 8350 O  O   . HOH G 7 .    ? 14.577 49.959  0.808   1.00 36.67 ? 5097 HOH A O   1 
HETATM 8351 O  O   . HOH G 7 .    ? 13.320 51.015  -1.683  1.00 32.31 ? 5098 HOH A O   1 
HETATM 8352 O  O   . HOH G 7 .    ? 11.834 47.525  -2.919  1.00 34.24 ? 5099 HOH A O   1 
HETATM 8353 O  O   . HOH G 7 .    ? 7.965  52.804  -7.091  1.00 32.24 ? 5100 HOH A O   1 
HETATM 8354 O  O   . HOH G 7 .    ? 8.711  54.727  -6.058  1.00 32.90 ? 5101 HOH A O   1 
HETATM 8355 O  O   . HOH G 7 .    ? 9.830  56.867  -5.734  1.00 24.86 ? 5102 HOH A O   1 
HETATM 8356 O  O   . HOH G 7 .    ? 11.931 59.386  -4.839  1.00 20.39 ? 5103 HOH A O   1 
HETATM 8357 O  O   . HOH G 7 .    ? 14.100 59.660  -3.166  1.00 15.73 ? 5104 HOH A O   1 
HETATM 8358 O  O   . HOH G 7 .    ? 14.079 57.832  -1.242  1.00 21.01 ? 5105 HOH A O   1 
HETATM 8359 O  O   . HOH G 7 .    ? 12.833 62.008  -2.191  1.00 29.70 ? 5106 HOH A O   1 
HETATM 8360 O  O   . HOH G 7 .    ? 10.916 65.270  -5.249  1.00 33.83 ? 5107 HOH A O   1 
HETATM 8361 O  O   . HOH G 7 .    ? 13.170 66.674  -4.467  1.00 17.42 ? 5108 HOH A O   1 
HETATM 8362 O  O   . HOH G 7 .    ? 14.165 68.294  -7.540  1.00 18.86 ? 5109 HOH A O   1 
HETATM 8363 O  O   . HOH G 7 .    ? 13.649 69.960  -9.602  1.00 30.96 ? 5110 HOH A O   1 
HETATM 8364 O  O   . HOH G 7 .    ? 12.855 66.337  -9.245  1.00 23.82 ? 5111 HOH A O   1 
HETATM 8365 O  O   . HOH G 7 .    ? 12.232 64.436  -12.039 1.00 37.22 ? 5112 HOH A O   1 
HETATM 8366 O  O   . HOH G 7 .    ? 14.291 62.834  -11.770 1.00 22.50 ? 5113 HOH A O   1 
HETATM 8367 O  O   . HOH G 7 .    ? 14.639 61.980  -14.364 1.00 23.27 ? 5114 HOH A O   1 
HETATM 8368 O  O   . HOH G 7 .    ? 14.491 63.926  -16.138 1.00 18.41 ? 5115 HOH A O   1 
HETATM 8369 O  O   . HOH G 7 .    ? 11.907 63.565  -16.590 1.00 20.75 ? 5116 HOH A O   1 
HETATM 8370 O  O   . HOH G 7 .    ? 10.238 62.822  -14.604 1.00 34.50 ? 5117 HOH A O   1 
HETATM 8371 O  O   . HOH G 7 .    ? 11.562 61.295  -18.151 1.00 19.60 ? 5118 HOH A O   1 
HETATM 8372 O  O   . HOH G 7 .    ? 13.503 62.466  -19.634 1.00 21.83 ? 5119 HOH A O   1 
HETATM 8373 O  O   . HOH G 7 .    ? 13.895 60.834  -22.277 1.00 16.05 ? 5120 HOH A O   1 
HETATM 8374 O  O   . HOH G 7 .    ? 12.427 61.907  -23.910 1.00 38.20 ? 5121 HOH A O   1 
HETATM 8375 O  O   . HOH G 7 .    ? 14.954 63.697  -25.414 1.00 22.44 ? 5122 HOH A O   1 
HETATM 8376 O  O   . HOH G 7 .    ? 17.037 67.156  -25.765 1.00 29.98 ? 5123 HOH A O   1 
HETATM 8377 O  O   . HOH G 7 .    ? 18.544 65.104  -26.694 1.00 25.13 ? 5124 HOH A O   1 
HETATM 8378 O  O   . HOH G 7 .    ? 16.822 60.497  -27.979 1.00 19.73 ? 5125 HOH A O   1 
HETATM 8379 O  O   . HOH G 7 .    ? 20.362 58.787  -21.762 1.00 11.00 ? 5126 HOH A O   1 
HETATM 8380 O  O   . HOH G 7 .    ? 18.258 59.721  -19.848 1.00 17.35 ? 5127 HOH A O   1 
HETATM 8381 O  O   . HOH G 7 .    ? 20.625 66.166  -19.499 1.00 12.65 ? 5128 HOH A O   1 
HETATM 8382 O  O   . HOH G 7 .    ? 16.584 67.874  -19.477 1.00 19.38 ? 5129 HOH A O   1 
HETATM 8383 O  O   . HOH G 7 .    ? 14.693 70.203  -19.995 1.00 28.03 ? 5130 HOH A O   1 
HETATM 8384 O  O   . HOH G 7 .    ? 14.659 70.644  -22.532 1.00 32.05 ? 5131 HOH A O   1 
HETATM 8385 O  O   . HOH G 7 .    ? 17.465 70.140  -23.211 1.00 18.66 ? 5132 HOH A O   1 
HETATM 8386 O  O   . HOH G 7 .    ? 15.021 73.861  -21.277 1.00 39.18 ? 5133 HOH A O   1 
HETATM 8387 O  O   . HOH G 7 .    ? 16.223 75.136  -23.804 1.00 37.94 ? 5134 HOH A O   1 
HETATM 8388 O  O   . HOH G 7 .    ? 16.058 72.079  -18.842 1.00 17.56 ? 5135 HOH A O   1 
HETATM 8389 O  O   . HOH G 7 .    ? 17.210 70.220  -15.995 1.00 14.85 ? 5136 HOH A O   1 
HETATM 8390 O  O   . HOH G 7 .    ? 14.857 66.367  -14.999 1.00 19.87 ? 5137 HOH A O   1 
HETATM 8391 O  O   . HOH G 7 .    ? 11.188 73.627  -17.458 1.00 30.03 ? 5138 HOH A O   1 
HETATM 8392 O  O   . HOH G 7 .    ? 12.913 74.721  -18.681 1.00 37.78 ? 5139 HOH A O   1 
HETATM 8393 O  O   . HOH G 7 .    ? 12.049 75.192  -13.670 1.00 29.19 ? 5140 HOH A O   1 
HETATM 8394 O  O   . HOH G 7 .    ? 15.466 76.999  -13.407 1.00 29.01 ? 5141 HOH A O   1 
HETATM 8395 O  O   . HOH G 7 .    ? 15.936 75.129  -11.340 1.00 23.35 ? 5142 HOH A O   1 
HETATM 8396 O  O   . HOH G 7 .    ? 20.258 74.225  -6.472  1.00 15.16 ? 5143 HOH A O   1 
HETATM 8397 O  O   . HOH G 7 .    ? 17.028 74.405  -2.727  1.00 16.57 ? 5144 HOH A O   1 
HETATM 8398 O  O   . HOH G 7 .    ? 12.757 70.958  -0.359  1.00 27.46 ? 5145 HOH A O   1 
HETATM 8399 O  O   . HOH G 7 .    ? 13.252 68.605  1.305   1.00 21.56 ? 5146 HOH A O   1 
HETATM 8400 O  O   . HOH G 7 .    ? 18.524 69.760  4.522   1.00 13.40 ? 5147 HOH A O   1 
HETATM 8401 O  O   . HOH G 7 .    ? 19.298 72.133  3.439   1.00 17.61 ? 5148 HOH A O   1 
HETATM 8402 O  O   . HOH G 7 .    ? 17.757 74.252  3.966   1.00 23.43 ? 5149 HOH A O   1 
HETATM 8403 O  O   . HOH G 7 .    ? 19.123 76.331  5.043   1.00 24.24 ? 5150 HOH A O   1 
HETATM 8404 O  O   . HOH G 7 .    ? 21.193 79.466  5.468   1.00 38.44 ? 5151 HOH A O   1 
HETATM 8405 O  O   . HOH G 7 .    ? 22.031 76.541  8.957   1.00 23.07 ? 5152 HOH A O   1 
HETATM 8406 O  O   . HOH G 7 .    ? 25.097 73.796  9.114   1.00 20.15 ? 5153 HOH A O   1 
HETATM 8407 O  O   . HOH G 7 .    ? 25.198 74.706  11.525  1.00 38.64 ? 5154 HOH A O   1 
HETATM 8408 O  O   . HOH G 7 .    ? 29.469 75.806  11.372  1.00 40.07 ? 5155 HOH A O   1 
HETATM 8409 O  O   . HOH G 7 .    ? 29.589 71.940  12.867  1.00 19.28 ? 5156 HOH A O   1 
HETATM 8410 O  O   . HOH G 7 .    ? 31.819 71.357  14.070  1.00 31.88 ? 5157 HOH A O   1 
HETATM 8411 O  O   . HOH G 7 .    ? 30.128 69.206  15.515  1.00 34.75 ? 5158 HOH A O   1 
HETATM 8412 O  O   . HOH G 7 .    ? 33.541 68.492  16.879  1.00 37.99 ? 5159 HOH A O   1 
HETATM 8413 O  O   . HOH G 7 .    ? 35.971 70.574  16.670  1.00 41.10 ? 5160 HOH A O   1 
HETATM 8414 O  O   . HOH G 7 .    ? 35.782 70.076  19.291  1.00 30.91 ? 5161 HOH A O   1 
HETATM 8415 O  O   . HOH G 7 .    ? 34.719 70.254  13.468  1.00 22.71 ? 5162 HOH A O   1 
HETATM 8416 O  O   . HOH G 7 .    ? 34.111 67.444  12.609  1.00 12.55 ? 5163 HOH A O   1 
HETATM 8417 O  O   . HOH G 7 .    ? 28.623 63.250  11.040  1.00 22.22 ? 5164 HOH A O   1 
HETATM 8418 O  O   . HOH G 7 .    ? 28.466 62.679  13.729  1.00 34.44 ? 5165 HOH A O   1 
HETATM 8419 O  O   . HOH G 7 .    ? 25.796 62.901  13.574  1.00 25.51 ? 5166 HOH A O   1 
HETATM 8420 O  O   . HOH G 7 .    ? 24.407 63.012  11.846  1.00 30.28 ? 5167 HOH A O   1 
HETATM 8421 O  O   . HOH G 7 .    ? 22.246 65.033  12.079  1.00 33.63 ? 5168 HOH A O   1 
HETATM 8422 O  O   . HOH G 7 .    ? 22.071 63.797  14.210  1.00 31.47 ? 5169 HOH A O   1 
HETATM 8423 O  O   . HOH G 7 .    ? 22.837 66.047  14.359  1.00 32.86 ? 5170 HOH A O   1 
HETATM 8424 O  O   . HOH G 7 .    ? 25.696 65.768  17.451  1.00 30.59 ? 5171 HOH A O   1 
HETATM 8425 O  O   . HOH G 7 .    ? 26.388 63.351  17.116  1.00 17.84 ? 5172 HOH A O   1 
HETATM 8426 O  O   . HOH G 7 .    ? 22.992 63.987  18.617  1.00 30.16 ? 5173 HOH A O   1 
HETATM 8427 O  O   . HOH G 7 .    ? 22.576 62.267  16.222  1.00 19.62 ? 5174 HOH A O   1 
HETATM 8428 O  O   . HOH G 7 .    ? 27.940 60.640  19.549  1.00 11.54 ? 5175 HOH A O   1 
HETATM 8429 O  O   . HOH G 7 .    ? 28.568 64.746  19.884  1.00 16.47 ? 5176 HOH A O   1 
HETATM 8430 O  O   . HOH G 7 .    ? 26.269 66.125  20.252  1.00 23.12 ? 5177 HOH A O   1 
HETATM 8431 O  O   . HOH G 7 .    ? 25.454 70.581  26.842  1.00 37.17 ? 5178 HOH A O   1 
HETATM 8432 O  O   . HOH G 7 .    ? 23.282 68.913  28.895  1.00 35.51 ? 5179 HOH A O   1 
HETATM 8433 O  O   . HOH G 7 .    ? 27.823 67.240  28.392  1.00 23.02 ? 5180 HOH A O   1 
HETATM 8434 O  O   . HOH G 7 .    ? 28.884 63.852  30.190  1.00 26.10 ? 5181 HOH A O   1 
HETATM 8435 O  O   . HOH G 7 .    ? 29.794 64.777  32.814  1.00 40.39 ? 5182 HOH A O   1 
HETATM 8436 O  O   . HOH G 7 .    ? 35.179 61.736  34.364  1.00 23.91 ? 5183 HOH A O   1 
HETATM 8437 O  O   . HOH G 7 .    ? 37.523 61.843  35.646  1.00 40.76 ? 5184 HOH A O   1 
HETATM 8438 O  O   . HOH G 7 .    ? 40.969 66.155  34.906  1.00 40.51 ? 5185 HOH A O   1 
HETATM 8439 O  O   . HOH G 7 .    ? 39.679 66.529  31.702  1.00 29.19 ? 5186 HOH A O   1 
HETATM 8440 O  O   . HOH G 7 .    ? 42.026 67.047  29.519  1.00 23.24 ? 5187 HOH A O   1 
HETATM 8441 O  O   . HOH G 7 .    ? 44.494 67.583  28.505  1.00 35.86 ? 5188 HOH A O   1 
HETATM 8442 O  O   . HOH G 7 .    ? 46.376 68.188  26.693  1.00 28.97 ? 5189 HOH A O   1 
HETATM 8443 O  O   . HOH G 7 .    ? 47.712 65.844  27.134  1.00 39.14 ? 5190 HOH A O   1 
HETATM 8444 O  O   . HOH G 7 .    ? 48.677 67.910  25.087  1.00 46.34 ? 5191 HOH A O   1 
HETATM 8445 O  O   . HOH G 7 .    ? 51.881 63.797  24.627  1.00 31.53 ? 5192 HOH A O   1 
HETATM 8446 O  O   . HOH G 7 .    ? 50.728 61.689  26.741  1.00 21.43 ? 5193 HOH A O   1 
HETATM 8447 O  O   . HOH G 7 .    ? 56.908 64.751  24.304  1.00 26.59 ? 5194 HOH A O   1 
HETATM 8448 O  O   . HOH G 7 .    ? 59.418 61.667  25.899  1.00 27.50 ? 5195 HOH A O   1 
HETATM 8449 O  O   . HOH G 7 .    ? 62.455 61.963  25.885  1.00 35.77 ? 5196 HOH A O   1 
HETATM 8450 O  O   . HOH G 7 .    ? 59.341 54.978  27.202  1.00 26.82 ? 5197 HOH A O   1 
HETATM 8451 O  O   . HOH G 7 .    ? 57.929 52.263  26.544  1.00 31.98 ? 5198 HOH A O   1 
HETATM 8452 O  O   . HOH G 7 .    ? 55.998 51.642  27.480  1.00 24.28 ? 5199 HOH A O   1 
HETATM 8453 O  O   . HOH G 7 .    ? 56.138 52.949  29.997  1.00 32.03 ? 5200 HOH A O   1 
HETATM 8454 O  O   . HOH G 7 .    ? 53.330 52.222  26.473  1.00 18.75 ? 5201 HOH A O   1 
HETATM 8455 O  O   . HOH G 7 .    ? 51.910 50.275  27.807  1.00 31.40 ? 5202 HOH A O   1 
HETATM 8456 O  O   . HOH G 7 .    ? 52.466 49.011  25.995  1.00 36.86 ? 5203 HOH A O   1 
HETATM 8457 O  O   . HOH G 7 .    ? 49.378 49.778  28.335  1.00 16.33 ? 5204 HOH A O   1 
HETATM 8458 O  O   . HOH G 7 .    ? 50.133 47.209  29.240  1.00 19.45 ? 5205 HOH A O   1 
HETATM 8459 O  O   . HOH G 7 .    ? 49.674 45.339  31.059  1.00 23.24 ? 5206 HOH A O   1 
HETATM 8460 O  O   . HOH G 7 .    ? 49.434 50.332  32.799  1.00 28.03 ? 5207 HOH A O   1 
HETATM 8461 O  O   . HOH G 7 .    ? 48.274 50.366  35.198  1.00 25.08 ? 5208 HOH A O   1 
HETATM 8462 O  O   . HOH G 7 .    ? 42.718 53.039  35.640  1.00 24.12 ? 5209 HOH A O   1 
HETATM 8463 O  O   . HOH G 7 .    ? 44.403 55.089  36.394  1.00 38.34 ? 5210 HOH A O   1 
HETATM 8464 O  O   . HOH G 7 .    ? 43.540 56.266  33.838  1.00 25.53 ? 5211 HOH A O   1 
HETATM 8465 O  O   . HOH G 7 .    ? 39.785 52.135  36.323  1.00 28.72 ? 5212 HOH A O   1 
HETATM 8466 O  O   . HOH G 7 .    ? 40.214 49.242  35.812  1.00 31.48 ? 5213 HOH A O   1 
HETATM 8467 O  O   . HOH G 7 .    ? 41.605 50.143  33.919  1.00 37.60 ? 5214 HOH A O   1 
HETATM 8468 O  O   . HOH G 7 .    ? 37.520 46.513  29.869  1.00 25.18 ? 5215 HOH A O   1 
HETATM 8469 O  O   . HOH G 7 .    ? 37.067 45.229  27.603  1.00 16.53 ? 5216 HOH A O   1 
HETATM 8470 O  O   . HOH G 7 .    ? 39.916 44.871  26.425  1.00 27.23 ? 5217 HOH A O   1 
HETATM 8471 O  O   . HOH G 7 .    ? 39.199 42.628  23.100  1.00 27.29 ? 5218 HOH A O   1 
HETATM 8472 O  O   . HOH G 7 .    ? 39.752 39.190  20.329  1.00 28.83 ? 5219 HOH A O   1 
HETATM 8473 O  O   . HOH G 7 .    ? 38.236 38.265  22.022  1.00 27.66 ? 5220 HOH A O   1 
HETATM 8474 O  O   . HOH G 7 .    ? 38.125 36.849  24.098  1.00 45.91 ? 5221 HOH A O   1 
HETATM 8475 O  O   . HOH G 7 .    ? 37.030 38.554  25.855  1.00 34.21 ? 5222 HOH A O   1 
HETATM 8476 O  O   . HOH G 7 .    ? 34.915 35.391  23.652  1.00 37.09 ? 5223 HOH A O   1 
HETATM 8477 O  O   . HOH G 7 .    ? 32.450 34.256  24.216  1.00 32.63 ? 5224 HOH A O   1 
HETATM 8478 O  O   . HOH G 7 .    ? 29.381 30.901  21.923  1.00 34.59 ? 5225 HOH A O   1 
HETATM 8479 O  O   . HOH G 7 .    ? 29.386 29.528  24.592  1.00 40.52 ? 5226 HOH A O   1 
HETATM 8480 O  O   . HOH G 7 .    ? 26.125 32.513  28.872  1.00 22.23 ? 5227 HOH A O   1 
HETATM 8481 O  O   . HOH G 7 .    ? 27.123 34.700  29.636  1.00 23.48 ? 5228 HOH A O   1 
HETATM 8482 O  O   . HOH G 7 .    ? 26.088 37.233  29.400  1.00 15.70 ? 5229 HOH A O   1 
HETATM 8483 O  O   . HOH G 7 .    ? 30.062 36.154  29.160  1.00 23.00 ? 5230 HOH A O   1 
HETATM 8484 O  O   . HOH G 7 .    ? 35.057 43.120  28.910  1.00 13.47 ? 5231 HOH A O   1 
HETATM 8485 O  O   . HOH G 7 .    ? 35.691 44.825  30.990  1.00 22.32 ? 5232 HOH A O   1 
HETATM 8486 O  O   . HOH G 7 .    ? 34.498 45.431  33.354  1.00 22.41 ? 5233 HOH A O   1 
HETATM 8487 O  O   . HOH G 7 .    ? 35.874 44.457  35.992  1.00 37.96 ? 5234 HOH A O   1 
HETATM 8488 O  O   . HOH G 7 .    ? 34.323 47.580  36.676  1.00 44.00 ? 5235 HOH A O   1 
HETATM 8489 O  O   . HOH G 7 .    ? 34.169 50.693  36.298  1.00 38.13 ? 5236 HOH A O   1 
HETATM 8490 O  O   . HOH G 7 .    ? 29.748 50.962  39.801  1.00 31.58 ? 5237 HOH A O   1 
HETATM 8491 O  O   . HOH G 7 .    ? 27.691 49.269  38.488  1.00 25.02 ? 5238 HOH A O   1 
HETATM 8492 O  O   . HOH G 7 .    ? 28.834 46.796  37.315  1.00 24.32 ? 5239 HOH A O   1 
HETATM 8493 O  O   . HOH G 7 .    ? 27.470 51.890  42.662  1.00 27.33 ? 5240 HOH A O   1 
HETATM 8494 O  O   . HOH G 7 .    ? 28.727 54.992  40.066  1.00 33.61 ? 5241 HOH A O   1 
HETATM 8495 O  O   . HOH G 7 .    ? 31.438 57.255  37.472  1.00 29.29 ? 5242 HOH A O   1 
HETATM 8496 O  O   . HOH G 7 .    ? 30.024 58.848  35.444  1.00 25.69 ? 5243 HOH A O   1 
HETATM 8497 O  O   . HOH G 7 .    ? 23.620 57.012  38.740  1.00 29.65 ? 5244 HOH A O   1 
HETATM 8498 O  O   . HOH G 7 .    ? 21.529 55.063  40.252  1.00 32.04 ? 5245 HOH A O   1 
HETATM 8499 O  O   . HOH G 7 .    ? 17.576 50.452  37.907  1.00 30.25 ? 5246 HOH A O   1 
HETATM 8500 O  O   . HOH G 7 .    ? 18.659 48.483  37.618  1.00 20.75 ? 5247 HOH A O   1 
HETATM 8501 O  O   . HOH G 7 .    ? 20.966 46.975  39.080  1.00 24.64 ? 5248 HOH A O   1 
HETATM 8502 O  O   . HOH G 7 .    ? 18.508 46.166  40.178  1.00 31.62 ? 5249 HOH A O   1 
HETATM 8503 O  O   . HOH G 7 .    ? 15.431 51.442  36.451  1.00 33.56 ? 5250 HOH A O   1 
HETATM 8504 O  O   . HOH G 7 .    ? 17.648 52.259  35.742  1.00 29.25 ? 5251 HOH A O   1 
HETATM 8505 O  O   . HOH G 7 .    ? 14.383 46.559  32.559  1.00 23.08 ? 5252 HOH A O   1 
HETATM 8506 O  O   . HOH G 7 .    ? 12.367 46.485  30.971  1.00 34.47 ? 5253 HOH A O   1 
HETATM 8507 O  O   . HOH G 7 .    ? 11.966 43.526  26.370  1.00 39.57 ? 5254 HOH A O   1 
HETATM 8508 O  O   . HOH G 7 .    ? 10.861 46.154  21.202  1.00 27.62 ? 5255 HOH A O   1 
HETATM 8509 O  O   . HOH G 7 .    ? 11.510 46.466  17.894  1.00 26.07 ? 5256 HOH A O   1 
HETATM 8510 O  O   . HOH G 7 .    ? 12.372 49.213  17.956  1.00 18.49 ? 5257 HOH A O   1 
HETATM 8511 O  O   . HOH G 7 .    ? 10.211 50.207  18.944  1.00 24.51 ? 5258 HOH A O   1 
HETATM 8512 O  O   . HOH G 7 .    ? 10.658 51.211  21.409  1.00 19.73 ? 5259 HOH A O   1 
HETATM 8513 O  O   . HOH G 7 .    ? 13.303 51.154  21.789  1.00 16.67 ? 5260 HOH A O   1 
HETATM 8514 O  O   . HOH G 7 .    ? 14.163 49.470  19.794  1.00 15.43 ? 5261 HOH A O   1 
HETATM 8515 O  O   . HOH G 7 .    ? 13.961 48.693  15.425  1.00 14.55 ? 5262 HOH A O   1 
HETATM 8516 O  O   . HOH G 7 .    ? 11.768 51.153  14.392  1.00 14.47 ? 5263 HOH A O   1 
HETATM 8517 O  O   . HOH G 7 .    ? 9.281  52.075  16.906  1.00 17.43 ? 5264 HOH A O   1 
HETATM 8518 O  O   . HOH G 7 .    ? 8.131  48.251  19.480  1.00 30.42 ? 5265 HOH A O   1 
HETATM 8519 O  O   . HOH G 7 .    ? 6.078  46.101  16.495  1.00 36.02 ? 5266 HOH A O   1 
HETATM 8520 O  O   . HOH G 7 .    ? 6.423  46.672  13.321  1.00 32.78 ? 5267 HOH A O   1 
HETATM 8521 O  O   . HOH G 7 .    ? 7.884  47.968  11.902  1.00 24.05 ? 5268 HOH A O   1 
HETATM 8522 O  O   . HOH G 7 .    ? 8.619  44.263  12.961  1.00 26.21 ? 5269 HOH A O   1 
HETATM 8523 O  O   . HOH G 7 .    ? 10.293 41.462  11.841  1.00 36.05 ? 5270 HOH A O   1 
HETATM 8524 O  O   . HOH G 7 .    ? 12.861 42.155  12.521  1.00 19.97 ? 5271 HOH A O   1 
HETATM 8525 O  O   . HOH G 7 .    ? 14.925 39.804  12.472  1.00 42.23 ? 5272 HOH A O   1 
HETATM 8526 O  O   . HOH G 7 .    ? 17.196 41.205  9.335   1.00 30.87 ? 5273 HOH A O   1 
HETATM 8527 O  O   . HOH G 7 .    ? 19.232 35.834  5.320   1.00 38.38 ? 5274 HOH A O   1 
HETATM 8528 O  O   . HOH G 7 .    ? 25.930 39.618  5.253   1.00 8.49  ? 5275 HOH A O   1 
HETATM 8529 O  O   . HOH G 7 .    ? 26.313 39.805  8.003   1.00 11.06 ? 5276 HOH A O   1 
HETATM 8530 O  O   . HOH G 7 .    ? 24.110 41.722  6.933   1.00 9.48  ? 5277 HOH A O   1 
HETATM 8531 O  O   . HOH G 7 .    ? 28.182 39.349  11.308  1.00 8.80  ? 5278 HOH A O   1 
HETATM 8532 O  O   . HOH G 7 .    ? 27.214 41.073  13.405  1.00 14.62 ? 5279 HOH A O   1 
HETATM 8533 O  O   . HOH G 7 .    ? 25.081 39.674  14.285  1.00 16.65 ? 5280 HOH A O   1 
HETATM 8534 O  O   . HOH G 7 .    ? 28.362 43.565  13.289  1.00 8.50  ? 5281 HOH A O   1 
HETATM 8535 O  O   . HOH G 7 .    ? 27.261 46.024  13.730  1.00 12.81 ? 5282 HOH A O   1 
HETATM 8536 O  O   . HOH G 7 .    ? 27.864 48.176  12.223  1.00 12.58 ? 5283 HOH A O   1 
HETATM 8537 O  O   . HOH G 7 .    ? 27.480 50.667  13.340  1.00 18.51 ? 5284 HOH A O   1 
HETATM 8538 O  O   . HOH G 7 .    ? 25.529 52.024  12.918  1.00 17.94 ? 5285 HOH A O   1 
HETATM 8539 O  O   . HOH G 7 .    ? 25.509 53.487  11.157  1.00 9.73  ? 5286 HOH A O   1 
HETATM 8540 O  O   . HOH G 7 .    ? 19.309 54.820  11.612  1.00 11.17 ? 5287 HOH A O   1 
HETATM 8541 O  O   . HOH G 7 .    ? 16.974 56.000  10.481  1.00 13.00 ? 5288 HOH A O   1 
HETATM 8542 O  O   . HOH G 7 .    ? 16.722 56.857  13.091  1.00 15.68 ? 5289 HOH A O   1 
HETATM 8543 O  O   . HOH G 7 .    ? 18.340 54.634  14.336  1.00 11.44 ? 5290 HOH A O   1 
HETATM 8544 O  O   . HOH G 7 .    ? 20.109 54.441  16.257  1.00 11.08 ? 5291 HOH A O   1 
HETATM 8545 O  O   . HOH G 7 .    ? 13.982 57.875  16.331  1.00 17.40 ? 5292 HOH A O   1 
HETATM 8546 O  O   . HOH G 7 .    ? 11.407 58.479  16.968  1.00 33.43 ? 5293 HOH A O   1 
HETATM 8547 O  O   . HOH G 7 .    ? 11.402 58.089  20.055  1.00 26.73 ? 5294 HOH A O   1 
HETATM 8548 O  O   . HOH G 7 .    ? 10.803 56.404  21.766  1.00 39.05 ? 5295 HOH A O   1 
HETATM 8549 O  O   . HOH G 7 .    ? 12.169 54.763  22.593  1.00 24.70 ? 5296 HOH A O   1 
HETATM 8550 O  O   . HOH G 7 .    ? 9.591  53.542  22.383  1.00 32.31 ? 5297 HOH A O   1 
HETATM 8551 O  O   . HOH G 7 .    ? 13.936 57.416  19.167  1.00 18.76 ? 5298 HOH A O   1 
HETATM 8552 O  O   . HOH G 7 .    ? 15.497 60.045  15.604  1.00 14.57 ? 5299 HOH A O   1 
HETATM 8553 O  O   . HOH G 7 .    ? 13.838 62.042  14.630  1.00 27.16 ? 5300 HOH A O   1 
HETATM 8554 O  O   . HOH G 7 .    ? 13.150 62.373  11.962  1.00 23.90 ? 5301 HOH A O   1 
HETATM 8555 O  O   . HOH G 7 .    ? 13.775 60.645  7.816   1.00 30.67 ? 5302 HOH A O   1 
HETATM 8556 O  O   . HOH G 7 .    ? 14.388 59.860  5.337   1.00 11.68 ? 5303 HOH A O   1 
HETATM 8557 O  O   . HOH G 7 .    ? 11.455 62.051  5.660   1.00 36.46 ? 5304 HOH A O   1 
HETATM 8558 O  O   . HOH G 7 .    ? 9.778  59.642  7.284   1.00 45.62 ? 5305 HOH A O   1 
HETATM 8559 O  O   . HOH G 7 .    ? 11.710 58.603  8.090   1.00 21.67 ? 5306 HOH A O   1 
HETATM 8560 O  O   . HOH G 7 .    ? 12.468 56.038  5.452   1.00 15.72 ? 5307 HOH A O   1 
HETATM 8561 O  O   . HOH G 7 .    ? 11.387 52.811  6.965   1.00 16.20 ? 5308 HOH A O   1 
HETATM 8562 O  O   . HOH G 7 .    ? 9.048  50.156  7.940   1.00 22.83 ? 5309 HOH A O   1 
HETATM 8563 O  O   . HOH G 7 .    ? 5.358  57.715  7.083   1.00 25.67 ? 5310 HOH A O   1 
HETATM 8564 O  O   . HOH G 7 .    ? 7.382  58.111  0.490   1.00 36.89 ? 5311 HOH A O   1 
HETATM 8565 O  O   . HOH G 7 .    ? 10.400 61.952  2.081   1.00 27.40 ? 5312 HOH A O   1 
HETATM 8566 O  O   . HOH G 7 .    ? 13.982 64.403  6.963   1.00 35.91 ? 5313 HOH A O   1 
HETATM 8567 O  O   . HOH G 7 .    ? 20.767 65.193  7.827   1.00 15.74 ? 5314 HOH A O   1 
HETATM 8568 O  O   . HOH G 7 .    ? 20.379 67.992  8.527   1.00 20.78 ? 5315 HOH A O   1 
HETATM 8569 O  O   . HOH G 7 .    ? 17.630 71.051  6.866   1.00 30.07 ? 5316 HOH A O   1 
HETATM 8570 O  O   . HOH G 7 .    ? 15.618 73.212  5.793   1.00 32.08 ? 5317 HOH A O   1 
HETATM 8571 O  O   . HOH G 7 .    ? 19.628 80.276  -0.401  1.00 26.88 ? 5318 HOH A O   1 
HETATM 8572 O  O   . HOH G 7 .    ? 21.564 78.328  -0.980  1.00 19.90 ? 5319 HOH A O   1 
HETATM 8573 O  O   . HOH G 7 .    ? 26.556 74.604  2.712   1.00 21.31 ? 5320 HOH A O   1 
HETATM 8574 O  O   . HOH G 7 .    ? 26.028 72.475  5.992   1.00 12.02 ? 5321 HOH A O   1 
HETATM 8575 O  O   . HOH G 7 .    ? 28.051 82.086  6.965   1.00 29.92 ? 5322 HOH A O   1 
HETATM 8576 O  O   . HOH G 7 .    ? 27.628 82.185  3.801   1.00 35.78 ? 5323 HOH A O   1 
HETATM 8577 O  O   . HOH G 7 .    ? 29.998 82.640  2.775   1.00 25.58 ? 5324 HOH A O   1 
HETATM 8578 O  O   . HOH G 7 .    ? 31.460 81.590  0.841   1.00 23.95 ? 5325 HOH A O   1 
HETATM 8579 O  O   . HOH G 7 .    ? 33.221 83.286  1.928   1.00 42.77 ? 5326 HOH A O   1 
HETATM 8580 O  O   . HOH G 7 .    ? 37.940 83.154  -0.340  1.00 22.33 ? 5327 HOH A O   1 
HETATM 8581 O  O   . HOH G 7 .    ? 37.647 80.492  -0.122  1.00 20.33 ? 5328 HOH A O   1 
HETATM 8582 O  O   . HOH G 7 .    ? 38.564 80.162  -2.537  1.00 30.69 ? 5329 HOH A O   1 
HETATM 8583 O  O   . HOH G 7 .    ? 36.484 79.050  -4.769  1.00 19.28 ? 5330 HOH A O   1 
HETATM 8584 O  O   . HOH G 7 .    ? 35.876 77.496  -6.981  1.00 15.47 ? 5331 HOH A O   1 
HETATM 8585 O  O   . HOH G 7 .    ? 34.672 78.965  -8.783  1.00 13.66 ? 5332 HOH A O   1 
HETATM 8586 O  O   . HOH G 7 .    ? 32.860 80.956  -11.428 1.00 10.98 ? 5333 HOH A O   1 
HETATM 8587 O  O   . HOH G 7 .    ? 33.695 83.553  -10.143 1.00 18.50 ? 5334 HOH A O   1 
HETATM 8588 O  O   . HOH G 7 .    ? 32.147 85.208  -8.234  1.00 25.39 ? 5335 HOH A O   1 
HETATM 8589 O  O   . HOH G 7 .    ? 32.889 85.234  -5.281  1.00 21.86 ? 5336 HOH A O   1 
HETATM 8590 O  O   . HOH G 7 .    ? 35.860 85.795  -7.481  1.00 35.88 ? 5337 HOH A O   1 
HETATM 8591 O  O   . HOH G 7 .    ? 34.214 87.098  -9.857  1.00 38.96 ? 5338 HOH A O   1 
HETATM 8592 O  O   . HOH G 7 .    ? 32.560 88.954  -13.367 1.00 31.93 ? 5339 HOH A O   1 
HETATM 8593 O  O   . HOH G 7 .    ? 30.524 87.218  -14.618 1.00 26.98 ? 5340 HOH A O   1 
HETATM 8594 O  O   . HOH G 7 .    ? 28.091 85.956  -14.228 1.00 36.08 ? 5341 HOH A O   1 
HETATM 8595 O  O   . HOH G 7 .    ? 29.544 87.367  -17.240 1.00 27.52 ? 5342 HOH A O   1 
HETATM 8596 O  O   . HOH G 7 .    ? 31.718 85.831  -19.543 1.00 19.26 ? 5343 HOH A O   1 
HETATM 8597 O  O   . HOH G 7 .    ? 33.361 84.296  -17.953 1.00 20.24 ? 5344 HOH A O   1 
HETATM 8598 O  O   . HOH G 7 .    ? 35.595 86.616  -17.654 1.00 36.28 ? 5345 HOH A O   1 
HETATM 8599 O  O   . HOH G 7 .    ? 40.386 86.655  -20.760 1.00 30.62 ? 5346 HOH A O   1 
HETATM 8600 O  O   . HOH G 7 .    ? 39.847 81.834  -21.623 1.00 28.41 ? 5347 HOH A O   1 
HETATM 8601 O  O   . HOH G 7 .    ? 42.303 79.646  -23.052 1.00 30.72 ? 5348 HOH A O   1 
HETATM 8602 O  O   . HOH G 7 .    ? 44.071 79.039  -20.791 1.00 29.74 ? 5349 HOH A O   1 
HETATM 8603 O  O   . HOH G 7 .    ? 47.071 80.649  -21.578 1.00 28.69 ? 5350 HOH A O   1 
HETATM 8604 O  O   . HOH G 7 .    ? 46.408 80.409  -24.959 1.00 39.76 ? 5351 HOH A O   1 
HETATM 8605 O  O   . HOH G 7 .    ? 45.821 82.873  -24.791 1.00 34.15 ? 5352 HOH A O   1 
HETATM 8606 O  O   . HOH G 7 .    ? 44.438 83.700  -27.568 1.00 30.00 ? 5353 HOH A O   1 
HETATM 8607 O  O   . HOH G 7 .    ? 44.900 82.683  -29.970 1.00 33.10 ? 5354 HOH A O   1 
HETATM 8608 O  O   . HOH G 7 .    ? 42.724 80.534  -31.751 1.00 47.52 ? 5355 HOH A O   1 
HETATM 8609 O  O   . HOH G 7 .    ? 44.761 79.299  -33.049 1.00 30.99 ? 5356 HOH A O   1 
HETATM 8610 O  O   . HOH G 7 .    ? 42.552 78.660  -29.746 1.00 29.43 ? 5357 HOH A O   1 
HETATM 8611 O  O   . HOH G 7 .    ? 43.084 79.861  -27.486 1.00 40.48 ? 5358 HOH A O   1 
HETATM 8612 O  O   . HOH G 7 .    ? 40.403 79.354  -28.079 1.00 28.65 ? 5359 HOH A O   1 
HETATM 8613 O  O   . HOH G 7 .    ? 41.343 82.966  -28.631 1.00 33.58 ? 5360 HOH A O   1 
HETATM 8614 O  O   . HOH G 7 .    ? 40.733 82.813  -31.065 1.00 32.48 ? 5361 HOH A O   1 
HETATM 8615 O  O   . HOH G 7 .    ? 38.275 81.732  -31.143 1.00 14.56 ? 5362 HOH A O   1 
HETATM 8616 O  O   . HOH G 7 .    ? 39.315 83.343  -27.070 1.00 22.57 ? 5363 HOH A O   1 
HETATM 8617 O  O   . HOH G 7 .    ? 46.452 77.785  -25.548 1.00 28.16 ? 5364 HOH A O   1 
HETATM 8618 O  O   . HOH G 7 .    ? 48.110 74.635  -28.514 1.00 32.32 ? 5365 HOH A O   1 
HETATM 8619 O  O   . HOH G 7 .    ? 48.696 72.263  -25.994 1.00 33.78 ? 5366 HOH A O   1 
HETATM 8620 O  O   . HOH G 7 .    ? 47.186 72.931  -24.307 1.00 34.45 ? 5367 HOH A O   1 
HETATM 8621 O  O   . HOH G 7 .    ? 50.514 73.580  -24.964 1.00 37.23 ? 5368 HOH A O   1 
HETATM 8622 O  O   . HOH G 7 .    ? 51.151 70.808  -23.318 1.00 18.98 ? 5369 HOH A O   1 
HETATM 8623 O  O   . HOH G 7 .    ? 50.053 73.263  -21.451 1.00 20.28 ? 5370 HOH A O   1 
HETATM 8624 O  O   . HOH G 7 .    ? 51.449 71.389  -20.012 1.00 21.76 ? 5371 HOH A O   1 
HETATM 8625 O  O   . HOH G 7 .    ? 53.752 72.656  -19.006 1.00 14.87 ? 5372 HOH A O   1 
HETATM 8626 O  O   . HOH G 7 .    ? 53.235 70.826  -16.740 1.00 27.62 ? 5373 HOH A O   1 
HETATM 8627 O  O   . HOH G 7 .    ? 50.146 70.828  -17.468 1.00 29.48 ? 5374 HOH A O   1 
HETATM 8628 O  O   . HOH G 7 .    ? 47.668 70.081  -16.592 1.00 25.01 ? 5375 HOH A O   1 
HETATM 8629 O  O   . HOH G 7 .    ? 45.341 69.510  -17.338 1.00 27.87 ? 5376 HOH A O   1 
HETATM 8630 O  O   . HOH G 7 .    ? 46.452 67.657  -15.383 1.00 13.40 ? 5377 HOH A O   1 
HETATM 8631 O  O   . HOH G 7 .    ? 47.165 72.462  -17.357 1.00 26.55 ? 5378 HOH A O   1 
HETATM 8632 O  O   . HOH G 7 .    ? 47.573 71.787  -20.106 1.00 22.47 ? 5379 HOH A O   1 
HETATM 8633 O  O   . HOH G 7 .    ? 47.763 67.403  -25.070 1.00 26.42 ? 5380 HOH A O   1 
HETATM 8634 O  O   . HOH G 7 .    ? 48.030 64.031  -25.510 1.00 24.38 ? 5381 HOH A O   1 
HETATM 8635 O  O   . HOH G 7 .    ? 46.637 61.784  -25.779 1.00 17.39 ? 5382 HOH A O   1 
HETATM 8636 O  O   . HOH G 7 .    ? 48.072 59.365  -25.417 1.00 13.66 ? 5383 HOH A O   1 
HETATM 8637 O  O   . HOH G 7 .    ? 49.539 59.324  -28.307 1.00 19.03 ? 5384 HOH A O   1 
HETATM 8638 O  O   . HOH G 7 .    ? 50.459 58.517  -30.684 1.00 30.56 ? 5385 HOH A O   1 
HETATM 8639 O  O   . HOH G 7 .    ? 50.516 60.979  -30.621 1.00 22.40 ? 5386 HOH A O   1 
HETATM 8640 O  O   . HOH G 7 .    ? 48.310 64.412  -28.380 1.00 21.19 ? 5387 HOH A O   1 
HETATM 8641 O  O   . HOH G 7 .    ? 47.461 68.083  -30.572 1.00 20.20 ? 5388 HOH A O   1 
HETATM 8642 O  O   . HOH G 7 .    ? 48.620 66.698  -33.424 1.00 36.45 ? 5389 HOH A O   1 
HETATM 8643 O  O   . HOH G 7 .    ? 48.961 69.215  -36.546 1.00 30.48 ? 5390 HOH A O   1 
HETATM 8644 O  O   . HOH G 7 .    ? 46.638 70.332  -36.386 1.00 21.00 ? 5391 HOH A O   1 
HETATM 8645 O  O   . HOH G 7 .    ? 46.298 70.320  -39.416 1.00 29.79 ? 5392 HOH A O   1 
HETATM 8646 O  O   . HOH G 7 .    ? 44.012 72.655  -41.693 1.00 18.91 ? 5393 HOH A O   1 
HETATM 8647 O  O   . HOH G 7 .    ? 42.392 74.698  -41.520 1.00 28.89 ? 5394 HOH A O   1 
HETATM 8648 O  O   . HOH G 7 .    ? 39.849 75.471  -39.915 1.00 23.93 ? 5395 HOH A O   1 
HETATM 8649 O  O   . HOH G 7 .    ? 37.826 75.687  -42.171 1.00 22.47 ? 5396 HOH A O   1 
HETATM 8650 O  O   . HOH G 7 .    ? 35.981 77.433  -42.689 1.00 35.63 ? 5397 HOH A O   1 
HETATM 8651 O  O   . HOH G 7 .    ? 31.268 79.003  -42.626 1.00 26.19 ? 5398 HOH A O   1 
HETATM 8652 O  O   . HOH G 7 .    ? 30.253 81.660  -42.967 1.00 31.74 ? 5399 HOH A O   1 
HETATM 8653 O  O   . HOH G 7 .    ? 34.160 86.944  -43.121 1.00 42.27 ? 5400 HOH A O   1 
HETATM 8654 O  O   . HOH G 7 .    ? 32.510 89.081  -42.809 1.00 24.07 ? 5401 HOH A O   1 
HETATM 8655 O  O   . HOH G 7 .    ? 28.292 90.646  -42.554 1.00 24.63 ? 5402 HOH A O   1 
HETATM 8656 O  O   . HOH G 7 .    ? 28.090 88.088  -41.323 1.00 24.44 ? 5403 HOH A O   1 
HETATM 8657 O  O   . HOH G 7 .    ? 25.799 87.717  -42.745 1.00 28.53 ? 5404 HOH A O   1 
HETATM 8658 O  O   . HOH G 7 .    ? 23.679 86.085  -40.596 1.00 36.50 ? 5405 HOH A O   1 
HETATM 8659 O  O   . HOH G 7 .    ? 23.183 88.319  -38.158 1.00 34.38 ? 5406 HOH A O   1 
HETATM 8660 O  O   . HOH G 7 .    ? 23.445 82.511  -40.374 1.00 20.86 ? 5407 HOH A O   1 
HETATM 8661 O  O   . HOH G 7 .    ? 22.249 80.489  -42.101 1.00 30.36 ? 5408 HOH A O   1 
HETATM 8662 O  O   . HOH G 7 .    ? 22.151 80.506  -35.667 1.00 27.01 ? 5409 HOH A O   1 
HETATM 8663 O  O   . HOH G 7 .    ? 20.667 80.488  -33.389 1.00 38.61 ? 5410 HOH A O   1 
HETATM 8664 O  O   . HOH G 7 .    ? 22.879 78.587  -30.380 1.00 23.40 ? 5411 HOH A O   1 
HETATM 8665 O  O   . HOH G 7 .    ? 22.538 77.398  -27.013 1.00 36.27 ? 5412 HOH A O   1 
HETATM 8666 O  O   . HOH G 7 .    ? 23.255 78.502  -24.461 1.00 21.62 ? 5413 HOH A O   1 
HETATM 8667 O  O   . HOH G 7 .    ? 21.034 79.332  -23.313 1.00 25.29 ? 5414 HOH A O   1 
HETATM 8668 O  O   . HOH G 7 .    ? 19.323 83.310  -25.696 1.00 35.18 ? 5415 HOH A O   1 
HETATM 8669 O  O   . HOH G 7 .    ? 18.828 86.474  -24.952 1.00 42.05 ? 5416 HOH A O   1 
HETATM 8670 O  O   . HOH G 7 .    ? 16.828 84.822  -23.555 1.00 42.49 ? 5417 HOH A O   1 
HETATM 8671 O  O   . HOH G 7 .    ? 19.985 84.212  -18.385 1.00 29.68 ? 5418 HOH A O   1 
HETATM 8672 O  O   . HOH G 7 .    ? 21.695 86.005  -18.722 1.00 48.20 ? 5419 HOH A O   1 
HETATM 8673 O  O   . HOH G 7 .    ? 18.789 83.778  -15.876 1.00 33.59 ? 5420 HOH A O   1 
HETATM 8674 O  O   . HOH G 7 .    ? 17.599 81.385  -16.391 1.00 32.29 ? 5421 HOH A O   1 
HETATM 8675 O  O   . HOH G 7 .    ? 18.545 82.125  -10.949 1.00 41.96 ? 5422 HOH A O   1 
HETATM 8676 O  O   . HOH G 7 .    ? 17.455 80.779  -7.112  1.00 18.31 ? 5423 HOH A O   1 
HETATM 8677 O  O   . HOH G 7 .    ? 10.594 77.073  -4.253  1.00 36.90 ? 5424 HOH A O   1 
HETATM 8678 O  O   . HOH G 7 .    ? 13.230 83.108  2.665   1.00 40.31 ? 5425 HOH A O   1 
HETATM 8679 O  O   . HOH G 7 .    ? 16.153 83.158  2.828   1.00 42.05 ? 5426 HOH A O   1 
HETATM 8680 O  O   . HOH G 7 .    ? 25.170 83.520  3.749   1.00 34.23 ? 5427 HOH A O   1 
HETATM 8681 O  O   . HOH G 7 .    ? 24.886 86.977  -0.690  1.00 39.10 ? 5428 HOH A O   1 
HETATM 8682 O  O   . HOH G 7 .    ? 27.957 88.652  -11.528 1.00 38.56 ? 5429 HOH A O   1 
HETATM 8683 O  O   . HOH G 7 .    ? 25.096 83.269  -16.466 1.00 25.32 ? 5430 HOH A O   1 
HETATM 8684 O  O   . HOH G 7 .    ? 26.980 87.608  -23.616 1.00 29.29 ? 5431 HOH A O   1 
HETATM 8685 O  O   . HOH G 7 .    ? 29.628 88.627  -26.020 1.00 16.71 ? 5432 HOH A O   1 
HETATM 8686 O  O   . HOH G 7 .    ? 28.222 90.835  -25.168 1.00 25.51 ? 5433 HOH A O   1 
HETATM 8687 O  O   . HOH G 7 .    ? 26.577 91.546  -27.422 1.00 27.63 ? 5434 HOH A O   1 
HETATM 8688 O  O   . HOH G 7 .    ? 23.909 90.832  -25.718 1.00 39.00 ? 5435 HOH A O   1 
HETATM 8689 O  O   . HOH G 7 .    ? 26.040 91.632  -31.827 1.00 34.20 ? 5436 HOH A O   1 
HETATM 8690 O  O   . HOH G 7 .    ? 27.332 89.710  -31.573 1.00 35.19 ? 5437 HOH A O   1 
HETATM 8691 O  O   . HOH G 7 .    ? 25.625 85.995  -31.620 1.00 21.87 ? 5438 HOH A O   1 
HETATM 8692 O  O   . HOH G 7 .    ? 23.509 86.986  -32.078 1.00 32.67 ? 5439 HOH A O   1 
HETATM 8693 O  O   . HOH G 7 .    ? 21.949 85.229  -31.137 1.00 55.36 ? 5440 HOH A O   1 
HETATM 8694 O  O   . HOH G 7 .    ? 28.168 84.508  -35.234 1.00 15.61 ? 5441 HOH A O   1 
HETATM 8695 O  O   . HOH G 7 .    ? 28.929 81.867  -35.461 1.00 20.12 ? 5442 HOH A O   1 
HETATM 8696 O  O   . HOH G 7 .    ? 32.433 77.600  -29.521 1.00 16.32 ? 5443 HOH A O   1 
HETATM 8697 O  O   . HOH G 7 .    ? 30.415 74.983  -29.056 1.00 17.72 ? 5444 HOH A O   1 
HETATM 8698 O  O   . HOH G 7 .    ? 34.214 64.653  -32.052 1.00 19.13 ? 5445 HOH A O   1 
HETATM 8699 O  O   . HOH G 7 .    ? 36.084 63.408  -33.407 1.00 25.63 ? 5446 HOH A O   1 
HETATM 8700 O  O   . HOH G 7 .    ? 37.681 61.539  -32.531 1.00 28.00 ? 5447 HOH A O   1 
HETATM 8701 O  O   . HOH G 7 .    ? 37.070 59.284  -33.491 1.00 25.87 ? 5448 HOH A O   1 
HETATM 8702 O  O   . HOH G 7 .    ? 34.943 59.617  -34.808 1.00 28.15 ? 5449 HOH A O   1 
HETATM 8703 O  O   . HOH G 7 .    ? 33.772 57.282  -35.798 1.00 19.38 ? 5450 HOH A O   1 
HETATM 8704 O  O   . HOH G 7 .    ? 35.375 55.362  -34.235 1.00 38.19 ? 5451 HOH A O   1 
HETATM 8705 O  O   . HOH G 7 .    ? 36.676 56.884  -32.208 1.00 35.08 ? 5452 HOH A O   1 
HETATM 8706 O  O   . HOH G 7 .    ? 38.762 55.276  -31.418 1.00 18.61 ? 5453 HOH A O   1 
HETATM 8707 O  O   . HOH G 7 .    ? 40.827 56.183  -33.241 1.00 26.79 ? 5454 HOH A O   1 
HETATM 8708 O  O   . HOH G 7 .    ? 43.117 57.035  -31.542 1.00 27.38 ? 5455 HOH A O   1 
HETATM 8709 O  O   . HOH G 7 .    ? 43.122 59.740  -31.381 1.00 33.64 ? 5456 HOH A O   1 
HETATM 8710 O  O   . HOH G 7 .    ? 41.775 61.469  -29.403 1.00 23.27 ? 5457 HOH A O   1 
HETATM 8711 O  O   . HOH G 7 .    ? 44.007 63.065  -28.360 1.00 35.76 ? 5458 HOH A O   1 
HETATM 8712 O  O   . HOH G 7 .    ? 43.616 64.213  -31.187 1.00 45.49 ? 5459 HOH A O   1 
HETATM 8713 O  O   . HOH G 7 .    ? 43.737 66.627  -31.852 1.00 20.71 ? 5460 HOH A O   1 
HETATM 8714 O  O   . HOH G 7 .    ? 41.351 68.236  -32.527 1.00 18.40 ? 5461 HOH A O   1 
HETATM 8715 O  O   . HOH G 7 .    ? 39.472 69.383  -35.277 1.00 19.64 ? 5462 HOH A O   1 
HETATM 8716 O  O   . HOH G 7 .    ? 38.718 69.212  -38.058 1.00 18.58 ? 5463 HOH A O   1 
HETATM 8717 O  O   . HOH G 7 .    ? 40.778 71.616  -43.810 1.00 33.96 ? 5464 HOH A O   1 
HETATM 8718 O  O   . HOH G 7 .    ? 44.230 77.484  -43.319 1.00 39.89 ? 5465 HOH A O   1 
HETATM 8719 O  O   . HOH G 7 .    ? 46.784 80.131  -42.397 1.00 34.79 ? 5466 HOH A O   1 
HETATM 8720 O  O   . HOH G 7 .    ? 47.526 79.068  -40.235 1.00 19.70 ? 5467 HOH A O   1 
HETATM 8721 O  O   . HOH G 7 .    ? 51.563 76.293  -40.638 1.00 23.79 ? 5468 HOH A O   1 
HETATM 8722 O  O   . HOH G 7 .    ? 52.030 70.273  -37.866 1.00 23.44 ? 5469 HOH A O   1 
HETATM 8723 O  O   . HOH G 7 .    ? 54.208 71.241  -36.667 1.00 13.77 ? 5470 HOH A O   1 
HETATM 8724 O  O   . HOH G 7 .    ? 55.485 68.967  -37.362 1.00 30.74 ? 5471 HOH A O   1 
HETATM 8725 O  O   . HOH G 7 .    ? 56.655 70.163  -39.289 1.00 31.03 ? 5472 HOH A O   1 
HETATM 8726 O  O   . HOH G 7 .    ? 56.896 67.614  -35.280 1.00 30.97 ? 5473 HOH A O   1 
HETATM 8727 O  O   . HOH G 7 .    ? 56.404 65.222  -35.975 1.00 22.87 ? 5474 HOH A O   1 
HETATM 8728 O  O   . HOH G 7 .    ? 59.518 67.128  -34.358 1.00 28.69 ? 5475 HOH A O   1 
HETATM 8729 O  O   . HOH G 7 .    ? 63.379 67.844  -31.271 1.00 29.24 ? 5476 HOH A O   1 
HETATM 8730 O  O   . HOH G 7 .    ? 65.921 68.147  -30.910 1.00 35.99 ? 5477 HOH A O   1 
HETATM 8731 O  O   . HOH G 7 .    ? 61.772 63.747  -30.590 1.00 37.78 ? 5478 HOH A O   1 
HETATM 8732 O  O   . HOH G 7 .    ? 67.074 60.045  -27.110 1.00 33.29 ? 5479 HOH A O   1 
HETATM 8733 O  O   . HOH G 7 .    ? 68.275 57.552  -26.517 1.00 36.03 ? 5480 HOH A O   1 
HETATM 8734 O  O   . HOH G 7 .    ? 68.113 58.719  -23.747 1.00 31.81 ? 5481 HOH A O   1 
HETATM 8735 O  O   . HOH G 7 .    ? 70.059 55.236  -22.283 1.00 30.05 ? 5482 HOH A O   1 
HETATM 8736 O  O   . HOH G 7 .    ? 66.749 56.361  -19.927 1.00 21.63 ? 5483 HOH A O   1 
HETATM 8737 O  O   . HOH G 7 .    ? 67.889 54.925  -17.873 1.00 23.22 ? 5484 HOH A O   1 
HETATM 8738 O  O   . HOH G 7 .    ? 70.807 52.053  -12.370 1.00 20.97 ? 5485 HOH A O   1 
HETATM 8739 O  O   . HOH G 7 .    ? 73.633 51.467  -11.230 1.00 29.48 ? 5486 HOH A O   1 
HETATM 8740 O  O   . HOH G 7 .    ? 70.337 53.740  -9.469  1.00 30.12 ? 5487 HOH A O   1 
HETATM 8741 O  O   . HOH G 7 .    ? 72.256 58.618  -10.503 1.00 28.99 ? 5488 HOH A O   1 
HETATM 8742 O  O   . HOH G 7 .    ? 74.748 62.876  -7.648  1.00 40.96 ? 5489 HOH A O   1 
HETATM 8743 O  O   . HOH G 7 .    ? 73.210 65.048  -7.267  1.00 21.07 ? 5490 HOH A O   1 
HETATM 8744 O  O   . HOH G 7 .    ? 73.201 66.704  -9.492  1.00 20.54 ? 5491 HOH A O   1 
HETATM 8745 O  O   . HOH G 7 .    ? 75.595 67.048  -9.471  1.00 35.12 ? 5492 HOH A O   1 
HETATM 8746 O  O   . HOH G 7 .    ? 78.929 69.080  -11.681 1.00 27.98 ? 5493 HOH A O   1 
HETATM 8747 O  O   . HOH G 7 .    ? 81.346 68.342  -11.172 1.00 22.28 ? 5494 HOH A O   1 
HETATM 8748 O  O   . HOH G 7 .    ? 81.766 67.095  -13.416 1.00 22.74 ? 5495 HOH A O   1 
HETATM 8749 O  O   . HOH G 7 .    ? 79.883 68.100  -14.976 1.00 35.33 ? 5496 HOH A O   1 
HETATM 8750 O  O   . HOH G 7 .    ? 84.448 68.231  -17.018 1.00 18.91 ? 5497 HOH A O   1 
HETATM 8751 O  O   . HOH G 7 .    ? 83.817 67.561  -22.276 1.00 26.87 ? 5498 HOH A O   1 
HETATM 8752 O  O   . HOH G 7 .    ? 80.531 64.176  -20.961 1.00 24.56 ? 5499 HOH A O   1 
HETATM 8753 O  O   . HOH G 7 .    ? 78.926 62.480  -22.636 1.00 36.01 ? 5500 HOH A O   1 
HETATM 8754 O  O   . HOH G 7 .    ? 73.002 64.332  -20.298 1.00 32.36 ? 5501 HOH A O   1 
HETATM 8755 O  O   . HOH G 7 .    ? 72.006 62.607  -17.556 1.00 31.22 ? 5502 HOH A O   1 
HETATM 8756 O  O   . HOH G 7 .    ? 70.494 61.810  -20.418 1.00 29.67 ? 5503 HOH A O   1 
HETATM 8757 O  O   . HOH G 7 .    ? 70.156 63.215  -23.726 1.00 35.03 ? 5504 HOH A O   1 
HETATM 8758 O  O   . HOH G 7 .    ? 72.040 63.441  -25.022 1.00 35.33 ? 5505 HOH A O   1 
HETATM 8759 O  O   . HOH G 7 .    ? 69.836 63.780  -28.652 1.00 23.43 ? 5506 HOH A O   1 
HETATM 8760 O  O   . HOH G 7 .    ? 71.883 69.601  -34.910 1.00 39.93 ? 5507 HOH A O   1 
HETATM 8761 O  O   . HOH G 7 .    ? 70.965 72.885  -33.858 1.00 32.75 ? 5508 HOH A O   1 
HETATM 8762 O  O   . HOH G 7 .    ? 68.078 75.131  -34.347 1.00 31.50 ? 5509 HOH A O   1 
HETATM 8763 O  O   . HOH G 7 .    ? 69.552 77.206  -33.731 1.00 32.95 ? 5510 HOH A O   1 
HETATM 8764 O  O   . HOH G 7 .    ? 68.515 79.684  -34.614 1.00 22.08 ? 5511 HOH A O   1 
HETATM 8765 O  O   . HOH G 7 .    ? 64.499 77.918  -34.923 1.00 17.17 ? 5512 HOH A O   1 
HETATM 8766 O  O   . HOH G 7 .    ? 63.733 78.701  -37.609 1.00 34.34 ? 5513 HOH A O   1 
HETATM 8767 O  O   . HOH G 7 .    ? 64.309 77.181  -40.002 1.00 34.36 ? 5514 HOH A O   1 
HETATM 8768 O  O   . HOH G 7 .    ? 61.644 76.773  -39.444 1.00 22.90 ? 5515 HOH A O   1 
HETATM 8769 O  O   . HOH G 7 .    ? 60.840 78.904  -41.289 1.00 28.62 ? 5516 HOH A O   1 
HETATM 8770 O  O   . HOH G 7 .    ? 58.544 77.331  -38.241 1.00 16.40 ? 5517 HOH A O   1 
HETATM 8771 O  O   . HOH G 7 .    ? 61.947 83.422  -37.858 1.00 25.32 ? 5518 HOH A O   1 
HETATM 8772 O  O   . HOH G 7 .    ? 67.531 85.534  -36.284 1.00 25.13 ? 5519 HOH A O   1 
HETATM 8773 O  O   . HOH G 7 .    ? 68.203 87.989  -35.798 1.00 45.49 ? 5520 HOH A O   1 
HETATM 8774 O  O   . HOH G 7 .    ? 69.571 83.909  -35.720 1.00 29.91 ? 5521 HOH A O   1 
HETATM 8775 O  O   . HOH G 7 .    ? 72.428 82.860  -30.801 1.00 44.72 ? 5522 HOH A O   1 
HETATM 8776 O  O   . HOH G 7 .    ? 70.172 82.975  -29.397 1.00 23.06 ? 5523 HOH A O   1 
HETATM 8777 O  O   . HOH G 7 .    ? 71.385 80.225  -27.358 1.00 33.17 ? 5524 HOH A O   1 
HETATM 8778 O  O   . HOH G 7 .    ? 70.707 78.183  -25.790 1.00 22.99 ? 5525 HOH A O   1 
HETATM 8779 O  O   . HOH G 7 .    ? 72.274 75.900  -26.532 1.00 31.37 ? 5526 HOH A O   1 
HETATM 8780 O  O   . HOH G 7 .    ? 71.742 73.937  -28.758 1.00 32.50 ? 5527 HOH A O   1 
HETATM 8781 O  O   . HOH G 7 .    ? 77.048 73.980  -25.921 1.00 28.81 ? 5528 HOH A O   1 
HETATM 8782 O  O   . HOH G 7 .    ? 75.594 74.293  -18.629 1.00 25.53 ? 5529 HOH A O   1 
HETATM 8783 O  O   . HOH G 7 .    ? 74.088 76.730  -19.093 1.00 32.59 ? 5530 HOH A O   1 
HETATM 8784 O  O   . HOH G 7 .    ? 72.718 79.793  -16.763 1.00 38.71 ? 5531 HOH A O   1 
HETATM 8785 O  O   . HOH G 7 .    ? 68.709 79.128  -17.447 1.00 28.67 ? 5532 HOH A O   1 
HETATM 8786 O  O   . HOH G 7 .    ? 66.614 82.087  -13.680 1.00 44.87 ? 5533 HOH A O   1 
HETATM 8787 O  O   . HOH G 7 .    ? 65.395 79.506  -8.351  1.00 35.12 ? 5534 HOH A O   1 
HETATM 8788 O  O   . HOH G 7 .    ? 61.929 76.403  -10.189 1.00 19.51 ? 5535 HOH A O   1 
HETATM 8789 O  O   . HOH G 7 .    ? 61.478 77.236  -12.715 1.00 27.88 ? 5536 HOH A O   1 
HETATM 8790 O  O   . HOH G 7 .    ? 59.604 76.486  -8.536  1.00 16.97 ? 5537 HOH A O   1 
HETATM 8791 O  O   . HOH G 7 .    ? 57.267 75.294  -2.636  1.00 36.85 ? 5538 HOH A O   1 
HETATM 8792 O  O   . HOH G 7 .    ? 57.994 77.206  -1.288  1.00 38.70 ? 5539 HOH A O   1 
HETATM 8793 O  O   . HOH G 7 .    ? 56.200 76.033  1.518   1.00 42.58 ? 5540 HOH A O   1 
HETATM 8794 O  O   . HOH G 7 .    ? 52.224 73.682  4.361   1.00 41.41 ? 5541 HOH A O   1 
HETATM 8795 O  O   . HOH G 7 .    ? 51.106 75.764  5.746   1.00 31.35 ? 5542 HOH A O   1 
HETATM 8796 O  O   . HOH G 7 .    ? 49.026 76.619  5.870   1.00 38.79 ? 5543 HOH A O   1 
HETATM 8797 O  O   . HOH G 7 .    ? 49.248 77.786  3.342   1.00 38.03 ? 5544 HOH A O   1 
HETATM 8798 O  O   . HOH G 7 .    ? 45.737 79.979  5.319   1.00 33.12 ? 5545 HOH A O   1 
HETATM 8799 O  O   . HOH G 7 .    ? 43.333 80.629  5.663   1.00 22.44 ? 5546 HOH A O   1 
HETATM 8800 O  O   . HOH G 7 .    ? 42.241 83.216  5.230   1.00 32.37 ? 5547 HOH A O   1 
HETATM 8801 O  O   . HOH G 7 .    ? 39.109 84.850  1.864   1.00 28.64 ? 5548 HOH A O   1 
HETATM 8802 O  O   . HOH G 7 .    ? 41.453 84.752  0.583   1.00 39.30 ? 5549 HOH A O   1 
HETATM 8803 O  O   . HOH G 7 .    ? 42.746 83.294  -1.896  1.00 43.43 ? 5550 HOH A O   1 
HETATM 8804 O  O   . HOH G 7 .    ? 44.043 82.728  -7.143  1.00 37.09 ? 5551 HOH A O   1 
HETATM 8805 O  O   . HOH G 7 .    ? 43.490 82.024  -10.231 1.00 28.49 ? 5552 HOH A O   1 
HETATM 8806 O  O   . HOH G 7 .    ? 44.697 84.465  -10.140 1.00 45.53 ? 5553 HOH A O   1 
HETATM 8807 O  O   . HOH G 7 .    ? 40.583 82.855  -10.639 1.00 19.41 ? 5554 HOH A O   1 
HETATM 8808 O  O   . HOH G 7 .    ? 40.831 85.385  -12.243 1.00 28.56 ? 5555 HOH A O   1 
HETATM 8809 O  O   . HOH G 7 .    ? 41.394 77.455  -13.787 1.00 13.87 ? 5556 HOH A O   1 
HETATM 8810 O  O   . HOH G 7 .    ? 42.210 75.226  -15.730 1.00 12.23 ? 5557 HOH A O   1 
HETATM 8811 O  O   . HOH G 7 .    ? 47.665 79.450  -18.299 1.00 16.90 ? 5558 HOH A O   1 
HETATM 8812 O  O   . HOH G 7 .    ? 50.653 78.953  -15.433 1.00 27.70 ? 5559 HOH A O   1 
HETATM 8813 O  O   . HOH G 7 .    ? 52.791 78.941  -16.870 1.00 25.02 ? 5560 HOH A O   1 
HETATM 8814 O  O   . HOH G 7 .    ? 54.262 80.437  -18.988 1.00 32.41 ? 5561 HOH A O   1 
HETATM 8815 O  O   . HOH G 7 .    ? 55.148 81.032  -23.230 1.00 16.60 ? 5562 HOH A O   1 
HETATM 8816 O  O   . HOH G 7 .    ? 53.239 87.235  -21.042 1.00 28.51 ? 5563 HOH A O   1 
HETATM 8817 O  O   . HOH G 7 .    ? 51.429 90.273  -21.153 1.00 39.28 ? 5564 HOH A O   1 
HETATM 8818 O  O   . HOH G 7 .    ? 53.075 91.863  -22.943 1.00 34.52 ? 5565 HOH A O   1 
HETATM 8819 O  O   . HOH G 7 .    ? 55.202 90.385  -23.131 1.00 20.19 ? 5566 HOH A O   1 
HETATM 8820 O  O   . HOH G 7 .    ? 56.428 91.086  -25.319 1.00 19.82 ? 5567 HOH A O   1 
HETATM 8821 O  O   . HOH G 7 .    ? 58.262 93.347  -24.910 1.00 19.86 ? 5568 HOH A O   1 
HETATM 8822 O  O   . HOH G 7 .    ? 56.312 92.988  -28.952 1.00 26.18 ? 5569 HOH A O   1 
HETATM 8823 O  O   . HOH G 7 .    ? 55.022 93.970  -30.973 1.00 29.23 ? 5570 HOH A O   1 
HETATM 8824 O  O   . HOH G 7 .    ? 60.558 91.322  -29.971 1.00 24.52 ? 5571 HOH A O   1 
HETATM 8825 O  O   . HOH G 7 .    ? 59.963 91.031  -35.260 1.00 23.07 ? 5572 HOH A O   1 
HETATM 8826 O  O   . HOH G 7 .    ? 56.537 89.890  -43.539 1.00 46.46 ? 5573 HOH A O   1 
HETATM 8827 O  O   . HOH G 7 .    ? 59.414 87.049  -45.600 1.00 34.57 ? 5574 HOH A O   1 
HETATM 8828 O  O   . HOH G 7 .    ? 54.549 82.389  -44.364 1.00 35.10 ? 5575 HOH A O   1 
HETATM 8829 O  O   . HOH G 7 .    ? 49.826 82.233  -43.692 1.00 20.35 ? 5576 HOH A O   1 
HETATM 8830 O  O   . HOH G 7 .    ? 42.338 87.752  -40.690 1.00 19.80 ? 5577 HOH A O   1 
HETATM 8831 O  O   . HOH G 7 .    ? 43.620 88.596  -38.285 1.00 18.76 ? 5578 HOH A O   1 
HETATM 8832 O  O   . HOH G 7 .    ? 43.430 93.847  -37.636 1.00 23.65 ? 5579 HOH A O   1 
HETATM 8833 O  O   . HOH G 7 .    ? 40.969 96.420  -37.102 1.00 25.78 ? 5580 HOH A O   1 
HETATM 8834 O  O   . HOH G 7 .    ? 43.233 98.280  -36.953 1.00 43.58 ? 5581 HOH A O   1 
HETATM 8835 O  O   . HOH G 7 .    ? 48.703 98.075  -33.474 1.00 38.68 ? 5582 HOH A O   1 
HETATM 8836 O  O   . HOH G 7 .    ? 44.302 95.791  -29.182 1.00 45.49 ? 5583 HOH A O   1 
HETATM 8837 O  O   . HOH G 7 .    ? 45.136 90.194  -25.225 1.00 22.02 ? 5584 HOH A O   1 
HETATM 8838 O  O   . HOH G 7 .    ? 47.145 89.621  -23.128 1.00 33.91 ? 5585 HOH A O   1 
HETATM 8839 O  O   . HOH G 7 .    ? 48.700 91.867  -23.787 1.00 28.62 ? 5586 HOH A O   1 
HETATM 8840 O  O   . HOH G 7 .    ? 48.515 89.229  -30.600 1.00 20.47 ? 5587 HOH A O   1 
HETATM 8841 O  O   . HOH G 7 .    ? 49.752 84.105  -18.528 1.00 30.95 ? 5588 HOH A O   1 
HETATM 8842 O  O   . HOH G 7 .    ? 56.573 87.729  -19.693 1.00 28.59 ? 5589 HOH A O   1 
HETATM 8843 O  O   . HOH G 7 .    ? 62.392 85.406  -22.620 1.00 25.99 ? 5590 HOH A O   1 
HETATM 8844 O  O   . HOH G 7 .    ? 66.109 84.825  -22.151 1.00 38.22 ? 5591 HOH A O   1 
HETATM 8845 O  O   . HOH G 7 .    ? 65.341 87.799  -23.847 1.00 28.37 ? 5592 HOH A O   1 
HETATM 8846 O  O   . HOH G 7 .    ? 67.711 88.330  -23.351 1.00 41.87 ? 5593 HOH A O   1 
HETATM 8847 O  O   . HOH G 7 .    ? 71.691 84.668  -19.610 1.00 31.96 ? 5594 HOH A O   1 
HETATM 8848 O  O   . HOH G 7 .    ? 73.337 82.392  -20.610 1.00 26.22 ? 5595 HOH A O   1 
HETATM 8849 O  O   . HOH G 7 .    ? 68.015 81.700  -25.392 1.00 13.48 ? 5596 HOH A O   1 
HETATM 8850 O  O   . HOH G 7 .    ? 68.000 78.928  -25.097 1.00 16.56 ? 5597 HOH A O   1 
HETATM 8851 O  O   . HOH G 7 .    ? 68.526 79.367  -28.270 1.00 18.05 ? 5598 HOH A O   1 
HETATM 8852 O  O   . HOH G 7 .    ? 62.202 80.591  -18.555 1.00 36.41 ? 5599 HOH A O   1 
HETATM 8853 O  O   . HOH G 7 .    ? 74.066 80.321  -12.651 1.00 31.37 ? 5600 HOH A O   1 
HETATM 8854 O  O   . HOH G 7 .    ? 74.880 77.054  -13.328 1.00 26.00 ? 5601 HOH A O   1 
HETATM 8855 O  O   . HOH G 7 .    ? 77.973 76.630  -11.565 1.00 42.48 ? 5602 HOH A O   1 
HETATM 8856 O  O   . HOH G 7 .    ? 78.275 71.999  -10.174 1.00 42.19 ? 5603 HOH A O   1 
HETATM 8857 O  O   . HOH G 7 .    ? 80.406 71.276  -7.208  1.00 37.66 ? 5604 HOH A O   1 
HETATM 8858 O  O   . HOH G 7 .    ? 78.986 69.224  -6.612  1.00 36.44 ? 5605 HOH A O   1 
HETATM 8859 O  O   . HOH G 7 .    ? 76.868 68.765  -4.427  1.00 40.47 ? 5606 HOH A O   1 
HETATM 8860 O  O   . HOH G 7 .    ? 75.720 70.952  -3.535  1.00 32.16 ? 5607 HOH A O   1 
HETATM 8861 O  O   . HOH G 7 .    ? 79.045 69.967  -3.305  1.00 37.33 ? 5608 HOH A O   1 
HETATM 8862 O  O   . HOH G 7 .    ? 78.760 71.719  -0.333  1.00 36.27 ? 5609 HOH A O   1 
HETATM 8863 O  O   . HOH G 7 .    ? 73.711 74.075  -5.268  1.00 27.17 ? 5610 HOH A O   1 
HETATM 8864 O  O   . HOH G 7 .    ? 74.370 76.377  -4.783  1.00 39.28 ? 5611 HOH A O   1 
HETATM 8865 O  O   . HOH G 7 .    ? 73.914 80.237  -4.491  1.00 23.87 ? 5612 HOH A O   1 
HETATM 8866 O  O   . HOH G 7 .    ? 70.989 80.464  -6.464  1.00 36.99 ? 5613 HOH A O   1 
HETATM 8867 O  O   . HOH G 7 .    ? 66.988 74.235  -3.927  1.00 29.52 ? 5614 HOH A O   1 
HETATM 8868 O  O   . HOH G 7 .    ? 66.777 71.158  -6.588  1.00 27.63 ? 5615 HOH A O   1 
HETATM 8869 O  O   . HOH G 7 .    ? 64.301 70.525  -5.264  1.00 23.02 ? 5616 HOH A O   1 
HETATM 8870 O  O   . HOH G 7 .    ? 68.043 65.383  -3.120  1.00 16.18 ? 5617 HOH A O   1 
HETATM 8871 O  O   . HOH G 7 .    ? 67.258 65.184  0.095   1.00 42.12 ? 5618 HOH A O   1 
HETATM 8872 O  O   . HOH G 7 .    ? 65.642 66.678  0.609   1.00 26.64 ? 5619 HOH A O   1 
HETATM 8873 O  O   . HOH G 7 .    ? 66.522 68.223  2.413   1.00 34.75 ? 5620 HOH A O   1 
HETATM 8874 O  O   . HOH G 7 .    ? 65.625 66.707  4.416   1.00 39.65 ? 5621 HOH A O   1 
HETATM 8875 O  O   . HOH G 7 .    ? 66.147 68.940  4.977   1.00 32.15 ? 5622 HOH A O   1 
HETATM 8876 O  O   . HOH G 7 .    ? 59.332 68.283  2.927   1.00 25.76 ? 5623 HOH A O   1 
HETATM 8877 O  O   . HOH G 7 .    ? 56.320 66.708  5.868   1.00 28.06 ? 5624 HOH A O   1 
HETATM 8878 O  O   . HOH G 7 .    ? 53.971 67.008  7.588   1.00 35.53 ? 5625 HOH A O   1 
HETATM 8879 O  O   . HOH G 7 .    ? 51.612 66.270  8.780   1.00 30.66 ? 5626 HOH A O   1 
HETATM 8880 O  O   . HOH G 7 .    ? 49.730 67.823  6.719   1.00 37.12 ? 5627 HOH A O   1 
HETATM 8881 O  O   . HOH G 7 .    ? 50.012 67.390  4.545   1.00 21.43 ? 5628 HOH A O   1 
HETATM 8882 O  O   . HOH G 7 .    ? 52.236 70.852  6.402   1.00 29.46 ? 5629 HOH A O   1 
HETATM 8883 O  O   . HOH G 7 .    ? 50.399 72.253  9.603   1.00 22.76 ? 5630 HOH A O   1 
HETATM 8884 O  O   . HOH G 7 .    ? 46.706 74.416  8.208   1.00 12.58 ? 5631 HOH A O   1 
HETATM 8885 O  O   . HOH G 7 .    ? 46.238 77.387  9.794   1.00 17.06 ? 5632 HOH A O   1 
HETATM 8886 O  O   . HOH G 7 .    ? 45.045 80.031  12.660  1.00 31.54 ? 5633 HOH A O   1 
HETATM 8887 O  O   . HOH G 7 .    ? 46.957 77.321  13.725  1.00 33.99 ? 5634 HOH A O   1 
HETATM 8888 O  O   . HOH G 7 .    ? 50.708 76.214  15.008  1.00 22.42 ? 5635 HOH A O   1 
HETATM 8889 O  O   . HOH G 7 .    ? 51.327 77.603  12.562  1.00 40.44 ? 5636 HOH A O   1 
HETATM 8890 O  O   . HOH G 7 .    ? 55.261 72.433  16.281  1.00 28.73 ? 5637 HOH A O   1 
HETATM 8891 O  O   . HOH G 7 .    ? 52.699 72.245  18.420  1.00 25.98 ? 5638 HOH A O   1 
HETATM 8892 O  O   . HOH G 7 .    ? 53.155 69.352  18.235  1.00 33.28 ? 5639 HOH A O   1 
HETATM 8893 O  O   . HOH G 7 .    ? 52.003 71.290  21.931  1.00 31.88 ? 5640 HOH A O   1 
HETATM 8894 O  O   . HOH G 7 .    ? 48.508 76.525  20.033  1.00 32.50 ? 5641 HOH A O   1 
HETATM 8895 O  O   . HOH G 7 .    ? 45.816 74.104  22.726  1.00 33.32 ? 5642 HOH A O   1 
HETATM 8896 O  O   . HOH G 7 .    ? 42.459 68.134  26.797  1.00 34.52 ? 5643 HOH A O   1 
HETATM 8897 O  O   . HOH G 7 .    ? 33.647 59.914  23.428  1.00 12.34 ? 5644 HOH A O   1 
HETATM 8898 O  O   . HOH G 7 .    ? 30.252 55.318  17.385  1.00 9.11  ? 5645 HOH A O   1 
HETATM 8899 O  O   . HOH G 7 .    ? 27.702 52.946  20.236  1.00 13.31 ? 5646 HOH A O   1 
HETATM 8900 O  O   . HOH G 7 .    ? 26.979 51.710  22.686  1.00 20.08 ? 5647 HOH A O   1 
HETATM 8901 O  O   . HOH G 7 .    ? 27.436 49.591  23.482  1.00 20.30 ? 5648 HOH A O   1 
HETATM 8902 O  O   . HOH G 7 .    ? 18.188 60.251  24.766  1.00 21.05 ? 5649 HOH A O   1 
HETATM 8903 O  O   . HOH G 7 .    ? 12.022 63.142  21.811  1.00 40.83 ? 5650 HOH A O   1 
HETATM 8904 O  O   . HOH G 7 .    ? 10.921 68.835  26.135  1.00 29.29 ? 5651 HOH A O   1 
HETATM 8905 O  O   . HOH G 7 .    ? 20.571 53.806  47.044  1.00 35.21 ? 5652 HOH A O   1 
HETATM 8906 O  O   . HOH G 7 .    ? 20.968 51.208  47.428  1.00 31.81 ? 5653 HOH A O   1 
HETATM 8907 O  O   . HOH G 7 .    ? 20.015 42.741  34.072  1.00 25.89 ? 5654 HOH A O   1 
HETATM 8908 O  O   . HOH G 7 .    ? 17.365 37.738  35.501  1.00 35.37 ? 5655 HOH A O   1 
HETATM 8909 O  O   . HOH G 7 .    ? 15.409 39.138  33.812  1.00 45.40 ? 5656 HOH A O   1 
HETATM 8910 O  O   . HOH G 7 .    ? 20.722 31.470  31.548  1.00 31.88 ? 5657 HOH A O   1 
HETATM 8911 O  O   . HOH G 7 .    ? 22.516 30.572  29.247  1.00 30.85 ? 5658 HOH A O   1 
HETATM 8912 O  O   . HOH G 7 .    ? 21.830 28.708  27.886  1.00 34.54 ? 5659 HOH A O   1 
HETATM 8913 O  O   . HOH G 7 .    ? 24.407 34.067  35.753  1.00 29.12 ? 5660 HOH A O   1 
HETATM 8914 O  O   . HOH G 7 .    ? 21.026 29.836  17.940  1.00 41.46 ? 5661 HOH A O   1 
HETATM 8915 O  O   . HOH G 7 .    ? 16.173 33.662  15.677  1.00 33.63 ? 5662 HOH A O   1 
HETATM 8916 O  O   . HOH G 7 .    ? 16.190 36.261  16.538  1.00 31.49 ? 5663 HOH A O   1 
HETATM 8917 O  O   . HOH G 7 .    ? 11.737 41.198  19.902  1.00 33.72 ? 5664 HOH A O   1 
HETATM 8918 O  O   . HOH G 7 .    ? 8.656  40.087  14.494  1.00 44.65 ? 5665 HOH A O   1 
HETATM 8919 O  O   . HOH G 7 .    ? 25.116 29.307  6.993   1.00 43.72 ? 5666 HOH A O   1 
HETATM 8920 O  O   . HOH G 7 .    ? 31.162 29.496  5.443   1.00 31.50 ? 5667 HOH A O   1 
HETATM 8921 O  O   . HOH G 7 .    ? 31.815 30.616  3.307   1.00 44.77 ? 5668 HOH A O   1 
HETATM 8922 O  O   . HOH G 7 .    ? 31.216 33.368  2.648   1.00 24.47 ? 5669 HOH A O   1 
HETATM 8923 O  O   . HOH G 7 .    ? 30.216 34.022  -1.235  1.00 25.32 ? 5670 HOH A O   1 
HETATM 8924 O  O   . HOH G 7 .    ? 32.300 34.341  -3.213  1.00 22.67 ? 5671 HOH A O   1 
HETATM 8925 O  O   . HOH G 7 .    ? 33.332 36.463  -4.381  1.00 14.98 ? 5672 HOH A O   1 
HETATM 8926 O  O   . HOH G 7 .    ? 32.484 38.991  -4.880  1.00 9.55  ? 5673 HOH A O   1 
HETATM 8927 O  O   . HOH G 7 .    ? 36.037 35.932  -4.517  1.00 18.87 ? 5674 HOH A O   1 
HETATM 8928 O  O   . HOH G 7 .    ? 39.019 34.349  -6.880  1.00 36.93 ? 5675 HOH A O   1 
HETATM 8929 O  O   . HOH G 7 .    ? 40.052 38.495  -3.326  1.00 25.81 ? 5676 HOH A O   1 
HETATM 8930 O  O   . HOH G 7 .    ? 40.042 39.449  -0.060  1.00 25.46 ? 5677 HOH A O   1 
HETATM 8931 O  O   . HOH G 7 .    ? 42.020 40.412  0.767   1.00 45.49 ? 5678 HOH A O   1 
HETATM 8932 O  O   . HOH G 7 .    ? 42.722 39.298  -1.263  1.00 22.19 ? 5679 HOH A O   1 
HETATM 8933 O  O   . HOH G 7 .    ? 44.775 41.658  -0.436  1.00 12.02 ? 5680 HOH A O   1 
HETATM 8934 O  O   . HOH G 7 .    ? 46.284 39.869  0.255   1.00 31.55 ? 5681 HOH A O   1 
HETATM 8935 O  O   . HOH G 7 .    ? 48.633 40.628  -0.878  1.00 20.10 ? 5682 HOH A O   1 
HETATM 8936 O  O   . HOH G 7 .    ? 47.617 42.763  -2.220  1.00 13.50 ? 5683 HOH A O   1 
HETATM 8937 O  O   . HOH G 7 .    ? 47.982 41.677  -5.263  1.00 28.88 ? 5684 HOH A O   1 
HETATM 8938 O  O   . HOH G 7 .    ? 48.936 44.129  -5.908  1.00 15.89 ? 5685 HOH A O   1 
HETATM 8939 O  O   . HOH G 7 .    ? 48.168 43.861  -8.365  1.00 17.77 ? 5686 HOH A O   1 
HETATM 8940 O  O   . HOH G 7 .    ? 51.191 44.198  -7.832  1.00 9.97  ? 5687 HOH A O   1 
HETATM 8941 O  O   . HOH G 7 .    ? 52.001 40.953  -13.059 1.00 24.65 ? 5688 HOH A O   1 
HETATM 8942 O  O   . HOH G 7 .    ? 51.109 40.253  -15.140 1.00 33.75 ? 5689 HOH A O   1 
HETATM 8943 O  O   . HOH G 7 .    ? 48.447 38.619  -14.992 1.00 45.49 ? 5690 HOH A O   1 
HETATM 8944 O  O   . HOH G 7 .    ? 48.352 36.805  -16.684 1.00 45.49 ? 5691 HOH A O   1 
HETATM 8945 O  O   . HOH G 7 .    ? 50.086 40.068  -18.874 1.00 41.95 ? 5692 HOH A O   1 
HETATM 8946 O  O   . HOH G 7 .    ? 54.227 40.732  -20.250 1.00 34.75 ? 5693 HOH A O   1 
HETATM 8947 O  O   . HOH G 7 .    ? 57.150 39.007  -19.272 1.00 30.42 ? 5694 HOH A O   1 
HETATM 8948 O  O   . HOH G 7 .    ? 58.628 37.267  -17.714 1.00 40.25 ? 5695 HOH A O   1 
HETATM 8949 O  O   . HOH G 7 .    ? 59.691 37.693  -15.251 1.00 25.15 ? 5696 HOH A O   1 
HETATM 8950 O  O   . HOH G 7 .    ? 57.394 35.984  -14.386 1.00 23.89 ? 5697 HOH A O   1 
HETATM 8951 O  O   . HOH G 7 .    ? 58.690 34.861  -12.087 1.00 40.72 ? 5698 HOH A O   1 
HETATM 8952 O  O   . HOH G 7 .    ? 63.705 34.758  -9.268  1.00 37.15 ? 5699 HOH A O   1 
HETATM 8953 O  O   . HOH G 7 .    ? 64.469 39.454  -9.952  1.00 20.04 ? 5700 HOH A O   1 
HETATM 8954 O  O   . HOH G 7 .    ? 67.083 38.283  -9.686  1.00 27.08 ? 5701 HOH A O   1 
HETATM 8955 O  O   . HOH G 7 .    ? 72.815 42.206  -12.962 1.00 37.93 ? 5702 HOH A O   1 
HETATM 8956 O  O   . HOH G 7 .    ? 71.266 43.193  -15.199 1.00 30.44 ? 5703 HOH A O   1 
HETATM 8957 O  O   . HOH G 7 .    ? 68.767 46.881  -16.755 1.00 29.49 ? 5704 HOH A O   1 
HETATM 8958 O  O   . HOH G 7 .    ? 63.991 50.121  -13.689 1.00 15.66 ? 5705 HOH A O   1 
HETATM 8959 O  O   . HOH G 7 .    ? 62.271 48.377  -20.759 1.00 33.69 ? 5706 HOH A O   1 
HETATM 8960 O  O   . HOH G 7 .    ? 60.867 46.534  -22.391 1.00 27.31 ? 5707 HOH A O   1 
HETATM 8961 O  O   . HOH G 7 .    ? 63.141 42.629  -20.649 1.00 27.74 ? 5708 HOH A O   1 
HETATM 8962 O  O   . HOH G 7 .    ? 57.144 43.165  -19.786 1.00 23.23 ? 5709 HOH A O   1 
HETATM 8963 O  O   . HOH G 7 .    ? 56.666 46.177  -17.155 1.00 12.88 ? 5710 HOH A O   1 
HETATM 8964 O  O   . HOH G 7 .    ? 53.458 47.098  -24.907 1.00 16.29 ? 5711 HOH A O   1 
HETATM 8965 O  O   . HOH G 7 .    ? 52.431 45.570  -27.308 1.00 32.31 ? 5712 HOH A O   1 
HETATM 8966 O  O   . HOH G 7 .    ? 50.541 44.880  -24.744 1.00 24.39 ? 5713 HOH A O   1 
HETATM 8967 O  O   . HOH G 7 .    ? 50.373 47.302  -23.318 1.00 50.58 ? 5714 HOH A O   1 
HETATM 8968 O  O   . HOH G 7 .    ? 46.980 42.921  -22.499 1.00 51.77 ? 5715 HOH A O   1 
HETATM 8969 O  O   . HOH G 7 .    ? 43.609 43.015  -24.681 1.00 29.63 ? 5716 HOH A O   1 
HETATM 8970 O  O   . HOH G 7 .    ? 41.727 44.746  -24.242 1.00 23.57 ? 5717 HOH A O   1 
HETATM 8971 O  O   . HOH G 7 .    ? 42.380 47.418  -24.498 1.00 14.66 ? 5718 HOH A O   1 
HETATM 8972 O  O   . HOH G 7 .    ? 40.562 45.777  -26.929 1.00 39.22 ? 5719 HOH A O   1 
HETATM 8973 O  O   . HOH G 7 .    ? 37.540 45.394  -25.381 1.00 23.75 ? 5720 HOH A O   1 
HETATM 8974 O  O   . HOH G 7 .    ? 35.716 45.259  -27.418 1.00 17.94 ? 5721 HOH A O   1 
HETATM 8975 O  O   . HOH G 7 .    ? 36.043 42.118  -26.575 1.00 35.99 ? 5722 HOH A O   1 
HETATM 8976 O  O   . HOH G 7 .    ? 37.171 41.331  -24.609 1.00 24.13 ? 5723 HOH A O   1 
HETATM 8977 O  O   . HOH G 7 .    ? 38.561 39.967  -26.575 1.00 37.53 ? 5724 HOH A O   1 
HETATM 8978 O  O   . HOH G 7 .    ? 38.923 42.098  -21.777 1.00 21.45 ? 5725 HOH A O   1 
HETATM 8979 O  O   . HOH G 7 .    ? 41.014 40.730  -21.306 1.00 23.41 ? 5726 HOH A O   1 
HETATM 8980 O  O   . HOH G 7 .    ? 43.439 40.411  -22.867 1.00 30.45 ? 5727 HOH A O   1 
HETATM 8981 O  O   . HOH G 7 .    ? 40.946 37.800  -22.358 1.00 34.83 ? 5728 HOH A O   1 
HETATM 8982 O  O   . HOH G 7 .    ? 41.707 41.213  -17.522 1.00 15.16 ? 5729 HOH A O   1 
HETATM 8983 O  O   . HOH G 7 .    ? 40.719 41.014  -15.056 1.00 38.70 ? 5730 HOH A O   1 
HETATM 8984 O  O   . HOH G 7 .    ? 40.137 42.656  -12.995 1.00 35.56 ? 5731 HOH A O   1 
HETATM 8985 O  O   . HOH G 7 .    ? 42.452 40.381  -9.792  1.00 29.37 ? 5732 HOH A O   1 
HETATM 8986 O  O   . HOH G 7 .    ? 43.837 41.796  -7.414  1.00 22.80 ? 5733 HOH A O   1 
HETATM 8987 O  O   . HOH G 7 .    ? 41.601 44.692  -6.804  1.00 13.77 ? 5734 HOH A O   1 
HETATM 8988 O  O   . HOH G 7 .    ? 36.833 44.790  -5.395  1.00 10.19 ? 5735 HOH A O   1 
HETATM 8989 O  O   . HOH G 7 .    ? 31.813 46.945  -7.999  1.00 7.69  ? 5736 HOH A O   1 
HETATM 8990 O  O   . HOH G 7 .    ? 33.653 48.011  -10.002 1.00 9.78  ? 5737 HOH A O   1 
HETATM 8991 O  O   . HOH G 7 .    ? 26.440 48.788  -10.935 1.00 8.62  ? 5738 HOH A O   1 
HETATM 8992 O  O   . HOH G 7 .    ? 26.210 49.585  -13.550 1.00 10.13 ? 5739 HOH A O   1 
HETATM 8993 O  O   . HOH G 7 .    ? 24.834 52.821  -11.667 1.00 9.52  ? 5740 HOH A O   1 
HETATM 8994 O  O   . HOH G 7 .    ? 22.348 54.219  -11.895 1.00 11.37 ? 5741 HOH A O   1 
HETATM 8995 O  O   . HOH G 7 .    ? 19.694 53.498  -11.638 1.00 11.04 ? 5742 HOH A O   1 
HETATM 8996 O  O   . HOH G 7 .    ? 18.681 50.921  -12.370 1.00 12.44 ? 5743 HOH A O   1 
HETATM 8997 O  O   . HOH G 7 .    ? 19.863 46.735  -14.364 1.00 21.89 ? 5744 HOH A O   1 
HETATM 8998 O  O   . HOH G 7 .    ? 17.547 45.619  -14.150 1.00 32.50 ? 5745 HOH A O   1 
HETATM 8999 O  O   . HOH G 7 .    ? 15.902 44.155  -11.864 1.00 38.69 ? 5746 HOH A O   1 
HETATM 9000 O  O   . HOH G 7 .    ? 12.097 46.543  -12.183 1.00 33.13 ? 5747 HOH A O   1 
HETATM 9001 O  O   . HOH G 7 .    ? 13.014 51.566  -12.117 1.00 28.04 ? 5748 HOH A O   1 
HETATM 9002 O  O   . HOH G 7 .    ? 13.145 51.932  -14.907 1.00 26.44 ? 5749 HOH A O   1 
HETATM 9003 O  O   . HOH G 7 .    ? 14.491 54.254  -16.097 1.00 15.68 ? 5750 HOH A O   1 
HETATM 9004 O  O   . HOH G 7 .    ? 12.380 55.628  -14.986 1.00 18.72 ? 5751 HOH A O   1 
HETATM 9005 O  O   . HOH G 7 .    ? 11.875 54.716  -12.363 1.00 17.23 ? 5752 HOH A O   1 
HETATM 9006 O  O   . HOH G 7 .    ? 19.854 57.272  -11.599 1.00 13.62 ? 5753 HOH A O   1 
HETATM 9007 O  O   . HOH G 7 .    ? 21.630 57.850  -7.709  1.00 9.54  ? 5754 HOH A O   1 
HETATM 9008 O  O   . HOH G 7 .    ? 20.656 57.276  -5.136  1.00 9.36  ? 5755 HOH A O   1 
HETATM 9009 O  O   . HOH G 7 .    ? 23.386 53.905  -3.610  1.00 13.71 ? 5756 HOH A O   1 
HETATM 9010 O  O   . HOH G 7 .    ? 24.424 55.443  -1.621  1.00 9.63  ? 5757 HOH A O   1 
HETATM 9011 O  O   . HOH G 7 .    ? 24.261 53.119  -6.104  1.00 18.41 ? 5758 HOH A O   1 
HETATM 9012 O  O   . HOH G 7 .    ? 23.136 51.727  -8.494  1.00 14.48 ? 5759 HOH A O   1 
HETATM 9013 O  O   . HOH G 7 .    ? 25.600 51.133  -9.423  1.00 10.63 ? 5760 HOH A O   1 
HETATM 9014 O  O   . HOH G 7 .    ? 22.754 45.391  -13.267 1.00 24.40 ? 5761 HOH A O   1 
HETATM 9015 O  O   . HOH G 7 .    ? 23.773 45.945  -15.826 1.00 21.34 ? 5762 HOH A O   1 
HETATM 9016 O  O   . HOH G 7 .    ? 21.214 46.545  -17.524 1.00 31.39 ? 5763 HOH A O   1 
HETATM 9017 O  O   . HOH G 7 .    ? 18.763 48.818  -20.190 1.00 42.77 ? 5764 HOH A O   1 
HETATM 9018 O  O   . HOH G 7 .    ? 17.132 50.753  -19.323 1.00 26.81 ? 5765 HOH A O   1 
HETATM 9019 O  O   . HOH G 7 .    ? 16.801 52.943  -22.199 1.00 32.58 ? 5766 HOH A O   1 
HETATM 9020 O  O   . HOH G 7 .    ? 20.209 52.597  -24.239 1.00 17.81 ? 5767 HOH A O   1 
HETATM 9021 O  O   . HOH G 7 .    ? 19.547 50.242  -23.687 1.00 38.79 ? 5768 HOH A O   1 
HETATM 9022 O  O   . HOH G 7 .    ? 21.541 48.730  -22.432 1.00 34.23 ? 5769 HOH A O   1 
HETATM 9023 O  O   . HOH G 7 .    ? 24.300 48.192  -24.221 1.00 38.69 ? 5770 HOH A O   1 
HETATM 9024 O  O   . HOH G 7 .    ? 26.958 47.714  -24.261 1.00 35.51 ? 5771 HOH A O   1 
HETATM 9025 O  O   . HOH G 7 .    ? 28.738 49.726  -24.327 1.00 15.89 ? 5772 HOH A O   1 
HETATM 9026 O  O   . HOH G 7 .    ? 31.408 50.030  -23.863 1.00 12.05 ? 5773 HOH A O   1 
HETATM 9027 O  O   . HOH G 7 .    ? 27.735 48.531  -21.641 1.00 18.45 ? 5774 HOH A O   1 
HETATM 9028 O  O   . HOH G 7 .    ? 25.308 46.946  -20.688 1.00 20.98 ? 5775 HOH A O   1 
HETATM 9029 O  O   . HOH G 7 .    ? 24.772 51.153  -23.977 1.00 13.50 ? 5776 HOH A O   1 
HETATM 9030 O  O   . HOH G 7 .    ? 22.964 53.249  -24.271 1.00 14.27 ? 5777 HOH A O   1 
HETATM 9031 O  O   . HOH G 7 .    ? 23.820 55.542  -23.366 1.00 10.98 ? 5778 HOH A O   1 
HETATM 9032 O  O   . HOH G 7 .    ? 19.988 52.630  -27.050 1.00 26.25 ? 5779 HOH A O   1 
HETATM 9033 O  O   . HOH G 7 .    ? 23.183 48.758  -26.980 1.00 44.86 ? 5780 HOH A O   1 
HETATM 9034 O  O   . HOH G 7 .    ? 23.135 48.976  -36.093 1.00 38.17 ? 5781 HOH A O   1 
HETATM 9035 O  O   . HOH G 7 .    ? 20.834 55.227  -35.387 1.00 35.69 ? 5782 HOH A O   1 
HETATM 9036 O  O   . HOH G 7 .    ? 19.460 54.954  -33.341 1.00 34.77 ? 5783 HOH A O   1 
HETATM 9037 O  O   . HOH G 7 .    ? 22.561 56.917  -34.020 1.00 19.26 ? 5784 HOH A O   1 
HETATM 9038 O  O   . HOH G 7 .    ? 20.825 59.010  -34.538 1.00 19.90 ? 5785 HOH A O   1 
HETATM 9039 O  O   . HOH G 7 .    ? 19.544 58.286  -36.592 1.00 29.04 ? 5786 HOH A O   1 
HETATM 9040 O  O   . HOH G 7 .    ? 18.984 60.589  -37.789 1.00 27.06 ? 5787 HOH A O   1 
HETATM 9041 O  O   . HOH G 7 .    ? 17.201 57.066  -36.035 1.00 25.28 ? 5788 HOH A O   1 
HETATM 9042 O  O   . HOH G 7 .    ? 22.062 61.631  -34.843 1.00 26.57 ? 5789 HOH A O   1 
HETATM 9043 O  O   . HOH G 7 .    ? 22.284 63.738  -32.539 1.00 27.68 ? 5790 HOH A O   1 
HETATM 9044 O  O   . HOH G 7 .    ? 18.684 70.593  -30.002 1.00 34.18 ? 5791 HOH A O   1 
HETATM 9045 O  O   . HOH G 7 .    ? 24.631 71.786  -39.538 1.00 28.51 ? 5792 HOH A O   1 
HETATM 9046 O  O   . HOH G 7 .    ? 24.548 74.111  -39.933 1.00 35.27 ? 5793 HOH A O   1 
HETATM 9047 O  O   . HOH G 7 .    ? 30.983 69.538  -45.152 1.00 33.07 ? 5794 HOH A O   1 
HETATM 9048 O  O   . HOH G 7 .    ? 34.787 65.934  -42.354 1.00 43.93 ? 5795 HOH A O   1 
HETATM 9049 O  O   . HOH G 7 .    ? 36.402 62.846  -38.531 1.00 33.95 ? 5796 HOH A O   1 
HETATM 9050 O  O   . HOH G 7 .    ? 39.695 58.892  -34.434 1.00 33.76 ? 5797 HOH A O   1 
HETATM 9051 O  O   . HOH G 7 .    ? 40.366 62.503  -31.787 1.00 21.10 ? 5798 HOH A O   1 
HETATM 9052 O  O   . HOH G 7 .    ? 45.694 61.417  -30.628 1.00 44.25 ? 5799 HOH A O   1 
HETATM 9053 O  O   . HOH G 7 .    ? 45.913 56.408  -32.722 1.00 33.46 ? 5800 HOH A O   1 
HETATM 9054 O  O   . HOH G 7 .    ? 46.633 54.106  -31.371 1.00 48.55 ? 5801 HOH A O   1 
HETATM 9055 O  O   . HOH G 7 .    ? 50.064 55.271  -28.878 1.00 15.25 ? 5802 HOH A O   1 
HETATM 9056 O  O   . HOH G 7 .    ? 51.398 53.095  -28.305 1.00 24.54 ? 5803 HOH A O   1 
HETATM 9057 O  O   . HOH G 7 .    ? 53.671 53.631  -29.967 1.00 32.31 ? 5804 HOH A O   1 
HETATM 9058 O  O   . HOH G 7 .    ? 52.204 56.450  -29.987 1.00 20.40 ? 5805 HOH A O   1 
HETATM 9059 O  O   . HOH G 7 .    ? 49.144 50.606  -29.419 1.00 18.67 ? 5806 HOH A O   1 
HETATM 9060 O  O   . HOH G 7 .    ? 49.996 49.595  -34.339 1.00 36.03 ? 5807 HOH A O   1 
HETATM 9061 O  O   . HOH G 7 .    ? 39.472 48.944  -32.837 1.00 27.77 ? 5808 HOH A O   1 
HETATM 9062 O  O   . HOH G 7 .    ? 38.670 45.350  -33.638 1.00 27.87 ? 5809 HOH A O   1 
HETATM 9063 O  O   . HOH G 7 .    ? 38.663 51.478  -29.802 1.00 25.26 ? 5810 HOH A O   1 
HETATM 9064 O  O   . HOH G 7 .    ? 44.032 54.982  -26.493 1.00 32.76 ? 5811 HOH A O   1 
HETATM 9065 O  O   . HOH G 7 .    ? 46.981 55.941  -25.315 1.00 14.99 ? 5812 HOH A O   1 
HETATM 9066 O  O   . HOH G 7 .    ? 48.849 55.066  -22.394 1.00 18.25 ? 5813 HOH A O   1 
HETATM 9067 O  O   . HOH G 7 .    ? 51.605 53.305  -23.755 1.00 13.40 ? 5814 HOH A O   1 
HETATM 9068 O  O   . HOH G 7 .    ? 46.208 52.800  -18.886 1.00 23.52 ? 5815 HOH A O   1 
HETATM 9069 O  O   . HOH G 7 .    ? 45.011 55.129  -18.195 1.00 26.61 ? 5816 HOH A O   1 
HETATM 9070 O  O   . HOH G 7 .    ? 42.576 54.990  -17.303 1.00 30.46 ? 5817 HOH A O   1 
HETATM 9071 O  O   . HOH G 7 .    ? 41.181 52.378  -16.811 1.00 12.85 ? 5818 HOH A O   1 
HETATM 9072 O  O   . HOH G 7 .    ? 37.721 51.633  -18.375 1.00 18.43 ? 5819 HOH A O   1 
HETATM 9073 O  O   . HOH G 7 .    ? 37.719 52.128  -21.005 1.00 11.09 ? 5820 HOH A O   1 
HETATM 9074 O  O   . HOH G 7 .    ? 39.764 53.938  -20.568 1.00 16.59 ? 5821 HOH A O   1 
HETATM 9075 O  O   . HOH G 7 .    ? 40.296 56.275  -18.857 1.00 27.59 ? 5822 HOH A O   1 
HETATM 9076 O  O   . HOH G 7 .    ? 39.814 58.915  -17.768 1.00 16.46 ? 5823 HOH A O   1 
HETATM 9077 O  O   . HOH G 7 .    ? 41.777 58.713  -15.831 1.00 12.84 ? 5824 HOH A O   1 
HETATM 9078 O  O   . HOH G 7 .    ? 44.781 58.804  -15.868 1.00 12.44 ? 5825 HOH A O   1 
HETATM 9079 O  O   . HOH G 7 .    ? 45.959 59.928  -18.057 1.00 14.79 ? 5826 HOH A O   1 
HETATM 9080 O  O   . HOH G 7 .    ? 46.806 57.362  -18.563 1.00 12.78 ? 5827 HOH A O   1 
HETATM 9081 O  O   . HOH G 7 .    ? 47.397 55.763  -14.996 1.00 12.97 ? 5828 HOH A O   1 
HETATM 9082 O  O   . HOH G 7 .    ? 44.656 56.122  -15.266 1.00 15.58 ? 5829 HOH A O   1 
HETATM 9083 O  O   . HOH G 7 .    ? 43.064 59.409  -18.881 1.00 21.59 ? 5830 HOH A O   1 
HETATM 9084 O  O   . HOH G 7 .    ? 39.340 62.895  -18.945 1.00 7.79  ? 5831 HOH A O   1 
HETATM 9085 O  O   . HOH G 7 .    ? 39.387 64.650  -14.613 1.00 9.97  ? 5832 HOH A O   1 
HETATM 9086 O  O   . HOH G 7 .    ? 32.743 64.581  -9.781  1.00 15.71 ? 5833 HOH A O   1 
HETATM 9087 O  O   . HOH G 7 .    ? 34.341 58.511  -8.575  1.00 7.29  ? 5834 HOH A O   1 
HETATM 9088 O  O   . HOH G 7 .    ? 30.314 58.376  -11.607 1.00 7.80  ? 5835 HOH A O   1 
HETATM 9089 O  O   . HOH G 7 .    ? 26.840 60.765  -3.208  1.00 9.15  ? 5836 HOH A O   1 
HETATM 9090 O  O   . HOH G 7 .    ? 32.676 59.964  -1.651  1.00 6.76  ? 5837 HOH A O   1 
HETATM 9091 O  O   . HOH G 7 .    ? 33.159 62.677  0.377   1.00 7.00  ? 5838 HOH A O   1 
HETATM 9092 O  O   . HOH G 7 .    ? 37.630 56.862  1.880   1.00 8.33  ? 5839 HOH A O   1 
HETATM 9093 O  O   . HOH G 7 .    ? 39.690 55.489  3.136   1.00 13.21 ? 5840 HOH A O   1 
HETATM 9094 O  O   . HOH G 7 .    ? 38.912 52.919  2.085   1.00 24.17 ? 5841 HOH A O   1 
HETATM 9095 O  O   . HOH G 7 .    ? 36.054 52.975  1.476   1.00 8.96  ? 5842 HOH A O   1 
HETATM 9096 O  O   . HOH G 7 .    ? 34.342 52.251  -0.771  1.00 7.29  ? 5843 HOH A O   1 
HETATM 9097 O  O   . HOH G 7 .    ? 36.872 51.444  3.906   1.00 9.71  ? 5844 HOH A O   1 
HETATM 9098 O  O   . HOH G 7 .    ? 40.223 56.062  5.939   1.00 10.86 ? 5845 HOH A O   1 
HETATM 9099 O  O   . HOH G 7 .    ? 43.061 56.596  6.412   1.00 7.47  ? 5846 HOH A O   1 
HETATM 9100 O  O   . HOH G 7 .    ? 42.704 56.148  3.031   1.00 22.71 ? 5847 HOH A O   1 
HETATM 9101 O  O   . HOH G 7 .    ? 40.342 62.603  6.374   1.00 10.94 ? 5848 HOH A O   1 
HETATM 9102 O  O   . HOH G 7 .    ? 38.862 62.079  8.673   1.00 9.61  ? 5849 HOH A O   1 
HETATM 9103 O  O   . HOH G 7 .    ? 37.852 58.763  11.316  1.00 8.87  ? 5850 HOH A O   1 
HETATM 9104 O  O   . HOH G 7 .    ? 36.992 57.401  13.519  1.00 9.57  ? 5851 HOH A O   1 
HETATM 9105 O  O   . HOH G 7 .    ? 39.362 57.030  14.972  1.00 8.48  ? 5852 HOH A O   1 
HETATM 9106 O  O   . HOH G 7 .    ? 41.295 58.740  13.702  1.00 8.91  ? 5853 HOH A O   1 
HETATM 9107 O  O   . HOH G 7 .    ? 43.087 47.823  11.335  1.00 11.32 ? 5854 HOH A O   1 
HETATM 9108 O  O   . HOH G 7 .    ? 44.421 45.718  10.102  1.00 12.42 ? 5855 HOH A O   1 
HETATM 9109 O  O   . HOH G 7 .    ? 46.737 45.902  12.014  1.00 26.79 ? 5856 HOH A O   1 
HETATM 9110 O  O   . HOH G 7 .    ? 47.219 48.329  11.718  1.00 17.07 ? 5857 HOH A O   1 
HETATM 9111 O  O   . HOH G 7 .    ? 48.028 49.186  14.086  1.00 11.10 ? 5858 HOH A O   1 
HETATM 9112 O  O   . HOH G 7 .    ? 48.134 47.956  16.586  1.00 16.60 ? 5859 HOH A O   1 
HETATM 9113 O  O   . HOH G 7 .    ? 46.174 45.752  16.339  1.00 36.50 ? 5860 HOH A O   1 
HETATM 9114 O  O   . HOH G 7 .    ? 43.742 39.774  18.588  1.00 30.78 ? 5861 HOH A O   1 
HETATM 9115 O  O   . HOH G 7 .    ? 41.976 38.746  16.469  1.00 24.77 ? 5862 HOH A O   1 
HETATM 9116 O  O   . HOH G 7 .    ? 42.545 36.130  15.944  1.00 29.10 ? 5863 HOH A O   1 
HETATM 9117 O  O   . HOH G 7 .    ? 39.299 38.559  17.342  1.00 16.79 ? 5864 HOH A O   1 
HETATM 9118 O  O   . HOH G 7 .    ? 35.679 36.148  18.986  1.00 38.99 ? 5865 HOH A O   1 
HETATM 9119 O  O   . HOH G 7 .    ? 34.336 34.295  16.363  1.00 18.32 ? 5866 HOH A O   1 
HETATM 9120 O  O   . HOH G 7 .    ? 31.962 33.210  16.975  1.00 35.02 ? 5867 HOH A O   1 
HETATM 9121 O  O   . HOH G 7 .    ? 32.893 31.013  15.794  1.00 33.57 ? 5868 HOH A O   1 
HETATM 9122 O  O   . HOH G 7 .    ? 36.801 28.995  13.134  1.00 31.70 ? 5869 HOH A O   1 
HETATM 9123 O  O   . HOH G 7 .    ? 40.183 35.076  11.421  1.00 23.54 ? 5870 HOH A O   1 
HETATM 9124 O  O   . HOH G 7 .    ? 40.159 39.031  9.191   1.00 18.69 ? 5871 HOH A O   1 
HETATM 9125 O  O   . HOH G 7 .    ? 41.711 43.039  8.179   1.00 13.97 ? 5872 HOH A O   1 
HETATM 9126 O  O   . HOH G 7 .    ? 44.435 40.458  8.071   1.00 36.63 ? 5873 HOH A O   1 
HETATM 9127 O  O   . HOH G 7 .    ? 46.719 42.473  10.307  1.00 45.88 ? 5874 HOH A O   1 
HETATM 9128 O  O   . HOH G 7 .    ? 49.156 41.720  8.448   1.00 29.79 ? 5875 HOH A O   1 
HETATM 9129 O  O   . HOH G 7 .    ? 50.123 44.004  7.337   1.00 16.96 ? 5876 HOH A O   1 
HETATM 9130 O  O   . HOH G 7 .    ? 49.444 43.964  4.591   1.00 16.12 ? 5877 HOH A O   1 
HETATM 9131 O  O   . HOH G 7 .    ? 48.194 41.644  3.922   1.00 19.40 ? 5878 HOH A O   1 
HETATM 9132 O  O   . HOH G 7 .    ? 49.887 40.813  1.682   1.00 29.01 ? 5879 HOH A O   1 
HETATM 9133 O  O   . HOH G 7 .    ? 51.866 44.264  3.189   1.00 26.00 ? 5880 HOH A O   1 
HETATM 9134 O  O   . HOH G 7 .    ? 52.034 46.381  1.516   1.00 10.80 ? 5881 HOH A O   1 
HETATM 9135 O  O   . HOH G 7 .    ? 49.987 48.266  1.574   1.00 6.87  ? 5882 HOH A O   1 
HETATM 9136 O  O   . HOH G 7 .    ? 47.550 45.826  3.781   1.00 10.59 ? 5883 HOH A O   1 
HETATM 9137 O  O   . HOH G 7 .    ? 52.227 50.340  6.496   1.00 11.14 ? 5884 HOH A O   1 
HETATM 9138 O  O   . HOH G 7 .    ? 54.241 46.062  8.220   1.00 26.66 ? 5885 HOH A O   1 
HETATM 9139 O  O   . HOH G 7 .    ? 52.896 43.392  8.093   1.00 33.21 ? 5886 HOH A O   1 
HETATM 9140 O  O   . HOH G 7 .    ? 51.394 44.815  10.078  1.00 33.84 ? 5887 HOH A O   1 
HETATM 9141 O  O   . HOH G 7 .    ? 54.385 47.545  15.642  1.00 23.30 ? 5888 HOH A O   1 
HETATM 9142 O  O   . HOH G 7 .    ? 55.269 50.139  16.851  1.00 24.18 ? 5889 HOH A O   1 
HETATM 9143 O  O   . HOH G 7 .    ? 57.933 48.967  16.873  1.00 28.34 ? 5890 HOH A O   1 
HETATM 9144 O  O   . HOH G 7 .    ? 59.059 48.686  19.264  1.00 36.45 ? 5891 HOH A O   1 
HETATM 9145 O  O   . HOH G 7 .    ? 57.498 48.605  21.459  1.00 23.49 ? 5892 HOH A O   1 
HETATM 9146 O  O   . HOH G 7 .    ? 56.931 46.809  23.361  1.00 32.79 ? 5893 HOH A O   1 
HETATM 9147 O  O   . HOH G 7 .    ? 53.897 46.296  23.316  1.00 29.43 ? 5894 HOH A O   1 
HETATM 9148 O  O   . HOH G 7 .    ? 53.344 43.876  22.897  1.00 28.91 ? 5895 HOH A O   1 
HETATM 9149 O  O   . HOH G 7 .    ? 46.215 44.978  23.681  1.00 30.06 ? 5896 HOH A O   1 
HETATM 9150 O  O   . HOH G 7 .    ? 58.670 50.892  22.403  1.00 20.49 ? 5897 HOH A O   1 
HETATM 9151 O  O   . HOH G 7 .    ? 60.550 50.779  20.517  1.00 39.11 ? 5898 HOH A O   1 
HETATM 9152 O  O   . HOH G 7 .    ? 59.601 50.333  24.972  1.00 30.48 ? 5899 HOH A O   1 
HETATM 9153 O  O   . HOH G 7 .    ? 60.041 53.789  15.204  1.00 35.34 ? 5900 HOH A O   1 
HETATM 9154 O  O   . HOH G 7 .    ? 61.770 57.597  15.383  1.00 31.19 ? 5901 HOH A O   1 
HETATM 9155 O  O   . HOH G 7 .    ? 60.966 59.988  14.476  1.00 44.48 ? 5902 HOH A O   1 
HETATM 9156 O  O   . HOH G 7 .    ? 57.781 62.348  8.110   1.00 30.99 ? 5903 HOH A O   1 
HETATM 9157 O  O   . HOH G 7 .    ? 58.568 60.625  6.535   1.00 33.14 ? 5904 HOH A O   1 
HETATM 9158 O  O   . HOH G 7 .    ? 57.728 58.177  5.850   1.00 26.58 ? 5905 HOH A O   1 
HETATM 9159 O  O   . HOH G 7 .    ? 55.358 58.917  4.168   1.00 14.95 ? 5906 HOH A O   1 
HETATM 9160 O  O   . HOH G 7 .    ? 56.634 58.461  1.778   1.00 25.90 ? 5907 HOH A O   1 
HETATM 9161 O  O   . HOH G 7 .    ? 58.780 57.834  1.297   1.00 29.59 ? 5908 HOH A O   1 
HETATM 9162 O  O   . HOH G 7 .    ? 59.812 57.509  3.617   1.00 35.01 ? 5909 HOH A O   1 
HETATM 9163 O  O   . HOH G 7 .    ? 61.139 55.962  2.317   1.00 32.46 ? 5910 HOH A O   1 
HETATM 9164 O  O   . HOH G 7 .    ? 60.708 54.693  -0.024  1.00 15.41 ? 5911 HOH A O   1 
HETATM 9165 O  O   . HOH G 7 .    ? 58.938 52.521  0.203   1.00 13.61 ? 5912 HOH A O   1 
HETATM 9166 O  O   . HOH G 7 .    ? 59.471 49.925  -0.263  1.00 15.76 ? 5913 HOH A O   1 
HETATM 9167 O  O   . HOH G 7 .    ? 59.659 48.752  2.431   1.00 27.43 ? 5914 HOH A O   1 
HETATM 9168 O  O   . HOH G 7 .    ? 59.986 51.653  3.478   1.00 40.40 ? 5915 HOH A O   1 
HETATM 9169 O  O   . HOH G 7 .    ? 58.567 52.709  4.855   1.00 25.46 ? 5916 HOH A O   1 
HETATM 9170 O  O   . HOH G 7 .    ? 60.185 51.060  6.055   1.00 41.64 ? 5917 HOH A O   1 
HETATM 9171 O  O   . HOH G 7 .    ? 59.850 48.929  9.776   1.00 35.73 ? 5918 HOH A O   1 
HETATM 9172 O  O   . HOH G 7 .    ? 60.015 44.941  4.974   1.00 32.61 ? 5919 HOH A O   1 
HETATM 9173 O  O   . HOH G 7 .    ? 60.471 45.885  1.270   1.00 35.93 ? 5920 HOH A O   1 
HETATM 9174 O  O   . HOH G 7 .    ? 59.127 46.271  -1.131  1.00 20.15 ? 5921 HOH A O   1 
HETATM 9175 O  O   . HOH G 7 .    ? 63.035 44.373  -0.286  1.00 27.02 ? 5922 HOH A O   1 
HETATM 9176 O  O   . HOH G 7 .    ? 66.133 45.418  -2.837  1.00 31.66 ? 5923 HOH A O   1 
HETATM 9177 O  O   . HOH G 7 .    ? 67.523 46.497  -1.085  1.00 21.13 ? 5924 HOH A O   1 
HETATM 9178 O  O   . HOH G 7 .    ? 68.300 49.203  -0.716  1.00 29.15 ? 5925 HOH A O   1 
HETATM 9179 O  O   . HOH G 7 .    ? 71.116 49.407  0.194   1.00 21.42 ? 5926 HOH A O   1 
HETATM 9180 O  O   . HOH G 7 .    ? 72.747 50.945  2.162   1.00 29.73 ? 5927 HOH A O   1 
HETATM 9181 O  O   . HOH G 7 .    ? 67.651 52.563  1.770   1.00 45.35 ? 5928 HOH A O   1 
HETATM 9182 O  O   . HOH G 7 .    ? 67.203 55.427  1.209   1.00 23.03 ? 5929 HOH A O   1 
HETATM 9183 O  O   . HOH G 7 .    ? 63.926 56.929  1.090   1.00 27.41 ? 5930 HOH A O   1 
HETATM 9184 O  O   . HOH G 7 .    ? 63.373 58.530  -1.176  1.00 18.62 ? 5931 HOH A O   1 
HETATM 9185 O  O   . HOH G 7 .    ? 60.942 58.171  -2.535  1.00 13.11 ? 5932 HOH A O   1 
HETATM 9186 O  O   . HOH G 7 .    ? 59.029 56.732  -1.119  1.00 13.50 ? 5933 HOH A O   1 
HETATM 9187 O  O   . HOH G 7 .    ? 56.502 55.699  -1.783  1.00 9.62  ? 5934 HOH A O   1 
HETATM 9188 O  O   . HOH G 7 .    ? 56.288 53.317  -0.472  1.00 7.69  ? 5935 HOH A O   1 
HETATM 9189 O  O   . HOH G 7 .    ? 55.078 57.514  -0.115  1.00 14.18 ? 5936 HOH A O   1 
HETATM 9190 O  O   . HOH G 7 .    ? 52.984 58.782  -1.569  1.00 15.64 ? 5937 HOH A O   1 
HETATM 9191 O  O   . HOH G 7 .    ? 51.624 56.585  -5.372  1.00 7.80  ? 5938 HOH A O   1 
HETATM 9192 O  O   . HOH G 7 .    ? 52.324 54.012  -4.696  1.00 8.05  ? 5939 HOH A O   1 
HETATM 9193 O  O   . HOH G 7 .    ? 49.900 57.650  -7.284  1.00 9.56  ? 5940 HOH A O   1 
HETATM 9194 O  O   . HOH G 7 .    ? 51.015 59.867  -8.672  1.00 12.18 ? 5941 HOH A O   1 
HETATM 9195 O  O   . HOH G 7 .    ? 50.144 59.538  -11.215 1.00 9.66  ? 5942 HOH A O   1 
HETATM 9196 O  O   . HOH G 7 .    ? 49.715 62.244  -8.416  1.00 10.19 ? 5943 HOH A O   1 
HETATM 9197 O  O   . HOH G 7 .    ? 53.793 59.912  -9.037  1.00 10.31 ? 5944 HOH A O   1 
HETATM 9198 O  O   . HOH G 7 .    ? 55.752 59.347  -11.247 1.00 8.53  ? 5945 HOH A O   1 
HETATM 9199 O  O   . HOH G 7 .    ? 61.158 59.684  -7.961  1.00 9.34  ? 5946 HOH A O   1 
HETATM 9200 O  O   . HOH G 7 .    ? 59.666 60.709  -5.882  1.00 16.61 ? 5947 HOH A O   1 
HETATM 9201 O  O   . HOH G 7 .    ? 60.852 60.918  -3.270  1.00 16.01 ? 5948 HOH A O   1 
HETATM 9202 O  O   . HOH G 7 .    ? 60.682 62.174  -0.974  1.00 15.00 ? 5949 HOH A O   1 
HETATM 9203 O  O   . HOH G 7 .    ? 62.519 60.599  0.825   1.00 28.73 ? 5950 HOH A O   1 
HETATM 9204 O  O   . HOH G 7 .    ? 60.643 59.935  3.050   1.00 32.70 ? 5951 HOH A O   1 
HETATM 9205 O  O   . HOH G 7 .    ? 57.051 60.945  1.862   1.00 15.72 ? 5952 HOH A O   1 
HETATM 9206 O  O   . HOH G 7 .    ? 56.493 64.483  9.211   1.00 35.42 ? 5953 HOH A O   1 
HETATM 9207 O  O   . HOH G 7 .    ? 57.560 67.392  13.727  1.00 40.84 ? 5954 HOH A O   1 
HETATM 9208 O  O   . HOH G 7 .    ? 61.507 73.712  0.434   1.00 32.14 ? 5955 HOH A O   1 
HETATM 9209 O  O   . HOH G 7 .    ? 62.126 76.032  0.849   1.00 35.47 ? 5956 HOH A O   1 
HETATM 9210 O  O   . HOH G 7 .    ? 65.132 77.199  0.391   1.00 44.45 ? 5957 HOH A O   1 
HETATM 9211 O  O   . HOH G 7 .    ? 70.170 69.895  -12.270 1.00 18.97 ? 5958 HOH A O   1 
HETATM 9212 O  O   . HOH G 7 .    ? 74.056 65.713  -17.266 1.00 19.04 ? 5959 HOH A O   1 
HETATM 9213 O  O   . HOH G 7 .    ? 75.084 64.277  -15.451 1.00 28.27 ? 5960 HOH A O   1 
HETATM 9214 O  O   . HOH G 7 .    ? 66.574 62.944  -12.905 1.00 30.70 ? 5961 HOH A O   1 
HETATM 9215 O  O   . HOH G 7 .    ? 65.865 60.363  -7.353  1.00 12.77 ? 5962 HOH A O   1 
HETATM 9216 O  O   . HOH G 7 .    ? 63.217 61.379  -7.191  1.00 12.52 ? 5963 HOH A O   1 
HETATM 9217 O  O   . HOH G 7 .    ? 63.338 61.025  -4.498  1.00 16.05 ? 5964 HOH A O   1 
HETATM 9218 O  O   . HOH G 7 .    ? 65.104 59.340  -3.242  1.00 14.49 ? 5965 HOH A O   1 
HETATM 9219 O  O   . HOH G 7 .    ? 67.652 60.770  -5.090  1.00 13.24 ? 5966 HOH A O   1 
HETATM 9220 O  O   . HOH G 7 .    ? 68.967 58.206  -4.769  1.00 14.85 ? 5967 HOH A O   1 
HETATM 9221 O  O   . HOH G 7 .    ? 69.352 61.397  -2.014  1.00 15.45 ? 5968 HOH A O   1 
HETATM 9222 O  O   . HOH G 7 .    ? 71.633 59.568  1.236   1.00 30.49 ? 5969 HOH A O   1 
HETATM 9223 O  O   . HOH G 7 .    ? 73.404 63.132  0.254   1.00 33.53 ? 5970 HOH A O   1 
HETATM 9224 O  O   . HOH G 7 .    ? 79.438 51.291  -0.444  1.00 25.09 ? 5971 HOH A O   1 
HETATM 9225 O  O   . HOH G 7 .    ? 76.050 48.349  -4.858  1.00 41.18 ? 5972 HOH A O   1 
HETATM 9226 O  O   . HOH G 7 .    ? 75.367 51.376  -6.475  1.00 38.16 ? 5973 HOH A O   1 
HETATM 9227 O  O   . HOH G 7 .    ? 78.865 50.175  -8.009  1.00 37.30 ? 5974 HOH A O   1 
HETATM 9228 O  O   . HOH G 7 .    ? 79.731 50.423  -10.120 1.00 49.09 ? 5975 HOH A O   1 
HETATM 9229 O  O   . HOH G 7 .    ? 77.483 49.410  -10.298 1.00 43.10 ? 5976 HOH A O   1 
HETATM 9230 O  O   . HOH G 7 .    ? 63.735 44.728  -6.338  1.00 18.36 ? 5977 HOH A O   1 
HETATM 9231 O  O   . HOH G 7 .    ? 63.628 51.776  0.174   1.00 30.75 ? 5978 HOH A O   1 
HETATM 9232 O  O   . HOH G 7 .    ? 62.346 51.082  2.300   1.00 42.22 ? 5979 HOH A O   1 
HETATM 9233 O  O   . HOH G 7 .    ? 58.188 42.432  1.920   1.00 21.90 ? 5980 HOH A O   1 
HETATM 9234 O  O   . HOH G 7 .    ? 55.989 38.570  1.528   1.00 41.29 ? 5981 HOH A O   1 
HETATM 9235 O  O   . HOH G 7 .    ? 52.438 36.705  -2.894  1.00 28.69 ? 5982 HOH A O   1 
HETATM 9236 O  O   . HOH G 7 .    ? 49.029 38.632  -3.154  1.00 39.11 ? 5983 HOH A O   1 
HETATM 9237 O  O   . HOH G 7 .    ? 58.546 34.635  -5.684  1.00 36.64 ? 5984 HOH A O   1 
HETATM 9238 O  O   . HOH G 7 .    ? 47.295 41.158  -14.757 1.00 22.21 ? 5985 HOH A O   1 
HETATM 9239 O  O   . HOH G 7 .    ? 45.224 39.686  -14.053 1.00 40.72 ? 5986 HOH A O   1 
HETATM 9240 O  O   . HOH G 7 .    ? 42.725 39.305  -15.650 1.00 20.97 ? 5987 HOH A O   1 
HETATM 9241 O  O   . HOH G 7 .    ? 39.449 38.659  -10.845 1.00 49.41 ? 5988 HOH A O   1 
HETATM 9242 O  O   . HOH G 7 .    ? 35.799 38.952  -16.056 1.00 21.95 ? 5989 HOH A O   1 
HETATM 9243 O  O   . HOH G 7 .    ? 36.203 36.333  -18.220 1.00 34.66 ? 5990 HOH A O   1 
HETATM 9244 O  O   . HOH G 7 .    ? 36.891 34.932  -15.821 1.00 26.44 ? 5991 HOH A O   1 
HETATM 9245 O  O   . HOH G 7 .    ? 30.592 35.180  -12.468 1.00 21.12 ? 5992 HOH A O   1 
HETATM 9246 O  O   . HOH G 7 .    ? 30.854 34.492  -9.843  1.00 32.39 ? 5993 HOH A O   1 
HETATM 9247 O  O   . HOH G 7 .    ? 30.751 33.504  -6.469  1.00 32.72 ? 5994 HOH A O   1 
HETATM 9248 O  O   . HOH G 7 .    ? 28.258 35.072  -6.744  1.00 18.48 ? 5995 HOH A O   1 
HETATM 9249 O  O   . HOH G 7 .    ? 25.400 34.316  -6.968  1.00 32.68 ? 5996 HOH A O   1 
HETATM 9250 O  O   . HOH G 7 .    ? 26.812 41.511  -13.165 1.00 9.92  ? 5997 HOH A O   1 
HETATM 9251 O  O   . HOH G 7 .    ? 28.994 42.683  -11.885 1.00 10.56 ? 5998 HOH A O   1 
HETATM 9252 O  O   . HOH G 7 .    ? 24.329 42.084  -14.378 1.00 29.16 ? 5999 HOH A O   1 
HETATM 9253 O  O   . HOH G 7 .    ? 21.920 42.582  -13.037 1.00 32.24 ? 6000 HOH A O   1 
HETATM 9254 O  O   . HOH G 7 .    ? 33.148 40.793  -18.115 1.00 23.70 ? 6001 HOH A O   1 
HETATM 9255 O  O   . HOH G 7 .    ? 35.356 50.640  -17.453 1.00 14.68 ? 6002 HOH A O   1 
HETATM 9256 O  O   . HOH G 7 .    ? 34.209 56.387  -26.131 1.00 11.40 ? 6003 HOH A O   1 
HETATM 9257 O  O   . HOH G 7 .    ? 32.198 58.646  -28.275 1.00 17.70 ? 6004 HOH A O   1 
HETATM 9258 O  O   . HOH G 7 .    ? 31.893 51.236  -35.375 1.00 24.20 ? 6005 HOH A O   1 
HETATM 9259 O  O   . HOH G 7 .    ? 28.580 59.749  -39.102 1.00 37.81 ? 6006 HOH A O   1 
HETATM 9260 O  O   . HOH G 7 .    ? 28.947 62.241  -39.767 1.00 22.54 ? 6007 HOH A O   1 
HETATM 9261 O  O   . HOH G 7 .    ? 43.676 68.356  -24.719 1.00 16.73 ? 6008 HOH A O   1 
HETATM 9262 O  O   . HOH G 7 .    ? 53.849 64.798  -19.644 1.00 10.55 ? 6009 HOH A O   1 
HETATM 9263 O  O   . HOH G 7 .    ? 60.597 60.901  -17.899 1.00 11.99 ? 6010 HOH A O   1 
HETATM 9264 O  O   . HOH G 7 .    ? 58.912 53.761  -21.958 1.00 24.07 ? 6011 HOH A O   1 
HETATM 9265 O  O   . HOH G 7 .    ? 61.685 54.360  -28.620 1.00 23.12 ? 6012 HOH A O   1 
HETATM 9266 O  O   . HOH G 7 .    ? 59.916 52.876  -30.306 1.00 27.43 ? 6013 HOH A O   1 
HETATM 9267 O  O   . HOH G 7 .    ? 58.730 44.164  -27.895 1.00 29.36 ? 6014 HOH A O   1 
HETATM 9268 O  O   . HOH G 7 .    ? 45.411 34.011  -18.732 1.00 37.59 ? 6015 HOH A O   1 
HETATM 9269 O  O   . HOH G 7 .    ? 38.457 39.874  1.802   1.00 9.57  ? 6016 HOH A O   1 
HETATM 9270 O  O   . HOH G 7 .    ? 37.814 37.270  3.141   1.00 36.27 ? 6017 HOH A O   1 
HETATM 9271 O  O   . HOH G 7 .    ? 39.640 37.153  4.715   1.00 35.40 ? 6018 HOH A O   1 
HETATM 9272 O  O   . HOH G 7 .    ? 37.549 33.963  5.363   1.00 40.17 ? 6019 HOH A O   1 
HETATM 9273 O  O   . HOH G 7 .    ? 35.211 36.193  3.567   1.00 30.78 ? 6020 HOH A O   1 
HETATM 9274 O  O   . HOH G 7 .    ? 30.745 57.027  4.968   1.00 25.91 ? 6021 HOH A O   1 
HETATM 9275 O  O   . HOH G 7 .    ? 36.661 72.560  0.624   1.00 9.65  ? 6022 HOH A O   1 
HETATM 9276 O  O   . HOH G 7 .    ? 38.011 73.230  -1.990  1.00 12.12 ? 6023 HOH A O   1 
HETATM 9277 O  O   . HOH G 7 .    ? 37.174 71.817  -4.208  1.00 9.60  ? 6024 HOH A O   1 
HETATM 9278 O  O   . HOH G 7 .    ? 33.464 78.510  -4.611  1.00 12.59 ? 6025 HOH A O   1 
HETATM 9279 O  O   . HOH G 7 .    ? 31.456 76.641  -5.999  1.00 11.31 ? 6026 HOH A O   1 
HETATM 9280 O  O   . HOH G 7 .    ? 37.511 83.100  -3.572  1.00 23.19 ? 6027 HOH A O   1 
HETATM 9281 O  O   . HOH G 7 .    ? 45.849 79.207  -7.461  1.00 24.39 ? 6028 HOH A O   1 
HETATM 9282 O  O   . HOH G 7 .    ? 48.390 77.934  -9.618  1.00 27.75 ? 6029 HOH A O   1 
HETATM 9283 O  O   . HOH G 7 .    ? 46.160 70.894  0.333   1.00 20.17 ? 6030 HOH A O   1 
HETATM 9284 O  O   . HOH G 7 .    ? 43.593 72.869  6.058   1.00 11.34 ? 6031 HOH A O   1 
HETATM 9285 O  O   . HOH G 7 .    ? 35.870 80.928  6.924   1.00 22.27 ? 6032 HOH A O   1 
HETATM 9286 O  O   . HOH G 7 .    ? 33.304 81.268  7.537   1.00 33.38 ? 6033 HOH A O   1 
HETATM 9287 O  O   . HOH G 7 .    ? 35.684 78.444  12.023  1.00 34.68 ? 6034 HOH A O   1 
HETATM 9288 O  O   . HOH G 7 .    ? 24.730 70.482  -8.445  1.00 9.01  ? 6035 HOH A O   1 
HETATM 9289 O  O   . HOH G 7 .    ? 26.858 68.861  -8.925  1.00 8.80  ? 6036 HOH A O   1 
HETATM 9290 O  O   . HOH G 7 .    ? 42.182 63.394  -6.917  1.00 5.86  ? 6037 HOH A O   1 
HETATM 9291 O  O   . HOH G 7 .    ? 10.741 58.143  -20.832 1.00 29.86 ? 6038 HOH A O   1 
HETATM 9292 O  O   . HOH G 7 .    ? 9.661  60.338  -20.173 1.00 34.54 ? 6039 HOH A O   1 
HETATM 9293 O  O   . HOH G 7 .    ? 3.774  55.120  -8.901  1.00 36.86 ? 6040 HOH A O   1 
HETATM 9294 O  O   . HOH G 7 .    ? 4.034  56.352  -6.297  1.00 33.92 ? 6041 HOH A O   1 
HETATM 9295 O  O   . HOH G 7 .    ? 4.994  52.801  -5.401  1.00 26.33 ? 6042 HOH A O   1 
HETATM 9296 O  O   . HOH G 7 .    ? 28.003 101.980 -19.409 1.00 34.26 ? 6043 HOH A O   1 
HETATM 9297 O  O   . HOH G 7 .    ? 30.258 102.729 -16.913 1.00 43.07 ? 6044 HOH A O   1 
HETATM 9298 O  O   . HOH G 7 .    ? 38.782 98.574  -23.973 1.00 49.11 ? 6045 HOH A O   1 
HETATM 9299 O  O   . HOH G 7 .    ? 28.990 93.596  -38.310 1.00 25.57 ? 6046 HOH A O   1 
HETATM 9300 O  O   . HOH G 7 .    ? 38.599 94.084  -41.716 1.00 26.17 ? 6047 HOH A O   1 
HETATM 9301 O  O   . HOH G 7 .    ? 40.793 87.389  -43.626 1.00 28.48 ? 6048 HOH A O   1 
HETATM 9302 O  O   . HOH G 7 .    ? 39.017 86.682  -41.347 1.00 32.78 ? 6049 HOH A O   1 
HETATM 9303 O  O   . HOH G 7 .    ? 38.622 83.434  -39.669 1.00 33.43 ? 6050 HOH A O   1 
HETATM 9304 O  O   . HOH G 7 .    ? 46.090 96.766  -43.916 1.00 27.98 ? 6051 HOH A O   1 
HETATM 9305 O  O   . HOH G 7 .    ? 63.211 74.593  -45.804 1.00 33.16 ? 6052 HOH A O   1 
HETATM 9306 O  O   . HOH G 7 .    ? 72.580 95.395  -31.637 1.00 29.35 ? 6053 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    5004 5004 NAG NAG A . 
C 3 ZN  1    5001 5001 ZN  ZN  A . 
D 4 PO4 1    5005 5005 PO4 PO4 A . 
E 5 MSN 1    5002 5002 MSN MSN A . 
F 6 MPD 1    5003 5003 MPD MPD A . 
G 7 HOH 1    5006 1    HOH HOH A . 
G 7 HOH 2    5007 2    HOH HOH A . 
G 7 HOH 3    5008 3    HOH HOH A . 
G 7 HOH 4    5009 4    HOH HOH A . 
G 7 HOH 5    5010 5    HOH HOH A . 
G 7 HOH 6    5011 6    HOH HOH A . 
G 7 HOH 7    5012 7    HOH HOH A . 
G 7 HOH 8    5013 8    HOH HOH A . 
G 7 HOH 9    5014 9    HOH HOH A . 
G 7 HOH 10   5015 10   HOH HOH A . 
G 7 HOH 11   5016 11   HOH HOH A . 
G 7 HOH 12   5017 12   HOH HOH A . 
G 7 HOH 13   5018 13   HOH HOH A . 
G 7 HOH 14   5019 14   HOH HOH A . 
G 7 HOH 15   5020 15   HOH HOH A . 
G 7 HOH 16   5021 16   HOH HOH A . 
G 7 HOH 17   5022 17   HOH HOH A . 
G 7 HOH 18   5023 18   HOH HOH A . 
G 7 HOH 19   5024 19   HOH HOH A . 
G 7 HOH 20   5025 20   HOH HOH A . 
G 7 HOH 21   5026 21   HOH HOH A . 
G 7 HOH 22   5027 22   HOH HOH A . 
G 7 HOH 23   5028 23   HOH HOH A . 
G 7 HOH 24   5029 24   HOH HOH A . 
G 7 HOH 25   5030 25   HOH HOH A . 
G 7 HOH 26   5031 26   HOH HOH A . 
G 7 HOH 27   5032 27   HOH HOH A . 
G 7 HOH 28   5033 28   HOH HOH A . 
G 7 HOH 29   5034 29   HOH HOH A . 
G 7 HOH 30   5035 30   HOH HOH A . 
G 7 HOH 31   5036 31   HOH HOH A . 
G 7 HOH 32   5037 32   HOH HOH A . 
G 7 HOH 33   5038 33   HOH HOH A . 
G 7 HOH 34   5039 34   HOH HOH A . 
G 7 HOH 35   5040 35   HOH HOH A . 
G 7 HOH 36   5041 36   HOH HOH A . 
G 7 HOH 37   5042 37   HOH HOH A . 
G 7 HOH 38   5043 38   HOH HOH A . 
G 7 HOH 39   5044 39   HOH HOH A . 
G 7 HOH 40   5045 40   HOH HOH A . 
G 7 HOH 41   5046 41   HOH HOH A . 
G 7 HOH 42   5047 42   HOH HOH A . 
G 7 HOH 43   5048 43   HOH HOH A . 
G 7 HOH 44   5049 44   HOH HOH A . 
G 7 HOH 45   5050 45   HOH HOH A . 
G 7 HOH 46   5051 46   HOH HOH A . 
G 7 HOH 47   5052 47   HOH HOH A . 
G 7 HOH 48   5053 48   HOH HOH A . 
G 7 HOH 49   5054 49   HOH HOH A . 
G 7 HOH 50   5055 50   HOH HOH A . 
G 7 HOH 51   5056 51   HOH HOH A . 
G 7 HOH 52   5057 52   HOH HOH A . 
G 7 HOH 53   5058 53   HOH HOH A . 
G 7 HOH 54   5059 54   HOH HOH A . 
G 7 HOH 55   5060 55   HOH HOH A . 
G 7 HOH 56   5061 56   HOH HOH A . 
G 7 HOH 57   5062 57   HOH HOH A . 
G 7 HOH 58   5063 58   HOH HOH A . 
G 7 HOH 59   5064 59   HOH HOH A . 
G 7 HOH 60   5065 60   HOH HOH A . 
G 7 HOH 61   5066 61   HOH HOH A . 
G 7 HOH 62   5067 62   HOH HOH A . 
G 7 HOH 63   5068 63   HOH HOH A . 
G 7 HOH 64   5069 64   HOH HOH A . 
G 7 HOH 65   5070 65   HOH HOH A . 
G 7 HOH 66   5071 66   HOH HOH A . 
G 7 HOH 67   5072 67   HOH HOH A . 
G 7 HOH 68   5073 68   HOH HOH A . 
G 7 HOH 69   5074 69   HOH HOH A . 
G 7 HOH 70   5075 70   HOH HOH A . 
G 7 HOH 71   5076 71   HOH HOH A . 
G 7 HOH 72   5077 72   HOH HOH A . 
G 7 HOH 73   5078 73   HOH HOH A . 
G 7 HOH 74   5079 74   HOH HOH A . 
G 7 HOH 75   5080 75   HOH HOH A . 
G 7 HOH 76   5081 76   HOH HOH A . 
G 7 HOH 77   5082 77   HOH HOH A . 
G 7 HOH 78   5083 78   HOH HOH A . 
G 7 HOH 79   5084 79   HOH HOH A . 
G 7 HOH 80   5085 80   HOH HOH A . 
G 7 HOH 81   5086 81   HOH HOH A . 
G 7 HOH 82   5087 82   HOH HOH A . 
G 7 HOH 83   5088 83   HOH HOH A . 
G 7 HOH 84   5089 84   HOH HOH A . 
G 7 HOH 85   5090 85   HOH HOH A . 
G 7 HOH 86   5091 86   HOH HOH A . 
G 7 HOH 87   5092 87   HOH HOH A . 
G 7 HOH 88   5093 88   HOH HOH A . 
G 7 HOH 89   5094 89   HOH HOH A . 
G 7 HOH 90   5095 90   HOH HOH A . 
G 7 HOH 91   5096 91   HOH HOH A . 
G 7 HOH 92   5097 92   HOH HOH A . 
G 7 HOH 93   5098 93   HOH HOH A . 
G 7 HOH 94   5099 94   HOH HOH A . 
G 7 HOH 95   5100 95   HOH HOH A . 
G 7 HOH 96   5101 96   HOH HOH A . 
G 7 HOH 97   5102 97   HOH HOH A . 
G 7 HOH 98   5103 98   HOH HOH A . 
G 7 HOH 99   5104 99   HOH HOH A . 
G 7 HOH 100  5105 100  HOH HOH A . 
G 7 HOH 101  5106 101  HOH HOH A . 
G 7 HOH 102  5107 102  HOH HOH A . 
G 7 HOH 103  5108 103  HOH HOH A . 
G 7 HOH 104  5109 104  HOH HOH A . 
G 7 HOH 105  5110 105  HOH HOH A . 
G 7 HOH 106  5111 106  HOH HOH A . 
G 7 HOH 107  5112 107  HOH HOH A . 
G 7 HOH 108  5113 108  HOH HOH A . 
G 7 HOH 109  5114 109  HOH HOH A . 
G 7 HOH 110  5115 110  HOH HOH A . 
G 7 HOH 111  5116 111  HOH HOH A . 
G 7 HOH 112  5117 112  HOH HOH A . 
G 7 HOH 113  5118 113  HOH HOH A . 
G 7 HOH 114  5119 114  HOH HOH A . 
G 7 HOH 115  5120 115  HOH HOH A . 
G 7 HOH 116  5121 116  HOH HOH A . 
G 7 HOH 117  5122 117  HOH HOH A . 
G 7 HOH 118  5123 118  HOH HOH A . 
G 7 HOH 119  5124 119  HOH HOH A . 
G 7 HOH 120  5125 120  HOH HOH A . 
G 7 HOH 121  5126 121  HOH HOH A . 
G 7 HOH 122  5127 122  HOH HOH A . 
G 7 HOH 123  5128 123  HOH HOH A . 
G 7 HOH 124  5129 124  HOH HOH A . 
G 7 HOH 125  5130 125  HOH HOH A . 
G 7 HOH 126  5131 126  HOH HOH A . 
G 7 HOH 127  5132 127  HOH HOH A . 
G 7 HOH 128  5133 128  HOH HOH A . 
G 7 HOH 129  5134 129  HOH HOH A . 
G 7 HOH 130  5135 130  HOH HOH A . 
G 7 HOH 131  5136 131  HOH HOH A . 
G 7 HOH 132  5137 132  HOH HOH A . 
G 7 HOH 133  5138 133  HOH HOH A . 
G 7 HOH 134  5139 134  HOH HOH A . 
G 7 HOH 135  5140 135  HOH HOH A . 
G 7 HOH 136  5141 136  HOH HOH A . 
G 7 HOH 137  5142 137  HOH HOH A . 
G 7 HOH 138  5143 138  HOH HOH A . 
G 7 HOH 139  5144 139  HOH HOH A . 
G 7 HOH 140  5145 140  HOH HOH A . 
G 7 HOH 141  5146 141  HOH HOH A . 
G 7 HOH 142  5147 142  HOH HOH A . 
G 7 HOH 143  5148 143  HOH HOH A . 
G 7 HOH 144  5149 144  HOH HOH A . 
G 7 HOH 145  5150 145  HOH HOH A . 
G 7 HOH 146  5151 146  HOH HOH A . 
G 7 HOH 147  5152 147  HOH HOH A . 
G 7 HOH 148  5153 148  HOH HOH A . 
G 7 HOH 149  5154 149  HOH HOH A . 
G 7 HOH 150  5155 150  HOH HOH A . 
G 7 HOH 151  5156 151  HOH HOH A . 
G 7 HOH 152  5157 152  HOH HOH A . 
G 7 HOH 153  5158 153  HOH HOH A . 
G 7 HOH 154  5159 154  HOH HOH A . 
G 7 HOH 155  5160 155  HOH HOH A . 
G 7 HOH 156  5161 156  HOH HOH A . 
G 7 HOH 157  5162 157  HOH HOH A . 
G 7 HOH 158  5163 158  HOH HOH A . 
G 7 HOH 159  5164 159  HOH HOH A . 
G 7 HOH 160  5165 160  HOH HOH A . 
G 7 HOH 161  5166 161  HOH HOH A . 
G 7 HOH 162  5167 162  HOH HOH A . 
G 7 HOH 163  5168 163  HOH HOH A . 
G 7 HOH 164  5169 164  HOH HOH A . 
G 7 HOH 165  5170 165  HOH HOH A . 
G 7 HOH 166  5171 166  HOH HOH A . 
G 7 HOH 167  5172 167  HOH HOH A . 
G 7 HOH 168  5173 168  HOH HOH A . 
G 7 HOH 169  5174 169  HOH HOH A . 
G 7 HOH 170  5175 170  HOH HOH A . 
G 7 HOH 171  5176 171  HOH HOH A . 
G 7 HOH 172  5177 172  HOH HOH A . 
G 7 HOH 173  5178 173  HOH HOH A . 
G 7 HOH 174  5179 174  HOH HOH A . 
G 7 HOH 175  5180 175  HOH HOH A . 
G 7 HOH 176  5181 176  HOH HOH A . 
G 7 HOH 177  5182 177  HOH HOH A . 
G 7 HOH 178  5183 178  HOH HOH A . 
G 7 HOH 179  5184 179  HOH HOH A . 
G 7 HOH 180  5185 180  HOH HOH A . 
G 7 HOH 181  5186 181  HOH HOH A . 
G 7 HOH 182  5187 182  HOH HOH A . 
G 7 HOH 183  5188 183  HOH HOH A . 
G 7 HOH 184  5189 184  HOH HOH A . 
G 7 HOH 185  5190 185  HOH HOH A . 
G 7 HOH 186  5191 186  HOH HOH A . 
G 7 HOH 187  5192 187  HOH HOH A . 
G 7 HOH 188  5193 188  HOH HOH A . 
G 7 HOH 189  5194 189  HOH HOH A . 
G 7 HOH 190  5195 190  HOH HOH A . 
G 7 HOH 191  5196 191  HOH HOH A . 
G 7 HOH 192  5197 192  HOH HOH A . 
G 7 HOH 193  5198 193  HOH HOH A . 
G 7 HOH 194  5199 194  HOH HOH A . 
G 7 HOH 195  5200 195  HOH HOH A . 
G 7 HOH 196  5201 196  HOH HOH A . 
G 7 HOH 197  5202 197  HOH HOH A . 
G 7 HOH 198  5203 198  HOH HOH A . 
G 7 HOH 199  5204 199  HOH HOH A . 
G 7 HOH 200  5205 200  HOH HOH A . 
G 7 HOH 201  5206 201  HOH HOH A . 
G 7 HOH 202  5207 202  HOH HOH A . 
G 7 HOH 203  5208 203  HOH HOH A . 
G 7 HOH 204  5209 204  HOH HOH A . 
G 7 HOH 205  5210 205  HOH HOH A . 
G 7 HOH 206  5211 206  HOH HOH A . 
G 7 HOH 207  5212 207  HOH HOH A . 
G 7 HOH 208  5213 208  HOH HOH A . 
G 7 HOH 209  5214 209  HOH HOH A . 
G 7 HOH 210  5215 210  HOH HOH A . 
G 7 HOH 211  5216 211  HOH HOH A . 
G 7 HOH 212  5217 212  HOH HOH A . 
G 7 HOH 213  5218 213  HOH HOH A . 
G 7 HOH 214  5219 214  HOH HOH A . 
G 7 HOH 215  5220 215  HOH HOH A . 
G 7 HOH 216  5221 216  HOH HOH A . 
G 7 HOH 217  5222 217  HOH HOH A . 
G 7 HOH 218  5223 218  HOH HOH A . 
G 7 HOH 219  5224 219  HOH HOH A . 
G 7 HOH 220  5225 220  HOH HOH A . 
G 7 HOH 221  5226 221  HOH HOH A . 
G 7 HOH 222  5227 222  HOH HOH A . 
G 7 HOH 223  5228 223  HOH HOH A . 
G 7 HOH 224  5229 224  HOH HOH A . 
G 7 HOH 225  5230 225  HOH HOH A . 
G 7 HOH 226  5231 226  HOH HOH A . 
G 7 HOH 227  5232 227  HOH HOH A . 
G 7 HOH 228  5233 228  HOH HOH A . 
G 7 HOH 229  5234 229  HOH HOH A . 
G 7 HOH 230  5235 230  HOH HOH A . 
G 7 HOH 231  5236 231  HOH HOH A . 
G 7 HOH 232  5237 232  HOH HOH A . 
G 7 HOH 233  5238 233  HOH HOH A . 
G 7 HOH 234  5239 234  HOH HOH A . 
G 7 HOH 235  5240 235  HOH HOH A . 
G 7 HOH 236  5241 236  HOH HOH A . 
G 7 HOH 237  5242 237  HOH HOH A . 
G 7 HOH 238  5243 238  HOH HOH A . 
G 7 HOH 239  5244 239  HOH HOH A . 
G 7 HOH 240  5245 240  HOH HOH A . 
G 7 HOH 241  5246 241  HOH HOH A . 
G 7 HOH 242  5247 242  HOH HOH A . 
G 7 HOH 243  5248 243  HOH HOH A . 
G 7 HOH 244  5249 244  HOH HOH A . 
G 7 HOH 245  5250 245  HOH HOH A . 
G 7 HOH 246  5251 246  HOH HOH A . 
G 7 HOH 247  5252 247  HOH HOH A . 
G 7 HOH 248  5253 248  HOH HOH A . 
G 7 HOH 249  5254 249  HOH HOH A . 
G 7 HOH 250  5255 250  HOH HOH A . 
G 7 HOH 251  5256 251  HOH HOH A . 
G 7 HOH 252  5257 252  HOH HOH A . 
G 7 HOH 253  5258 253  HOH HOH A . 
G 7 HOH 254  5259 254  HOH HOH A . 
G 7 HOH 255  5260 255  HOH HOH A . 
G 7 HOH 256  5261 256  HOH HOH A . 
G 7 HOH 257  5262 257  HOH HOH A . 
G 7 HOH 258  5263 258  HOH HOH A . 
G 7 HOH 259  5264 259  HOH HOH A . 
G 7 HOH 260  5265 260  HOH HOH A . 
G 7 HOH 261  5266 261  HOH HOH A . 
G 7 HOH 262  5267 262  HOH HOH A . 
G 7 HOH 263  5268 263  HOH HOH A . 
G 7 HOH 264  5269 264  HOH HOH A . 
G 7 HOH 265  5270 265  HOH HOH A . 
G 7 HOH 266  5271 266  HOH HOH A . 
G 7 HOH 267  5272 267  HOH HOH A . 
G 7 HOH 268  5273 268  HOH HOH A . 
G 7 HOH 269  5274 269  HOH HOH A . 
G 7 HOH 270  5275 270  HOH HOH A . 
G 7 HOH 271  5276 271  HOH HOH A . 
G 7 HOH 272  5277 272  HOH HOH A . 
G 7 HOH 273  5278 273  HOH HOH A . 
G 7 HOH 274  5279 274  HOH HOH A . 
G 7 HOH 275  5280 275  HOH HOH A . 
G 7 HOH 276  5281 276  HOH HOH A . 
G 7 HOH 277  5282 277  HOH HOH A . 
G 7 HOH 278  5283 278  HOH HOH A . 
G 7 HOH 279  5284 279  HOH HOH A . 
G 7 HOH 280  5285 280  HOH HOH A . 
G 7 HOH 281  5286 281  HOH HOH A . 
G 7 HOH 282  5287 282  HOH HOH A . 
G 7 HOH 283  5288 283  HOH HOH A . 
G 7 HOH 284  5289 284  HOH HOH A . 
G 7 HOH 285  5290 285  HOH HOH A . 
G 7 HOH 286  5291 286  HOH HOH A . 
G 7 HOH 287  5292 287  HOH HOH A . 
G 7 HOH 288  5293 288  HOH HOH A . 
G 7 HOH 289  5294 289  HOH HOH A . 
G 7 HOH 290  5295 290  HOH HOH A . 
G 7 HOH 291  5296 291  HOH HOH A . 
G 7 HOH 292  5297 292  HOH HOH A . 
G 7 HOH 293  5298 293  HOH HOH A . 
G 7 HOH 294  5299 294  HOH HOH A . 
G 7 HOH 295  5300 295  HOH HOH A . 
G 7 HOH 296  5301 296  HOH HOH A . 
G 7 HOH 297  5302 297  HOH HOH A . 
G 7 HOH 298  5303 298  HOH HOH A . 
G 7 HOH 299  5304 299  HOH HOH A . 
G 7 HOH 300  5305 300  HOH HOH A . 
G 7 HOH 301  5306 301  HOH HOH A . 
G 7 HOH 302  5307 302  HOH HOH A . 
G 7 HOH 303  5308 303  HOH HOH A . 
G 7 HOH 304  5309 304  HOH HOH A . 
G 7 HOH 305  5310 305  HOH HOH A . 
G 7 HOH 306  5311 306  HOH HOH A . 
G 7 HOH 307  5312 307  HOH HOH A . 
G 7 HOH 308  5313 308  HOH HOH A . 
G 7 HOH 309  5314 309  HOH HOH A . 
G 7 HOH 310  5315 310  HOH HOH A . 
G 7 HOH 311  5316 311  HOH HOH A . 
G 7 HOH 312  5317 312  HOH HOH A . 
G 7 HOH 313  5318 313  HOH HOH A . 
G 7 HOH 314  5319 314  HOH HOH A . 
G 7 HOH 315  5320 315  HOH HOH A . 
G 7 HOH 316  5321 316  HOH HOH A . 
G 7 HOH 317  5322 317  HOH HOH A . 
G 7 HOH 318  5323 318  HOH HOH A . 
G 7 HOH 319  5324 319  HOH HOH A . 
G 7 HOH 320  5325 320  HOH HOH A . 
G 7 HOH 321  5326 321  HOH HOH A . 
G 7 HOH 322  5327 322  HOH HOH A . 
G 7 HOH 323  5328 323  HOH HOH A . 
G 7 HOH 324  5329 324  HOH HOH A . 
G 7 HOH 325  5330 325  HOH HOH A . 
G 7 HOH 326  5331 326  HOH HOH A . 
G 7 HOH 327  5332 327  HOH HOH A . 
G 7 HOH 328  5333 328  HOH HOH A . 
G 7 HOH 329  5334 329  HOH HOH A . 
G 7 HOH 330  5335 330  HOH HOH A . 
G 7 HOH 331  5336 331  HOH HOH A . 
G 7 HOH 332  5337 332  HOH HOH A . 
G 7 HOH 333  5338 333  HOH HOH A . 
G 7 HOH 334  5339 334  HOH HOH A . 
G 7 HOH 335  5340 335  HOH HOH A . 
G 7 HOH 336  5341 336  HOH HOH A . 
G 7 HOH 337  5342 337  HOH HOH A . 
G 7 HOH 338  5343 338  HOH HOH A . 
G 7 HOH 339  5344 339  HOH HOH A . 
G 7 HOH 340  5345 340  HOH HOH A . 
G 7 HOH 341  5346 341  HOH HOH A . 
G 7 HOH 342  5347 342  HOH HOH A . 
G 7 HOH 343  5348 343  HOH HOH A . 
G 7 HOH 344  5349 344  HOH HOH A . 
G 7 HOH 345  5350 345  HOH HOH A . 
G 7 HOH 346  5351 346  HOH HOH A . 
G 7 HOH 347  5352 347  HOH HOH A . 
G 7 HOH 348  5353 348  HOH HOH A . 
G 7 HOH 349  5354 349  HOH HOH A . 
G 7 HOH 350  5355 350  HOH HOH A . 
G 7 HOH 351  5356 351  HOH HOH A . 
G 7 HOH 352  5357 352  HOH HOH A . 
G 7 HOH 353  5358 353  HOH HOH A . 
G 7 HOH 354  5359 354  HOH HOH A . 
G 7 HOH 355  5360 355  HOH HOH A . 
G 7 HOH 356  5361 356  HOH HOH A . 
G 7 HOH 357  5362 357  HOH HOH A . 
G 7 HOH 358  5363 358  HOH HOH A . 
G 7 HOH 359  5364 359  HOH HOH A . 
G 7 HOH 360  5365 360  HOH HOH A . 
G 7 HOH 361  5366 361  HOH HOH A . 
G 7 HOH 362  5367 362  HOH HOH A . 
G 7 HOH 363  5368 363  HOH HOH A . 
G 7 HOH 364  5369 364  HOH HOH A . 
G 7 HOH 365  5370 365  HOH HOH A . 
G 7 HOH 366  5371 366  HOH HOH A . 
G 7 HOH 367  5372 367  HOH HOH A . 
G 7 HOH 368  5373 368  HOH HOH A . 
G 7 HOH 369  5374 369  HOH HOH A . 
G 7 HOH 370  5375 370  HOH HOH A . 
G 7 HOH 371  5376 371  HOH HOH A . 
G 7 HOH 372  5377 372  HOH HOH A . 
G 7 HOH 373  5378 373  HOH HOH A . 
G 7 HOH 374  5379 374  HOH HOH A . 
G 7 HOH 375  5380 375  HOH HOH A . 
G 7 HOH 376  5381 376  HOH HOH A . 
G 7 HOH 377  5382 377  HOH HOH A . 
G 7 HOH 378  5383 378  HOH HOH A . 
G 7 HOH 379  5384 379  HOH HOH A . 
G 7 HOH 380  5385 380  HOH HOH A . 
G 7 HOH 381  5386 381  HOH HOH A . 
G 7 HOH 382  5387 382  HOH HOH A . 
G 7 HOH 383  5388 383  HOH HOH A . 
G 7 HOH 384  5389 384  HOH HOH A . 
G 7 HOH 385  5390 385  HOH HOH A . 
G 7 HOH 386  5391 386  HOH HOH A . 
G 7 HOH 387  5392 387  HOH HOH A . 
G 7 HOH 388  5393 388  HOH HOH A . 
G 7 HOH 389  5394 389  HOH HOH A . 
G 7 HOH 390  5395 390  HOH HOH A . 
G 7 HOH 391  5396 391  HOH HOH A . 
G 7 HOH 392  5397 392  HOH HOH A . 
G 7 HOH 393  5398 393  HOH HOH A . 
G 7 HOH 394  5399 394  HOH HOH A . 
G 7 HOH 395  5400 395  HOH HOH A . 
G 7 HOH 396  5401 396  HOH HOH A . 
G 7 HOH 397  5402 397  HOH HOH A . 
G 7 HOH 398  5403 398  HOH HOH A . 
G 7 HOH 399  5404 399  HOH HOH A . 
G 7 HOH 400  5405 400  HOH HOH A . 
G 7 HOH 401  5406 401  HOH HOH A . 
G 7 HOH 402  5407 402  HOH HOH A . 
G 7 HOH 403  5408 403  HOH HOH A . 
G 7 HOH 404  5409 404  HOH HOH A . 
G 7 HOH 405  5410 405  HOH HOH A . 
G 7 HOH 406  5411 406  HOH HOH A . 
G 7 HOH 407  5412 407  HOH HOH A . 
G 7 HOH 408  5413 408  HOH HOH A . 
G 7 HOH 409  5414 409  HOH HOH A . 
G 7 HOH 410  5415 410  HOH HOH A . 
G 7 HOH 411  5416 411  HOH HOH A . 
G 7 HOH 412  5417 412  HOH HOH A . 
G 7 HOH 413  5418 413  HOH HOH A . 
G 7 HOH 414  5419 414  HOH HOH A . 
G 7 HOH 415  5420 415  HOH HOH A . 
G 7 HOH 416  5421 416  HOH HOH A . 
G 7 HOH 417  5422 417  HOH HOH A . 
G 7 HOH 418  5423 418  HOH HOH A . 
G 7 HOH 419  5424 419  HOH HOH A . 
G 7 HOH 420  5425 420  HOH HOH A . 
G 7 HOH 421  5426 421  HOH HOH A . 
G 7 HOH 422  5427 422  HOH HOH A . 
G 7 HOH 423  5428 423  HOH HOH A . 
G 7 HOH 424  5429 424  HOH HOH A . 
G 7 HOH 425  5430 425  HOH HOH A . 
G 7 HOH 426  5431 426  HOH HOH A . 
G 7 HOH 427  5432 427  HOH HOH A . 
G 7 HOH 428  5433 428  HOH HOH A . 
G 7 HOH 429  5434 429  HOH HOH A . 
G 7 HOH 430  5435 430  HOH HOH A . 
G 7 HOH 431  5436 431  HOH HOH A . 
G 7 HOH 432  5437 432  HOH HOH A . 
G 7 HOH 433  5438 433  HOH HOH A . 
G 7 HOH 434  5439 434  HOH HOH A . 
G 7 HOH 435  5440 435  HOH HOH A . 
G 7 HOH 436  5441 436  HOH HOH A . 
G 7 HOH 437  5442 437  HOH HOH A . 
G 7 HOH 438  5443 438  HOH HOH A . 
G 7 HOH 439  5444 439  HOH HOH A . 
G 7 HOH 440  5445 440  HOH HOH A . 
G 7 HOH 441  5446 441  HOH HOH A . 
G 7 HOH 442  5447 442  HOH HOH A . 
G 7 HOH 443  5448 443  HOH HOH A . 
G 7 HOH 444  5449 444  HOH HOH A . 
G 7 HOH 445  5450 445  HOH HOH A . 
G 7 HOH 446  5451 446  HOH HOH A . 
G 7 HOH 447  5452 447  HOH HOH A . 
G 7 HOH 448  5453 448  HOH HOH A . 
G 7 HOH 449  5454 449  HOH HOH A . 
G 7 HOH 450  5455 450  HOH HOH A . 
G 7 HOH 451  5456 451  HOH HOH A . 
G 7 HOH 452  5457 452  HOH HOH A . 
G 7 HOH 453  5458 453  HOH HOH A . 
G 7 HOH 454  5459 454  HOH HOH A . 
G 7 HOH 455  5460 455  HOH HOH A . 
G 7 HOH 456  5461 456  HOH HOH A . 
G 7 HOH 457  5462 457  HOH HOH A . 
G 7 HOH 458  5463 458  HOH HOH A . 
G 7 HOH 459  5464 459  HOH HOH A . 
G 7 HOH 460  5465 460  HOH HOH A . 
G 7 HOH 461  5466 461  HOH HOH A . 
G 7 HOH 462  5467 462  HOH HOH A . 
G 7 HOH 463  5468 463  HOH HOH A . 
G 7 HOH 464  5469 464  HOH HOH A . 
G 7 HOH 465  5470 465  HOH HOH A . 
G 7 HOH 466  5471 466  HOH HOH A . 
G 7 HOH 467  5472 467  HOH HOH A . 
G 7 HOH 468  5473 468  HOH HOH A . 
G 7 HOH 469  5474 469  HOH HOH A . 
G 7 HOH 470  5475 470  HOH HOH A . 
G 7 HOH 471  5476 471  HOH HOH A . 
G 7 HOH 472  5477 472  HOH HOH A . 
G 7 HOH 473  5478 473  HOH HOH A . 
G 7 HOH 474  5479 474  HOH HOH A . 
G 7 HOH 475  5480 475  HOH HOH A . 
G 7 HOH 476  5481 476  HOH HOH A . 
G 7 HOH 477  5482 477  HOH HOH A . 
G 7 HOH 478  5483 478  HOH HOH A . 
G 7 HOH 479  5484 479  HOH HOH A . 
G 7 HOH 480  5485 480  HOH HOH A . 
G 7 HOH 481  5486 481  HOH HOH A . 
G 7 HOH 482  5487 482  HOH HOH A . 
G 7 HOH 483  5488 483  HOH HOH A . 
G 7 HOH 484  5489 484  HOH HOH A . 
G 7 HOH 485  5490 485  HOH HOH A . 
G 7 HOH 486  5491 486  HOH HOH A . 
G 7 HOH 487  5492 487  HOH HOH A . 
G 7 HOH 488  5493 488  HOH HOH A . 
G 7 HOH 489  5494 489  HOH HOH A . 
G 7 HOH 490  5495 490  HOH HOH A . 
G 7 HOH 491  5496 491  HOH HOH A . 
G 7 HOH 492  5497 492  HOH HOH A . 
G 7 HOH 493  5498 493  HOH HOH A . 
G 7 HOH 494  5499 494  HOH HOH A . 
G 7 HOH 495  5500 495  HOH HOH A . 
G 7 HOH 496  5501 496  HOH HOH A . 
G 7 HOH 497  5502 497  HOH HOH A . 
G 7 HOH 498  5503 498  HOH HOH A . 
G 7 HOH 499  5504 499  HOH HOH A . 
G 7 HOH 500  5505 500  HOH HOH A . 
G 7 HOH 501  5506 501  HOH HOH A . 
G 7 HOH 502  5507 502  HOH HOH A . 
G 7 HOH 503  5508 503  HOH HOH A . 
G 7 HOH 504  5509 504  HOH HOH A . 
G 7 HOH 505  5510 505  HOH HOH A . 
G 7 HOH 506  5511 506  HOH HOH A . 
G 7 HOH 507  5512 507  HOH HOH A . 
G 7 HOH 508  5513 508  HOH HOH A . 
G 7 HOH 509  5514 509  HOH HOH A . 
G 7 HOH 510  5515 510  HOH HOH A . 
G 7 HOH 511  5516 511  HOH HOH A . 
G 7 HOH 512  5517 512  HOH HOH A . 
G 7 HOH 513  5518 513  HOH HOH A . 
G 7 HOH 514  5519 514  HOH HOH A . 
G 7 HOH 515  5520 515  HOH HOH A . 
G 7 HOH 516  5521 516  HOH HOH A . 
G 7 HOH 517  5522 517  HOH HOH A . 
G 7 HOH 518  5523 518  HOH HOH A . 
G 7 HOH 519  5524 519  HOH HOH A . 
G 7 HOH 520  5525 520  HOH HOH A . 
G 7 HOH 521  5526 521  HOH HOH A . 
G 7 HOH 522  5527 522  HOH HOH A . 
G 7 HOH 523  5528 523  HOH HOH A . 
G 7 HOH 524  5529 524  HOH HOH A . 
G 7 HOH 525  5530 525  HOH HOH A . 
G 7 HOH 526  5531 526  HOH HOH A . 
G 7 HOH 527  5532 527  HOH HOH A . 
G 7 HOH 528  5533 528  HOH HOH A . 
G 7 HOH 529  5534 529  HOH HOH A . 
G 7 HOH 530  5535 530  HOH HOH A . 
G 7 HOH 531  5536 531  HOH HOH A . 
G 7 HOH 532  5537 532  HOH HOH A . 
G 7 HOH 533  5538 533  HOH HOH A . 
G 7 HOH 534  5539 534  HOH HOH A . 
G 7 HOH 535  5540 535  HOH HOH A . 
G 7 HOH 536  5541 536  HOH HOH A . 
G 7 HOH 537  5542 537  HOH HOH A . 
G 7 HOH 538  5543 538  HOH HOH A . 
G 7 HOH 539  5544 539  HOH HOH A . 
G 7 HOH 540  5545 540  HOH HOH A . 
G 7 HOH 541  5546 541  HOH HOH A . 
G 7 HOH 542  5547 542  HOH HOH A . 
G 7 HOH 543  5548 543  HOH HOH A . 
G 7 HOH 544  5549 544  HOH HOH A . 
G 7 HOH 545  5550 545  HOH HOH A . 
G 7 HOH 546  5551 546  HOH HOH A . 
G 7 HOH 547  5552 547  HOH HOH A . 
G 7 HOH 548  5553 548  HOH HOH A . 
G 7 HOH 549  5554 549  HOH HOH A . 
G 7 HOH 550  5555 550  HOH HOH A . 
G 7 HOH 551  5556 551  HOH HOH A . 
G 7 HOH 552  5557 552  HOH HOH A . 
G 7 HOH 553  5558 553  HOH HOH A . 
G 7 HOH 554  5559 554  HOH HOH A . 
G 7 HOH 555  5560 555  HOH HOH A . 
G 7 HOH 556  5561 556  HOH HOH A . 
G 7 HOH 557  5562 557  HOH HOH A . 
G 7 HOH 558  5563 558  HOH HOH A . 
G 7 HOH 559  5564 559  HOH HOH A . 
G 7 HOH 560  5565 560  HOH HOH A . 
G 7 HOH 561  5566 561  HOH HOH A . 
G 7 HOH 562  5567 562  HOH HOH A . 
G 7 HOH 563  5568 563  HOH HOH A . 
G 7 HOH 564  5569 564  HOH HOH A . 
G 7 HOH 565  5570 565  HOH HOH A . 
G 7 HOH 566  5571 566  HOH HOH A . 
G 7 HOH 567  5572 567  HOH HOH A . 
G 7 HOH 568  5573 568  HOH HOH A . 
G 7 HOH 569  5574 569  HOH HOH A . 
G 7 HOH 570  5575 570  HOH HOH A . 
G 7 HOH 571  5576 571  HOH HOH A . 
G 7 HOH 572  5577 572  HOH HOH A . 
G 7 HOH 573  5578 573  HOH HOH A . 
G 7 HOH 574  5579 574  HOH HOH A . 
G 7 HOH 575  5580 575  HOH HOH A . 
G 7 HOH 576  5581 576  HOH HOH A . 
G 7 HOH 577  5582 577  HOH HOH A . 
G 7 HOH 578  5583 578  HOH HOH A . 
G 7 HOH 579  5584 579  HOH HOH A . 
G 7 HOH 580  5585 580  HOH HOH A . 
G 7 HOH 581  5586 581  HOH HOH A . 
G 7 HOH 582  5587 582  HOH HOH A . 
G 7 HOH 583  5588 583  HOH HOH A . 
G 7 HOH 584  5589 584  HOH HOH A . 
G 7 HOH 585  5590 585  HOH HOH A . 
G 7 HOH 586  5591 586  HOH HOH A . 
G 7 HOH 587  5592 587  HOH HOH A . 
G 7 HOH 588  5593 588  HOH HOH A . 
G 7 HOH 589  5594 589  HOH HOH A . 
G 7 HOH 590  5595 590  HOH HOH A . 
G 7 HOH 591  5596 591  HOH HOH A . 
G 7 HOH 592  5597 592  HOH HOH A . 
G 7 HOH 593  5598 593  HOH HOH A . 
G 7 HOH 594  5599 594  HOH HOH A . 
G 7 HOH 595  5600 595  HOH HOH A . 
G 7 HOH 596  5601 596  HOH HOH A . 
G 7 HOH 597  5602 597  HOH HOH A . 
G 7 HOH 598  5603 598  HOH HOH A . 
G 7 HOH 599  5604 599  HOH HOH A . 
G 7 HOH 600  5605 600  HOH HOH A . 
G 7 HOH 601  5606 601  HOH HOH A . 
G 7 HOH 602  5607 602  HOH HOH A . 
G 7 HOH 603  5608 603  HOH HOH A . 
G 7 HOH 604  5609 604  HOH HOH A . 
G 7 HOH 605  5610 605  HOH HOH A . 
G 7 HOH 606  5611 606  HOH HOH A . 
G 7 HOH 607  5612 607  HOH HOH A . 
G 7 HOH 608  5613 608  HOH HOH A . 
G 7 HOH 609  5614 609  HOH HOH A . 
G 7 HOH 610  5615 610  HOH HOH A . 
G 7 HOH 611  5616 611  HOH HOH A . 
G 7 HOH 612  5617 612  HOH HOH A . 
G 7 HOH 613  5618 613  HOH HOH A . 
G 7 HOH 614  5619 614  HOH HOH A . 
G 7 HOH 615  5620 615  HOH HOH A . 
G 7 HOH 616  5621 616  HOH HOH A . 
G 7 HOH 617  5622 617  HOH HOH A . 
G 7 HOH 618  5623 618  HOH HOH A . 
G 7 HOH 619  5624 619  HOH HOH A . 
G 7 HOH 620  5625 620  HOH HOH A . 
G 7 HOH 621  5626 621  HOH HOH A . 
G 7 HOH 622  5627 622  HOH HOH A . 
G 7 HOH 623  5628 623  HOH HOH A . 
G 7 HOH 624  5629 624  HOH HOH A . 
G 7 HOH 625  5630 625  HOH HOH A . 
G 7 HOH 626  5631 626  HOH HOH A . 
G 7 HOH 627  5632 627  HOH HOH A . 
G 7 HOH 628  5633 628  HOH HOH A . 
G 7 HOH 629  5634 629  HOH HOH A . 
G 7 HOH 630  5635 630  HOH HOH A . 
G 7 HOH 631  5636 631  HOH HOH A . 
G 7 HOH 632  5637 632  HOH HOH A . 
G 7 HOH 633  5638 633  HOH HOH A . 
G 7 HOH 634  5639 634  HOH HOH A . 
G 7 HOH 635  5640 635  HOH HOH A . 
G 7 HOH 636  5641 636  HOH HOH A . 
G 7 HOH 637  5642 637  HOH HOH A . 
G 7 HOH 638  5643 638  HOH HOH A . 
G 7 HOH 639  5644 639  HOH HOH A . 
G 7 HOH 640  5645 640  HOH HOH A . 
G 7 HOH 641  5646 641  HOH HOH A . 
G 7 HOH 642  5647 642  HOH HOH A . 
G 7 HOH 643  5648 643  HOH HOH A . 
G 7 HOH 644  5649 644  HOH HOH A . 
G 7 HOH 645  5650 645  HOH HOH A . 
G 7 HOH 646  5651 646  HOH HOH A . 
G 7 HOH 647  5652 647  HOH HOH A . 
G 7 HOH 648  5653 648  HOH HOH A . 
G 7 HOH 649  5654 649  HOH HOH A . 
G 7 HOH 650  5655 650  HOH HOH A . 
G 7 HOH 651  5656 651  HOH HOH A . 
G 7 HOH 652  5657 652  HOH HOH A . 
G 7 HOH 653  5658 653  HOH HOH A . 
G 7 HOH 654  5659 654  HOH HOH A . 
G 7 HOH 655  5660 655  HOH HOH A . 
G 7 HOH 656  5661 656  HOH HOH A . 
G 7 HOH 657  5662 657  HOH HOH A . 
G 7 HOH 658  5663 658  HOH HOH A . 
G 7 HOH 659  5664 659  HOH HOH A . 
G 7 HOH 660  5665 660  HOH HOH A . 
G 7 HOH 661  5666 661  HOH HOH A . 
G 7 HOH 662  5667 662  HOH HOH A . 
G 7 HOH 663  5668 663  HOH HOH A . 
G 7 HOH 664  5669 664  HOH HOH A . 
G 7 HOH 665  5670 665  HOH HOH A . 
G 7 HOH 666  5671 666  HOH HOH A . 
G 7 HOH 667  5672 667  HOH HOH A . 
G 7 HOH 668  5673 668  HOH HOH A . 
G 7 HOH 669  5674 669  HOH HOH A . 
G 7 HOH 670  5675 670  HOH HOH A . 
G 7 HOH 671  5676 671  HOH HOH A . 
G 7 HOH 672  5677 672  HOH HOH A . 
G 7 HOH 673  5678 673  HOH HOH A . 
G 7 HOH 674  5679 674  HOH HOH A . 
G 7 HOH 675  5680 675  HOH HOH A . 
G 7 HOH 676  5681 676  HOH HOH A . 
G 7 HOH 677  5682 677  HOH HOH A . 
G 7 HOH 678  5683 678  HOH HOH A . 
G 7 HOH 679  5684 679  HOH HOH A . 
G 7 HOH 680  5685 680  HOH HOH A . 
G 7 HOH 681  5686 681  HOH HOH A . 
G 7 HOH 682  5687 682  HOH HOH A . 
G 7 HOH 683  5688 683  HOH HOH A . 
G 7 HOH 684  5689 684  HOH HOH A . 
G 7 HOH 685  5690 685  HOH HOH A . 
G 7 HOH 686  5691 686  HOH HOH A . 
G 7 HOH 687  5692 687  HOH HOH A . 
G 7 HOH 688  5693 688  HOH HOH A . 
G 7 HOH 689  5694 689  HOH HOH A . 
G 7 HOH 690  5695 690  HOH HOH A . 
G 7 HOH 691  5696 691  HOH HOH A . 
G 7 HOH 692  5697 692  HOH HOH A . 
G 7 HOH 693  5698 693  HOH HOH A . 
G 7 HOH 694  5699 694  HOH HOH A . 
G 7 HOH 695  5700 695  HOH HOH A . 
G 7 HOH 696  5701 696  HOH HOH A . 
G 7 HOH 697  5702 697  HOH HOH A . 
G 7 HOH 698  5703 698  HOH HOH A . 
G 7 HOH 699  5704 699  HOH HOH A . 
G 7 HOH 700  5705 700  HOH HOH A . 
G 7 HOH 701  5706 701  HOH HOH A . 
G 7 HOH 702  5707 702  HOH HOH A . 
G 7 HOH 703  5708 703  HOH HOH A . 
G 7 HOH 704  5709 704  HOH HOH A . 
G 7 HOH 705  5710 705  HOH HOH A . 
G 7 HOH 706  5711 706  HOH HOH A . 
G 7 HOH 707  5712 707  HOH HOH A . 
G 7 HOH 708  5713 708  HOH HOH A . 
G 7 HOH 709  5714 709  HOH HOH A . 
G 7 HOH 710  5715 710  HOH HOH A . 
G 7 HOH 711  5716 711  HOH HOH A . 
G 7 HOH 712  5717 712  HOH HOH A . 
G 7 HOH 713  5718 713  HOH HOH A . 
G 7 HOH 714  5719 714  HOH HOH A . 
G 7 HOH 715  5720 715  HOH HOH A . 
G 7 HOH 716  5721 716  HOH HOH A . 
G 7 HOH 717  5722 717  HOH HOH A . 
G 7 HOH 718  5723 718  HOH HOH A . 
G 7 HOH 719  5724 719  HOH HOH A . 
G 7 HOH 720  5725 720  HOH HOH A . 
G 7 HOH 721  5726 721  HOH HOH A . 
G 7 HOH 722  5727 722  HOH HOH A . 
G 7 HOH 723  5728 723  HOH HOH A . 
G 7 HOH 724  5729 724  HOH HOH A . 
G 7 HOH 725  5730 725  HOH HOH A . 
G 7 HOH 726  5731 726  HOH HOH A . 
G 7 HOH 727  5732 727  HOH HOH A . 
G 7 HOH 728  5733 728  HOH HOH A . 
G 7 HOH 729  5734 729  HOH HOH A . 
G 7 HOH 730  5735 730  HOH HOH A . 
G 7 HOH 731  5736 731  HOH HOH A . 
G 7 HOH 732  5737 732  HOH HOH A . 
G 7 HOH 733  5738 733  HOH HOH A . 
G 7 HOH 734  5739 734  HOH HOH A . 
G 7 HOH 735  5740 735  HOH HOH A . 
G 7 HOH 736  5741 736  HOH HOH A . 
G 7 HOH 737  5742 737  HOH HOH A . 
G 7 HOH 738  5743 738  HOH HOH A . 
G 7 HOH 739  5744 739  HOH HOH A . 
G 7 HOH 740  5745 740  HOH HOH A . 
G 7 HOH 741  5746 741  HOH HOH A . 
G 7 HOH 742  5747 742  HOH HOH A . 
G 7 HOH 743  5748 743  HOH HOH A . 
G 7 HOH 744  5749 744  HOH HOH A . 
G 7 HOH 745  5750 745  HOH HOH A . 
G 7 HOH 746  5751 746  HOH HOH A . 
G 7 HOH 747  5752 747  HOH HOH A . 
G 7 HOH 748  5753 748  HOH HOH A . 
G 7 HOH 749  5754 749  HOH HOH A . 
G 7 HOH 750  5755 750  HOH HOH A . 
G 7 HOH 751  5756 751  HOH HOH A . 
G 7 HOH 752  5757 752  HOH HOH A . 
G 7 HOH 753  5758 753  HOH HOH A . 
G 7 HOH 754  5759 754  HOH HOH A . 
G 7 HOH 755  5760 755  HOH HOH A . 
G 7 HOH 756  5761 756  HOH HOH A . 
G 7 HOH 757  5762 757  HOH HOH A . 
G 7 HOH 758  5763 758  HOH HOH A . 
G 7 HOH 759  5764 759  HOH HOH A . 
G 7 HOH 760  5765 760  HOH HOH A . 
G 7 HOH 761  5766 761  HOH HOH A . 
G 7 HOH 762  5767 762  HOH HOH A . 
G 7 HOH 763  5768 763  HOH HOH A . 
G 7 HOH 764  5769 764  HOH HOH A . 
G 7 HOH 765  5770 765  HOH HOH A . 
G 7 HOH 766  5771 766  HOH HOH A . 
G 7 HOH 767  5772 767  HOH HOH A . 
G 7 HOH 768  5773 768  HOH HOH A . 
G 7 HOH 769  5774 769  HOH HOH A . 
G 7 HOH 770  5775 770  HOH HOH A . 
G 7 HOH 771  5776 771  HOH HOH A . 
G 7 HOH 772  5777 772  HOH HOH A . 
G 7 HOH 773  5778 773  HOH HOH A . 
G 7 HOH 774  5779 774  HOH HOH A . 
G 7 HOH 775  5780 775  HOH HOH A . 
G 7 HOH 776  5781 776  HOH HOH A . 
G 7 HOH 777  5782 777  HOH HOH A . 
G 7 HOH 778  5783 778  HOH HOH A . 
G 7 HOH 779  5784 779  HOH HOH A . 
G 7 HOH 780  5785 780  HOH HOH A . 
G 7 HOH 781  5786 781  HOH HOH A . 
G 7 HOH 782  5787 782  HOH HOH A . 
G 7 HOH 783  5788 783  HOH HOH A . 
G 7 HOH 784  5789 784  HOH HOH A . 
G 7 HOH 785  5790 785  HOH HOH A . 
G 7 HOH 786  5791 786  HOH HOH A . 
G 7 HOH 787  5792 787  HOH HOH A . 
G 7 HOH 788  5793 788  HOH HOH A . 
G 7 HOH 789  5794 789  HOH HOH A . 
G 7 HOH 790  5795 790  HOH HOH A . 
G 7 HOH 791  5796 791  HOH HOH A . 
G 7 HOH 792  5797 792  HOH HOH A . 
G 7 HOH 793  5798 793  HOH HOH A . 
G 7 HOH 794  5799 794  HOH HOH A . 
G 7 HOH 795  5800 795  HOH HOH A . 
G 7 HOH 796  5801 796  HOH HOH A . 
G 7 HOH 797  5802 797  HOH HOH A . 
G 7 HOH 798  5803 798  HOH HOH A . 
G 7 HOH 799  5804 799  HOH HOH A . 
G 7 HOH 800  5805 800  HOH HOH A . 
G 7 HOH 801  5806 801  HOH HOH A . 
G 7 HOH 802  5807 802  HOH HOH A . 
G 7 HOH 803  5808 803  HOH HOH A . 
G 7 HOH 804  5809 804  HOH HOH A . 
G 7 HOH 805  5810 805  HOH HOH A . 
G 7 HOH 806  5811 806  HOH HOH A . 
G 7 HOH 807  5812 807  HOH HOH A . 
G 7 HOH 808  5813 808  HOH HOH A . 
G 7 HOH 809  5814 809  HOH HOH A . 
G 7 HOH 810  5815 810  HOH HOH A . 
G 7 HOH 811  5816 811  HOH HOH A . 
G 7 HOH 812  5817 812  HOH HOH A . 
G 7 HOH 813  5818 813  HOH HOH A . 
G 7 HOH 814  5819 814  HOH HOH A . 
G 7 HOH 815  5820 815  HOH HOH A . 
G 7 HOH 816  5821 816  HOH HOH A . 
G 7 HOH 817  5822 817  HOH HOH A . 
G 7 HOH 818  5823 818  HOH HOH A . 
G 7 HOH 819  5824 819  HOH HOH A . 
G 7 HOH 820  5825 820  HOH HOH A . 
G 7 HOH 821  5826 821  HOH HOH A . 
G 7 HOH 822  5827 822  HOH HOH A . 
G 7 HOH 823  5828 823  HOH HOH A . 
G 7 HOH 824  5829 824  HOH HOH A . 
G 7 HOH 825  5830 825  HOH HOH A . 
G 7 HOH 826  5831 826  HOH HOH A . 
G 7 HOH 827  5832 827  HOH HOH A . 
G 7 HOH 828  5833 828  HOH HOH A . 
G 7 HOH 829  5834 829  HOH HOH A . 
G 7 HOH 830  5835 830  HOH HOH A . 
G 7 HOH 831  5836 831  HOH HOH A . 
G 7 HOH 832  5837 832  HOH HOH A . 
G 7 HOH 833  5838 833  HOH HOH A . 
G 7 HOH 834  5839 834  HOH HOH A . 
G 7 HOH 835  5840 835  HOH HOH A . 
G 7 HOH 836  5841 836  HOH HOH A . 
G 7 HOH 837  5842 837  HOH HOH A . 
G 7 HOH 838  5843 838  HOH HOH A . 
G 7 HOH 839  5844 839  HOH HOH A . 
G 7 HOH 840  5845 840  HOH HOH A . 
G 7 HOH 841  5846 841  HOH HOH A . 
G 7 HOH 842  5847 842  HOH HOH A . 
G 7 HOH 843  5848 843  HOH HOH A . 
G 7 HOH 844  5849 844  HOH HOH A . 
G 7 HOH 845  5850 845  HOH HOH A . 
G 7 HOH 846  5851 846  HOH HOH A . 
G 7 HOH 847  5852 847  HOH HOH A . 
G 7 HOH 848  5853 848  HOH HOH A . 
G 7 HOH 849  5854 849  HOH HOH A . 
G 7 HOH 850  5855 850  HOH HOH A . 
G 7 HOH 851  5856 851  HOH HOH A . 
G 7 HOH 852  5857 852  HOH HOH A . 
G 7 HOH 853  5858 853  HOH HOH A . 
G 7 HOH 854  5859 854  HOH HOH A . 
G 7 HOH 855  5860 855  HOH HOH A . 
G 7 HOH 856  5861 856  HOH HOH A . 
G 7 HOH 857  5862 857  HOH HOH A . 
G 7 HOH 858  5863 858  HOH HOH A . 
G 7 HOH 859  5864 859  HOH HOH A . 
G 7 HOH 860  5865 860  HOH HOH A . 
G 7 HOH 861  5866 861  HOH HOH A . 
G 7 HOH 862  5867 862  HOH HOH A . 
G 7 HOH 863  5868 863  HOH HOH A . 
G 7 HOH 864  5869 864  HOH HOH A . 
G 7 HOH 865  5870 865  HOH HOH A . 
G 7 HOH 866  5871 866  HOH HOH A . 
G 7 HOH 867  5872 867  HOH HOH A . 
G 7 HOH 868  5873 868  HOH HOH A . 
G 7 HOH 869  5874 869  HOH HOH A . 
G 7 HOH 870  5875 870  HOH HOH A . 
G 7 HOH 871  5876 871  HOH HOH A . 
G 7 HOH 872  5877 872  HOH HOH A . 
G 7 HOH 873  5878 873  HOH HOH A . 
G 7 HOH 874  5879 874  HOH HOH A . 
G 7 HOH 875  5880 875  HOH HOH A . 
G 7 HOH 876  5881 876  HOH HOH A . 
G 7 HOH 877  5882 877  HOH HOH A . 
G 7 HOH 878  5883 878  HOH HOH A . 
G 7 HOH 879  5884 879  HOH HOH A . 
G 7 HOH 880  5885 880  HOH HOH A . 
G 7 HOH 881  5886 881  HOH HOH A . 
G 7 HOH 882  5887 882  HOH HOH A . 
G 7 HOH 883  5888 883  HOH HOH A . 
G 7 HOH 884  5889 884  HOH HOH A . 
G 7 HOH 885  5890 885  HOH HOH A . 
G 7 HOH 886  5891 886  HOH HOH A . 
G 7 HOH 887  5892 887  HOH HOH A . 
G 7 HOH 888  5893 888  HOH HOH A . 
G 7 HOH 889  5894 889  HOH HOH A . 
G 7 HOH 890  5895 890  HOH HOH A . 
G 7 HOH 891  5896 891  HOH HOH A . 
G 7 HOH 892  5897 892  HOH HOH A . 
G 7 HOH 893  5898 893  HOH HOH A . 
G 7 HOH 894  5899 894  HOH HOH A . 
G 7 HOH 895  5900 895  HOH HOH A . 
G 7 HOH 896  5901 896  HOH HOH A . 
G 7 HOH 897  5902 897  HOH HOH A . 
G 7 HOH 898  5903 898  HOH HOH A . 
G 7 HOH 899  5904 899  HOH HOH A . 
G 7 HOH 900  5905 900  HOH HOH A . 
G 7 HOH 901  5906 901  HOH HOH A . 
G 7 HOH 902  5907 902  HOH HOH A . 
G 7 HOH 903  5908 903  HOH HOH A . 
G 7 HOH 904  5909 904  HOH HOH A . 
G 7 HOH 905  5910 905  HOH HOH A . 
G 7 HOH 906  5911 906  HOH HOH A . 
G 7 HOH 907  5912 907  HOH HOH A . 
G 7 HOH 908  5913 908  HOH HOH A . 
G 7 HOH 909  5914 909  HOH HOH A . 
G 7 HOH 910  5915 910  HOH HOH A . 
G 7 HOH 911  5916 911  HOH HOH A . 
G 7 HOH 912  5917 912  HOH HOH A . 
G 7 HOH 913  5918 913  HOH HOH A . 
G 7 HOH 914  5919 914  HOH HOH A . 
G 7 HOH 915  5920 915  HOH HOH A . 
G 7 HOH 916  5921 916  HOH HOH A . 
G 7 HOH 917  5922 917  HOH HOH A . 
G 7 HOH 918  5923 918  HOH HOH A . 
G 7 HOH 919  5924 919  HOH HOH A . 
G 7 HOH 920  5925 920  HOH HOH A . 
G 7 HOH 921  5926 921  HOH HOH A . 
G 7 HOH 922  5927 922  HOH HOH A . 
G 7 HOH 923  5928 923  HOH HOH A . 
G 7 HOH 924  5929 924  HOH HOH A . 
G 7 HOH 925  5930 925  HOH HOH A . 
G 7 HOH 926  5931 926  HOH HOH A . 
G 7 HOH 927  5932 927  HOH HOH A . 
G 7 HOH 928  5933 928  HOH HOH A . 
G 7 HOH 929  5934 929  HOH HOH A . 
G 7 HOH 930  5935 930  HOH HOH A . 
G 7 HOH 931  5936 931  HOH HOH A . 
G 7 HOH 932  5937 932  HOH HOH A . 
G 7 HOH 933  5938 933  HOH HOH A . 
G 7 HOH 934  5939 934  HOH HOH A . 
G 7 HOH 935  5940 935  HOH HOH A . 
G 7 HOH 936  5941 936  HOH HOH A . 
G 7 HOH 937  5942 937  HOH HOH A . 
G 7 HOH 938  5943 938  HOH HOH A . 
G 7 HOH 939  5944 939  HOH HOH A . 
G 7 HOH 940  5945 940  HOH HOH A . 
G 7 HOH 941  5946 941  HOH HOH A . 
G 7 HOH 942  5947 942  HOH HOH A . 
G 7 HOH 943  5948 943  HOH HOH A . 
G 7 HOH 944  5949 944  HOH HOH A . 
G 7 HOH 945  5950 945  HOH HOH A . 
G 7 HOH 946  5951 946  HOH HOH A . 
G 7 HOH 947  5952 947  HOH HOH A . 
G 7 HOH 948  5953 948  HOH HOH A . 
G 7 HOH 949  5954 949  HOH HOH A . 
G 7 HOH 950  5955 950  HOH HOH A . 
G 7 HOH 951  5956 951  HOH HOH A . 
G 7 HOH 952  5957 952  HOH HOH A . 
G 7 HOH 953  5958 953  HOH HOH A . 
G 7 HOH 954  5959 954  HOH HOH A . 
G 7 HOH 955  5960 955  HOH HOH A . 
G 7 HOH 956  5961 956  HOH HOH A . 
G 7 HOH 957  5962 957  HOH HOH A . 
G 7 HOH 958  5963 958  HOH HOH A . 
G 7 HOH 959  5964 959  HOH HOH A . 
G 7 HOH 960  5965 960  HOH HOH A . 
G 7 HOH 961  5966 961  HOH HOH A . 
G 7 HOH 962  5967 962  HOH HOH A . 
G 7 HOH 963  5968 963  HOH HOH A . 
G 7 HOH 964  5969 964  HOH HOH A . 
G 7 HOH 965  5970 965  HOH HOH A . 
G 7 HOH 966  5971 966  HOH HOH A . 
G 7 HOH 967  5972 967  HOH HOH A . 
G 7 HOH 968  5973 968  HOH HOH A . 
G 7 HOH 969  5974 969  HOH HOH A . 
G 7 HOH 970  5975 970  HOH HOH A . 
G 7 HOH 971  5976 971  HOH HOH A . 
G 7 HOH 972  5977 972  HOH HOH A . 
G 7 HOH 973  5978 973  HOH HOH A . 
G 7 HOH 974  5979 974  HOH HOH A . 
G 7 HOH 975  5980 975  HOH HOH A . 
G 7 HOH 976  5981 976  HOH HOH A . 
G 7 HOH 977  5982 977  HOH HOH A . 
G 7 HOH 978  5983 978  HOH HOH A . 
G 7 HOH 979  5984 979  HOH HOH A . 
G 7 HOH 980  5985 980  HOH HOH A . 
G 7 HOH 981  5986 981  HOH HOH A . 
G 7 HOH 982  5987 982  HOH HOH A . 
G 7 HOH 983  5988 983  HOH HOH A . 
G 7 HOH 984  5989 984  HOH HOH A . 
G 7 HOH 985  5990 985  HOH HOH A . 
G 7 HOH 986  5991 986  HOH HOH A . 
G 7 HOH 987  5992 987  HOH HOH A . 
G 7 HOH 988  5993 988  HOH HOH A . 
G 7 HOH 989  5994 989  HOH HOH A . 
G 7 HOH 990  5995 990  HOH HOH A . 
G 7 HOH 991  5996 991  HOH HOH A . 
G 7 HOH 992  5997 992  HOH HOH A . 
G 7 HOH 993  5998 993  HOH HOH A . 
G 7 HOH 994  5999 994  HOH HOH A . 
G 7 HOH 995  6000 995  HOH HOH A . 
G 7 HOH 996  6001 996  HOH HOH A . 
G 7 HOH 997  6002 997  HOH HOH A . 
G 7 HOH 998  6003 998  HOH HOH A . 
G 7 HOH 999  6004 999  HOH HOH A . 
G 7 HOH 1000 6005 1000 HOH HOH A . 
G 7 HOH 1001 6006 1001 HOH HOH A . 
G 7 HOH 1002 6007 1002 HOH HOH A . 
G 7 HOH 1003 6008 1003 HOH HOH A . 
G 7 HOH 1004 6009 1004 HOH HOH A . 
G 7 HOH 1005 6010 1005 HOH HOH A . 
G 7 HOH 1006 6011 1006 HOH HOH A . 
G 7 HOH 1007 6012 1007 HOH HOH A . 
G 7 HOH 1008 6013 1008 HOH HOH A . 
G 7 HOH 1009 6014 1009 HOH HOH A . 
G 7 HOH 1010 6015 1010 HOH HOH A . 
G 7 HOH 1011 6016 1011 HOH HOH A . 
G 7 HOH 1012 6017 1012 HOH HOH A . 
G 7 HOH 1013 6018 1013 HOH HOH A . 
G 7 HOH 1014 6019 1014 HOH HOH A . 
G 7 HOH 1015 6020 1015 HOH HOH A . 
G 7 HOH 1016 6021 1016 HOH HOH A . 
G 7 HOH 1017 6022 1017 HOH HOH A . 
G 7 HOH 1018 6023 1018 HOH HOH A . 
G 7 HOH 1019 6024 1019 HOH HOH A . 
G 7 HOH 1020 6025 1020 HOH HOH A . 
G 7 HOH 1021 6026 1021 HOH HOH A . 
G 7 HOH 1022 6027 1022 HOH HOH A . 
G 7 HOH 1023 6028 1023 HOH HOH A . 
G 7 HOH 1024 6029 1024 HOH HOH A . 
G 7 HOH 1025 6030 1025 HOH HOH A . 
G 7 HOH 1026 6031 1026 HOH HOH A . 
G 7 HOH 1027 6032 1027 HOH HOH A . 
G 7 HOH 1028 6033 1028 HOH HOH A . 
G 7 HOH 1029 6034 1029 HOH HOH A . 
G 7 HOH 1030 6035 1030 HOH HOH A . 
G 7 HOH 1031 6036 1031 HOH HOH A . 
G 7 HOH 1032 6037 1032 HOH HOH A . 
G 7 HOH 1033 6038 1033 HOH HOH A . 
G 7 HOH 1034 6039 1034 HOH HOH A . 
G 7 HOH 1035 6040 1035 HOH HOH A . 
G 7 HOH 1036 6041 1036 HOH HOH A . 
G 7 HOH 1037 6042 1037 HOH HOH A . 
G 7 HOH 1038 6043 1038 HOH HOH A . 
G 7 HOH 1039 6044 1039 HOH HOH A . 
G 7 HOH 1040 6045 1040 HOH HOH A . 
G 7 HOH 1041 6046 1041 HOH HOH A . 
G 7 HOH 1042 6047 1042 HOH HOH A . 
G 7 HOH 1043 6048 1043 HOH HOH A . 
G 7 HOH 1044 6049 1044 HOH HOH A . 
G 7 HOH 1045 6050 1045 HOH HOH A . 
G 7 HOH 1046 6051 1046 HOH HOH A . 
G 7 HOH 1047 6052 1047 HOH HOH A . 
G 7 HOH 1048 6053 1048 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  O3  ? E MSN .   ? A MSN 5002 ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 O4  ? E MSN .   ? A MSN 5002 ? 1_555 76.5  ? 
2  O3  ? E MSN .   ? A MSN 5002 ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 92.9  ? 
3  O4  ? E MSN .   ? A MSN 5002 ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 169.3 ? 
4  O3  ? E MSN .   ? A MSN 5002 ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 165.9 ? 
5  O4  ? E MSN .   ? A MSN 5002 ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 89.6  ? 
6  NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 101.0 ? 
7  O3  ? E MSN .   ? A MSN 5002 ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 85.0  ? 
8  O4  ? E MSN .   ? A MSN 5002 ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 86.5  ? 
9  NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 91.3  ? 
10 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 92.2  ? 
11 O3  ? E MSN .   ? A MSN 5002 ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 86.7  ? 
12 O4  ? E MSN .   ? A MSN 5002 ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 81.9  ? 
13 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 99.0  ? 
14 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 93.5  ? 
15 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 5001 ? 1_555 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 167.0 ? 
# 
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 2006-07-04 
2 'Structure model' 1 1 2008-05-01 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-10-18 
# 
_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' 
4 4 'Structure model' 'Refinement description'    
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    4 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
DENZO     'data reduction' . ? 1 
SCALEPACK 'data scaling'   . ? 2 
CNS       refinement       . ? 3 
CNS       phasing          . ? 4 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             117 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             117 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            B 
_pdbx_validate_rmsd_bond.bond_value                1.374 
_pdbx_validate_rmsd_bond.bond_target_value         1.492 
_pdbx_validate_rmsd_bond.bond_deviation            -0.118 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.016 
_pdbx_validate_rmsd_bond.linker_flag               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 NE A ARG 540 ? ? CZ A ARG 540 ? ? NH1 A ARG 540 ? ? 123.72 120.30 3.42  0.50 N 
2 1 NE A ARG 818 ? ? CZ A ARG 818 ? ? NH2 A ARG 818 ? ? 117.01 120.30 -3.29 0.50 N 
3 1 NE A ARG 868 ? ? CZ A ARG 868 ? ? NH1 A ARG 868 ? ? 123.34 120.30 3.04  0.50 N 
4 1 NE A ARG 963 ? ? CZ A ARG 963 ? ? NH2 A ARG 963 ? ? 116.80 120.30 -3.50 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  ? ? -105.44 74.67   
2  1 HIS A 79  ? ? -159.12 84.91   
3  1 TRP A 95  ? ? -168.22 -90.06  
4  1 ASP A 106 ? ? -130.88 -58.31  
5  1 THR A 162 ? ? 65.15   -62.88  
6  1 GLN A 227 ? ? -137.22 -45.49  
7  1 ASP A 340 ? ? -168.96 -164.40 
8  1 LYS A 345 ? ? -90.03  -66.12  
9  1 SER A 411 ? ? 36.23   -123.50 
10 1 HIS A 471 ? ? -65.27  4.48    
11 1 PHE A 519 ? ? -59.29  -5.33   
12 1 ILE A 549 ? ? -149.09 -51.96  
13 1 LEU A 550 ? ? -164.73 117.19  
14 1 PRO A 562 ? ? -81.58  37.51   
15 1 PRO A 665 ? ? -59.27  -72.49  
16 1 SER A 762 ? ? 74.16   -4.62   
17 1 ILE A 831 ? ? -118.83 77.32   
18 1 SER A 833 ? ? -147.57 -17.39  
19 1 GLU A 991 ? ? 25.92   95.55   
20 1 GLU A 992 ? ? -143.73 17.82   
21 1 HIS A 993 ? ? -111.96 77.09   
# 
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 SER A 53  ? B 13.46  
2 1 LEU A 979 ? B -12.41 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    TYR 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     102 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.065 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_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     5003 
_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 'ZINC ION'                                                        ZN  
4 'PHOSPHATE ION'                                                   PO4 
5 '(1R,2R,3R,4S,5R)-4-AMINO-5-(METHYLTHIO)CYCLOPENTANE-1,2,3-TRIOL' MSN 
6 '(4S)-2-METHYL-2,4-PENTANEDIOL'                                   MPD 
7 water                                                             HOH 
# 
