data_3BUB
# 
_entry.id   3BUB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3BUB         
RCSB  RCSB045964   
WWPDB D_1000045964 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1HTY 'dGMII + Tris'                                                                                       unspecified 
PDB 1HWW 'dGMII + Swainsonine'                                                                                unspecified 
PDB 1HXK 'dGMII + Deoxymannojirimicin'                                                                        unspecified 
PDB 1PS2 'dGMII + Kifunensine'                                                                                unspecified 
PDB 1QWN 'dGMII + 5fluoro-Gulosylfluoride'                                                                    unspecified 
PDB 1QX1 'dGMII_D341N + 2F-mannosylF'                                                                         unspecified 
PDB 1R33 'dGMII + 5-thio-D-mannopyranosylamine'                                                               unspecified 
PDB 1R34 'dGMII + 5-thio-D-mannopyranosylamidinium salt'                                                      unspecified 
PDB 1TQS 'dGMII + Salacinol'                                                                                  unspecified 
PDB 1TQT 'dGMII + Diastereomer of Salacinol'                                                                  unspecified 
PDB 1TQU 'dGMII + Ghavamiol'                                                                                  unspecified 
PDB 1TQV 'dGMII + Blintol'                                                                                    unspecified 
PDB 1TQW 'dGMII + Blintol Diastereomer'                                                                       unspecified 
PDB 2ALW 'dGMII + Noeuromycin'                                                                                unspecified 
PDB 2F18 'dGMII + (2R,3R,4S)-2-({[(1R)-2-hydroxy-1-phenylethyl]amino}methyl)pyrrolidine-3,4-diol'             unspecified 
PDB 2F1A 'dGMII + (2R,3R,4S)-2-({[(1S)-2-hydroxy-1-phenylethyl]amino}methyl)pyrrolidine-3,4-diol'             unspecified 
PDB 2F1B 'dGMII + (2R,3R,4S,5R)-2-({[(1R)-2-hydroxy-1-phenylethyl]amino}methyl)-5-methylpyrrolidine-3,4-diol' unspecified 
PDB 2F7O 'dGMII + Mannostatin A'                                                                              unspecified 
PDB 2F7P 'dGMII + Benzyl-mannostatin A'                                                                       unspecified 
PDB 2F7Q 'dGMII + Aminocyclopentitetrol'                                                                      unspecified 
PDB 2F7R 'dGMII + Benzyl-aminocyclopentitetrol'                                                               unspecified 
PDB 3BUD 'dGMII_D204A + MPD, NAG, Zn, PO4'                                                                    unspecified 
PDB 3BUI 'dGMII_D204A + MPD, TRIS, Zn'                                                                        unspecified 
# 
_pdbx_database_status.entry_id                        3BUB 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2008-01-02 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_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                     
;Probing the substrate specificity of Golgi alpha-mannosidase II by use of synthetic oligosaccharides and a catalytic nucleophile mutant.
;
_citation.journal_abbrev            J.Am.Chem.Soc. 
_citation.journal_volume            130 
_citation.page_first                8975 
_citation.page_last                 8983 
_citation.year                      2008 
_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   18558690 
_citation.pdbx_database_id_DOI      10.1021/ja711248y 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Zhong, W.'     1 
primary 'Kuntz, D.A.'   2 
primary 'Ember, B.'     3 
primary 'Singh, H.'     4 
primary 'Moremen, K.W.' 5 
primary 'Rose, D.R.'    6 
primary 'Boons, G.J.'   7 
# 
_cell.length_a           68.765 
_cell.length_b           109.624 
_cell.length_c           138.649 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.entry_id           3BUB 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              4 
_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.space_group_name_H-M             'P 21 21 21' 
_symmetry.entry_id                         3BUB 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.Int_Tables_number                19 
_symmetry.cell_setting                     ? 
_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 2'           119701.617 1    3.2.1.114 ? 'Catalytic domain; UNP residues 76-1108' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE          221.208    1    ?         ? ?                                        ? 
3 non-polymer syn 'ZINC ION'                      65.409     1    ?         ? ?                                        ? 
4 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL' 118.174    3    ?         ? ?                                        ? 
5 water       nat water                           18.015     1470 ?         ? ?                                        ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Alpha-mannosidase II, Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase, MAN II, Golgi alpha-mannosidase II, AMAN II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;RSSHHHHHHGEFDDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHK
LKVFVVPHSHNDPGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEF
VTGGWVMPDEANSHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQ
RQLEFLWRQIWDNKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVD
QWKKKAELYRTNVLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTL
SGDFFTYADRSDNYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKT
HVVVDYEQRMQEALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNT
LPHWREQLVDFYVSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSK
PEHTSYASNLLLRKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSH
GDRSGAYLFLPNGPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDS
GDIFYTDLNGLQFIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQ
GVLDNKPVLHIYRLVLEKVNNCVRPSKLHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVS
VMRRLTKSSAKTQRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYV
SSHSS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;RSSHHHHHHGEFDDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHK
LKVFVVPHSHNDPGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEF
VTGGWVMPDEANSHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQ
RQLEFLWRQIWDNKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVD
QWKKKAELYRTNVLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTL
SGDFFTYADRSDNYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKT
HVVVDYEQRMQEALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNT
LPHWREQLVDFYVSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSK
PEHTSYASNLLLRKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSH
GDRSGAYLFLPNGPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDS
GDIFYTDLNGLQFIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQ
GVLDNKPVLHIYRLVLEKVNNCVRPSKLHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVS
VMRRLTKSSAKTQRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYV
SSHSS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    ARG n 
1 2    SER n 
1 3    SER n 
1 4    HIS n 
1 5    HIS n 
1 6    HIS n 
1 7    HIS n 
1 8    HIS n 
1 9    HIS n 
1 10   GLY n 
1 11   GLU n 
1 12   PHE n 
1 13   ASP n 
1 14   ASP n 
1 15   PRO n 
1 16   ILE n 
1 17   ARG n 
1 18   PRO n 
1 19   PRO n 
1 20   LEU n 
1 21   LYS n 
1 22   VAL n 
1 23   ALA n 
1 24   ARG n 
1 25   SER n 
1 26   PRO n 
1 27   ARG n 
1 28   PRO n 
1 29   GLY n 
1 30   GLN n 
1 31   CYS n 
1 32   GLN n 
1 33   ASP n 
1 34   VAL n 
1 35   VAL n 
1 36   GLN n 
1 37   ASP n 
1 38   VAL n 
1 39   PRO n 
1 40   ASN n 
1 41   VAL n 
1 42   ASP n 
1 43   VAL n 
1 44   GLN n 
1 45   MET n 
1 46   LEU n 
1 47   GLU n 
1 48   LEU n 
1 49   TYR n 
1 50   ASP n 
1 51   ARG n 
1 52   MET n 
1 53   SER n 
1 54   PHE n 
1 55   LYS n 
1 56   ASP n 
1 57   ILE n 
1 58   ASP n 
1 59   GLY n 
1 60   GLY n 
1 61   VAL n 
1 62   TRP n 
1 63   LYS n 
1 64   GLN n 
1 65   GLY n 
1 66   TRP n 
1 67   ASN n 
1 68   ILE n 
1 69   LYS n 
1 70   TYR n 
1 71   ASP n 
1 72   PRO n 
1 73   LEU n 
1 74   LYS n 
1 75   TYR n 
1 76   ASN n 
1 77   ALA n 
1 78   HIS n 
1 79   HIS n 
1 80   LYS n 
1 81   LEU n 
1 82   LYS n 
1 83   VAL n 
1 84   PHE n 
1 85   VAL n 
1 86   VAL n 
1 87   PRO n 
1 88   HIS n 
1 89   SER n 
1 90   HIS n 
1 91   ASN n 
1 92   ASP n 
1 93   PRO n 
1 94   GLY n 
1 95   TRP n 
1 96   ILE n 
1 97   GLN n 
1 98   THR n 
1 99   PHE n 
1 100  GLU n 
1 101  GLU n 
1 102  TYR n 
1 103  TYR n 
1 104  GLN n 
1 105  HIS n 
1 106  ASP n 
1 107  THR n 
1 108  LYS n 
1 109  HIS n 
1 110  ILE n 
1 111  LEU n 
1 112  SER n 
1 113  ASN n 
1 114  ALA n 
1 115  LEU n 
1 116  ARG n 
1 117  HIS n 
1 118  LEU n 
1 119  HIS n 
1 120  ASP n 
1 121  ASN n 
1 122  PRO n 
1 123  GLU n 
1 124  MET n 
1 125  LYS n 
1 126  PHE n 
1 127  ILE n 
1 128  TRP n 
1 129  ALA n 
1 130  GLU n 
1 131  ILE n 
1 132  SER n 
1 133  TYR n 
1 134  PHE n 
1 135  ALA n 
1 136  ARG n 
1 137  PHE n 
1 138  TYR n 
1 139  HIS n 
1 140  ASP n 
1 141  LEU n 
1 142  GLY n 
1 143  GLU n 
1 144  ASN n 
1 145  LYS n 
1 146  LYS n 
1 147  LEU n 
1 148  GLN n 
1 149  MET n 
1 150  LYS n 
1 151  SER n 
1 152  ILE n 
1 153  VAL n 
1 154  LYS n 
1 155  ASN n 
1 156  GLY n 
1 157  GLN n 
1 158  LEU n 
1 159  GLU n 
1 160  PHE n 
1 161  VAL n 
1 162  THR n 
1 163  GLY n 
1 164  GLY n 
1 165  TRP n 
1 166  VAL n 
1 167  MET n 
1 168  PRO n 
1 169  ASP n 
1 170  GLU n 
1 171  ALA n 
1 172  ASN n 
1 173  SER n 
1 174  HIS n 
1 175  TRP n 
1 176  ARG n 
1 177  ASN n 
1 178  VAL n 
1 179  LEU n 
1 180  LEU n 
1 181  GLN n 
1 182  LEU n 
1 183  THR n 
1 184  GLU n 
1 185  GLY n 
1 186  GLN n 
1 187  THR n 
1 188  TRP n 
1 189  LEU n 
1 190  LYS n 
1 191  GLN n 
1 192  PHE n 
1 193  MET n 
1 194  ASN n 
1 195  VAL n 
1 196  THR n 
1 197  PRO n 
1 198  THR n 
1 199  ALA n 
1 200  SER n 
1 201  TRP n 
1 202  ALA n 
1 203  ILE n 
1 204  ASP n 
1 205  PRO n 
1 206  PHE n 
1 207  GLY n 
1 208  HIS n 
1 209  SER n 
1 210  PRO n 
1 211  THR n 
1 212  MET n 
1 213  PRO n 
1 214  TYR n 
1 215  ILE n 
1 216  LEU n 
1 217  GLN n 
1 218  LYS n 
1 219  SER n 
1 220  GLY n 
1 221  PHE n 
1 222  LYS n 
1 223  ASN n 
1 224  MET n 
1 225  LEU n 
1 226  ILE n 
1 227  GLN n 
1 228  ARG n 
1 229  THR n 
1 230  HIS n 
1 231  TYR n 
1 232  SER n 
1 233  VAL n 
1 234  LYS n 
1 235  LYS n 
1 236  GLU n 
1 237  LEU n 
1 238  ALA n 
1 239  GLN n 
1 240  GLN n 
1 241  ARG n 
1 242  GLN n 
1 243  LEU n 
1 244  GLU n 
1 245  PHE n 
1 246  LEU n 
1 247  TRP n 
1 248  ARG n 
1 249  GLN n 
1 250  ILE n 
1 251  TRP n 
1 252  ASP n 
1 253  ASN n 
1 254  LYS n 
1 255  GLY n 
1 256  ASP n 
1 257  THR n 
1 258  ALA n 
1 259  LEU n 
1 260  PHE n 
1 261  THR n 
1 262  HIS n 
1 263  MET n 
1 264  MET n 
1 265  PRO n 
1 266  PHE n 
1 267  TYR n 
1 268  SER n 
1 269  TYR n 
1 270  ASP n 
1 271  ILE n 
1 272  PRO n 
1 273  HIS n 
1 274  THR n 
1 275  CYS n 
1 276  GLY n 
1 277  PRO n 
1 278  ASP n 
1 279  PRO n 
1 280  LYS n 
1 281  VAL n 
1 282  CYS n 
1 283  CYS n 
1 284  GLN n 
1 285  PHE n 
1 286  ASP n 
1 287  PHE n 
1 288  LYS n 
1 289  ARG n 
1 290  MET n 
1 291  GLY n 
1 292  SER n 
1 293  PHE n 
1 294  GLY n 
1 295  LEU n 
1 296  SER n 
1 297  CYS n 
1 298  PRO n 
1 299  TRP n 
1 300  LYS n 
1 301  VAL n 
1 302  PRO n 
1 303  PRO n 
1 304  ARG n 
1 305  THR n 
1 306  ILE n 
1 307  SER n 
1 308  ASP n 
1 309  GLN n 
1 310  ASN n 
1 311  VAL n 
1 312  ALA n 
1 313  ALA n 
1 314  ARG n 
1 315  SER n 
1 316  ASP n 
1 317  LEU n 
1 318  LEU n 
1 319  VAL n 
1 320  ASP n 
1 321  GLN n 
1 322  TRP n 
1 323  LYS n 
1 324  LYS n 
1 325  LYS n 
1 326  ALA n 
1 327  GLU n 
1 328  LEU n 
1 329  TYR n 
1 330  ARG n 
1 331  THR n 
1 332  ASN n 
1 333  VAL n 
1 334  LEU n 
1 335  LEU n 
1 336  ILE n 
1 337  PRO n 
1 338  LEU n 
1 339  GLY n 
1 340  ASP n 
1 341  ASP n 
1 342  PHE n 
1 343  ARG n 
1 344  PHE n 
1 345  LYS n 
1 346  GLN n 
1 347  ASN n 
1 348  THR n 
1 349  GLU n 
1 350  TRP n 
1 351  ASP n 
1 352  VAL n 
1 353  GLN n 
1 354  ARG n 
1 355  VAL n 
1 356  ASN n 
1 357  TYR n 
1 358  GLU n 
1 359  ARG n 
1 360  LEU n 
1 361  PHE n 
1 362  GLU n 
1 363  HIS n 
1 364  ILE n 
1 365  ASN n 
1 366  SER n 
1 367  GLN n 
1 368  ALA n 
1 369  HIS n 
1 370  PHE n 
1 371  ASN n 
1 372  VAL n 
1 373  GLN n 
1 374  ALA n 
1 375  GLN n 
1 376  PHE n 
1 377  GLY n 
1 378  THR n 
1 379  LEU n 
1 380  GLN n 
1 381  GLU n 
1 382  TYR n 
1 383  PHE n 
1 384  ASP n 
1 385  ALA n 
1 386  VAL n 
1 387  HIS n 
1 388  GLN n 
1 389  ALA n 
1 390  GLU n 
1 391  ARG n 
1 392  ALA n 
1 393  GLY n 
1 394  GLN n 
1 395  ALA n 
1 396  GLU n 
1 397  PHE n 
1 398  PRO n 
1 399  THR n 
1 400  LEU n 
1 401  SER n 
1 402  GLY n 
1 403  ASP n 
1 404  PHE n 
1 405  PHE n 
1 406  THR n 
1 407  TYR n 
1 408  ALA n 
1 409  ASP n 
1 410  ARG n 
1 411  SER n 
1 412  ASP n 
1 413  ASN n 
1 414  TYR n 
1 415  TRP n 
1 416  SER n 
1 417  GLY n 
1 418  TYR n 
1 419  TYR n 
1 420  THR n 
1 421  SER n 
1 422  ARG n 
1 423  PRO n 
1 424  TYR n 
1 425  HIS n 
1 426  LYS n 
1 427  ARG n 
1 428  MET n 
1 429  ASP n 
1 430  ARG n 
1 431  VAL n 
1 432  LEU n 
1 433  MET n 
1 434  HIS n 
1 435  TYR n 
1 436  VAL n 
1 437  ARG n 
1 438  ALA n 
1 439  ALA n 
1 440  GLU n 
1 441  MET n 
1 442  LEU n 
1 443  SER n 
1 444  ALA n 
1 445  TRP n 
1 446  HIS n 
1 447  SER n 
1 448  TRP n 
1 449  ASP n 
1 450  GLY n 
1 451  MET n 
1 452  ALA n 
1 453  ARG n 
1 454  ILE n 
1 455  GLU n 
1 456  GLU n 
1 457  ARG n 
1 458  LEU n 
1 459  GLU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  ARG n 
1 464  GLU n 
1 465  LEU n 
1 466  SER n 
1 467  LEU n 
1 468  PHE n 
1 469  GLN n 
1 470  HIS n 
1 471  HIS n 
1 472  ASP n 
1 473  GLY n 
1 474  ILE n 
1 475  THR n 
1 476  GLY n 
1 477  THR n 
1 478  ALA n 
1 479  LYS n 
1 480  THR n 
1 481  HIS n 
1 482  VAL n 
1 483  VAL n 
1 484  VAL n 
1 485  ASP n 
1 486  TYR n 
1 487  GLU n 
1 488  GLN n 
1 489  ARG n 
1 490  MET n 
1 491  GLN n 
1 492  GLU n 
1 493  ALA n 
1 494  LEU n 
1 495  LYS n 
1 496  ALA n 
1 497  CYS n 
1 498  GLN n 
1 499  MET n 
1 500  VAL n 
1 501  MET n 
1 502  GLN n 
1 503  GLN n 
1 504  SER n 
1 505  VAL n 
1 506  TYR n 
1 507  ARG n 
1 508  LEU n 
1 509  LEU n 
1 510  THR n 
1 511  LYS n 
1 512  PRO n 
1 513  SER n 
1 514  ILE n 
1 515  TYR n 
1 516  SER n 
1 517  PRO n 
1 518  ASP n 
1 519  PHE n 
1 520  SER n 
1 521  PHE n 
1 522  SER n 
1 523  TYR n 
1 524  PHE n 
1 525  THR n 
1 526  LEU n 
1 527  ASP n 
1 528  ASP n 
1 529  SER n 
1 530  ARG n 
1 531  TRP n 
1 532  PRO n 
1 533  GLY n 
1 534  SER n 
1 535  GLY n 
1 536  VAL n 
1 537  GLU n 
1 538  ASP n 
1 539  SER n 
1 540  ARG n 
1 541  THR n 
1 542  THR n 
1 543  ILE n 
1 544  ILE n 
1 545  LEU n 
1 546  GLY n 
1 547  GLU n 
1 548  ASP n 
1 549  ILE n 
1 550  LEU n 
1 551  PRO n 
1 552  SER n 
1 553  LYS n 
1 554  HIS n 
1 555  VAL n 
1 556  VAL n 
1 557  MET n 
1 558  HIS n 
1 559  ASN n 
1 560  THR n 
1 561  LEU n 
1 562  PRO n 
1 563  HIS n 
1 564  TRP n 
1 565  ARG n 
1 566  GLU n 
1 567  GLN n 
1 568  LEU n 
1 569  VAL n 
1 570  ASP n 
1 571  PHE n 
1 572  TYR n 
1 573  VAL n 
1 574  SER n 
1 575  SER n 
1 576  PRO n 
1 577  PHE n 
1 578  VAL n 
1 579  SER n 
1 580  VAL n 
1 581  THR n 
1 582  ASP n 
1 583  LEU n 
1 584  ALA n 
1 585  ASN n 
1 586  ASN n 
1 587  PRO n 
1 588  VAL n 
1 589  GLU n 
1 590  ALA n 
1 591  GLN n 
1 592  VAL n 
1 593  SER n 
1 594  PRO n 
1 595  VAL n 
1 596  TRP n 
1 597  SER n 
1 598  TRP n 
1 599  HIS n 
1 600  HIS n 
1 601  ASP n 
1 602  THR n 
1 603  LEU n 
1 604  THR n 
1 605  LYS n 
1 606  THR n 
1 607  ILE n 
1 608  HIS n 
1 609  PRO n 
1 610  GLN n 
1 611  GLY n 
1 612  SER n 
1 613  THR n 
1 614  THR n 
1 615  LYS n 
1 616  TYR n 
1 617  ARG n 
1 618  ILE n 
1 619  ILE n 
1 620  PHE n 
1 621  LYS n 
1 622  ALA n 
1 623  ARG n 
1 624  VAL n 
1 625  PRO n 
1 626  PRO n 
1 627  MET n 
1 628  GLY n 
1 629  LEU n 
1 630  ALA n 
1 631  THR n 
1 632  TYR n 
1 633  VAL n 
1 634  LEU n 
1 635  THR n 
1 636  ILE n 
1 637  SER n 
1 638  ASP n 
1 639  SER n 
1 640  LYS n 
1 641  PRO n 
1 642  GLU n 
1 643  HIS n 
1 644  THR n 
1 645  SER n 
1 646  TYR n 
1 647  ALA n 
1 648  SER n 
1 649  ASN n 
1 650  LEU n 
1 651  LEU n 
1 652  LEU n 
1 653  ARG n 
1 654  LYS n 
1 655  ASN n 
1 656  PRO n 
1 657  THR n 
1 658  SER n 
1 659  LEU n 
1 660  PRO n 
1 661  LEU n 
1 662  GLY n 
1 663  GLN n 
1 664  TYR n 
1 665  PRO n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LYS n 
1 670  PHE n 
1 671  GLY n 
1 672  ASP n 
1 673  PRO n 
1 674  ARG n 
1 675  GLU n 
1 676  ILE n 
1 677  SER n 
1 678  LEU n 
1 679  ARG n 
1 680  VAL n 
1 681  GLY n 
1 682  ASN n 
1 683  GLY n 
1 684  PRO n 
1 685  THR n 
1 686  LEU n 
1 687  ALA n 
1 688  PHE n 
1 689  SER n 
1 690  GLU n 
1 691  GLN n 
1 692  GLY n 
1 693  LEU n 
1 694  LEU n 
1 695  LYS n 
1 696  SER n 
1 697  ILE n 
1 698  GLN n 
1 699  LEU n 
1 700  THR n 
1 701  GLN n 
1 702  ASP n 
1 703  SER n 
1 704  PRO n 
1 705  HIS n 
1 706  VAL n 
1 707  PRO n 
1 708  VAL n 
1 709  HIS n 
1 710  PHE n 
1 711  LYS n 
1 712  PHE n 
1 713  LEU n 
1 714  LYS n 
1 715  TYR n 
1 716  GLY n 
1 717  VAL n 
1 718  ARG n 
1 719  SER n 
1 720  HIS n 
1 721  GLY n 
1 722  ASP n 
1 723  ARG n 
1 724  SER n 
1 725  GLY n 
1 726  ALA n 
1 727  TYR n 
1 728  LEU n 
1 729  PHE n 
1 730  LEU n 
1 731  PRO n 
1 732  ASN n 
1 733  GLY n 
1 734  PRO n 
1 735  ALA n 
1 736  SER n 
1 737  PRO n 
1 738  VAL n 
1 739  GLU n 
1 740  LEU n 
1 741  GLY n 
1 742  GLN n 
1 743  PRO n 
1 744  VAL n 
1 745  VAL n 
1 746  LEU n 
1 747  VAL n 
1 748  THR n 
1 749  LYS n 
1 750  GLY n 
1 751  LYS n 
1 752  LEU n 
1 753  GLU n 
1 754  SER n 
1 755  SER n 
1 756  VAL n 
1 757  SER n 
1 758  VAL n 
1 759  GLY n 
1 760  LEU n 
1 761  PRO n 
1 762  SER n 
1 763  VAL n 
1 764  VAL n 
1 765  HIS n 
1 766  GLN n 
1 767  THR n 
1 768  ILE n 
1 769  MET n 
1 770  ARG n 
1 771  GLY n 
1 772  GLY n 
1 773  ALA n 
1 774  PRO n 
1 775  GLU n 
1 776  ILE n 
1 777  ARG n 
1 778  ASN n 
1 779  LEU n 
1 780  VAL n 
1 781  ASP n 
1 782  ILE n 
1 783  GLY n 
1 784  SER n 
1 785  LEU n 
1 786  ASP n 
1 787  ASN n 
1 788  THR n 
1 789  GLU n 
1 790  ILE n 
1 791  VAL n 
1 792  MET n 
1 793  ARG n 
1 794  LEU n 
1 795  GLU n 
1 796  THR n 
1 797  HIS n 
1 798  ILE n 
1 799  ASP n 
1 800  SER n 
1 801  GLY n 
1 802  ASP n 
1 803  ILE n 
1 804  PHE n 
1 805  TYR n 
1 806  THR n 
1 807  ASP n 
1 808  LEU n 
1 809  ASN n 
1 810  GLY n 
1 811  LEU n 
1 812  GLN n 
1 813  PHE n 
1 814  ILE n 
1 815  LYS n 
1 816  ARG n 
1 817  ARG n 
1 818  ARG n 
1 819  LEU n 
1 820  ASP n 
1 821  LYS n 
1 822  LEU n 
1 823  PRO n 
1 824  LEU n 
1 825  GLN n 
1 826  ALA n 
1 827  ASN n 
1 828  TYR n 
1 829  TYR n 
1 830  PRO n 
1 831  ILE n 
1 832  PRO n 
1 833  SER n 
1 834  GLY n 
1 835  MET n 
1 836  PHE n 
1 837  ILE n 
1 838  GLU n 
1 839  ASP n 
1 840  ALA n 
1 841  ASN n 
1 842  THR n 
1 843  ARG n 
1 844  LEU n 
1 845  THR n 
1 846  LEU n 
1 847  LEU n 
1 848  THR n 
1 849  GLY n 
1 850  GLN n 
1 851  PRO n 
1 852  LEU n 
1 853  GLY n 
1 854  GLY n 
1 855  SER n 
1 856  SER n 
1 857  LEU n 
1 858  ALA n 
1 859  SER n 
1 860  GLY n 
1 861  GLU n 
1 862  LEU n 
1 863  GLU n 
1 864  ILE n 
1 865  MET n 
1 866  GLN n 
1 867  ASP n 
1 868  ARG n 
1 869  ARG n 
1 870  LEU n 
1 871  ALA n 
1 872  SER n 
1 873  ASP n 
1 874  ASP n 
1 875  GLU n 
1 876  ARG n 
1 877  GLY n 
1 878  LEU n 
1 879  GLY n 
1 880  GLN n 
1 881  GLY n 
1 882  VAL n 
1 883  LEU n 
1 884  ASP n 
1 885  ASN n 
1 886  LYS n 
1 887  PRO n 
1 888  VAL n 
1 889  LEU n 
1 890  HIS n 
1 891  ILE n 
1 892  TYR n 
1 893  ARG n 
1 894  LEU n 
1 895  VAL n 
1 896  LEU n 
1 897  GLU n 
1 898  LYS n 
1 899  VAL n 
1 900  ASN n 
1 901  ASN n 
1 902  CYS n 
1 903  VAL n 
1 904  ARG n 
1 905  PRO n 
1 906  SER n 
1 907  LYS n 
1 908  LEU n 
1 909  HIS n 
1 910  PRO n 
1 911  ALA n 
1 912  GLY n 
1 913  TYR n 
1 914  LEU n 
1 915  THR n 
1 916  SER n 
1 917  ALA n 
1 918  ALA n 
1 919  HIS n 
1 920  LYS n 
1 921  ALA n 
1 922  SER n 
1 923  GLN n 
1 924  SER n 
1 925  LEU n 
1 926  LEU n 
1 927  ASP n 
1 928  PRO n 
1 929  LEU n 
1 930  ASP n 
1 931  LYS n 
1 932  PHE n 
1 933  ILE n 
1 934  PHE n 
1 935  ALA n 
1 936  GLU n 
1 937  ASN n 
1 938  GLU n 
1 939  TRP n 
1 940  ILE n 
1 941  GLY n 
1 942  ALA n 
1 943  GLN n 
1 944  GLY n 
1 945  GLN n 
1 946  PHE n 
1 947  GLY n 
1 948  GLY n 
1 949  ASP n 
1 950  HIS n 
1 951  PRO n 
1 952  SER n 
1 953  ALA n 
1 954  ARG n 
1 955  GLU n 
1 956  ASP n 
1 957  LEU n 
1 958  ASP n 
1 959  VAL n 
1 960  SER n 
1 961  VAL n 
1 962  MET n 
1 963  ARG n 
1 964  ARG n 
1 965  LEU n 
1 966  THR n 
1 967  LYS n 
1 968  SER n 
1 969  SER n 
1 970  ALA n 
1 971  LYS n 
1 972  THR n 
1 973  GLN n 
1 974  ARG n 
1 975  VAL n 
1 976  GLY n 
1 977  TYR n 
1 978  VAL n 
1 979  LEU n 
1 980  HIS n 
1 981  ARG n 
1 982  THR n 
1 983  ASN n 
1 984  LEU n 
1 985  MET n 
1 986  GLN n 
1 987  CYS n 
1 988  GLY n 
1 989  THR n 
1 990  PRO n 
1 991  GLU n 
1 992  GLU n 
1 993  HIS n 
1 994  THR n 
1 995  GLN n 
1 996  LYS n 
1 997  LEU n 
1 998  ASP n 
1 999  VAL n 
1 1000 CYS n 
1 1001 HIS n 
1 1002 LEU n 
1 1003 LEU n 
1 1004 PRO n 
1 1005 ASN n 
1 1006 VAL n 
1 1007 ALA n 
1 1008 ARG n 
1 1009 CYS n 
1 1010 GLU n 
1 1011 ARG n 
1 1012 THR n 
1 1013 THR n 
1 1014 LEU n 
1 1015 THR n 
1 1016 PHE n 
1 1017 LEU n 
1 1018 GLN n 
1 1019 ASN n 
1 1020 LEU n 
1 1021 GLU n 
1 1022 HIS n 
1 1023 LEU n 
1 1024 ASP n 
1 1025 GLY n 
1 1026 MET n 
1 1027 VAL n 
1 1028 ALA n 
1 1029 PRO n 
1 1030 GLU n 
1 1031 VAL n 
1 1032 CYS n 
1 1033 PRO n 
1 1034 MET n 
1 1035 GLU n 
1 1036 THR n 
1 1037 ALA n 
1 1038 ALA n 
1 1039 TYR n 
1 1040 VAL n 
1 1041 SER n 
1 1042 SER n 
1 1043 HIS n 
1 1044 SER n 
1 1045 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               'Fruit fly' 
_entity_src_gen.gene_src_genus                     ? 
_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     ? 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Drosophila melanogaster' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     ? 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               '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_seq_one_letter_code   
;DDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHKLKVFVVPHSHND
PGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEFVTGGWVMPDEAN
SHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQRQLEFLWRQIWD
NKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVDQWKKKAELYRTN
VLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTLSGDFFTYADRSD
NYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKTHVVVDYEQRMQE
ALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNTLPHWREQLVDFY
VSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSKPEHTSYASNLLL
RKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSHGDRSGAYLFLPN
GPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDSGDIFYTDLNGLQ
FIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQGVLDNKPVLHIY
RLVLEKVNNCVRPSELHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVSVMRRLTKSSAKT
QRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYVSSHSS
;
_struct_ref.pdbx_align_begin           76 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3BUB 
_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 3BUB ARG A 1   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 1   1  
1 3BUB SER A 2   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 2   2  
1 3BUB SER A 3   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 3   3  
1 3BUB HIS A 4   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 4   4  
1 3BUB HIS A 5   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 5   5  
1 3BUB HIS A 6   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 6   6  
1 3BUB HIS A 7   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 7   7  
1 3BUB HIS A 8   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 8   8  
1 3BUB HIS A 9   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 9   9  
1 3BUB GLY A 10  ? UNP Q24451 ?   ?   'EXPRESSION TAG' 10  10 
1 3BUB GLU A 11  ? UNP Q24451 ?   ?   'EXPRESSION TAG' 11  11 
1 3BUB PHE A 12  ? UNP Q24451 ?   ?   'EXPRESSION TAG' 12  12 
1 3BUB LYS A 907 ? UNP Q24451 GLU 970 'SEE REMARK 999' 907 13 
# 
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 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE          ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE                   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'                      ? 'Zn 2'           65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          3BUB 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.18 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   43.65 
_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              7.0 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_details    
;Tris, NaCl, PEG6000, MPD;
Tris found in the active site under normal 
crystallization conditions was removed by 
soaking crystals in phosphate buffered 
resevoir solution, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
;
_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   2007-04-20 
_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   0.9770 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.pdbx_wavelength_list        0.9770 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'CHESS BEAMLINE A1' 
_diffrn_source.pdbx_synchrotron_site       CHESS 
_diffrn_source.pdbx_synchrotron_beamline   A1 
# 
_reflns.entry_id                     3BUB 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.d_resolution_high            1.38 
_reflns.d_resolution_low             20 
_reflns.number_all                   214738 
_reflns.number_obs                   211715 
_reflns.percent_possible_obs         98.5 
_reflns.pdbx_Rmerge_I_obs            0.06 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        20.7 
_reflns.B_iso_Wilson_estimate        18.0 
_reflns.pdbx_redundancy              6.4 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.38 
_reflns_shell.d_res_low              1.40 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.percent_possible_all   82.0 
_reflns_shell.Rmerge_I_obs           0.33 
_reflns_shell.meanI_over_sigI_obs    3.5 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_redundancy        2.3 
_reflns_shell.number_unique_all      3723 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 3BUB 
_refine.ls_d_res_high                            1.380 
_refine.ls_d_res_low                             19.810 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.ls_percent_reflns_obs                    97.990 
_refine.ls_number_reflns_obs                     210432 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_obs                          0.180 
_refine.ls_R_factor_R_work                       0.180 
_refine.ls_R_factor_R_free                       0.204 
_refine.ls_percent_reflns_R_free                 1.500 
_refine.ls_number_reflns_R_free                  3138 
_refine.B_iso_mean                               14.616 
_refine.aniso_B[1][1]                            0.010 
_refine.aniso_B[2][2]                            -0.010 
_refine.aniso_B[3][3]                            0.000 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.946 
_refine.pdbx_overall_ESU_R                       0.062 
_refine.pdbx_overall_ESU_R_Free                  0.063 
_refine.overall_SU_ML                            0.042 
_refine.overall_SU_B                             1.042 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     214738 
_refine.ls_R_factor_all                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB entry 1HTY' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_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_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        3BUB 
_refine_analyze.Luzzati_coordinate_error_obs    0.16 
_refine_analyze.Luzzati_sigma_a_obs             0.14 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_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        8196 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_refine_hist.number_atoms_solvent             1470 
_refine_hist.number_atoms_total               9705 
_refine_hist.d_res_high                       1.380 
_refine_hist.d_res_low                        19.810 
# 
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 
r_bond_refined_d         8882  0.014  0.021  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      12138 1.544  1.937  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   1115  6.080  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   439   36.699 23.667 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   1515  12.552 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   61    18.041 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           1285  0.103  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     6949  0.008  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            4462  0.206  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          6151  0.316  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    1330  0.152  0.200  ? 'X-RAY DIFFRACTION' ? 
r_metal_ion_refined      2     0.038  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   85    0.227  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 82    0.156  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              5430  1.044  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             8681  1.680  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              3895  2.411  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             3432  3.720  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.380 
_refine_ls_shell.d_res_low                        1.416 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               83.890 
_refine_ls_shell.number_reflns_R_work             12978 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.277 
_refine_ls_shell.R_factor_R_free                  0.274 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             196 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                13174 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3BUB 
_struct.title                     'Golgi alpha-mannosidase II with an empty active site' 
_struct.pdbx_descriptor           'Alpha-mannosidase 2 (E.C.3.2.1.114)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3BUB 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
'GLYCOSYL HYDROLASE FAMILY 38, Glycosidase, Golgi apparatus, Membrane, Signal-anchor, Transmembrane, 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 4 ? 
F N N 4 ? 
G N N 5 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  MET A 45   ? MET A 52   ? MET A 45   MET A 52   1 ? 8  
HELX_P HELX_P2  2  ASP A 71   ? TYR A 75   ? ASP A 71   TYR A 75   5 ? 5  
HELX_P HELX_P3  3  THR A 98   ? ASP A 106  ? THR A 98   ASP A 106  1 ? 9  
HELX_P HELX_P4  4  ASP A 106  ? ASN A 121  ? ASP A 106  ASN A 121  1 ? 16 
HELX_P HELX_P5  5  GLU A 130  ? HIS A 139  ? GLU A 130  HIS A 139  1 ? 10 
HELX_P HELX_P6  6  GLY A 142  ? ASN A 155  ? GLY A 142  ASN A 155  1 ? 14 
HELX_P HELX_P7  7  HIS A 174  ? ASN A 194  ? HIS A 174  ASN A 194  1 ? 21 
HELX_P HELX_P8  8  PRO A 210  ? LYS A 218  ? PRO A 210  LYS A 218  1 ? 9  
HELX_P HELX_P9  9  HIS A 230  ? GLN A 240  ? HIS A 230  GLN A 240  1 ? 11 
HELX_P HELX_P10 10 ASP A 270  ? THR A 274  ? ASP A 270  THR A 274  5 ? 5  
HELX_P HELX_P11 11 ASP A 278  ? CYS A 283  ? ASP A 278  CYS A 283  1 ? 6  
HELX_P HELX_P12 12 GLN A 284  ? MET A 290  ? GLN A 284  MET A 290  5 ? 7  
HELX_P HELX_P13 13 ASN A 310  ? GLU A 327  ? ASN A 310  GLU A 327  1 ? 18 
HELX_P HELX_P14 14 GLN A 346  ? GLN A 367  ? GLN A 346  GLN A 367  1 ? 22 
HELX_P HELX_P15 15 ALA A 368  ? PHE A 370  ? ALA A 368  PHE A 370  5 ? 3  
HELX_P HELX_P16 16 THR A 378  ? ALA A 392  ? THR A 378  ALA A 392  1 ? 15 
HELX_P HELX_P17 17 SER A 416  ? THR A 420  ? SER A 416  THR A 420  5 ? 5  
HELX_P HELX_P18 18 ARG A 422  ? TRP A 445  ? ARG A 422  TRP A 445  1 ? 24 
HELX_P HELX_P19 19 ASP A 449  ? ALA A 452  ? ASP A 449  ALA A 452  5 ? 4  
HELX_P HELX_P20 20 ARG A 453  ? GLN A 469  ? ARG A 453  GLN A 469  1 ? 17 
HELX_P HELX_P21 21 LYS A 479  ? LEU A 509  ? LYS A 479  LEU A 509  1 ? 31 
HELX_P HELX_P22 22 PRO A 823  ? TYR A 828  ? PRO A 823  TYR A 828  5 ? 6  
HELX_P HELX_P23 23 THR A 915  ? ASP A 927  ? THR A 915  ASP A 927  1 ? 13 
HELX_P HELX_P24 24 ASP A 998  ? LEU A 1002 ? ASP A 998  LEU A 1002 5 ? 5  
HELX_P HELX_P25 25 ASP A 1024 ? VAL A 1027 ? ASP A 1024 VAL A 1027 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1 disulf ? ? A CYS 31   SG  ? ? ? 1_555 A CYS 1032 SG ? ? A CYS 31   A CYS 1032 1_555 ? ? ? ? ? ? ? 2.060 ? 
disulf2 disulf ? ? A CYS 275  SG  ? ? ? 1_555 A CYS 282  SG ? ? A CYS 275  A CYS 282  1_555 ? ? ? ? ? ? ? 2.017 ? 
disulf3 disulf ? ? A CYS 283  SG  ? ? ? 1_555 A CYS 297  SG ? ? A CYS 283  A CYS 297  1_555 ? ? ? ? ? ? ? 2.085 ? 
disulf4 disulf ? ? A CYS 902  SG  ? ? ? 1_555 A CYS 987  SG ? ? A CYS 902  A CYS 987  1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf5 disulf ? ? A CYS 1000 SG  ? ? ? 1_555 A CYS 1009 SG ? ? A CYS 1000 A CYS 1009 1_555 ? ? ? ? ? ? ? 2.011 ? 
covale1 covale ? ? A ASN 194  ND2 ? ? ? 1_555 B NAG .    C1 ? ? A ASN 194  A NAG 1046 1_555 ? ? ? ? ? ? ? 1.457 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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 -8.08 
2 TRP 531 A . ? TRP 531 A PRO 532 A ? PRO 532 A 1 6.52  
# 
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  HIS A 705  ? TYR A 715  ? HIS A 705  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  HIS A 705  ? TYR A 715  ? HIS A 705  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  THR A 972  ? ARG A 981  ? THR A 972  ARG A 981  
K 3  THR A 1036 ? SER A 1044 ? THR A 1036 SER A 1044 
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 LEU A 334  ? O LEU A 334  N LYS A 82   ? N LYS A 82   
B 2  3  N VAL A 85   ? N VAL A 85   O GLN A 375  ? O GLN A 375  
C 1  2  N PHE A 126  ? N PHE A 126  O GLU A 159  ? O GLU A 159  
D 1  2  N 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 ARG A 617  ? O ARG A 617  N SER A 593  ? N SER A 593  
G 4  5  N VAL A 592  ? N VAL A 592  O SER A 645  ? O SER A 645  
H 1  2  O LYS A 669  ? O LYS A 669  N LEU A 651  ? N LEU A 651  
H 2  3  N LEU A 652  ? N LEU A 652  O VAL A 745  ? O VAL A 745  
H 3  4  N LEU A 746  ? N LEU A 746  O SER A 757  ? O SER A 757  
H 4  5  N SER A 754  ? N SER A 754  O MET A 769  ? O MET A 769  
H 5  6  N ILE A 768  ? N ILE A 768  O GLU A 775  ? O GLU A 775  
H 6  7  N VAL A 780  ? N VAL A 780  O VAL A 888  ? O VAL A 888  
H 7  8  O VAL A 895  ? O VAL A 895  N THR A 845  ? N THR A 845  
H 8  9  O LEU A 846  ? O LEU A 846  N MET A 835  ? N MET A 835  
H 9  10 O PHE A 836  ? O PHE A 836  N TYR A 805  ? N TYR A 805  
H 10 11 N PHE A 804  ? N PHE A 804  O ARG A 816  ? O ARG A 816  
H 11 12 N PHE A 813  ? N PHE A 813  O GLY A 912  ? O GLY A 912  
I 1  2  N ILE A 676  ? N ILE A 676  O PHE A 688  ? O PHE A 688  
I 2  3  N ALA A 687  ? N ALA A 687  O LYS A 695  ? O LYS A 695  
I 3  4  N ILE A 697  ? N ILE A 697  O VAL A 706  ? O VAL A 706  
I 4  5  N LYS A 714  ? N LYS A 714  O SER A 736  ? O SER A 736  
J 1  2  N ILE A 676  ? N ILE A 676  O PHE A 688  ? O PHE A 688  
J 2  3  N ALA A 687  ? N ALA A 687  O LYS A 695  ? O LYS A 695  
J 3  4  N ILE A 697  ? N ILE A 697  O VAL A 706  ? O VAL A 706  
J 4  5  N LYS A 711  ? N LYS A 711  O ARG A 793  ? O ARG A 793  
J 5  6  N ILE A 790  ? N ILE A 790  O GLN A 866  ? O GLN A 866  
J 6  7  O MET A 865  ? O MET A 865  N GLY A 853  ? N GLY A 853  
J 7  8  O LEU A 852  ? O LEU A 852  N ILE A 831  ? N ILE A 831  
K 1  2  N ARG A 963  ? N ARG A 963  O GLY A 976  ? O GLY A 976  
K 2  3  N LEU A 979  ? N LEU A 979  O ALA A 1037 ? O ALA A 1037 
K 3  4  O SER A 1042 ? O SER A 1042 N 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 ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 1046' 
AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 1047'  
AC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE MPD A 1048' 
AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MPD A 1049' 
AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MPD A 1050' 
# 
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 3 LYS A 154 ? LYS A 154  . ? 1_555 ? 
2  AC1 3 ASN A 194 ? ASN A 194  . ? 1_555 ? 
3  AC1 3 HOH G .   ? HOH A 2328 . ? 1_555 ? 
4  AC2 5 HIS A 90  ? HIS A 90   . ? 1_555 ? 
5  AC2 5 ASP A 92  ? ASP A 92   . ? 1_555 ? 
6  AC2 5 ASP A 204 ? ASP A 204  . ? 1_555 ? 
7  AC2 5 HIS A 471 ? HIS A 471  . ? 1_555 ? 
8  AC2 5 HOH G .   ? HOH A 1051 . ? 1_555 ? 
9  AC3 8 LYS A 63  ? LYS A 63   . ? 1_555 ? 
10 AC3 8 GLN A 64  ? GLN A 64   . ? 1_555 ? 
11 AC3 8 TYR A 267 ? TYR A 267  . ? 1_555 ? 
12 AC3 8 HIS A 273 ? HIS A 273  . ? 1_555 ? 
13 AC3 8 HOH G .   ? HOH A 1071 . ? 1_555 ? 
14 AC3 8 HOH G .   ? HOH A 1072 . ? 1_555 ? 
15 AC3 8 HOH G .   ? HOH A 1519 . ? 1_555 ? 
16 AC3 8 HOH G .   ? HOH A 2188 . ? 1_555 ? 
17 AC4 4 TYR A 435 ? TYR A 435  . ? 1_555 ? 
18 AC4 4 GLN A 491 ? GLN A 491  . ? 1_555 ? 
19 AC4 4 GLN A 498 ? GLN A 498  . ? 1_555 ? 
20 AC4 4 HOH G .   ? HOH A 1170 . ? 1_555 ? 
21 AC5 4 ARG A 457 ? ARG A 457  . ? 4_465 ? 
22 AC5 4 LYS A 495 ? LYS A 495  . ? 4_465 ? 
23 AC5 4 HOH G .   ? HOH A 1479 . ? 1_555 ? 
24 AC5 4 HOH G .   ? HOH A 2182 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3BUB 
_atom_sites.fract_transf_matrix[1][1]   0.014542 
_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]   0.009122 
_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]   0.007212 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . GLN A 1 30   ? 46.782 34.124  -18.803 1.00 32.19 ? 30   GLN A N   1 
ATOM   2     C  CA  . GLN A 1 30   ? 45.390 34.192  -19.339 1.00 31.75 ? 30   GLN A CA  1 
ATOM   3     C  C   . GLN A 1 30   ? 44.538 35.210  -18.589 1.00 30.22 ? 30   GLN A C   1 
ATOM   4     O  O   . GLN A 1 30   ? 44.225 35.050  -17.407 1.00 31.22 ? 30   GLN A O   1 
ATOM   5     C  CB  . GLN A 1 30   ? 44.720 32.816  -19.368 1.00 32.61 ? 30   GLN A CB  1 
ATOM   6     C  CG  . GLN A 1 30   ? 43.331 32.850  -20.001 1.00 35.80 ? 30   GLN A CG  1 
ATOM   7     C  CD  . GLN A 1 30   ? 43.347 33.202  -21.482 1.00 39.34 ? 30   GLN A CD  1 
ATOM   8     O  OE1 . GLN A 1 30   ? 44.170 32.679  -22.240 1.00 40.67 ? 30   GLN A OE1 1 
ATOM   9     N  NE2 . GLN A 1 30   ? 42.443 34.100  -21.897 1.00 40.33 ? 30   GLN A NE2 1 
ATOM   10    N  N   . CYS A 1 31   ? 44.288 36.242  -19.394 1.00 27.89 ? 31   CYS A N   1 
ATOM   11    C  CA  . CYS A 1 31   ? 43.537 37.354  -18.832 1.00 25.06 ? 31   CYS A CA  1 
ATOM   12    C  C   . CYS A 1 31   ? 42.047 37.039  -18.811 1.00 23.19 ? 31   CYS A C   1 
ATOM   13    O  O   . CYS A 1 31   ? 41.532 36.430  -19.753 1.00 22.37 ? 31   CYS A O   1 
ATOM   14    C  CB  . CYS A 1 31   ? 43.800 38.582  -19.690 1.00 24.92 ? 31   CYS A CB  1 
ATOM   15    S  SG  . CYS A 1 31   ? 45.539 39.095  -19.613 1.00 26.54 ? 31   CYS A SG  1 
ATOM   16    N  N   . GLN A 1 32   ? 41.358 37.458  -17.751 1.00 20.68 ? 32   GLN A N   1 
ATOM   17    C  CA  . GLN A 1 32   ? 39.895 37.438  -17.720 1.00 19.64 ? 32   GLN A CA  1 
ATOM   18    C  C   . GLN A 1 32   ? 39.352 38.363  -18.799 1.00 17.46 ? 32   GLN A C   1 
ATOM   19    O  O   . GLN A 1 32   ? 39.890 39.446  -19.035 1.00 15.80 ? 32   GLN A O   1 
ATOM   20    C  CB  . GLN A 1 32   ? 39.341 37.969  -16.393 1.00 21.07 ? 32   GLN A CB  1 
ATOM   21    C  CG  . GLN A 1 32   ? 39.227 36.987  -15.262 1.00 23.87 ? 32   GLN A CG  1 
ATOM   22    C  CD  . GLN A 1 32   ? 38.226 37.458  -14.196 1.00 25.92 ? 32   GLN A CD  1 
ATOM   23    O  OE1 . GLN A 1 32   ? 37.111 36.915  -14.106 1.00 25.85 ? 32   GLN A OE1 1 
ATOM   24    N  NE2 . GLN A 1 32   ? 38.616 38.463  -13.397 1.00 28.25 ? 32   GLN A NE2 1 
ATOM   25    N  N   . ASP A 1 33   ? 38.281 37.934  -19.441 1.00 15.79 ? 33   ASP A N   1 
ATOM   26    C  CA  . ASP A 1 33   ? 37.544 38.769  -20.388 1.00 15.04 ? 33   ASP A CA  1 
ATOM   27    C  C   . ASP A 1 33   ? 36.630 39.748  -19.631 1.00 14.86 ? 33   ASP A C   1 
ATOM   28    O  O   . ASP A 1 33   ? 35.703 39.339  -18.945 1.00 16.56 ? 33   ASP A O   1 
ATOM   29    C  CB  . ASP A 1 33   ? 36.739 37.841  -21.309 1.00 15.09 ? 33   ASP A CB  1 
ATOM   30    C  CG  . ASP A 1 33   ? 36.094 38.550  -22.471 1.00 18.10 ? 33   ASP A CG  1 
ATOM   31    O  OD1 . ASP A 1 33   ? 35.579 39.680  -22.337 1.00 18.69 ? 33   ASP A OD1 1 
ATOM   32    O  OD2 . ASP A 1 33   ? 35.998 37.991  -23.578 1.00 22.11 ? 33   ASP A OD2 1 
ATOM   33    N  N   . VAL A 1 34   ? 36.863 41.047  -19.766 1.00 10.54 ? 34   VAL A N   1 
ATOM   34    C  CA  . VAL A 1 34   ? 36.104 42.034  -19.007 1.00 10.25 ? 34   VAL A CA  1 
ATOM   35    C  C   . VAL A 1 34   ? 34.895 42.578  -19.761 1.00 9.40  ? 34   VAL A C   1 
ATOM   36    O  O   . VAL A 1 34   ? 34.226 43.503  -19.295 1.00 8.98  ? 34   VAL A O   1 
ATOM   37    C  CB  . VAL A 1 34   ? 37.025 43.192  -18.558 1.00 10.20 ? 34   VAL A CB  1 
ATOM   38    C  CG1 . VAL A 1 34   ? 38.193 42.655  -17.736 1.00 12.08 ? 34   VAL A CG1 1 
ATOM   39    C  CG2 . VAL A 1 34   ? 37.557 43.989  -19.733 1.00 11.35 ? 34   VAL A CG2 1 
ATOM   40    N  N   . VAL A 1 35   ? 34.625 42.024  -20.950 1.00 8.96  ? 35   VAL A N   1 
ATOM   41    C  CA  . VAL A 1 35   ? 33.548 42.539  -21.797 1.00 9.41  ? 35   VAL A CA  1 
ATOM   42    C  C   . VAL A 1 35   ? 32.362 41.587  -21.965 1.00 9.14  ? 35   VAL A C   1 
ATOM   43    O  O   . VAL A 1 35   ? 31.223 42.001  -21.926 1.00 9.16  ? 35   VAL A O   1 
ATOM   44    C  CB  . VAL A 1 35   ? 34.098 42.888  -23.192 1.00 9.48  ? 35   VAL A CB  1 
ATOM   45    C  CG1 . VAL A 1 35   ? 32.964 43.335  -24.141 1.00 10.30 ? 35   VAL A CG1 1 
ATOM   46    C  CG2 . VAL A 1 35   ? 35.200 43.956  -23.081 1.00 10.98 ? 35   VAL A CG2 1 
ATOM   47    N  N   . GLN A 1 36   ? 32.680 40.312  -22.194 1.00 10.54 ? 36   GLN A N   1 
ATOM   48    C  CA  . GLN A 1 36   ? 31.685 39.350  -22.739 1.00 12.57 ? 36   GLN A CA  1 
ATOM   49    C  C   . GLN A 1 36   ? 30.963 38.474  -21.728 1.00 14.86 ? 36   GLN A C   1 
ATOM   50    O  O   . GLN A 1 36   ? 29.938 37.855  -22.064 1.00 18.14 ? 36   GLN A O   1 
ATOM   51    C  CB  . GLN A 1 36   ? 32.346 38.481  -23.790 1.00 12.26 ? 36   GLN A CB  1 
ATOM   52    C  CG  . GLN A 1 36   ? 33.025 39.320  -24.812 1.00 13.05 ? 36   GLN A CG  1 
ATOM   53    C  CD  . GLN A 1 36   ? 33.512 38.494  -25.960 1.00 13.82 ? 36   GLN A CD  1 
ATOM   54    O  OE1 . GLN A 1 36   ? 32.755 38.267  -26.907 1.00 15.35 ? 36   GLN A OE1 1 
ATOM   55    N  NE2 . GLN A 1 36   ? 34.748 38.024  -25.884 1.00 13.87 ? 36   GLN A NE2 1 
ATOM   56    N  N   . ASP A 1 37   ? 31.479 38.395  -20.507 1.00 15.46 ? 37   ASP A N   1 
ATOM   57    C  CA  . ASP A 1 37   ? 30.897 37.526  -19.488 1.00 16.68 ? 37   ASP A CA  1 
ATOM   58    C  C   . ASP A 1 37   ? 30.241 38.412  -18.436 1.00 15.37 ? 37   ASP A C   1 
ATOM   59    O  O   . ASP A 1 37   ? 30.939 39.148  -17.748 1.00 17.87 ? 37   ASP A O   1 
ATOM   60    C  CB  . ASP A 1 37   ? 31.992 36.672  -18.834 1.00 18.00 ? 37   ASP A CB  1 
ATOM   61    C  CG  . ASP A 1 37   ? 32.695 35.738  -19.805 1.00 21.14 ? 37   ASP A CG  1 
ATOM   62    O  OD1 . ASP A 1 37   ? 32.000 35.111  -20.635 1.00 25.01 ? 37   ASP A OD1 1 
ATOM   63    O  OD2 . ASP A 1 37   ? 33.940 35.554  -19.792 1.00 24.45 ? 37   ASP A OD2 1 
ATOM   64    N  N   . VAL A 1 38   ? 28.921 38.356  -18.314 1.00 14.10 ? 38   VAL A N   1 
ATOM   65    C  CA  . VAL A 1 38   ? 28.245 39.097  -17.227 1.00 13.39 ? 38   VAL A CA  1 
ATOM   66    C  C   . VAL A 1 38   ? 28.401 38.388  -15.870 1.00 13.04 ? 38   VAL A C   1 
ATOM   67    O  O   . VAL A 1 38   ? 27.936 37.255  -15.705 1.00 13.07 ? 38   VAL A O   1 
ATOM   68    C  CB  . VAL A 1 38   ? 26.760 39.335  -17.549 1.00 13.26 ? 38   VAL A CB  1 
ATOM   69    C  CG1 . VAL A 1 38   ? 26.037 40.054  -16.419 1.00 14.53 ? 38   VAL A CG1 1 
ATOM   70    C  CG2 . VAL A 1 38   ? 26.611 40.077  -18.916 1.00 13.80 ? 38   VAL A CG2 1 
ATOM   71    N  N   . PRO A 1 39   ? 29.072 39.015  -14.909 1.00 12.10 ? 39   PRO A N   1 
ATOM   72    C  CA  . PRO A 1 39   ? 29.298 38.354  -13.615 1.00 11.73 ? 39   PRO A CA  1 
ATOM   73    C  C   . PRO A 1 39   ? 28.009 38.005  -12.915 1.00 11.91 ? 39   PRO A C   1 
ATOM   74    O  O   . PRO A 1 39   ? 27.024 38.729  -12.948 1.00 11.79 ? 39   PRO A O   1 
ATOM   75    C  CB  . PRO A 1 39   ? 30.059 39.418  -12.818 1.00 12.28 ? 39   PRO A CB  1 
ATOM   76    C  CG  . PRO A 1 39   ? 30.776 40.178  -13.896 1.00 11.00 ? 39   PRO A CG  1 
ATOM   77    C  CD  . PRO A 1 39   ? 29.752 40.335  -14.983 1.00 12.27 ? 39   PRO A CD  1 
ATOM   78    N  N   . ASN A 1 40   ? 28.013 36.829  -12.283 1.00 12.67 ? 40   ASN A N   1 
ATOM   79    C  CA  . ASN A 1 40   ? 26.864 36.430  -11.518 1.00 13.65 ? 40   ASN A CA  1 
ATOM   80    C  C   . ASN A 1 40   ? 27.142 36.803  -10.065 1.00 12.78 ? 40   ASN A C   1 
ATOM   81    O  O   . ASN A 1 40   ? 28.051 36.252  -9.428  1.00 14.19 ? 40   ASN A O   1 
ATOM   82    C  CB  . ASN A 1 40   ? 26.604 34.919  -11.706 1.00 15.42 ? 40   ASN A CB  1 
ATOM   83    C  CG  . ASN A 1 40   ? 25.419 34.427  -10.902 1.00 19.32 ? 40   ASN A CG  1 
ATOM   84    O  OD1 . ASN A 1 40   ? 24.432 35.151  -10.697 1.00 25.43 ? 40   ASN A OD1 1 
ATOM   85    N  ND2 . ASN A 1 40   ? 25.504 33.183  -10.439 1.00 26.59 ? 40   ASN A ND2 1 
ATOM   86    N  N   . VAL A 1 41   ? 26.397 37.787  -9.584  1.00 11.57 ? 41   VAL A N   1 
ATOM   87    C  CA  . VAL A 1 41   ? 26.570 38.246  -8.190  1.00 10.31 ? 41   VAL A CA  1 
ATOM   88    C  C   . VAL A 1 41   ? 25.241 38.228  -7.495  1.00 10.90 ? 41   VAL A C   1 
ATOM   89    O  O   . VAL A 1 41   ? 24.183 38.288  -8.135  1.00 11.93 ? 41   VAL A O   1 
ATOM   90    C  CB  . VAL A 1 41   ? 27.207 39.669  -8.110  1.00 9.94  ? 41   VAL A CB  1 
ATOM   91    C  CG1 . VAL A 1 41   ? 28.643 39.632  -8.526  1.00 11.77 ? 41   VAL A CG1 1 
ATOM   92    C  CG2 . VAL A 1 41   ? 26.427 40.663  -8.957  1.00 10.82 ? 41   VAL A CG2 1 
ATOM   93    N  N   . ASP A 1 42   ? 25.243 38.171  -6.174  1.00 9.42  ? 42   ASP A N   1 
ATOM   94    C  CA  . ASP A 1 42   ? 23.988 38.198  -5.447  1.00 9.02  ? 42   ASP A CA  1 
ATOM   95    C  C   . ASP A 1 42   ? 23.292 39.546  -5.486  1.00 9.42  ? 42   ASP A C   1 
ATOM   96    O  O   . ASP A 1 42   ? 22.084 39.640  -5.565  1.00 11.43 ? 42   ASP A O   1 
ATOM   97    C  CB  . ASP A 1 42   ? 24.188 37.767  -3.990  1.00 9.81  ? 42   ASP A CB  1 
ATOM   98    C  CG  . ASP A 1 42   ? 24.696 36.347  -3.876  1.00 12.55 ? 42   ASP A CG  1 
ATOM   99    O  OD1 . ASP A 1 42   ? 24.018 35.447  -4.389  1.00 16.23 ? 42   ASP A OD1 1 
ATOM   100   O  OD2 . ASP A 1 42   ? 25.750 36.107  -3.289  1.00 13.40 ? 42   ASP A OD2 1 
ATOM   101   N  N   . VAL A 1 43   ? 24.086 40.598  -5.392  1.00 7.75  ? 43   VAL A N   1 
ATOM   102   C  CA  . VAL A 1 43   ? 23.544 41.956  -5.423  1.00 7.96  ? 43   VAL A CA  1 
ATOM   103   C  C   . VAL A 1 43   ? 24.308 42.711  -6.491  1.00 7.61  ? 43   VAL A C   1 
ATOM   104   O  O   . VAL A 1 43   ? 25.542 42.814  -6.433  1.00 8.10  ? 43   VAL A O   1 
ATOM   105   C  CB  . VAL A 1 43   ? 23.701 42.677  -4.094  1.00 7.97  ? 43   VAL A CB  1 
ATOM   106   C  CG1 . VAL A 1 43   ? 23.091 44.090  -4.196  1.00 9.74  ? 43   VAL A CG1 1 
ATOM   107   C  CG2 . VAL A 1 43   ? 22.996 41.836  -2.993  1.00 10.72 ? 43   VAL A CG2 1 
ATOM   108   N  N   . GLN A 1 44   ? 23.600 43.204  -7.494  1.00 6.90  ? 44   GLN A N   1 
ATOM   109   C  CA  . GLN A 1 44   ? 24.209 44.056  -8.517  1.00 7.29  ? 44   GLN A CA  1 
ATOM   110   C  C   . GLN A 1 44   ? 23.502 45.392  -8.431  1.00 6.62  ? 44   GLN A C   1 
ATOM   111   O  O   . GLN A 1 44   ? 22.298 45.466  -8.555  1.00 7.57  ? 44   GLN A O   1 
ATOM   112   C  CB  . GLN A 1 44   ? 24.087 43.403  -9.910  1.00 8.21  ? 44   GLN A CB  1 
ATOM   113   C  CG  . GLN A 1 44   ? 25.175 43.857  -10.888 1.00 6.55  ? 44   GLN A CG  1 
ATOM   114   C  CD  . GLN A 1 44   ? 25.234 45.368  -11.021 1.00 7.77  ? 44   GLN A CD  1 
ATOM   115   O  OE1 . GLN A 1 44   ? 24.218 45.994  -11.365 1.00 9.00  ? 44   GLN A OE1 1 
ATOM   116   N  NE2 . GLN A 1 44   ? 26.414 45.957  -10.725 1.00 6.51  ? 44   GLN A NE2 1 
ATOM   117   N  N   . MET A 1 45   ? 24.238 46.466  -8.086  1.00 6.25  ? 45   MET A N   1 
ATOM   118   C  CA  . MET A 1 45   ? 23.538 47.671  -7.657  1.00 5.83  ? 45   MET A CA  1 
ATOM   119   C  C   . MET A 1 45   ? 22.633 48.328  -8.718  1.00 6.32  ? 45   MET A C   1 
ATOM   120   O  O   . MET A 1 45   ? 21.643 48.958  -8.345  1.00 6.98  ? 45   MET A O   1 
ATOM   121   C  CB  . MET A 1 45   ? 24.536 48.686  -7.082  1.00 6.39  ? 45   MET A CB  1 
ATOM   122   C  CG  . MET A 1 45   ? 25.171 48.238  -5.752  1.00 6.52  ? 45   MET A CG  1 
ATOM   123   S  SD  . MET A 1 45   ? 23.956 47.960  -4.473  1.00 9.68  ? 45   MET A SD  1 
ATOM   124   C  CE  . MET A 1 45   ? 23.225 49.636  -4.296  1.00 11.34 ? 45   MET A CE  1 
ATOM   125   N  N   . LEU A 1 46   ? 23.013 48.216  -9.983  1.00 6.49  ? 46   LEU A N   1 
ATOM   126   C  CA  . LEU A 1 46   ? 22.168 48.794  -11.043 1.00 7.09  ? 46   LEU A CA  1 
ATOM   127   C  C   . LEU A 1 46   ? 20.839 48.008  -11.079 1.00 7.67  ? 46   LEU A C   1 
ATOM   128   O  O   . LEU A 1 46   ? 19.766 48.607  -11.188 1.00 8.26  ? 46   LEU A O   1 
ATOM   129   C  CB  . LEU A 1 46   ? 22.864 48.790  -12.376 1.00 8.68  ? 46   LEU A CB  1 
ATOM   130   C  CG  . LEU A 1 46   ? 22.078 49.530  -13.465 1.00 8.80  ? 46   LEU A CG  1 
ATOM   131   C  CD1 . LEU A 1 46   ? 22.078 51.041  -13.218 1.00 9.81  ? 46   LEU A CD1 1 
ATOM   132   C  CD2 . LEU A 1 46   ? 22.614 49.174  -14.853 1.00 9.77  ? 46   LEU A CD2 1 
ATOM   133   N  N   A GLU A 1 47   ? 20.929 46.693  -10.933 0.50 8.05  ? 47   GLU A N   1 
ATOM   134   N  N   B GLU A 1 47   ? 20.923 46.682  -10.957 0.50 8.11  ? 47   GLU A N   1 
ATOM   135   C  CA  A GLU A 1 47   ? 19.733 45.855  -10.970 0.50 8.97  ? 47   GLU A CA  1 
ATOM   136   C  CA  B GLU A 1 47   ? 19.712 45.846  -10.969 0.50 8.94  ? 47   GLU A CA  1 
ATOM   137   C  C   A GLU A 1 47   ? 18.897 46.070  -9.731  0.50 9.03  ? 47   GLU A C   1 
ATOM   138   C  C   B GLU A 1 47   ? 18.889 46.140  -9.737  0.50 9.04  ? 47   GLU A C   1 
ATOM   139   O  O   A GLU A 1 47   ? 17.673 46.103  -9.800  0.50 9.69  ? 47   GLU A O   1 
ATOM   140   O  O   B GLU A 1 47   ? 17.668 46.277  -9.814  0.50 9.42  ? 47   GLU A O   1 
ATOM   141   C  CB  A GLU A 1 47   ? 20.137 44.392  -11.109 0.50 9.51  ? 47   GLU A CB  1 
ATOM   142   C  CB  B GLU A 1 47   ? 20.070 44.351  -11.013 0.50 9.65  ? 47   GLU A CB  1 
ATOM   143   C  CG  A GLU A 1 47   ? 20.778 44.112  -12.448 0.50 11.16 ? 47   GLU A CG  1 
ATOM   144   C  CG  B GLU A 1 47   ? 18.882 43.414  -11.266 0.50 10.98 ? 47   GLU A CG  1 
ATOM   145   C  CD  A GLU A 1 47   ? 21.254 42.691  -12.618 0.50 15.23 ? 47   GLU A CD  1 
ATOM   146   C  CD  B GLU A 1 47   ? 18.111 43.026  -10.006 0.50 16.67 ? 47   GLU A CD  1 
ATOM   147   O  OE1 A GLU A 1 47   ? 20.947 41.845  -11.755 0.50 17.94 ? 47   GLU A OE1 1 
ATOM   148   O  OE1 B GLU A 1 47   ? 18.671 43.131  -8.888  0.50 14.16 ? 47   GLU A OE1 1 
ATOM   149   O  OE2 A GLU A 1 47   ? 21.942 42.435  -13.629 0.50 14.52 ? 47   GLU A OE2 1 
ATOM   150   O  OE2 B GLU A 1 47   ? 16.925 42.606  -10.124 0.50 17.86 ? 47   GLU A OE2 1 
ATOM   151   N  N   . LEU A 1 48   ? 19.557 46.265  -8.594  1.00 8.63  ? 48   LEU A N   1 
ATOM   152   C  CA  . LEU A 1 48   ? 18.852 46.567  -7.356  1.00 9.20  ? 48   LEU A CA  1 
ATOM   153   C  C   . LEU A 1 48   ? 18.113 47.875  -7.453  1.00 9.03  ? 48   LEU A C   1 
ATOM   154   O  O   . LEU A 1 48   ? 16.926 47.948  -7.162  1.00 9.67  ? 48   LEU A O   1 
ATOM   155   C  CB  . LEU A 1 48   ? 19.820 46.609  -6.165  1.00 9.12  ? 48   LEU A CB  1 
ATOM   156   C  CG  . LEU A 1 48   ? 19.122 46.814  -4.821  1.00 11.05 ? 48   LEU A CG  1 
ATOM   157   C  CD1 . LEU A 1 48   ? 18.123 45.680  -4.538  1.00 16.35 ? 48   LEU A CD1 1 
ATOM   158   C  CD2 . LEU A 1 48   ? 20.125 46.972  -3.691  1.00 13.46 ? 48   LEU A CD2 1 
ATOM   159   N  N   . TYR A 1 49   ? 18.789 48.893  -7.980  1.00 8.54  ? 49   TYR A N   1 
ATOM   160   C  CA  . TYR A 1 49   ? 18.145 50.176  -8.207  1.00 7.96  ? 49   TYR A CA  1 
ATOM   161   C  C   . TYR A 1 49   ? 16.907 50.074  -9.103  1.00 9.55  ? 49   TYR A C   1 
ATOM   162   O  O   . TYR A 1 49   ? 15.896 50.735  -8.856  1.00 9.83  ? 49   TYR A O   1 
ATOM   163   C  CB  . TYR A 1 49   ? 19.179 51.161  -8.788  1.00 7.85  ? 49   TYR A CB  1 
ATOM   164   C  CG  . TYR A 1 49   ? 19.692 52.098  -7.733  1.00 9.07  ? 49   TYR A CG  1 
ATOM   165   C  CD1 . TYR A 1 49   ? 20.141 51.619  -6.489  1.00 8.02  ? 49   TYR A CD1 1 
ATOM   166   C  CD2 . TYR A 1 49   ? 19.704 53.476  -7.965  1.00 8.27  ? 49   TYR A CD2 1 
ATOM   167   C  CE1 . TYR A 1 49   ? 20.572 52.470  -5.512  1.00 9.31  ? 49   TYR A CE1 1 
ATOM   168   C  CE2 . TYR A 1 49   ? 20.148 54.365  -6.975  1.00 8.26  ? 49   TYR A CE2 1 
ATOM   169   C  CZ  . TYR A 1 49   ? 20.576 53.841  -5.751  1.00 7.65  ? 49   TYR A CZ  1 
ATOM   170   O  OH  . TYR A 1 49   ? 20.970 54.660  -4.729  1.00 8.15  ? 49   TYR A OH  1 
ATOM   171   N  N   . ASP A 1 50   ? 16.974 49.218  -10.104 1.00 9.57  ? 50   ASP A N   1 
ATOM   172   C  CA  . ASP A 1 50   ? 15.873 49.130  -11.059 1.00 13.22 ? 50   ASP A CA  1 
ATOM   173   C  C   . ASP A 1 50   ? 14.636 48.567  -10.367 1.00 13.64 ? 50   ASP A C   1 
ATOM   174   O  O   . ASP A 1 50   ? 13.503 48.938  -10.748 1.00 14.06 ? 50   ASP A O   1 
ATOM   175   C  CB  . ASP A 1 50   ? 16.306 48.283  -12.244 1.00 13.32 ? 50   ASP A CB  1 
ATOM   176   C  CG  . ASP A 1 50   ? 15.464 48.512  -13.474 1.00 18.66 ? 50   ASP A CG  1 
ATOM   177   O  OD1 . ASP A 1 50   ? 14.903 49.611  -13.634 1.00 21.67 ? 50   ASP A OD1 1 
ATOM   178   O  OD2 . ASP A 1 50   ? 15.350 47.646  -14.367 1.00 24.71 ? 50   ASP A OD2 1 
ATOM   179   N  N   A ARG A 1 51   ? 14.837 47.679  -9.388  0.50 14.14 ? 51   ARG A N   1 
ATOM   180   N  N   B ARG A 1 51   ? 14.825 47.729  -9.355  0.50 14.37 ? 51   ARG A N   1 
ATOM   181   C  CA  A ARG A 1 51   ? 13.721 47.012  -8.696  0.50 14.67 ? 51   ARG A CA  1 
ATOM   182   C  CA  B ARG A 1 51   ? 13.689 47.047  -8.740  0.50 15.08 ? 51   ARG A CA  1 
ATOM   183   C  C   A ARG A 1 51   ? 13.205 47.726  -7.447  0.50 14.79 ? 51   ARG A C   1 
ATOM   184   C  C   B ARG A 1 51   ? 13.302 47.519  -7.321  0.50 15.15 ? 51   ARG A C   1 
ATOM   185   O  O   A ARG A 1 51   ? 12.013 47.646  -7.139  0.50 13.95 ? 51   ARG A O   1 
ATOM   186   O  O   B ARG A 1 51   ? 12.280 47.089  -6.783  0.50 15.44 ? 51   ARG A O   1 
ATOM   187   C  CB  A ARG A 1 51   ? 14.016 45.522  -8.406  0.50 15.12 ? 51   ARG A CB  1 
ATOM   188   C  CB  B ARG A 1 51   ? 13.851 45.523  -8.861  0.50 15.85 ? 51   ARG A CB  1 
ATOM   189   C  CG  A ARG A 1 51   ? 15.111 45.186  -7.416  0.50 15.81 ? 51   ARG A CG  1 
ATOM   190   C  CG  B ARG A 1 51   ? 15.001 44.913  -8.092  0.50 16.23 ? 51   ARG A CG  1 
ATOM   191   C  CD  A ARG A 1 51   ? 15.216 43.667  -7.129  0.50 16.26 ? 51   ARG A CD  1 
ATOM   192   C  CD  B ARG A 1 51   ? 14.980 43.386  -8.119  0.50 16.16 ? 51   ARG A CD  1 
ATOM   193   N  NE  A ARG A 1 51   ? 16.522 43.280  -6.599  0.50 19.53 ? 51   ARG A NE  1 
ATOM   194   N  NE  B ARG A 1 51   ? 15.929 42.777  -7.194  0.50 18.84 ? 51   ARG A NE  1 
ATOM   195   C  CZ  A ARG A 1 51   ? 17.567 42.931  -7.345  0.50 18.64 ? 51   ARG A CZ  1 
ATOM   196   C  CZ  B ARG A 1 51   ? 15.750 42.675  -5.876  0.50 22.01 ? 51   ARG A CZ  1 
ATOM   197   N  NH1 A ARG A 1 51   ? 17.484 42.924  -8.668  0.50 19.31 ? 51   ARG A NH1 1 
ATOM   198   N  NH1 B ARG A 1 51   ? 14.660 43.161  -5.297  0.50 24.30 ? 51   ARG A NH1 1 
ATOM   199   N  NH2 A ARG A 1 51   ? 18.709 42.600  -6.768  0.50 20.98 ? 51   ARG A NH2 1 
ATOM   200   N  NH2 B ARG A 1 51   ? 16.678 42.088  -5.127  0.50 25.64 ? 51   ARG A NH2 1 
ATOM   201   N  N   . MET A 1 52   ? 14.083 48.422  -6.743  1.00 14.86 ? 52   MET A N   1 
ATOM   202   C  CA  A MET A 1 52   ? 13.732 49.050  -5.457  0.50 16.31 ? 52   MET A CA  1 
ATOM   203   C  CA  B MET A 1 52   ? 13.742 49.045  -5.461  0.50 14.84 ? 52   MET A CA  1 
ATOM   204   C  C   . MET A 1 52   ? 12.737 50.190  -5.560  1.00 15.17 ? 52   MET A C   1 
ATOM   205   O  O   . MET A 1 52   ? 12.797 50.866  -6.536  1.00 16.58 ? 52   MET A O   1 
ATOM   206   C  CB  A MET A 1 52   ? 15.002 49.623  -4.812  0.50 16.51 ? 52   MET A CB  1 
ATOM   207   C  CB  B MET A 1 52   ? 14.994 49.717  -4.877  0.50 15.15 ? 52   MET A CB  1 
ATOM   208   C  CG  A MET A 1 52   ? 15.836 48.627  -4.070  0.50 18.09 ? 52   MET A CG  1 
ATOM   209   C  CG  B MET A 1 52   ? 15.924 48.833  -4.207  0.50 15.02 ? 52   MET A CG  1 
ATOM   210   S  SD  A MET A 1 52   ? 17.232 49.482  -3.297  0.50 18.29 ? 52   MET A SD  1 
ATOM   211   S  SD  B MET A 1 52   ? 17.373 49.830  -3.793  0.50 11.64 ? 52   MET A SD  1 
ATOM   212   C  CE  A MET A 1 52   ? 16.364 50.467  -2.149  0.50 19.48 ? 52   MET A CE  1 
ATOM   213   C  CE  B MET A 1 52   ? 16.685 50.959  -2.538  0.50 11.70 ? 52   MET A CE  1 
ATOM   214   N  N   . SER A 1 53   ? 11.906 50.450  -4.555  1.00 16.90 ? 53   SER A N   1 
ATOM   215   C  CA  . SER A 1 53   ? 10.885 51.514  -4.680  1.00 17.68 ? 53   SER A CA  1 
ATOM   216   C  C   . SER A 1 53   ? 11.226 52.932  -4.102  1.00 17.36 ? 53   SER A C   1 
ATOM   217   O  O   . SER A 1 53   ? 10.548 53.943  -4.381  1.00 19.52 ? 53   SER A O   1 
ATOM   218   C  CB  . SER A 1 53   ? 9.549  51.017  -4.096  1.00 18.63 ? 53   SER A CB  1 
ATOM   219   O  OG  . SER A 1 53   ? 9.431  51.422  -2.754  1.00 21.78 ? 53   SER A OG  1 
ATOM   220   N  N   . PHE A 1 54   ? 12.242 52.966  -3.262  1.00 15.09 ? 54   PHE A N   1 
ATOM   221   C  CA  . PHE A 1 54   ? 12.769 54.190  -2.637  1.00 13.81 ? 54   PHE A CA  1 
ATOM   222   C  C   . PHE A 1 54   ? 11.742 54.986  -1.835  1.00 14.64 ? 54   PHE A C   1 
ATOM   223   O  O   . PHE A 1 54   ? 11.896 56.185  -1.640  1.00 14.98 ? 54   PHE A O   1 
ATOM   224   C  CB  . PHE A 1 54   ? 13.440 55.121  -3.674  1.00 12.98 ? 54   PHE A CB  1 
ATOM   225   C  CG  . PHE A 1 54   ? 14.694 54.549  -4.295  1.00 10.19 ? 54   PHE A CG  1 
ATOM   226   C  CD1 . PHE A 1 54   ? 14.626 53.736  -5.413  1.00 11.85 ? 54   PHE A CD1 1 
ATOM   227   C  CD2 . PHE A 1 54   ? 15.934 54.824  -3.753  1.00 9.93  ? 54   PHE A CD2 1 
ATOM   228   C  CE1 . PHE A 1 54   ? 15.770 53.196  -5.975  1.00 10.28 ? 54   PHE A CE1 1 
ATOM   229   C  CE2 . PHE A 1 54   ? 17.078 54.291  -4.313  1.00 11.40 ? 54   PHE A CE2 1 
ATOM   230   C  CZ  . PHE A 1 54   ? 16.997 53.490  -5.429  1.00 11.44 ? 54   PHE A CZ  1 
ATOM   231   N  N   . LYS A 1 55   ? 10.679 54.334  -1.352  1.00 14.62 ? 55   LYS A N   1 
ATOM   232   C  CA  . LYS A 1 55   ? 9.695  55.096  -0.569  1.00 16.43 ? 55   LYS A CA  1 
ATOM   233   C  C   . LYS A 1 55   ? 10.276 55.479  0.775   1.00 16.04 ? 55   LYS A C   1 
ATOM   234   O  O   . LYS A 1 55   ? 10.959 54.688  1.442   1.00 16.81 ? 55   LYS A O   1 
ATOM   235   C  CB  . LYS A 1 55   ? 8.406  54.284  -0.349  1.00 17.34 ? 55   LYS A CB  1 
ATOM   236   C  CG  . LYS A 1 55   ? 7.703  53.833  -1.609  1.00 20.20 ? 55   LYS A CG  1 
ATOM   237   C  CD  . LYS A 1 55   ? 7.487  54.954  -2.556  1.00 19.16 ? 55   LYS A CD  1 
ATOM   238   C  CE  . LYS A 1 55   ? 6.492  54.552  -3.621  1.00 23.57 ? 55   LYS A CE  1 
ATOM   239   N  NZ  . LYS A 1 55   ? 6.353  55.614  -4.641  1.00 22.99 ? 55   LYS A NZ  1 
ATOM   240   N  N   . ASP A 1 56   ? 10.015 56.713  1.169   1.00 15.50 ? 56   ASP A N   1 
ATOM   241   C  CA  . ASP A 1 56   ? 10.558 57.256  2.394   1.00 15.33 ? 56   ASP A CA  1 
ATOM   242   C  C   . ASP A 1 56   ? 9.485  57.177  3.489   1.00 16.48 ? 56   ASP A C   1 
ATOM   243   O  O   . ASP A 1 56   ? 8.838  58.165  3.818   1.00 18.84 ? 56   ASP A O   1 
ATOM   244   C  CB  . ASP A 1 56   ? 11.070 58.683  2.156   1.00 15.12 ? 56   ASP A CB  1 
ATOM   245   C  CG  . ASP A 1 56   ? 11.689 59.309  3.390   1.00 15.67 ? 56   ASP A CG  1 
ATOM   246   O  OD1 . ASP A 1 56   ? 12.177 58.596  4.306   1.00 13.73 ? 56   ASP A OD1 1 
ATOM   247   O  OD2 . ASP A 1 56   ? 11.733 60.555  3.525   1.00 16.40 ? 56   ASP A OD2 1 
ATOM   248   N  N   . ILE A 1 57   ? 9.323  55.991  4.052   1.00 17.87 ? 57   ILE A N   1 
ATOM   249   C  CA  . ILE A 1 57   ? 8.291  55.814  5.064   1.00 19.13 ? 57   ILE A CA  1 
ATOM   250   C  C   . ILE A 1 57   ? 8.897  55.838  6.458   1.00 18.90 ? 57   ILE A C   1 
ATOM   251   O  O   . ILE A 1 57   ? 10.063 55.466  6.661   1.00 18.05 ? 57   ILE A O   1 
ATOM   252   C  CB  . ILE A 1 57   ? 7.456  54.534  4.831   1.00 20.92 ? 57   ILE A CB  1 
ATOM   253   C  CG1 . ILE A 1 57   ? 8.280  53.284  5.067   1.00 23.38 ? 57   ILE A CG1 1 
ATOM   254   C  CG2 . ILE A 1 57   ? 6.798  54.517  3.434   1.00 21.58 ? 57   ILE A CG2 1 
ATOM   255   C  CD1 . ILE A 1 57   ? 7.458  52.144  5.641   1.00 26.78 ? 57   ILE A CD1 1 
ATOM   256   N  N   . ASP A 1 58   ? 8.092  56.285  7.414   1.00 18.14 ? 58   ASP A N   1 
ATOM   257   C  CA  . ASP A 1 58   ? 8.462  56.388  8.812   1.00 17.90 ? 58   ASP A CA  1 
ATOM   258   C  C   . ASP A 1 58   ? 8.463  54.986  9.403   1.00 17.10 ? 58   ASP A C   1 
ATOM   259   O  O   . ASP A 1 58   ? 7.404  54.385  9.589   1.00 17.76 ? 58   ASP A O   1 
ATOM   260   C  CB  . ASP A 1 58   ? 7.430  57.262  9.536   1.00 18.90 ? 58   ASP A CB  1 
ATOM   261   C  CG  . ASP A 1 58   ? 7.814  57.593  10.963  1.00 20.85 ? 58   ASP A CG  1 
ATOM   262   O  OD1 . ASP A 1 58   ? 8.633  56.871  11.589  1.00 20.37 ? 58   ASP A OD1 1 
ATOM   263   O  OD2 . ASP A 1 58   ? 7.329  58.587  11.566  1.00 28.51 ? 58   ASP A OD2 1 
ATOM   264   N  N   . GLY A 1 59   ? 9.649  54.457  9.695   1.00 14.47 ? 59   GLY A N   1 
ATOM   265   C  CA  . GLY A 1 59   ? 9.783  53.124  10.241  1.00 13.89 ? 59   GLY A CA  1 
ATOM   266   C  C   . GLY A 1 59   ? 9.742  53.031  11.764  1.00 12.93 ? 59   GLY A C   1 
ATOM   267   O  O   . GLY A 1 59   ? 10.000 51.958  12.277  1.00 13.79 ? 59   GLY A O   1 
ATOM   268   N  N   . GLY A 1 60   ? 9.442  54.124  12.462  1.00 12.46 ? 60   GLY A N   1 
ATOM   269   C  CA  . GLY A 1 60   ? 9.398  54.115  13.911  1.00 13.13 ? 60   GLY A CA  1 
ATOM   270   C  C   . GLY A 1 60   ? 10.672 54.725  14.487  1.00 12.12 ? 60   GLY A C   1 
ATOM   271   O  O   . GLY A 1 60   ? 11.194 55.680  13.927  1.00 13.19 ? 60   GLY A O   1 
ATOM   272   N  N   . VAL A 1 61   ? 11.147 54.212  15.620  1.00 11.66 ? 61   VAL A N   1 
ATOM   273   C  CA  . VAL A 1 61   ? 12.354 54.767  16.236  1.00 10.74 ? 61   VAL A CA  1 
ATOM   274   C  C   . VAL A 1 61   ? 13.558 54.691  15.262  1.00 10.40 ? 61   VAL A C   1 
ATOM   275   O  O   . VAL A 1 61   ? 14.381 55.611  15.194  1.00 10.21 ? 61   VAL A O   1 
ATOM   276   C  CB  . VAL A 1 61   ? 12.703 54.108  17.575  1.00 12.20 ? 61   VAL A CB  1 
ATOM   277   C  CG1 . VAL A 1 61   ? 11.563 54.380  18.592  1.00 13.03 ? 61   VAL A CG1 1 
ATOM   278   C  CG2 . VAL A 1 61   ? 12.921 52.626  17.416  1.00 12.17 ? 61   VAL A CG2 1 
ATOM   279   N  N   . TRP A 1 62   ? 13.623 53.612  14.496  1.00 9.54  ? 62   TRP A N   1 
ATOM   280   C  CA  . TRP A 1 62   ? 14.580 53.540  13.396  1.00 9.18  ? 62   TRP A CA  1 
ATOM   281   C  C   . TRP A 1 62   ? 13.822 54.170  12.244  1.00 9.86  ? 62   TRP A C   1 
ATOM   282   O  O   . TRP A 1 62   ? 13.060 53.522  11.523  1.00 10.06 ? 62   TRP A O   1 
ATOM   283   C  CB  . TRP A 1 62   ? 14.989 52.108  13.092  1.00 9.12  ? 62   TRP A CB  1 
ATOM   284   C  CG  . TRP A 1 62   ? 15.959 52.005  11.950  1.00 8.55  ? 62   TRP A CG  1 
ATOM   285   C  CD1 . TRP A 1 62   ? 16.660 53.046  11.324  1.00 8.22  ? 62   TRP A CD1 1 
ATOM   286   C  CD2 . TRP A 1 62   ? 16.324 50.817  11.268  1.00 7.61  ? 62   TRP A CD2 1 
ATOM   287   N  NE1 . TRP A 1 62   ? 17.408 52.533  10.289  1.00 8.24  ? 62   TRP A NE1 1 
ATOM   288   C  CE2 . TRP A 1 62   ? 17.235 51.178  10.235  1.00 10.03 ? 62   TRP A CE2 1 
ATOM   289   C  CE3 . TRP A 1 62   ? 15.983 49.461  11.412  1.00 7.48  ? 62   TRP A CE3 1 
ATOM   290   C  CZ2 . TRP A 1 62   ? 17.775 50.258  9.364   1.00 8.98  ? 62   TRP A CZ2 1 
ATOM   291   C  CZ3 . TRP A 1 62   ? 16.519 48.546  10.543  1.00 7.31  ? 62   TRP A CZ3 1 
ATOM   292   C  CH2 . TRP A 1 62   ? 17.426 48.945  9.526   1.00 8.46  ? 62   TRP A CH2 1 
ATOM   293   N  N   . LYS A 1 63   ? 14.034 55.468  12.048  1.00 9.67  ? 63   LYS A N   1 
ATOM   294   C  CA  . LYS A 1 63   ? 13.145 56.242  11.165  1.00 11.01 ? 63   LYS A CA  1 
ATOM   295   C  C   . LYS A 1 63   ? 13.119 55.734  9.739   1.00 11.03 ? 63   LYS A C   1 
ATOM   296   O  O   . LYS A 1 63   ? 12.089 55.766  9.065   1.00 12.02 ? 63   LYS A O   1 
ATOM   297   C  CB  . LYS A 1 63   ? 13.495 57.733  11.213  1.00 11.40 ? 63   LYS A CB  1 
ATOM   298   C  CG  . LYS A 1 63   ? 12.953 58.451  12.441  1.00 15.80 ? 63   LYS A CG  1 
ATOM   299   C  CD  . LYS A 1 63   ? 11.591 59.094  12.110  1.00 22.93 ? 63   LYS A CD  1 
ATOM   300   C  CE  . LYS A 1 63   ? 10.765 59.397  13.332  1.00 27.18 ? 63   LYS A CE  1 
ATOM   301   N  NZ  . LYS A 1 63   ? 9.828  58.261  13.580  1.00 29.08 ? 63   LYS A NZ  1 
ATOM   302   N  N   . GLN A 1 64   ? 14.259 55.243  9.281   1.00 9.23  ? 64   GLN A N   1 
ATOM   303   C  CA  . GLN A 1 64   ? 14.373 54.806  7.909   1.00 9.28  ? 64   GLN A CA  1 
ATOM   304   C  C   . GLN A 1 64   ? 14.441 53.293  7.745   1.00 9.14  ? 64   GLN A C   1 
ATOM   305   O  O   . GLN A 1 64   ? 14.777 52.792  6.677   1.00 8.70  ? 64   GLN A O   1 
ATOM   306   C  CB  . GLN A 1 64   ? 15.612 55.472  7.303   1.00 8.77  ? 64   GLN A CB  1 
ATOM   307   C  CG  . GLN A 1 64   ? 15.474 56.978  7.258   1.00 9.63  ? 64   GLN A CG  1 
ATOM   308   C  CD  . GLN A 1 64   ? 16.830 57.651  7.119   1.00 9.82  ? 64   GLN A CD  1 
ATOM   309   O  OE1 . GLN A 1 64   ? 17.769 57.303  7.835   1.00 9.34  ? 64   GLN A OE1 1 
ATOM   310   N  NE2 . GLN A 1 64   ? 16.912 58.624  6.227   1.00 8.06  ? 64   GLN A NE2 1 
ATOM   311   N  N   . GLY A 1 65   ? 14.067 52.560  8.806   1.00 9.31  ? 65   GLY A N   1 
ATOM   312   C  CA  . GLY A 1 65   ? 14.019 51.106  8.769   1.00 8.78  ? 65   GLY A CA  1 
ATOM   313   C  C   . GLY A 1 65   ? 12.669 50.556  9.209   1.00 9.74  ? 65   GLY A C   1 
ATOM   314   O  O   . GLY A 1 65   ? 11.638 50.946  8.647   1.00 11.27 ? 65   GLY A O   1 
ATOM   315   N  N   . TRP A 1 66   ? 12.696 49.658  10.196  1.00 10.58 ? 66   TRP A N   1 
ATOM   316   C  CA  . TRP A 1 66   ? 11.450 49.053  10.716  1.00 11.18 ? 66   TRP A CA  1 
ATOM   317   C  C   . TRP A 1 66   ? 11.713 48.698  12.156  1.00 11.69 ? 66   TRP A C   1 
ATOM   318   O  O   . TRP A 1 66   ? 12.847 48.844  12.648  1.00 11.50 ? 66   TRP A O   1 
ATOM   319   C  CB  . TRP A 1 66   ? 11.051 47.815  9.895   1.00 10.76 ? 66   TRP A CB  1 
ATOM   320   C  CG  . TRP A 1 66   ? 11.997 46.653  10.051  1.00 11.17 ? 66   TRP A CG  1 
ATOM   321   C  CD1 . TRP A 1 66   ? 11.880 45.615  10.941  1.00 11.93 ? 66   TRP A CD1 1 
ATOM   322   C  CD2 . TRP A 1 66   ? 13.237 46.425  9.354   1.00 10.22 ? 66   TRP A CD2 1 
ATOM   323   N  NE1 . TRP A 1 66   ? 12.956 44.767  10.842  1.00 11.80 ? 66   TRP A NE1 1 
ATOM   324   C  CE2 . TRP A 1 66   ? 13.795 45.225  9.856   1.00 10.90 ? 66   TRP A CE2 1 
ATOM   325   C  CE3 . TRP A 1 66   ? 13.920 47.099  8.331   1.00 10.51 ? 66   TRP A CE3 1 
ATOM   326   C  CZ2 . TRP A 1 66   ? 15.001 44.689  9.379   1.00 11.44 ? 66   TRP A CZ2 1 
ATOM   327   C  CZ3 . TRP A 1 66   ? 15.129 46.562  7.862   1.00 10.71 ? 66   TRP A CZ3 1 
ATOM   328   C  CH2 . TRP A 1 66   ? 15.667 45.388  8.402   1.00 10.49 ? 66   TRP A CH2 1 
ATOM   329   N  N   . ASN A 1 67   ? 10.668 48.258  12.877  1.00 12.64 ? 67   ASN A N   1 
ATOM   330   C  CA  . ASN A 1 67   ? 10.827 47.830  14.263  1.00 12.54 ? 67   ASN A CA  1 
ATOM   331   C  C   . ASN A 1 67   ? 11.434 46.427  14.294  1.00 12.75 ? 67   ASN A C   1 
ATOM   332   O  O   . ASN A 1 67   ? 10.759 45.425  13.972  1.00 12.79 ? 67   ASN A O   1 
ATOM   333   C  CB  . ASN A 1 67   ? 9.456  47.787  14.958  1.00 13.03 ? 67   ASN A CB  1 
ATOM   334   C  CG  . ASN A 1 67   ? 8.881  49.146  15.232  1.00 18.15 ? 67   ASN A CG  1 
ATOM   335   O  OD1 . ASN A 1 67   ? 9.580  50.153  15.323  1.00 20.15 ? 67   ASN A OD1 1 
ATOM   336   N  ND2 . ASN A 1 67   ? 7.562  49.172  15.406  1.00 20.06 ? 67   ASN A ND2 1 
ATOM   337   N  N   . ILE A 1 68   ? 12.709 46.347  14.649  1.00 11.30 ? 68   ILE A N   1 
ATOM   338   C  CA  . ILE A 1 68   ? 13.433 45.096  14.586  1.00 12.05 ? 68   ILE A CA  1 
ATOM   339   C  C   . ILE A 1 68   ? 12.986 44.199  15.728  1.00 13.15 ? 68   ILE A C   1 
ATOM   340   O  O   . ILE A 1 68   ? 12.941 44.648  16.869  1.00 13.48 ? 68   ILE A O   1 
ATOM   341   C  CB  . ILE A 1 68   ? 14.994 45.304  14.668  1.00 11.39 ? 68   ILE A CB  1 
ATOM   342   C  CG1 . ILE A 1 68   ? 15.526 46.137  13.488  1.00 11.96 ? 68   ILE A CG1 1 
ATOM   343   C  CG2 . ILE A 1 68   ? 15.675 43.962  14.681  1.00 13.53 ? 68   ILE A CG2 1 
ATOM   344   C  CD1 . ILE A 1 68   ? 16.976 46.598  13.699  1.00 11.60 ? 68   ILE A CD1 1 
ATOM   345   N  N   . LYS A 1 69   ? 12.743 42.929  15.404  1.00 14.65 ? 69   LYS A N   1 
ATOM   346   C  CA  . LYS A 1 69   ? 12.389 41.930  16.422  1.00 15.38 ? 69   LYS A CA  1 
ATOM   347   C  C   . LYS A 1 69   ? 13.461 40.862  16.434  1.00 15.19 ? 69   LYS A C   1 
ATOM   348   O  O   . LYS A 1 69   ? 14.043 40.554  15.409  1.00 15.18 ? 69   LYS A O   1 
ATOM   349   C  CB  . LYS A 1 69   ? 11.039 41.296  16.071  1.00 17.01 ? 69   LYS A CB  1 
ATOM   350   C  CG  . LYS A 1 69   ? 9.892  42.294  16.038  1.00 19.70 ? 69   LYS A CG  1 
ATOM   351   C  CD  . LYS A 1 69   ? 8.739  41.797  15.146  1.00 28.55 ? 69   LYS A CD  1 
ATOM   352   C  CE  . LYS A 1 69   ? 7.907  40.698  15.826  1.00 32.29 ? 69   LYS A CE  1 
ATOM   353   N  NZ  . LYS A 1 69   ? 6.752  40.250  14.977  1.00 35.19 ? 69   LYS A NZ  1 
ATOM   354   N  N   . TYR A 1 70   ? 13.693 40.271  17.597  1.00 15.31 ? 70   TYR A N   1 
ATOM   355   C  CA  . TYR A 1 70   ? 14.638 39.167  17.676  1.00 15.14 ? 70   TYR A CA  1 
ATOM   356   C  C   . TYR A 1 70   ? 14.097 38.094  18.596  1.00 16.25 ? 70   TYR A C   1 
ATOM   357   O  O   . TYR A 1 70   ? 13.255 38.382  19.453  1.00 16.76 ? 70   TYR A O   1 
ATOM   358   C  CB  . TYR A 1 70   ? 16.026 39.625  18.161  1.00 15.39 ? 70   TYR A CB  1 
ATOM   359   C  CG  . TYR A 1 70   ? 16.057 40.258  19.521  1.00 14.02 ? 70   TYR A CG  1 
ATOM   360   C  CD1 . TYR A 1 70   ? 15.878 41.614  19.663  1.00 14.60 ? 70   TYR A CD1 1 
ATOM   361   C  CD2 . TYR A 1 70   ? 16.272 39.489  20.675  1.00 14.16 ? 70   TYR A CD2 1 
ATOM   362   C  CE1 . TYR A 1 70   ? 15.921 42.221  20.894  1.00 13.96 ? 70   TYR A CE1 1 
ATOM   363   C  CE2 . TYR A 1 70   ? 16.290 40.073  21.915  1.00 14.62 ? 70   TYR A CE2 1 
ATOM   364   C  CZ  . TYR A 1 70   ? 16.122 41.450  22.027  1.00 14.11 ? 70   TYR A CZ  1 
ATOM   365   O  OH  . TYR A 1 70   ? 16.128 42.062  23.265  1.00 17.78 ? 70   TYR A OH  1 
ATOM   366   N  N   . ASP A 1 71   ? 14.603 36.881  18.406  1.00 17.83 ? 71   ASP A N   1 
ATOM   367   C  CA  . ASP A 1 71   ? 14.253 35.750  19.264  1.00 19.01 ? 71   ASP A CA  1 
ATOM   368   C  C   . ASP A 1 71   ? 15.223 35.731  20.432  1.00 19.27 ? 71   ASP A C   1 
ATOM   369   O  O   . ASP A 1 71   ? 16.405 35.522  20.222  1.00 18.00 ? 71   ASP A O   1 
ATOM   370   C  CB  . ASP A 1 71   ? 14.390 34.457  18.471  1.00 19.86 ? 71   ASP A CB  1 
ATOM   371   C  CG  . ASP A 1 71   ? 13.850 33.237  19.226  1.00 22.99 ? 71   ASP A CG  1 
ATOM   372   O  OD1 . ASP A 1 71   ? 13.640 33.302  20.463  1.00 26.08 ? 71   ASP A OD1 1 
ATOM   373   O  OD2 . ASP A 1 71   ? 13.605 32.177  18.620  1.00 27.49 ? 71   ASP A OD2 1 
ATOM   374   N  N   . PRO A 1 72   ? 14.745 35.923  21.661  1.00 20.78 ? 72   PRO A N   1 
ATOM   375   C  CA  . PRO A 1 72   ? 15.638 35.909  22.825  1.00 21.69 ? 72   PRO A CA  1 
ATOM   376   C  C   . PRO A 1 72   ? 16.410 34.583  22.949  1.00 22.06 ? 72   PRO A C   1 
ATOM   377   O  O   . PRO A 1 72   ? 17.549 34.556  23.424  1.00 23.24 ? 72   PRO A O   1 
ATOM   378   C  CB  . PRO A 1 72   ? 14.691 36.127  24.014  1.00 22.35 ? 72   PRO A CB  1 
ATOM   379   C  CG  . PRO A 1 72   ? 13.436 36.693  23.426  1.00 22.83 ? 72   PRO A CG  1 
ATOM   380   C  CD  . PRO A 1 72   ? 13.338 36.173  22.036  1.00 20.91 ? 72   PRO A CD  1 
ATOM   381   N  N   . LEU A 1 73   ? 15.826 33.503  22.435  1.00 22.06 ? 73   LEU A N   1 
ATOM   382   C  CA  . LEU A 1 73   ? 16.437 32.177  22.520  1.00 21.96 ? 73   LEU A CA  1 
ATOM   383   C  C   . LEU A 1 73   ? 17.543 31.933  21.494  1.00 20.96 ? 73   LEU A C   1 
ATOM   384   O  O   . LEU A 1 73   ? 18.194 30.885  21.503  1.00 20.22 ? 73   LEU A O   1 
ATOM   385   C  CB  . LEU A 1 73   ? 15.359 31.087  22.406  1.00 22.61 ? 73   LEU A CB  1 
ATOM   386   C  CG  . LEU A 1 73   ? 14.287 31.052  23.500  1.00 25.01 ? 73   LEU A CG  1 
ATOM   387   C  CD1 . LEU A 1 73   ? 13.382 29.846  23.269  1.00 26.46 ? 73   LEU A CD1 1 
ATOM   388   C  CD2 . LEU A 1 73   ? 14.927 30.987  24.888  1.00 25.93 ? 73   LEU A CD2 1 
ATOM   389   N  N   . LYS A 1 74   ? 17.773 32.917  20.623  1.00 19.42 ? 74   LYS A N   1 
ATOM   390   C  CA  . LYS A 1 74   ? 18.828 32.814  19.624  1.00 19.00 ? 74   LYS A CA  1 
ATOM   391   C  C   . LYS A 1 74   ? 20.221 32.660  20.225  1.00 18.34 ? 74   LYS A C   1 
ATOM   392   O  O   . LYS A 1 74   ? 21.037 31.892  19.720  1.00 19.08 ? 74   LYS A O   1 
ATOM   393   C  CB  . LYS A 1 74   ? 18.817 34.015  18.676  1.00 18.98 ? 74   LYS A CB  1 
ATOM   394   C  CG  . LYS A 1 74   ? 19.921 33.936  17.626  1.00 20.59 ? 74   LYS A CG  1 
ATOM   395   C  CD  . LYS A 1 74   ? 19.819 35.097  16.627  1.00 22.26 ? 74   LYS A CD  1 
ATOM   396   C  CE  . LYS A 1 74   ? 20.663 34.822  15.385  1.00 24.11 ? 74   LYS A CE  1 
ATOM   397   N  NZ  . LYS A 1 74   ? 20.412 35.831  14.299  1.00 27.13 ? 74   LYS A NZ  1 
ATOM   398   N  N   A TYR A 1 75   ? 20.517 33.429  21.273  0.50 17.89 ? 75   TYR A N   1 
ATOM   399   N  N   B TYR A 1 75   ? 20.476 33.398  21.293  0.50 18.19 ? 75   TYR A N   1 
ATOM   400   C  CA  A TYR A 1 75   ? 21.805 33.318  21.969  0.50 17.39 ? 75   TYR A CA  1 
ATOM   401   C  CA  B TYR A 1 75   ? 21.722 33.253  22.017  0.50 17.97 ? 75   TYR A CA  1 
ATOM   402   C  C   A TYR A 1 75   ? 21.615 32.622  23.325  0.50 18.04 ? 75   TYR A C   1 
ATOM   403   C  C   B TYR A 1 75   ? 21.474 32.386  23.224  0.50 18.19 ? 75   TYR A C   1 
ATOM   404   O  O   A TYR A 1 75   ? 20.666 32.922  24.052  0.50 18.70 ? 75   TYR A O   1 
ATOM   405   O  O   B TYR A 1 75   ? 20.367 32.328  23.754  0.50 18.21 ? 75   TYR A O   1 
ATOM   406   C  CB  A TYR A 1 75   ? 22.515 34.688  22.086  0.50 16.59 ? 75   TYR A CB  1 
ATOM   407   C  CB  B TYR A 1 75   ? 22.263 34.612  22.426  0.50 17.64 ? 75   TYR A CB  1 
ATOM   408   C  CG  A TYR A 1 75   ? 22.813 35.287  20.721  0.50 13.80 ? 75   TYR A CG  1 
ATOM   409   C  CG  B TYR A 1 75   ? 22.250 35.555  21.265  0.50 16.42 ? 75   TYR A CG  1 
ATOM   410   C  CD1 A TYR A 1 75   ? 23.818 34.760  19.917  0.50 13.43 ? 75   TYR A CD1 1 
ATOM   411   C  CD1 B TYR A 1 75   ? 23.208 35.464  20.259  0.50 13.97 ? 75   TYR A CD1 1 
ATOM   412   C  CD2 A TYR A 1 75   ? 22.055 36.350  20.209  0.50 13.94 ? 75   TYR A CD2 1 
ATOM   413   C  CD2 B TYR A 1 75   ? 21.254 36.508  21.147  0.50 16.66 ? 75   TYR A CD2 1 
ATOM   414   C  CE1 A TYR A 1 75   ? 24.066 35.269  18.647  0.50 13.74 ? 75   TYR A CE1 1 
ATOM   415   C  CE1 B TYR A 1 75   ? 23.170 36.324  19.166  0.50 15.04 ? 75   TYR A CE1 1 
ATOM   416   C  CE2 A TYR A 1 75   ? 22.301 36.866  18.934  0.50 13.92 ? 75   TYR A CE2 1 
ATOM   417   C  CE2 B TYR A 1 75   ? 21.204 37.359  20.076  0.50 15.62 ? 75   TYR A CE2 1 
ATOM   418   C  CZ  A TYR A 1 75   ? 23.312 36.315  18.167  0.50 13.32 ? 75   TYR A CZ  1 
ATOM   419   C  CZ  B TYR A 1 75   ? 22.156 37.275  19.097  0.50 16.21 ? 75   TYR A CZ  1 
ATOM   420   O  OH  A TYR A 1 75   ? 23.575 36.808  16.899  0.50 12.46 ? 75   TYR A OH  1 
ATOM   421   O  OH  B TYR A 1 75   ? 22.062 38.157  18.063  0.50 17.56 ? 75   TYR A OH  1 
ATOM   422   N  N   . ASN A 1 76   ? 22.516 31.686  23.626  1.00 18.44 ? 76   ASN A N   1 
ATOM   423   C  CA  . ASN A 1 76   ? 22.449 30.840  24.815  1.00 20.46 ? 76   ASN A CA  1 
ATOM   424   C  C   . ASN A 1 76   ? 23.860 30.541  25.289  1.00 21.13 ? 76   ASN A C   1 
ATOM   425   O  O   . ASN A 1 76   ? 24.830 31.052  24.728  1.00 21.12 ? 76   ASN A O   1 
ATOM   426   C  CB  . ASN A 1 76   ? 21.659 29.548  24.532  1.00 21.30 ? 76   ASN A CB  1 
ATOM   427   C  CG  . ASN A 1 76   ? 22.200 28.763  23.349  1.00 21.57 ? 76   ASN A CG  1 
ATOM   428   O  OD1 . ASN A 1 76   ? 23.402 28.538  23.222  1.00 24.11 ? 76   ASN A OD1 1 
ATOM   429   N  ND2 . ASN A 1 76   ? 21.293 28.321  22.480  1.00 26.94 ? 76   ASN A ND2 1 
ATOM   430   N  N   . ALA A 1 77   ? 23.988 29.703  26.319  1.00 23.22 ? 77   ALA A N   1 
ATOM   431   C  CA  . ALA A 1 77   ? 25.303 29.375  26.872  1.00 24.58 ? 77   ALA A CA  1 
ATOM   432   C  C   . ALA A 1 77   ? 26.291 28.907  25.802  1.00 24.85 ? 77   ALA A C   1 
ATOM   433   O  O   . ALA A 1 77   ? 27.485 29.183  25.883  1.00 25.59 ? 77   ALA A O   1 
ATOM   434   C  CB  . ALA A 1 77   ? 25.171 28.313  27.972  1.00 25.10 ? 77   ALA A CB  1 
ATOM   435   N  N   . HIS A 1 78   ? 25.788 28.219  24.785  1.00 25.61 ? 78   HIS A N   1 
ATOM   436   C  CA  . HIS A 1 78   ? 26.677 27.600  23.800  1.00 26.04 ? 78   HIS A CA  1 
ATOM   437   C  C   . HIS A 1 78   ? 26.949 28.509  22.601  1.00 24.78 ? 78   HIS A C   1 
ATOM   438   O  O   . HIS A 1 78   ? 27.832 28.230  21.779  1.00 25.86 ? 78   HIS A O   1 
ATOM   439   C  CB  . HIS A 1 78   ? 26.129 26.229  23.368  1.00 27.07 ? 78   HIS A CB  1 
ATOM   440   C  CG  . HIS A 1 78   ? 25.740 25.349  24.520  1.00 30.47 ? 78   HIS A CG  1 
ATOM   441   N  ND1 . HIS A 1 78   ? 26.621 25.003  25.524  1.00 33.93 ? 78   HIS A ND1 1 
ATOM   442   C  CD2 . HIS A 1 78   ? 24.564 24.749  24.827  1.00 32.83 ? 78   HIS A CD2 1 
ATOM   443   C  CE1 . HIS A 1 78   ? 26.005 24.227  26.401  1.00 34.50 ? 78   HIS A CE1 1 
ATOM   444   N  NE2 . HIS A 1 78   ? 24.755 24.058  26.001  1.00 35.34 ? 78   HIS A NE2 1 
ATOM   445   N  N   . HIS A 1 79   ? 26.211 29.617  22.540  1.00 22.39 ? 79   HIS A N   1 
ATOM   446   C  CA  . HIS A 1 79   ? 26.233 30.501  21.378  1.00 19.55 ? 79   HIS A CA  1 
ATOM   447   C  C   . HIS A 1 79   ? 25.967 31.918  21.859  1.00 16.79 ? 79   HIS A C   1 
ATOM   448   O  O   . HIS A 1 79   ? 24.825 32.358  21.928  1.00 16.97 ? 79   HIS A O   1 
ATOM   449   C  CB  . HIS A 1 79   ? 25.150 30.063  20.397  1.00 19.30 ? 79   HIS A CB  1 
ATOM   450   C  CG  . HIS A 1 79   ? 25.144 30.833  19.110  1.00 19.92 ? 79   HIS A CG  1 
ATOM   451   N  ND1 . HIS A 1 79   ? 26.138 30.714  18.163  1.00 22.91 ? 79   HIS A ND1 1 
ATOM   452   C  CD2 . HIS A 1 79   ? 24.248 31.717  18.611  1.00 20.12 ? 79   HIS A CD2 1 
ATOM   453   C  CE1 . HIS A 1 79   ? 25.864 31.511  17.143  1.00 19.66 ? 79   HIS A CE1 1 
ATOM   454   N  NE2 . HIS A 1 79   ? 24.729 32.139  17.395  1.00 21.17 ? 79   HIS A NE2 1 
ATOM   455   N  N   . LYS A 1 80   ? 27.031 32.593  22.256  1.00 15.59 ? 80   LYS A N   1 
ATOM   456   C  CA  . LYS A 1 80   ? 26.890 33.926  22.830  1.00 14.38 ? 80   LYS A CA  1 
ATOM   457   C  C   . LYS A 1 80   ? 27.058 34.998  21.757  1.00 13.77 ? 80   LYS A C   1 
ATOM   458   O  O   . LYS A 1 80   ? 27.665 34.756  20.723  1.00 14.67 ? 80   LYS A O   1 
ATOM   459   C  CB  . LYS A 1 80   ? 27.914 34.150  23.916  1.00 15.14 ? 80   LYS A CB  1 
ATOM   460   C  CG  . LYS A 1 80   ? 27.810 33.146  25.063  1.00 18.61 ? 80   LYS A CG  1 
ATOM   461   C  CD  . LYS A 1 80   ? 29.038 33.252  25.912  1.00 24.29 ? 80   LYS A CD  1 
ATOM   462   C  CE  . LYS A 1 80   ? 28.981 34.467  26.806  1.00 25.23 ? 80   LYS A CE  1 
ATOM   463   N  NZ  . LYS A 1 80   ? 30.003 34.327  27.902  1.00 26.99 ? 80   LYS A NZ  1 
ATOM   464   N  N   . LEU A 1 81   ? 26.457 36.151  21.995  1.00 11.39 ? 81   LEU A N   1 
ATOM   465   C  CA  . LEU A 1 81   ? 26.721 37.332  21.128  1.00 10.53 ? 81   LEU A CA  1 
ATOM   466   C  C   . LEU A 1 81   ? 28.017 37.991  21.598  1.00 10.66 ? 81   LEU A C   1 
ATOM   467   O  O   . LEU A 1 81   ? 28.114 38.434  22.753  1.00 10.03 ? 81   LEU A O   1 
ATOM   468   C  CB  . LEU A 1 81   ? 25.586 38.348  21.246  1.00 10.04 ? 81   LEU A CB  1 
ATOM   469   C  CG  . LEU A 1 81   ? 25.666 39.602  20.338  1.00 10.92 ? 81   LEU A CG  1 
ATOM   470   C  CD1 . LEU A 1 81   ? 25.751 39.246  18.829  1.00 12.19 ? 81   LEU A CD1 1 
ATOM   471   C  CD2 . LEU A 1 81   ? 24.516 40.570  20.636  1.00 13.29 ? 81   LEU A CD2 1 
ATOM   472   N  N   . LYS A 1 82   ? 28.999 38.072  20.716  1.00 8.96  ? 82   LYS A N   1 
ATOM   473   C  CA  A LYS A 1 82   ? 30.284 38.707  21.042  0.50 8.38  ? 82   LYS A CA  1 
ATOM   474   C  CA  B LYS A 1 82   ? 30.264 38.707  21.040  0.50 8.81  ? 82   LYS A CA  1 
ATOM   475   C  C   . LYS A 1 82   ? 30.222 40.141  20.541  1.00 8.97  ? 82   LYS A C   1 
ATOM   476   O  O   . LYS A 1 82   ? 30.024 40.337  19.356  1.00 9.98  ? 82   LYS A O   1 
ATOM   477   C  CB  A LYS A 1 82   ? 31.432 37.948  20.367  0.50 8.77  ? 82   LYS A CB  1 
ATOM   478   C  CB  B LYS A 1 82   ? 31.433 37.957  20.392  0.50 9.30  ? 82   LYS A CB  1 
ATOM   479   C  CG  A LYS A 1 82   ? 31.601 36.511  20.863  0.50 9.31  ? 82   LYS A CG  1 
ATOM   480   C  CG  B LYS A 1 82   ? 32.798 38.601  20.659  0.50 12.23 ? 82   LYS A CG  1 
ATOM   481   C  CD  A LYS A 1 82   ? 32.098 35.599  19.742  0.50 15.36 ? 82   LYS A CD  1 
ATOM   482   C  CD  B LYS A 1 82   ? 33.024 38.841  22.153  0.50 16.26 ? 82   LYS A CD  1 
ATOM   483   C  CE  A LYS A 1 82   ? 33.543 35.875  19.373  0.50 17.84 ? 82   LYS A CE  1 
ATOM   484   C  CE  B LYS A 1 82   ? 34.448 38.494  22.532  0.50 18.47 ? 82   LYS A CE  1 
ATOM   485   N  NZ  A LYS A 1 82   ? 34.050 34.906  18.367  0.50 18.64 ? 82   LYS A NZ  1 
ATOM   486   N  NZ  B LYS A 1 82   ? 35.094 37.783  21.401  0.50 18.97 ? 82   LYS A NZ  1 
ATOM   487   N  N   . VAL A 1 83   ? 30.385 41.104  21.450  1.00 7.45  ? 83   VAL A N   1 
ATOM   488   C  CA  . VAL A 1 83   ? 30.220 42.521  21.081  1.00 7.37  ? 83   VAL A CA  1 
ATOM   489   C  C   . VAL A 1 83   ? 31.556 43.248  21.234  1.00 8.06  ? 83   VAL A C   1 
ATOM   490   O  O   . VAL A 1 83   ? 32.169 43.242  22.308  1.00 8.75  ? 83   VAL A O   1 
ATOM   491   C  CB  . VAL A 1 83   ? 29.183 43.196  21.990  1.00 7.66  ? 83   VAL A CB  1 
ATOM   492   C  CG1 . VAL A 1 83   ? 29.005 44.677  21.655  1.00 9.51  ? 83   VAL A CG1 1 
ATOM   493   C  CG2 . VAL A 1 83   ? 27.832 42.498  21.834  1.00 9.47  ? 83   VAL A CG2 1 
ATOM   494   N  N   . PHE A 1 84   ? 32.002 43.888  20.149  1.00 7.52  ? 84   PHE A N   1 
ATOM   495   C  CA  . PHE A 1 84   ? 33.219 44.718  20.163  1.00 8.25  ? 84   PHE A CA  1 
ATOM   496   C  C   . PHE A 1 84   ? 32.836 46.162  20.089  1.00 7.09  ? 84   PHE A C   1 
ATOM   497   O  O   . PHE A 1 84   ? 32.305 46.613  19.073  1.00 7.55  ? 84   PHE A O   1 
ATOM   498   C  CB  . PHE A 1 84   ? 34.119 44.358  18.980  1.00 9.27  ? 84   PHE A CB  1 
ATOM   499   C  CG  . PHE A 1 84   ? 34.740 43.008  19.113  1.00 10.02 ? 84   PHE A CG  1 
ATOM   500   C  CD1 . PHE A 1 84   ? 35.787 42.822  20.009  1.00 12.90 ? 84   PHE A CD1 1 
ATOM   501   C  CD2 . PHE A 1 84   ? 34.249 41.916  18.410  1.00 12.42 ? 84   PHE A CD2 1 
ATOM   502   C  CE1 . PHE A 1 84   ? 36.388 41.567  20.169  1.00 13.01 ? 84   PHE A CE1 1 
ATOM   503   C  CE2 . PHE A 1 84   ? 34.835 40.661  18.562  1.00 14.91 ? 84   PHE A CE2 1 
ATOM   504   C  CZ  . PHE A 1 84   ? 35.929 40.491  19.417  1.00 13.62 ? 84   PHE A CZ  1 
ATOM   505   N  N   . VAL A 1 85   ? 33.098 46.885  21.174  1.00 5.87  ? 85   VAL A N   1 
ATOM   506   C  CA  . VAL A 1 85   ? 32.876 48.315  21.240  1.00 6.34  ? 85   VAL A CA  1 
ATOM   507   C  C   . VAL A 1 85   ? 34.182 48.968  20.838  1.00 5.93  ? 85   VAL A C   1 
ATOM   508   O  O   . VAL A 1 85   ? 35.196 48.767  21.498  1.00 6.50  ? 85   VAL A O   1 
ATOM   509   C  CB  . VAL A 1 85   ? 32.439 48.737  22.663  1.00 6.14  ? 85   VAL A CB  1 
ATOM   510   C  CG1 . VAL A 1 85   ? 32.262 50.245  22.746  1.00 9.49  ? 85   VAL A CG1 1 
ATOM   511   C  CG2 . VAL A 1 85   ? 31.124 48.066  22.990  1.00 7.99  ? 85   VAL A CG2 1 
ATOM   512   N  N   . VAL A 1 86   ? 34.154 49.752  19.738  1.00 6.28  ? 86   VAL A N   1 
ATOM   513   C  CA  . VAL A 1 86   ? 35.384 50.251  19.145  1.00 6.64  ? 86   VAL A CA  1 
ATOM   514   C  C   . VAL A 1 86   ? 35.459 51.774  19.262  1.00 5.91  ? 86   VAL A C   1 
ATOM   515   O  O   . VAL A 1 86   ? 34.803 52.492  18.469  1.00 5.72  ? 86   VAL A O   1 
ATOM   516   C  CB  . VAL A 1 86   ? 35.458 49.816  17.654  1.00 6.68  ? 86   VAL A CB  1 
ATOM   517   C  CG1 . VAL A 1 86   ? 36.748 50.376  17.002  1.00 8.47  ? 86   VAL A CG1 1 
ATOM   518   C  CG2 . VAL A 1 86   ? 35.403 48.274  17.564  1.00 8.56  ? 86   VAL A CG2 1 
ATOM   519   N  N   . PRO A 1 87   ? 36.218 52.294  20.219  1.00 5.37  ? 87   PRO A N   1 
ATOM   520   C  CA  . PRO A 1 87   ? 36.293 53.763  20.388  1.00 5.85  ? 87   PRO A CA  1 
ATOM   521   C  C   . PRO A 1 87   ? 37.029 54.396  19.206  1.00 5.87  ? 87   PRO A C   1 
ATOM   522   O  O   . PRO A 1 87   ? 38.039 53.841  18.709  1.00 5.79  ? 87   PRO A O   1 
ATOM   523   C  CB  . PRO A 1 87   ? 37.109 53.938  21.668  1.00 6.01  ? 87   PRO A CB  1 
ATOM   524   C  CG  . PRO A 1 87   ? 36.877 52.582  22.418  1.00 6.32  ? 87   PRO A CG  1 
ATOM   525   C  CD  . PRO A 1 87   ? 36.923 51.563  21.302  1.00 6.49  ? 87   PRO A CD  1 
ATOM   526   N  N   . HIS A 1 88   ? 36.530 55.566  18.791  1.00 4.82  ? 88   HIS A N   1 
ATOM   527   C  CA  . HIS A 1 88   ? 37.109 56.248  17.610  1.00 5.28  ? 88   HIS A CA  1 
ATOM   528   C  C   . HIS A 1 88   ? 36.845 57.743  17.703  1.00 5.71  ? 88   HIS A C   1 
ATOM   529   O  O   . HIS A 1 88   ? 36.033 58.202  18.506  1.00 5.86  ? 88   HIS A O   1 
ATOM   530   C  CB  . HIS A 1 88   ? 36.542 55.657  16.316  1.00 5.68  ? 88   HIS A CB  1 
ATOM   531   C  CG  . HIS A 1 88   ? 35.105 55.971  16.067  1.00 5.82  ? 88   HIS A CG  1 
ATOM   532   N  ND1 . HIS A 1 88   ? 34.701 57.017  15.255  1.00 5.74  ? 88   HIS A ND1 1 
ATOM   533   C  CD2 . HIS A 1 88   ? 33.970 55.359  16.490  1.00 6.40  ? 88   HIS A CD2 1 
ATOM   534   C  CE1 . HIS A 1 88   ? 33.376 57.028  15.194  1.00 6.10  ? 88   HIS A CE1 1 
ATOM   535   N  NE2 . HIS A 1 88   ? 32.915 56.038  15.943  1.00 8.50  ? 88   HIS A NE2 1 
ATOM   536   N  N   . SER A 1 89   ? 37.562 58.502  16.880  1.00 4.87  ? 89   SER A N   1 
ATOM   537   C  CA  . SER A 1 89   ? 37.487 59.942  16.873  1.00 6.64  ? 89   SER A CA  1 
ATOM   538   C  C   . SER A 1 89   ? 37.661 60.389  15.426  1.00 6.38  ? 89   SER A C   1 
ATOM   539   O  O   . SER A 1 89   ? 38.722 60.177  14.865  1.00 6.45  ? 89   SER A O   1 
ATOM   540   C  CB  . SER A 1 89   ? 38.607 60.503  17.745  1.00 7.03  ? 89   SER A CB  1 
ATOM   541   O  OG  . SER A 1 89   ? 38.547 61.914  17.701  1.00 7.25  ? 89   SER A OG  1 
ATOM   542   N  N   . HIS A 1 90   ? 36.625 60.969  14.851  1.00 5.87  ? 90   HIS A N   1 
ATOM   543   C  CA  . HIS A 1 90   ? 36.670 61.363  13.437  1.00 5.72  ? 90   HIS A CA  1 
ATOM   544   C  C   . HIS A 1 90   ? 37.332 62.745  13.363  1.00 5.83  ? 90   HIS A C   1 
ATOM   545   O  O   . HIS A 1 90   ? 36.812 63.718  13.901  1.00 6.24  ? 90   HIS A O   1 
ATOM   546   C  CB  . HIS A 1 90   ? 35.278 61.371  12.839  1.00 7.27  ? 90   HIS A CB  1 
ATOM   547   C  CG  . HIS A 1 90   ? 35.272 61.698  11.385  1.00 5.32  ? 90   HIS A CG  1 
ATOM   548   N  ND1 . HIS A 1 90   ? 35.844 60.878  10.427  1.00 6.81  ? 90   HIS A ND1 1 
ATOM   549   C  CD2 . HIS A 1 90   ? 34.766 62.763  10.726  1.00 6.91  ? 90   HIS A CD2 1 
ATOM   550   C  CE1 . HIS A 1 90   ? 35.646 61.428  9.229   1.00 6.05  ? 90   HIS A CE1 1 
ATOM   551   N  NE2 . HIS A 1 90   ? 35.012 62.580  9.383   1.00 6.52  ? 90   HIS A NE2 1 
ATOM   552   N  N   . ASN A 1 91   ? 38.518 62.808  12.758  1.00 6.18  ? 91   ASN A N   1 
ATOM   553   C  CA  . ASN A 1 91   ? 39.309 64.044  12.729  1.00 6.54  ? 91   ASN A CA  1 
ATOM   554   C  C   . ASN A 1 91   ? 39.469 64.494  11.288  1.00 7.60  ? 91   ASN A C   1 
ATOM   555   O  O   . ASN A 1 91   ? 40.352 64.012  10.560  1.00 8.97  ? 91   ASN A O   1 
ATOM   556   C  CB  . ASN A 1 91   ? 40.707 63.803  13.332  1.00 7.25  ? 91   ASN A CB  1 
ATOM   557   C  CG  . ASN A 1 91   ? 40.686 63.783  14.861  1.00 7.76  ? 91   ASN A CG  1 
ATOM   558   O  OD1 . ASN A 1 91   ? 41.309 64.621  15.542  1.00 7.93  ? 91   ASN A OD1 1 
ATOM   559   N  ND2 . ASN A 1 91   ? 39.982 62.823  15.404  1.00 7.39  ? 91   ASN A ND2 1 
ATOM   560   N  N   . ASP A 1 92   ? 38.684 65.463  10.882  1.00 6.70  ? 92   ASP A N   1 
ATOM   561   C  CA  . ASP A 1 92   ? 38.782 66.004  9.524   1.00 6.88  ? 92   ASP A CA  1 
ATOM   562   C  C   . ASP A 1 92   ? 40.036 66.837  9.351   1.00 6.54  ? 92   ASP A C   1 
ATOM   563   O  O   . ASP A 1 92   ? 40.213 67.804  10.094  1.00 6.84  ? 92   ASP A O   1 
ATOM   564   C  CB  . ASP A 1 92   ? 37.595 66.911  9.289   1.00 7.00  ? 92   ASP A CB  1 
ATOM   565   C  CG  . ASP A 1 92   ? 36.334 66.160  9.177   1.00 8.92  ? 92   ASP A CG  1 
ATOM   566   O  OD1 . ASP A 1 92   ? 36.305 65.181  8.411   1.00 9.14  ? 92   ASP A OD1 1 
ATOM   567   O  OD2 . ASP A 1 92   ? 35.333 66.466  9.845   1.00 14.27 ? 92   ASP A OD2 1 
ATOM   568   N  N   . PRO A 1 93   ? 40.894 66.519  8.376   1.00 6.34  ? 93   PRO A N   1 
ATOM   569   C  CA  . PRO A 1 93   ? 42.044 67.370  8.025   1.00 6.29  ? 93   PRO A CA  1 
ATOM   570   C  C   . PRO A 1 93   ? 41.651 68.633  7.269   1.00 7.58  ? 93   PRO A C   1 
ATOM   571   O  O   . PRO A 1 93   ? 42.054 68.851  6.124   1.00 9.14  ? 93   PRO A O   1 
ATOM   572   C  CB  . PRO A 1 93   ? 42.941 66.448  7.166   1.00 7.13  ? 93   PRO A CB  1 
ATOM   573   C  CG  . PRO A 1 93   ? 42.384 65.056  7.337   1.00 9.94  ? 93   PRO A CG  1 
ATOM   574   C  CD  . PRO A 1 93   ? 40.895 65.242  7.640   1.00 5.90  ? 93   PRO A CD  1 
ATOM   575   N  N   . GLY A 1 94   ? 40.915 69.467  7.981   1.00 6.27  ? 94   GLY A N   1 
ATOM   576   C  CA  . GLY A 1 94   ? 40.338 70.679  7.414   1.00 6.22  ? 94   GLY A CA  1 
ATOM   577   C  C   . GLY A 1 94   ? 38.848 70.462  7.131   1.00 6.92  ? 94   GLY A C   1 
ATOM   578   O  O   . GLY A 1 94   ? 38.418 69.411  6.596   1.00 7.58  ? 94   GLY A O   1 
ATOM   579   N  N   . TRP A 1 95   ? 38.061 71.426  7.549   1.00 6.33  ? 95   TRP A N   1 
ATOM   580   C  CA  . TRP A 1 95   ? 36.632 71.454  7.244   1.00 6.13  ? 95   TRP A CA  1 
ATOM   581   C  C   . TRP A 1 95   ? 36.084 72.828  7.661   1.00 7.42  ? 95   TRP A C   1 
ATOM   582   O  O   . TRP A 1 95   ? 36.004 73.752  6.836   1.00 7.14  ? 95   TRP A O   1 
ATOM   583   C  CB  . TRP A 1 95   ? 35.841 70.316  7.934   1.00 6.72  ? 95   TRP A CB  1 
ATOM   584   C  CG  . TRP A 1 95   ? 34.360 70.385  7.570   1.00 6.73  ? 95   TRP A CG  1 
ATOM   585   C  CD1 . TRP A 1 95   ? 33.819 70.797  6.391   1.00 6.75  ? 95   TRP A CD1 1 
ATOM   586   C  CD2 . TRP A 1 95   ? 33.271 69.992  8.390   1.00 8.18  ? 95   TRP A CD2 1 
ATOM   587   N  NE1 . TRP A 1 95   ? 32.445 70.722  6.446   1.00 7.51  ? 95   TRP A NE1 1 
ATOM   588   C  CE2 . TRP A 1 95   ? 32.083 70.242  7.671   1.00 7.59  ? 95   TRP A CE2 1 
ATOM   589   C  CE3 . TRP A 1 95   ? 33.169 69.481  9.693   1.00 11.53 ? 95   TRP A CE3 1 
ATOM   590   C  CZ2 . TRP A 1 95   ? 30.795 69.939  8.194   1.00 9.26  ? 95   TRP A CZ2 1 
ATOM   591   C  CZ3 . TRP A 1 95   ? 31.887 69.213  10.218  1.00 11.34 ? 95   TRP A CZ3 1 
ATOM   592   C  CH2 . TRP A 1 95   ? 30.730 69.438  9.469   1.00 11.88 ? 95   TRP A CH2 1 
ATOM   593   N  N   . ILE A 1 96   ? 35.770 72.987  8.947   1.00 7.10  ? 96   ILE A N   1 
ATOM   594   C  CA  A ILE A 1 96   ? 35.330 74.247  9.581   0.50 8.85  ? 96   ILE A CA  1 
ATOM   595   C  CA  B ILE A 1 96   ? 35.367 74.315  9.388   0.50 8.16  ? 96   ILE A CA  1 
ATOM   596   C  C   . ILE A 1 96   ? 36.505 75.069  10.082  1.00 8.68  ? 96   ILE A C   1 
ATOM   597   O  O   . ILE A 1 96   ? 36.375 76.255  10.357  1.00 10.80 ? 96   ILE A O   1 
ATOM   598   C  CB  A ILE A 1 96   ? 34.426 73.960  10.825  0.50 9.57  ? 96   ILE A CB  1 
ATOM   599   C  CB  B ILE A 1 96   ? 34.007 74.310  10.165  0.50 7.50  ? 96   ILE A CB  1 
ATOM   600   C  CG1 A ILE A 1 96   ? 33.162 73.175  10.476  0.50 11.37 ? 96   ILE A CG1 1 
ATOM   601   C  CG1 B ILE A 1 96   ? 34.089 73.557  11.488  0.50 9.51  ? 96   ILE A CG1 1 
ATOM   602   C  CG2 A ILE A 1 96   ? 34.076 75.239  11.574  0.50 9.90  ? 96   ILE A CG2 1 
ATOM   603   C  CG2 B ILE A 1 96   ? 32.929 73.661  9.299   0.50 8.47  ? 96   ILE A CG2 1 
ATOM   604   C  CD1 A ILE A 1 96   ? 32.405 73.678  9.283   0.50 13.32 ? 96   ILE A CD1 1 
ATOM   605   C  CD1 B ILE A 1 96   ? 33.016 73.989  12.477  0.50 12.63 ? 96   ILE A CD1 1 
ATOM   606   N  N   A GLN A 1 97   ? 37.629 74.393  10.298  0.50 6.96  ? 97   GLN A N   1 
ATOM   607   N  N   B GLN A 1 97   ? 37.611 74.367  10.319  0.50 7.23  ? 97   GLN A N   1 
ATOM   608   C  CA  A GLN A 1 97   ? 38.901 75.015  10.620  0.50 6.87  ? 97   GLN A CA  1 
ATOM   609   C  CA  B GLN A 1 97   ? 38.904 74.957  10.630  0.50 7.46  ? 97   GLN A CA  1 
ATOM   610   C  C   A GLN A 1 97   ? 39.951 74.419  9.689   0.50 6.32  ? 97   GLN A C   1 
ATOM   611   C  C   B GLN A 1 97   ? 39.955 74.407  9.673   0.50 6.69  ? 97   GLN A C   1 
ATOM   612   O  O   A GLN A 1 97   ? 39.687 73.403  9.025   0.50 6.24  ? 97   GLN A O   1 
ATOM   613   O  O   B GLN A 1 97   ? 39.703 73.408  8.984   0.50 6.47  ? 97   GLN A O   1 
ATOM   614   C  CB  A GLN A 1 97   ? 39.287 74.730  12.080  0.50 7.11  ? 97   GLN A CB  1 
ATOM   615   C  CB  B GLN A 1 97   ? 39.309 74.610  12.063  0.50 8.18  ? 97   GLN A CB  1 
ATOM   616   C  CG  A GLN A 1 97   ? 38.166 74.975  13.107  0.50 7.36  ? 97   GLN A CG  1 
ATOM   617   C  CG  B GLN A 1 97   ? 38.421 75.242  13.114  0.50 11.16 ? 97   GLN A CG  1 
ATOM   618   C  CD  A GLN A 1 97   ? 38.661 74.894  14.556  0.50 7.74  ? 97   GLN A CD  1 
ATOM   619   C  CD  B GLN A 1 97   ? 38.710 76.713  13.293  0.50 16.18 ? 97   GLN A CD  1 
ATOM   620   O  OE1 A GLN A 1 97   ? 39.827 75.166  14.844  0.50 12.32 ? 97   GLN A OE1 1 
ATOM   621   O  OE1 B GLN A 1 97   ? 39.426 77.094  14.213  0.50 19.06 ? 97   GLN A OE1 1 
ATOM   622   N  NE2 A GLN A 1 97   ? 37.781 74.491  15.451  0.50 11.47 ? 97   GLN A NE2 1 
ATOM   623   N  NE2 B GLN A 1 97   ? 38.177 77.543  12.406  0.50 17.73 ? 97   GLN A NE2 1 
ATOM   624   N  N   . THR A 1 98   ? 41.120 75.028  9.611   1.00 6.61  ? 98   THR A N   1 
ATOM   625   C  CA  . THR A 1 98   ? 42.186 74.455  8.799   1.00 6.00  ? 98   THR A CA  1 
ATOM   626   C  C   . THR A 1 98   ? 42.797 73.246  9.493   1.00 5.92  ? 98   THR A C   1 
ATOM   627   O  O   . THR A 1 98   ? 42.568 73.047  10.667  1.00 5.91  ? 98   THR A O   1 
ATOM   628   C  CB  . THR A 1 98   ? 43.298 75.439  8.538   1.00 6.61  ? 98   THR A CB  1 
ATOM   629   O  OG1 . THR A 1 98   ? 43.886 75.808  9.782   1.00 8.07  ? 98   THR A OG1 1 
ATOM   630   C  CG2 . THR A 1 98   ? 42.754 76.700  7.859   1.00 7.77  ? 98   THR A CG2 1 
ATOM   631   N  N   . PHE A 1 99   ? 43.567 72.465  8.745   1.00 5.58  ? 99   PHE A N   1 
ATOM   632   C  CA  . PHE A 1 99   ? 44.335 71.380  9.328   1.00 6.00  ? 99   PHE A CA  1 
ATOM   633   C  C   . PHE A 1 99   ? 45.100 71.863  10.539  1.00 6.58  ? 99   PHE A C   1 
ATOM   634   O  O   . PHE A 1 99   ? 45.026 71.261  11.595  1.00 7.23  ? 99   PHE A O   1 
ATOM   635   C  CB  . PHE A 1 99   ? 45.283 70.812  8.268   1.00 7.12  ? 99   PHE A CB  1 
ATOM   636   C  CG  . PHE A 1 99   ? 46.162 69.707  8.767   1.00 7.12  ? 99   PHE A CG  1 
ATOM   637   C  CD1 . PHE A 1 99   ? 47.396 70.009  9.325   1.00 7.72  ? 99   PHE A CD1 1 
ATOM   638   C  CD2 . PHE A 1 99   ? 45.777 68.359  8.630   1.00 6.39  ? 99   PHE A CD2 1 
ATOM   639   C  CE1 . PHE A 1 99   ? 48.223 69.003  9.816   1.00 9.00  ? 99   PHE A CE1 1 
ATOM   640   C  CE2 . PHE A 1 99   ? 46.578 67.345  9.096   1.00 7.33  ? 99   PHE A CE2 1 
ATOM   641   C  CZ  . PHE A 1 99   ? 47.825 67.659  9.673   1.00 7.63  ? 99   PHE A CZ  1 
ATOM   642   N  N   . GLU A 1 100  ? 45.849 72.943  10.409  1.00 6.67  ? 100  GLU A N   1 
ATOM   643   C  CA  . GLU A 1 100  ? 46.686 73.360  11.530  1.00 7.72  ? 100  GLU A CA  1 
ATOM   644   C  C   . GLU A 1 100  ? 45.861 73.899  12.682  1.00 7.53  ? 100  GLU A C   1 
ATOM   645   O  O   . GLU A 1 100  ? 46.206 73.639  13.845  1.00 7.93  ? 100  GLU A O   1 
ATOM   646   C  CB  . GLU A 1 100  ? 47.729 74.398  11.102  1.00 9.08  ? 100  GLU A CB  1 
ATOM   647   C  CG  . GLU A 1 100  ? 48.736 74.734  12.214  1.00 12.11 ? 100  GLU A CG  1 
ATOM   648   C  CD  . GLU A 1 100  ? 49.629 73.574  12.636  1.00 14.03 ? 100  GLU A CD  1 
ATOM   649   O  OE1 . GLU A 1 100  ? 49.752 72.548  11.900  1.00 13.38 ? 100  GLU A OE1 1 
ATOM   650   O  OE2 . GLU A 1 100  ? 50.249 73.712  13.730  1.00 17.56 ? 100  GLU A OE2 1 
ATOM   651   N  N   . GLU A 1 101  ? 44.741 74.572  12.405  1.00 6.88  ? 101  GLU A N   1 
ATOM   652   C  CA  . GLU A 1 101  ? 43.877 75.011  13.489  1.00 8.82  ? 101  GLU A CA  1 
ATOM   653   C  C   . GLU A 1 101  ? 43.281 73.860  14.257  1.00 8.19  ? 101  GLU A C   1 
ATOM   654   O  O   . GLU A 1 101  ? 43.273 73.862  15.494  1.00 8.64  ? 101  GLU A O   1 
ATOM   655   C  CB  . GLU A 1 101  ? 42.745 75.874  12.944  1.00 8.52  ? 101  GLU A CB  1 
ATOM   656   C  CG  . GLU A 1 101  ? 43.176 77.280  12.543  1.00 12.78 ? 101  GLU A CG  1 
ATOM   657   C  CD  . GLU A 1 101  ? 42.148 78.018  11.670  1.00 14.23 ? 101  GLU A CD  1 
ATOM   658   O  OE1 . GLU A 1 101  ? 41.176 77.434  11.125  1.00 10.75 ? 101  GLU A OE1 1 
ATOM   659   O  OE2 . GLU A 1 101  ? 42.308 79.261  11.524  1.00 18.61 ? 101  GLU A OE2 1 
ATOM   660   N  N   . TYR A 1 102  ? 42.734 72.871  13.569  1.00 7.13  ? 102  TYR A N   1 
ATOM   661   C  CA  . TYR A 1 102  ? 42.236 71.701  14.267  1.00 7.07  ? 102  TYR A CA  1 
ATOM   662   C  C   . TYR A 1 102  ? 43.349 70.972  15.022  1.00 6.78  ? 102  TYR A C   1 
ATOM   663   O  O   . TYR A 1 102  ? 43.115 70.431  16.090  1.00 7.40  ? 102  TYR A O   1 
ATOM   664   C  CB  . TYR A 1 102  ? 41.669 70.717  13.264  1.00 6.47  ? 102  TYR A CB  1 
ATOM   665   C  CG  . TYR A 1 102  ? 40.251 70.907  12.801  1.00 5.91  ? 102  TYR A CG  1 
ATOM   666   C  CD1 . TYR A 1 102  ? 39.208 71.154  13.678  1.00 6.55  ? 102  TYR A CD1 1 
ATOM   667   C  CD2 . TYR A 1 102  ? 39.950 70.768  11.471  1.00 5.82  ? 102  TYR A CD2 1 
ATOM   668   C  CE1 . TYR A 1 102  ? 37.907 71.262  13.211  1.00 7.16  ? 102  TYR A CE1 1 
ATOM   669   C  CE2 . TYR A 1 102  ? 38.694 70.856  11.019  1.00 6.30  ? 102  TYR A CE2 1 
ATOM   670   C  CZ  . TYR A 1 102  ? 37.673 71.111  11.874  1.00 6.38  ? 102  TYR A CZ  1 
ATOM   671   O  OH  . TYR A 1 102  ? 36.414 71.216  11.366  1.00 8.27  ? 102  TYR A OH  1 
ATOM   672   N  N   . TYR A 1 103  ? 44.534 70.905  14.432  1.00 6.83  ? 103  TYR A N   1 
ATOM   673   C  CA  . TYR A 1 103  ? 45.606 70.227  15.138  1.00 7.59  ? 103  TYR A CA  1 
ATOM   674   C  C   . TYR A 1 103  ? 45.895 70.902  16.462  1.00 8.12  ? 103  TYR A C   1 
ATOM   675   O  O   . TYR A 1 103  ? 46.043 70.222  17.492  1.00 8.11  ? 103  TYR A O   1 
ATOM   676   C  CB  . TYR A 1 103  ? 46.865 70.148  14.279  1.00 8.40  ? 103  TYR A CB  1 
ATOM   677   C  CG  . TYR A 1 103  ? 47.992 69.505  15.036  1.00 7.80  ? 103  TYR A CG  1 
ATOM   678   C  CD1 . TYR A 1 103  ? 48.011 68.138  15.299  1.00 8.57  ? 103  TYR A CD1 1 
ATOM   679   C  CD2 . TYR A 1 103  ? 49.029 70.296  15.534  1.00 7.60  ? 103  TYR A CD2 1 
ATOM   680   C  CE1 . TYR A 1 103  ? 49.028 67.575  16.033  1.00 8.57  ? 103  TYR A CE1 1 
ATOM   681   C  CE2 . TYR A 1 103  ? 50.052 69.743  16.283  1.00 8.40  ? 103  TYR A CE2 1 
ATOM   682   C  CZ  . TYR A 1 103  ? 50.038 68.390  16.536  1.00 7.86  ? 103  TYR A CZ  1 
ATOM   683   O  OH  . TYR A 1 103  ? 51.044 67.789  17.276  1.00 10.14 ? 103  TYR A OH  1 
ATOM   684   N  N   . GLN A 1 104  ? 45.963 72.223  16.440  1.00 8.74  ? 104  GLN A N   1 
ATOM   685   C  CA  . GLN A 1 104  ? 46.303 72.953  17.662  1.00 9.61  ? 104  GLN A CA  1 
ATOM   686   C  C   . GLN A 1 104  ? 45.184 72.952  18.669  1.00 10.56 ? 104  GLN A C   1 
ATOM   687   O  O   . GLN A 1 104  ? 45.452 72.890  19.888  1.00 12.06 ? 104  GLN A O   1 
ATOM   688   C  CB  . GLN A 1 104  ? 46.666 74.403  17.319  1.00 10.02 ? 104  GLN A CB  1 
ATOM   689   C  CG  . GLN A 1 104  ? 47.979 74.536  16.580  1.00 11.20 ? 104  GLN A CG  1 
ATOM   690   C  CD  . GLN A 1 104  ? 49.166 74.037  17.393  1.00 12.58 ? 104  GLN A CD  1 
ATOM   691   O  OE1 . GLN A 1 104  ? 49.159 74.086  18.628  1.00 14.66 ? 104  GLN A OE1 1 
ATOM   692   N  NE2 . GLN A 1 104  ? 50.184 73.572  16.704  1.00 13.19 ? 104  GLN A NE2 1 
ATOM   693   N  N   A HIS A 1 105  ? 43.940 73.035  18.207  0.50 10.24 ? 105  HIS A N   1 
ATOM   694   N  N   B HIS A 1 105  ? 43.948 73.065  18.211  0.50 10.61 ? 105  HIS A N   1 
ATOM   695   C  CA  A HIS A 1 105  ? 42.767 73.191  19.093  0.50 10.31 ? 105  HIS A CA  1 
ATOM   696   C  CA  B HIS A 1 105  ? 42.829 73.170  19.143  0.50 11.06 ? 105  HIS A CA  1 
ATOM   697   C  C   A HIS A 1 105  ? 42.138 71.884  19.543  0.50 10.43 ? 105  HIS A C   1 
ATOM   698   C  C   B HIS A 1 105  ? 42.391 71.826  19.674  0.50 10.84 ? 105  HIS A C   1 
ATOM   699   O  O   A HIS A 1 105  ? 41.412 71.856  20.540  0.50 10.80 ? 105  HIS A O   1 
ATOM   700   O  O   B HIS A 1 105  ? 42.079 71.721  20.866  0.50 10.55 ? 105  HIS A O   1 
ATOM   701   C  CB  A HIS A 1 105  ? 41.674 74.014  18.406  0.50 11.54 ? 105  HIS A CB  1 
ATOM   702   C  CB  B HIS A 1 105  ? 41.631 73.875  18.517  0.50 12.60 ? 105  HIS A CB  1 
ATOM   703   C  CG  A HIS A 1 105  ? 42.119 75.376  17.983  0.50 12.15 ? 105  HIS A CG  1 
ATOM   704   C  CG  B HIS A 1 105  ? 40.675 74.416  19.531  0.50 15.85 ? 105  HIS A CG  1 
ATOM   705   N  ND1 A HIS A 1 105  ? 41.568 76.034  16.906  0.50 14.03 ? 105  HIS A ND1 1 
ATOM   706   N  ND1 B HIS A 1 105  ? 39.500 73.777  19.865  0.50 19.21 ? 105  HIS A ND1 1 
ATOM   707   C  CD2 A HIS A 1 105  ? 43.072 76.194  18.481  0.50 14.43 ? 105  HIS A CD2 1 
ATOM   708   C  CD2 B HIS A 1 105  ? 40.740 75.517  20.316  0.50 19.51 ? 105  HIS A CD2 1 
ATOM   709   C  CE1 A HIS A 1 105  ? 42.159 77.207  16.764  0.50 15.50 ? 105  HIS A CE1 1 
ATOM   710   C  CE1 B HIS A 1 105  ? 38.870 74.475  20.794  0.50 19.37 ? 105  HIS A CE1 1 
ATOM   711   N  NE2 A HIS A 1 105  ? 43.080 77.328  17.706  0.50 15.15 ? 105  HIS A NE2 1 
ATOM   712   N  NE2 B HIS A 1 105  ? 39.601 75.536  21.084  0.50 22.28 ? 105  HIS A NE2 1 
ATOM   713   N  N   . ASP A 1 106  ? 42.389 70.811  18.795  1.00 9.99  ? 106  ASP A N   1 
ATOM   714   C  CA  . ASP A 1 106  ? 41.743 69.531  19.083  1.00 10.27 ? 106  ASP A CA  1 
ATOM   715   C  C   . ASP A 1 106  ? 42.649 68.322  18.993  1.00 8.69  ? 106  ASP A C   1 
ATOM   716   O  O   . ASP A 1 106  ? 42.839 67.618  19.987  1.00 8.66  ? 106  ASP A O   1 
ATOM   717   C  CB  . ASP A 1 106  ? 40.529 69.329  18.156  1.00 10.87 ? 106  ASP A CB  1 
ATOM   718   C  CG  . ASP A 1 106  ? 39.488 70.384  18.359  1.00 15.98 ? 106  ASP A CG  1 
ATOM   719   O  OD1 . ASP A 1 106  ? 38.687 70.229  19.307  1.00 18.27 ? 106  ASP A OD1 1 
ATOM   720   O  OD2 . ASP A 1 106  ? 39.423 71.397  17.616  1.00 19.72 ? 106  ASP A OD2 1 
ATOM   721   N  N   . THR A 1 107  ? 43.189 68.061  17.807  1.00 7.98  ? 107  THR A N   1 
ATOM   722   C  CA  . THR A 1 107  ? 43.785 66.764  17.529  1.00 7.06  ? 107  THR A CA  1 
ATOM   723   C  C   . THR A 1 107  ? 45.011 66.493  18.367  1.00 7.81  ? 107  THR A C   1 
ATOM   724   O  O   . THR A 1 107  ? 45.228 65.361  18.784  1.00 6.33  ? 107  THR A O   1 
ATOM   725   C  CB  . THR A 1 107  ? 44.079 66.629  16.022  1.00 7.69  ? 107  THR A CB  1 
ATOM   726   O  OG1 . THR A 1 107  ? 42.843 66.877  15.334  1.00 8.67  ? 107  THR A OG1 1 
ATOM   727   C  CG2 . THR A 1 107  ? 44.564 65.182  15.646  1.00 8.29  ? 107  THR A CG2 1 
ATOM   728   N  N   . LYS A 1 108  ? 45.825 67.505  18.618  1.00 6.86  ? 108  LYS A N   1 
ATOM   729   C  CA  . LYS A 1 108  ? 47.024 67.217  19.394  1.00 7.85  ? 108  LYS A CA  1 
ATOM   730   C  C   . LYS A 1 108  ? 46.648 66.789  20.805  1.00 7.37  ? 108  LYS A C   1 
ATOM   731   O  O   . LYS A 1 108  ? 47.341 65.967  21.404  1.00 8.19  ? 108  LYS A O   1 
ATOM   732   C  CB  . LYS A 1 108  ? 48.010 68.401  19.393  1.00 8.06  ? 108  LYS A CB  1 
ATOM   733   C  CG  . LYS A 1 108  ? 47.716 69.547  20.317  1.00 11.14 ? 108  LYS A CG  1 
ATOM   734   C  CD  . LYS A 1 108  ? 48.838 70.585  20.225  1.00 11.13 ? 108  LYS A CD  1 
ATOM   735   C  CE  . LYS A 1 108  ? 48.516 71.776  21.087  1.00 15.56 ? 108  LYS A CE  1 
ATOM   736   N  NZ  . LYS A 1 108  ? 49.626 72.786  20.947  1.00 16.09 ? 108  LYS A NZ  1 
ATOM   737   N  N   . HIS A 1 109  ? 45.545 67.335  21.299  1.00 7.51  ? 109  HIS A N   1 
ATOM   738   C  CA  . HIS A 1 109  ? 45.027 66.954  22.631  1.00 8.00  ? 109  HIS A CA  1 
ATOM   739   C  C   . HIS A 1 109  ? 44.415 65.583  22.633  1.00 8.08  ? 109  HIS A C   1 
ATOM   740   O  O   . HIS A 1 109  ? 44.642 64.789  23.540  1.00 7.70  ? 109  HIS A O   1 
ATOM   741   C  CB  . HIS A 1 109  ? 44.041 68.004  23.130  1.00 9.29  ? 109  HIS A CB  1 
ATOM   742   C  CG  . HIS A 1 109  ? 44.653 69.358  23.201  1.00 11.22 ? 109  HIS A CG  1 
ATOM   743   N  ND1 . HIS A 1 109  ? 45.684 69.654  24.070  1.00 17.15 ? 109  HIS A ND1 1 
ATOM   744   C  CD2 . HIS A 1 109  ? 44.466 70.459  22.440  1.00 14.64 ? 109  HIS A CD2 1 
ATOM   745   C  CE1 . HIS A 1 109  ? 46.059 70.909  23.879  1.00 15.78 ? 109  HIS A CE1 1 
ATOM   746   N  NE2 . HIS A 1 109  ? 45.333 71.420  22.900  1.00 16.38 ? 109  HIS A NE2 1 
ATOM   747   N  N   . ILE A 1 110  ? 43.669 65.244  21.588  1.00 7.42  ? 110  ILE A N   1 
ATOM   748   C  CA  . ILE A 1 110  ? 43.151 63.884  21.469  1.00 7.09  ? 110  ILE A CA  1 
ATOM   749   C  C   . ILE A 1 110  ? 44.270 62.854  21.471  1.00 6.85  ? 110  ILE A C   1 
ATOM   750   O  O   . ILE A 1 110  ? 44.200 61.853  22.182  1.00 7.61  ? 110  ILE A O   1 
ATOM   751   C  CB  . ILE A 1 110  ? 42.305 63.772  20.157  1.00 7.02  ? 110  ILE A CB  1 
ATOM   752   C  CG1 . ILE A 1 110  ? 41.092 64.699  20.241  1.00 6.39  ? 110  ILE A CG1 1 
ATOM   753   C  CG2 . ILE A 1 110  ? 41.941 62.314  19.812  1.00 7.32  ? 110  ILE A CG2 1 
ATOM   754   C  CD1 . ILE A 1 110  ? 40.390 64.969  18.889  1.00 7.70  ? 110  ILE A CD1 1 
ATOM   755   N  N   . LEU A 1 111  ? 45.266 63.060  20.627  1.00 6.72  ? 111  LEU A N   1 
ATOM   756   C  CA  . LEU A 1 111  ? 46.320 62.086  20.532  1.00 6.44  ? 111  LEU A CA  1 
ATOM   757   C  C   . LEU A 1 111  ? 47.188 61.996  21.788  1.00 6.79  ? 111  LEU A C   1 
ATOM   758   O  O   . LEU A 1 111  ? 47.578 60.921  22.203  1.00 7.36  ? 111  LEU A O   1 
ATOM   759   C  CB  . LEU A 1 111  ? 47.171 62.355  19.277  1.00 7.64  ? 111  LEU A CB  1 
ATOM   760   C  CG  . LEU A 1 111  ? 46.419 62.050  17.995  1.00 7.91  ? 111  LEU A CG  1 
ATOM   761   C  CD1 . LEU A 1 111  ? 47.255 62.540  16.854  1.00 9.12  ? 111  LEU A CD1 1 
ATOM   762   C  CD2 . LEU A 1 111  ? 46.247 60.562  17.933  1.00 9.57  ? 111  LEU A CD2 1 
ATOM   763   N  N   . SER A 1 112  ? 47.441 63.135  22.415  1.00 6.95  ? 112  SER A N   1 
ATOM   764   C  CA  A SER A 1 112  ? 48.235 63.118  23.632  0.50 8.38  ? 112  SER A CA  1 
ATOM   765   C  CA  B SER A 1 112  ? 48.192 63.202  23.672  0.50 8.75  ? 112  SER A CA  1 
ATOM   766   C  C   . SER A 1 112  ? 47.454 62.447  24.767  1.00 8.84  ? 112  SER A C   1 
ATOM   767   O  O   . SER A 1 112  ? 48.028 61.662  25.542  1.00 9.65  ? 112  SER A O   1 
ATOM   768   C  CB  A SER A 1 112  ? 48.671 64.532  24.002  0.50 8.63  ? 112  SER A CB  1 
ATOM   769   C  CB  B SER A 1 112  ? 48.345 64.668  24.099  0.50 9.08  ? 112  SER A CB  1 
ATOM   770   O  OG  A SER A 1 112  ? 49.344 64.536  25.245  0.50 10.25 ? 112  SER A OG  1 
ATOM   771   O  OG  B SER A 1 112  ? 49.233 65.337  23.237  0.50 12.34 ? 112  SER A OG  1 
ATOM   772   N  N   . ASN A 1 113  ? 46.153 62.698  24.845  1.00 8.62  ? 113  ASN A N   1 
ATOM   773   C  CA  . ASN A 1 113  ? 45.366 62.068  25.895  1.00 9.00  ? 113  ASN A CA  1 
ATOM   774   C  C   . ASN A 1 113  ? 45.099 60.608  25.577  1.00 8.89  ? 113  ASN A C   1 
ATOM   775   O  O   . ASN A 1 113  ? 45.029 59.780  26.503  1.00 9.34  ? 113  ASN A O   1 
ATOM   776   C  CB  . ASN A 1 113  ? 44.128 62.895  26.227  1.00 9.38  ? 113  ASN A CB  1 
ATOM   777   C  CG  . ASN A 1 113  ? 44.505 64.214  26.884  1.00 11.79 ? 113  ASN A CG  1 
ATOM   778   O  OD1 . ASN A 1 113  ? 45.596 64.344  27.489  1.00 17.14 ? 113  ASN A OD1 1 
ATOM   779   N  ND2 . ASN A 1 113  ? 43.661 65.200  26.744  1.00 12.69 ? 113  ASN A ND2 1 
ATOM   780   N  N   . ALA A 1 114  ? 45.033 60.229  24.291  1.00 8.53  ? 114  ALA A N   1 
ATOM   781   C  CA  . ALA A 1 114  ? 44.919 58.817  23.941  1.00 9.12  ? 114  ALA A CA  1 
ATOM   782   C  C   . ALA A 1 114  ? 46.161 58.062  24.395  1.00 8.88  ? 114  ALA A C   1 
ATOM   783   O  O   . ALA A 1 114  ? 46.088 56.939  24.942  1.00 9.31  ? 114  ALA A O   1 
ATOM   784   C  CB  . ALA A 1 114  ? 44.735 58.632  22.432  1.00 9.01  ? 114  ALA A CB  1 
ATOM   785   N  N   . LEU A 1 115  ? 47.318 58.676  24.192  1.00 8.97  ? 115  LEU A N   1 
ATOM   786   C  CA  . LEU A 1 115  ? 48.540 58.020  24.583  1.00 9.93  ? 115  LEU A CA  1 
ATOM   787   C  C   . LEU A 1 115  ? 48.544 57.753  26.086  1.00 10.47 ? 115  LEU A C   1 
ATOM   788   O  O   . LEU A 1 115  ? 48.813 56.637  26.519  1.00 11.73 ? 115  LEU A O   1 
ATOM   789   C  CB  . LEU A 1 115  ? 49.731 58.871  24.165  1.00 9.48  ? 115  LEU A CB  1 
ATOM   790   C  CG  . LEU A 1 115  ? 51.135 58.391  24.544  1.00 11.01 ? 115  LEU A CG  1 
ATOM   791   C  CD1 . LEU A 1 115  ? 51.345 56.931  24.165  1.00 14.43 ? 115  LEU A CD1 1 
ATOM   792   C  CD2 . LEU A 1 115  ? 52.199 59.275  23.880  1.00 13.19 ? 115  LEU A CD2 1 
ATOM   793   N  N   . ARG A 1 116  ? 48.159 58.760  26.848  1.00 10.63 ? 116  ARG A N   1 
ATOM   794   C  CA  . ARG A 1 116  ? 48.162 58.634  28.302  1.00 11.36 ? 116  ARG A CA  1 
ATOM   795   C  C   . ARG A 1 116  ? 47.122 57.614  28.766  1.00 10.24 ? 116  ARG A C   1 
ATOM   796   O  O   . ARG A 1 116  ? 47.418 56.715  29.565  1.00 10.97 ? 116  ARG A O   1 
ATOM   797   C  CB  . ARG A 1 116  ? 47.909 59.998  28.925  1.00 12.34 ? 116  ARG A CB  1 
ATOM   798   C  CG  . ARG A 1 116  ? 47.466 59.955  30.380  1.00 17.33 ? 116  ARG A CG  1 
ATOM   799   C  CD  . ARG A 1 116  ? 46.738 61.224  30.796  1.00 24.31 ? 116  ARG A CD  1 
ATOM   800   N  NE  . ARG A 1 116  ? 46.244 61.154  32.172  1.00 28.44 ? 116  ARG A NE  1 
ATOM   801   C  CZ  . ARG A 1 116  ? 45.879 62.212  32.889  1.00 31.77 ? 116  ARG A CZ  1 
ATOM   802   N  NH1 . ARG A 1 116  ? 45.957 63.432  32.369  1.00 32.87 ? 116  ARG A NH1 1 
ATOM   803   N  NH2 . ARG A 1 116  ? 45.438 62.046  34.137  1.00 33.78 ? 116  ARG A NH2 1 
ATOM   804   N  N   . HIS A 1 117  ? 45.905 57.732  28.270  1.00 9.95  ? 117  HIS A N   1 
ATOM   805   C  CA  A HIS A 1 117  ? 44.851 56.870  28.772  0.50 9.93  ? 117  HIS A CA  1 
ATOM   806   C  CA  B HIS A 1 117  ? 44.822 56.887  28.740  0.50 10.42 ? 117  HIS A CA  1 
ATOM   807   C  C   . HIS A 1 117  ? 44.985 55.436  28.333  1.00 10.17 ? 117  HIS A C   1 
ATOM   808   O  O   . HIS A 1 117  ? 44.653 54.541  29.101  1.00 9.76  ? 117  HIS A O   1 
ATOM   809   C  CB  A HIS A 1 117  ? 43.464 57.413  28.457  0.50 9.85  ? 117  HIS A CB  1 
ATOM   810   C  CB  B HIS A 1 117  ? 43.480 57.402  28.245  0.50 10.71 ? 117  HIS A CB  1 
ATOM   811   C  CG  A HIS A 1 117  ? 43.127 58.639  29.239  0.50 9.04  ? 117  HIS A CG  1 
ATOM   812   C  CG  B HIS A 1 117  ? 42.338 57.077  29.153  0.50 12.23 ? 117  HIS A CG  1 
ATOM   813   N  ND1 A HIS A 1 117  ? 42.482 58.596  30.458  0.50 10.32 ? 117  HIS A ND1 1 
ATOM   814   N  ND1 B HIS A 1 117  ? 42.039 57.826  30.274  0.50 12.31 ? 117  HIS A ND1 1 
ATOM   815   C  CD2 A HIS A 1 117  ? 43.371 59.945  28.988  0.50 10.10 ? 117  HIS A CD2 1 
ATOM   816   C  CD2 B HIS A 1 117  ? 41.423 56.079  29.116  0.50 12.67 ? 117  HIS A CD2 1 
ATOM   817   C  CE1 A HIS A 1 117  ? 42.343 59.824  30.923  0.50 9.42  ? 117  HIS A CE1 1 
ATOM   818   C  CE1 B HIS A 1 117  ? 40.985 57.307  30.881  0.50 13.68 ? 117  HIS A CE1 1 
ATOM   819   N  NE2 A HIS A 1 117  ? 42.868 60.664  30.047  0.50 8.92  ? 117  HIS A NE2 1 
ATOM   820   N  NE2 B HIS A 1 117  ? 40.587 56.254  30.194  0.50 11.48 ? 117  HIS A NE2 1 
ATOM   821   N  N   . LEU A 1 118  ? 45.453 55.179  27.114  1.00 8.92  ? 118  LEU A N   1 
ATOM   822   C  CA  . LEU A 1 118  ? 45.684 53.803  26.678  1.00 9.47  ? 118  LEU A CA  1 
ATOM   823   C  C   . LEU A 1 118  ? 46.847 53.182  27.450  1.00 9.61  ? 118  LEU A C   1 
ATOM   824   O  O   . LEU A 1 118  ? 46.775 52.016  27.900  1.00 11.16 ? 118  LEU A O   1 
ATOM   825   C  CB  . LEU A 1 118  ? 45.954 53.729  25.153  1.00 9.05  ? 118  LEU A CB  1 
ATOM   826   C  CG  . LEU A 1 118  ? 44.715 54.144  24.321  1.00 11.07 ? 118  LEU A CG  1 
ATOM   827   C  CD1 . LEU A 1 118  ? 45.103 54.444  22.840  1.00 12.32 ? 118  LEU A CD1 1 
ATOM   828   C  CD2 . LEU A 1 118  ? 43.604 53.169  24.418  1.00 11.83 ? 118  LEU A CD2 1 
ATOM   829   N  N   . HIS A 1 119  ? 47.910 53.939  27.637  1.00 10.65 ? 119  HIS A N   1 
ATOM   830   C  CA  . HIS A 1 119  ? 49.044 53.455  28.409  1.00 11.46 ? 119  HIS A CA  1 
ATOM   831   C  C   . HIS A 1 119  ? 48.561 53.031  29.804  1.00 12.53 ? 119  HIS A C   1 
ATOM   832   O  O   . HIS A 1 119  ? 48.903 51.982  30.275  1.00 13.64 ? 119  HIS A O   1 
ATOM   833   C  CB  . HIS A 1 119  ? 50.093 54.562  28.504  1.00 13.42 ? 119  HIS A CB  1 
ATOM   834   C  CG  . HIS A 1 119  ? 51.231 54.266  29.426  1.00 17.87 ? 119  HIS A CG  1 
ATOM   835   N  ND1 . HIS A 1 119  ? 52.272 53.434  29.083  1.00 23.46 ? 119  HIS A ND1 1 
ATOM   836   C  CD2 . HIS A 1 119  ? 51.522 54.740  30.661  1.00 20.91 ? 119  HIS A CD2 1 
ATOM   837   C  CE1 . HIS A 1 119  ? 53.134 53.377  30.081  1.00 23.29 ? 119  HIS A CE1 1 
ATOM   838   N  NE2 . HIS A 1 119  ? 52.709 54.165  31.045  1.00 22.41 ? 119  HIS A NE2 1 
ATOM   839   N  N   . ASP A 1 120  ? 47.735 53.854  30.424  1.00 12.53 ? 120  ASP A N   1 
ATOM   840   C  CA  . ASP A 1 120  ? 47.305 53.605  31.814  1.00 13.76 ? 120  ASP A CA  1 
ATOM   841   C  C   . ASP A 1 120  ? 46.208 52.545  31.964  1.00 13.92 ? 120  ASP A C   1 
ATOM   842   O  O   . ASP A 1 120  ? 45.975 52.045  33.069  1.00 14.76 ? 120  ASP A O   1 
ATOM   843   C  CB  . ASP A 1 120  ? 46.846 54.918  32.461  1.00 14.47 ? 120  ASP A CB  1 
ATOM   844   C  CG  . ASP A 1 120  ? 48.002 55.838  32.789  1.00 17.34 ? 120  ASP A CG  1 
ATOM   845   O  OD1 . ASP A 1 120  ? 49.174 55.396  32.729  1.00 21.82 ? 120  ASP A OD1 1 
ATOM   846   O  OD2 . ASP A 1 120  ? 47.828 57.028  33.111  1.00 21.76 ? 120  ASP A OD2 1 
ATOM   847   N  N   . ASN A 1 121  ? 45.507 52.211  30.888  1.00 12.60 ? 121  ASN A N   1 
ATOM   848   C  CA  . ASN A 1 121  ? 44.331 51.339  30.937  1.00 12.01 ? 121  ASN A CA  1 
ATOM   849   C  C   . ASN A 1 121  ? 44.453 50.258  29.897  1.00 12.86 ? 121  ASN A C   1 
ATOM   850   O  O   . ASN A 1 121  ? 43.971 50.420  28.773  1.00 11.96 ? 121  ASN A O   1 
ATOM   851   C  CB  . ASN A 1 121  ? 43.029 52.115  30.728  1.00 11.53 ? 121  ASN A CB  1 
ATOM   852   C  CG  . ASN A 1 121  ? 42.790 53.131  31.832  1.00 12.44 ? 121  ASN A CG  1 
ATOM   853   O  OD1 . ASN A 1 121  ? 42.249 52.790  32.922  1.00 13.89 ? 121  ASN A OD1 1 
ATOM   854   N  ND2 . ASN A 1 121  ? 43.210 54.350  31.598  1.00 11.95 ? 121  ASN A ND2 1 
ATOM   855   N  N   . PRO A 1 122  ? 45.130 49.176  30.234  1.00 12.49 ? 122  PRO A N   1 
ATOM   856   C  CA  . PRO A 1 122  ? 45.498 48.179  29.232  1.00 13.05 ? 122  PRO A CA  1 
ATOM   857   C  C   . PRO A 1 122  ? 44.375 47.520  28.451  1.00 12.65 ? 122  PRO A C   1 
ATOM   858   O  O   . PRO A 1 122  ? 44.664 47.010  27.350  1.00 13.36 ? 122  PRO A O   1 
ATOM   859   C  CB  . PRO A 1 122  ? 46.289 47.139  30.045  1.00 14.13 ? 122  PRO A CB  1 
ATOM   860   C  CG  . PRO A 1 122  ? 46.815 47.934  31.209  1.00 14.79 ? 122  PRO A CG  1 
ATOM   861   C  CD  . PRO A 1 122  ? 45.665 48.834  31.583  1.00 13.79 ? 122  PRO A CD  1 
ATOM   862   N  N   . GLU A 1 123  ? 43.143 47.521  28.952  1.00 11.57 ? 123  GLU A N   1 
ATOM   863   C  CA  . GLU A 1 123  ? 42.026 46.946  28.172  1.00 12.64 ? 123  GLU A CA  1 
ATOM   864   C  C   . GLU A 1 123  ? 41.322 47.942  27.254  1.00 11.74 ? 123  GLU A C   1 
ATOM   865   O  O   . GLU A 1 123  ? 40.492 47.536  26.447  1.00 11.99 ? 123  GLU A O   1 
ATOM   866   C  CB  . GLU A 1 123  ? 40.977 46.265  29.061  1.00 14.80 ? 123  GLU A CB  1 
ATOM   867   C  CG  . GLU A 1 123  ? 41.521 45.069  29.853  1.00 20.00 ? 123  GLU A CG  1 
ATOM   868   C  CD  . GLU A 1 123  ? 42.007 43.936  28.959  1.00 26.88 ? 123  GLU A CD  1 
ATOM   869   O  OE1 . GLU A 1 123  ? 41.173 43.309  28.257  1.00 31.03 ? 123  GLU A OE1 1 
ATOM   870   O  OE2 . GLU A 1 123  ? 43.233 43.660  28.951  1.00 32.23 ? 123  GLU A OE2 1 
ATOM   871   N  N   . MET A 1 124  ? 41.634 49.223  27.400  1.00 10.60 ? 124  MET A N   1 
ATOM   872   C  CA  . MET A 1 124  ? 41.021 50.241  26.545  1.00 9.28  ? 124  MET A CA  1 
ATOM   873   C  C   . MET A 1 124  ? 41.664 50.140  25.154  1.00 9.68  ? 124  MET A C   1 
ATOM   874   O  O   . MET A 1 124  ? 42.823 49.805  25.032  1.00 9.51  ? 124  MET A O   1 
ATOM   875   C  CB  . MET A 1 124  ? 41.229 51.627  27.175  1.00 11.32 ? 124  MET A CB  1 
ATOM   876   C  CG  . MET A 1 124  ? 40.552 52.791  26.446  1.00 11.53 ? 124  MET A CG  1 
ATOM   877   S  SD  . MET A 1 124  ? 38.791 52.477  26.293  1.00 13.63 ? 124  MET A SD  1 
ATOM   878   C  CE  . MET A 1 124  ? 38.245 53.991  25.443  1.00 15.51 ? 124  MET A CE  1 
ATOM   879   N  N   . LYS A 1 125  ? 40.877 50.490  24.131  1.00 8.67  ? 125  LYS A N   1 
ATOM   880   C  CA  . LYS A 1 125  ? 41.285 50.402  22.718  1.00 8.20  ? 125  LYS A CA  1 
ATOM   881   C  C   . LYS A 1 125  ? 40.892 51.698  22.026  1.00 8.06  ? 125  LYS A C   1 
ATOM   882   O  O   . LYS A 1 125  ? 40.070 52.489  22.524  1.00 8.66  ? 125  LYS A O   1 
ATOM   883   C  CB  . LYS A 1 125  ? 40.587 49.226  22.025  1.00 9.69  ? 125  LYS A CB  1 
ATOM   884   C  CG  . LYS A 1 125  ? 40.877 47.873  22.660  1.00 12.51 ? 125  LYS A CG  1 
ATOM   885   C  CD  . LYS A 1 125  ? 42.175 47.317  22.173  1.00 15.35 ? 125  LYS A CD  1 
ATOM   886   C  CE  . LYS A 1 125  ? 42.732 46.285  23.133  1.00 23.37 ? 125  LYS A CE  1 
ATOM   887   N  NZ  . LYS A 1 125  ? 41.915 45.074  23.119  1.00 22.98 ? 125  LYS A NZ  1 
ATOM   888   N  N   . PHE A 1 126  ? 41.485 51.926  20.845  1.00 7.75  ? 126  PHE A N   1 
ATOM   889   C  CA  . PHE A 1 126  ? 41.196 53.162  20.073  1.00 6.87  ? 126  PHE A CA  1 
ATOM   890   C  C   . PHE A 1 126  ? 41.695 52.900  18.657  1.00 6.16  ? 126  PHE A C   1 
ATOM   891   O  O   . PHE A 1 126  ? 42.754 52.305  18.457  1.00 7.61  ? 126  PHE A O   1 
ATOM   892   C  CB  . PHE A 1 126  ? 41.976 54.335  20.668  1.00 8.17  ? 126  PHE A CB  1 
ATOM   893   C  CG  . PHE A 1 126  ? 41.589 55.720  20.217  1.00 7.16  ? 126  PHE A CG  1 
ATOM   894   C  CD1 . PHE A 1 126  ? 40.283 56.169  20.241  1.00 8.66  ? 126  PHE A CD1 1 
ATOM   895   C  CD2 . PHE A 1 126  ? 42.594 56.634  19.872  1.00 8.91  ? 126  PHE A CD2 1 
ATOM   896   C  CE1 . PHE A 1 126  ? 39.976 57.505  19.875  1.00 7.70  ? 126  PHE A CE1 1 
ATOM   897   C  CE2 . PHE A 1 126  ? 42.321 57.941  19.533  1.00 8.08  ? 126  PHE A CE2 1 
ATOM   898   C  CZ  . PHE A 1 126  ? 41.013 58.386  19.513  1.00 7.64  ? 126  PHE A CZ  1 
ATOM   899   N  N   . ILE A 1 127  ? 40.917 53.352  17.678  1.00 6.06  ? 127  ILE A N   1 
ATOM   900   C  CA  . ILE A 1 127  ? 41.358 53.250  16.279  1.00 6.13  ? 127  ILE A CA  1 
ATOM   901   C  C   . ILE A 1 127  ? 41.623 54.647  15.741  1.00 6.58  ? 127  ILE A C   1 
ATOM   902   O  O   . ILE A 1 127  ? 41.001 55.637  16.191  1.00 6.11  ? 127  ILE A O   1 
ATOM   903   C  CB  . ILE A 1 127  ? 40.371 52.517  15.382  1.00 6.52  ? 127  ILE A CB  1 
ATOM   904   C  CG1 . ILE A 1 127  ? 38.964 53.104  15.392  1.00 6.96  ? 127  ILE A CG1 1 
ATOM   905   C  CG2 . ILE A 1 127  ? 40.317 51.023  15.800  1.00 7.99  ? 127  ILE A CG2 1 
ATOM   906   C  CD1 . ILE A 1 127  ? 38.060 52.545  14.282  1.00 7.06  ? 127  ILE A CD1 1 
ATOM   907   N  N   . TRP A 1 128  ? 42.574 54.705  14.808  1.00 6.80  ? 128  TRP A N   1 
ATOM   908   C  CA  . TRP A 1 128  ? 42.948 55.977  14.207  1.00 5.93  ? 128  TRP A CA  1 
ATOM   909   C  C   . TRP A 1 128  ? 43.045 55.838  12.703  1.00 5.47  ? 128  TRP A C   1 
ATOM   910   O  O   . TRP A 1 128  ? 43.705 54.916  12.228  1.00 6.01  ? 128  TRP A O   1 
ATOM   911   C  CB  . TRP A 1 128  ? 44.288 56.461  14.769  1.00 6.24  ? 128  TRP A CB  1 
ATOM   912   C  CG  . TRP A 1 128  ? 44.513 57.893  14.407  1.00 7.02  ? 128  TRP A CG  1 
ATOM   913   C  CD1 . TRP A 1 128  ? 45.229 58.388  13.329  1.00 6.46  ? 128  TRP A CD1 1 
ATOM   914   C  CD2 . TRP A 1 128  ? 43.947 59.011  15.064  1.00 6.27  ? 128  TRP A CD2 1 
ATOM   915   N  NE1 . TRP A 1 128  ? 45.164 59.764  13.317  1.00 5.65  ? 128  TRP A NE1 1 
ATOM   916   C  CE2 . TRP A 1 128  ? 44.369 60.178  14.368  1.00 6.17  ? 128  TRP A CE2 1 
ATOM   917   C  CE3 . TRP A 1 128  ? 43.114 59.153  16.195  1.00 6.56  ? 128  TRP A CE3 1 
ATOM   918   C  CZ2 . TRP A 1 128  ? 43.968 61.479  14.765  1.00 6.93  ? 128  TRP A CZ2 1 
ATOM   919   C  CZ3 . TRP A 1 128  ? 42.728 60.404  16.575  1.00 6.50  ? 128  TRP A CZ3 1 
ATOM   920   C  CH2 . TRP A 1 128  ? 43.171 61.572  15.869  1.00 7.65  ? 128  TRP A CH2 1 
ATOM   921   N  N   . ALA A 1 129  ? 42.481 56.797  11.967  1.00 6.64  ? 129  ALA A N   1 
ATOM   922   C  CA  . ALA A 1 129  ? 42.457 56.736  10.503  1.00 7.87  ? 129  ALA A CA  1 
ATOM   923   C  C   . ALA A 1 129  ? 43.409 57.702  9.772   1.00 9.38  ? 129  ALA A C   1 
ATOM   924   O  O   . ALA A 1 129  ? 43.976 57.329  8.737   1.00 10.63 ? 129  ALA A O   1 
ATOM   925   C  CB  . ALA A 1 129  ? 41.036 57.010  9.995   1.00 9.01  ? 129  ALA A CB  1 
ATOM   926   N  N   . GLU A 1 130  ? 43.493 58.948  10.234  1.00 9.19  ? 130  GLU A N   1 
ATOM   927   C  CA  . GLU A 1 130  ? 44.086 60.064  9.442   1.00 7.83  ? 130  GLU A CA  1 
ATOM   928   C  C   . GLU A 1 130  ? 45.578 60.224  9.743   1.00 6.58  ? 130  GLU A C   1 
ATOM   929   O  O   . GLU A 1 130  ? 45.968 60.805  10.763  1.00 6.17  ? 130  GLU A O   1 
ATOM   930   C  CB  . GLU A 1 130  ? 43.348 61.383  9.719   1.00 9.74  ? 130  GLU A CB  1 
ATOM   931   C  CG  . GLU A 1 130  ? 41.839 61.323  9.397   1.00 10.84 ? 130  GLU A CG  1 
ATOM   932   C  CD  . GLU A 1 130  ? 40.956 60.906  10.577  1.00 15.95 ? 130  GLU A CD  1 
ATOM   933   O  OE1 . GLU A 1 130  ? 41.501 60.596  11.682  1.00 15.86 ? 130  GLU A OE1 1 
ATOM   934   O  OE2 . GLU A 1 130  ? 39.699 60.880  10.421  1.00 15.99 ? 130  GLU A OE2 1 
ATOM   935   N  N   . ILE A 1 131  ? 46.442 59.720  8.863   1.00 5.29  ? 131  ILE A N   1 
ATOM   936   C  CA  . ILE A 1 131  ? 47.855 59.692  9.183   1.00 5.90  ? 131  ILE A CA  1 
ATOM   937   C  C   . ILE A 1 131  ? 48.482 61.052  9.042   1.00 6.75  ? 131  ILE A C   1 
ATOM   938   O  O   . ILE A 1 131  ? 49.492 61.335  9.707   1.00 7.82  ? 131  ILE A O   1 
ATOM   939   C  CB  . ILE A 1 131  ? 48.576 58.594  8.359   1.00 7.09  ? 131  ILE A CB  1 
ATOM   940   C  CG1 . ILE A 1 131  ? 47.959 57.217  8.653   1.00 7.25  ? 131  ILE A CG1 1 
ATOM   941   C  CG2 . ILE A 1 131  ? 50.046 58.585  8.650   1.00 8.34  ? 131  ILE A CG2 1 
ATOM   942   C  CD1 . ILE A 1 131  ? 47.847 56.900  10.211  1.00 10.50 ? 131  ILE A CD1 1 
ATOM   943   N  N   . SER A 1 132  ? 47.914 61.930  8.235   1.00 5.05  ? 132  SER A N   1 
ATOM   944   C  CA  . SER A 1 132  ? 48.403 63.317  8.212   1.00 5.83  ? 132  SER A CA  1 
ATOM   945   C  C   . SER A 1 132  ? 48.489 63.908  9.625   1.00 5.91  ? 132  SER A C   1 
ATOM   946   O  O   . SER A 1 132  ? 49.537 64.470  10.007  1.00 6.54  ? 132  SER A O   1 
ATOM   947   C  CB  . SER A 1 132  ? 47.507 64.173  7.350   1.00 6.23  ? 132  SER A CB  1 
ATOM   948   O  OG  . SER A 1 132  ? 46.146 64.086  7.735   1.00 6.24  ? 132  SER A OG  1 
ATOM   949   N  N   . TYR A 1 133  ? 47.439 63.744  10.411  1.00 5.71  ? 133  TYR A N   1 
ATOM   950   C  CA  . TYR A 1 133  ? 47.469 64.244  11.773  1.00 5.90  ? 133  TYR A CA  1 
ATOM   951   C  C   . TYR A 1 133  ? 48.424 63.447  12.634  1.00 6.08  ? 133  TYR A C   1 
ATOM   952   O  O   . TYR A 1 133  ? 49.098 64.032  13.517  1.00 7.10  ? 133  TYR A O   1 
ATOM   953   C  CB  . TYR A 1 133  ? 46.093 64.185  12.415  1.00 5.61  ? 133  TYR A CB  1 
ATOM   954   C  CG  . TYR A 1 133  ? 45.162 65.310  12.071  1.00 5.25  ? 133  TYR A CG  1 
ATOM   955   C  CD1 . TYR A 1 133  ? 45.498 66.624  12.353  1.00 6.89  ? 133  TYR A CD1 1 
ATOM   956   C  CD2 . TYR A 1 133  ? 43.901 65.053  11.532  1.00 5.94  ? 133  TYR A CD2 1 
ATOM   957   C  CE1 . TYR A 1 133  ? 44.627 67.667  12.038  1.00 5.53  ? 133  TYR A CE1 1 
ATOM   958   C  CE2 . TYR A 1 133  ? 43.004 66.096  11.250  1.00 6.28  ? 133  TYR A CE2 1 
ATOM   959   C  CZ  . TYR A 1 133  ? 43.393 67.395  11.519  1.00 6.84  ? 133  TYR A CZ  1 
ATOM   960   O  OH  . TYR A 1 133  ? 42.564 68.458  11.219  1.00 7.65  ? 133  TYR A OH  1 
ATOM   961   N  N   . PHE A 1 134  ? 48.446 62.128  12.455  1.00 5.57  ? 134  PHE A N   1 
ATOM   962   C  CA  . PHE A 1 134  ? 49.277 61.326  13.353  1.00 6.71  ? 134  PHE A CA  1 
ATOM   963   C  C   . PHE A 1 134  ? 50.739 61.660  13.135  1.00 7.47  ? 134  PHE A C   1 
ATOM   964   O  O   . PHE A 1 134  ? 51.513 61.762  14.104  1.00 7.68  ? 134  PHE A O   1 
ATOM   965   C  CB  . PHE A 1 134  ? 48.998 59.837  13.183  1.00 6.41  ? 134  PHE A CB  1 
ATOM   966   C  CG  . PHE A 1 134  ? 49.568 59.022  14.299  1.00 7.22  ? 134  PHE A CG  1 
ATOM   967   C  CD1 . PHE A 1 134  ? 48.833 58.802  15.468  1.00 8.90  ? 134  PHE A CD1 1 
ATOM   968   C  CD2 . PHE A 1 134  ? 50.849 58.498  14.181  1.00 10.59 ? 134  PHE A CD2 1 
ATOM   969   C  CE1 . PHE A 1 134  ? 49.401 58.047  16.515  1.00 10.45 ? 134  PHE A CE1 1 
ATOM   970   C  CE2 . PHE A 1 134  ? 51.427 57.735  15.243  1.00 7.72  ? 134  PHE A CE2 1 
ATOM   971   C  CZ  . PHE A 1 134  ? 50.673 57.507  16.390  1.00 9.61  ? 134  PHE A CZ  1 
ATOM   972   N  N   . ALA A 1 135  ? 51.146 61.821  11.876  1.00 7.19  ? 135  ALA A N   1 
ATOM   973   C  CA  . ALA A 1 135  ? 52.531 62.185  11.547  1.00 7.73  ? 135  ALA A CA  1 
ATOM   974   C  C   . ALA A 1 135  ? 52.865 63.567  12.092  1.00 8.35  ? 135  ALA A C   1 
ATOM   975   O  O   . ALA A 1 135  ? 53.985 63.752  12.636  1.00 11.38 ? 135  ALA A O   1 
ATOM   976   C  CB  . ALA A 1 135  ? 52.767 62.110  10.036  1.00 9.22  ? 135  ALA A CB  1 
ATOM   977   N  N   . ARG A 1 136  ? 51.920 64.503  12.008  1.00 8.68  ? 136  ARG A N   1 
ATOM   978   C  CA  . ARG A 1 136  ? 52.087 65.878  12.541  1.00 9.43  ? 136  ARG A CA  1 
ATOM   979   C  C   . ARG A 1 136  ? 52.310 65.803  14.061  1.00 10.57 ? 136  ARG A C   1 
ATOM   980   O  O   . ARG A 1 136  ? 53.143 66.542  14.609  1.00 12.48 ? 136  ARG A O   1 
ATOM   981   C  CB  . ARG A 1 136  ? 50.846 66.720  12.244  1.00 9.66  ? 136  ARG A CB  1 
ATOM   982   C  CG  . ARG A 1 136  ? 50.839 68.134  12.831  1.00 12.07 ? 136  ARG A CG  1 
ATOM   983   C  CD  . ARG A 1 136  ? 51.761 69.104  12.109  1.00 14.20 ? 136  ARG A CD  1 
ATOM   984   N  NE  . ARG A 1 136  ? 51.694 70.403  12.785  1.00 13.89 ? 136  ARG A NE  1 
ATOM   985   C  CZ  . ARG A 1 136  ? 52.416 70.724  13.850  1.00 14.66 ? 136  ARG A CZ  1 
ATOM   986   N  NH1 . ARG A 1 136  ? 53.284 69.851  14.360  1.00 15.57 ? 136  ARG A NH1 1 
ATOM   987   N  NH2 . ARG A 1 136  ? 52.260 71.936  14.412  1.00 13.62 ? 136  ARG A NH2 1 
ATOM   988   N  N   . PHE A 1 137  ? 51.627 64.884  14.748  1.00 8.86  ? 137  PHE A N   1 
ATOM   989   C  CA  . PHE A 1 137  ? 51.757 64.734  16.189  1.00 9.41  ? 137  PHE A CA  1 
ATOM   990   C  C   . PHE A 1 137  ? 53.035 64.025  16.581  1.00 10.58 ? 137  PHE A C   1 
ATOM   991   O  O   . PHE A 1 137  ? 53.800 64.515  17.432  1.00 10.57 ? 137  PHE A O   1 
ATOM   992   C  CB  . PHE A 1 137  ? 50.563 63.922  16.676  1.00 8.46  ? 137  PHE A CB  1 
ATOM   993   C  CG  . PHE A 1 137  ? 50.582 63.654  18.140  1.00 9.06  ? 137  PHE A CG  1 
ATOM   994   C  CD1 . PHE A 1 137  ? 50.309 64.689  19.008  1.00 9.92  ? 137  PHE A CD1 1 
ATOM   995   C  CD2 . PHE A 1 137  ? 50.849 62.394  18.614  1.00 10.16 ? 137  PHE A CD2 1 
ATOM   996   C  CE1 . PHE A 1 137  ? 50.287 64.485  20.359  1.00 12.57 ? 137  PHE A CE1 1 
ATOM   997   C  CE2 . PHE A 1 137  ? 50.868 62.167  20.013  1.00 10.78 ? 137  PHE A CE2 1 
ATOM   998   C  CZ  . PHE A 1 137  ? 50.568 63.227  20.852  1.00 9.23  ? 137  PHE A CZ  1 
ATOM   999   N  N   . TYR A 1 138  ? 53.304 62.904  15.935  1.00 10.59 ? 138  TYR A N   1 
ATOM   1000  C  CA  A TYR A 1 138  ? 54.404 62.034  16.316  0.50 12.06 ? 138  TYR A CA  1 
ATOM   1001  C  CA  B TYR A 1 138  ? 54.395 62.018  16.349  0.50 12.80 ? 138  TYR A CA  1 
ATOM   1002  C  C   . TYR A 1 138  ? 55.729 62.755  16.203  1.00 13.93 ? 138  TYR A C   1 
ATOM   1003  O  O   . TYR A 1 138  ? 56.622 62.601  17.036  1.00 13.78 ? 138  TYR A O   1 
ATOM   1004  C  CB  A TYR A 1 138  ? 54.430 60.812  15.416  0.50 10.53 ? 138  TYR A CB  1 
ATOM   1005  C  CB  B TYR A 1 138  ? 54.544 60.856  15.365  0.50 12.62 ? 138  TYR A CB  1 
ATOM   1006  C  CG  A TYR A 1 138  ? 55.421 59.749  15.816  0.50 9.24  ? 138  TYR A CG  1 
ATOM   1007  C  CG  B TYR A 1 138  ? 55.771 60.006  15.603  0.50 12.43 ? 138  TYR A CG  1 
ATOM   1008  C  CD1 A TYR A 1 138  ? 55.092 58.818  16.777  0.50 6.75  ? 138  TYR A CD1 1 
ATOM   1009  C  CD1 B TYR A 1 138  ? 56.979 60.309  14.989  0.50 12.85 ? 138  TYR A CD1 1 
ATOM   1010  C  CD2 A TYR A 1 138  ? 56.645 59.660  15.213  0.50 8.35  ? 138  TYR A CD2 1 
ATOM   1011  C  CD2 B TYR A 1 138  ? 55.722 58.901  16.442  0.50 13.84 ? 138  TYR A CD2 1 
ATOM   1012  C  CE1 A TYR A 1 138  ? 55.967 57.827  17.140  0.50 6.96  ? 138  TYR A CE1 1 
ATOM   1013  C  CE1 B TYR A 1 138  ? 58.104 59.535  15.203  0.50 13.97 ? 138  TYR A CE1 1 
ATOM   1014  C  CE2 A TYR A 1 138  ? 57.550 58.651  15.574  0.50 6.06  ? 138  TYR A CE2 1 
ATOM   1015  C  CE2 B TYR A 1 138  ? 56.841 58.121  16.663  0.50 15.14 ? 138  TYR A CE2 1 
ATOM   1016  C  CZ  A TYR A 1 138  ? 57.190 57.748  16.534  0.50 8.23  ? 138  TYR A CZ  1 
ATOM   1017  C  CZ  B TYR A 1 138  ? 58.029 58.442  16.041  0.50 14.28 ? 138  TYR A CZ  1 
ATOM   1018  O  OH  A TYR A 1 138  ? 58.045 56.731  16.922  0.50 9.18  ? 138  TYR A OH  1 
ATOM   1019  O  OH  B TYR A 1 138  ? 59.146 57.669  16.258  0.50 15.90 ? 138  TYR A OH  1 
ATOM   1020  N  N   A HIS A 1 139  ? 55.866 63.539  15.152  0.50 14.42 ? 139  HIS A N   1 
ATOM   1021  N  N   B HIS A 1 139  ? 55.858 63.546  15.173  0.50 14.92 ? 139  HIS A N   1 
ATOM   1022  C  CA  A HIS A 1 139  ? 57.156 64.178  14.873  0.50 15.98 ? 139  HIS A CA  1 
ATOM   1023  C  CA  B HIS A 1 139  ? 57.133 64.151  14.883  0.50 16.67 ? 139  HIS A CA  1 
ATOM   1024  C  C   A HIS A 1 139  ? 57.424 65.367  15.815  0.50 16.85 ? 139  HIS A C   1 
ATOM   1025  C  C   B HIS A 1 139  ? 57.455 65.185  15.962  0.50 16.95 ? 139  HIS A C   1 
ATOM   1026  O  O   A HIS A 1 139  ? 58.510 65.978  15.804  0.50 16.94 ? 139  HIS A O   1 
ATOM   1027  O  O   B HIS A 1 139  ? 58.611 65.517  16.176  0.50 16.63 ? 139  HIS A O   1 
ATOM   1028  C  CB  A HIS A 1 139  ? 57.234 64.606  13.407  0.50 15.75 ? 139  HIS A CB  1 
ATOM   1029  C  CB  B HIS A 1 139  ? 57.090 64.798  13.494  0.50 17.26 ? 139  HIS A CB  1 
ATOM   1030  C  CG  A HIS A 1 139  ? 57.464 63.477  12.453  0.50 15.82 ? 139  HIS A CG  1 
ATOM   1031  C  CG  B HIS A 1 139  ? 58.422 65.236  12.983  0.50 18.89 ? 139  HIS A CG  1 
ATOM   1032  N  ND1 A HIS A 1 139  ? 58.641 62.760  12.417  0.50 17.74 ? 139  HIS A ND1 1 
ATOM   1033  N  ND1 B HIS A 1 139  ? 58.800 66.561  12.910  0.50 19.71 ? 139  HIS A ND1 1 
ATOM   1034  C  CD2 A HIS A 1 139  ? 56.677 62.962  11.481  0.50 14.65 ? 139  HIS A CD2 1 
ATOM   1035  C  CD2 B HIS A 1 139  ? 59.464 64.519  12.511  0.50 20.68 ? 139  HIS A CD2 1 
ATOM   1036  C  CE1 A HIS A 1 139  ? 58.564 61.842  11.469  0.50 17.87 ? 139  HIS A CE1 1 
ATOM   1037  C  CE1 B HIS A 1 139  ? 60.023 66.637  12.421  0.50 21.79 ? 139  HIS A CE1 1 
ATOM   1038  N  NE2 A HIS A 1 139  ? 57.390 61.956  10.872  0.50 14.90 ? 139  HIS A NE2 1 
ATOM   1039  N  NE2 B HIS A 1 139  ? 60.445 65.414  12.161  0.50 21.11 ? 139  HIS A NE2 1 
ATOM   1040  N  N   . ASP A 1 140  ? 56.439 65.691  16.643  1.00 16.68 ? 140  ASP A N   1 
ATOM   1041  C  CA  . ASP A 1 140  ? 56.618 66.660  17.729  1.00 17.65 ? 140  ASP A CA  1 
ATOM   1042  C  C   . ASP A 1 140  ? 56.810 66.024  19.113  1.00 16.69 ? 140  ASP A C   1 
ATOM   1043  O  O   . ASP A 1 140  ? 57.075 66.736  20.108  1.00 17.32 ? 140  ASP A O   1 
ATOM   1044  C  CB  . ASP A 1 140  ? 55.437 67.596  17.792  1.00 18.03 ? 140  ASP A CB  1 
ATOM   1045  C  CG  . ASP A 1 140  ? 55.561 68.754  16.829  1.00 21.71 ? 140  ASP A CG  1 
ATOM   1046  O  OD1 . ASP A 1 140  ? 56.463 68.703  15.958  1.00 26.50 ? 140  ASP A OD1 1 
ATOM   1047  O  OD2 . ASP A 1 140  ? 54.805 69.746  16.890  1.00 22.58 ? 140  ASP A OD2 1 
ATOM   1048  N  N   . LEU A 1 141  ? 56.674 64.713  19.195  1.00 15.90 ? 141  LEU A N   1 
ATOM   1049  C  CA  . LEU A 1 141  ? 56.873 63.997  20.453  1.00 15.04 ? 141  LEU A CA  1 
ATOM   1050  C  C   . LEU A 1 141  ? 58.322 63.822  20.806  1.00 15.69 ? 141  LEU A C   1 
ATOM   1051  O  O   . LEU A 1 141  ? 59.141 63.581  19.941  1.00 15.67 ? 141  LEU A O   1 
ATOM   1052  C  CB  . LEU A 1 141  ? 56.293 62.587  20.362  1.00 14.52 ? 141  LEU A CB  1 
ATOM   1053  C  CG  . LEU A 1 141  ? 54.781 62.469  20.349  1.00 15.37 ? 141  LEU A CG  1 
ATOM   1054  C  CD1 . LEU A 1 141  ? 54.409 60.984  20.295  1.00 13.77 ? 141  LEU A CD1 1 
ATOM   1055  C  CD2 . LEU A 1 141  ? 54.184 63.156  21.581  1.00 14.88 ? 141  LEU A CD2 1 
ATOM   1056  N  N   . GLY A 1 142  ? 58.621 63.927  22.099  1.00 16.66 ? 142  GLY A N   1 
ATOM   1057  C  CA  . GLY A 1 142  ? 59.907 63.515  22.616  1.00 17.64 ? 142  GLY A CA  1 
ATOM   1058  C  C   . GLY A 1 142  ? 60.081 62.010  22.490  1.00 18.58 ? 142  GLY A C   1 
ATOM   1059  O  O   . GLY A 1 142  ? 59.083 61.254  22.355  1.00 17.97 ? 142  GLY A O   1 
ATOM   1060  N  N   . GLU A 1 143  ? 61.330 61.563  22.549  1.00 18.87 ? 143  GLU A N   1 
ATOM   1061  C  CA  . GLU A 1 143  ? 61.651 60.150  22.364  1.00 19.70 ? 143  GLU A CA  1 
ATOM   1062  C  C   . GLU A 1 143  ? 60.950 59.234  23.381  1.00 19.40 ? 143  GLU A C   1 
ATOM   1063  O  O   . GLU A 1 143  ? 60.465 58.158  23.021  1.00 18.79 ? 143  GLU A O   1 
ATOM   1064  C  CB  . GLU A 1 143  ? 63.173 59.926  22.331  1.00 20.86 ? 143  GLU A CB  1 
ATOM   1065  C  CG  . GLU A 1 143  ? 63.605 58.594  21.740  1.00 24.30 ? 143  GLU A CG  1 
ATOM   1066  C  CD  . GLU A 1 143  ? 63.383 58.480  20.226  1.00 30.04 ? 143  GLU A CD  1 
ATOM   1067  O  OE1 . GLU A 1 143  ? 63.087 59.498  19.539  1.00 33.24 ? 143  GLU A OE1 1 
ATOM   1068  O  OE2 . GLU A 1 143  ? 63.515 57.347  19.711  1.00 34.36 ? 143  GLU A OE2 1 
ATOM   1069  N  N   . ASN A 1 144  ? 60.856 59.668  24.622  1.00 20.30 ? 144  ASN A N   1 
ATOM   1070  C  CA  . ASN A 1 144  ? 60.142 58.916  25.641  1.00 20.08 ? 144  ASN A CA  1 
ATOM   1071  C  C   . ASN A 1 144  ? 58.700 58.586  25.201  1.00 19.11 ? 144  ASN A C   1 
ATOM   1072  O  O   . ASN A 1 144  ? 58.276 57.454  25.242  1.00 18.63 ? 144  ASN A O   1 
ATOM   1073  C  CB  . ASN A 1 144  ? 60.165 59.708  26.954  1.00 21.79 ? 144  ASN A CB  1 
ATOM   1074  C  CG  . ASN A 1 144  ? 59.498 58.985  28.093  1.00 26.15 ? 144  ASN A CG  1 
ATOM   1075  O  OD1 . ASN A 1 144  ? 60.125 58.189  28.790  1.00 31.81 ? 144  ASN A OD1 1 
ATOM   1076  N  ND2 . ASN A 1 144  ? 58.218 59.264  28.300  1.00 30.14 ? 144  ASN A ND2 1 
ATOM   1077  N  N   . LYS A 1 145  ? 57.986 59.604  24.753  1.00 17.35 ? 145  LYS A N   1 
ATOM   1078  C  CA  . LYS A 1 145  ? 56.607 59.452  24.280  1.00 15.97 ? 145  LYS A CA  1 
ATOM   1079  C  C   . LYS A 1 145  ? 56.482 58.682  22.959  1.00 14.69 ? 145  LYS A C   1 
ATOM   1080  O  O   . LYS A 1 145  ? 55.536 57.908  22.817  1.00 14.38 ? 145  LYS A O   1 
ATOM   1081  C  CB  . LYS A 1 145  ? 55.895 60.802  24.194  1.00 16.87 ? 145  LYS A CB  1 
ATOM   1082  C  CG  . LYS A 1 145  ? 55.730 61.501  25.557  1.00 18.25 ? 145  LYS A CG  1 
ATOM   1083  C  CD  . LYS A 1 145  ? 54.696 60.825  26.456  1.00 24.17 ? 145  LYS A CD  1 
ATOM   1084  C  CE  . LYS A 1 145  ? 54.596 61.559  27.797  1.00 24.79 ? 145  LYS A CE  1 
ATOM   1085  N  NZ  . LYS A 1 145  ? 55.712 61.225  28.730  1.00 30.25 ? 145  LYS A NZ  1 
ATOM   1086  N  N   A LYS A 1 146  ? 57.418 58.880  22.026  0.50 14.29 ? 146  LYS A N   1 
ATOM   1087  N  N   B LYS A 1 146  ? 57.404 58.903  22.016  0.50 14.16 ? 146  LYS A N   1 
ATOM   1088  C  CA  A LYS A 1 146  ? 57.464 58.081  20.798  0.50 14.29 ? 146  LYS A CA  1 
ATOM   1089  C  CA  B LYS A 1 146  ? 57.462 58.090  20.800  0.50 14.09 ? 146  LYS A CA  1 
ATOM   1090  C  C   A LYS A 1 146  ? 57.558 56.597  21.104  0.50 14.35 ? 146  LYS A C   1 
ATOM   1091  C  C   B LYS A 1 146  ? 57.477 56.615  21.186  0.50 14.05 ? 146  LYS A C   1 
ATOM   1092  O  O   A LYS A 1 146  ? 56.901 55.781  20.456  0.50 14.34 ? 146  LYS A O   1 
ATOM   1093  O  O   B LYS A 1 146  ? 56.659 55.830  20.704  0.50 13.51 ? 146  LYS A O   1 
ATOM   1094  C  CB  A LYS A 1 146  ? 58.643 58.474  19.921  0.50 13.99 ? 146  LYS A CB  1 
ATOM   1095  C  CB  B LYS A 1 146  ? 58.686 58.428  19.945  0.50 13.80 ? 146  LYS A CB  1 
ATOM   1096  C  CG  A LYS A 1 146  ? 58.523 59.811  19.243  0.50 13.97 ? 146  LYS A CG  1 
ATOM   1097  C  CG  B LYS A 1 146  ? 58.613 59.748  19.181  0.50 13.73 ? 146  LYS A CG  1 
ATOM   1098  C  CD  A LYS A 1 146  ? 59.661 59.952  18.266  0.50 14.35 ? 146  LYS A CD  1 
ATOM   1099  C  CD  B LYS A 1 146  ? 59.804 59.885  18.236  0.50 14.20 ? 146  LYS A CD  1 
ATOM   1100  C  CE  A LYS A 1 146  ? 59.651 61.279  17.542  0.50 15.10 ? 146  LYS A CE  1 
ATOM   1101  C  CE  B LYS A 1 146  ? 59.609 60.966  17.156  0.50 14.39 ? 146  LYS A CE  1 
ATOM   1102  N  NZ  A LYS A 1 146  ? 60.862 61.395  16.687  0.50 16.78 ? 146  LYS A NZ  1 
ATOM   1103  N  NZ  B LYS A 1 146  ? 59.747 62.361  17.650  0.50 16.24 ? 146  LYS A NZ  1 
ATOM   1104  N  N   . LEU A 1 147  ? 58.385 56.247  22.091  1.00 14.33 ? 147  LEU A N   1 
ATOM   1105  C  CA  . LEU A 1 147  ? 58.507 54.866  22.547  1.00 14.91 ? 147  LEU A CA  1 
ATOM   1106  C  C   . LEU A 1 147  ? 57.210 54.356  23.206  1.00 13.82 ? 147  LEU A C   1 
ATOM   1107  O  O   . LEU A 1 147  ? 56.770 53.244  22.888  1.00 14.46 ? 147  LEU A O   1 
ATOM   1108  C  CB  . LEU A 1 147  ? 59.725 54.703  23.492  1.00 15.43 ? 147  LEU A CB  1 
ATOM   1109  C  CG  . LEU A 1 147  ? 61.080 54.818  22.793  1.00 18.68 ? 147  LEU A CG  1 
ATOM   1110  C  CD1 . LEU A 1 147  ? 62.210 54.923  23.791  1.00 20.19 ? 147  LEU A CD1 1 
ATOM   1111  C  CD2 . LEU A 1 147  ? 61.302 53.618  21.905  1.00 20.26 ? 147  LEU A CD2 1 
ATOM   1112  N  N   . GLN A 1 148  ? 56.595 55.153  24.085  1.00 14.31 ? 148  GLN A N   1 
ATOM   1113  C  CA  . GLN A 1 148  ? 55.290 54.792  24.633  1.00 13.85 ? 148  GLN A CA  1 
ATOM   1114  C  C   . GLN A 1 148  ? 54.243 54.576  23.522  1.00 12.93 ? 148  GLN A C   1 
ATOM   1115  O  O   . GLN A 1 148  ? 53.460 53.650  23.592  1.00 13.11 ? 148  GLN A O   1 
ATOM   1116  C  CB  . GLN A 1 148  ? 54.780 55.870  25.566  1.00 15.00 ? 148  GLN A CB  1 
ATOM   1117  C  CG  . GLN A 1 148  ? 55.509 56.010  26.858  1.00 19.98 ? 148  GLN A CG  1 
ATOM   1118  C  CD  . GLN A 1 148  ? 54.658 56.756  27.865  1.00 26.68 ? 148  GLN A CD  1 
ATOM   1119  O  OE1 . GLN A 1 148  ? 53.528 57.182  27.544  1.00 29.10 ? 148  GLN A OE1 1 
ATOM   1120  N  NE2 . GLN A 1 148  ? 55.173 56.908  29.081  1.00 29.52 ? 148  GLN A NE2 1 
ATOM   1121  N  N   . MET A 1 149  ? 54.253 55.451  22.521  1.00 12.05 ? 149  MET A N   1 
ATOM   1122  C  CA  . MET A 1 149  ? 53.298 55.325  21.423  1.00 12.00 ? 149  MET A CA  1 
ATOM   1123  C  C   . MET A 1 149  ? 53.530 54.050  20.630  1.00 12.12 ? 149  MET A C   1 
ATOM   1124  O  O   . MET A 1 149  ? 52.588 53.328  20.336  1.00 11.24 ? 149  MET A O   1 
ATOM   1125  C  CB  . MET A 1 149  ? 53.398 56.549  20.536  1.00 12.80 ? 149  MET A CB  1 
ATOM   1126  C  CG  . MET A 1 149  ? 52.392 56.567  19.407  1.00 12.23 ? 149  MET A CG  1 
ATOM   1127  S  SD  . MET A 1 149  ? 50.695 56.748  19.969  1.00 14.32 ? 149  MET A SD  1 
ATOM   1128  C  CE  . MET A 1 149  ? 50.543 58.580  20.023  1.00 18.20 ? 149  MET A CE  1 
ATOM   1129  N  N   . LYS A 1 150  ? 54.785 53.742  20.323  1.00 11.97 ? 150  LYS A N   1 
ATOM   1130  C  CA  . LYS A 1 150  ? 55.078 52.506  19.617  1.00 13.49 ? 150  LYS A CA  1 
ATOM   1131  C  C   . LYS A 1 150  ? 54.618 51.277  20.394  1.00 12.53 ? 150  LYS A C   1 
ATOM   1132  O  O   . LYS A 1 150  ? 54.131 50.305  19.789  1.00 13.76 ? 150  LYS A O   1 
ATOM   1133  C  CB  . LYS A 1 150  ? 56.559 52.412  19.250  1.00 12.63 ? 150  LYS A CB  1 
ATOM   1134  C  CG  . LYS A 1 150  ? 56.966 53.394  18.153  1.00 14.84 ? 150  LYS A CG  1 
ATOM   1135  C  CD  . LYS A 1 150  ? 58.385 53.159  17.635  1.00 17.96 ? 150  LYS A CD  1 
ATOM   1136  C  CE  . LYS A 1 150  ? 59.361 54.092  18.293  1.00 24.99 ? 150  LYS A CE  1 
ATOM   1137  N  NZ  . LYS A 1 150  ? 60.737 53.918  17.723  1.00 28.25 ? 150  LYS A NZ  1 
ATOM   1138  N  N   A SER A 1 151  ? 54.722 51.321  21.727  0.50 12.10 ? 151  SER A N   1 
ATOM   1139  N  N   B SER A 1 151  ? 54.748 51.322  21.722  0.50 11.96 ? 151  SER A N   1 
ATOM   1140  C  CA  A SER A 1 151  ? 54.339 50.192  22.578  0.50 12.31 ? 151  SER A CA  1 
ATOM   1141  C  CA  B SER A 1 151  ? 54.337 50.206  22.557  0.50 12.05 ? 151  SER A CA  1 
ATOM   1142  C  C   A SER A 1 151  ? 52.821 49.946  22.624  0.50 12.00 ? 151  SER A C   1 
ATOM   1143  C  C   B SER A 1 151  ? 52.837 49.956  22.450  0.50 11.67 ? 151  SER A C   1 
ATOM   1144  O  O   A SER A 1 151  ? 52.363 48.807  22.725  0.50 11.69 ? 151  SER A O   1 
ATOM   1145  O  O   B SER A 1 151  ? 52.411 48.822  22.249  0.50 10.95 ? 151  SER A O   1 
ATOM   1146  C  CB  A SER A 1 151  ? 54.894 50.384  23.993  0.50 13.43 ? 151  SER A CB  1 
ATOM   1147  C  CB  B SER A 1 151  ? 54.736 50.426  24.015  0.50 13.15 ? 151  SER A CB  1 
ATOM   1148  O  OG  A SER A 1 151  ? 54.156 51.365  24.697  0.50 14.90 ? 151  SER A OG  1 
ATOM   1149  O  OG  B SER A 1 151  ? 54.651 49.202  24.723  0.50 14.52 ? 151  SER A OG  1 
ATOM   1150  N  N   . ILE A 1 152  ? 52.026 51.012  22.563  1.00 10.83 ? 152  ILE A N   1 
ATOM   1151  C  CA  . ILE A 1 152  ? 50.573 50.833  22.516  1.00 10.71 ? 152  ILE A CA  1 
ATOM   1152  C  C   . ILE A 1 152  ? 50.062 50.415  21.134  1.00 10.05 ? 152  ILE A C   1 
ATOM   1153  O  O   . ILE A 1 152  ? 48.981 49.862  21.013  1.00 11.28 ? 152  ILE A O   1 
ATOM   1154  C  CB  . ILE A 1 152  ? 49.752 52.009  23.113  1.00 10.83 ? 152  ILE A CB  1 
ATOM   1155  C  CG1 . ILE A 1 152  ? 50.016 53.322  22.403  1.00 11.77 ? 152  ILE A CG1 1 
ATOM   1156  C  CG2 . ILE A 1 152  ? 49.993 52.124  24.657  1.00 12.48 ? 152  ILE A CG2 1 
ATOM   1157  C  CD1 . ILE A 1 152  ? 48.957 54.394  22.734  1.00 12.01 ? 152  ILE A CD1 1 
ATOM   1158  N  N   . VAL A 1 153  ? 50.838 50.689  20.098  1.00 9.90  ? 153  VAL A N   1 
ATOM   1159  C  CA  . VAL A 1 153  ? 50.537 50.158  18.767  1.00 10.73 ? 153  VAL A CA  1 
ATOM   1160  C  C   . VAL A 1 153  ? 50.969 48.693  18.677  1.00 11.51 ? 153  VAL A C   1 
ATOM   1161  O  O   . VAL A 1 153  ? 50.214 47.813  18.216  1.00 12.54 ? 153  VAL A O   1 
ATOM   1162  C  CB  . VAL A 1 153  ? 51.206 51.032  17.714  1.00 11.32 ? 153  VAL A CB  1 
ATOM   1163  C  CG1 . VAL A 1 153  ? 51.079 50.418  16.320  1.00 12.78 ? 153  VAL A CG1 1 
ATOM   1164  C  CG2 . VAL A 1 153  ? 50.621 52.431  17.774  1.00 10.57 ? 153  VAL A CG2 1 
ATOM   1165  N  N   . LYS A 1 154  ? 52.183 48.419  19.158  1.00 12.52 ? 154  LYS A N   1 
ATOM   1166  C  CA  . LYS A 1 154  ? 52.694 47.054  19.076  1.00 14.77 ? 154  LYS A CA  1 
ATOM   1167  C  C   . LYS A 1 154  ? 51.814 46.064  19.857  1.00 14.46 ? 154  LYS A C   1 
ATOM   1168  O  O   . LYS A 1 154  ? 51.625 44.908  19.429  1.00 16.13 ? 154  LYS A O   1 
ATOM   1169  C  CB  . LYS A 1 154  ? 54.155 47.001  19.549  1.00 14.79 ? 154  LYS A CB  1 
ATOM   1170  C  CG  . LYS A 1 154  ? 54.852 45.675  19.240  1.00 19.58 ? 154  LYS A CG  1 
ATOM   1171  C  CD  . LYS A 1 154  ? 56.354 45.774  19.477  1.00 22.18 ? 154  LYS A CD  1 
ATOM   1172  C  CE  . LYS A 1 154  ? 57.036 44.462  19.067  1.00 25.34 ? 154  LYS A CE  1 
ATOM   1173  N  NZ  . LYS A 1 154  ? 56.955 44.267  17.575  1.00 26.38 ? 154  LYS A NZ  1 
ATOM   1174  N  N   . ASN A 1 155  ? 51.254 46.504  20.983  1.00 14.28 ? 155  ASN A N   1 
ATOM   1175  C  CA  . ASN A 1 155  ? 50.427 45.646  21.837  1.00 15.20 ? 155  ASN A CA  1 
ATOM   1176  C  C   . ASN A 1 155  ? 48.938 45.631  21.442  1.00 14.63 ? 155  ASN A C   1 
ATOM   1177  O  O   . ASN A 1 155  ? 48.122 45.011  22.104  1.00 15.53 ? 155  ASN A O   1 
ATOM   1178  C  CB  . ASN A 1 155  ? 50.588 46.011  23.326  1.00 16.78 ? 155  ASN A CB  1 
ATOM   1179  C  CG  . ASN A 1 155  ? 49.712 47.199  23.757  1.00 19.09 ? 155  ASN A CG  1 
ATOM   1180  O  OD1 . ASN A 1 155  ? 48.993 47.776  22.943  1.00 18.97 ? 155  ASN A OD1 1 
ATOM   1181  N  ND2 . ASN A 1 155  ? 49.775 47.573  25.042  1.00 20.30 ? 155  ASN A ND2 1 
ATOM   1182  N  N   . GLY A 1 156  ? 48.579 46.369  20.402  1.00 12.79 ? 156  GLY A N   1 
ATOM   1183  C  CA  . GLY A 1 156  ? 47.237 46.252  19.842  1.00 12.80 ? 156  GLY A CA  1 
ATOM   1184  C  C   . GLY A 1 156  ? 46.207 47.174  20.460  1.00 11.38 ? 156  GLY A C   1 
ATOM   1185  O  O   . GLY A 1 156  ? 45.026 47.085  20.083  1.00 13.82 ? 156  GLY A O   1 
ATOM   1186  N  N   . GLN A 1 157  ? 46.606 48.106  21.336  1.00 9.61  ? 157  GLN A N   1 
ATOM   1187  C  CA  . GLN A 1 157  ? 45.619 48.972  21.955  1.00 8.95  ? 157  GLN A CA  1 
ATOM   1188  C  C   . GLN A 1 157  ? 45.209 50.111  21.030  1.00 8.28  ? 157  GLN A C   1 
ATOM   1189  O  O   . GLN A 1 157  ? 44.043 50.465  20.973  1.00 8.21  ? 157  GLN A O   1 
ATOM   1190  C  CB  . GLN A 1 157  ? 46.142 49.577  23.233  1.00 9.26  ? 157  GLN A CB  1 
ATOM   1191  C  CG  . GLN A 1 157  ? 46.075 48.640  24.431  1.00 9.26  ? 157  GLN A CG  1 
ATOM   1192  C  CD  . GLN A 1 157  ? 46.440 49.399  25.671  1.00 8.82  ? 157  GLN A CD  1 
ATOM   1193  O  OE1 . GLN A 1 157  ? 47.628 49.427  26.017  1.00 10.90 ? 157  GLN A OE1 1 
ATOM   1194  N  NE2 . GLN A 1 157  ? 45.476 50.094  26.266  1.00 9.29  ? 157  GLN A NE2 1 
ATOM   1195  N  N   . LEU A 1 158  ? 46.192 50.701  20.354  1.00 8.11  ? 158  LEU A N   1 
ATOM   1196  C  CA  A LEU A 1 158  ? 45.889 51.705  19.328  0.50 8.19  ? 158  LEU A CA  1 
ATOM   1197  C  CA  B LEU A 1 158  ? 45.936 51.708  19.332  0.50 8.06  ? 158  LEU A CA  1 
ATOM   1198  C  C   . LEU A 1 158  ? 46.107 51.032  17.986  1.00 8.05  ? 158  LEU A C   1 
ATOM   1199  O  O   . LEU A 1 158  ? 47.187 50.494  17.717  1.00 9.57  ? 158  LEU A O   1 
ATOM   1200  C  CB  A LEU A 1 158  ? 46.762 52.958  19.473  0.50 8.51  ? 158  LEU A CB  1 
ATOM   1201  C  CB  B LEU A 1 158  ? 46.948 52.835  19.465  0.50 8.12  ? 158  LEU A CB  1 
ATOM   1202  C  CG  A LEU A 1 158  ? 46.549 54.224  18.613  0.50 9.33  ? 158  LEU A CG  1 
ATOM   1203  C  CG  B LEU A 1 158  ? 46.961 53.872  18.351  0.50 8.86  ? 158  LEU A CG  1 
ATOM   1204  C  CD1 A LEU A 1 158  ? 47.544 55.308  19.056  0.50 11.41 ? 158  LEU A CD1 1 
ATOM   1205  C  CD1 B LEU A 1 158  ? 45.599 54.553  18.316  0.50 8.29  ? 158  LEU A CD1 1 
ATOM   1206  C  CD2 A LEU A 1 158  ? 46.742 53.962  17.131  0.50 13.98 ? 158  LEU A CD2 1 
ATOM   1207  C  CD2 B LEU A 1 158  ? 48.090 54.877  18.614  0.50 7.31  ? 158  LEU A CD2 1 
ATOM   1208  N  N   . GLU A 1 159  ? 45.073 51.066  17.148  1.00 7.67  ? 159  GLU A N   1 
ATOM   1209  C  CA  . GLU A 1 159  ? 45.144 50.397  15.858  1.00 7.83  ? 159  GLU A CA  1 
ATOM   1210  C  C   . GLU A 1 159  ? 44.832 51.390  14.754  1.00 6.51  ? 159  GLU A C   1 
ATOM   1211  O  O   . GLU A 1 159  ? 43.842 52.129  14.820  1.00 7.23  ? 159  GLU A O   1 
ATOM   1212  C  CB  . GLU A 1 159  ? 44.130 49.275  15.808  1.00 8.90  ? 159  GLU A CB  1 
ATOM   1213  C  CG  . GLU A 1 159  ? 44.160 48.516  14.515  1.00 11.33 ? 159  GLU A CG  1 
ATOM   1214  C  CD  . GLU A 1 159  ? 43.161 47.406  14.543  1.00 14.67 ? 159  GLU A CD  1 
ATOM   1215  O  OE1 . GLU A 1 159  ? 43.464 46.404  15.249  1.00 14.30 ? 159  GLU A OE1 1 
ATOM   1216  O  OE2 . GLU A 1 159  ? 42.091 47.560  13.893  1.00 10.89 ? 159  GLU A OE2 1 
ATOM   1217  N  N   . PHE A 1 160  ? 45.686 51.397  13.739  1.00 6.08  ? 160  PHE A N   1 
ATOM   1218  C  CA  . PHE A 1 160  ? 45.448 52.233  12.574  1.00 6.16  ? 160  PHE A CA  1 
ATOM   1219  C  C   . PHE A 1 160  ? 44.525 51.508  11.624  1.00 6.10  ? 160  PHE A C   1 
ATOM   1220  O  O   . PHE A 1 160  ? 44.694 50.315  11.349  1.00 6.71  ? 160  PHE A O   1 
ATOM   1221  C  CB  . PHE A 1 160  ? 46.780 52.558  11.930  1.00 7.04  ? 160  PHE A CB  1 
ATOM   1222  C  CG  . PHE A 1 160  ? 47.654 53.388  12.820  1.00 6.53  ? 160  PHE A CG  1 
ATOM   1223  C  CD1 . PHE A 1 160  ? 47.374 54.729  13.008  1.00 7.61  ? 160  PHE A CD1 1 
ATOM   1224  C  CD2 . PHE A 1 160  ? 48.728 52.804  13.507  1.00 8.16  ? 160  PHE A CD2 1 
ATOM   1225  C  CE1 . PHE A 1 160  ? 48.156 55.499  13.855  1.00 8.41  ? 160  PHE A CE1 1 
ATOM   1226  C  CE2 . PHE A 1 160  ? 49.503 53.598  14.341  1.00 9.65  ? 160  PHE A CE2 1 
ATOM   1227  C  CZ  . PHE A 1 160  ? 49.208 54.915  14.501  1.00 8.25  ? 160  PHE A CZ  1 
ATOM   1228  N  N   . VAL A 1 161  ? 43.550 52.242  11.131  1.00 4.96  ? 161  VAL A N   1 
ATOM   1229  C  CA  . VAL A 1 161  ? 42.581 51.747  10.179  1.00 5.75  ? 161  VAL A CA  1 
ATOM   1230  C  C   . VAL A 1 161  ? 42.780 52.543  8.898   1.00 6.48  ? 161  VAL A C   1 
ATOM   1231  O  O   . VAL A 1 161  ? 42.902 53.764  8.929   1.00 7.55  ? 161  VAL A O   1 
ATOM   1232  C  CB  . VAL A 1 161  ? 41.136 51.807  10.747  1.00 5.70  ? 161  VAL A CB  1 
ATOM   1233  C  CG1 . VAL A 1 161  ? 40.996 50.790  11.879  1.00 6.45  ? 161  VAL A CG1 1 
ATOM   1234  C  CG2 . VAL A 1 161  ? 40.783 53.163  11.242  1.00 6.89  ? 161  VAL A CG2 1 
ATOM   1235  N  N   . THR A 1 162  ? 42.839 51.788  7.799   1.00 6.61  ? 162  THR A N   1 
ATOM   1236  C  CA  . THR A 1 162  ? 43.192 52.295  6.456   1.00 7.59  ? 162  THR A CA  1 
ATOM   1237  C  C   . THR A 1 162  ? 44.657 52.725  6.394   1.00 6.52  ? 162  THR A C   1 
ATOM   1238  O  O   . THR A 1 162  ? 45.460 52.163  5.660   1.00 7.87  ? 162  THR A O   1 
ATOM   1239  C  CB  . THR A 1 162  ? 42.304 53.444  5.956   1.00 8.79  ? 162  THR A CB  1 
ATOM   1240  O  OG1 . THR A 1 162  ? 40.917 53.081  6.071   1.00 10.63 ? 162  THR A OG1 1 
ATOM   1241  C  CG2 . THR A 1 162  ? 42.535 53.622  4.427   1.00 12.35 ? 162  THR A CG2 1 
ATOM   1242  N  N   . GLY A 1 163  ? 44.981 53.747  7.155   1.00 6.67  ? 163  GLY A N   1 
ATOM   1243  C  CA  . GLY A 1 163  ? 46.344 54.224  7.189   1.00 6.17  ? 163  GLY A CA  1 
ATOM   1244  C  C   . GLY A 1 163  ? 46.681 55.161  6.032   1.00 5.19  ? 163  GLY A C   1 
ATOM   1245  O  O   . GLY A 1 163  ? 47.843 55.388  5.744   1.00 6.53  ? 163  GLY A O   1 
ATOM   1246  N  N   . GLY A 1 164  ? 45.670 55.752  5.406   1.00 5.25  ? 164  GLY A N   1 
ATOM   1247  C  CA  . GLY A 1 164  ? 45.957 56.783  4.422   1.00 5.18  ? 164  GLY A CA  1 
ATOM   1248  C  C   . GLY A 1 164  ? 46.259 58.121  5.048   1.00 5.00  ? 164  GLY A C   1 
ATOM   1249  O  O   . GLY A 1 164  ? 45.970 58.373  6.232   1.00 5.94  ? 164  GLY A O   1 
ATOM   1250  N  N   . TRP A 1 165  ? 46.866 58.994  4.259   1.00 4.48  ? 165  TRP A N   1 
ATOM   1251  C  CA  . TRP A 1 165  ? 47.099 60.335  4.750   1.00 4.71  ? 165  TRP A CA  1 
ATOM   1252  C  C   . TRP A 1 165  ? 45.785 60.982  5.205   1.00 4.61  ? 165  TRP A C   1 
ATOM   1253  O  O   . TRP A 1 165  ? 45.753 61.737  6.194   1.00 4.89  ? 165  TRP A O   1 
ATOM   1254  C  CB  . TRP A 1 165  ? 47.719 61.151  3.613   1.00 4.98  ? 165  TRP A CB  1 
ATOM   1255  C  CG  . TRP A 1 165  ? 48.525 62.299  4.072   1.00 4.98  ? 165  TRP A CG  1 
ATOM   1256  C  CD1 . TRP A 1 165  ? 48.319 63.615  3.773   1.00 6.45  ? 165  TRP A CD1 1 
ATOM   1257  C  CD2 . TRP A 1 165  ? 49.741 62.240  4.840   1.00 5.71  ? 165  TRP A CD2 1 
ATOM   1258  N  NE1 . TRP A 1 165  ? 49.308 64.400  4.344   1.00 6.65  ? 165  TRP A NE1 1 
ATOM   1259  C  CE2 . TRP A 1 165  ? 50.190 63.574  5.005   1.00 5.70  ? 165  TRP A CE2 1 
ATOM   1260  C  CE3 . TRP A 1 165  ? 50.467 61.200  5.427   1.00 7.25  ? 165  TRP A CE3 1 
ATOM   1261  C  CZ2 . TRP A 1 165  ? 51.353 63.879  5.776   1.00 7.59  ? 165  TRP A CZ2 1 
ATOM   1262  C  CZ3 . TRP A 1 165  ? 51.626 61.509  6.164   1.00 8.69  ? 165  TRP A CZ3 1 
ATOM   1263  C  CH2 . TRP A 1 165  ? 52.038 62.827  6.315   1.00 7.47  ? 165  TRP A CH2 1 
ATOM   1264  N  N   . VAL A 1 166  ? 44.702 60.679  4.498   1.00 3.85  ? 166  VAL A N   1 
ATOM   1265  C  CA  . VAL A 1 166  ? 43.367 61.173  4.798   1.00 4.90  ? 166  VAL A CA  1 
ATOM   1266  C  C   . VAL A 1 166  ? 42.374 60.045  4.612   1.00 5.47  ? 166  VAL A C   1 
ATOM   1267  O  O   . VAL A 1 166  ? 42.766 58.912  4.281   1.00 6.22  ? 166  VAL A O   1 
ATOM   1268  C  CB  . VAL A 1 166  ? 42.967 62.327  3.855   1.00 4.69  ? 166  VAL A CB  1 
ATOM   1269  C  CG1 . VAL A 1 166  ? 43.955 63.463  3.967   1.00 5.26  ? 166  VAL A CG1 1 
ATOM   1270  C  CG2 . VAL A 1 166  ? 42.921 61.843  2.386   1.00 6.06  ? 166  VAL A CG2 1 
ATOM   1271  N  N   . MET A 1 167  ? 41.104 60.350  4.831   1.00 5.93  ? 167  MET A N   1 
ATOM   1272  C  CA  . MET A 1 167  ? 40.014 59.452  4.454   1.00 6.26  ? 167  MET A CA  1 
ATOM   1273  C  C   . MET A 1 167  ? 39.413 60.096  3.212   1.00 5.94  ? 167  MET A C   1 
ATOM   1274  O  O   . MET A 1 167  ? 38.685 61.068  3.328   1.00 6.42  ? 167  MET A O   1 
ATOM   1275  C  CB  . MET A 1 167  ? 39.000 59.380  5.594   1.00 5.86  ? 167  MET A CB  1 
ATOM   1276  C  CG  . MET A 1 167  ? 37.726 58.559  5.273   1.00 5.90  ? 167  MET A CG  1 
ATOM   1277  S  SD  . MET A 1 167  ? 36.536 58.735  6.677   1.00 7.75  ? 167  MET A SD  1 
ATOM   1278  C  CE  . MET A 1 167  ? 37.521 58.078  8.034   1.00 8.94  ? 167  MET A CE  1 
ATOM   1279  N  N   . PRO A 1 168  ? 39.754 59.612  2.028   1.00 4.98  ? 168  PRO A N   1 
ATOM   1280  C  CA  . PRO A 1 168  ? 39.478 60.402  0.837   1.00 4.75  ? 168  PRO A CA  1 
ATOM   1281  C  C   . PRO A 1 168  ? 38.040 60.440  0.403   1.00 4.02  ? 168  PRO A C   1 
ATOM   1282  O  O   . PRO A 1 168  ? 37.264 59.496  0.659   1.00 4.83  ? 168  PRO A O   1 
ATOM   1283  C  CB  . PRO A 1 168  ? 40.316 59.718  -0.245  1.00 4.97  ? 168  PRO A CB  1 
ATOM   1284  C  CG  . PRO A 1 168  ? 40.418 58.311  0.211   1.00 6.65  ? 168  PRO A CG  1 
ATOM   1285  C  CD  . PRO A 1 168  ? 40.509 58.367  1.751   1.00 6.53  ? 168  PRO A CD  1 
ATOM   1286  N  N   . ASP A 1 169  ? 37.690 61.518  -0.294  1.00 4.53  ? 169  ASP A N   1 
ATOM   1287  C  CA  . ASP A 1 169  ? 36.491 61.498  -1.102  1.00 5.02  ? 169  ASP A CA  1 
ATOM   1288  C  C   . ASP A 1 169  ? 36.588 60.365  -2.094  1.00 5.52  ? 169  ASP A C   1 
ATOM   1289  O  O   . ASP A 1 169  ? 37.685 59.984  -2.529  1.00 5.47  ? 169  ASP A O   1 
ATOM   1290  C  CB  . ASP A 1 169  ? 36.427 62.829  -1.854  1.00 5.66  ? 169  ASP A CB  1 
ATOM   1291  C  CG  . ASP A 1 169  ? 35.289 62.900  -2.837  1.00 7.07  ? 169  ASP A CG  1 
ATOM   1292  O  OD1 . ASP A 1 169  ? 34.150 62.447  -2.549  1.00 7.87  ? 169  ASP A OD1 1 
ATOM   1293  O  OD2 . ASP A 1 169  ? 35.451 63.439  -3.940  1.00 9.70  ? 169  ASP A OD2 1 
ATOM   1294  N  N   . GLU A 1 170  ? 35.427 59.808  -2.410  1.00 4.87  ? 170  GLU A N   1 
ATOM   1295  C  CA  . GLU A 1 170  ? 35.377 58.694  -3.353  1.00 5.74  ? 170  GLU A CA  1 
ATOM   1296  C  C   . GLU A 1 170  ? 34.693 59.065  -4.667  1.00 4.50  ? 170  GLU A C   1 
ATOM   1297  O  O   . GLU A 1 170  ? 34.749 58.277  -5.614  1.00 4.90  ? 170  GLU A O   1 
ATOM   1298  C  CB  . GLU A 1 170  ? 34.740 57.451  -2.688  1.00 5.84  ? 170  GLU A CB  1 
ATOM   1299  C  CG  . GLU A 1 170  ? 35.505 57.066  -1.418  1.00 8.24  ? 170  GLU A CG  1 
ATOM   1300  C  CD  . GLU A 1 170  ? 35.039 55.783  -0.768  1.00 9.24  ? 170  GLU A CD  1 
ATOM   1301  O  OE1 . GLU A 1 170  ? 34.357 54.983  -1.446  1.00 8.10  ? 170  GLU A OE1 1 
ATOM   1302  O  OE2 . GLU A 1 170  ? 35.401 55.564  0.405   1.00 9.76  ? 170  GLU A OE2 1 
ATOM   1303  N  N   . ALA A 1 171  ? 34.109 60.256  -4.753  1.00 4.72  ? 171  ALA A N   1 
ATOM   1304  C  CA  . ALA A 1 171  ? 33.379 60.642  -5.949  1.00 4.81  ? 171  ALA A CA  1 
ATOM   1305  C  C   . ALA A 1 171  ? 34.254 61.412  -6.936  1.00 4.45  ? 171  ALA A C   1 
ATOM   1306  O  O   . ALA A 1 171  ? 34.264 61.128  -8.129  1.00 6.33  ? 171  ALA A O   1 
ATOM   1307  C  CB  . ALA A 1 171  ? 32.176 61.464  -5.577  1.00 5.65  ? 171  ALA A CB  1 
ATOM   1308  N  N   . ASN A 1 172  ? 34.982 62.413  -6.431  1.00 4.93  ? 172  ASN A N   1 
ATOM   1309  C  CA  . ASN A 1 172  ? 35.696 63.317  -7.336  1.00 4.66  ? 172  ASN A CA  1 
ATOM   1310  C  C   . ASN A 1 172  ? 37.156 62.952  -7.507  1.00 5.32  ? 172  ASN A C   1 
ATOM   1311  O  O   . ASN A 1 172  ? 37.820 63.413  -8.425  1.00 5.21  ? 172  ASN A O   1 
ATOM   1312  C  CB  . ASN A 1 172  ? 35.674 64.743  -6.755  1.00 4.74  ? 172  ASN A CB  1 
ATOM   1313  C  CG  . ASN A 1 172  ? 34.283 65.288  -6.649  1.00 8.01  ? 172  ASN A CG  1 
ATOM   1314  O  OD1 . ASN A 1 172  ? 33.588 65.442  -7.646  1.00 12.18 ? 172  ASN A OD1 1 
ATOM   1315  N  ND2 . ASN A 1 172  ? 33.872 65.622  -5.433  1.00 8.27  ? 172  ASN A ND2 1 
ATOM   1316  N  N   . SER A 1 173  ? 37.660 62.136  -6.595  1.00 4.05  ? 173  SER A N   1 
ATOM   1317  C  CA  . SER A 1 173  ? 39.090 61.816  -6.564  1.00 4.83  ? 173  SER A CA  1 
ATOM   1318  C  C   . SER A 1 173  ? 39.478 60.919  -7.716  1.00 4.99  ? 173  SER A C   1 
ATOM   1319  O  O   . SER A 1 173  ? 38.754 59.991  -8.095  1.00 5.64  ? 173  SER A O   1 
ATOM   1320  C  CB  . SER A 1 173  ? 39.420 61.114  -5.248  1.00 5.53  ? 173  SER A CB  1 
ATOM   1321  O  OG  . SER A 1 173  ? 38.518 60.023  -5.084  1.00 6.15  ? 173  SER A OG  1 
ATOM   1322  N  N   . HIS A 1 174  ? 40.659 61.159  -8.262  1.00 4.00  ? 174  HIS A N   1 
ATOM   1323  C  CA  . HIS A 1 174  ? 41.175 60.266  -9.300  1.00 3.04  ? 174  HIS A CA  1 
ATOM   1324  C  C   . HIS A 1 174  ? 41.816 59.086  -8.583  1.00 3.44  ? 174  HIS A C   1 
ATOM   1325  O  O   . HIS A 1 174  ? 42.464 59.268  -7.545  1.00 4.02  ? 174  HIS A O   1 
ATOM   1326  C  CB  . HIS A 1 174  ? 42.205 60.997  -10.113 1.00 5.19  ? 174  HIS A CB  1 
ATOM   1327  C  CG  . HIS A 1 174  ? 42.477 60.327  -11.385 1.00 5.81  ? 174  HIS A CG  1 
ATOM   1328  N  ND1 . HIS A 1 174  ? 43.274 59.214  -11.445 1.00 6.34  ? 174  HIS A ND1 1 
ATOM   1329  C  CD2 . HIS A 1 174  ? 42.037 60.577  -12.651 1.00 6.46  ? 174  HIS A CD2 1 
ATOM   1330  C  CE1 . HIS A 1 174  ? 43.321 58.804  -12.708 1.00 8.28  ? 174  HIS A CE1 1 
ATOM   1331  N  NE2 . HIS A 1 174  ? 42.569 59.602  -13.447 1.00 7.79  ? 174  HIS A NE2 1 
ATOM   1332  N  N   . TRP A 1 175  ? 41.707 57.878  -9.138  1.00 3.26  ? 175  TRP A N   1 
ATOM   1333  C  CA  . TRP A 1 175  ? 42.308 56.726  -8.475  1.00 3.22  ? 175  TRP A CA  1 
ATOM   1334  C  C   . TRP A 1 175  ? 43.790 56.890  -8.216  1.00 4.40  ? 175  TRP A C   1 
ATOM   1335  O  O   . TRP A 1 175  ? 44.303 56.355  -7.242  1.00 4.72  ? 175  TRP A O   1 
ATOM   1336  C  CB  . TRP A 1 175  ? 42.057 55.448  -9.278  1.00 4.65  ? 175  TRP A CB  1 
ATOM   1337  C  CG  . TRP A 1 175  ? 42.862 55.256  -10.539 1.00 4.88  ? 175  TRP A CG  1 
ATOM   1338  C  CD1 . TRP A 1 175  ? 42.526 55.633  -11.829 1.00 5.85  ? 175  TRP A CD1 1 
ATOM   1339  C  CD2 . TRP A 1 175  ? 44.125 54.624  -10.615 1.00 4.87  ? 175  TRP A CD2 1 
ATOM   1340  N  NE1 . TRP A 1 175  ? 43.537 55.240  -12.693 1.00 5.46  ? 175  TRP A NE1 1 
ATOM   1341  C  CE2 . TRP A 1 175  ? 44.521 54.607  -11.979 1.00 5.76  ? 175  TRP A CE2 1 
ATOM   1342  C  CE3 . TRP A 1 175  ? 44.968 54.026  -9.663  1.00 6.39  ? 175  TRP A CE3 1 
ATOM   1343  C  CZ2 . TRP A 1 175  ? 45.751 54.053  -12.415 1.00 7.11  ? 175  TRP A CZ2 1 
ATOM   1344  C  CZ3 . TRP A 1 175  ? 46.166 53.461  -10.107 1.00 6.88  ? 175  TRP A CZ3 1 
ATOM   1345  C  CH2 . TRP A 1 175  ? 46.548 53.487  -11.471 1.00 7.10  ? 175  TRP A CH2 1 
ATOM   1346  N  N   . ARG A 1 176  ? 44.495 57.583  -9.087  1.00 4.68  ? 176  ARG A N   1 
ATOM   1347  C  CA  . ARG A 1 176  ? 45.925 57.743  -8.922  1.00 4.90  ? 176  ARG A CA  1 
ATOM   1348  C  C   . ARG A 1 176  ? 46.197 58.516  -7.624  1.00 4.86  ? 176  ARG A C   1 
ATOM   1349  O  O   . ARG A 1 176  ? 47.152 58.236  -6.913  1.00 5.16  ? 176  ARG A O   1 
ATOM   1350  C  CB  . ARG A 1 176  ? 46.509 58.467  -10.149 1.00 7.21  ? 176  ARG A CB  1 
ATOM   1351  C  CG  . ARG A 1 176  ? 46.564 57.580  -11.386 1.00 8.92  ? 176  ARG A CG  1 
ATOM   1352  C  CD  . ARG A 1 176  ? 46.565 58.384  -12.694 1.00 12.64 ? 176  ARG A CD  1 
ATOM   1353  N  NE  . ARG A 1 176  ? 47.595 59.402  -12.745 1.00 12.85 ? 176  ARG A NE  1 
ATOM   1354  C  CZ  . ARG A 1 176  ? 47.718 60.269  -13.740 1.00 12.28 ? 176  ARG A CZ  1 
ATOM   1355  N  NH1 . ARG A 1 176  ? 46.857 60.234  -14.744 1.00 12.58 ? 176  ARG A NH1 1 
ATOM   1356  N  NH2 . ARG A 1 176  ? 48.649 61.201  -13.693 1.00 12.80 ? 176  ARG A NH2 1 
ATOM   1357  N  N   . ASN A 1 177  ? 45.316 59.457  -7.288  1.00 4.16  ? 177  ASN A N   1 
ATOM   1358  C  CA  . ASN A 1 177  ? 45.509 60.232  -6.058  1.00 4.76  ? 177  ASN A CA  1 
ATOM   1359  C  C   . ASN A 1 177  ? 44.986 59.524  -4.830  1.00 3.90  ? 177  ASN A C   1 
ATOM   1360  O  O   . ASN A 1 177  ? 45.508 59.731  -3.726  1.00 3.98  ? 177  ASN A O   1 
ATOM   1361  C  CB  . ASN A 1 177  ? 44.894 61.626  -6.158  1.00 5.74  ? 177  ASN A CB  1 
ATOM   1362  C  CG  . ASN A 1 177  ? 45.550 62.467  -7.215  1.00 7.26  ? 177  ASN A CG  1 
ATOM   1363  O  OD1 . ASN A 1 177  ? 46.740 62.314  -7.488  1.00 7.05  ? 177  ASN A OD1 1 
ATOM   1364  N  ND2 . ASN A 1 177  ? 44.775 63.385  -7.794  1.00 8.76  ? 177  ASN A ND2 1 
ATOM   1365  N  N   . VAL A 1 178  ? 43.995 58.660  -4.993  1.00 3.86  ? 178  VAL A N   1 
ATOM   1366  C  CA  . VAL A 1 178  ? 43.587 57.811  -3.879  1.00 3.79  ? 178  VAL A CA  1 
ATOM   1367  C  C   . VAL A 1 178  ? 44.774 56.911  -3.541  1.00 4.36  ? 178  VAL A C   1 
ATOM   1368  O  O   . VAL A 1 178  ? 45.111 56.724  -2.356  1.00 4.45  ? 178  VAL A O   1 
ATOM   1369  C  CB  . VAL A 1 178  ? 42.377 56.956  -4.283  1.00 4.29  ? 178  VAL A CB  1 
ATOM   1370  C  CG1 . VAL A 1 178  ? 42.045 56.002  -3.193  1.00 6.06  ? 178  VAL A CG1 1 
ATOM   1371  C  CG2 . VAL A 1 178  ? 41.181 57.862  -4.537  1.00 7.38  ? 178  VAL A CG2 1 
ATOM   1372  N  N   . LEU A 1 179  ? 45.446 56.354  -4.547  1.00 4.04  ? 179  LEU A N   1 
ATOM   1373  C  CA  . LEU A 1 179  ? 46.611 55.505  -4.294  1.00 4.05  ? 179  LEU A CA  1 
ATOM   1374  C  C   . LEU A 1 179  ? 47.741 56.335  -3.692  1.00 5.15  ? 179  LEU A C   1 
ATOM   1375  O  O   . LEU A 1 179  ? 48.420 55.895  -2.746  1.00 4.78  ? 179  LEU A O   1 
ATOM   1376  C  CB  . LEU A 1 179  ? 47.051 54.792  -5.592  1.00 4.98  ? 179  LEU A CB  1 
ATOM   1377  C  CG  . LEU A 1 179  ? 48.362 54.018  -5.449  1.00 4.64  ? 179  LEU A CG  1 
ATOM   1378  C  CD1 . LEU A 1 179  ? 48.198 52.934  -4.379  1.00 6.12  ? 179  LEU A CD1 1 
ATOM   1379  C  CD2 . LEU A 1 179  ? 48.730 53.398  -6.801  1.00 7.23  ? 179  LEU A CD2 1 
ATOM   1380  N  N   . LEU A 1 180  ? 47.938 57.554  -4.189  1.00 4.66  ? 180  LEU A N   1 
ATOM   1381  C  CA  . LEU A 1 180  ? 49.022 58.393  -3.675  1.00 4.71  ? 180  LEU A CA  1 
ATOM   1382  C  C   . LEU A 1 180  ? 48.872 58.623  -2.189  1.00 4.48  ? 180  LEU A C   1 
ATOM   1383  O  O   . LEU A 1 180  ? 49.825 58.491  -1.408  1.00 4.33  ? 180  LEU A O   1 
ATOM   1384  C  CB  . LEU A 1 180  ? 49.030 59.730  -4.453  1.00 5.41  ? 180  LEU A CB  1 
ATOM   1385  C  CG  . LEU A 1 180  ? 50.095 60.725  -4.026  1.00 6.71  ? 180  LEU A CG  1 
ATOM   1386  C  CD1 . LEU A 1 180  ? 51.381 60.231  -4.617  1.00 10.72 ? 180  LEU A CD1 1 
ATOM   1387  C  CD2 . LEU A 1 180  ? 49.710 62.072  -4.593  1.00 9.81  ? 180  LEU A CD2 1 
ATOM   1388  N  N   . GLN A 1 181  ? 47.662 59.033  -1.791  1.00 3.96  ? 181  GLN A N   1 
ATOM   1389  C  CA  . GLN A 1 181  ? 47.481 59.351  -0.370  1.00 4.23  ? 181  GLN A CA  1 
ATOM   1390  C  C   . GLN A 1 181  ? 47.563 58.097  0.497   1.00 4.07  ? 181  GLN A C   1 
ATOM   1391  O  O   . GLN A 1 181  ? 48.075 58.137  1.643   1.00 4.61  ? 181  GLN A O   1 
ATOM   1392  C  CB  . GLN A 1 181  ? 46.193 60.153  -0.150  1.00 4.72  ? 181  GLN A CB  1 
ATOM   1393  C  CG  . GLN A 1 181  ? 44.920 59.391  -0.366  1.00 3.90  ? 181  GLN A CG  1 
ATOM   1394  C  CD  . GLN A 1 181  ? 44.540 58.490  0.774   1.00 5.40  ? 181  GLN A CD  1 
ATOM   1395  O  OE1 . GLN A 1 181  ? 44.788 58.797  1.949   1.00 7.03  ? 181  GLN A OE1 1 
ATOM   1396  N  NE2 . GLN A 1 181  ? 43.899 57.389  0.422   1.00 6.43  ? 181  GLN A NE2 1 
ATOM   1397  N  N   . LEU A 1 182  ? 47.059 56.969  -0.015  1.00 3.87  ? 182  LEU A N   1 
ATOM   1398  C  CA  . LEU A 1 182  ? 47.174 55.717  0.738   1.00 4.02  ? 182  LEU A CA  1 
ATOM   1399  C  C   . LEU A 1 182  ? 48.639 55.389  0.939   1.00 5.02  ? 182  LEU A C   1 
ATOM   1400  O  O   . LEU A 1 182  ? 49.068 54.987  2.026   1.00 5.20  ? 182  LEU A O   1 
ATOM   1401  C  CB  . LEU A 1 182  ? 46.485 54.569  -0.006  1.00 4.31  ? 182  LEU A CB  1 
ATOM   1402  C  CG  . LEU A 1 182  ? 46.512 53.207  0.690   1.00 4.74  ? 182  LEU A CG  1 
ATOM   1403  C  CD1 . LEU A 1 182  ? 45.745 53.236  2.020   1.00 7.03  ? 182  LEU A CD1 1 
ATOM   1404  C  CD2 . LEU A 1 182  ? 45.924 52.165  -0.276  1.00 7.17  ? 182  LEU A CD2 1 
ATOM   1405  N  N   . THR A 1 183  ? 49.425 55.544  -0.113  1.00 4.44  ? 183  THR A N   1 
ATOM   1406  C  CA  . THR A 1 183  ? 50.846 55.188  -0.052  1.00 4.44  ? 183  THR A CA  1 
ATOM   1407  C  C   . THR A 1 183  ? 51.548 56.157  0.883   1.00 5.14  ? 183  THR A C   1 
ATOM   1408  O  O   . THR A 1 183  ? 52.441 55.740  1.644   1.00 5.35  ? 183  THR A O   1 
ATOM   1409  C  CB  . THR A 1 183  ? 51.425 55.287  -1.469  1.00 5.34  ? 183  THR A CB  1 
ATOM   1410  O  OG1 . THR A 1 183  ? 50.772 54.351  -2.318  1.00 5.87  ? 183  THR A OG1 1 
ATOM   1411  C  CG2 . THR A 1 183  ? 52.924 54.894  -1.483  1.00 6.79  ? 183  THR A CG2 1 
ATOM   1412  N  N   . GLU A 1 184  ? 51.165 57.413  0.892   1.00 5.23  ? 184  GLU A N   1 
ATOM   1413  C  CA  . GLU A 1 184  ? 51.848 58.382  1.759   1.00 6.01  ? 184  GLU A CA  1 
ATOM   1414  C  C   . GLU A 1 184  ? 51.652 57.999  3.219   1.00 5.89  ? 184  GLU A C   1 
ATOM   1415  O  O   . GLU A 1 184  ? 52.612 57.989  4.011   1.00 6.96  ? 184  GLU A O   1 
ATOM   1416  C  CB  . GLU A 1 184  ? 51.317 59.795  1.507   1.00 6.28  ? 184  GLU A CB  1 
ATOM   1417  C  CG  . GLU A 1 184  ? 52.220 60.919  1.980   1.00 9.24  ? 184  GLU A CG  1 
ATOM   1418  C  CD  . GLU A 1 184  ? 53.603 60.933  1.328   1.00 10.82 ? 184  GLU A CD  1 
ATOM   1419  O  OE1 . GLU A 1 184  ? 53.789 60.507  0.171   1.00 11.90 ? 184  GLU A OE1 1 
ATOM   1420  O  OE2 . GLU A 1 184  ? 54.527 61.378  2.016   1.00 13.62 ? 184  GLU A OE2 1 
ATOM   1421  N  N   . GLY A 1 185  ? 50.418 57.700  3.608   1.00 5.13  ? 185  GLY A N   1 
ATOM   1422  C  CA  . GLY A 1 185  ? 50.163 57.311  4.984   1.00 4.89  ? 185  GLY A CA  1 
ATOM   1423  C  C   . GLY A 1 185  ? 50.760 55.973  5.318   1.00 5.30  ? 185  GLY A C   1 
ATOM   1424  O  O   . GLY A 1 185  ? 51.346 55.808  6.416   1.00 5.71  ? 185  GLY A O   1 
ATOM   1425  N  N   . GLN A 1 186  ? 50.616 54.992  4.439   1.00 4.74  ? 186  GLN A N   1 
ATOM   1426  C  CA  . GLN A 1 186  ? 51.105 53.671  4.804   1.00 4.98  ? 186  GLN A CA  1 
ATOM   1427  C  C   . GLN A 1 186  ? 52.623 53.626  4.816   1.00 5.04  ? 186  GLN A C   1 
ATOM   1428  O  O   . GLN A 1 186  ? 53.206 52.876  5.607   1.00 5.08  ? 186  GLN A O   1 
ATOM   1429  C  CB  . GLN A 1 186  ? 50.541 52.568  3.896   1.00 5.65  ? 186  GLN A CB  1 
ATOM   1430  C  CG  . GLN A 1 186  ? 49.058 52.381  4.172   1.00 6.50  ? 186  GLN A CG  1 
ATOM   1431  C  CD  . GLN A 1 186  ? 48.609 51.001  3.914   1.00 8.84  ? 186  GLN A CD  1 
ATOM   1432  O  OE1 . GLN A 1 186  ? 49.258 50.309  3.160   1.00 11.81 ? 186  GLN A OE1 1 
ATOM   1433  N  NE2 . GLN A 1 186  ? 47.534 50.564  4.547   1.00 8.38  ? 186  GLN A NE2 1 
ATOM   1434  N  N   . THR A 1 187  ? 53.277 54.382  3.955   1.00 5.68  ? 187  THR A N   1 
ATOM   1435  C  CA  . THR A 1 187  ? 54.739 54.415  3.987   1.00 5.12  ? 187  THR A CA  1 
ATOM   1436  C  C   . THR A 1 187  ? 55.224 55.008  5.296   1.00 5.92  ? 187  THR A C   1 
ATOM   1437  O  O   . THR A 1 187  ? 56.170 54.455  5.910   1.00 6.51  ? 187  THR A O   1 
ATOM   1438  C  CB  . THR A 1 187  ? 55.261 55.164  2.773   1.00 5.94  ? 187  THR A CB  1 
ATOM   1439  O  OG1 . THR A 1 187  ? 54.795 54.459  1.609   1.00 6.07  ? 187  THR A OG1 1 
ATOM   1440  C  CG2 . THR A 1 187  ? 56.810 55.117  2.692   1.00 7.77  ? 187  THR A CG2 1 
ATOM   1441  N  N   . TRP A 1 188  ? 54.572 56.080  5.735   1.00 5.39  ? 188  TRP A N   1 
ATOM   1442  C  CA  . TRP A 1 188  ? 54.884 56.669  7.033   1.00 6.73  ? 188  TRP A CA  1 
ATOM   1443  C  C   . TRP A 1 188  ? 54.663 55.608  8.125   1.00 6.30  ? 188  TRP A C   1 
ATOM   1444  O  O   . TRP A 1 188  ? 55.545 55.390  8.986   1.00 6.32  ? 188  TRP A O   1 
ATOM   1445  C  CB  . TRP A 1 188  ? 54.011 57.913  7.268   1.00 6.69  ? 188  TRP A CB  1 
ATOM   1446  C  CG  . TRP A 1 188  ? 54.491 58.672  8.455   1.00 7.72  ? 188  TRP A CG  1 
ATOM   1447  C  CD1 . TRP A 1 188  ? 55.382 59.705  8.447   1.00 8.47  ? 188  TRP A CD1 1 
ATOM   1448  C  CD2 . TRP A 1 188  ? 54.181 58.403  9.831   1.00 7.82  ? 188  TRP A CD2 1 
ATOM   1449  N  NE1 . TRP A 1 188  ? 55.657 60.104  9.741   1.00 8.30  ? 188  TRP A NE1 1 
ATOM   1450  C  CE2 . TRP A 1 188  ? 54.930 59.326  10.612  1.00 6.71  ? 188  TRP A CE2 1 
ATOM   1451  C  CE3 . TRP A 1 188  ? 53.337 57.491  10.486  1.00 6.90  ? 188  TRP A CE3 1 
ATOM   1452  C  CZ2 . TRP A 1 188  ? 54.870 59.355  12.015  1.00 9.14  ? 188  TRP A CZ2 1 
ATOM   1453  C  CZ3 . TRP A 1 188  ? 53.302 57.500  11.892  1.00 8.79  ? 188  TRP A CZ3 1 
ATOM   1454  C  CH2 . TRP A 1 188  ? 54.069 58.443  12.632  1.00 7.74  ? 188  TRP A CH2 1 
ATOM   1455  N  N   . LEU A 1 189  ? 53.541 54.903  8.108   1.00 6.25  ? 189  LEU A N   1 
ATOM   1456  C  CA  . LEU A 1 189  ? 53.297 53.946  9.199   1.00 6.81  ? 189  LEU A CA  1 
ATOM   1457  C  C   . LEU A 1 189  ? 54.304 52.847  9.188   1.00 7.43  ? 189  LEU A C   1 
ATOM   1458  O  O   . LEU A 1 189  ? 54.683 52.375  10.295  1.00 7.85  ? 189  LEU A O   1 
ATOM   1459  C  CB  . LEU A 1 189  ? 51.900 53.322  9.090   1.00 7.26  ? 189  LEU A CB  1 
ATOM   1460  C  CG  . LEU A 1 189  ? 50.753 54.208  9.510   1.00 6.01  ? 189  LEU A CG  1 
ATOM   1461  C  CD1 . LEU A 1 189  ? 49.431 53.484  9.195   1.00 7.75  ? 189  LEU A CD1 1 
ATOM   1462  C  CD2 . LEU A 1 189  ? 50.854 54.459  11.025  1.00 8.11  ? 189  LEU A CD2 1 
ATOM   1463  N  N   . LYS A 1 190  ? 54.700 52.350  8.021   1.00 7.04  ? 190  LYS A N   1 
ATOM   1464  C  CA  . LYS A 1 190  ? 55.658 51.244  7.992   1.00 9.07  ? 190  LYS A CA  1 
ATOM   1465  C  C   . LYS A 1 190  ? 56.970 51.721  8.594   1.00 9.18  ? 190  LYS A C   1 
ATOM   1466  O  O   . LYS A 1 190  ? 57.570 51.017  9.412   1.00 10.00 ? 190  LYS A O   1 
ATOM   1467  C  CB  . LYS A 1 190  ? 55.899 50.714  6.583   1.00 10.12 ? 190  LYS A CB  1 
ATOM   1468  C  CG  . LYS A 1 190  ? 56.799 49.464  6.569   1.00 12.97 ? 190  LYS A CG  1 
ATOM   1469  C  CD  . LYS A 1 190  ? 56.997 48.946  5.168   1.00 19.00 ? 190  LYS A CD  1 
ATOM   1470  C  CE  . LYS A 1 190  ? 57.641 47.568  5.154   1.00 23.62 ? 190  LYS A CE  1 
ATOM   1471  N  NZ  . LYS A 1 190  ? 58.111 47.273  3.764   1.00 23.03 ? 190  LYS A NZ  1 
ATOM   1472  N  N   . GLN A 1 191  ? 57.412 52.913  8.214   1.00 9.51  ? 191  GLN A N   1 
ATOM   1473  C  CA  . GLN A 1 191  ? 58.708 53.414  8.639   1.00 13.32 ? 191  GLN A CA  1 
ATOM   1474  C  C   . GLN A 1 191  ? 58.728 53.693  10.124  1.00 12.35 ? 191  GLN A C   1 
ATOM   1475  O  O   . GLN A 1 191  ? 59.691 53.327  10.811  1.00 14.76 ? 191  GLN A O   1 
ATOM   1476  C  CB  . GLN A 1 191  ? 59.044 54.683  7.857   1.00 13.03 ? 191  GLN A CB  1 
ATOM   1477  C  CG  . GLN A 1 191  ? 60.432 55.267  8.187   1.00 18.97 ? 191  GLN A CG  1 
ATOM   1478  C  CD  . GLN A 1 191  ? 60.767 56.485  7.326   1.00 19.60 ? 191  GLN A CD  1 
ATOM   1479  O  OE1 . GLN A 1 191  ? 60.029 56.820  6.379   1.00 27.96 ? 191  GLN A OE1 1 
ATOM   1480  N  NE2 . GLN A 1 191  ? 61.860 57.164  7.665   1.00 28.91 ? 191  GLN A NE2 1 
ATOM   1481  N  N   . PHE A 1 192  ? 57.711 54.358  10.648  1.00 10.54 ? 192  PHE A N   1 
ATOM   1482  C  CA  . PHE A 1 192  ? 57.741 54.810  12.036  1.00 10.83 ? 192  PHE A CA  1 
ATOM   1483  C  C   . PHE A 1 192  ? 57.044 53.938  13.045  1.00 12.30 ? 192  PHE A C   1 
ATOM   1484  O  O   . PHE A 1 192  ? 57.474 53.913  14.215  1.00 14.00 ? 192  PHE A O   1 
ATOM   1485  C  CB  . PHE A 1 192  ? 57.247 56.251  12.121  1.00 10.50 ? 192  PHE A CB  1 
ATOM   1486  C  CG  . PHE A 1 192  ? 58.146 57.202  11.392  1.00 10.67 ? 192  PHE A CG  1 
ATOM   1487  C  CD1 . PHE A 1 192  ? 59.391 57.546  11.944  1.00 11.57 ? 192  PHE A CD1 1 
ATOM   1488  C  CD2 . PHE A 1 192  ? 57.829 57.686  10.134  1.00 12.13 ? 192  PHE A CD2 1 
ATOM   1489  C  CE1 . PHE A 1 192  ? 60.277 58.404  11.254  1.00 12.75 ? 192  PHE A CE1 1 
ATOM   1490  C  CE2 . PHE A 1 192  ? 58.712 58.538  9.425   1.00 12.74 ? 192  PHE A CE2 1 
ATOM   1491  C  CZ  . PHE A 1 192  ? 59.954 58.902  10.011  1.00 12.14 ? 192  PHE A CZ  1 
ATOM   1492  N  N   . MET A 1 193  ? 55.988 53.229  12.633  1.00 9.85  ? 193  MET A N   1 
ATOM   1493  C  CA  A MET A 1 193  ? 55.161 52.429  13.540  0.50 10.01 ? 193  MET A CA  1 
ATOM   1494  C  CA  B MET A 1 193  ? 55.195 52.432  13.561  0.50 10.17 ? 193  MET A CA  1 
ATOM   1495  C  C   . MET A 1 193  ? 55.303 50.938  13.289  1.00 10.14 ? 193  MET A C   1 
ATOM   1496  O  O   . MET A 1 193  ? 54.770 50.129  14.073  1.00 11.50 ? 193  MET A O   1 
ATOM   1497  C  CB  A MET A 1 193  ? 53.678 52.809  13.423  0.50 10.05 ? 193  MET A CB  1 
ATOM   1498  C  CB  B MET A 1 193  ? 53.734 52.890  13.535  0.50 10.21 ? 193  MET A CB  1 
ATOM   1499  C  CG  A MET A 1 193  ? 53.333 54.125  14.085  0.50 9.24  ? 193  MET A CG  1 
ATOM   1500  C  CG  B MET A 1 193  ? 53.600 54.403  13.641  0.50 10.28 ? 193  MET A CG  1 
ATOM   1501  S  SD  A MET A 1 193  ? 53.484 54.104  15.898  0.50 10.88 ? 193  MET A SD  1 
ATOM   1502  S  SD  B MET A 1 193  ? 54.465 55.166  15.034  0.50 15.65 ? 193  MET A SD  1 
ATOM   1503  C  CE  A MET A 1 193  ? 54.435 55.613  16.228  0.50 13.50 ? 193  MET A CE  1 
ATOM   1504  C  CE  B MET A 1 193  ? 53.415 54.699  16.318  0.50 11.73 ? 193  MET A CE  1 
ATOM   1505  N  N   . ASN A 1 194  ? 55.977 50.578  12.198  1.00 9.84  ? 194  ASN A N   1 
ATOM   1506  C  CA  . ASN A 1 194  ? 56.156 49.190  11.774  1.00 10.86 ? 194  ASN A CA  1 
ATOM   1507  C  C   . ASN A 1 194  ? 54.853 48.393  11.659  1.00 10.66 ? 194  ASN A C   1 
ATOM   1508  O  O   . ASN A 1 194  ? 54.752 47.234  12.120  1.00 12.02 ? 194  ASN A O   1 
ATOM   1509  C  CB  . ASN A 1 194  ? 57.109 48.479  12.750  1.00 12.40 ? 194  ASN A CB  1 
ATOM   1510  C  CG  . ASN A 1 194  ? 57.551 47.123  12.245  1.00 15.10 ? 194  ASN A CG  1 
ATOM   1511  O  OD1 . ASN A 1 194  ? 57.633 46.903  11.037  1.00 15.13 ? 194  ASN A OD1 1 
ATOM   1512  N  ND2 . ASN A 1 194  ? 57.819 46.193  13.178  1.00 17.14 ? 194  ASN A ND2 1 
ATOM   1513  N  N   . VAL A 1 195  ? 53.823 49.020  11.088  1.00 9.81  ? 195  VAL A N   1 
ATOM   1514  C  CA  . VAL A 1 195  ? 52.547 48.340  10.895  1.00 9.82  ? 195  VAL A CA  1 
ATOM   1515  C  C   . VAL A 1 195  ? 52.003 48.742  9.540   1.00 8.50  ? 195  VAL A C   1 
ATOM   1516  O  O   . VAL A 1 195  ? 52.262 49.869  9.094   1.00 8.51  ? 195  VAL A O   1 
ATOM   1517  C  CB  . VAL A 1 195  ? 51.479 48.717  11.991  1.00 10.70 ? 195  VAL A CB  1 
ATOM   1518  C  CG1 . VAL A 1 195  ? 51.828 48.179  13.386  1.00 15.27 ? 195  VAL A CG1 1 
ATOM   1519  C  CG2 . VAL A 1 195  ? 51.192 50.212  12.040  1.00 11.36 ? 195  VAL A CG2 1 
ATOM   1520  N  N   . THR A 1 196  ? 51.239 47.825  8.935   1.00 8.88  ? 196  THR A N   1 
ATOM   1521  C  CA  . THR A 1 196  ? 50.519 48.105  7.697   1.00 9.41  ? 196  THR A CA  1 
ATOM   1522  C  C   . THR A 1 196  ? 49.077 47.635  7.872   1.00 8.33  ? 196  THR A C   1 
ATOM   1523  O  O   . THR A 1 196  ? 48.839 46.419  7.938   1.00 8.94  ? 196  THR A O   1 
ATOM   1524  C  CB  . THR A 1 196  ? 51.170 47.335  6.513   1.00 10.43 ? 196  THR A CB  1 
ATOM   1525  O  OG1 . THR A 1 196  ? 52.531 47.784  6.323   1.00 12.37 ? 196  THR A OG1 1 
ATOM   1526  C  CG2 . THR A 1 196  ? 50.477 47.640  5.207   1.00 12.44 ? 196  THR A CG2 1 
ATOM   1527  N  N   . PRO A 1 197  ? 48.123 48.558  7.972   1.00 7.04  ? 197  PRO A N   1 
ATOM   1528  C  CA  . PRO A 1 197  ? 46.724 48.171  8.161   1.00 6.44  ? 197  PRO A CA  1 
ATOM   1529  C  C   . PRO A 1 197  ? 46.201 47.309  7.034   1.00 7.61  ? 197  PRO A C   1 
ATOM   1530  O  O   . PRO A 1 197  ? 46.555 47.568  5.883   1.00 7.08  ? 197  PRO A O   1 
ATOM   1531  C  CB  . PRO A 1 197  ? 45.988 49.527  8.165   1.00 7.90  ? 197  PRO A CB  1 
ATOM   1532  C  CG  . PRO A 1 197  ? 46.999 50.471  8.658   1.00 8.17  ? 197  PRO A CG  1 
ATOM   1533  C  CD  . PRO A 1 197  ? 48.298 50.016  8.085   1.00 7.91  ? 197  PRO A CD  1 
ATOM   1534  N  N   . THR A 1 198  ? 45.350 46.334  7.373   1.00 6.08  ? 198  THR A N   1 
ATOM   1535  C  CA  . THR A 1 198  ? 44.695 45.512  6.353   1.00 6.52  ? 198  THR A CA  1 
ATOM   1536  C  C   . THR A 1 198  ? 43.169 45.662  6.440   1.00 5.44  ? 198  THR A C   1 
ATOM   1537  O  O   . THR A 1 198  ? 42.455 44.972  5.725   1.00 6.22  ? 198  THR A O   1 
ATOM   1538  C  CB  . THR A 1 198  ? 45.057 44.031  6.478   1.00 8.39  ? 198  THR A CB  1 
ATOM   1539  O  OG1 . THR A 1 198  ? 44.659 43.577  7.785   1.00 10.76 ? 198  THR A OG1 1 
ATOM   1540  C  CG2 . THR A 1 198  ? 46.557 43.784  6.386   1.00 10.17 ? 198  THR A CG2 1 
ATOM   1541  N  N   . ALA A 1 199  ? 42.689 46.554  7.310   1.00 5.75  ? 199  ALA A N   1 
ATOM   1542  C  CA  . ALA A 1 199  ? 41.258 46.888  7.403   1.00 5.85  ? 199  ALA A CA  1 
ATOM   1543  C  C   . ALA A 1 199  ? 41.112 48.369  7.174   1.00 7.20  ? 199  ALA A C   1 
ATOM   1544  O  O   . ALA A 1 199  ? 41.877 49.156  7.737   1.00 6.55  ? 199  ALA A O   1 
ATOM   1545  C  CB  . ALA A 1 199  ? 40.727 46.564  8.807   1.00 8.00  ? 199  ALA A CB  1 
ATOM   1546  N  N   . SER A 1 200  ? 40.130 48.723  6.351   1.00 6.24  ? 200  SER A N   1 
ATOM   1547  C  CA  . SER A 1 200  ? 39.854 50.118  6.049   1.00 7.10  ? 200  SER A CA  1 
ATOM   1548  C  C   . SER A 1 200  ? 38.556 50.589  6.734   1.00 6.84  ? 200  SER A C   1 
ATOM   1549  O  O   . SER A 1 200  ? 37.618 49.796  6.917   1.00 7.17  ? 200  SER A O   1 
ATOM   1550  C  CB  . SER A 1 200  ? 39.749 50.263  4.546   1.00 7.38  ? 200  SER A CB  1 
ATOM   1551  O  OG  . SER A 1 200  ? 39.430 51.606  4.188   1.00 11.17 ? 200  SER A OG  1 
ATOM   1552  N  N   . TRP A 1 201  ? 38.531 51.875  7.083   1.00 6.88  ? 201  TRP A N   1 
ATOM   1553  C  CA  . TRP A 1 201  ? 37.427 52.520  7.807   1.00 7.32  ? 201  TRP A CA  1 
ATOM   1554  C  C   . TRP A 1 201  ? 37.098 53.798  7.065   1.00 7.54  ? 201  TRP A C   1 
ATOM   1555  O  O   . TRP A 1 201  ? 37.903 54.754  7.057   1.00 8.77  ? 201  TRP A O   1 
ATOM   1556  C  CB  . TRP A 1 201  ? 37.935 52.829  9.201   1.00 7.54  ? 201  TRP A CB  1 
ATOM   1557  C  CG  . TRP A 1 201  ? 37.146 53.636  10.163  1.00 7.16  ? 201  TRP A CG  1 
ATOM   1558  C  CD1 . TRP A 1 201  ? 37.332 54.965  10.472  1.00 7.66  ? 201  TRP A CD1 1 
ATOM   1559  C  CD2 . TRP A 1 201  ? 36.188 53.149  11.098  1.00 7.29  ? 201  TRP A CD2 1 
ATOM   1560  N  NE1 . TRP A 1 201  ? 36.511 55.329  11.513  1.00 8.35  ? 201  TRP A NE1 1 
ATOM   1561  C  CE2 . TRP A 1 201  ? 35.802 54.239  11.920  1.00 7.64  ? 201  TRP A CE2 1 
ATOM   1562  C  CE3 . TRP A 1 201  ? 35.598 51.908  11.312  1.00 7.96  ? 201  TRP A CE3 1 
ATOM   1563  C  CZ2 . TRP A 1 201  ? 34.860 54.115  12.937  1.00 8.75  ? 201  TRP A CZ2 1 
ATOM   1564  C  CZ3 . TRP A 1 201  ? 34.644 51.771  12.322  1.00 9.53  ? 201  TRP A CZ3 1 
ATOM   1565  C  CH2 . TRP A 1 201  ? 34.301 52.881  13.119  1.00 9.17  ? 201  TRP A CH2 1 
ATOM   1566  N  N   . ALA A 1 202  ? 35.941 53.818  6.407   1.00 6.25  ? 202  ALA A N   1 
ATOM   1567  C  CA  . ALA A 1 202  ? 35.513 55.006  5.657   1.00 6.52  ? 202  ALA A CA  1 
ATOM   1568  C  C   . ALA A 1 202  ? 34.109 55.383  6.107   1.00 6.29  ? 202  ALA A C   1 
ATOM   1569  O  O   . ALA A 1 202  ? 33.116 54.969  5.531   1.00 7.46  ? 202  ALA A O   1 
ATOM   1570  C  CB  . ALA A 1 202  ? 35.545 54.742  4.162   1.00 7.66  ? 202  ALA A CB  1 
ATOM   1571  N  N   . ILE A 1 203  ? 34.035 56.170  7.171   1.00 5.39  ? 203  ILE A N   1 
ATOM   1572  C  CA  . ILE A 1 203  ? 32.745 56.464  7.809   1.00 6.21  ? 203  ILE A CA  1 
ATOM   1573  C  C   . ILE A 1 203  ? 32.087 57.737  7.314   1.00 6.05  ? 203  ILE A C   1 
ATOM   1574  O  O   . ILE A 1 203  ? 30.903 57.946  7.561   1.00 6.89  ? 203  ILE A O   1 
ATOM   1575  C  CB  . ILE A 1 203  ? 32.856 56.472  9.355   1.00 5.61  ? 203  ILE A CB  1 
ATOM   1576  C  CG1 . ILE A 1 203  ? 33.928 57.456  9.829   1.00 6.35  ? 203  ILE A CG1 1 
ATOM   1577  C  CG2 . ILE A 1 203  ? 33.102 55.034  9.820   1.00 7.94  ? 203  ILE A CG2 1 
ATOM   1578  C  CD1 . ILE A 1 203  ? 33.884 57.763  11.304  1.00 6.41  ? 203  ILE A CD1 1 
ATOM   1579  N  N   . ASP A 1 204  ? 32.839 58.578  6.597   1.00 6.48  ? 204  ASP A N   1 
ATOM   1580  C  CA  . ASP A 1 204  ? 32.327 59.883  6.243   1.00 6.99  ? 204  ASP A CA  1 
ATOM   1581  C  C   . ASP A 1 204  ? 32.311 60.285  4.756   1.00 6.60  ? 204  ASP A C   1 
ATOM   1582  O  O   . ASP A 1 204  ? 31.581 61.246  4.460   1.00 8.43  ? 204  ASP A O   1 
ATOM   1583  C  CB  . ASP A 1 204  ? 33.023 60.973  7.076   1.00 6.72  ? 204  ASP A CB  1 
ATOM   1584  C  CG  . ASP A 1 204  ? 32.157 62.223  7.300   1.00 8.00  ? 204  ASP A CG  1 
ATOM   1585  O  OD1 . ASP A 1 204  ? 30.887 62.111  7.350   1.00 8.81  ? 204  ASP A OD1 1 
ATOM   1586  O  OD2 . ASP A 1 204  ? 32.654 63.347  7.507   1.00 7.80  ? 204  ASP A OD2 1 
ATOM   1587  N  N   . PRO A 1 205  ? 33.001 59.631  3.814   1.00 6.32  ? 205  PRO A N   1 
ATOM   1588  C  CA  . PRO A 1 205  ? 32.863 60.136  2.419   1.00 6.92  ? 205  PRO A CA  1 
ATOM   1589  C  C   . PRO A 1 205  ? 31.413 60.009  1.948   1.00 6.28  ? 205  PRO A C   1 
ATOM   1590  O  O   . PRO A 1 205  ? 30.641 59.149  2.393   1.00 6.63  ? 205  PRO A O   1 
ATOM   1591  C  CB  . PRO A 1 205  ? 33.787 59.236  1.603   1.00 8.10  ? 205  PRO A CB  1 
ATOM   1592  C  CG  . PRO A 1 205  ? 34.782 58.704  2.643   1.00 11.86 ? 205  PRO A CG  1 
ATOM   1593  C  CD  . PRO A 1 205  ? 33.904 58.461  3.878   1.00 8.88  ? 205  PRO A CD  1 
ATOM   1594  N  N   . PHE A 1 206  ? 31.025 60.896  1.025   1.00 5.17  ? 206  PHE A N   1 
ATOM   1595  C  CA  . PHE A 1 206  ? 29.594 61.069  0.784   1.00 6.68  ? 206  PHE A CA  1 
ATOM   1596  C  C   . PHE A 1 206  ? 29.117 60.161  -0.357  1.00 6.30  ? 206  PHE A C   1 
ATOM   1597  O  O   . PHE A 1 206  ? 28.898 60.604  -1.488  1.00 6.19  ? 206  PHE A O   1 
ATOM   1598  C  CB  . PHE A 1 206  ? 29.281 62.538  0.504   1.00 6.55  ? 206  PHE A CB  1 
ATOM   1599  C  CG  . PHE A 1 206  ? 30.082 63.527  1.357   1.00 6.59  ? 206  PHE A CG  1 
ATOM   1600  C  CD1 . PHE A 1 206  ? 30.299 63.305  2.706   1.00 6.12  ? 206  PHE A CD1 1 
ATOM   1601  C  CD2 . PHE A 1 206  ? 30.634 64.658  0.753   1.00 6.86  ? 206  PHE A CD2 1 
ATOM   1602  C  CE1 . PHE A 1 206  ? 31.051 64.233  3.458   1.00 7.84  ? 206  PHE A CE1 1 
ATOM   1603  C  CE2 . PHE A 1 206  ? 31.378 65.564  1.507   1.00 6.64  ? 206  PHE A CE2 1 
ATOM   1604  C  CZ  . PHE A 1 206  ? 31.575 65.343  2.839   1.00 7.43  ? 206  PHE A CZ  1 
ATOM   1605  N  N   . GLY A 1 207  ? 29.004 58.876  -0.039  1.00 5.87  ? 207  GLY A N   1 
ATOM   1606  C  CA  . GLY A 1 207  ? 28.816 57.848  -1.043  1.00 6.13  ? 207  GLY A CA  1 
ATOM   1607  C  C   . GLY A 1 207  ? 30.146 57.141  -1.275  1.00 5.45  ? 207  GLY A C   1 
ATOM   1608  O  O   . GLY A 1 207  ? 31.246 57.667  -0.988  1.00 6.22  ? 207  GLY A O   1 
ATOM   1609  N  N   . HIS A 1 208  ? 30.080 55.931  -1.813  1.00 5.12  ? 208  HIS A N   1 
ATOM   1610  C  CA  . HIS A 1 208  ? 31.249 55.048  -1.895  1.00 5.17  ? 208  HIS A CA  1 
ATOM   1611  C  C   . HIS A 1 208  ? 31.440 54.418  -3.282  1.00 5.05  ? 208  HIS A C   1 
ATOM   1612  O  O   . HIS A 1 208  ? 30.467 54.111  -3.984  1.00 5.43  ? 208  HIS A O   1 
ATOM   1613  C  CB  . HIS A 1 208  ? 31.151 53.929  -0.818  1.00 5.82  ? 208  HIS A CB  1 
ATOM   1614  C  CG  . HIS A 1 208  ? 31.198 54.432  0.595   1.00 6.02  ? 208  HIS A CG  1 
ATOM   1615  N  ND1 . HIS A 1 208  ? 32.385 54.701  1.242   1.00 8.99  ? 208  HIS A ND1 1 
ATOM   1616  C  CD2 . HIS A 1 208  ? 30.204 54.742  1.459   1.00 7.88  ? 208  HIS A CD2 1 
ATOM   1617  C  CE1 . HIS A 1 208  ? 32.101 55.140  2.463   1.00 8.78  ? 208  HIS A CE1 1 
ATOM   1618  N  NE2 . HIS A 1 208  ? 30.794 55.164  2.622   1.00 8.13  ? 208  HIS A NE2 1 
ATOM   1619  N  N   . SER A 1 209  ? 32.714 54.276  -3.651  1.00 4.21  ? 209  SER A N   1 
ATOM   1620  C  CA  . SER A 1 209  ? 33.110 53.832  -4.968  1.00 4.65  ? 209  SER A CA  1 
ATOM   1621  C  C   . SER A 1 209  ? 33.814 52.483  -4.914  1.00 4.39  ? 209  SER A C   1 
ATOM   1622  O  O   . SER A 1 209  ? 34.615 52.248  -4.016  1.00 5.18  ? 209  SER A O   1 
ATOM   1623  C  CB  . SER A 1 209  ? 34.114 54.829  -5.519  1.00 6.23  ? 209  SER A CB  1 
ATOM   1624  O  OG  . SER A 1 209  ? 34.582 54.327  -6.767  1.00 5.78  ? 209  SER A OG  1 
ATOM   1625  N  N   . PRO A 1 210  ? 33.568 51.605  -5.891  1.00 4.31  ? 210  PRO A N   1 
ATOM   1626  C  CA  . PRO A 1 210  ? 34.286 50.321  -5.931  1.00 4.59  ? 210  PRO A CA  1 
ATOM   1627  C  C   . PRO A 1 210  ? 35.755 50.521  -6.272  1.00 4.99  ? 210  PRO A C   1 
ATOM   1628  O  O   . PRO A 1 210  ? 36.536 49.579  -6.193  1.00 5.13  ? 210  PRO A O   1 
ATOM   1629  C  CB  . PRO A 1 210  ? 33.564 49.547  -7.041  1.00 4.50  ? 210  PRO A CB  1 
ATOM   1630  C  CG  . PRO A 1 210  ? 32.975 50.635  -7.899  1.00 5.51  ? 210  PRO A CG  1 
ATOM   1631  C  CD  . PRO A 1 210  ? 32.571 51.738  -6.969  1.00 4.51  ? 210  PRO A CD  1 
ATOM   1632  N  N   . THR A 1 211  ? 36.164 51.737  -6.642  1.00 4.79  ? 211  THR A N   1 
ATOM   1633  C  CA  . THR A 1 211  ? 37.588 51.979  -6.806  1.00 5.42  ? 211  THR A CA  1 
ATOM   1634  C  C   . THR A 1 211  ? 38.342 51.730  -5.515  1.00 5.37  ? 211  THR A C   1 
ATOM   1635  O  O   . THR A 1 211  ? 39.519 51.357  -5.544  1.00 5.51  ? 211  THR A O   1 
ATOM   1636  C  CB  . THR A 1 211  ? 37.788 53.421  -7.279  1.00 6.37  ? 211  THR A CB  1 
ATOM   1637  O  OG1 . THR A 1 211  ? 37.283 53.471  -8.618  1.00 7.49  ? 211  THR A OG1 1 
ATOM   1638  C  CG2 . THR A 1 211  ? 39.301 53.760  -7.324  1.00 8.24  ? 211  THR A CG2 1 
ATOM   1639  N  N   A MET A 1 212  ? 37.719 51.992  -4.382  0.50 4.97  ? 212  MET A N   1 
ATOM   1640  N  N   B MET A 1 212  ? 37.715 51.992  -4.388  0.50 5.42  ? 212  MET A N   1 
ATOM   1641  C  CA  A MET A 1 212  ? 38.370 51.723  -3.109  0.50 5.31  ? 212  MET A CA  1 
ATOM   1642  C  CA  B MET A 1 212  ? 38.365 51.723  -3.123  0.50 6.36  ? 212  MET A CA  1 
ATOM   1643  C  C   A MET A 1 212  ? 38.726 50.263  -2.844  0.50 5.46  ? 212  MET A C   1 
ATOM   1644  C  C   B MET A 1 212  ? 38.722 50.265  -2.843  0.50 5.87  ? 212  MET A C   1 
ATOM   1645  O  O   A MET A 1 212  ? 39.882 49.966  -2.631  0.50 5.63  ? 212  MET A O   1 
ATOM   1646  O  O   B MET A 1 212  ? 39.880 49.970  -2.628  0.50 6.10  ? 212  MET A O   1 
ATOM   1647  C  CB  A MET A 1 212  ? 37.571 52.312  -1.954  0.50 6.07  ? 212  MET A CB  1 
ATOM   1648  C  CB  B MET A 1 212  ? 37.613 52.371  -1.971  0.50 7.26  ? 212  MET A CB  1 
ATOM   1649  C  CG  A MET A 1 212  ? 37.299 53.766  -2.058  0.50 5.37  ? 212  MET A CG  1 
ATOM   1650  C  CG  B MET A 1 212  ? 38.445 52.395  -0.710  0.50 10.48 ? 212  MET A CG  1 
ATOM   1651  S  SD  A MET A 1 212  ? 38.773 54.780  -2.234  0.50 8.11  ? 212  MET A SD  1 
ATOM   1652  S  SD  B MET A 1 212  ? 39.754 53.605  -0.884  0.50 17.40 ? 212  MET A SD  1 
ATOM   1653  C  CE  A MET A 1 212  ? 39.552 54.636  -0.656  0.50 8.43  ? 212  MET A CE  1 
ATOM   1654  C  CE  B MET A 1 212  ? 38.892 54.716  -2.098  0.50 7.06  ? 212  MET A CE  1 
ATOM   1655  N  N   . PRO A 1 213  ? 37.760 49.348  -2.881  1.00 4.91  ? 213  PRO A N   1 
ATOM   1656  C  CA  . PRO A 1 213  ? 38.171 47.939  -2.749  1.00 4.86  ? 213  PRO A CA  1 
ATOM   1657  C  C   . PRO A 1 213  ? 39.158 47.521  -3.838  1.00 6.55  ? 213  PRO A C   1 
ATOM   1658  O  O   . PRO A 1 213  ? 40.023 46.659  -3.580  1.00 6.00  ? 213  PRO A O   1 
ATOM   1659  C  CB  . PRO A 1 213  ? 36.863 47.122  -2.807  1.00 6.23  ? 213  PRO A CB  1 
ATOM   1660  C  CG  . PRO A 1 213  ? 35.885 48.080  -3.466  1.00 6.63  ? 213  PRO A CG  1 
ATOM   1661  C  CD  . PRO A 1 213  ? 36.277 49.448  -2.936  1.00 6.07  ? 213  PRO A CD  1 
ATOM   1662  N  N   . TYR A 1 214  ? 39.035 48.076  -5.055  1.00 6.41  ? 214  TYR A N   1 
ATOM   1663  C  CA  . TYR A 1 214  ? 39.992 47.737  -6.117  1.00 6.63  ? 214  TYR A CA  1 
ATOM   1664  C  C   . TYR A 1 214  ? 41.414 48.020  -5.662  1.00 6.61  ? 214  TYR A C   1 
ATOM   1665  O  O   . TYR A 1 214  ? 42.305 47.155  -5.731  1.00 6.84  ? 214  TYR A O   1 
ATOM   1666  C  CB  . TYR A 1 214  ? 39.691 48.552  -7.353  1.00 7.59  ? 214  TYR A CB  1 
ATOM   1667  C  CG  . TYR A 1 214  ? 40.603 48.340  -8.557  1.00 8.85  ? 214  TYR A CG  1 
ATOM   1668  C  CD1 . TYR A 1 214  ? 40.305 47.368  -9.476  1.00 12.41 ? 214  TYR A CD1 1 
ATOM   1669  C  CD2 . TYR A 1 214  ? 41.720 49.110  -8.750  1.00 7.25  ? 214  TYR A CD2 1 
ATOM   1670  C  CE1 . TYR A 1 214  ? 41.107 47.170  -10.589 1.00 13.53 ? 214  TYR A CE1 1 
ATOM   1671  C  CE2 . TYR A 1 214  ? 42.540 48.917  -9.839  1.00 8.25  ? 214  TYR A CE2 1 
ATOM   1672  C  CZ  . TYR A 1 214  ? 42.220 47.954  -10.745 1.00 11.36 ? 214  TYR A CZ  1 
ATOM   1673  O  OH  . TYR A 1 214  ? 42.999 47.766  -11.874 1.00 12.27 ? 214  TYR A OH  1 
ATOM   1674  N  N   . ILE A 1 215  ? 41.646 49.245  -5.202  1.00 5.47  ? 215  ILE A N   1 
ATOM   1675  C  CA  . ILE A 1 215  ? 42.983 49.628  -4.781  1.00 4.99  ? 215  ILE A CA  1 
ATOM   1676  C  C   . ILE A 1 215  ? 43.380 48.929  -3.478  1.00 5.01  ? 215  ILE A C   1 
ATOM   1677  O  O   . ILE A 1 215  ? 44.522 48.481  -3.330  1.00 6.19  ? 215  ILE A O   1 
ATOM   1678  C  CB  . ILE A 1 215  ? 43.044 51.156  -4.574  1.00 4.67  ? 215  ILE A CB  1 
ATOM   1679  C  CG1 . ILE A 1 215  ? 42.885 51.886  -5.904  1.00 5.92  ? 215  ILE A CG1 1 
ATOM   1680  C  CG2 . ILE A 1 215  ? 44.351 51.552  -3.825  1.00 7.13  ? 215  ILE A CG2 1 
ATOM   1681  C  CD1 . ILE A 1 215  ? 42.781 53.353  -5.709  1.00 9.94  ? 215  ILE A CD1 1 
ATOM   1682  N  N   . LEU A 1 216  ? 42.460 48.859  -2.528  1.00 4.19  ? 216  LEU A N   1 
ATOM   1683  C  CA  . LEU A 1 216  ? 42.793 48.259  -1.248  1.00 4.89  ? 216  LEU A CA  1 
ATOM   1684  C  C   . LEU A 1 216  ? 43.159 46.799  -1.384  1.00 5.23  ? 216  LEU A C   1 
ATOM   1685  O  O   . LEU A 1 216  ? 44.153 46.344  -0.778  1.00 5.25  ? 216  LEU A O   1 
ATOM   1686  C  CB  . LEU A 1 216  ? 41.641 48.406  -0.273  1.00 5.39  ? 216  LEU A CB  1 
ATOM   1687  C  CG  . LEU A 1 216  ? 41.274 49.835  0.124   1.00 5.70  ? 216  LEU A CG  1 
ATOM   1688  C  CD1 . LEU A 1 216  ? 39.965 49.797  0.896   1.00 7.44  ? 216  LEU A CD1 1 
ATOM   1689  C  CD2 . LEU A 1 216  ? 42.345 50.497  0.983   1.00 7.96  ? 216  LEU A CD2 1 
ATOM   1690  N  N   . GLN A 1 217  ? 42.383 46.048  -2.162  1.00 5.33  ? 217  GLN A N   1 
ATOM   1691  C  CA  . GLN A 1 217  ? 42.684 44.635  -2.315  1.00 5.94  ? 217  GLN A CA  1 
ATOM   1692  C  C   . GLN A 1 217  ? 44.061 44.396  -2.943  1.00 6.93  ? 217  GLN A C   1 
ATOM   1693  O  O   . GLN A 1 217  ? 44.701 43.380  -2.665  1.00 8.78  ? 217  GLN A O   1 
ATOM   1694  C  CB  . GLN A 1 217  ? 41.534 43.958  -3.066  1.00 8.52  ? 217  GLN A CB  1 
ATOM   1695  C  CG  . GLN A 1 217  ? 41.567 42.413  -3.128  1.00 9.22  ? 217  GLN A CG  1 
ATOM   1696  C  CD  . GLN A 1 217  ? 42.469 41.879  -4.213  1.00 13.79 ? 217  GLN A CD  1 
ATOM   1697  O  OE1 . GLN A 1 217  ? 42.636 42.513  -5.248  1.00 13.92 ? 217  GLN A OE1 1 
ATOM   1698  N  NE2 . GLN A 1 217  ? 43.013 40.681  -4.002  1.00 16.31 ? 217  GLN A NE2 1 
ATOM   1699  N  N   . LYS A 1 218  ? 44.497 45.285  -3.826  1.00 5.76  ? 218  LYS A N   1 
ATOM   1700  C  CA  . LYS A 1 218  ? 45.819 45.185  -4.458  1.00 5.83  ? 218  LYS A CA  1 
ATOM   1701  C  C   . LYS A 1 218  ? 46.904 45.831  -3.592  1.00 6.32  ? 218  LYS A C   1 
ATOM   1702  O  O   . LYS A 1 218  ? 48.069 45.876  -3.970  1.00 5.95  ? 218  LYS A O   1 
ATOM   1703  C  CB  . LYS A 1 218  ? 45.771 45.874  -5.809  1.00 7.16  ? 218  LYS A CB  1 
ATOM   1704  C  CG  . LYS A 1 218  ? 44.905 45.152  -6.813  1.00 8.69  ? 218  LYS A CG  1 
ATOM   1705  C  CD  . LYS A 1 218  ? 44.664 45.989  -8.068  1.00 7.73  ? 218  LYS A CD  1 
ATOM   1706  C  CE  . LYS A 1 218  ? 44.311 45.109  -9.278  1.00 14.00 ? 218  LYS A CE  1 
ATOM   1707  N  NZ  . LYS A 1 218  ? 43.226 44.094  -9.099  1.00 14.79 ? 218  LYS A NZ  1 
ATOM   1708  N  N   . SER A 1 219  ? 46.511 46.290  -2.411  1.00 5.20  ? 219  SER A N   1 
ATOM   1709  C  CA  . SER A 1 219  ? 47.407 46.901  -1.424  1.00 5.70  ? 219  SER A CA  1 
ATOM   1710  C  C   . SER A 1 219  ? 47.422 46.098  -0.127  1.00 6.49  ? 219  SER A C   1 
ATOM   1711  O  O   . SER A 1 219  ? 47.802 46.657  0.897   1.00 6.74  ? 219  SER A O   1 
ATOM   1712  C  CB  . SER A 1 219  ? 47.018 48.356  -1.153  1.00 6.52  ? 219  SER A CB  1 
ATOM   1713  O  OG  . SER A 1 219  ? 47.104 49.094  -2.388  1.00 6.34  ? 219  SER A OG  1 
ATOM   1714  N  N   . GLY A 1 220  ? 47.059 44.820  -0.179  1.00 6.53  ? 220  GLY A N   1 
ATOM   1715  C  CA  . GLY A 1 220  ? 47.179 43.936  0.970   1.00 6.88  ? 220  GLY A CA  1 
ATOM   1716  C  C   . GLY A 1 220  ? 45.946 43.880  1.864   1.00 6.52  ? 220  GLY A C   1 
ATOM   1717  O  O   . GLY A 1 220  ? 45.939 43.117  2.844   1.00 7.83  ? 220  GLY A O   1 
ATOM   1718  N  N   . PHE A 1 221  ? 44.904 44.686  1.596   1.00 5.98  ? 221  PHE A N   1 
ATOM   1719  C  CA  . PHE A 1 221  ? 43.783 44.703  2.532   1.00 6.39  ? 221  PHE A CA  1 
ATOM   1720  C  C   . PHE A 1 221  ? 42.953 43.463  2.440   1.00 6.80  ? 221  PHE A C   1 
ATOM   1721  O  O   . PHE A 1 221  ? 42.861 42.815  1.388   1.00 7.38  ? 221  PHE A O   1 
ATOM   1722  C  CB  . PHE A 1 221  ? 42.884 45.912  2.278   1.00 6.44  ? 221  PHE A CB  1 
ATOM   1723  C  CG  . PHE A 1 221  ? 43.448 47.174  2.825   1.00 5.12  ? 221  PHE A CG  1 
ATOM   1724  C  CD1 . PHE A 1 221  ? 44.577 47.767  2.236   1.00 5.86  ? 221  PHE A CD1 1 
ATOM   1725  C  CD2 . PHE A 1 221  ? 42.864 47.809  3.907   1.00 5.60  ? 221  PHE A CD2 1 
ATOM   1726  C  CE1 . PHE A 1 221  ? 45.114 48.945  2.761   1.00 5.76  ? 221  PHE A CE1 1 
ATOM   1727  C  CE2 . PHE A 1 221  ? 43.403 48.941  4.443   1.00 7.75  ? 221  PHE A CE2 1 
ATOM   1728  C  CZ  . PHE A 1 221  ? 44.496 49.535  3.861   1.00 6.44  ? 221  PHE A CZ  1 
ATOM   1729  N  N   . LYS A 1 222  ? 42.296 43.172  3.564   1.00 6.52  ? 222  LYS A N   1 
ATOM   1730  C  CA  . LYS A 1 222  ? 41.403 42.034  3.661   1.00 7.49  ? 222  LYS A CA  1 
ATOM   1731  C  C   . LYS A 1 222  ? 39.991 42.433  3.999   1.00 6.81  ? 222  LYS A C   1 
ATOM   1732  O  O   . LYS A 1 222  ? 39.101 41.636  3.781   1.00 7.31  ? 222  LYS A O   1 
ATOM   1733  C  CB  . LYS A 1 222  ? 41.897 41.037  4.689   1.00 8.76  ? 222  LYS A CB  1 
ATOM   1734  C  CG  . LYS A 1 222  ? 43.282 40.525  4.453   1.00 12.92 ? 222  LYS A CG  1 
ATOM   1735  C  CD  . LYS A 1 222  ? 43.380 39.706  3.223   1.00 20.44 ? 222  LYS A CD  1 
ATOM   1736  C  CE  . LYS A 1 222  ? 44.826 39.284  3.004   1.00 26.33 ? 222  LYS A CE  1 
ATOM   1737  N  NZ  . LYS A 1 222  ? 44.994 38.730  1.635   1.00 30.02 ? 222  LYS A NZ  1 
ATOM   1738  N  N   . ASN A 1 223  ? 39.751 43.640  4.519   1.00 4.62  ? 223  ASN A N   1 
ATOM   1739  C  CA  . ASN A 1 223  ? 38.415 44.029  4.945   1.00 4.68  ? 223  ASN A CA  1 
ATOM   1740  C  C   . ASN A 1 223  ? 38.251 45.524  4.830   1.00 5.81  ? 223  ASN A C   1 
ATOM   1741  O  O   . ASN A 1 223  ? 39.216 46.269  4.944   1.00 6.20  ? 223  ASN A O   1 
ATOM   1742  C  CB  . ASN A 1 223  ? 38.179 43.678  6.425   1.00 5.32  ? 223  ASN A CB  1 
ATOM   1743  C  CG  . ASN A 1 223  ? 38.219 42.191  6.672   1.00 7.50  ? 223  ASN A CG  1 
ATOM   1744  O  OD1 . ASN A 1 223  ? 37.250 41.478  6.413   1.00 8.30  ? 223  ASN A OD1 1 
ATOM   1745  N  ND2 . ASN A 1 223  ? 39.355 41.726  7.157   1.00 8.08  ? 223  ASN A ND2 1 
ATOM   1746  N  N   . MET A 1 224  ? 37.017 45.961  4.646   1.00 4.86  ? 224  MET A N   1 
ATOM   1747  C  CA  . MET A 1 224  ? 36.719 47.386  4.624   1.00 6.20  ? 224  MET A CA  1 
ATOM   1748  C  C   . MET A 1 224  ? 35.352 47.674  5.191   1.00 5.98  ? 224  MET A C   1 
ATOM   1749  O  O   . MET A 1 224  ? 34.483 46.842  5.181   1.00 5.59  ? 224  MET A O   1 
ATOM   1750  C  CB  . MET A 1 224  ? 36.846 47.977  3.208   1.00 7.51  ? 224  MET A CB  1 
ATOM   1751  C  CG  . MET A 1 224  ? 35.829 47.466  2.232   1.00 8.69  ? 224  MET A CG  1 
ATOM   1752  S  SD  . MET A 1 224  ? 36.080 48.255  0.614   1.00 10.01 ? 224  MET A SD  1 
ATOM   1753  C  CE  . MET A 1 224  ? 35.766 49.938  1.017   1.00 12.47 ? 224  MET A CE  1 
ATOM   1754  N  N   . LEU A 1 225  ? 35.203 48.889  5.694   1.00 5.19  ? 225  LEU A N   1 
ATOM   1755  C  CA  . LEU A 1 225  ? 33.953 49.304  6.299   1.00 4.71  ? 225  LEU A CA  1 
ATOM   1756  C  C   . LEU A 1 225  ? 33.524 50.613  5.624   1.00 5.58  ? 225  LEU A C   1 
ATOM   1757  O  O   . LEU A 1 225  ? 34.327 51.509  5.413   1.00 5.62  ? 225  LEU A O   1 
ATOM   1758  C  CB  . LEU A 1 225  ? 34.144 49.482  7.813   1.00 5.87  ? 225  LEU A CB  1 
ATOM   1759  C  CG  . LEU A 1 225  ? 32.920 50.004  8.554   1.00 6.97  ? 225  LEU A CG  1 
ATOM   1760  C  CD1 . LEU A 1 225  ? 32.846 49.407  9.966   1.00 7.08  ? 225  LEU A CD1 1 
ATOM   1761  C  CD2 . LEU A 1 225  ? 32.924 51.542  8.582   1.00 7.12  ? 225  LEU A CD2 1 
ATOM   1762  N  N   . ILE A 1 226  ? 32.229 50.713  5.354   1.00 5.08  ? 226  ILE A N   1 
ATOM   1763  C  CA  . ILE A 1 226  ? 31.665 51.927  4.765   1.00 5.63  ? 226  ILE A CA  1 
ATOM   1764  C  C   . ILE A 1 226  ? 30.386 52.304  5.509   1.00 5.20  ? 226  ILE A C   1 
ATOM   1765  O  O   . ILE A 1 226  ? 29.801 51.462  6.233   1.00 5.91  ? 226  ILE A O   1 
ATOM   1766  C  CB  . ILE A 1 226  ? 31.379 51.702  3.253   1.00 5.76  ? 226  ILE A CB  1 
ATOM   1767  C  CG1 . ILE A 1 226  ? 30.303 50.633  3.038   1.00 6.31  ? 226  ILE A CG1 1 
ATOM   1768  C  CG2 . ILE A 1 226  ? 32.682 51.405  2.532   1.00 6.86  ? 226  ILE A CG2 1 
ATOM   1769  C  CD1 . ILE A 1 226  ? 29.955 50.418  1.519   1.00 7.21  ? 226  ILE A CD1 1 
ATOM   1770  N  N   . GLN A 1 227  ? 29.959 53.549  5.353   1.00 6.12  ? 227  GLN A N   1 
ATOM   1771  C  CA  . GLN A 1 227  ? 28.814 54.051  6.113   1.00 6.04  ? 227  GLN A CA  1 
ATOM   1772  C  C   . GLN A 1 227  ? 27.828 54.890  5.285   1.00 6.17  ? 227  GLN A C   1 
ATOM   1773  O  O   . GLN A 1 227  ? 26.616 54.736  5.476   1.00 6.94  ? 227  GLN A O   1 
ATOM   1774  C  CB  . GLN A 1 227  ? 29.319 54.901  7.273   1.00 7.38  ? 227  GLN A CB  1 
ATOM   1775  C  CG  . GLN A 1 227  ? 28.347 55.972  7.868   1.00 10.35 ? 227  GLN A CG  1 
ATOM   1776  C  CD  . GLN A 1 227  ? 27.041 55.450  8.414   1.00 10.38 ? 227  GLN A CD  1 
ATOM   1777  O  OE1 . GLN A 1 227  ? 26.944 54.306  8.820   1.00 13.53 ? 227  GLN A OE1 1 
ATOM   1778  N  NE2 . GLN A 1 227  ? 26.047 56.306  8.463   1.00 10.98 ? 227  GLN A NE2 1 
ATOM   1779  N  N   . ARG A 1 228  ? 28.295 55.804  4.464   1.00 5.99  ? 228  ARG A N   1 
ATOM   1780  C  CA  . ARG A 1 228  ? 27.351 56.726  3.876   1.00 6.44  ? 228  ARG A CA  1 
ATOM   1781  C  C   . ARG A 1 228  ? 26.802 56.155  2.592   1.00 6.22  ? 228  ARG A C   1 
ATOM   1782  O  O   . ARG A 1 228  ? 27.311 56.401  1.521   1.00 7.29  ? 228  ARG A O   1 
ATOM   1783  C  CB  . ARG A 1 228  ? 27.970 58.103  3.670   1.00 7.29  ? 228  ARG A CB  1 
ATOM   1784  C  CG  . ARG A 1 228  ? 28.066 58.945  4.921   1.00 7.22  ? 228  ARG A CG  1 
ATOM   1785  C  CD  . ARG A 1 228  ? 28.350 60.354  4.526   1.00 9.17  ? 228  ARG A CD  1 
ATOM   1786  N  NE  . ARG A 1 228  ? 28.672 61.257  5.625   1.00 7.67  ? 228  ARG A NE  1 
ATOM   1787  C  CZ  . ARG A 1 228  ? 27.780 61.980  6.279   1.00 10.53 ? 228  ARG A CZ  1 
ATOM   1788  N  NH1 . ARG A 1 228  ? 26.494 61.818  6.032   1.00 10.17 ? 228  ARG A NH1 1 
ATOM   1789  N  NH2 . ARG A 1 228  ? 28.163 62.800  7.234   1.00 13.20 ? 228  ARG A NH2 1 
ATOM   1790  N  N   . THR A 1 229  ? 25.754 55.366  2.742   1.00 6.36  ? 229  THR A N   1 
ATOM   1791  C  CA  . THR A 1 229  ? 25.039 54.871  1.590   1.00 5.38  ? 229  THR A CA  1 
ATOM   1792  C  C   . THR A 1 229  ? 23.581 55.270  1.734   1.00 6.29  ? 229  THR A C   1 
ATOM   1793  O  O   . THR A 1 229  ? 23.084 55.535  2.814   1.00 7.19  ? 229  THR A O   1 
ATOM   1794  C  CB  . THR A 1 229  ? 25.144 53.353  1.441   1.00 6.41  ? 229  THR A CB  1 
ATOM   1795  O  OG1 . THR A 1 229  ? 24.552 52.776  2.614   1.00 8.98  ? 229  THR A OG1 1 
ATOM   1796  C  CG2 . THR A 1 229  ? 26.590 52.910  1.439   1.00 6.91  ? 229  THR A CG2 1 
ATOM   1797  N  N   . HIS A 1 230  ? 22.905 55.331  0.606   1.00 5.35  ? 230  HIS A N   1 
ATOM   1798  C  CA  . HIS A 1 230  ? 21.508 55.772  0.615   1.00 6.20  ? 230  HIS A CA  1 
ATOM   1799  C  C   . HIS A 1 230  ? 20.666 55.016  1.636   1.00 6.41  ? 230  HIS A C   1 
ATOM   1800  O  O   . HIS A 1 230  ? 20.740 53.807  1.758   1.00 7.56  ? 230  HIS A O   1 
ATOM   1801  C  CB  . HIS A 1 230  ? 20.966 55.525  -0.792  1.00 6.14  ? 230  HIS A CB  1 
ATOM   1802  C  CG  . HIS A 1 230  ? 19.674 56.220  -1.116  1.00 7.64  ? 230  HIS A CG  1 
ATOM   1803  N  ND1 . HIS A 1 230  ? 18.491 55.936  -0.463  1.00 7.41  ? 230  HIS A ND1 1 
ATOM   1804  C  CD2 . HIS A 1 230  ? 19.377 57.145  -2.065  1.00 9.24  ? 230  HIS A CD2 1 
ATOM   1805  C  CE1 . HIS A 1 230  ? 17.530 56.695  -0.965  1.00 7.57  ? 230  HIS A CE1 1 
ATOM   1806  N  NE2 . HIS A 1 230  ? 18.036 57.425  -1.944  1.00 7.64  ? 230  HIS A NE2 1 
ATOM   1807  N  N   . TYR A 1 231  ? 19.833 55.760  2.359   1.00 7.39  ? 231  TYR A N   1 
ATOM   1808  C  CA  . TYR A 1 231  ? 19.033 55.128  3.392   1.00 7.05  ? 231  TYR A CA  1 
ATOM   1809  C  C   . TYR A 1 231  ? 18.135 54.019  2.858   1.00 7.39  ? 231  TYR A C   1 
ATOM   1810  O  O   . TYR A 1 231  ? 17.859 53.048  3.570   1.00 7.70  ? 231  TYR A O   1 
ATOM   1811  C  CB  . TYR A 1 231  ? 18.213 56.156  4.157   1.00 6.97  ? 231  TYR A CB  1 
ATOM   1812  C  CG  . TYR A 1 231  ? 17.211 56.934  3.319   1.00 8.14  ? 231  TYR A CG  1 
ATOM   1813  C  CD1 . TYR A 1 231  ? 15.897 56.464  3.135   1.00 7.76  ? 231  TYR A CD1 1 
ATOM   1814  C  CD2 . TYR A 1 231  ? 17.557 58.142  2.735   1.00 6.70  ? 231  TYR A CD2 1 
ATOM   1815  C  CE1 . TYR A 1 231  ? 14.975 57.179  2.364   1.00 9.67  ? 231  TYR A CE1 1 
ATOM   1816  C  CE2 . TYR A 1 231  ? 16.644 58.872  1.980   1.00 7.35  ? 231  TYR A CE2 1 
ATOM   1817  C  CZ  . TYR A 1 231  ? 15.354 58.372  1.806   1.00 7.55  ? 231  TYR A CZ  1 
ATOM   1818  O  OH  . TYR A 1 231  ? 14.441 59.093  1.053   1.00 10.25 ? 231  TYR A OH  1 
ATOM   1819  N  N   . SER A 1 232  ? 17.699 54.120  1.619   1.00 7.12  ? 232  SER A N   1 
ATOM   1820  C  CA  . SER A 1 232  ? 16.863 53.042  1.054   1.00 8.34  ? 232  SER A CA  1 
ATOM   1821  C  C   . SER A 1 232  ? 17.667 51.787  0.788   1.00 8.51  ? 232  SER A C   1 
ATOM   1822  O  O   . SER A 1 232  ? 17.154 50.660  0.887   1.00 8.77  ? 232  SER A O   1 
ATOM   1823  C  CB  . SER A 1 232  ? 16.207 53.463  -0.254  1.00 9.11  ? 232  SER A CB  1 
ATOM   1824  O  OG  . SER A 1 232  ? 15.331 54.532  -0.072  1.00 11.42 ? 232  SER A OG  1 
ATOM   1825  N  N   . VAL A 1 233  ? 18.931 51.960  0.395   1.00 7.88  ? 233  VAL A N   1 
ATOM   1826  C  CA  . VAL A 1 233  ? 19.835 50.842  0.197   1.00 7.86  ? 233  VAL A CA  1 
ATOM   1827  C  C   . VAL A 1 233  ? 20.119 50.133  1.535   1.00 7.95  ? 233  VAL A C   1 
ATOM   1828  O  O   . VAL A 1 233  ? 20.127 48.901  1.597   1.00 8.23  ? 233  VAL A O   1 
ATOM   1829  C  CB  . VAL A 1 233  ? 21.155 51.331  -0.469  1.00 7.99  ? 233  VAL A CB  1 
ATOM   1830  C  CG1 . VAL A 1 233  ? 22.158 50.211  -0.462  1.00 8.05  ? 233  VAL A CG1 1 
ATOM   1831  C  CG2 . VAL A 1 233  ? 20.838 51.702  -1.910  1.00 8.31  ? 233  VAL A CG2 1 
ATOM   1832  N  N   . LYS A 1 234  ? 20.409 50.910  2.576   1.00 6.76  ? 234  LYS A N   1 
ATOM   1833  C  CA  . LYS A 1 234  ? 20.618 50.307  3.906   1.00 7.27  ? 234  LYS A CA  1 
ATOM   1834  C  C   . LYS A 1 234  ? 19.390 49.467  4.263   1.00 7.31  ? 234  LYS A C   1 
ATOM   1835  O  O   . LYS A 1 234  ? 19.545 48.364  4.742   1.00 7.96  ? 234  LYS A O   1 
ATOM   1836  C  CB  . LYS A 1 234  ? 20.826 51.396  4.951   1.00 7.26  ? 234  LYS A CB  1 
ATOM   1837  C  CG  . LYS A 1 234  ? 22.195 52.077  4.875   1.00 7.93  ? 234  LYS A CG  1 
ATOM   1838  C  CD  . LYS A 1 234  ? 22.238 53.314  5.728   1.00 8.19  ? 234  LYS A CD  1 
ATOM   1839  C  CE  . LYS A 1 234  ? 23.631 54.031  5.685   1.00 8.03  ? 234  LYS A CE  1 
ATOM   1840  N  NZ  . LYS A 1 234  ? 24.513 53.520  6.783   1.00 8.06  ? 234  LYS A NZ  1 
ATOM   1841  N  N   . LYS A 1 235  ? 18.181 50.013  4.088   1.00 8.09  ? 235  LYS A N   1 
ATOM   1842  C  CA  . LYS A 1 235  ? 16.963 49.253  4.469   1.00 8.35  ? 235  LYS A CA  1 
ATOM   1843  C  C   . LYS A 1 235  ? 16.861 47.973  3.670   1.00 9.11  ? 235  LYS A C   1 
ATOM   1844  O  O   . LYS A 1 235  ? 16.609 46.909  4.240   1.00 9.48  ? 235  LYS A O   1 
ATOM   1845  C  CB  . LYS A 1 235  ? 15.726 50.110  4.287   1.00 9.00  ? 235  LYS A CB  1 
ATOM   1846  C  CG  . LYS A 1 235  ? 14.425 49.394  4.745   1.00 10.73 ? 235  LYS A CG  1 
ATOM   1847  C  CD  . LYS A 1 235  ? 13.282 50.390  4.706   1.00 12.87 ? 235  LYS A CD  1 
ATOM   1848  C  CE  . LYS A 1 235  ? 11.988 49.770  5.235   1.00 16.28 ? 235  LYS A CE  1 
ATOM   1849  N  NZ  . LYS A 1 235  ? 10.848 50.658  4.820   1.00 20.90 ? 235  LYS A NZ  1 
ATOM   1850  N  N   . GLU A 1 236  ? 17.097 48.051  2.365   1.00 9.11  ? 236  GLU A N   1 
ATOM   1851  C  CA  . GLU A 1 236  ? 16.967 46.893  1.482   1.00 9.92  ? 236  GLU A CA  1 
ATOM   1852  C  C   . GLU A 1 236  ? 17.982 45.807  1.836   1.00 10.36 ? 236  GLU A C   1 
ATOM   1853  O  O   . GLU A 1 236  ? 17.663 44.613  1.942   1.00 10.46 ? 236  GLU A O   1 
ATOM   1854  C  CB  . GLU A 1 236  ? 17.119 47.354  0.022   1.00 12.39 ? 236  GLU A CB  1 
ATOM   1855  C  CG  . GLU A 1 236  ? 16.873 46.298  -1.048  1.00 17.26 ? 236  GLU A CG  1 
ATOM   1856  C  CD  . GLU A 1 236  ? 15.398 45.901  -1.181  1.00 23.05 ? 236  GLU A CD  1 
ATOM   1857  O  OE1 . GLU A 1 236  ? 14.495 46.674  -0.767  1.00 27.28 ? 236  GLU A OE1 1 
ATOM   1858  O  OE2 . GLU A 1 236  ? 15.138 44.806  -1.714  1.00 29.00 ? 236  GLU A OE2 1 
ATOM   1859  N  N   . LEU A 1 237  ? 19.239 46.191  1.987   1.00 9.10  ? 237  LEU A N   1 
ATOM   1860  C  CA  . LEU A 1 237  ? 20.263 45.219  2.319   1.00 8.80  ? 237  LEU A CA  1 
ATOM   1861  C  C   . LEU A 1 237  ? 20.050 44.684  3.730   1.00 8.58  ? 237  LEU A C   1 
ATOM   1862  O  O   . LEU A 1 237  ? 20.299 43.509  3.991   1.00 9.58  ? 237  LEU A O   1 
ATOM   1863  C  CB  . LEU A 1 237  ? 21.669 45.804  2.148   1.00 7.90  ? 237  LEU A CB  1 
ATOM   1864  C  CG  . LEU A 1 237  ? 22.008 46.260  0.728   1.00 8.21  ? 237  LEU A CG  1 
ATOM   1865  C  CD1 . LEU A 1 237  ? 23.422 46.838  0.753   1.00 10.73 ? 237  LEU A CD1 1 
ATOM   1866  C  CD2 . LEU A 1 237  ? 21.951 45.141  -0.318  1.00 10.85 ? 237  LEU A CD2 1 
ATOM   1867  N  N   . ALA A 1 238  ? 19.623 45.529  4.659   1.00 8.27  ? 238  ALA A N   1 
ATOM   1868  C  CA  . ALA A 1 238  ? 19.438 45.054  6.041   1.00 8.53  ? 238  ALA A CA  1 
ATOM   1869  C  C   . ALA A 1 238  ? 18.350 43.974  6.098   1.00 9.77  ? 238  ALA A C   1 
ATOM   1870  O  O   . ALA A 1 238  ? 18.503 42.970  6.816   1.00 9.70  ? 238  ALA A O   1 
ATOM   1871  C  CB  . ALA A 1 238  ? 19.085 46.224  6.946   1.00 8.33  ? 238  ALA A CB  1 
ATOM   1872  N  N   . GLN A 1 239  ? 17.285 44.176  5.335   1.00 10.25 ? 239  GLN A N   1 
ATOM   1873  C  CA  . GLN A 1 239  ? 16.184 43.191  5.313   1.00 12.40 ? 239  GLN A CA  1 
ATOM   1874  C  C   . GLN A 1 239  ? 16.652 41.813  4.875   1.00 12.66 ? 239  GLN A C   1 
ATOM   1875  O  O   . GLN A 1 239  ? 16.086 40.817  5.291   1.00 14.47 ? 239  GLN A O   1 
ATOM   1876  C  CB  . GLN A 1 239  ? 15.041 43.703  4.447   1.00 14.06 ? 239  GLN A CB  1 
ATOM   1877  C  CG  . GLN A 1 239  ? 14.229 44.748  5.177   1.00 18.37 ? 239  GLN A CG  1 
ATOM   1878  C  CD  . GLN A 1 239  ? 13.235 45.497  4.306   1.00 23.25 ? 239  GLN A CD  1 
ATOM   1879  O  OE1 . GLN A 1 239  ? 13.364 45.551  3.083   1.00 25.82 ? 239  GLN A OE1 1 
ATOM   1880  N  NE2 . GLN A 1 239  ? 12.246 46.106  4.953   1.00 25.94 ? 239  GLN A NE2 1 
ATOM   1881  N  N   . GLN A 1 240  ? 17.696 41.756  4.063   1.00 11.42 ? 240  GLN A N   1 
ATOM   1882  C  CA  . GLN A 1 240  ? 18.195 40.514  3.505   1.00 10.74 ? 240  GLN A CA  1 
ATOM   1883  C  C   . GLN A 1 240  ? 19.500 40.055  4.168   1.00 9.58  ? 240  GLN A C   1 
ATOM   1884  O  O   . GLN A 1 240  ? 20.143 39.105  3.718   1.00 9.52  ? 240  GLN A O   1 
ATOM   1885  C  CB  . GLN A 1 240  ? 18.441 40.673  1.991   1.00 12.45 ? 240  GLN A CB  1 
ATOM   1886  C  CG  . GLN A 1 240  ? 17.231 41.168  1.197   1.00 15.46 ? 240  GLN A CG  1 
ATOM   1887  C  CD  . GLN A 1 240  ? 16.072 40.200  1.264   1.00 19.60 ? 240  GLN A CD  1 
ATOM   1888  O  OE1 . GLN A 1 240  ? 16.270 38.981  1.362   1.00 23.01 ? 240  GLN A OE1 1 
ATOM   1889  N  NE2 . GLN A 1 240  ? 14.849 40.737  1.231   1.00 24.84 ? 240  GLN A NE2 1 
ATOM   1890  N  N   . ARG A 1 241  ? 19.883 40.769  5.240   1.00 9.14  ? 241  ARG A N   1 
ATOM   1891  C  CA  A ARG A 1 241  ? 21.188 40.567  5.878   0.50 7.98  ? 241  ARG A CA  1 
ATOM   1892  C  CA  B ARG A 1 241  ? 21.194 40.561  5.871   0.50 8.11  ? 241  ARG A CA  1 
ATOM   1893  C  C   . ARG A 1 241  ? 22.306 40.529  4.845   1.00 7.67  ? 241  ARG A C   1 
ATOM   1894  O  O   . ARG A 1 241  ? 23.167 39.626  4.839   1.00 7.67  ? 241  ARG A O   1 
ATOM   1895  C  CB  A ARG A 1 241  ? 21.189 39.310  6.756   0.50 8.69  ? 241  ARG A CB  1 
ATOM   1896  C  CB  B ARG A 1 241  ? 21.229 39.291  6.730   0.50 8.79  ? 241  ARG A CB  1 
ATOM   1897  C  CG  A ARG A 1 241  ? 19.998 39.281  7.706   0.50 9.17  ? 241  ARG A CG  1 
ATOM   1898  C  CG  B ARG A 1 241  ? 20.420 39.447  7.986   0.50 10.19 ? 241  ARG A CG  1 
ATOM   1899  C  CD  A ARG A 1 241  ? 20.080 38.202  8.751   0.50 11.33 ? 241  ARG A CD  1 
ATOM   1900  C  CD  B ARG A 1 241  ? 20.351 38.200  8.828   0.50 12.78 ? 241  ARG A CD  1 
ATOM   1901  N  NE  A ARG A 1 241  ? 20.233 36.890  8.135   0.50 11.43 ? 241  ARG A NE  1 
ATOM   1902  N  NE  B ARG A 1 241  ? 19.323 38.348  9.854   0.50 15.45 ? 241  ARG A NE  1 
ATOM   1903  C  CZ  A ARG A 1 241  ? 20.708 35.827  8.765   0.50 11.97 ? 241  ARG A CZ  1 
ATOM   1904  C  CZ  B ARG A 1 241  ? 18.672 37.344  10.424  0.50 18.79 ? 241  ARG A CZ  1 
ATOM   1905  N  NH1 A ARG A 1 241  ? 21.064 35.918  10.030  0.50 12.74 ? 241  ARG A NH1 1 
ATOM   1906  N  NH1 B ARG A 1 241  ? 18.926 36.090  10.069  0.50 19.84 ? 241  ARG A NH1 1 
ATOM   1907  N  NH2 A ARG A 1 241  ? 20.825 34.669  8.124   0.50 12.48 ? 241  ARG A NH2 1 
ATOM   1908  N  NH2 B ARG A 1 241  ? 17.765 37.599  11.358  0.50 18.06 ? 241  ARG A NH2 1 
ATOM   1909  N  N   . GLN A 1 242  ? 22.300 41.563  3.989   1.00 6.58  ? 242  GLN A N   1 
ATOM   1910  C  CA  . GLN A 1 242  ? 23.336 41.697  2.957   1.00 7.40  ? 242  GLN A CA  1 
ATOM   1911  C  C   . GLN A 1 242  ? 24.173 42.959  3.193   1.00 6.98  ? 242  GLN A C   1 
ATOM   1912  O  O   . GLN A 1 242  ? 24.727 43.497  2.236   1.00 8.45  ? 242  GLN A O   1 
ATOM   1913  C  CB  . GLN A 1 242  ? 22.718 41.732  1.573   1.00 8.05  ? 242  GLN A CB  1 
ATOM   1914  C  CG  . GLN A 1 242  ? 22.060 40.434  1.171   1.00 9.04  ? 242  GLN A CG  1 
ATOM   1915  C  CD  . GLN A 1 242  ? 21.222 40.549  -0.096  1.00 9.65  ? 242  GLN A CD  1 
ATOM   1916  O  OE1 . GLN A 1 242  ? 20.641 41.601  -0.363  1.00 12.04 ? 242  GLN A OE1 1 
ATOM   1917  N  NE2 . GLN A 1 242  ? 21.174 39.468  -0.879  1.00 11.80 ? 242  GLN A NE2 1 
ATOM   1918  N  N   . LEU A 1 243  ? 24.279 43.382  4.457   1.00 6.38  ? 243  LEU A N   1 
ATOM   1919  C  CA  . LEU A 1 243  ? 25.132 44.515  4.799   1.00 5.61  ? 243  LEU A CA  1 
ATOM   1920  C  C   . LEU A 1 243  ? 26.598 44.148  4.870   1.00 6.33  ? 243  LEU A C   1 
ATOM   1921  O  O   . LEU A 1 243  ? 27.452 45.048  4.883   1.00 7.48  ? 243  LEU A O   1 
ATOM   1922  C  CB  . LEU A 1 243  ? 24.694 45.097  6.137   1.00 7.13  ? 243  LEU A CB  1 
ATOM   1923  C  CG  . LEU A 1 243  ? 23.301 45.726  6.132   1.00 7.65  ? 243  LEU A CG  1 
ATOM   1924  C  CD1 . LEU A 1 243  ? 22.807 45.852  7.559   1.00 10.54 ? 243  LEU A CD1 1 
ATOM   1925  C  CD2 . LEU A 1 243  ? 23.315 47.110  5.463   1.00 9.23  ? 243  LEU A CD2 1 
ATOM   1926  N  N   . GLU A 1 244  ? 26.933 42.870  4.949   1.00 5.96  ? 244  GLU A N   1 
ATOM   1927  C  CA  . GLU A 1 244  ? 28.314 42.422  4.807   1.00 6.19  ? 244  GLU A CA  1 
ATOM   1928  C  C   . GLU A 1 244  ? 28.350 41.611  3.541   1.00 6.21  ? 244  GLU A C   1 
ATOM   1929  O  O   . GLU A 1 244  ? 27.510 40.700  3.327   1.00 7.30  ? 244  GLU A O   1 
ATOM   1930  C  CB  . GLU A 1 244  ? 28.779 41.599  6.013   1.00 6.41  ? 244  GLU A CB  1 
ATOM   1931  C  CG  . GLU A 1 244  ? 29.010 42.496  7.224   1.00 7.76  ? 244  GLU A CG  1 
ATOM   1932  C  CD  . GLU A 1 244  ? 29.361 41.789  8.524   1.00 8.94  ? 244  GLU A CD  1 
ATOM   1933  O  OE1 . GLU A 1 244  ? 28.784 40.694  8.807   1.00 9.33  ? 244  GLU A OE1 1 
ATOM   1934  O  OE2 . GLU A 1 244  ? 30.216 42.353  9.268   1.00 8.36  ? 244  GLU A OE2 1 
ATOM   1935  N  N   . PHE A 1 245  ? 29.323 41.903  2.689   1.00 5.50  ? 245  PHE A N   1 
ATOM   1936  C  CA  . PHE A 1 245  ? 29.322 41.315  1.346   1.00 5.43  ? 245  PHE A CA  1 
ATOM   1937  C  C   . PHE A 1 245  ? 30.725 41.262  0.807   1.00 5.70  ? 245  PHE A C   1 
ATOM   1938  O  O   . PHE A 1 245  ? 31.596 42.017  1.230   1.00 6.12  ? 245  PHE A O   1 
ATOM   1939  C  CB  . PHE A 1 245  ? 28.406 42.077  0.355   1.00 6.69  ? 245  PHE A CB  1 
ATOM   1940  C  CG  . PHE A 1 245  ? 28.545 43.570  0.408   1.00 5.92  ? 245  PHE A CG  1 
ATOM   1941  C  CD1 . PHE A 1 245  ? 29.486 44.226  -0.383  1.00 5.66  ? 245  PHE A CD1 1 
ATOM   1942  C  CD2 . PHE A 1 245  ? 27.755 44.328  1.254   1.00 6.98  ? 245  PHE A CD2 1 
ATOM   1943  C  CE1 . PHE A 1 245  ? 29.609 45.609  -0.375  1.00 4.92  ? 245  PHE A CE1 1 
ATOM   1944  C  CE2 . PHE A 1 245  ? 27.894 45.726  1.292   1.00 6.79  ? 245  PHE A CE2 1 
ATOM   1945  C  CZ  . PHE A 1 245  ? 28.821 46.352  0.468   1.00 5.65  ? 245  PHE A CZ  1 
ATOM   1946  N  N   . LEU A 1 246  ? 30.923 40.420  -0.191  1.00 5.39  ? 246  LEU A N   1 
ATOM   1947  C  CA  . LEU A 1 246  ? 32.183 40.375  -0.910  1.00 6.03  ? 246  LEU A CA  1 
ATOM   1948  C  C   . LEU A 1 246  ? 32.072 41.290  -2.130  1.00 5.97  ? 246  LEU A C   1 
ATOM   1949  O  O   . LEU A 1 246  ? 31.370 40.984  -3.113  1.00 5.58  ? 246  LEU A O   1 
ATOM   1950  C  CB  . LEU A 1 246  ? 32.544 38.931  -1.305  1.00 6.86  ? 246  LEU A CB  1 
ATOM   1951  C  CG  . LEU A 1 246  ? 32.882 38.024  -0.109  1.00 10.13 ? 246  LEU A CG  1 
ATOM   1952  C  CD1 . LEU A 1 246  ? 32.725 36.562  -0.570  1.00 12.48 ? 246  LEU A CD1 1 
ATOM   1953  C  CD2 . LEU A 1 246  ? 34.299 38.348  0.384   1.00 13.26 ? 246  LEU A CD2 1 
ATOM   1954  N  N   . TRP A 1 247  ? 32.719 42.438  -2.032  1.00 5.19  ? 247  TRP A N   1 
ATOM   1955  C  CA  . TRP A 1 247  ? 32.534 43.469  -3.051  1.00 4.71  ? 247  TRP A CA  1 
ATOM   1956  C  C   . TRP A 1 247  ? 33.544 43.276  -4.141  1.00 4.84  ? 247  TRP A C   1 
ATOM   1957  O  O   . TRP A 1 247  ? 34.740 43.440  -3.904  1.00 4.96  ? 247  TRP A O   1 
ATOM   1958  C  CB  . TRP A 1 247  ? 32.739 44.832  -2.390  1.00 5.01  ? 247  TRP A CB  1 
ATOM   1959  C  CG  . TRP A 1 247  ? 32.252 46.017  -3.216  1.00 4.63  ? 247  TRP A CG  1 
ATOM   1960  C  CD1 . TRP A 1 247  ? 31.722 46.003  -4.476  1.00 5.20  ? 247  TRP A CD1 1 
ATOM   1961  C  CD2 . TRP A 1 247  ? 32.263 47.386  -2.800  1.00 4.42  ? 247  TRP A CD2 1 
ATOM   1962  N  NE1 . TRP A 1 247  ? 31.411 47.290  -4.883  1.00 4.72  ? 247  TRP A NE1 1 
ATOM   1963  C  CE2 . TRP A 1 247  ? 31.707 48.152  -3.844  1.00 4.43  ? 247  TRP A CE2 1 
ATOM   1964  C  CE3 . TRP A 1 247  ? 32.672 48.036  -1.632  1.00 4.85  ? 247  TRP A CE3 1 
ATOM   1965  C  CZ2 . TRP A 1 247  ? 31.607 49.558  -3.762  1.00 5.55  ? 247  TRP A CZ2 1 
ATOM   1966  C  CZ3 . TRP A 1 247  ? 32.534 49.415  -1.548  1.00 4.48  ? 247  TRP A CZ3 1 
ATOM   1967  C  CH2 . TRP A 1 247  ? 32.033 50.155  -2.599  1.00 5.78  ? 247  TRP A CH2 1 
ATOM   1968  N  N   . ARG A 1 248  ? 33.049 42.870  -5.334  1.00 4.87  ? 248  ARG A N   1 
ATOM   1969  C  CA  . ARG A 1 248  ? 33.921 42.677  -6.480  1.00 5.05  ? 248  ARG A CA  1 
ATOM   1970  C  C   . ARG A 1 248  ? 33.668 43.765  -7.521  1.00 5.42  ? 248  ARG A C   1 
ATOM   1971  O  O   . ARG A 1 248  ? 32.625 44.436  -7.500  1.00 5.88  ? 248  ARG A O   1 
ATOM   1972  C  CB  . ARG A 1 248  ? 33.696 41.301  -7.129  1.00 5.93  ? 248  ARG A CB  1 
ATOM   1973  C  CG  . ARG A 1 248  ? 32.356 41.146  -7.762  1.00 6.79  ? 248  ARG A CG  1 
ATOM   1974  C  CD  . ARG A 1 248  ? 32.280 39.877  -8.629  1.00 9.02  ? 248  ARG A CD  1 
ATOM   1975  N  NE  . ARG A 1 248  ? 32.317 38.702  -7.751  1.00 8.13  ? 248  ARG A NE  1 
ATOM   1976  C  CZ  . ARG A 1 248  ? 32.231 37.451  -8.197  1.00 12.56 ? 248  ARG A CZ  1 
ATOM   1977  N  NH1 . ARG A 1 248  ? 32.111 37.214  -9.504  1.00 13.18 ? 248  ARG A NH1 1 
ATOM   1978  N  NH2 . ARG A 1 248  ? 32.236 36.435  -7.338  1.00 12.59 ? 248  ARG A NH2 1 
ATOM   1979  N  N   . GLN A 1 249  ? 34.633 43.890  -8.440  1.00 5.49  ? 249  GLN A N   1 
ATOM   1980  C  CA  . GLN A 1 249  ? 34.483 44.854  -9.528  1.00 5.70  ? 249  GLN A CA  1 
ATOM   1981  C  C   . GLN A 1 249  ? 33.371 44.428  -10.492 1.00 6.93  ? 249  GLN A C   1 
ATOM   1982  O  O   . GLN A 1 249  ? 33.092 43.235  -10.651 1.00 7.41  ? 249  GLN A O   1 
ATOM   1983  C  CB  . GLN A 1 249  ? 35.821 45.028  -10.232 1.00 6.67  ? 249  GLN A CB  1 
ATOM   1984  C  CG  . GLN A 1 249  ? 36.900 45.558  -9.291  1.00 6.87  ? 249  GLN A CG  1 
ATOM   1985  C  CD  . GLN A 1 249  ? 36.494 46.876  -8.645  1.00 7.02  ? 249  GLN A CD  1 
ATOM   1986  O  OE1 . GLN A 1 249  ? 36.164 47.856  -9.341  1.00 6.86  ? 249  GLN A OE1 1 
ATOM   1987  N  NE2 . GLN A 1 249  ? 36.479 46.908  -7.322  1.00 6.30  ? 249  GLN A NE2 1 
ATOM   1988  N  N   . ILE A 1 250  ? 32.763 45.409  -11.155 1.00 6.99  ? 250  ILE A N   1 
ATOM   1989  C  CA  . ILE A 1 250  ? 31.605 45.132  -11.993 1.00 7.31  ? 250  ILE A CA  1 
ATOM   1990  C  C   . ILE A 1 250  ? 31.888 44.189  -13.152 1.00 8.23  ? 250  ILE A C   1 
ATOM   1991  O  O   . ILE A 1 250  ? 30.984 43.543  -13.621 1.00 8.81  ? 250  ILE A O   1 
ATOM   1992  C  CB  . ILE A 1 250  ? 30.907 46.433  -12.498 1.00 8.24  ? 250  ILE A CB  1 
ATOM   1993  C  CG1 . ILE A 1 250  ? 31.863 47.329  -13.262 1.00 9.03  ? 250  ILE A CG1 1 
ATOM   1994  C  CG2 . ILE A 1 250  ? 30.254 47.209  -11.343 1.00 9.34  ? 250  ILE A CG2 1 
ATOM   1995  C  CD1 . ILE A 1 250  ? 31.257 48.659  -13.755 1.00 11.08 ? 250  ILE A CD1 1 
ATOM   1996  N  N   . TRP A 1 251  ? 33.136 44.143  -13.596 1.00 8.89  ? 251  TRP A N   1 
ATOM   1997  C  CA  . TRP A 1 251  ? 33.462 43.290  -14.750 1.00 10.62 ? 251  TRP A CA  1 
ATOM   1998  C  C   . TRP A 1 251  ? 34.046 41.938  -14.334 1.00 12.64 ? 251  TRP A C   1 
ATOM   1999  O  O   . TRP A 1 251  ? 34.374 41.096  -15.181 1.00 12.54 ? 251  TRP A O   1 
ATOM   2000  C  CB  . TRP A 1 251  ? 34.490 43.999  -15.618 1.00 10.82 ? 251  TRP A CB  1 
ATOM   2001  C  CG  . TRP A 1 251  ? 35.723 44.147  -14.890 1.00 13.25 ? 251  TRP A CG  1 
ATOM   2002  C  CD1 . TRP A 1 251  ? 36.691 43.190  -14.703 1.00 16.12 ? 251  TRP A CD1 1 
ATOM   2003  C  CD2 . TRP A 1 251  ? 36.144 45.295  -14.197 1.00 11.98 ? 251  TRP A CD2 1 
ATOM   2004  N  NE1 . TRP A 1 251  ? 37.692 43.694  -13.924 1.00 15.09 ? 251  TRP A NE1 1 
ATOM   2005  C  CE2 . TRP A 1 251  ? 37.394 44.995  -13.609 1.00 12.46 ? 251  TRP A CE2 1 
ATOM   2006  C  CE3 . TRP A 1 251  ? 35.596 46.557  -13.997 1.00 11.41 ? 251  TRP A CE3 1 
ATOM   2007  C  CZ2 . TRP A 1 251  ? 38.085 45.903  -12.834 1.00 12.83 ? 251  TRP A CZ2 1 
ATOM   2008  C  CZ3 . TRP A 1 251  ? 36.278 47.459  -13.232 1.00 13.37 ? 251  TRP A CZ3 1 
ATOM   2009  C  CH2 . TRP A 1 251  ? 37.522 47.147  -12.680 1.00 13.93 ? 251  TRP A CH2 1 
ATOM   2010  N  N   . ASP A 1 252  ? 34.227 41.719  -13.041 1.00 11.06 ? 252  ASP A N   1 
ATOM   2011  C  CA  . ASP A 1 252  ? 34.991 40.577  -12.563 1.00 11.99 ? 252  ASP A CA  1 
ATOM   2012  C  C   . ASP A 1 252  ? 34.153 39.314  -12.452 1.00 12.77 ? 252  ASP A C   1 
ATOM   2013  O  O   . ASP A 1 252  ? 33.370 39.140  -11.525 1.00 12.05 ? 252  ASP A O   1 
ATOM   2014  C  CB  . ASP A 1 252  ? 35.611 40.952  -11.215 1.00 10.76 ? 252  ASP A CB  1 
ATOM   2015  C  CG  . ASP A 1 252  ? 36.351 39.821  -10.568 1.00 14.78 ? 252  ASP A CG  1 
ATOM   2016  O  OD1 . ASP A 1 252  ? 36.619 38.779  -11.215 1.00 16.51 ? 252  ASP A OD1 1 
ATOM   2017  O  OD2 . ASP A 1 252  ? 36.694 39.913  -9.377  1.00 13.03 ? 252  ASP A OD2 1 
ATOM   2018  N  N   A ASN A 1 253  ? 34.344 38.434  -13.428 0.50 13.62 ? 253  ASN A N   1 
ATOM   2019  N  N   B ASN A 1 253  ? 34.297 38.413  -13.426 0.50 13.75 ? 253  ASN A N   1 
ATOM   2020  C  CA  A ASN A 1 253  ? 33.568 37.225  -13.499 0.50 14.51 ? 253  ASN A CA  1 
ATOM   2021  C  CA  B ASN A 1 253  ? 33.504 37.189  -13.423 0.50 14.79 ? 253  ASN A CA  1 
ATOM   2022  C  C   A ASN A 1 253  ? 33.933 36.187  -12.446 0.50 14.82 ? 253  ASN A C   1 
ATOM   2023  C  C   B ASN A 1 253  ? 33.924 36.171  -12.391 0.50 15.03 ? 253  ASN A C   1 
ATOM   2024  O  O   A ASN A 1 253  ? 33.049 35.516  -11.906 0.50 15.46 ? 253  ASN A O   1 
ATOM   2025  O  O   B ASN A 1 253  ? 33.072 35.489  -11.815 0.50 15.85 ? 253  ASN A O   1 
ATOM   2026  C  CB  A ASN A 1 253  ? 33.708 36.613  -14.883 0.50 14.60 ? 253  ASN A CB  1 
ATOM   2027  C  CB  B ASN A 1 253  ? 33.518 36.535  -14.796 0.50 15.17 ? 253  ASN A CB  1 
ATOM   2028  C  CG  A ASN A 1 253  ? 32.774 35.471  -15.080 0.50 15.19 ? 253  ASN A CG  1 
ATOM   2029  C  CG  B ASN A 1 253  ? 32.569 37.195  -15.732 0.50 15.91 ? 253  ASN A CG  1 
ATOM   2030  O  OD1 A ASN A 1 253  ? 31.582 35.567  -14.784 0.50 13.79 ? 253  ASN A OD1 1 
ATOM   2031  O  OD1 B ASN A 1 253  ? 31.368 36.907  -15.724 0.50 18.73 ? 253  ASN A OD1 1 
ATOM   2032  N  ND2 A ASN A 1 253  ? 33.311 34.357  -15.558 0.50 15.61 ? 253  ASN A ND2 1 
ATOM   2033  N  ND2 B ASN A 1 253  ? 33.091 38.096  -16.552 0.50 17.97 ? 253  ASN A ND2 1 
ATOM   2034  N  N   . LYS A 1 254  ? 35.227 36.084  -12.169 1.00 16.26 ? 254  LYS A N   1 
ATOM   2035  C  CA  . LYS A 1 254  ? 35.783 35.049  -11.315 1.00 17.37 ? 254  LYS A CA  1 
ATOM   2036  C  C   . LYS A 1 254  ? 35.674 35.433  -9.854  1.00 17.63 ? 254  LYS A C   1 
ATOM   2037  O  O   . LYS A 1 254  ? 35.355 34.590  -9.017  1.00 19.13 ? 254  LYS A O   1 
ATOM   2038  C  CB  . LYS A 1 254  ? 37.234 34.789  -11.715 1.00 18.87 ? 254  LYS A CB  1 
ATOM   2039  C  CG  . LYS A 1 254  ? 37.922 33.668  -10.948 1.00 23.33 ? 254  LYS A CG  1 
ATOM   2040  C  CD  . LYS A 1 254  ? 39.132 33.157  -11.739 1.00 27.67 ? 254  LYS A CD  1 
ATOM   2041  C  CE  . LYS A 1 254  ? 40.222 32.574  -10.832 1.00 30.10 ? 254  LYS A CE  1 
ATOM   2042  N  NZ  . LYS A 1 254  ? 39.732 31.952  -9.554  1.00 31.03 ? 254  LYS A NZ  1 
ATOM   2043  N  N   . GLY A 1 255  ? 35.900 36.705  -9.554  1.00 16.78 ? 255  GLY A N   1 
ATOM   2044  C  CA  . GLY A 1 255  ? 35.816 37.145  -8.169  1.00 15.81 ? 255  GLY A CA  1 
ATOM   2045  C  C   . GLY A 1 255  ? 37.146 37.448  -7.511  1.00 15.29 ? 255  GLY A C   1 
ATOM   2046  O  O   . GLY A 1 255  ? 37.161 37.750  -6.330  1.00 14.52 ? 255  GLY A O   1 
ATOM   2047  N  N   . ASP A 1 256  ? 38.248 37.453  -8.258  1.00 15.07 ? 256  ASP A N   1 
ATOM   2048  C  CA  . ASP A 1 256  ? 39.557 37.670  -7.626  1.00 16.52 ? 256  ASP A CA  1 
ATOM   2049  C  C   . ASP A 1 256  ? 39.756 39.079  -7.065  1.00 14.59 ? 256  ASP A C   1 
ATOM   2050  O  O   . ASP A 1 256  ? 40.639 39.301  -6.232  1.00 14.76 ? 256  ASP A O   1 
ATOM   2051  C  CB  . ASP A 1 256  ? 40.719 37.356  -8.563  1.00 19.06 ? 256  ASP A CB  1 
ATOM   2052  C  CG  . ASP A 1 256  ? 40.742 35.914  -9.010  1.00 25.11 ? 256  ASP A CG  1 
ATOM   2053  O  OD1 . ASP A 1 256  ? 40.225 35.031  -8.272  1.00 30.83 ? 256  ASP A OD1 1 
ATOM   2054  O  OD2 . ASP A 1 256  ? 41.282 35.585  -10.093 1.00 31.54 ? 256  ASP A OD2 1 
ATOM   2055  N  N   . THR A 1 257  ? 38.911 40.011  -7.494  1.00 12.21 ? 257  THR A N   1 
ATOM   2056  C  CA  . THR A 1 257  ? 39.012 41.371  -6.952  1.00 11.46 ? 257  THR A CA  1 
ATOM   2057  C  C   . THR A 1 257  ? 38.266 41.559  -5.628  1.00 11.07 ? 257  THR A C   1 
ATOM   2058  O  O   . THR A 1 257  ? 38.336 42.639  -5.035  1.00 11.40 ? 257  THR A O   1 
ATOM   2059  C  CB  . THR A 1 257  ? 38.475 42.431  -7.940  1.00 11.84 ? 257  THR A CB  1 
ATOM   2060  O  OG1 . THR A 1 257  ? 37.069 42.205  -8.174  1.00 9.40  ? 257  THR A OG1 1 
ATOM   2061  C  CG2 . THR A 1 257  ? 39.190 42.316  -9.301  1.00 13.45 ? 257  THR A CG2 1 
ATOM   2062  N  N   . ALA A 1 258  ? 37.525 40.535  -5.201  1.00 10.11 ? 258  ALA A N   1 
ATOM   2063  C  CA  . ALA A 1 258  ? 36.590 40.699  -4.079  1.00 8.30  ? 258  ALA A CA  1 
ATOM   2064  C  C   . ALA A 1 258  ? 37.261 41.101  -2.764  1.00 8.18  ? 258  ALA A C   1 
ATOM   2065  O  O   . ALA A 1 258  ? 38.346 40.609  -2.409  1.00 9.86  ? 258  ALA A O   1 
ATOM   2066  C  CB  . ALA A 1 258  ? 35.791 39.459  -3.850  1.00 9.56  ? 258  ALA A CB  1 
ATOM   2067  N  N   . LEU A 1 259  ? 36.612 42.025  -2.075  1.00 6.31  ? 259  LEU A N   1 
ATOM   2068  C  CA  . LEU A 1 259  ? 37.074 42.465  -0.756  1.00 6.10  ? 259  LEU A CA  1 
ATOM   2069  C  C   . LEU A 1 259  ? 35.889 42.445  0.172   1.00 5.54  ? 259  LEU A C   1 
ATOM   2070  O  O   . LEU A 1 259  ? 34.842 43.026  -0.119  1.00 5.65  ? 259  LEU A O   1 
ATOM   2071  C  CB  . LEU A 1 259  ? 37.650 43.864  -0.830  1.00 6.92  ? 259  LEU A CB  1 
ATOM   2072  C  CG  . LEU A 1 259  ? 38.395 44.270  0.445   1.00 6.27  ? 259  LEU A CG  1 
ATOM   2073  C  CD1 . LEU A 1 259  ? 39.646 43.406  0.686   1.00 8.34  ? 259  LEU A CD1 1 
ATOM   2074  C  CD2 . LEU A 1 259  ? 38.843 45.716  0.350   1.00 8.22  ? 259  LEU A CD2 1 
ATOM   2075  N  N   . PHE A 1 260  ? 36.046 41.775  1.326   1.00 5.92  ? 260  PHE A N   1 
ATOM   2076  C  CA  . PHE A 1 260  ? 34.985 41.744  2.309   1.00 5.57  ? 260  PHE A CA  1 
ATOM   2077  C  C   . PHE A 1 260  ? 34.657 43.142  2.824   1.00 4.40  ? 260  PHE A C   1 
ATOM   2078  O  O   . PHE A 1 260  ? 35.585 43.877  3.243   1.00 5.22  ? 260  PHE A O   1 
ATOM   2079  C  CB  . PHE A 1 260  ? 35.354 40.810  3.479   1.00 5.96  ? 260  PHE A CB  1 
ATOM   2080  C  CG  . PHE A 1 260  ? 34.256 40.640  4.484   1.00 6.74  ? 260  PHE A CG  1 
ATOM   2081  C  CD1 . PHE A 1 260  ? 33.291 39.681  4.277   1.00 9.60  ? 260  PHE A CD1 1 
ATOM   2082  C  CD2 . PHE A 1 260  ? 34.184 41.425  5.620   1.00 8.02  ? 260  PHE A CD2 1 
ATOM   2083  C  CE1 . PHE A 1 260  ? 32.263 39.504  5.211   1.00 11.08 ? 260  PHE A CE1 1 
ATOM   2084  C  CE2 . PHE A 1 260  ? 33.145 41.272  6.548   1.00 9.95  ? 260  PHE A CE2 1 
ATOM   2085  C  CZ  . PHE A 1 260  ? 32.194 40.304  6.324   1.00 9.85  ? 260  PHE A CZ  1 
ATOM   2086  N  N   . THR A 1 261  ? 33.364 43.506  2.785   1.00 4.76  ? 261  THR A N   1 
ATOM   2087  C  CA  . THR A 1 261  ? 32.936 44.853  3.101   1.00 5.00  ? 261  THR A CA  1 
ATOM   2088  C  C   . THR A 1 261  ? 31.816 44.797  4.126   1.00 4.38  ? 261  THR A C   1 
ATOM   2089  O  O   . THR A 1 261  ? 30.860 44.037  3.979   1.00 6.16  ? 261  THR A O   1 
ATOM   2090  C  CB  . THR A 1 261  ? 32.426 45.545  1.816   1.00 5.41  ? 261  THR A CB  1 
ATOM   2091  O  OG1 . THR A 1 261  ? 33.511 45.613  0.878   1.00 6.29  ? 261  THR A OG1 1 
ATOM   2092  C  CG2 . THR A 1 261  ? 31.998 46.980  2.109   1.00 6.13  ? 261  THR A CG2 1 
ATOM   2093  N  N   . HIS A 1 262  ? 31.918 45.637  5.149   1.00 4.92  ? 262  HIS A N   1 
ATOM   2094  C  CA  . HIS A 1 262  ? 30.850 45.817  6.115   1.00 4.85  ? 262  HIS A CA  1 
ATOM   2095  C  C   . HIS A 1 262  ? 30.235 47.200  5.917   1.00 5.32  ? 262  HIS A C   1 
ATOM   2096  O  O   . HIS A 1 262  ? 30.946 48.196  6.036   1.00 5.78  ? 262  HIS A O   1 
ATOM   2097  C  CB  . HIS A 1 262  ? 31.472 45.765  7.525   1.00 5.87  ? 262  HIS A CB  1 
ATOM   2098  C  CG  . HIS A 1 262  ? 30.510 46.104  8.622   1.00 5.75  ? 262  HIS A CG  1 
ATOM   2099  N  ND1 . HIS A 1 262  ? 29.946 45.139  9.431   1.00 6.63  ? 262  HIS A ND1 1 
ATOM   2100  C  CD2 . HIS A 1 262  ? 30.044 47.296  9.072   1.00 7.27  ? 262  HIS A CD2 1 
ATOM   2101  C  CE1 . HIS A 1 262  ? 29.174 45.724  10.339  1.00 9.22  ? 262  HIS A CE1 1 
ATOM   2102  N  NE2 . HIS A 1 262  ? 29.183 47.028  10.121  1.00 7.85  ? 262  HIS A NE2 1 
ATOM   2103  N  N   . MET A 1 263  ? 28.939 47.257  5.634   1.00 4.98  ? 263  MET A N   1 
ATOM   2104  C  CA  . MET A 1 263  ? 28.212 48.505  5.579   1.00 5.50  ? 263  MET A CA  1 
ATOM   2105  C  C   . MET A 1 263  ? 27.481 48.708  6.890   1.00 6.35  ? 263  MET A C   1 
ATOM   2106  O  O   . MET A 1 263  ? 26.717 47.811  7.335   1.00 6.55  ? 263  MET A O   1 
ATOM   2107  C  CB  . MET A 1 263  ? 27.209 48.465  4.425   1.00 6.56  ? 263  MET A CB  1 
ATOM   2108  C  CG  . MET A 1 263  ? 26.425 49.761  4.294   1.00 6.45  ? 263  MET A CG  1 
ATOM   2109  S  SD  . MET A 1 263  ? 25.072 49.605  3.064   1.00 7.68  ? 263  MET A SD  1 
ATOM   2110  C  CE  . MET A 1 263  ? 25.949 49.246  1.499   1.00 8.39  ? 263  MET A CE  1 
ATOM   2111  N  N   A MET A 1 264  ? 27.722 49.847  7.541   0.50 5.50  ? 264  MET A N   1 
ATOM   2112  N  N   B MET A 1 264  ? 27.712 49.843  7.549   0.50 6.02  ? 264  MET A N   1 
ATOM   2113  C  CA  A MET A 1 264  ? 26.994 50.199  8.750   0.50 6.09  ? 264  MET A CA  1 
ATOM   2114  C  CA  B MET A 1 264  ? 26.987 50.132  8.777   0.50 7.21  ? 264  MET A CA  1 
ATOM   2115  C  C   A MET A 1 264  ? 25.524 50.415  8.397   0.50 6.43  ? 264  MET A C   1 
ATOM   2116  C  C   B MET A 1 264  ? 25.540 50.481  8.443   0.50 7.11  ? 264  MET A C   1 
ATOM   2117  O  O   A MET A 1 264  ? 25.195 50.816  7.264   0.50 6.33  ? 264  MET A O   1 
ATOM   2118  O  O   B MET A 1 264  ? 25.252 51.062  7.386   0.50 7.52  ? 264  MET A O   1 
ATOM   2119  C  CB  A MET A 1 264  ? 27.614 51.438  9.388   0.50 5.94  ? 264  MET A CB  1 
ATOM   2120  C  CB  B MET A 1 264  ? 27.678 51.227  9.577   0.50 7.17  ? 264  MET A CB  1 
ATOM   2121  C  CG  A MET A 1 264  ? 29.055 51.179  9.837   0.50 5.78  ? 264  MET A CG  1 
ATOM   2122  C  CG  B MET A 1 264  ? 29.111 50.851  9.936   0.50 7.87  ? 264  MET A CG  1 
ATOM   2123  S  SD  A MET A 1 264  ? 30.032 52.601  10.392  0.50 8.17  ? 264  MET A SD  1 
ATOM   2124  S  SD  B MET A 1 264  ? 29.697 51.649  11.414  0.50 10.78 ? 264  MET A SD  1 
ATOM   2125  C  CE  A MET A 1 264  ? 28.934 53.387  11.543  0.50 8.66  ? 264  MET A CE  1 
ATOM   2126  C  CE  B MET A 1 264  ? 29.665 53.304  10.912  0.50 10.03 ? 264  MET A CE  1 
ATOM   2127  N  N   . PRO A 1 265  ? 24.603 50.109  9.320   1.00 6.84  ? 265  PRO A N   1 
ATOM   2128  C  CA  . PRO A 1 265  ? 23.186 50.115  8.938   1.00 7.06  ? 265  PRO A CA  1 
ATOM   2129  C  C   . PRO A 1 265  ? 22.377 51.394  9.118   1.00 7.47  ? 265  PRO A C   1 
ATOM   2130  O  O   . PRO A 1 265  ? 21.259 51.463  8.575   1.00 6.33  ? 265  PRO A O   1 
ATOM   2131  C  CB  . PRO A 1 265  ? 22.600 49.035  9.852   1.00 7.89  ? 265  PRO A CB  1 
ATOM   2132  C  CG  . PRO A 1 265  ? 23.416 49.068  11.041  1.00 8.65  ? 265  PRO A CG  1 
ATOM   2133  C  CD  . PRO A 1 265  ? 24.815 49.583  10.700  1.00 7.05  ? 265  PRO A CD  1 
ATOM   2134  N  N   . PHE A 1 266  ? 22.878 52.329  9.925   1.00 6.74  ? 266  PHE A N   1 
ATOM   2135  C  CA  . PHE A 1 266  ? 22.088 53.459  10.417  1.00 7.45  ? 266  PHE A CA  1 
ATOM   2136  C  C   . PHE A 1 266  ? 22.488 54.825  9.831   1.00 6.89  ? 266  PHE A C   1 
ATOM   2137  O  O   . PHE A 1 266  ? 23.360 54.921  8.980   1.00 7.68  ? 266  PHE A O   1 
ATOM   2138  C  CB  . PHE A 1 266  ? 22.049 53.439  11.953  1.00 7.12  ? 266  PHE A CB  1 
ATOM   2139  C  CG  . PHE A 1 266  ? 21.506 52.119  12.546  1.00 7.23  ? 266  PHE A CG  1 
ATOM   2140  C  CD1 . PHE A 1 266  ? 20.361 51.508  12.038  1.00 9.21  ? 266  PHE A CD1 1 
ATOM   2141  C  CD2 . PHE A 1 266  ? 22.160 51.510  13.586  1.00 7.34  ? 266  PHE A CD2 1 
ATOM   2142  C  CE1 . PHE A 1 266  ? 19.866 50.324  12.613  1.00 7.42  ? 266  PHE A CE1 1 
ATOM   2143  C  CE2 . PHE A 1 266  ? 21.668 50.312  14.151  1.00 8.08  ? 266  PHE A CE2 1 
ATOM   2144  C  CZ  . PHE A 1 266  ? 20.550 49.721  13.638  1.00 6.71  ? 266  PHE A CZ  1 
ATOM   2145  N  N   . TYR A 1 267  ? 21.848 55.881  10.280  1.00 7.32  ? 267  TYR A N   1 
ATOM   2146  C  CA  . TYR A 1 267  ? 21.882 57.154  9.598   1.00 6.85  ? 267  TYR A CA  1 
ATOM   2147  C  C   . TYR A 1 267  ? 23.223 57.850  9.801   1.00 7.54  ? 267  TYR A C   1 
ATOM   2148  O  O   . TYR A 1 267  ? 23.616 58.660  8.964   1.00 7.37  ? 267  TYR A O   1 
ATOM   2149  C  CB  . TYR A 1 267  ? 20.759 58.017  10.186  1.00 8.75  ? 267  TYR A CB  1 
ATOM   2150  C  CG  . TYR A 1 267  ? 20.866 59.509  10.000  1.00 8.34  ? 267  TYR A CG  1 
ATOM   2151  C  CD1 . TYR A 1 267  ? 20.485 60.121  8.815   1.00 10.98 ? 267  TYR A CD1 1 
ATOM   2152  C  CD2 . TYR A 1 267  ? 21.238 60.306  11.074  1.00 10.19 ? 267  TYR A CD2 1 
ATOM   2153  C  CE1 . TYR A 1 267  ? 20.557 61.519  8.694   1.00 10.30 ? 267  TYR A CE1 1 
ATOM   2154  C  CE2 . TYR A 1 267  ? 21.312 61.637  10.964  1.00 11.28 ? 267  TYR A CE2 1 
ATOM   2155  C  CZ  . TYR A 1 267  ? 20.975 62.243  9.788   1.00 11.95 ? 267  TYR A CZ  1 
ATOM   2156  O  OH  . TYR A 1 267  ? 21.042 63.632  9.743   1.00 15.75 ? 267  TYR A OH  1 
ATOM   2157  N  N   . SER A 1 268  ? 23.913 57.575  10.893  1.00 7.34  ? 268  SER A N   1 
ATOM   2158  C  CA  . SER A 1 268  ? 25.176 58.258  11.179  1.00 7.75  ? 268  SER A CA  1 
ATOM   2159  C  C   . SER A 1 268  ? 26.177 57.324  11.827  1.00 7.61  ? 268  SER A C   1 
ATOM   2160  O  O   . SER A 1 268  ? 25.822 56.201  12.238  1.00 7.64  ? 268  SER A O   1 
ATOM   2161  C  CB  . SER A 1 268  ? 24.901 59.499  12.068  1.00 8.20  ? 268  SER A CB  1 
ATOM   2162  O  OG  . SER A 1 268  ? 26.112 60.123  12.458  1.00 11.62 ? 268  SER A OG  1 
ATOM   2163  N  N   . TYR A 1 269  ? 27.432 57.782  11.949  1.00 6.97  ? 269  TYR A N   1 
ATOM   2164  C  CA  . TYR A 1 269  ? 28.435 57.058  12.712  1.00 6.99  ? 269  TYR A CA  1 
ATOM   2165  C  C   . TYR A 1 269  ? 28.544 57.550  14.152  1.00 7.59  ? 269  TYR A C   1 
ATOM   2166  O  O   . TYR A 1 269  ? 29.412 57.088  14.884  1.00 8.49  ? 269  TYR A O   1 
ATOM   2167  C  CB  . TYR A 1 269  ? 29.829 57.190  12.050  1.00 6.94  ? 269  TYR A CB  1 
ATOM   2168  C  CG  . TYR A 1 269  ? 30.249 58.622  11.791  1.00 7.57  ? 269  TYR A CG  1 
ATOM   2169  C  CD1 . TYR A 1 269  ? 30.680 59.436  12.836  1.00 8.12  ? 269  TYR A CD1 1 
ATOM   2170  C  CD2 . TYR A 1 269  ? 30.178 59.178  10.510  1.00 8.33  ? 269  TYR A CD2 1 
ATOM   2171  C  CE1 . TYR A 1 269  ? 31.061 60.748  12.634  1.00 8.62  ? 269  TYR A CE1 1 
ATOM   2172  C  CE2 . TYR A 1 269  ? 30.568 60.505  10.281  1.00 8.34  ? 269  TYR A CE2 1 
ATOM   2173  C  CZ  . TYR A 1 269  ? 30.976 61.282  11.366  1.00 9.12  ? 269  TYR A CZ  1 
ATOM   2174  O  OH  . TYR A 1 269  ? 31.333 62.594  11.113  1.00 10.76 ? 269  TYR A OH  1 
ATOM   2175  N  N   . ASP A 1 270  ? 27.677 58.463  14.561  1.00 6.94  ? 270  ASP A N   1 
ATOM   2176  C  CA  . ASP A 1 270  ? 27.749 58.973  15.929  1.00 7.23  ? 270  ASP A CA  1 
ATOM   2177  C  C   . ASP A 1 270  ? 27.143 57.970  16.890  1.00 6.87  ? 270  ASP A C   1 
ATOM   2178  O  O   . ASP A 1 270  ? 26.568 56.977  16.450  1.00 7.55  ? 270  ASP A O   1 
ATOM   2179  C  CB  . ASP A 1 270  ? 27.127 60.364  16.025  1.00 8.08  ? 270  ASP A CB  1 
ATOM   2180  C  CG  . ASP A 1 270  ? 25.641 60.394  15.782  1.00 12.02 ? 270  ASP A CG  1 
ATOM   2181  O  OD1 . ASP A 1 270  ? 24.978 59.339  15.601  1.00 11.77 ? 270  ASP A OD1 1 
ATOM   2182  O  OD2 . ASP A 1 270  ? 25.051 61.490  15.783  1.00 14.89 ? 270  ASP A OD2 1 
ATOM   2183  N  N   . ILE A 1 271  ? 27.352 58.170  18.186  1.00 7.78  ? 271  ILE A N   1 
ATOM   2184  C  CA  . ILE A 1 271  ? 26.936 57.148  19.148  1.00 7.06  ? 271  ILE A CA  1 
ATOM   2185  C  C   . ILE A 1 271  ? 25.421 56.882  19.108  1.00 7.81  ? 271  ILE A C   1 
ATOM   2186  O  O   . ILE A 1 271  ? 25.023 55.730  19.174  1.00 7.69  ? 271  ILE A O   1 
ATOM   2187  C  CB  . ILE A 1 271  ? 27.494 57.457  20.522  1.00 7.76  ? 271  ILE A CB  1 
ATOM   2188  C  CG1 . ILE A 1 271  ? 29.025 57.328  20.479  1.00 6.68  ? 271  ILE A CG1 1 
ATOM   2189  C  CG2 . ILE A 1 271  ? 26.911 56.500  21.602  1.00 6.93  ? 271  ILE A CG2 1 
ATOM   2190  C  CD1 . ILE A 1 271  ? 29.689 57.962  21.678  1.00 8.26  ? 271  ILE A CD1 1 
ATOM   2191  N  N   . PRO A 1 272  ? 24.583 57.908  19.005  1.00 7.45  ? 272  PRO A N   1 
ATOM   2192  C  CA  . PRO A 1 272  ? 23.128 57.642  18.890  1.00 7.37  ? 272  PRO A CA  1 
ATOM   2193  C  C   . PRO A 1 272  ? 22.757 56.706  17.760  1.00 7.03  ? 272  PRO A C   1 
ATOM   2194  O  O   . PRO A 1 272  ? 21.679 56.085  17.809  1.00 8.70  ? 272  PRO A O   1 
ATOM   2195  C  CB  . PRO A 1 272  ? 22.518 59.026  18.683  1.00 7.77  ? 272  PRO A CB  1 
ATOM   2196  C  CG  . PRO A 1 272  ? 23.483 59.969  19.383  1.00 9.64  ? 272  PRO A CG  1 
ATOM   2197  C  CD  . PRO A 1 272  ? 24.852 59.350  19.165  1.00 8.51  ? 272  PRO A CD  1 
ATOM   2198  N  N   . HIS A 1 273  ? 23.585 56.657  16.704  1.00 6.72  ? 273  HIS A N   1 
ATOM   2199  C  CA  . HIS A 1 273  ? 23.226 55.794  15.570  1.00 7.68  ? 273  HIS A CA  1 
ATOM   2200  C  C   . HIS A 1 273  ? 24.144 54.611  15.389  1.00 7.93  ? 273  HIS A C   1 
ATOM   2201  O  O   . HIS A 1 273  ? 24.168 54.006  14.320  1.00 8.65  ? 273  HIS A O   1 
ATOM   2202  C  CB  . HIS A 1 273  ? 23.108 56.617  14.281  1.00 8.02  ? 273  HIS A CB  1 
ATOM   2203  C  CG  . HIS A 1 273  ? 22.038 57.661  14.357  1.00 7.62  ? 273  HIS A CG  1 
ATOM   2204  N  ND1 . HIS A 1 273  ? 22.271 58.951  14.800  1.00 8.65  ? 273  HIS A ND1 1 
ATOM   2205  C  CD2 . HIS A 1 273  ? 20.712 57.601  14.056  1.00 7.45  ? 273  HIS A CD2 1 
ATOM   2206  C  CE1 . HIS A 1 273  ? 21.121 59.619  14.798  1.00 8.67  ? 273  HIS A CE1 1 
ATOM   2207  N  NE2 . HIS A 1 273  ? 20.170 58.824  14.352  1.00 9.44  ? 273  HIS A NE2 1 
ATOM   2208  N  N   . THR A 1 274  ? 24.840 54.222  16.442  1.00 8.10  ? 274  THR A N   1 
ATOM   2209  C  CA  . THR A 1 274  ? 25.715 53.056  16.330  1.00 8.31  ? 274  THR A CA  1 
ATOM   2210  C  C   . THR A 1 274  ? 25.487 51.978  17.386  1.00 9.54  ? 274  THR A C   1 
ATOM   2211  O  O   . THR A 1 274  ? 26.020 50.885  17.256  1.00 10.67 ? 274  THR A O   1 
ATOM   2212  C  CB  . THR A 1 274  ? 27.210 53.432  16.287  1.00 9.14  ? 274  THR A CB  1 
ATOM   2213  O  OG1 . THR A 1 274  ? 27.478 54.378  17.332  1.00 8.78  ? 274  THR A OG1 1 
ATOM   2214  C  CG2 . THR A 1 274  ? 27.514 54.134  14.948  1.00 9.23  ? 274  THR A CG2 1 
ATOM   2215  N  N   . CYS A 1 275  ? 24.714 52.252  18.433  1.00 10.14 ? 275  CYS A N   1 
ATOM   2216  C  CA  . CYS A 1 275  ? 24.491 51.194  19.416  1.00 11.00 ? 275  CYS A CA  1 
ATOM   2217  C  C   . CYS A 1 275  ? 23.358 50.242  19.006  1.00 10.08 ? 275  CYS A C   1 
ATOM   2218  O  O   . CYS A 1 275  ? 23.263 49.114  19.468  1.00 10.55 ? 275  CYS A O   1 
ATOM   2219  C  CB  . CYS A 1 275  ? 24.209 51.818  20.786  1.00 11.21 ? 275  CYS A CB  1 
ATOM   2220  S  SG  . CYS A 1 275  ? 22.476 51.834  21.330  1.00 13.84 ? 275  CYS A SG  1 
ATOM   2221  N  N   . GLY A 1 276  ? 22.455 50.717  18.166  1.00 9.21  ? 276  GLY A N   1 
ATOM   2222  C  CA  . GLY A 1 276  ? 21.224 49.999  17.854  1.00 9.35  ? 276  GLY A CA  1 
ATOM   2223  C  C   . GLY A 1 276  ? 20.281 50.916  17.127  1.00 9.30  ? 276  GLY A C   1 
ATOM   2224  O  O   . GLY A 1 276  ? 20.655 52.039  16.779  1.00 9.27  ? 276  GLY A O   1 
ATOM   2225  N  N   . PRO A 1 277  ? 19.067 50.452  16.817  1.00 8.51  ? 277  PRO A N   1 
ATOM   2226  C  CA  . PRO A 1 277  ? 18.141 51.216  15.985  1.00 8.59  ? 277  PRO A CA  1 
ATOM   2227  C  C   . PRO A 1 277  ? 17.459 52.397  16.599  1.00 8.56  ? 277  PRO A C   1 
ATOM   2228  O  O   . PRO A 1 277  ? 16.875 53.120  15.807  1.00 9.19  ? 277  PRO A O   1 
ATOM   2229  C  CB  . PRO A 1 277  ? 17.027 50.199  15.667  1.00 8.82  ? 277  PRO A CB  1 
ATOM   2230  C  CG  . PRO A 1 277  ? 17.115 49.185  16.810  1.00 8.08  ? 277  PRO A CG  1 
ATOM   2231  C  CD  . PRO A 1 277  ? 18.556 49.098  17.120  1.00 9.14  ? 277  PRO A CD  1 
ATOM   2232  N  N   . ASP A 1 278  ? 17.470 52.545  17.917  1.00 8.95  ? 278  ASP A N   1 
ATOM   2233  C  CA  . ASP A 1 278  ? 16.720 53.647  18.508  1.00 9.68  ? 278  ASP A CA  1 
ATOM   2234  C  C   . ASP A 1 278  ? 17.667 54.694  19.083  1.00 9.23  ? 278  ASP A C   1 
ATOM   2235  O  O   . ASP A 1 278  ? 18.275 54.469  20.132  1.00 9.20  ? 278  ASP A O   1 
ATOM   2236  C  CB  . ASP A 1 278  ? 15.828 53.116  19.655  1.00 9.80  ? 278  ASP A CB  1 
ATOM   2237  C  CG  . ASP A 1 278  ? 14.968 54.199  20.258  1.00 12.24 ? 278  ASP A CG  1 
ATOM   2238  O  OD1 . ASP A 1 278  ? 15.089 55.391  19.871  1.00 13.13 ? 278  ASP A OD1 1 
ATOM   2239  O  OD2 . ASP A 1 278  ? 14.098 53.889  21.108  1.00 15.09 ? 278  ASP A OD2 1 
ATOM   2240  N  N   . PRO A 1 279  ? 17.810 55.828  18.401  1.00 9.52  ? 279  PRO A N   1 
ATOM   2241  C  CA  . PRO A 1 279  ? 18.771 56.834  18.877  1.00 9.03  ? 279  PRO A CA  1 
ATOM   2242  C  C   . PRO A 1 279  ? 18.412 57.427  20.227  1.00 9.05  ? 279  PRO A C   1 
ATOM   2243  O  O   . PRO A 1 279  ? 19.276 57.890  20.927  1.00 9.37  ? 279  PRO A O   1 
ATOM   2244  C  CB  . PRO A 1 279  ? 18.780 57.883  17.751  1.00 9.60  ? 279  PRO A CB  1 
ATOM   2245  C  CG  . PRO A 1 279  ? 17.488 57.712  17.083  1.00 10.42 ? 279  PRO A CG  1 
ATOM   2246  C  CD  . PRO A 1 279  ? 17.064 56.273  17.214  1.00 9.68  ? 279  PRO A CD  1 
ATOM   2247  N  N   . LYS A 1 280  ? 17.136 57.405  20.600  1.00 9.17  ? 280  LYS A N   1 
ATOM   2248  C  CA  . LYS A 1 280  ? 16.749 57.933  21.908  1.00 11.08 ? 280  LYS A CA  1 
ATOM   2249  C  C   . LYS A 1 280  ? 17.345 57.096  23.028  1.00 10.58 ? 280  LYS A C   1 
ATOM   2250  O  O   . LYS A 1 280  ? 17.696 57.614  24.089  1.00 11.47 ? 280  LYS A O   1 
ATOM   2251  C  CB  . LYS A 1 280  ? 15.230 57.981  22.031  1.00 12.09 ? 280  LYS A CB  1 
ATOM   2252  C  CG  . LYS A 1 280  ? 14.756 58.503  23.370  1.00 14.42 ? 280  LYS A CG  1 
ATOM   2253  C  CD  . LYS A 1 280  ? 13.227 58.511  23.409  1.00 18.24 ? 280  LYS A CD  1 
ATOM   2254  C  CE  . LYS A 1 280  ? 12.699 58.588  24.852  1.00 25.94 ? 280  LYS A CE  1 
ATOM   2255  N  NZ  . LYS A 1 280  ? 13.239 57.502  25.776  1.00 30.84 ? 280  LYS A NZ  1 
ATOM   2256  N  N   . VAL A 1 281  ? 17.508 55.796  22.780  1.00 10.33 ? 281  VAL A N   1 
ATOM   2257  C  CA  . VAL A 1 281  ? 18.203 54.933  23.725  1.00 10.51 ? 281  VAL A CA  1 
ATOM   2258  C  C   . VAL A 1 281  ? 19.714 55.023  23.606  1.00 10.13 ? 281  VAL A C   1 
ATOM   2259  O  O   . VAL A 1 281  ? 20.411 55.167  24.596  1.00 9.21  ? 281  VAL A O   1 
ATOM   2260  C  CB  . VAL A 1 281  ? 17.747 53.453  23.571  1.00 10.15 ? 281  VAL A CB  1 
ATOM   2261  C  CG1 . VAL A 1 281  ? 18.536 52.514  24.475  1.00 11.18 ? 281  VAL A CG1 1 
ATOM   2262  C  CG2 . VAL A 1 281  ? 16.238 53.331  23.832  1.00 10.43 ? 281  VAL A CG2 1 
ATOM   2263  N  N   . CYS A 1 282  ? 20.230 54.922  22.370  1.00 9.39  ? 282  CYS A N   1 
ATOM   2264  C  CA  . CYS A 1 282  ? 21.682 54.934  22.202  1.00 9.57  ? 282  CYS A CA  1 
ATOM   2265  C  C   . CYS A 1 282  ? 22.311 56.232  22.696  1.00 8.66  ? 282  CYS A C   1 
ATOM   2266  O  O   . CYS A 1 282  ? 23.417 56.213  23.212  1.00 8.97  ? 282  CYS A O   1 
ATOM   2267  C  CB  . CYS A 1 282  ? 22.036 54.758  20.733  1.00 10.68 ? 282  CYS A CB  1 
ATOM   2268  S  SG  . CYS A 1 282  ? 21.598 53.141  20.070  1.00 12.31 ? 282  CYS A SG  1 
ATOM   2269  N  N   . CYS A 1 283  ? 21.593 57.344  22.542  1.00 9.14  ? 283  CYS A N   1 
ATOM   2270  C  CA  . CYS A 1 283  ? 22.137 58.596  23.018  1.00 9.05  ? 283  CYS A CA  1 
ATOM   2271  C  C   . CYS A 1 283  ? 22.431 58.614  24.524  1.00 8.88  ? 283  CYS A C   1 
ATOM   2272  O  O   . CYS A 1 283  ? 23.321 59.341  24.978  1.00 9.06  ? 283  CYS A O   1 
ATOM   2273  C  CB  . CYS A 1 283  ? 21.220 59.740  22.609  1.00 9.96  ? 283  CYS A CB  1 
ATOM   2274  S  SG  . CYS A 1 283  ? 21.993 61.365  22.765  1.00 13.72 ? 283  CYS A SG  1 
ATOM   2275  N  N   . GLN A 1 284  ? 21.687 57.784  25.284  1.00 9.35  ? 284  GLN A N   1 
ATOM   2276  C  CA  . GLN A 1 284  ? 21.936 57.617  26.717  1.00 9.39  ? 284  GLN A CA  1 
ATOM   2277  C  C   . GLN A 1 284  ? 23.212 56.881  27.062  1.00 9.26  ? 284  GLN A C   1 
ATOM   2278  O  O   . GLN A 1 284  ? 23.565 56.784  28.229  1.00 10.26 ? 284  GLN A O   1 
ATOM   2279  C  CB  . GLN A 1 284  ? 20.751 56.900  27.378  1.00 10.24 ? 284  GLN A CB  1 
ATOM   2280  C  CG  . GLN A 1 284  ? 19.435 57.653  27.187  1.00 11.26 ? 284  GLN A CG  1 
ATOM   2281  C  CD  . GLN A 1 284  ? 18.258 56.886  27.735  1.00 11.71 ? 284  GLN A CD  1 
ATOM   2282  O  OE1 . GLN A 1 284  ? 18.287 56.459  28.896  1.00 14.33 ? 284  GLN A OE1 1 
ATOM   2283  N  NE2 . GLN A 1 284  ? 17.264 56.674  26.906  1.00 13.35 ? 284  GLN A NE2 1 
ATOM   2284  N  N   . PHE A 1 285  ? 23.897 56.366  26.032  1.00 8.46  ? 285  PHE A N   1 
ATOM   2285  C  CA  . PHE A 1 285  ? 25.141 55.666  26.253  1.00 8.04  ? 285  PHE A CA  1 
ATOM   2286  C  C   . PHE A 1 285  ? 26.296 56.408  25.602  1.00 7.54  ? 285  PHE A C   1 
ATOM   2287  O  O   . PHE A 1 285  ? 27.360 55.831  25.399  1.00 8.28  ? 285  PHE A O   1 
ATOM   2288  C  CB  . PHE A 1 285  ? 25.007 54.206  25.814  1.00 9.16  ? 285  PHE A CB  1 
ATOM   2289  C  CG  . PHE A 1 285  ? 23.983 53.474  26.651  1.00 9.26  ? 285  PHE A CG  1 
ATOM   2290  C  CD1 . PHE A 1 285  ? 24.369 52.889  27.840  1.00 9.59  ? 285  PHE A CD1 1 
ATOM   2291  C  CD2 . PHE A 1 285  ? 22.629 53.441  26.275  1.00 10.58 ? 285  PHE A CD2 1 
ATOM   2292  C  CE1 . PHE A 1 285  ? 23.414 52.231  28.660  1.00 8.83  ? 285  PHE A CE1 1 
ATOM   2293  C  CE2 . PHE A 1 285  ? 21.666 52.809  27.092  1.00 11.46 ? 285  PHE A CE2 1 
ATOM   2294  C  CZ  . PHE A 1 285  ? 22.082 52.202  28.275  1.00 10.62 ? 285  PHE A CZ  1 
ATOM   2295  N  N   . ASP A 1 286  ? 26.052 57.700  25.335  1.00 7.34  ? 286  ASP A N   1 
ATOM   2296  C  CA  . ASP A 1 286  ? 27.124 58.624  24.983  1.00 6.83  ? 286  ASP A CA  1 
ATOM   2297  C  C   . ASP A 1 286  ? 27.378 59.484  26.222  1.00 7.00  ? 286  ASP A C   1 
ATOM   2298  O  O   . ASP A 1 286  ? 26.665 60.468  26.467  1.00 8.46  ? 286  ASP A O   1 
ATOM   2299  C  CB  . ASP A 1 286  ? 26.735 59.469  23.799  1.00 6.77  ? 286  ASP A CB  1 
ATOM   2300  C  CG  . ASP A 1 286  ? 27.861 60.363  23.330  1.00 6.35  ? 286  ASP A CG  1 
ATOM   2301  O  OD1 . ASP A 1 286  ? 28.895 60.445  24.025  1.00 7.50  ? 286  ASP A OD1 1 
ATOM   2302  O  OD2 . ASP A 1 286  ? 27.687 61.048  22.282  1.00 7.93  ? 286  ASP A OD2 1 
ATOM   2303  N  N   . PHE A 1 287  ? 28.365 59.072  27.011  1.00 7.37  ? 287  PHE A N   1 
ATOM   2304  C  CA  . PHE A 1 287  ? 28.516 59.677  28.341  1.00 8.03  ? 287  PHE A CA  1 
ATOM   2305  C  C   . PHE A 1 287  ? 29.104 61.059  28.317  1.00 9.06  ? 287  PHE A C   1 
ATOM   2306  O  O   . PHE A 1 287  ? 29.235 61.703  29.364  1.00 10.27 ? 287  PHE A O   1 
ATOM   2307  C  CB  . PHE A 1 287  ? 29.234 58.715  29.307  1.00 8.41  ? 287  PHE A CB  1 
ATOM   2308  C  CG  . PHE A 1 287  ? 28.446 57.448  29.538  1.00 9.13  ? 287  PHE A CG  1 
ATOM   2309  C  CD1 . PHE A 1 287  ? 27.417 57.441  30.503  1.00 9.94  ? 287  PHE A CD1 1 
ATOM   2310  C  CD2 . PHE A 1 287  ? 28.629 56.318  28.757  1.00 10.37 ? 287  PHE A CD2 1 
ATOM   2311  C  CE1 . PHE A 1 287  ? 26.655 56.307  30.735  1.00 10.00 ? 287  PHE A CE1 1 
ATOM   2312  C  CE2 . PHE A 1 287  ? 27.862 55.170  28.972  1.00 11.53 ? 287  PHE A CE2 1 
ATOM   2313  C  CZ  . PHE A 1 287  ? 26.852 55.167  29.961  1.00 9.51  ? 287  PHE A CZ  1 
ATOM   2314  N  N   . LYS A 1 288  ? 29.435 61.549  27.119  1.00 8.26  ? 288  LYS A N   1 
ATOM   2315  C  CA  . LYS A 1 288  ? 29.825 62.947  26.990  1.00 8.49  ? 288  LYS A CA  1 
ATOM   2316  C  C   . LYS A 1 288  ? 28.614 63.887  26.956  1.00 9.61  ? 288  LYS A C   1 
ATOM   2317  O  O   . LYS A 1 288  ? 28.790 65.106  26.956  1.00 10.77 ? 288  LYS A O   1 
ATOM   2318  C  CB  . LYS A 1 288  ? 30.688 63.149  25.718  1.00 9.05  ? 288  LYS A CB  1 
ATOM   2319  C  CG  . LYS A 1 288  ? 31.545 64.415  25.802  1.00 8.30  ? 288  LYS A CG  1 
ATOM   2320  C  CD  . LYS A 1 288  ? 32.430 64.579  24.543  1.00 10.07 ? 288  LYS A CD  1 
ATOM   2321  C  CE  . LYS A 1 288  ? 33.199 65.873  24.674  1.00 9.72  ? 288  LYS A CE  1 
ATOM   2322  N  NZ  . LYS A 1 288  ? 34.382 65.951  23.716  1.00 12.14 ? 288  LYS A NZ  1 
ATOM   2323  N  N   . ARG A 1 289  ? 27.383 63.361  26.939  1.00 9.98  ? 289  ARG A N   1 
ATOM   2324  C  CA  . ARG A 1 289  ? 26.210 64.212  26.783  1.00 11.27 ? 289  ARG A CA  1 
ATOM   2325  C  C   . ARG A 1 289  ? 25.431 64.519  28.091  1.00 12.58 ? 289  ARG A C   1 
ATOM   2326  O  O   . ARG A 1 289  ? 24.238 64.766  28.039  1.00 13.01 ? 289  ARG A O   1 
ATOM   2327  C  CB  . ARG A 1 289  ? 25.261 63.583  25.767  1.00 10.80 ? 289  ARG A CB  1 
ATOM   2328  C  CG  . ARG A 1 289  ? 25.861 63.457  24.379  1.00 10.40 ? 289  ARG A CG  1 
ATOM   2329  C  CD  . ARG A 1 289  ? 24.862 62.998  23.379  1.00 11.80 ? 289  ARG A CD  1 
ATOM   2330  N  NE  . ARG A 1 289  ? 25.412 62.706  22.047  1.00 9.45  ? 289  ARG A NE  1 
ATOM   2331  C  CZ  . ARG A 1 289  ? 25.018 63.270  20.928  1.00 11.28 ? 289  ARG A CZ  1 
ATOM   2332  N  NH1 . ARG A 1 289  ? 24.051 64.201  20.897  1.00 12.11 ? 289  ARG A NH1 1 
ATOM   2333  N  NH2 . ARG A 1 289  ? 25.562 62.835  19.805  1.00 10.01 ? 289  ARG A NH2 1 
ATOM   2334  N  N   . MET A 1 290  ? 26.092 64.482  29.245  1.00 15.63 ? 290  MET A N   1 
ATOM   2335  C  CA  . MET A 1 290  ? 25.350 64.752  30.498  1.00 17.93 ? 290  MET A CA  1 
ATOM   2336  C  C   . MET A 1 290  ? 25.241 66.246  30.879  1.00 19.30 ? 290  MET A C   1 
ATOM   2337  O  O   . MET A 1 290  ? 24.410 66.617  31.740  1.00 21.25 ? 290  MET A O   1 
ATOM   2338  C  CB  . MET A 1 290  ? 25.826 63.848  31.657  1.00 17.18 ? 290  MET A CB  1 
ATOM   2339  C  CG  . MET A 1 290  ? 25.714 62.390  31.318  1.00 19.33 ? 290  MET A CG  1 
ATOM   2340  S  SD  . MET A 1 290  ? 26.093 61.232  32.644  1.00 21.13 ? 290  MET A SD  1 
ATOM   2341  C  CE  . MET A 1 290  ? 27.893 61.193  32.509  1.00 20.21 ? 290  MET A CE  1 
ATOM   2342  N  N   . GLY A 1 291  ? 26.050 67.101  30.238  1.00 19.22 ? 291  GLY A N   1 
ATOM   2343  C  CA  . GLY A 1 291  ? 25.915 68.544  30.398  1.00 18.75 ? 291  GLY A CA  1 
ATOM   2344  C  C   . GLY A 1 291  ? 27.197 69.371  30.482  1.00 18.68 ? 291  GLY A C   1 
ATOM   2345  O  O   . GLY A 1 291  ? 27.315 70.438  29.840  1.00 19.34 ? 291  GLY A O   1 
ATOM   2346  N  N   . SER A 1 292  ? 28.159 68.902  31.279  1.00 16.95 ? 292  SER A N   1 
ATOM   2347  C  CA  . SER A 1 292  ? 29.402 69.638  31.516  1.00 15.15 ? 292  SER A CA  1 
ATOM   2348  C  C   . SER A 1 292  ? 30.278 69.833  30.265  1.00 13.46 ? 292  SER A C   1 
ATOM   2349  O  O   . SER A 1 292  ? 31.145 70.713  30.250  1.00 12.11 ? 292  SER A O   1 
ATOM   2350  C  CB  . SER A 1 292  ? 30.214 68.939  32.609  1.00 15.48 ? 292  SER A CB  1 
ATOM   2351  O  OG  . SER A 1 292  ? 30.686 67.682  32.144  1.00 17.76 ? 292  SER A OG  1 
ATOM   2352  N  N   . PHE A 1 293  ? 30.060 69.014  29.234  1.00 11.64 ? 293  PHE A N   1 
ATOM   2353  C  CA  . PHE A 1 293  ? 30.798 69.123  27.974  1.00 12.23 ? 293  PHE A CA  1 
ATOM   2354  C  C   . PHE A 1 293  ? 30.065 69.961  26.934  1.00 12.38 ? 293  PHE A C   1 
ATOM   2355  O  O   . PHE A 1 293  ? 30.517 70.039  25.794  1.00 13.00 ? 293  PHE A O   1 
ATOM   2356  C  CB  . PHE A 1 293  ? 31.110 67.734  27.398  1.00 12.11 ? 293  PHE A CB  1 
ATOM   2357  C  CG  . PHE A 1 293  ? 31.977 66.889  28.280  1.00 10.67 ? 293  PHE A CG  1 
ATOM   2358  C  CD1 . PHE A 1 293  ? 33.355 66.975  28.207  1.00 10.91 ? 293  PHE A CD1 1 
ATOM   2359  C  CD2 . PHE A 1 293  ? 31.401 65.972  29.125  1.00 11.53 ? 293  PHE A CD2 1 
ATOM   2360  C  CE1 . PHE A 1 293  ? 34.172 66.165  28.998  1.00 11.43 ? 293  PHE A CE1 1 
ATOM   2361  C  CE2 . PHE A 1 293  ? 32.206 65.147  29.941  1.00 12.04 ? 293  PHE A CE2 1 
ATOM   2362  C  CZ  . PHE A 1 293  ? 33.581 65.269  29.872  1.00 12.57 ? 293  PHE A CZ  1 
ATOM   2363  N  N   . GLY A 1 294  ? 28.941 70.556  27.316  1.00 12.32 ? 294  GLY A N   1 
ATOM   2364  C  CA  . GLY A 1 294  ? 28.179 71.371  26.388  1.00 13.31 ? 294  GLY A CA  1 
ATOM   2365  C  C   . GLY A 1 294  ? 27.458 70.568  25.314  1.00 14.19 ? 294  GLY A C   1 
ATOM   2366  O  O   . GLY A 1 294  ? 27.147 71.094  24.237  1.00 15.66 ? 294  GLY A O   1 
ATOM   2367  N  N   . LEU A 1 295  ? 27.229 69.286  25.581  1.00 13.10 ? 295  LEU A N   1 
ATOM   2368  C  CA  . LEU A 1 295  ? 26.466 68.462  24.678  1.00 13.01 ? 295  LEU A CA  1 
ATOM   2369  C  C   . LEU A 1 295  ? 25.226 67.951  25.383  1.00 13.55 ? 295  LEU A C   1 
ATOM   2370  O  O   . LEU A 1 295  ? 25.194 67.838  26.606  1.00 14.11 ? 295  LEU A O   1 
ATOM   2371  C  CB  . LEU A 1 295  ? 27.299 67.289  24.180  1.00 13.00 ? 295  LEU A CB  1 
ATOM   2372  C  CG  . LEU A 1 295  ? 28.634 67.646  23.528  1.00 13.69 ? 295  LEU A CG  1 
ATOM   2373  C  CD1 . LEU A 1 295  ? 29.432 66.379  23.253  1.00 15.28 ? 295  LEU A CD1 1 
ATOM   2374  C  CD2 . LEU A 1 295  ? 28.412 68.416  22.227  1.00 15.84 ? 295  LEU A CD2 1 
ATOM   2375  N  N   . SER A 1 296  ? 24.203 67.661  24.596  1.00 13.97 ? 296  SER A N   1 
ATOM   2376  C  CA  . SER A 1 296  ? 22.967 67.103  25.144  1.00 15.02 ? 296  SER A CA  1 
ATOM   2377  C  C   . SER A 1 296  ? 22.388 66.087  24.170  1.00 15.30 ? 296  SER A C   1 
ATOM   2378  O  O   . SER A 1 296  ? 22.946 65.869  23.091  1.00 14.04 ? 296  SER A O   1 
ATOM   2379  C  CB  . SER A 1 296  ? 21.992 68.232  25.479  1.00 15.27 ? 296  SER A CB  1 
ATOM   2380  O  OG  . SER A 1 296  ? 21.698 68.988  24.322  1.00 17.08 ? 296  SER A OG  1 
ATOM   2381  N  N   . CYS A 1 297  ? 21.296 65.424  24.563  1.00 15.09 ? 297  CYS A N   1 
ATOM   2382  C  CA  . CYS A 1 297  ? 20.592 64.484  23.677  1.00 15.21 ? 297  CYS A CA  1 
ATOM   2383  C  C   . CYS A 1 297  ? 19.361 65.135  23.015  1.00 15.01 ? 297  CYS A C   1 
ATOM   2384  O  O   . CYS A 1 297  ? 18.459 65.584  23.729  1.00 15.20 ? 297  CYS A O   1 
ATOM   2385  C  CB  . CYS A 1 297  ? 20.175 63.213  24.453  1.00 15.31 ? 297  CYS A CB  1 
ATOM   2386  S  SG  . CYS A 1 297  ? 21.566 62.033  24.693  1.00 19.59 ? 297  CYS A SG  1 
ATOM   2387  N  N   . PRO A 1 298  ? 19.328 65.224  21.682  1.00 15.42 ? 298  PRO A N   1 
ATOM   2388  C  CA  . PRO A 1 298  ? 18.184 65.763  20.928  1.00 15.78 ? 298  PRO A CA  1 
ATOM   2389  C  C   . PRO A 1 298  ? 16.869 65.057  21.282  1.00 15.49 ? 298  PRO A C   1 
ATOM   2390  O  O   . PRO A 1 298  ? 15.783 65.641  21.132  1.00 16.33 ? 298  PRO A O   1 
ATOM   2391  C  CB  . PRO A 1 298  ? 18.541 65.406  19.475  1.00 17.26 ? 298  PRO A CB  1 
ATOM   2392  C  CG  . PRO A 1 298  ? 19.976 65.367  19.433  1.00 17.44 ? 298  PRO A CG  1 
ATOM   2393  C  CD  . PRO A 1 298  ? 20.443 64.877  20.773  1.00 15.42 ? 298  PRO A CD  1 
ATOM   2394  N  N   . TRP A 1 299  ? 16.970 63.801  21.700  1.00 14.86 ? 299  TRP A N   1 
ATOM   2395  C  CA  . TRP A 1 299  ? 15.781 62.988  21.992  1.00 14.46 ? 299  TRP A CA  1 
ATOM   2396  C  C   . TRP A 1 299  ? 15.309 63.163  23.428  1.00 15.18 ? 299  TRP A C   1 
ATOM   2397  O  O   . TRP A 1 299  ? 14.341 62.513  23.849  1.00 14.88 ? 299  TRP A O   1 
ATOM   2398  C  CB  . TRP A 1 299  ? 16.029 61.497  21.657  1.00 13.69 ? 299  TRP A CB  1 
ATOM   2399  C  CG  . TRP A 1 299  ? 16.372 61.346  20.224  1.00 12.30 ? 299  TRP A CG  1 
ATOM   2400  C  CD1 . TRP A 1 299  ? 15.506 61.141  19.199  1.00 12.69 ? 299  TRP A CD1 1 
ATOM   2401  C  CD2 . TRP A 1 299  ? 17.677 61.440  19.639  1.00 11.90 ? 299  TRP A CD2 1 
ATOM   2402  N  NE1 . TRP A 1 299  ? 16.184 61.089  18.001  1.00 13.23 ? 299  TRP A NE1 1 
ATOM   2403  C  CE2 . TRP A 1 299  ? 17.519 61.264  18.242  1.00 10.75 ? 299  TRP A CE2 1 
ATOM   2404  C  CE3 . TRP A 1 299  ? 18.957 61.628  20.153  1.00 10.82 ? 299  TRP A CE3 1 
ATOM   2405  C  CZ2 . TRP A 1 299  ? 18.597 61.316  17.343  1.00 11.04 ? 299  TRP A CZ2 1 
ATOM   2406  C  CZ3 . TRP A 1 299  ? 20.030 61.670  19.262  1.00 11.54 ? 299  TRP A CZ3 1 
ATOM   2407  C  CH2 . TRP A 1 299  ? 19.833 61.511  17.874  1.00 10.99 ? 299  TRP A CH2 1 
ATOM   2408  N  N   . LYS A 1 300  ? 16.008 64.023  24.174  1.00 14.40 ? 300  LYS A N   1 
ATOM   2409  C  CA  . LYS A 1 300  ? 15.501 64.567  25.460  1.00 15.74 ? 300  LYS A CA  1 
ATOM   2410  C  C   . LYS A 1 300  ? 15.610 63.630  26.645  1.00 15.92 ? 300  LYS A C   1 
ATOM   2411  O  O   . LYS A 1 300  ? 15.103 63.936  27.746  1.00 17.00 ? 300  LYS A O   1 
ATOM   2412  C  CB  . LYS A 1 300  ? 14.062 65.079  25.325  1.00 16.42 ? 300  LYS A CB  1 
ATOM   2413  C  CG  . LYS A 1 300  ? 13.927 66.171  24.327  1.00 19.31 ? 300  LYS A CG  1 
ATOM   2414  C  CD  . LYS A 1 300  ? 12.487 66.666  24.235  1.00 23.71 ? 300  LYS A CD  1 
ATOM   2415  C  CE  . LYS A 1 300  ? 12.340 67.676  23.106  1.00 27.11 ? 300  LYS A CE  1 
ATOM   2416  N  NZ  . LYS A 1 300  ? 11.304 68.709  23.435  1.00 30.36 ? 300  LYS A NZ  1 
ATOM   2417  N  N   . VAL A 1 301  ? 16.268 62.492  26.465  1.00 15.02 ? 301  VAL A N   1 
ATOM   2418  C  CA  . VAL A 1 301  ? 16.591 61.651  27.608  1.00 14.49 ? 301  VAL A CA  1 
ATOM   2419  C  C   . VAL A 1 301  ? 18.114 61.620  27.754  1.00 14.25 ? 301  VAL A C   1 
ATOM   2420  O  O   . VAL A 1 301  ? 18.799 61.107  26.856  1.00 15.42 ? 301  VAL A O   1 
ATOM   2421  C  CB  . VAL A 1 301  ? 16.066 60.205  27.469  1.00 14.39 ? 301  VAL A CB  1 
ATOM   2422  C  CG1 . VAL A 1 301  ? 16.357 59.443  28.746  1.00 15.05 ? 301  VAL A CG1 1 
ATOM   2423  C  CG2 . VAL A 1 301  ? 14.580 60.188  27.189  1.00 16.38 ? 301  VAL A CG2 1 
ATOM   2424  N  N   . PRO A 1 302  ? 18.656 62.165  28.837  1.00 13.25 ? 302  PRO A N   1 
ATOM   2425  C  CA  . PRO A 1 302  ? 20.105 62.264  28.974  1.00 13.89 ? 302  PRO A CA  1 
ATOM   2426  C  C   . PRO A 1 302  ? 20.718 60.935  29.373  1.00 13.37 ? 302  PRO A C   1 
ATOM   2427  O  O   . PRO A 1 302  ? 20.035 60.054  29.883  1.00 13.29 ? 302  PRO A O   1 
ATOM   2428  C  CB  . PRO A 1 302  ? 20.281 63.318  30.080  1.00 14.39 ? 302  PRO A CB  1 
ATOM   2429  C  CG  . PRO A 1 302  ? 19.030 63.204  30.909  1.00 15.44 ? 302  PRO A CG  1 
ATOM   2430  C  CD  . PRO A 1 302  ? 17.944 62.751  30.004  1.00 14.13 ? 302  PRO A CD  1 
ATOM   2431  N  N   . PRO A 1 303  ? 22.022 60.790  29.178  1.00 12.15 ? 303  PRO A N   1 
ATOM   2432  C  CA  . PRO A 1 303  ? 22.720 59.658  29.780  1.00 12.15 ? 303  PRO A CA  1 
ATOM   2433  C  C   . PRO A 1 303  ? 22.670 59.794  31.286  1.00 14.12 ? 303  PRO A C   1 
ATOM   2434  O  O   . PRO A 1 303  ? 22.585 60.916  31.816  1.00 14.94 ? 303  PRO A O   1 
ATOM   2435  C  CB  . PRO A 1 303  ? 24.179 59.835  29.307  1.00 11.75 ? 303  PRO A CB  1 
ATOM   2436  C  CG  . PRO A 1 303  ? 24.140 60.904  28.255  1.00 13.64 ? 303  PRO A CG  1 
ATOM   2437  C  CD  . PRO A 1 303  ? 22.935 61.709  28.476  1.00 13.41 ? 303  PRO A CD  1 
ATOM   2438  N  N   . ARG A 1 304  ? 22.747 58.653  31.962  1.00 14.46 ? 304  ARG A N   1 
ATOM   2439  C  CA  . ARG A 1 304  ? 22.916 58.631  33.404  1.00 15.50 ? 304  ARG A CA  1 
ATOM   2440  C  C   . ARG A 1 304  ? 24.146 57.814  33.753  1.00 13.85 ? 304  ARG A C   1 
ATOM   2441  O  O   . ARG A 1 304  ? 24.392 56.756  33.136  1.00 12.38 ? 304  ARG A O   1 
ATOM   2442  C  CB  . ARG A 1 304  ? 21.680 58.044  34.081  1.00 17.42 ? 304  ARG A CB  1 
ATOM   2443  C  CG  . ARG A 1 304  ? 20.482 58.992  33.996  1.00 21.65 ? 304  ARG A CG  1 
ATOM   2444  C  CD  . ARG A 1 304  ? 19.244 58.515  34.707  1.00 28.59 ? 304  ARG A CD  1 
ATOM   2445  N  NE  . ARG A 1 304  ? 18.393 57.689  33.847  1.00 32.07 ? 304  ARG A NE  1 
ATOM   2446  C  CZ  . ARG A 1 304  ? 18.121 56.404  34.069  1.00 35.00 ? 304  ARG A CZ  1 
ATOM   2447  N  NH1 . ARG A 1 304  ? 18.630 55.776  35.125  1.00 34.96 ? 304  ARG A NH1 1 
ATOM   2448  N  NH2 . ARG A 1 304  ? 17.325 55.745  33.236  1.00 36.04 ? 304  ARG A NH2 1 
ATOM   2449  N  N   . THR A 1 305  ? 24.925 58.313  34.703  1.00 12.94 ? 305  THR A N   1 
ATOM   2450  C  CA  . THR A 1 305  ? 26.100 57.620  35.199  1.00 13.12 ? 305  THR A CA  1 
ATOM   2451  C  C   . THR A 1 305  ? 25.717 56.215  35.643  1.00 12.57 ? 305  THR A C   1 
ATOM   2452  O  O   . THR A 1 305  ? 24.687 56.039  36.320  1.00 13.37 ? 305  THR A O   1 
ATOM   2453  C  CB  . THR A 1 305  ? 26.697 58.400  36.372  1.00 13.45 ? 305  THR A CB  1 
ATOM   2454  O  OG1 . THR A 1 305  ? 27.204 59.645  35.860  1.00 16.52 ? 305  THR A OG1 1 
ATOM   2455  C  CG2 . THR A 1 305  ? 27.891 57.714  36.962  1.00 15.42 ? 305  THR A CG2 1 
ATOM   2456  N  N   . ILE A 1 306  ? 26.468 55.212  35.199  1.00 11.75 ? 306  ILE A N   1 
ATOM   2457  C  CA  . ILE A 1 306  ? 26.182 53.829  35.601  1.00 11.62 ? 306  ILE A CA  1 
ATOM   2458  C  C   . ILE A 1 306  ? 26.616 53.610  37.050  1.00 13.44 ? 306  ILE A C   1 
ATOM   2459  O  O   . ILE A 1 306  ? 27.725 53.952  37.449  1.00 13.96 ? 306  ILE A O   1 
ATOM   2460  C  CB  . ILE A 1 306  ? 26.863 52.816  34.624  1.00 11.68 ? 306  ILE A CB  1 
ATOM   2461  C  CG1 . ILE A 1 306  ? 26.508 53.090  33.149  1.00 10.29 ? 306  ILE A CG1 1 
ATOM   2462  C  CG2 . ILE A 1 306  ? 26.515 51.353  35.003  1.00 13.09 ? 306  ILE A CG2 1 
ATOM   2463  C  CD1 . ILE A 1 306  ? 25.039 53.080  32.831  1.00 12.45 ? 306  ILE A CD1 1 
ATOM   2464  N  N   . SER A 1 307  ? 25.718 52.986  37.824  1.00 15.16 ? 307  SER A N   1 
ATOM   2465  C  CA  . SER A 1 307  ? 25.929 52.710  39.235  1.00 17.03 ? 307  SER A CA  1 
ATOM   2466  C  C   . SER A 1 307  ? 25.432 51.301  39.505  1.00 17.68 ? 307  SER A C   1 
ATOM   2467  O  O   . SER A 1 307  ? 24.711 50.724  38.691  1.00 16.84 ? 307  SER A O   1 
ATOM   2468  C  CB  . SER A 1 307  ? 25.065 53.662  40.073  1.00 16.83 ? 307  SER A CB  1 
ATOM   2469  O  OG  . SER A 1 307  ? 23.687 53.374  39.919  1.00 17.18 ? 307  SER A OG  1 
ATOM   2470  N  N   . ASP A 1 308  ? 25.694 50.795  40.702  1.00 18.84 ? 308  ASP A N   1 
ATOM   2471  C  CA  . ASP A 1 308  ? 25.093 49.507  41.085  1.00 20.31 ? 308  ASP A CA  1 
ATOM   2472  C  C   . ASP A 1 308  ? 23.551 49.464  41.080  1.00 19.62 ? 308  ASP A C   1 
ATOM   2473  O  O   . ASP A 1 308  ? 22.988 48.414  40.752  1.00 19.19 ? 308  ASP A O   1 
ATOM   2474  C  CB  . ASP A 1 308  ? 25.652 48.979  42.410  1.00 22.88 ? 308  ASP A CB  1 
ATOM   2475  C  CG  . ASP A 1 308  ? 27.183 48.977  42.468  1.00 25.82 ? 308  ASP A CG  1 
ATOM   2476  O  OD1 . ASP A 1 308  ? 27.879 48.805  41.434  1.00 30.98 ? 308  ASP A OD1 1 
ATOM   2477  O  OD2 . ASP A 1 308  ? 27.791 49.137  43.549  1.00 32.34 ? 308  ASP A OD2 1 
ATOM   2478  N  N   A GLN A 1 309  ? 22.880 50.577  41.393  0.50 18.41 ? 309  GLN A N   1 
ATOM   2479  N  N   B GLN A 1 309  ? 22.899 50.571  41.444  0.50 19.40 ? 309  GLN A N   1 
ATOM   2480  C  CA  A GLN A 1 309  ? 21.404 50.633  41.469  0.50 17.90 ? 309  GLN A CA  1 
ATOM   2481  C  CA  B GLN A 1 309  ? 21.436 50.656  41.470  0.50 19.73 ? 309  GLN A CA  1 
ATOM   2482  C  C   A GLN A 1 309  ? 20.726 50.841  40.127  0.50 17.34 ? 309  GLN A C   1 
ATOM   2483  C  C   B GLN A 1 309  ? 20.849 50.496  40.088  0.50 19.08 ? 309  GLN A C   1 
ATOM   2484  O  O   A GLN A 1 309  ? 19.488 50.806  40.021  0.50 15.24 ? 309  GLN A O   1 
ATOM   2485  O  O   B GLN A 1 309  ? 19.771 49.921  39.927  0.50 19.92 ? 309  GLN A O   1 
ATOM   2486  C  CB  A GLN A 1 309  ? 20.913 51.731  42.431  0.50 17.63 ? 309  GLN A CB  1 
ATOM   2487  C  CB  B GLN A 1 309  ? 20.944 52.016  41.983  0.50 19.75 ? 309  GLN A CB  1 
ATOM   2488  C  CG  A GLN A 1 309  ? 21.398 51.597  43.868  0.50 17.76 ? 309  GLN A CG  1 
ATOM   2489  C  CG  B GLN A 1 309  ? 21.011 52.295  43.469  0.50 21.07 ? 309  GLN A CG  1 
ATOM   2490  C  CD  A GLN A 1 309  ? 22.875 51.878  44.014  0.50 17.54 ? 309  GLN A CD  1 
ATOM   2491  C  CD  B GLN A 1 309  ? 20.617 53.735  43.751  0.50 20.20 ? 309  GLN A CD  1 
ATOM   2492  O  OE1 A GLN A 1 309  ? 23.371 52.916  43.550  0.50 16.46 ? 309  GLN A OE1 1 
ATOM   2493  O  OE1 B GLN A 1 309  ? 19.721 54.278  43.094  0.50 20.15 ? 309  GLN A OE1 1 
ATOM   2494  N  NE2 A GLN A 1 309  ? 23.589 50.956  44.646  0.50 18.24 ? 309  GLN A NE2 1 
ATOM   2495  N  NE2 B GLN A 1 309  ? 21.304 54.369  44.684  0.50 22.56 ? 309  GLN A NE2 1 
ATOM   2496  N  N   . ASN A 1 310  ? 21.525 51.066  39.089  1.00 17.24 ? 310  ASN A N   1 
ATOM   2497  C  CA  . ASN A 1 310  ? 20.926 51.195  37.789  1.00 15.87 ? 310  ASN A CA  1 
ATOM   2498  C  C   . ASN A 1 310  ? 21.557 50.279  36.746  1.00 13.98 ? 310  ASN A C   1 
ATOM   2499  O  O   . ASN A 1 310  ? 21.003 50.191  35.688  1.00 14.15 ? 310  ASN A O   1 
ATOM   2500  C  CB  . ASN A 1 310  ? 20.862 52.657  37.323  1.00 15.07 ? 310  ASN A CB  1 
ATOM   2501  C  CG  . ASN A 1 310  ? 22.239 53.220  36.964  1.00 14.97 ? 310  ASN A CG  1 
ATOM   2502  O  OD1 . ASN A 1 310  ? 23.212 52.477  36.744  1.00 14.08 ? 310  ASN A OD1 1 
ATOM   2503  N  ND2 . ASN A 1 310  ? 22.321 54.539  36.929  1.00 16.22 ? 310  ASN A ND2 1 
ATOM   2504  N  N   . VAL A 1 311  ? 22.658 49.613  37.069  1.00 13.26 ? 311  VAL A N   1 
ATOM   2505  C  CA  . VAL A 1 311  ? 23.416 48.914  36.004  1.00 13.38 ? 311  VAL A CA  1 
ATOM   2506  C  C   . VAL A 1 311  ? 22.557 47.803  35.406  1.00 14.02 ? 311  VAL A C   1 
ATOM   2507  O  O   . VAL A 1 311  ? 22.582 47.600  34.198  1.00 13.46 ? 311  VAL A O   1 
ATOM   2508  C  CB  . VAL A 1 311  ? 24.788 48.395  36.435  1.00 13.30 ? 311  VAL A CB  1 
ATOM   2509  C  CG1 . VAL A 1 311  ? 24.684 47.305  37.521  1.00 15.22 ? 311  VAL A CG1 1 
ATOM   2510  C  CG2 . VAL A 1 311  ? 25.590 47.887  35.210  1.00 14.07 ? 311  VAL A CG2 1 
ATOM   2511  N  N   . ALA A 1 312  ? 21.756 47.107  36.216  1.00 13.61 ? 312  ALA A N   1 
ATOM   2512  C  CA  . ALA A 1 312  ? 20.936 46.037  35.637  1.00 13.96 ? 312  ALA A CA  1 
ATOM   2513  C  C   . ALA A 1 312  ? 19.960 46.588  34.623  1.00 13.77 ? 312  ALA A C   1 
ATOM   2514  O  O   . ALA A 1 312  ? 19.806 46.034  33.518  1.00 14.44 ? 312  ALA A O   1 
ATOM   2515  C  CB  . ALA A 1 312  ? 20.189 45.237  36.741  1.00 14.60 ? 312  ALA A CB  1 
ATOM   2516  N  N   . ALA A 1 313  ? 19.285 47.688  34.955  1.00 14.09 ? 313  ALA A N   1 
ATOM   2517  C  CA  . ALA A 1 313  ? 18.303 48.286  34.055  1.00 13.65 ? 313  ALA A CA  1 
ATOM   2518  C  C   . ALA A 1 313  ? 18.969 48.867  32.794  1.00 13.35 ? 313  ALA A C   1 
ATOM   2519  O  O   . ALA A 1 313  ? 18.480 48.690  31.696  1.00 13.28 ? 313  ALA A O   1 
ATOM   2520  C  CB  . ALA A 1 313  ? 17.485 49.390  34.757  1.00 14.79 ? 313  ALA A CB  1 
ATOM   2521  N  N   . ARG A 1 314  ? 20.060 49.591  33.001  1.00 12.92 ? 314  ARG A N   1 
ATOM   2522  C  CA  . ARG A 1 314  ? 20.806 50.198  31.882  1.00 11.95 ? 314  ARG A CA  1 
ATOM   2523  C  C   . ARG A 1 314  ? 21.311 49.113  30.937  1.00 10.97 ? 314  ARG A C   1 
ATOM   2524  O  O   . ARG A 1 314  ? 21.233 49.288  29.717  1.00 11.67 ? 314  ARG A O   1 
ATOM   2525  C  CB  . ARG A 1 314  ? 21.990 50.965  32.431  1.00 10.85 ? 314  ARG A CB  1 
ATOM   2526  C  CG  . ARG A 1 314  ? 21.621 52.185  33.272  1.00 13.24 ? 314  ARG A CG  1 
ATOM   2527  C  CD  . ARG A 1 314  ? 21.318 53.453  32.456  1.00 16.74 ? 314  ARG A CD  1 
ATOM   2528  N  NE  . ARG A 1 314  ? 19.942 53.492  31.991  1.00 17.12 ? 314  ARG A NE  1 
ATOM   2529  C  CZ  . ARG A 1 314  ? 19.436 54.391  31.157  1.00 16.89 ? 314  ARG A CZ  1 
ATOM   2530  N  NH1 . ARG A 1 314  ? 20.206 55.340  30.618  1.00 17.35 ? 314  ARG A NH1 1 
ATOM   2531  N  NH2 . ARG A 1 314  ? 18.154 54.346  30.836  1.00 19.07 ? 314  ARG A NH2 1 
ATOM   2532  N  N   . SER A 1 315  ? 21.798 48.012  31.499  1.00 12.54 ? 315  SER A N   1 
ATOM   2533  C  CA  . SER A 1 315  ? 22.311 46.894  30.697  1.00 12.04 ? 315  SER A CA  1 
ATOM   2534  C  C   . SER A 1 315  ? 21.210 46.253  29.905  1.00 13.44 ? 315  SER A C   1 
ATOM   2535  O  O   . SER A 1 315  ? 21.413 45.847  28.748  1.00 13.47 ? 315  SER A O   1 
ATOM   2536  C  CB  . SER A 1 315  ? 22.952 45.850  31.595  1.00 11.75 ? 315  SER A CB  1 
ATOM   2537  O  OG  . SER A 1 315  ? 24.151 46.299  32.161  1.00 12.01 ? 315  SER A OG  1 
ATOM   2538  N  N   . ASP A 1 316  ? 20.036 46.083  30.518  1.00 12.85 ? 316  ASP A N   1 
ATOM   2539  C  CA  A ASP A 1 316  ? 18.902 45.555  29.794  0.50 13.30 ? 316  ASP A CA  1 
ATOM   2540  C  CA  B ASP A 1 316  ? 18.844 45.592  29.799  0.50 13.71 ? 316  ASP A CA  1 
ATOM   2541  C  C   . ASP A 1 316  ? 18.597 46.404  28.544  1.00 12.91 ? 316  ASP A C   1 
ATOM   2542  O  O   . ASP A 1 316  ? 18.388 45.855  27.460  1.00 13.34 ? 316  ASP A O   1 
ATOM   2543  C  CB  A ASP A 1 316  ? 17.709 45.497  30.745  0.50 13.67 ? 316  ASP A CB  1 
ATOM   2544  C  CB  B ASP A 1 316  ? 17.550 45.748  30.613  0.50 14.54 ? 316  ASP A CB  1 
ATOM   2545  C  CG  A ASP A 1 316  ? 16.718 44.427  30.389  0.50 15.29 ? 316  ASP A CG  1 
ATOM   2546  C  CG  B ASP A 1 316  ? 17.448 44.817  31.798  0.50 17.13 ? 316  ASP A CG  1 
ATOM   2547  O  OD1 A ASP A 1 316  ? 17.124 43.364  29.887  0.50 16.71 ? 316  ASP A OD1 1 
ATOM   2548  O  OD1 B ASP A 1 316  ? 18.309 43.942  32.005  0.50 19.96 ? 316  ASP A OD1 1 
ATOM   2549  O  OD2 A ASP A 1 316  ? 15.503 44.560  30.616  0.50 18.44 ? 316  ASP A OD2 1 
ATOM   2550  O  OD2 B ASP A 1 316  ? 16.485 44.909  32.594  0.50 21.34 ? 316  ASP A OD2 1 
ATOM   2551  N  N   . LEU A 1 317  ? 18.578 47.731  28.693  1.00 12.97 ? 317  LEU A N   1 
ATOM   2552  C  CA  . LEU A 1 317  ? 18.268 48.601  27.576  1.00 12.66 ? 317  LEU A CA  1 
ATOM   2553  C  C   . LEU A 1 317  ? 19.319 48.498  26.481  1.00 11.40 ? 317  LEU A C   1 
ATOM   2554  O  O   . LEU A 1 317  ? 18.967 48.406  25.307  1.00 11.33 ? 317  LEU A O   1 
ATOM   2555  C  CB  . LEU A 1 317  ? 18.167 50.070  28.020  1.00 14.10 ? 317  LEU A CB  1 
ATOM   2556  C  CG  . LEU A 1 317  ? 16.786 50.575  28.439  1.00 17.45 ? 317  LEU A CG  1 
ATOM   2557  C  CD1 . LEU A 1 317  ? 16.918 51.912  29.186  1.00 21.85 ? 317  LEU A CD1 1 
ATOM   2558  C  CD2 . LEU A 1 317  ? 15.845 50.689  27.245  1.00 19.50 ? 317  LEU A CD2 1 
ATOM   2559  N  N   . LEU A 1 318  ? 20.576 48.470  26.905  1.00 10.70 ? 318  LEU A N   1 
ATOM   2560  C  CA  . LEU A 1 318  ? 21.687 48.480  25.954  1.00 9.88  ? 318  LEU A CA  1 
ATOM   2561  C  C   . LEU A 1 318  ? 21.791 47.139  25.226  1.00 10.37 ? 318  LEU A C   1 
ATOM   2562  O  O   . LEU A 1 318  ? 21.896 47.108  23.980  1.00 9.83  ? 318  LEU A O   1 
ATOM   2563  C  CB  . LEU A 1 318  ? 22.991 48.855  26.647  1.00 10.17 ? 318  LEU A CB  1 
ATOM   2564  C  CG  . LEU A 1 318  ? 24.219 48.905  25.730  1.00 11.94 ? 318  LEU A CG  1 
ATOM   2565  C  CD1 . LEU A 1 318  ? 24.029 49.945  24.639  1.00 11.32 ? 318  LEU A CD1 1 
ATOM   2566  C  CD2 . LEU A 1 318  ? 25.450 49.224  26.555  1.00 14.18 ? 318  LEU A CD2 1 
ATOM   2567  N  N   . VAL A 1 319  ? 21.712 46.027  25.961  1.00 9.62  ? 319  VAL A N   1 
ATOM   2568  C  CA  . VAL A 1 319  ? 21.802 44.719  25.308  1.00 9.63  ? 319  VAL A CA  1 
ATOM   2569  C  C   . VAL A 1 319  ? 20.648 44.531  24.320  1.00 9.28  ? 319  VAL A C   1 
ATOM   2570  O  O   . VAL A 1 319  ? 20.823 43.945  23.263  1.00 9.80  ? 319  VAL A O   1 
ATOM   2571  C  CB  . VAL A 1 319  ? 21.826 43.589  26.344  1.00 9.74  ? 319  VAL A CB  1 
ATOM   2572  C  CG1 . VAL A 1 319  ? 21.654 42.217  25.648  1.00 11.70 ? 319  VAL A CG1 1 
ATOM   2573  C  CG2 . VAL A 1 319  ? 23.130 43.629  27.117  1.00 10.15 ? 319  VAL A CG2 1 
ATOM   2574  N  N   . ASP A 1 320  ? 19.463 45.029  24.650  1.00 9.94  ? 320  ASP A N   1 
ATOM   2575  C  CA  . ASP A 1 320  ? 18.338 44.976  23.735  1.00 10.08 ? 320  ASP A CA  1 
ATOM   2576  C  C   . ASP A 1 320  ? 18.661 45.714  22.425  1.00 9.71  ? 320  ASP A C   1 
ATOM   2577  O  O   . ASP A 1 320  ? 18.325 45.216  21.343  1.00 10.35 ? 320  ASP A O   1 
ATOM   2578  C  CB  . ASP A 1 320  ? 17.068 45.539  24.417  1.00 11.66 ? 320  ASP A CB  1 
ATOM   2579  C  CG  . ASP A 1 320  ? 15.907 45.631  23.496  1.00 12.43 ? 320  ASP A CG  1 
ATOM   2580  O  OD1 . ASP A 1 320  ? 15.370 44.547  23.124  1.00 15.46 ? 320  ASP A OD1 1 
ATOM   2581  O  OD2 . ASP A 1 320  ? 15.429 46.726  23.109  1.00 14.31 ? 320  ASP A OD2 1 
ATOM   2582  N  N   . GLN A 1 321  ? 19.284 46.888  22.517  1.00 9.60  ? 321  GLN A N   1 
ATOM   2583  C  CA  . GLN A 1 321  ? 19.679 47.584  21.278  1.00 8.23  ? 321  GLN A CA  1 
ATOM   2584  C  C   . GLN A 1 321  ? 20.694 46.747  20.483  1.00 7.20  ? 321  GLN A C   1 
ATOM   2585  O  O   . GLN A 1 321  ? 20.566 46.611  19.269  1.00 8.05  ? 321  GLN A O   1 
ATOM   2586  C  CB  . GLN A 1 321  ? 20.319 48.934  21.637  1.00 7.82  ? 321  GLN A CB  1 
ATOM   2587  C  CG  . GLN A 1 321  ? 19.313 49.992  22.066  1.00 9.35  ? 321  GLN A CG  1 
ATOM   2588  C  CD  . GLN A 1 321  ? 18.243 50.213  20.984  1.00 10.23 ? 321  GLN A CD  1 
ATOM   2589  O  OE1 . GLN A 1 321  ? 18.579 50.579  19.864  1.00 11.28 ? 321  GLN A OE1 1 
ATOM   2590  N  NE2 . GLN A 1 321  ? 16.962 49.968  21.303  1.00 11.44 ? 321  GLN A NE2 1 
ATOM   2591  N  N   . TRP A 1 322  ? 21.695 46.211  21.168  1.00 7.55  ? 322  TRP A N   1 
ATOM   2592  C  CA  . TRP A 1 322  ? 22.698 45.387  20.516  1.00 8.23  ? 322  TRP A CA  1 
ATOM   2593  C  C   . TRP A 1 322  ? 22.087 44.185  19.817  1.00 8.92  ? 322  TRP A C   1 
ATOM   2594  O  O   . TRP A 1 322  ? 22.441 43.835  18.672  1.00 9.18  ? 322  TRP A O   1 
ATOM   2595  C  CB  . TRP A 1 322  ? 23.692 44.900  21.546  1.00 8.59  ? 322  TRP A CB  1 
ATOM   2596  C  CG  . TRP A 1 322  ? 24.636 45.960  22.080  1.00 7.44  ? 322  TRP A CG  1 
ATOM   2597  C  CD1 . TRP A 1 322  ? 24.816 47.255  21.631  1.00 9.50  ? 322  TRP A CD1 1 
ATOM   2598  C  CD2 . TRP A 1 322  ? 25.524 45.796  23.189  1.00 7.77  ? 322  TRP A CD2 1 
ATOM   2599  N  NE1 . TRP A 1 322  ? 25.786 47.876  22.392  1.00 10.44 ? 322  TRP A NE1 1 
ATOM   2600  C  CE2 . TRP A 1 322  ? 26.251 46.992  23.338  1.00 8.67  ? 322  TRP A CE2 1 
ATOM   2601  C  CE3 . TRP A 1 322  ? 25.823 44.717  24.041  1.00 9.56  ? 322  TRP A CE3 1 
ATOM   2602  C  CZ2 . TRP A 1 322  ? 27.207 47.162  24.336  1.00 8.96  ? 322  TRP A CZ2 1 
ATOM   2603  C  CZ3 . TRP A 1 322  ? 26.768 44.895  25.022  1.00 9.30  ? 322  TRP A CZ3 1 
ATOM   2604  C  CH2 . TRP A 1 322  ? 27.454 46.090  25.152  1.00 9.16  ? 322  TRP A CH2 1 
ATOM   2605  N  N   . LYS A 1 323  ? 21.160 43.528  20.507  1.00 8.26  ? 323  LYS A N   1 
ATOM   2606  C  CA  . LYS A 1 323  ? 20.550 42.337  19.903  1.00 8.83  ? 323  LYS A CA  1 
ATOM   2607  C  C   . LYS A 1 323  ? 19.692 42.660  18.705  1.00 9.09  ? 323  LYS A C   1 
ATOM   2608  O  O   . LYS A 1 323  ? 19.613 41.866  17.758  1.00 10.43 ? 323  LYS A O   1 
ATOM   2609  C  CB  . LYS A 1 323  ? 19.779 41.510  20.954  1.00 9.13  ? 323  LYS A CB  1 
ATOM   2610  C  CG  . LYS A 1 323  ? 20.754 40.764  21.887  1.00 11.04 ? 323  LYS A CG  1 
ATOM   2611  C  CD  . LYS A 1 323  ? 20.070 39.838  22.885  1.00 11.65 ? 323  LYS A CD  1 
ATOM   2612  C  CE  . LYS A 1 323  ? 21.090 38.978  23.602  1.00 14.30 ? 323  LYS A CE  1 
ATOM   2613  N  NZ  . LYS A 1 323  ? 20.376 38.062  24.523  1.00 18.92 ? 323  LYS A NZ  1 
ATOM   2614  N  N   . LYS A 1 324  ? 19.046 43.814  18.714  1.00 8.93  ? 324  LYS A N   1 
ATOM   2615  C  CA  . LYS A 1 324  ? 18.363 44.293  17.514  1.00 8.14  ? 324  LYS A CA  1 
ATOM   2616  C  C   . LYS A 1 324  ? 19.347 44.575  16.362  1.00 8.53  ? 324  LYS A C   1 
ATOM   2617  O  O   . LYS A 1 324  ? 19.108 44.172  15.228  1.00 8.72  ? 324  LYS A O   1 
ATOM   2618  C  CB  . LYS A 1 324  ? 17.539 45.540  17.838  1.00 9.05  ? 324  LYS A CB  1 
ATOM   2619  C  CG  . LYS A 1 324  ? 16.288 45.201  18.654  1.00 9.94  ? 324  LYS A CG  1 
ATOM   2620  C  CD  . LYS A 1 324  ? 15.647 46.440  19.180  1.00 10.20 ? 324  LYS A CD  1 
ATOM   2621  C  CE  . LYS A 1 324  ? 14.399 46.045  19.987  1.00 12.31 ? 324  LYS A CE  1 
ATOM   2622  N  NZ  . LYS A 1 324  ? 13.824 47.177  20.757  1.00 12.94 ? 324  LYS A NZ  1 
ATOM   2623  N  N   . LYS A 1 325  ? 20.443 45.272  16.660  1.00 7.67  ? 325  LYS A N   1 
ATOM   2624  C  CA  . LYS A 1 325  ? 21.430 45.545  15.610  1.00 7.42  ? 325  LYS A CA  1 
ATOM   2625  C  C   . LYS A 1 325  ? 21.953 44.207  15.069  1.00 7.38  ? 325  LYS A C   1 
ATOM   2626  O  O   . LYS A 1 325  ? 22.109 44.036  13.840  1.00 7.66  ? 325  LYS A O   1 
ATOM   2627  C  CB  . LYS A 1 325  ? 22.583 46.379  16.154  1.00 7.95  ? 325  LYS A CB  1 
ATOM   2628  C  CG  . LYS A 1 325  ? 23.482 46.943  15.038  1.00 7.51  ? 325  LYS A CG  1 
ATOM   2629  C  CD  . LYS A 1 325  ? 24.607 47.774  15.632  1.00 8.12  ? 325  LYS A CD  1 
ATOM   2630  C  CE  . LYS A 1 325  ? 25.281 48.560  14.510  1.00 8.42  ? 325  LYS A CE  1 
ATOM   2631  N  NZ  . LYS A 1 325  ? 26.480 49.227  15.103  1.00 8.63  ? 325  LYS A NZ  1 
ATOM   2632  N  N   . ALA A 1 326  ? 22.177 43.228  15.954  1.00 8.17  ? 326  ALA A N   1 
ATOM   2633  C  CA  . ALA A 1 326  ? 22.727 41.954  15.524  1.00 8.18  ? 326  ALA A CA  1 
ATOM   2634  C  C   . ALA A 1 326  ? 21.794 41.195  14.587  1.00 8.71  ? 326  ALA A C   1 
ATOM   2635  O  O   . ALA A 1 326  ? 22.233 40.326  13.832  1.00 8.80  ? 326  ALA A O   1 
ATOM   2636  C  CB  . ALA A 1 326  ? 23.034 41.092  16.736  1.00 8.66  ? 326  ALA A CB  1 
ATOM   2637  N  N   . GLU A 1 327  ? 20.503 41.474  14.678  1.00 8.89  ? 327  GLU A N   1 
ATOM   2638  C  CA  . GLU A 1 327  ? 19.549 40.832  13.765  1.00 10.43 ? 327  GLU A CA  1 
ATOM   2639  C  C   . GLU A 1 327  ? 19.802 41.154  12.307  1.00 9.86  ? 327  GLU A C   1 
ATOM   2640  O  O   . GLU A 1 327  ? 19.347 40.429  11.396  1.00 11.48 ? 327  GLU A O   1 
ATOM   2641  C  CB  . GLU A 1 327  ? 18.134 41.270  14.085  1.00 11.65 ? 327  GLU A CB  1 
ATOM   2642  C  CG  . GLU A 1 327  ? 17.509 40.466  15.189  1.00 16.63 ? 327  GLU A CG  1 
ATOM   2643  C  CD  . GLU A 1 327  ? 17.513 38.966  14.897  1.00 18.02 ? 327  GLU A CD  1 
ATOM   2644  O  OE1 . GLU A 1 327  ? 16.865 38.504  13.936  1.00 20.81 ? 327  GLU A OE1 1 
ATOM   2645  O  OE2 . GLU A 1 327  ? 18.163 38.230  15.633  1.00 20.09 ? 327  GLU A OE2 1 
ATOM   2646  N  N   . LEU A 1 328  ? 20.545 42.234  12.055  1.00 8.82  ? 328  LEU A N   1 
ATOM   2647  C  CA  . LEU A 1 328  ? 20.744 42.691  10.690  1.00 9.28  ? 328  LEU A CA  1 
ATOM   2648  C  C   . LEU A 1 328  ? 21.958 42.039  10.053  1.00 8.98  ? 328  LEU A C   1 
ATOM   2649  O  O   . LEU A 1 328  ? 22.241 42.278  8.861   1.00 10.40 ? 328  LEU A O   1 
ATOM   2650  C  CB  . LEU A 1 328  ? 20.945 44.198  10.716  1.00 8.91  ? 328  LEU A CB  1 
ATOM   2651  C  CG  . LEU A 1 328  ? 19.829 45.002  11.371  1.00 9.44  ? 328  LEU A CG  1 
ATOM   2652  C  CD1 . LEU A 1 328  ? 20.072 46.524  11.241  1.00 8.47  ? 328  LEU A CD1 1 
ATOM   2653  C  CD2 . LEU A 1 328  ? 18.443 44.643  10.805  1.00 10.51 ? 328  LEU A CD2 1 
ATOM   2654  N  N   . TYR A 1 329  ? 22.681 41.227  10.810  1.00 8.07  ? 329  TYR A N   1 
ATOM   2655  C  CA  . TYR A 1 329  ? 23.923 40.619  10.326  1.00 7.24  ? 329  TYR A CA  1 
ATOM   2656  C  C   . TYR A 1 329  ? 23.930 39.130  10.534  1.00 9.43  ? 329  TYR A C   1 
ATOM   2657  O  O   . TYR A 1 329  ? 23.083 38.619  11.280  1.00 10.80 ? 329  TYR A O   1 
ATOM   2658  C  CB  . TYR A 1 329  ? 25.155 41.231  11.039  1.00 8.72  ? 329  TYR A CB  1 
ATOM   2659  C  CG  . TYR A 1 329  ? 25.343 42.700  10.689  1.00 7.00  ? 329  TYR A CG  1 
ATOM   2660  C  CD1 . TYR A 1 329  ? 26.096 43.078  9.612   1.00 8.50  ? 329  TYR A CD1 1 
ATOM   2661  C  CD2 . TYR A 1 329  ? 24.732 43.691  11.448  1.00 8.16  ? 329  TYR A CD2 1 
ATOM   2662  C  CE1 . TYR A 1 329  ? 26.232 44.428  9.258   1.00 7.70  ? 329  TYR A CE1 1 
ATOM   2663  C  CE2 . TYR A 1 329  ? 24.861 45.043  11.120  1.00 8.76  ? 329  TYR A CE2 1 
ATOM   2664  C  CZ  . TYR A 1 329  ? 25.613 45.396  10.011  1.00 8.56  ? 329  TYR A CZ  1 
ATOM   2665  O  OH  . TYR A 1 329  ? 25.741 46.753  9.674   1.00 10.01 ? 329  TYR A OH  1 
ATOM   2666  N  N   . ARG A 1 330  ? 24.875 38.439  9.919   1.00 9.07  ? 330  ARG A N   1 
ATOM   2667  C  CA  . ARG A 1 330  ? 24.796 36.985  9.830   1.00 8.75  ? 330  ARG A CA  1 
ATOM   2668  C  C   . ARG A 1 330  ? 25.562 36.217  10.876  1.00 10.36 ? 330  ARG A C   1 
ATOM   2669  O  O   . ARG A 1 330  ? 25.343 34.998  10.989  1.00 12.52 ? 330  ARG A O   1 
ATOM   2670  C  CB  . ARG A 1 330  ? 25.233 36.473  8.447   1.00 9.55  ? 330  ARG A CB  1 
ATOM   2671  C  CG  . ARG A 1 330  ? 24.308 36.908  7.356   1.00 9.67  ? 330  ARG A CG  1 
ATOM   2672  C  CD  . ARG A 1 330  ? 24.667 36.398  6.001   1.00 10.72 ? 330  ARG A CD  1 
ATOM   2673  N  NE  . ARG A 1 330  ? 23.700 36.934  5.056   1.00 11.61 ? 330  ARG A NE  1 
ATOM   2674  C  CZ  . ARG A 1 330  ? 23.344 36.385  3.896   1.00 13.06 ? 330  ARG A CZ  1 
ATOM   2675  N  NH1 . ARG A 1 330  ? 23.920 35.271  3.453   1.00 13.42 ? 330  ARG A NH1 1 
ATOM   2676  N  NH2 . ARG A 1 330  ? 22.433 37.011  3.155   1.00 13.42 ? 330  ARG A NH2 1 
ATOM   2677  N  N   . THR A 1 331  ? 26.518 36.845  11.553  1.00 10.02 ? 331  THR A N   1 
ATOM   2678  C  CA  . THR A 1 331  ? 27.313 36.101  12.549  1.00 9.95  ? 331  THR A CA  1 
ATOM   2679  C  C   . THR A 1 331  ? 26.924 36.508  13.959  1.00 9.99  ? 331  THR A C   1 
ATOM   2680  O  O   . THR A 1 331  ? 26.102 37.383  14.141  1.00 13.06 ? 331  THR A O   1 
ATOM   2681  C  CB  . THR A 1 331  ? 28.826 36.301  12.384  1.00 10.42 ? 331  THR A CB  1 
ATOM   2682  O  OG1 . THR A 1 331  ? 29.182 37.639  12.826  1.00 10.40 ? 331  THR A OG1 1 
ATOM   2683  C  CG2 . THR A 1 331  ? 29.288 36.141  10.873  1.00 11.45 ? 331  THR A CG2 1 
ATOM   2684  N  N   . ASN A 1 332  ? 27.557 35.858  14.938  1.00 10.40 ? 332  ASN A N   1 
ATOM   2685  C  CA  . ASN A 1 332  ? 27.344 36.230  16.328  1.00 10.30 ? 332  ASN A CA  1 
ATOM   2686  C  C   . ASN A 1 332  ? 28.411 37.178  16.844  1.00 10.35 ? 332  ASN A C   1 
ATOM   2687  O  O   . ASN A 1 332  ? 28.698 37.209  18.043  1.00 10.34 ? 332  ASN A O   1 
ATOM   2688  C  CB  . ASN A 1 332  ? 27.299 34.990  17.237  1.00 10.92 ? 332  ASN A CB  1 
ATOM   2689  C  CG  . ASN A 1 332  ? 28.642 34.272  17.337  1.00 14.14 ? 332  ASN A CG  1 
ATOM   2690  O  OD1 . ASN A 1 332  ? 29.429 34.248  16.410  1.00 14.41 ? 332  ASN A OD1 1 
ATOM   2691  N  ND2 . ASN A 1 332  ? 28.895 33.654  18.494  1.00 18.04 ? 332  ASN A ND2 1 
ATOM   2692  N  N   . VAL A 1 333  ? 28.996 37.971  15.942  1.00 9.11  ? 333  VAL A N   1 
ATOM   2693  C  CA  . VAL A 1 333  ? 30.020 38.938  16.314  1.00 9.17  ? 333  VAL A CA  1 
ATOM   2694  C  C   . VAL A 1 333  ? 29.468 40.282  15.880  1.00 7.99  ? 333  VAL A C   1 
ATOM   2695  O  O   . VAL A 1 333  ? 29.124 40.455  14.709  1.00 8.97  ? 333  VAL A O   1 
ATOM   2696  C  CB  . VAL A 1 333  ? 31.330 38.673  15.562  1.00 9.37  ? 333  VAL A CB  1 
ATOM   2697  C  CG1 . VAL A 1 333  ? 32.404 39.661  15.999  1.00 9.55  ? 333  VAL A CG1 1 
ATOM   2698  C  CG2 . VAL A 1 333  ? 31.798 37.240  15.802  1.00 10.83 ? 333  VAL A CG2 1 
ATOM   2699  N  N   . LEU A 1 334  ? 29.381 41.242  16.811  1.00 7.74  ? 334  LEU A N   1 
ATOM   2700  C  CA  . LEU A 1 334  ? 28.746 42.527  16.569  1.00 7.28  ? 334  LEU A CA  1 
ATOM   2701  C  C   . LEU A 1 334  ? 29.733 43.683  16.716  1.00 6.12  ? 334  LEU A C   1 
ATOM   2702  O  O   . LEU A 1 334  ? 30.427 43.805  17.725  1.00 7.39  ? 334  LEU A O   1 
ATOM   2703  C  CB  . LEU A 1 334  ? 27.594 42.720  17.569  1.00 6.68  ? 334  LEU A CB  1 
ATOM   2704  C  CG  . LEU A 1 334  ? 26.742 43.969  17.359  1.00 8.03  ? 334  LEU A CG  1 
ATOM   2705  C  CD1 . LEU A 1 334  ? 25.984 43.898  16.048  1.00 7.83  ? 334  LEU A CD1 1 
ATOM   2706  C  CD2 . LEU A 1 334  ? 25.778 44.089  18.522  1.00 8.31  ? 334  LEU A CD2 1 
ATOM   2707  N  N   . LEU A 1 335  ? 29.725 44.588  15.725  1.00 6.64  ? 335  LEU A N   1 
ATOM   2708  C  CA  . LEU A 1 335  ? 30.531 45.805  15.777  1.00 6.11  ? 335  LEU A CA  1 
ATOM   2709  C  C   . LEU A 1 335  ? 29.722 46.971  16.314  1.00 5.44  ? 335  LEU A C   1 
ATOM   2710  O  O   . LEU A 1 335  ? 28.691 47.309  15.740  1.00 6.66  ? 335  LEU A O   1 
ATOM   2711  C  CB  . LEU A 1 335  ? 31.012 46.136  14.348  1.00 7.30  ? 335  LEU A CB  1 
ATOM   2712  C  CG  . LEU A 1 335  ? 31.886 47.362  14.241  1.00 6.26  ? 335  LEU A CG  1 
ATOM   2713  C  CD1 . LEU A 1 335  ? 33.204 47.204  14.959  1.00 9.67  ? 335  LEU A CD1 1 
ATOM   2714  C  CD2 . LEU A 1 335  ? 32.129 47.717  12.796  1.00 10.10 ? 335  LEU A CD2 1 
ATOM   2715  N  N   . ILE A 1 336  ? 30.221 47.606  17.389  1.00 5.48  ? 336  ILE A N   1 
ATOM   2716  C  CA  . ILE A 1 336  ? 29.624 48.811  17.954  1.00 6.15  ? 336  ILE A CA  1 
ATOM   2717  C  C   . ILE A 1 336  ? 30.664 49.928  17.983  1.00 5.51  ? 336  ILE A C   1 
ATOM   2718  O  O   . ILE A 1 336  ? 31.428 50.052  18.928  1.00 6.97  ? 336  ILE A O   1 
ATOM   2719  C  CB  . ILE A 1 336  ? 29.084 48.549  19.376  1.00 6.95  ? 336  ILE A CB  1 
ATOM   2720  C  CG1 . ILE A 1 336  ? 28.068 47.390  19.393  1.00 7.16  ? 336  ILE A CG1 1 
ATOM   2721  C  CG2 . ILE A 1 336  ? 28.519 49.841  19.942  1.00 7.45  ? 336  ILE A CG2 1 
ATOM   2722  C  CD1 . ILE A 1 336  ? 26.805 47.641  18.648  1.00 8.10  ? 336  ILE A CD1 1 
ATOM   2723  N  N   . PRO A 1 337  ? 30.707 50.749  16.942  1.00 6.08  ? 337  PRO A N   1 
ATOM   2724  C  CA  . PRO A 1 337  ? 31.572 51.930  17.012  1.00 6.66  ? 337  PRO A CA  1 
ATOM   2725  C  C   . PRO A 1 337  ? 31.186 52.845  18.180  1.00 7.06  ? 337  PRO A C   1 
ATOM   2726  O  O   . PRO A 1 337  ? 29.976 52.972  18.471  1.00 8.12  ? 337  PRO A O   1 
ATOM   2727  C  CB  . PRO A 1 337  ? 31.330 52.610  15.658  1.00 7.25  ? 337  PRO A CB  1 
ATOM   2728  C  CG  . PRO A 1 337  ? 30.901 51.465  14.781  1.00 7.58  ? 337  PRO A CG  1 
ATOM   2729  C  CD  . PRO A 1 337  ? 29.972 50.672  15.662  1.00 7.44  ? 337  PRO A CD  1 
ATOM   2730  N  N   . LEU A 1 338  ? 32.175 53.473  18.817  1.00 5.68  ? 338  LEU A N   1 
ATOM   2731  C  CA  . LEU A 1 338  ? 31.887 54.399  19.921  1.00 5.66  ? 338  LEU A CA  1 
ATOM   2732  C  C   . LEU A 1 338  ? 32.700 55.672  19.697  1.00 6.11  ? 338  LEU A C   1 
ATOM   2733  O  O   . LEU A 1 338  ? 33.843 55.779  20.117  1.00 5.79  ? 338  LEU A O   1 
ATOM   2734  C  CB  . LEU A 1 338  ? 32.227 53.746  21.281  1.00 6.12  ? 338  LEU A CB  1 
ATOM   2735  C  CG  . LEU A 1 338  ? 31.873 54.618  22.486  1.00 7.80  ? 338  LEU A CG  1 
ATOM   2736  C  CD1 . LEU A 1 338  ? 30.386 54.447  22.748  1.00 8.76  ? 338  LEU A CD1 1 
ATOM   2737  C  CD2 . LEU A 1 338  ? 32.645 54.111  23.704  1.00 9.10  ? 338  LEU A CD2 1 
ATOM   2738  N  N   . GLY A 1 339  ? 32.094 56.639  19.029  1.00 6.76  ? 339  GLY A N   1 
ATOM   2739  C  CA  . GLY A 1 339  ? 32.849 57.858  18.739  1.00 7.16  ? 339  GLY A CA  1 
ATOM   2740  C  C   . GLY A 1 339  ? 32.015 58.845  17.956  1.00 6.69  ? 339  GLY A C   1 
ATOM   2741  O  O   . GLY A 1 339  ? 30.848 58.594  17.669  1.00 7.50  ? 339  GLY A O   1 
ATOM   2742  N  N   . ASP A 1 340  ? 32.649 59.956  17.553  1.00 6.26  ? 340  ASP A N   1 
ATOM   2743  C  CA  . ASP A 1 340  ? 32.023 61.045  16.847  1.00 6.62  ? 340  ASP A CA  1 
ATOM   2744  C  C   . ASP A 1 340  ? 33.207 61.984  16.519  1.00 6.03  ? 340  ASP A C   1 
ATOM   2745  O  O   . ASP A 1 340  ? 34.388 61.671  16.716  1.00 6.61  ? 340  ASP A O   1 
ATOM   2746  C  CB  . ASP A 1 340  ? 30.973 61.698  17.777  1.00 6.88  ? 340  ASP A CB  1 
ATOM   2747  C  CG  . ASP A 1 340  ? 29.890 62.472  17.055  1.00 8.82  ? 340  ASP A CG  1 
ATOM   2748  O  OD1 . ASP A 1 340  ? 30.075 62.827  15.849  1.00 10.11 ? 340  ASP A OD1 1 
ATOM   2749  O  OD2 . ASP A 1 340  ? 28.834 62.782  17.704  1.00 9.71  ? 340  ASP A OD2 1 
ATOM   2750  N  N   . ASP A 1 341  ? 32.835 63.129  15.971  1.00 6.70  ? 341  ASP A N   1 
ATOM   2751  C  CA  . ASP A 1 341  ? 33.799 64.105  15.465  1.00 6.34  ? 341  ASP A CA  1 
ATOM   2752  C  C   . ASP A 1 341  ? 34.673 64.662  16.577  1.00 6.66  ? 341  ASP A C   1 
ATOM   2753  O  O   . ASP A 1 341  ? 34.165 65.168  17.587  1.00 7.00  ? 341  ASP A O   1 
ATOM   2754  C  CB  . ASP A 1 341  ? 33.107 65.271  14.784  1.00 8.13  ? 341  ASP A CB  1 
ATOM   2755  C  CG  . ASP A 1 341  ? 32.492 64.906  13.468  1.00 10.28 ? 341  ASP A CG  1 
ATOM   2756  O  OD1 . ASP A 1 341  ? 32.458 63.738  13.068  1.00 9.97  ? 341  ASP A OD1 1 
ATOM   2757  O  OD2 . ASP A 1 341  ? 32.081 65.807  12.715  1.00 13.90 ? 341  ASP A OD2 1 
ATOM   2758  N  N   . PHE A 1 342  ? 35.981 64.587  16.389  1.00 6.13  ? 342  PHE A N   1 
ATOM   2759  C  CA  . PHE A 1 342  ? 36.932 65.141  17.345  1.00 6.42  ? 342  PHE A CA  1 
ATOM   2760  C  C   . PHE A 1 342  ? 36.632 64.732  18.795  1.00 6.46  ? 342  PHE A C   1 
ATOM   2761  O  O   . PHE A 1 342  ? 36.848 65.505  19.753  1.00 8.83  ? 342  PHE A O   1 
ATOM   2762  C  CB  . PHE A 1 342  ? 37.057 66.667  17.160  1.00 7.25  ? 342  PHE A CB  1 
ATOM   2763  C  CG  . PHE A 1 342  ? 37.673 67.049  15.842  1.00 6.85  ? 342  PHE A CG  1 
ATOM   2764  C  CD1 . PHE A 1 342  ? 39.041 66.977  15.647  1.00 6.56  ? 342  PHE A CD1 1 
ATOM   2765  C  CD2 . PHE A 1 342  ? 36.863 67.465  14.785  1.00 7.73  ? 342  PHE A CD2 1 
ATOM   2766  C  CE1 . PHE A 1 342  ? 39.586 67.329  14.423  1.00 7.18  ? 342  PHE A CE1 1 
ATOM   2767  C  CE2 . PHE A 1 342  ? 37.417 67.800  13.538  1.00 7.57  ? 342  PHE A CE2 1 
ATOM   2768  C  CZ  . PHE A 1 342  ? 38.769 67.728  13.377  1.00 7.23  ? 342  PHE A CZ  1 
ATOM   2769  N  N   . ARG A 1 343  ? 36.229 63.476  18.957  1.00 6.57  ? 343  ARG A N   1 
ATOM   2770  C  CA  . ARG A 1 343  ? 36.000 62.956  20.308  1.00 6.87  ? 343  ARG A CA  1 
ATOM   2771  C  C   . ARG A 1 343  ? 37.293 62.495  20.972  1.00 8.08  ? 343  ARG A C   1 
ATOM   2772  O  O   . ARG A 1 343  ? 38.362 62.401  20.367  1.00 7.37  ? 343  ARG A O   1 
ATOM   2773  C  CB  . ARG A 1 343  ? 35.000 61.810  20.246  1.00 6.58  ? 343  ARG A CB  1 
ATOM   2774  C  CG  . ARG A 1 343  ? 33.570 62.285  20.023  1.00 7.01  ? 343  ARG A CG  1 
ATOM   2775  C  CD  . ARG A 1 343  ? 33.085 63.200  21.124  1.00 7.01  ? 343  ARG A CD  1 
ATOM   2776  N  NE  . ARG A 1 343  ? 31.641 63.452  21.025  1.00 7.47  ? 343  ARG A NE  1 
ATOM   2777  C  CZ  . ARG A 1 343  ? 30.723 62.747  21.671  1.00 7.46  ? 343  ARG A CZ  1 
ATOM   2778  N  NH1 . ARG A 1 343  ? 31.069 61.692  22.419  1.00 6.73  ? 343  ARG A NH1 1 
ATOM   2779  N  NH2 . ARG A 1 343  ? 29.447 63.101  21.535  1.00 7.66  ? 343  ARG A NH2 1 
ATOM   2780  N  N   . PHE A 1 344  ? 37.183 62.223  22.274  1.00 8.20  ? 344  PHE A N   1 
ATOM   2781  C  CA  . PHE A 1 344  ? 38.314 61.712  23.091  1.00 8.66  ? 344  PHE A CA  1 
ATOM   2782  C  C   . PHE A 1 344  ? 39.401 62.747  23.227  1.00 9.82  ? 344  PHE A C   1 
ATOM   2783  O  O   . PHE A 1 344  ? 40.580 62.449  23.167  1.00 10.89 ? 344  PHE A O   1 
ATOM   2784  C  CB  . PHE A 1 344  ? 38.745 60.333  22.577  1.00 9.65  ? 344  PHE A CB  1 
ATOM   2785  C  CG  . PHE A 1 344  ? 37.699 59.304  22.783  1.00 8.20  ? 344  PHE A CG  1 
ATOM   2786  C  CD1 . PHE A 1 344  ? 37.486 58.771  24.062  1.00 10.00 ? 344  PHE A CD1 1 
ATOM   2787  C  CD2 . PHE A 1 344  ? 36.883 58.895  21.743  1.00 9.60  ? 344  PHE A CD2 1 
ATOM   2788  C  CE1 . PHE A 1 344  ? 36.492 57.823  24.267  1.00 11.17 ? 344  PHE A CE1 1 
ATOM   2789  C  CE2 . PHE A 1 344  ? 35.886 57.970  21.940  1.00 9.27  ? 344  PHE A CE2 1 
ATOM   2790  C  CZ  . PHE A 1 344  ? 35.695 57.437  23.215  1.00 10.18 ? 344  PHE A CZ  1 
ATOM   2791  N  N   A LYS A 1 345  ? 38.958 63.978  23.415  0.50 10.66 ? 345  LYS A N   1 
ATOM   2792  N  N   B LYS A 1 345  ? 38.990 63.985  23.484  0.50 10.84 ? 345  LYS A N   1 
ATOM   2793  C  CA  A LYS A 1 345  ? 39.833 65.098  23.649  0.50 11.31 ? 345  LYS A CA  1 
ATOM   2794  C  CA  B LYS A 1 345  ? 39.900 65.126  23.545  0.50 11.86 ? 345  LYS A CA  1 
ATOM   2795  C  C   A LYS A 1 345  ? 40.117 65.147  25.166  0.50 11.21 ? 345  LYS A C   1 
ATOM   2796  C  C   B LYS A 1 345  ? 40.400 65.452  24.927  0.50 12.07 ? 345  LYS A C   1 
ATOM   2797  O  O   A LYS A 1 345  ? 41.171 64.681  25.614  0.50 10.90 ? 345  LYS A O   1 
ATOM   2798  O  O   B LYS A 1 345  ? 41.537 65.864  25.112  0.50 11.49 ? 345  LYS A O   1 
ATOM   2799  C  CB  . LYS A 1 345  ? 39.202 66.379  23.061  1.00 12.46 ? 345  LYS A CB  1 
ATOM   2800  C  CG  . LYS A 1 345  ? 40.096 67.607  23.063  1.00 14.25 ? 345  LYS A CG  1 
ATOM   2801  C  CD  . LYS A 1 345  ? 39.309 68.810  22.596  1.00 18.45 ? 345  LYS A CD  1 
ATOM   2802  C  CE  . LYS A 1 345  ? 40.034 70.095  22.840  1.00 21.93 ? 345  LYS A CE  1 
ATOM   2803  N  NZ  . LYS A 1 345  ? 39.268 71.199  22.186  1.00 24.07 ? 345  LYS A NZ  1 
ATOM   2804  N  N   A GLN A 1 346  ? 39.146 65.632  25.941  0.50 11.28 ? 346  GLN A N   1 
ATOM   2805  N  N   B GLN A 1 346  ? 39.499 65.337  25.882  0.50 13.01 ? 346  GLN A N   1 
ATOM   2806  C  CA  A GLN A 1 346  ? 39.331 65.830  27.391  0.50 11.17 ? 346  GLN A CA  1 
ATOM   2807  C  CA  B GLN A 1 346  ? 39.799 65.750  27.229  0.50 13.29 ? 346  GLN A CA  1 
ATOM   2808  C  C   A GLN A 1 346  ? 39.719 64.547  28.162  0.50 11.86 ? 346  GLN A C   1 
ATOM   2809  C  C   B GLN A 1 346  ? 39.828 64.539  28.101  0.50 13.15 ? 346  GLN A C   1 
ATOM   2810  O  O   A GLN A 1 346  ? 39.150 63.492  27.899  0.50 10.57 ? 346  GLN A O   1 
ATOM   2811  O  O   B GLN A 1 346  ? 39.102 63.570  27.886  0.50 11.80 ? 346  GLN A O   1 
ATOM   2812  C  CB  A GLN A 1 346  ? 38.038 66.425  27.972  0.50 11.27 ? 346  GLN A CB  1 
ATOM   2813  C  CB  B GLN A 1 346  ? 38.737 66.706  27.738  0.50 14.46 ? 346  GLN A CB  1 
ATOM   2814  C  CG  A GLN A 1 346  ? 37.642 67.758  27.343  0.50 11.06 ? 346  GLN A CG  1 
ATOM   2815  C  CG  B GLN A 1 346  ? 39.013 68.146  27.441  0.50 16.47 ? 346  GLN A CG  1 
ATOM   2816  C  CD  A GLN A 1 346  ? 36.565 67.637  26.273  0.50 12.94 ? 346  GLN A CD  1 
ATOM   2817  C  CD  B GLN A 1 346  ? 38.022 69.054  28.125  0.50 19.35 ? 346  GLN A CD  1 
ATOM   2818  O  OE1 A GLN A 1 346  ? 36.368 66.577  25.671  0.50 8.43  ? 346  GLN A OE1 1 
ATOM   2819  O  OE1 B GLN A 1 346  ? 38.398 69.857  28.984  0.50 22.39 ? 346  GLN A OE1 1 
ATOM   2820  N  NE2 A GLN A 1 346  ? 35.840 68.716  26.062  0.50 14.33 ? 346  GLN A NE2 1 
ATOM   2821  N  NE2 B GLN A 1 346  ? 36.751 68.929  27.757  0.50 20.65 ? 346  GLN A NE2 1 
ATOM   2822  N  N   . ASN A 1 347  ? 40.668 64.619  29.116  1.00 12.84 ? 347  ASN A N   1 
ATOM   2823  C  CA  . ASN A 1 347  ? 40.865 63.527  30.060  1.00 12.58 ? 347  ASN A CA  1 
ATOM   2824  C  C   . ASN A 1 347  ? 39.575 63.087  30.719  1.00 11.77 ? 347  ASN A C   1 
ATOM   2825  O  O   . ASN A 1 347  ? 39.333 61.879  30.844  1.00 11.19 ? 347  ASN A O   1 
ATOM   2826  C  CB  . ASN A 1 347  ? 41.839 63.947  31.160  1.00 13.50 ? 347  ASN A CB  1 
ATOM   2827  C  CG  . ASN A 1 347  ? 43.216 64.095  30.642  1.00 16.98 ? 347  ASN A CG  1 
ATOM   2828  O  OD1 . ASN A 1 347  ? 43.688 63.245  29.897  1.00 19.47 ? 347  ASN A OD1 1 
ATOM   2829  N  ND2 . ASN A 1 347  ? 43.879 65.203  31.002  1.00 22.23 ? 347  ASN A ND2 1 
ATOM   2830  N  N   . THR A 1 348  ? 38.739 64.052  31.090  1.00 11.22 ? 348  THR A N   1 
ATOM   2831  C  CA  . THR A 1 348  ? 37.468 63.735  31.734  1.00 12.03 ? 348  THR A CA  1 
ATOM   2832  C  C   . THR A 1 348  ? 36.547 62.974  30.800  1.00 12.17 ? 348  THR A C   1 
ATOM   2833  O  O   . THR A 1 348  ? 35.735 62.186  31.261  1.00 10.99 ? 348  THR A O   1 
ATOM   2834  C  CB  . THR A 1 348  ? 36.760 64.993  32.251  1.00 13.33 ? 348  THR A CB  1 
ATOM   2835  O  OG1 . THR A 1 348  ? 36.719 65.969  31.212  1.00 15.34 ? 348  THR A OG1 1 
ATOM   2836  C  CG2 . THR A 1 348  ? 37.606 65.640  33.351  1.00 13.89 ? 348  THR A CG2 1 
ATOM   2837  N  N   . GLU A 1 349  ? 36.673 63.205  29.488  1.00 9.25  ? 349  GLU A N   1 
ATOM   2838  C  CA  . GLU A 1 349  ? 35.863 62.489  28.510  1.00 9.23  ? 349  GLU A CA  1 
ATOM   2839  C  C   . GLU A 1 349  ? 36.347 61.041  28.370  1.00 8.09  ? 349  GLU A C   1 
ATOM   2840  O  O   . GLU A 1 349  ? 35.550 60.113  28.346  1.00 8.32  ? 349  GLU A O   1 
ATOM   2841  C  CB  . GLU A 1 349  ? 35.971 63.192  27.150  1.00 8.84  ? 349  GLU A CB  1 
ATOM   2842  C  CG  . GLU A 1 349  ? 35.254 62.424  26.072  1.00 11.20 ? 349  GLU A CG  1 
ATOM   2843  C  CD  . GLU A 1 349  ? 35.470 63.017  24.687  1.00 10.35 ? 349  GLU A CD  1 
ATOM   2844  O  OE1 . GLU A 1 349  ? 36.156 64.049  24.534  1.00 11.70 ? 349  GLU A OE1 1 
ATOM   2845  O  OE2 . GLU A 1 349  ? 34.932 62.408  23.763  1.00 10.79 ? 349  GLU A OE2 1 
ATOM   2846  N  N   . TRP A 1 350  ? 37.657 60.835  28.311  1.00 8.89  ? 350  TRP A N   1 
ATOM   2847  C  CA  . TRP A 1 350  ? 38.170 59.461  28.343  1.00 9.55  ? 350  TRP A CA  1 
ATOM   2848  C  C   . TRP A 1 350  ? 37.622 58.697  29.545  1.00 9.56  ? 350  TRP A C   1 
ATOM   2849  O  O   . TRP A 1 350  ? 37.123 57.600  29.436  1.00 9.70  ? 350  TRP A O   1 
ATOM   2850  C  CB  . TRP A 1 350  ? 39.691 59.425  28.381  1.00 9.00  ? 350  TRP A CB  1 
ATOM   2851  C  CG  . TRP A 1 350  ? 40.321 59.658  27.015  1.00 8.62  ? 350  TRP A CG  1 
ATOM   2852  C  CD1 . TRP A 1 350  ? 40.657 60.860  26.461  1.00 9.02  ? 350  TRP A CD1 1 
ATOM   2853  C  CD2 . TRP A 1 350  ? 40.620 58.654  26.038  1.00 8.69  ? 350  TRP A CD2 1 
ATOM   2854  N  NE1 . TRP A 1 350  ? 41.197 60.655  25.209  1.00 8.77  ? 350  TRP A NE1 1 
ATOM   2855  C  CE2 . TRP A 1 350  ? 41.177 59.318  24.921  1.00 8.52  ? 350  TRP A CE2 1 
ATOM   2856  C  CE3 . TRP A 1 350  ? 40.511 57.270  26.006  1.00 12.68 ? 350  TRP A CE3 1 
ATOM   2857  C  CZ2 . TRP A 1 350  ? 41.588 58.639  23.781  1.00 12.91 ? 350  TRP A CZ2 1 
ATOM   2858  C  CZ3 . TRP A 1 350  ? 40.933 56.600  24.865  1.00 13.17 ? 350  TRP A CZ3 1 
ATOM   2859  C  CH2 . TRP A 1 350  ? 41.446 57.289  23.772  1.00 12.47 ? 350  TRP A CH2 1 
ATOM   2860  N  N   . ASP A 1 351  ? 37.672 59.335  30.709  1.00 10.27 ? 351  ASP A N   1 
ATOM   2861  C  CA  . ASP A 1 351  ? 37.213 58.660  31.918  1.00 10.94 ? 351  ASP A CA  1 
ATOM   2862  C  C   . ASP A 1 351  ? 35.731 58.388  31.895  1.00 10.69 ? 351  ASP A C   1 
ATOM   2863  O  O   . ASP A 1 351  ? 35.311 57.289  32.280  1.00 10.53 ? 351  ASP A O   1 
ATOM   2864  C  CB  . ASP A 1 351  ? 37.493 59.497  33.160  1.00 12.27 ? 351  ASP A CB  1 
ATOM   2865  C  CG  . ASP A 1 351  ? 38.956 59.585  33.511  1.00 17.82 ? 351  ASP A CG  1 
ATOM   2866  O  OD1 . ASP A 1 351  ? 39.736 58.688  33.149  1.00 20.69 ? 351  ASP A OD1 1 
ATOM   2867  O  OD2 . ASP A 1 351  ? 39.416 60.530  34.205  1.00 24.65 ? 351  ASP A OD2 1 
ATOM   2868  N  N   . VAL A 1 352  ? 34.931 59.368  31.474  1.00 10.21 ? 352  VAL A N   1 
ATOM   2869  C  CA  . VAL A 1 352  ? 33.509 59.193  31.578  1.00 11.22 ? 352  VAL A CA  1 
ATOM   2870  C  C   . VAL A 1 352  ? 33.049 58.070  30.626  1.00 10.73 ? 352  VAL A C   1 
ATOM   2871  O  O   . VAL A 1 352  ? 32.172 57.261  30.980  1.00 12.14 ? 352  VAL A O   1 
ATOM   2872  C  CB  . VAL A 1 352  ? 32.733 60.528  31.420  1.00 12.91 ? 352  VAL A CB  1 
ATOM   2873  C  CG1 . VAL A 1 352  ? 32.646 60.944  29.978  1.00 13.43 ? 352  VAL A CG1 1 
ATOM   2874  C  CG2 . VAL A 1 352  ? 31.363 60.453  32.057  1.00 15.53 ? 352  VAL A CG2 1 
ATOM   2875  N  N   . GLN A 1 353  ? 33.662 57.945  29.447  1.00 9.64  ? 353  GLN A N   1 
ATOM   2876  C  CA  . GLN A 1 353  ? 33.245 56.884  28.539  1.00 9.11  ? 353  GLN A CA  1 
ATOM   2877  C  C   . GLN A 1 353  ? 33.779 55.539  29.020  1.00 9.08  ? 353  GLN A C   1 
ATOM   2878  O  O   . GLN A 1 353  ? 33.016 54.578  29.115  1.00 9.65  ? 353  GLN A O   1 
ATOM   2879  C  CB  . GLN A 1 353  ? 33.740 57.167  27.103  1.00 8.21  ? 353  GLN A CB  1 
ATOM   2880  C  CG  . GLN A 1 353  ? 33.196 58.473  26.456  1.00 9.91  ? 353  GLN A CG  1 
ATOM   2881  C  CD  . GLN A 1 353  ? 31.743 58.390  25.997  1.00 9.85  ? 353  GLN A CD  1 
ATOM   2882  O  OE1 . GLN A 1 353  ? 30.927 57.652  26.561  1.00 8.41  ? 353  GLN A OE1 1 
ATOM   2883  N  NE2 . GLN A 1 353  ? 31.403 59.147  24.969  1.00 8.48  ? 353  GLN A NE2 1 
ATOM   2884  N  N   . ARG A 1 354  ? 35.066 55.472  29.355  1.00 8.44  ? 354  ARG A N   1 
ATOM   2885  C  CA  . ARG A 1 354  ? 35.644 54.194  29.782  1.00 9.12  ? 354  ARG A CA  1 
ATOM   2886  C  C   . ARG A 1 354  ? 35.005 53.637  31.044  1.00 9.97  ? 354  ARG A C   1 
ATOM   2887  O  O   . ARG A 1 354  ? 34.673 52.465  31.092  1.00 10.47 ? 354  ARG A O   1 
ATOM   2888  C  CB  . ARG A 1 354  ? 37.137 54.329  30.008  1.00 10.02 ? 354  ARG A CB  1 
ATOM   2889  C  CG  . ARG A 1 354  ? 37.797 53.037  30.455  1.00 10.11 ? 354  ARG A CG  1 
ATOM   2890  C  CD  . ARG A 1 354  ? 39.289 53.191  30.756  1.00 11.53 ? 354  ARG A CD  1 
ATOM   2891  N  NE  . ARG A 1 354  ? 39.536 54.266  31.718  1.00 12.74 ? 354  ARG A NE  1 
ATOM   2892  C  CZ  . ARG A 1 354  ? 39.432 54.166  33.047  1.00 13.95 ? 354  ARG A CZ  1 
ATOM   2893  N  NH1 . ARG A 1 354  ? 39.098 53.015  33.611  1.00 14.98 ? 354  ARG A NH1 1 
ATOM   2894  N  NH2 . ARG A 1 354  ? 39.696 55.212  33.806  1.00 16.27 ? 354  ARG A NH2 1 
ATOM   2895  N  N   . VAL A 1 355  ? 34.875 54.449  32.089  1.00 8.62  ? 355  VAL A N   1 
ATOM   2896  C  CA  . VAL A 1 355  ? 34.436 53.866  33.357  1.00 10.35 ? 355  VAL A CA  1 
ATOM   2897  C  C   . VAL A 1 355  ? 32.998 53.391  33.248  1.00 9.65  ? 355  VAL A C   1 
ATOM   2898  O  O   . VAL A 1 355  ? 32.655 52.319  33.787  1.00 10.69 ? 355  VAL A O   1 
ATOM   2899  C  CB  . VAL A 1 355  ? 34.641 54.866  34.513  1.00 10.62 ? 355  VAL A CB  1 
ATOM   2900  C  CG1 . VAL A 1 355  ? 34.022 54.371  35.844  1.00 15.02 ? 355  VAL A CG1 1 
ATOM   2901  C  CG2 . VAL A 1 355  ? 36.107 55.162  34.721  1.00 12.78 ? 355  VAL A CG2 1 
ATOM   2902  N  N   . ASN A 1 356  ? 32.134 54.173  32.601  1.00 8.31  ? 356  ASN A N   1 
ATOM   2903  C  CA  . ASN A 1 356  ? 30.750 53.769  32.452  1.00 8.92  ? 356  ASN A CA  1 
ATOM   2904  C  C   . ASN A 1 356  ? 30.618 52.491  31.621  1.00 9.71  ? 356  ASN A C   1 
ATOM   2905  O  O   . ASN A 1 356  ? 29.902 51.554  32.002  1.00 9.73  ? 356  ASN A O   1 
ATOM   2906  C  CB  . ASN A 1 356  ? 29.886 54.912  31.977  1.00 8.59  ? 356  ASN A CB  1 
ATOM   2907  C  CG  . ASN A 1 356  ? 29.664 55.920  33.048  1.00 10.58 ? 356  ASN A CG  1 
ATOM   2908  O  OD1 . ASN A 1 356  ? 28.973 55.617  34.026  1.00 12.16 ? 356  ASN A OD1 1 
ATOM   2909  N  ND2 . ASN A 1 356  ? 30.243 57.101  32.918  1.00 11.22 ? 356  ASN A ND2 1 
ATOM   2910  N  N   . TYR A 1 357  ? 31.336 52.427  30.496  1.00 8.65  ? 357  TYR A N   1 
ATOM   2911  C  CA  . TYR A 1 357  ? 31.339 51.179  29.721  1.00 8.82  ? 357  TYR A CA  1 
ATOM   2912  C  C   . TYR A 1 357  ? 31.920 49.976  30.483  1.00 8.79  ? 357  TYR A C   1 
ATOM   2913  O  O   . TYR A 1 357  ? 31.380 48.860  30.377  1.00 9.86  ? 357  TYR A O   1 
ATOM   2914  C  CB  . TYR A 1 357  ? 31.982 51.357  28.296  1.00 8.35  ? 357  TYR A CB  1 
ATOM   2915  C  CG  . TYR A 1 357  ? 30.960 51.872  27.320  1.00 7.37  ? 357  TYR A CG  1 
ATOM   2916  C  CD1 . TYR A 1 357  ? 30.133 50.986  26.626  1.00 8.87  ? 357  TYR A CD1 1 
ATOM   2917  C  CD2 . TYR A 1 357  ? 30.763 53.247  27.126  1.00 7.16  ? 357  TYR A CD2 1 
ATOM   2918  C  CE1 . TYR A 1 357  ? 29.131 51.460  25.732  1.00 8.56  ? 357  TYR A CE1 1 
ATOM   2919  C  CE2 . TYR A 1 357  ? 29.758 53.733  26.264  1.00 6.69  ? 357  TYR A CE2 1 
ATOM   2920  C  CZ  . TYR A 1 357  ? 28.944 52.846  25.570  1.00 8.55  ? 357  TYR A CZ  1 
ATOM   2921  O  OH  . TYR A 1 357  ? 27.953 53.267  24.730  1.00 9.81  ? 357  TYR A OH  1 
ATOM   2922  N  N   . GLU A 1 358  ? 33.003 50.182  31.235  1.00 9.57  ? 358  GLU A N   1 
ATOM   2923  C  CA  . GLU A 1 358  ? 33.566 49.084  32.042  1.00 10.34 ? 358  GLU A CA  1 
ATOM   2924  C  C   . GLU A 1 358  ? 32.527 48.553  33.016  1.00 10.54 ? 358  GLU A C   1 
ATOM   2925  O  O   . GLU A 1 358  ? 32.425 47.330  33.187  1.00 10.46 ? 358  GLU A O   1 
ATOM   2926  C  CB  . GLU A 1 358  ? 34.785 49.555  32.806  1.00 10.85 ? 358  GLU A CB  1 
ATOM   2927  C  CG  . GLU A 1 358  ? 36.062 49.700  31.988  1.00 14.66 ? 358  GLU A CG  1 
ATOM   2928  C  CD  . GLU A 1 358  ? 37.247 50.110  32.876  1.00 13.98 ? 358  GLU A CD  1 
ATOM   2929  O  OE1 . GLU A 1 358  ? 37.152 50.000  34.136  1.00 22.15 ? 358  GLU A OE1 1 
ATOM   2930  O  OE2 . GLU A 1 358  ? 38.312 50.505  32.359  1.00 19.28 ? 358  GLU A OE2 1 
ATOM   2931  N  N   . ARG A 1 359  ? 31.742 49.437  33.636  1.00 9.69  ? 359  ARG A N   1 
ATOM   2932  C  CA  . ARG A 1 359  ? 30.718 48.938  34.566  1.00 10.54 ? 359  ARG A CA  1 
ATOM   2933  C  C   . ARG A 1 359  ? 29.649 48.163  33.824  1.00 10.22 ? 359  ARG A C   1 
ATOM   2934  O  O   . ARG A 1 359  ? 29.176 47.121  34.309  1.00 10.73 ? 359  ARG A O   1 
ATOM   2935  C  CB  . ARG A 1 359  ? 30.060 50.081  35.318  1.00 10.78 ? 359  ARG A CB  1 
ATOM   2936  C  CG  . ARG A 1 359  ? 30.946 50.803  36.290  1.00 14.52 ? 359  ARG A CG  1 
ATOM   2937  C  CD  . ARG A 1 359  ? 30.217 51.999  36.868  1.00 19.23 ? 359  ARG A CD  1 
ATOM   2938  N  NE  . ARG A 1 359  ? 31.082 52.863  37.662  1.00 22.77 ? 359  ARG A NE  1 
ATOM   2939  C  CZ  . ARG A 1 359  ? 31.134 54.188  37.525  1.00 25.09 ? 359  ARG A CZ  1 
ATOM   2940  N  NH1 . ARG A 1 359  ? 30.358 54.831  36.623  1.00 22.30 ? 359  ARG A NH1 1 
ATOM   2941  N  NH2 . ARG A 1 359  ? 31.962 54.878  38.306  1.00 28.00 ? 359  ARG A NH2 1 
ATOM   2942  N  N   . LEU A 1 360  ? 29.220 48.639  32.652  1.00 9.46  ? 360  LEU A N   1 
ATOM   2943  C  CA  . LEU A 1 360  ? 28.280 47.862  31.839  1.00 8.99  ? 360  LEU A CA  1 
ATOM   2944  C  C   . LEU A 1 360  ? 28.835 46.481  31.451  1.00 9.61  ? 360  LEU A C   1 
ATOM   2945  O  O   . LEU A 1 360  ? 28.131 45.470  31.579  1.00 10.61 ? 360  LEU A O   1 
ATOM   2946  C  CB  . LEU A 1 360  ? 27.881 48.657  30.587  1.00 9.59  ? 360  LEU A CB  1 
ATOM   2947  C  CG  . LEU A 1 360  ? 27.010 49.858  30.914  1.00 10.93 ? 360  LEU A CG  1 
ATOM   2948  C  CD1 . LEU A 1 360  ? 27.131 50.863  29.768  1.00 11.57 ? 360  LEU A CD1 1 
ATOM   2949  C  CD2 . LEU A 1 360  ? 25.545 49.461  31.128  1.00 12.02 ? 360  LEU A CD2 1 
ATOM   2950  N  N   . PHE A 1 361  ? 30.079 46.423  30.983  1.00 9.42  ? 361  PHE A N   1 
ATOM   2951  C  CA  . PHE A 1 361  ? 30.649 45.136  30.563  1.00 9.33  ? 361  PHE A CA  1 
ATOM   2952  C  C   . PHE A 1 361  ? 30.726 44.159  31.750  1.00 10.78 ? 361  PHE A C   1 
ATOM   2953  O  O   . PHE A 1 361  ? 30.509 42.945  31.615  1.00 10.29 ? 361  PHE A O   1 
ATOM   2954  C  CB  . PHE A 1 361  ? 32.073 45.305  30.023  1.00 9.65  ? 361  PHE A CB  1 
ATOM   2955  C  CG  . PHE A 1 361  ? 32.185 46.151  28.773  1.00 9.23  ? 361  PHE A CG  1 
ATOM   2956  C  CD1 . PHE A 1 361  ? 31.120 46.315  27.903  1.00 8.48  ? 361  PHE A CD1 1 
ATOM   2957  C  CD2 . PHE A 1 361  ? 33.401 46.772  28.507  1.00 9.60  ? 361  PHE A CD2 1 
ATOM   2958  C  CE1 . PHE A 1 361  ? 31.273 47.110  26.736  1.00 10.10 ? 361  PHE A CE1 1 
ATOM   2959  C  CE2 . PHE A 1 361  ? 33.568 47.550  27.342  1.00 9.90  ? 361  PHE A CE2 1 
ATOM   2960  C  CZ  . PHE A 1 361  ? 32.495 47.722  26.481  1.00 9.32  ? 361  PHE A CZ  1 
ATOM   2961  N  N   . GLU A 1 362  ? 31.133 44.670  32.900  1.00 11.01 ? 362  GLU A N   1 
ATOM   2962  C  CA  . GLU A 1 362  ? 31.304 43.772  34.045  1.00 11.55 ? 362  GLU A CA  1 
ATOM   2963  C  C   . GLU A 1 362  ? 29.945 43.146  34.391  1.00 12.70 ? 362  GLU A C   1 
ATOM   2964  O  O   . GLU A 1 362  ? 29.855 41.929  34.605  1.00 13.44 ? 362  GLU A O   1 
ATOM   2965  C  CB  . GLU A 1 362  ? 31.902 44.473  35.270  1.00 13.68 ? 362  GLU A CB  1 
ATOM   2966  C  CG  . GLU A 1 362  ? 31.935 43.506  36.455  1.00 16.38 ? 362  GLU A CG  1 
ATOM   2967  C  CD  . GLU A 1 362  ? 32.472 44.087  37.753  1.00 24.60 ? 362  GLU A CD  1 
ATOM   2968  O  OE1 . GLU A 1 362  ? 32.871 45.266  37.783  1.00 29.06 ? 362  GLU A OE1 1 
ATOM   2969  O  OE2 . GLU A 1 362  ? 32.508 43.313  38.752  1.00 26.81 ? 362  GLU A OE2 1 
ATOM   2970  N  N   . HIS A 1 363  ? 28.898 43.961  34.410  1.00 11.05 ? 363  HIS A N   1 
ATOM   2971  C  CA  . HIS A 1 363  ? 27.577 43.427  34.690  1.00 12.38 ? 363  HIS A CA  1 
ATOM   2972  C  C   . HIS A 1 363  ? 27.094 42.492  33.578  1.00 12.47 ? 363  HIS A C   1 
ATOM   2973  O  O   . HIS A 1 363  ? 26.662 41.376  33.820  1.00 13.27 ? 363  HIS A O   1 
ATOM   2974  C  CB  . HIS A 1 363  ? 26.575 44.535  34.937  1.00 12.00 ? 363  HIS A CB  1 
ATOM   2975  C  CG  . HIS A 1 363  ? 25.193 44.039  35.231  1.00 14.11 ? 363  HIS A CG  1 
ATOM   2976  N  ND1 . HIS A 1 363  ? 24.814 43.575  36.479  1.00 18.11 ? 363  HIS A ND1 1 
ATOM   2977  C  CD2 . HIS A 1 363  ? 24.107 43.922  34.435  1.00 16.79 ? 363  HIS A CD2 1 
ATOM   2978  C  CE1 . HIS A 1 363  ? 23.547 43.202  36.432  1.00 17.66 ? 363  HIS A CE1 1 
ATOM   2979  N  NE2 . HIS A 1 363  ? 23.091 43.404  35.208  1.00 19.26 ? 363  HIS A NE2 1 
ATOM   2980  N  N   . ILE A 1 364  ? 27.136 42.934  32.329  1.00 11.24 ? 364  ILE A N   1 
ATOM   2981  C  CA  . ILE A 1 364  ? 26.604 42.138  31.230  1.00 11.16 ? 364  ILE A CA  1 
ATOM   2982  C  C   . ILE A 1 364  ? 27.335 40.813  31.143  1.00 11.17 ? 364  ILE A C   1 
ATOM   2983  O  O   . ILE A 1 364  ? 26.708 39.753  30.959  1.00 11.90 ? 364  ILE A O   1 
ATOM   2984  C  CB  . ILE A 1 364  ? 26.715 42.931  29.888  1.00 10.71 ? 364  ILE A CB  1 
ATOM   2985  C  CG1 . ILE A 1 364  ? 25.723 44.096  29.920  1.00 10.63 ? 364  ILE A CG1 1 
ATOM   2986  C  CG2 . ILE A 1 364  ? 26.510 41.993  28.678  1.00 12.09 ? 364  ILE A CG2 1 
ATOM   2987  C  CD1 . ILE A 1 364  ? 26.033 45.253  28.935  1.00 11.97 ? 364  ILE A CD1 1 
ATOM   2988  N  N   . ASN A 1 365  ? 28.645 40.841  31.262  1.00 10.32 ? 365  ASN A N   1 
ATOM   2989  C  CA  . ASN A 1 365  ? 29.422 39.636  30.985  1.00 11.47 ? 365  ASN A CA  1 
ATOM   2990  C  C   . ASN A 1 365  ? 29.265 38.571  32.093  1.00 13.54 ? 365  ASN A C   1 
ATOM   2991  O  O   . ASN A 1 365  ? 29.552 37.395  31.888  1.00 14.52 ? 365  ASN A O   1 
ATOM   2992  C  CB  . ASN A 1 365  ? 30.888 39.959  30.776  1.00 10.24 ? 365  ASN A CB  1 
ATOM   2993  C  CG  . ASN A 1 365  ? 31.113 40.776  29.521  1.00 9.29  ? 365  ASN A CG  1 
ATOM   2994  O  OD1 . ASN A 1 365  ? 30.196 40.940  28.695  1.00 11.42 ? 365  ASN A OD1 1 
ATOM   2995  N  ND2 . ASN A 1 365  ? 32.328 41.266  29.386  1.00 8.82  ? 365  ASN A ND2 1 
ATOM   2996  N  N   . SER A 1 366  ? 28.822 39.037  33.261  1.00 16.01 ? 366  SER A N   1 
ATOM   2997  C  CA  . SER A 1 366  ? 28.706 38.180  34.461  1.00 17.83 ? 366  SER A CA  1 
ATOM   2998  C  C   . SER A 1 366  ? 27.293 37.647  34.651  1.00 19.01 ? 366  SER A C   1 
ATOM   2999  O  O   . SER A 1 366  ? 27.070 36.802  35.528  1.00 19.61 ? 366  SER A O   1 
ATOM   3000  C  CB  . SER A 1 366  ? 29.126 38.956  35.714  1.00 18.42 ? 366  SER A CB  1 
ATOM   3001  O  OG  . SER A 1 366  ? 28.119 39.894  36.056  1.00 20.89 ? 366  SER A OG  1 
ATOM   3002  N  N   . GLN A 1 367  ? 26.346 38.132  33.854  1.00 18.39 ? 367  GLN A N   1 
ATOM   3003  C  CA  . GLN A 1 367  ? 24.932 37.773  33.927  1.00 20.01 ? 367  GLN A CA  1 
ATOM   3004  C  C   . GLN A 1 367  ? 24.606 36.847  32.772  1.00 19.63 ? 367  GLN A C   1 
ATOM   3005  O  O   . GLN A 1 367  ? 24.331 37.282  31.654  1.00 18.41 ? 367  GLN A O   1 
ATOM   3006  C  CB  . GLN A 1 367  ? 24.037 39.014  33.820  1.00 20.10 ? 367  GLN A CB  1 
ATOM   3007  C  CG  . GLN A 1 367  ? 24.059 39.915  35.034  1.00 24.58 ? 367  GLN A CG  1 
ATOM   3008  C  CD  . GLN A 1 367  ? 23.329 39.298  36.194  1.00 28.32 ? 367  GLN A CD  1 
ATOM   3009  O  OE1 . GLN A 1 367  ? 22.107 39.102  36.139  1.00 31.36 ? 367  GLN A OE1 1 
ATOM   3010  N  NE2 . GLN A 1 367  ? 24.069 38.981  37.249  1.00 31.27 ? 367  GLN A NE2 1 
ATOM   3011  N  N   . ALA A 1 368  ? 24.581 35.553  33.053  1.00 19.92 ? 368  ALA A N   1 
ATOM   3012  C  CA  . ALA A 1 368  ? 24.448 34.552  32.004  1.00 19.28 ? 368  ALA A CA  1 
ATOM   3013  C  C   . ALA A 1 368  ? 23.212 34.729  31.135  1.00 19.20 ? 368  ALA A C   1 
ATOM   3014  O  O   . ALA A 1 368  ? 23.250 34.382  29.943  1.00 18.69 ? 368  ALA A O   1 
ATOM   3015  C  CB  . ALA A 1 368  ? 24.475 33.149  32.623  1.00 20.25 ? 368  ALA A CB  1 
ATOM   3016  N  N   . HIS A 1 369  ? 22.134 35.280  31.703  1.00 18.36 ? 369  HIS A N   1 
ATOM   3017  C  CA  . HIS A 1 369  ? 20.863 35.401  30.979  1.00 18.99 ? 369  HIS A CA  1 
ATOM   3018  C  C   . HIS A 1 369  ? 20.973 36.258  29.703  1.00 18.09 ? 369  HIS A C   1 
ATOM   3019  O  O   . HIS A 1 369  ? 20.185 36.099  28.757  1.00 19.18 ? 369  HIS A O   1 
ATOM   3020  C  CB  . HIS A 1 369  ? 19.719 35.896  31.885  1.00 20.17 ? 369  HIS A CB  1 
ATOM   3021  C  CG  . HIS A 1 369  ? 19.879 37.304  32.360  1.00 21.53 ? 369  HIS A CG  1 
ATOM   3022  N  ND1 . HIS A 1 369  ? 19.361 38.389  31.677  1.00 25.09 ? 369  HIS A ND1 1 
ATOM   3023  C  CD2 . HIS A 1 369  ? 20.478 37.804  33.462  1.00 23.48 ? 369  HIS A CD2 1 
ATOM   3024  C  CE1 . HIS A 1 369  ? 19.651 39.497  32.337  1.00 23.08 ? 369  HIS A CE1 1 
ATOM   3025  N  NE2 . HIS A 1 369  ? 20.333 39.169  33.419  1.00 25.27 ? 369  HIS A NE2 1 
ATOM   3026  N  N   . PHE A 1 370  ? 21.949 37.161  29.682  1.00 17.49 ? 370  PHE A N   1 
ATOM   3027  C  CA  . PHE A 1 370  ? 22.156 37.978  28.489  1.00 15.39 ? 370  PHE A CA  1 
ATOM   3028  C  C   . PHE A 1 370  ? 22.794 37.178  27.348  1.00 14.36 ? 370  PHE A C   1 
ATOM   3029  O  O   . PHE A 1 370  ? 22.594 37.509  26.176  1.00 13.52 ? 370  PHE A O   1 
ATOM   3030  C  CB  . PHE A 1 370  ? 23.096 39.158  28.768  1.00 15.91 ? 370  PHE A CB  1 
ATOM   3031  C  CG  . PHE A 1 370  ? 22.510 40.256  29.642  1.00 15.44 ? 370  PHE A CG  1 
ATOM   3032  C  CD1 . PHE A 1 370  ? 21.330 40.914  29.289  1.00 16.25 ? 370  PHE A CD1 1 
ATOM   3033  C  CD2 . PHE A 1 370  ? 23.192 40.656  30.775  1.00 17.92 ? 370  PHE A CD2 1 
ATOM   3034  C  CE1 . PHE A 1 370  ? 20.829 41.950  30.111  1.00 18.78 ? 370  PHE A CE1 1 
ATOM   3035  C  CE2 . PHE A 1 370  ? 22.704 41.675  31.582  1.00 18.98 ? 370  PHE A CE2 1 
ATOM   3036  C  CZ  . PHE A 1 370  ? 21.530 42.321  31.237  1.00 17.18 ? 370  PHE A CZ  1 
ATOM   3037  N  N   . ASN A 1 371  ? 23.637 36.207  27.702  1.00 13.38 ? 371  ASN A N   1 
ATOM   3038  C  CA  . ASN A 1 371  ? 24.430 35.441  26.737  1.00 12.80 ? 371  ASN A CA  1 
ATOM   3039  C  C   . ASN A 1 371  ? 25.207 36.356  25.803  1.00 12.10 ? 371  ASN A C   1 
ATOM   3040  O  O   . ASN A 1 371  ? 25.249 36.147  24.583  1.00 12.24 ? 371  ASN A O   1 
ATOM   3041  C  CB  . ASN A 1 371  ? 23.553 34.469  25.944  1.00 13.02 ? 371  ASN A CB  1 
ATOM   3042  C  CG  . ASN A 1 371  ? 22.871 33.442  26.861  1.00 13.55 ? 371  ASN A CG  1 
ATOM   3043  O  OD1 . ASN A 1 371  ? 23.549 32.646  27.510  1.00 17.49 ? 371  ASN A OD1 1 
ATOM   3044  N  ND2 . ASN A 1 371  ? 21.562 33.503  26.932  1.00 17.40 ? 371  ASN A ND2 1 
ATOM   3045  N  N   . VAL A 1 372  ? 25.853 37.330  26.421  1.00 10.44 ? 372  VAL A N   1 
ATOM   3046  C  CA  . VAL A 1 372  ? 26.683 38.317  25.716  1.00 10.80 ? 372  VAL A CA  1 
ATOM   3047  C  C   . VAL A 1 372  ? 28.072 38.345  26.326  1.00 11.26 ? 372  VAL A C   1 
ATOM   3048  O  O   . VAL A 1 372  ? 28.219 38.263  27.570  1.00 11.94 ? 372  VAL A O   1 
ATOM   3049  C  CB  . VAL A 1 372  ? 26.050 39.765  25.824  1.00 10.94 ? 372  VAL A CB  1 
ATOM   3050  C  CG1 . VAL A 1 372  ? 27.050 40.847  25.333  1.00 10.67 ? 372  VAL A CG1 1 
ATOM   3051  C  CG2 . VAL A 1 372  ? 24.739 39.875  25.026  1.00 12.54 ? 372  VAL A CG2 1 
ATOM   3052  N  N   . GLN A 1 373  ? 29.094 38.451  25.491  1.00 9.95  ? 373  GLN A N   1 
ATOM   3053  C  CA  . GLN A 1 373  ? 30.421 38.831  25.948  1.00 9.89  ? 373  GLN A CA  1 
ATOM   3054  C  C   . GLN A 1 373  ? 30.853 40.110  25.225  1.00 9.34  ? 373  GLN A C   1 
ATOM   3055  O  O   . GLN A 1 373  ? 31.024 40.122  24.025  1.00 9.75  ? 373  GLN A O   1 
ATOM   3056  C  CB  . GLN A 1 373  ? 31.414 37.685  25.708  1.00 10.72 ? 373  GLN A CB  1 
ATOM   3057  C  CG  . GLN A 1 373  ? 32.897 37.976  26.015  1.00 13.14 ? 373  GLN A CG  1 
ATOM   3058  C  CD  . GLN A 1 373  ? 33.188 38.320  27.470  1.00 16.15 ? 373  GLN A CD  1 
ATOM   3059  O  OE1 . GLN A 1 373  ? 34.129 39.043  27.766  1.00 17.36 ? 373  GLN A OE1 1 
ATOM   3060  N  NE2 . GLN A 1 373  ? 32.396 37.796  28.365  1.00 16.64 ? 373  GLN A NE2 1 
ATOM   3061  N  N   . ALA A 1 374  ? 30.971 41.184  25.983  1.00 7.84  ? 374  ALA A N   1 
ATOM   3062  C  CA  . ALA A 1 374  ? 31.218 42.496  25.404  1.00 8.34  ? 374  ALA A CA  1 
ATOM   3063  C  C   . ALA A 1 374  ? 32.536 43.049  25.893  1.00 8.73  ? 374  ALA A C   1 
ATOM   3064  O  O   . ALA A 1 374  ? 32.869 42.884  27.044  1.00 9.04  ? 374  ALA A O   1 
ATOM   3065  C  CB  . ALA A 1 374  ? 30.107 43.429  25.772  1.00 8.18  ? 374  ALA A CB  1 
ATOM   3066  N  N   . GLN A 1 375  ? 33.245 43.762  25.027  1.00 8.56  ? 375  GLN A N   1 
ATOM   3067  C  CA  A GLN A 1 375  ? 34.568 44.296  25.377  0.50 8.61  ? 375  GLN A CA  1 
ATOM   3068  C  CA  B GLN A 1 375  ? 34.556 44.306  25.376  0.50 8.94  ? 375  GLN A CA  1 
ATOM   3069  C  C   . GLN A 1 375  ? 34.927 45.440  24.439  1.00 7.86  ? 375  GLN A C   1 
ATOM   3070  O  O   . GLN A 1 375  ? 34.379 45.544  23.356  1.00 8.81  ? 375  GLN A O   1 
ATOM   3071  C  CB  A GLN A 1 375  ? 35.659 43.220  25.300  0.50 9.56  ? 375  GLN A CB  1 
ATOM   3072  C  CB  B GLN A 1 375  ? 35.638 43.230  25.293  0.50 10.15 ? 375  GLN A CB  1 
ATOM   3073  C  CG  A GLN A 1 375  ? 35.639 42.382  24.022  0.50 11.43 ? 375  GLN A CG  1 
ATOM   3074  C  CG  B GLN A 1 375  ? 35.628 42.497  23.988  0.50 13.51 ? 375  GLN A CG  1 
ATOM   3075  C  CD  A GLN A 1 375  ? 34.767 41.152  24.156  0.50 12.32 ? 375  GLN A CD  1 
ATOM   3076  C  CD  B GLN A 1 375  ? 35.930 41.061  24.166  0.50 17.81 ? 375  GLN A CD  1 
ATOM   3077  O  OE1 A GLN A 1 375  ? 34.941 40.358  25.089  0.50 14.49 ? 375  GLN A OE1 1 
ATOM   3078  O  OE1 B GLN A 1 375  ? 35.203 40.333  24.838  0.50 19.96 ? 375  GLN A OE1 1 
ATOM   3079  N  NE2 A GLN A 1 375  ? 33.815 40.988  23.239  0.50 10.73 ? 375  GLN A NE2 1 
ATOM   3080  N  NE2 B GLN A 1 375  ? 37.045 40.643  23.610  0.50 19.67 ? 375  GLN A NE2 1 
ATOM   3081  N  N   . PHE A 1 376  ? 35.869 46.272  24.862  1.00 7.68  ? 376  PHE A N   1 
ATOM   3082  C  CA  . PHE A 1 376  ? 36.478 47.192  23.897  1.00 7.12  ? 376  PHE A CA  1 
ATOM   3083  C  C   . PHE A 1 376  ? 37.244 46.360  22.902  1.00 8.09  ? 376  PHE A C   1 
ATOM   3084  O  O   . PHE A 1 376  ? 37.886 45.354  23.240  1.00 9.59  ? 376  PHE A O   1 
ATOM   3085  C  CB  . PHE A 1 376  ? 37.432 48.142  24.601  1.00 7.29  ? 376  PHE A CB  1 
ATOM   3086  C  CG  . PHE A 1 376  ? 36.742 49.090  25.534  1.00 8.79  ? 376  PHE A CG  1 
ATOM   3087  C  CD1 . PHE A 1 376  ? 35.713 49.913  25.087  1.00 9.57  ? 376  PHE A CD1 1 
ATOM   3088  C  CD2 . PHE A 1 376  ? 37.107 49.157  26.892  1.00 9.89  ? 376  PHE A CD2 1 
ATOM   3089  C  CE1 . PHE A 1 376  ? 35.055 50.789  25.985  1.00 11.86 ? 376  PHE A CE1 1 
ATOM   3090  C  CE2 . PHE A 1 376  ? 36.442 50.031  27.774  1.00 10.99 ? 376  PHE A CE2 1 
ATOM   3091  C  CZ  . PHE A 1 376  ? 35.442 50.836  27.312  1.00 11.41 ? 376  PHE A CZ  1 
ATOM   3092  N  N   . GLY A 1 377  ? 37.192 46.814  21.649  1.00 7.67  ? 377  GLY A N   1 
ATOM   3093  C  CA  . GLY A 1 377  ? 37.892 46.094  20.598  1.00 8.48  ? 377  GLY A CA  1 
ATOM   3094  C  C   . GLY A 1 377  ? 38.431 47.075  19.571  1.00 8.09  ? 377  GLY A C   1 
ATOM   3095  O  O   . GLY A 1 377  ? 38.126 48.255  19.609  1.00 9.09  ? 377  GLY A O   1 
ATOM   3096  N  N   . THR A 1 378  ? 39.187 46.519  18.622  1.00 9.14  ? 378  THR A N   1 
ATOM   3097  C  CA  . THR A 1 378  ? 39.606 47.259  17.434  1.00 9.52  ? 378  THR A CA  1 
ATOM   3098  C  C   . THR A 1 378  ? 38.836 46.722  16.245  1.00 8.35  ? 378  THR A C   1 
ATOM   3099  O  O   . THR A 1 378  ? 38.158 45.687  16.285  1.00 8.75  ? 378  THR A O   1 
ATOM   3100  C  CB  . THR A 1 378  ? 41.122 47.175  17.181  1.00 10.11 ? 378  THR A CB  1 
ATOM   3101  O  OG1 . THR A 1 378  ? 41.448 45.811  16.879  1.00 11.13 ? 378  THR A OG1 1 
ATOM   3102  C  CG2 . THR A 1 378  ? 41.933 47.563  18.423  1.00 13.43 ? 378  THR A CG2 1 
ATOM   3103  N  N   . LEU A 1 379  ? 38.967 47.435  15.139  1.00 7.72  ? 379  LEU A N   1 
ATOM   3104  C  CA  . LEU A 1 379  ? 38.323 47.034  13.917  1.00 7.61  ? 379  LEU A CA  1 
ATOM   3105  C  C   . LEU A 1 379  ? 38.829 45.672  13.419  1.00 7.55  ? 379  LEU A C   1 
ATOM   3106  O  O   . LEU A 1 379  ? 38.051 44.818  12.991  1.00 8.06  ? 379  LEU A O   1 
ATOM   3107  C  CB  . LEU A 1 379  ? 38.501 48.143  12.850  1.00 8.06  ? 379  LEU A CB  1 
ATOM   3108  C  CG  . LEU A 1 379  ? 37.745 47.914  11.523  1.00 7.14  ? 379  LEU A CG  1 
ATOM   3109  C  CD1 . LEU A 1 379  ? 36.243 47.860  11.726  1.00 8.23  ? 379  LEU A CD1 1 
ATOM   3110  C  CD2 . LEU A 1 379  ? 38.147 48.963  10.472  1.00 9.68  ? 379  LEU A CD2 1 
ATOM   3111  N  N   . GLN A 1 380  ? 40.151 45.494  13.392  1.00 7.42  ? 380  GLN A N   1 
ATOM   3112  C  CA  . GLN A 1 380  ? 40.728 44.201  12.994  1.00 8.84  ? 380  GLN A CA  1 
ATOM   3113  C  C   . GLN A 1 380  ? 40.222 43.059  13.857  1.00 9.15  ? 380  GLN A C   1 
ATOM   3114  O  O   . GLN A 1 380  ? 39.980 41.972  13.348  1.00 8.80  ? 380  GLN A O   1 
ATOM   3115  C  CB  . GLN A 1 380  ? 42.262 44.241  13.005  1.00 9.49  ? 380  GLN A CB  1 
ATOM   3116  C  CG  . GLN A 1 380  ? 42.922 42.981  12.451  1.00 12.33 ? 380  GLN A CG  1 
ATOM   3117  C  CD  . GLN A 1 380  ? 42.607 42.790  10.994  1.00 15.55 ? 380  GLN A CD  1 
ATOM   3118  O  OE1 . GLN A 1 380  ? 42.670 43.747  10.211  1.00 16.58 ? 380  GLN A OE1 1 
ATOM   3119  N  NE2 . GLN A 1 380  ? 42.239 41.561  10.616  1.00 18.55 ? 380  GLN A NE2 1 
ATOM   3120  N  N   . GLU A 1 381  ? 40.060 43.308  15.152  1.00 8.56  ? 381  GLU A N   1 
ATOM   3121  C  CA  . GLU A 1 381  ? 39.575 42.262  16.033  1.00 9.01  ? 381  GLU A CA  1 
ATOM   3122  C  C   . GLU A 1 381  ? 38.165 41.825  15.629  1.00 8.74  ? 381  GLU A C   1 
ATOM   3123  O  O   . GLU A 1 381  ? 37.870 40.636  15.640  1.00 9.57  ? 381  GLU A O   1 
ATOM   3124  C  CB  . GLU A 1 381  ? 39.525 42.761  17.470  1.00 10.27 ? 381  GLU A CB  1 
ATOM   3125  C  CG  . GLU A 1 381  ? 40.788 42.663  18.286  1.00 15.83 ? 381  GLU A CG  1 
ATOM   3126  C  CD  . GLU A 1 381  ? 40.415 42.983  19.715  1.00 21.58 ? 381  GLU A CD  1 
ATOM   3127  O  OE1 . GLU A 1 381  ? 40.361 44.165  20.005  1.00 19.44 ? 381  GLU A OE1 1 
ATOM   3128  O  OE2 . GLU A 1 381  ? 40.103 42.059  20.523  1.00 26.08 ? 381  GLU A OE2 1 
ATOM   3129  N  N   . TYR A 1 382  ? 37.305 42.785  15.291  1.00 7.30  ? 382  TYR A N   1 
ATOM   3130  C  CA  . TYR A 1 382  ? 35.968 42.480  14.811  1.00 6.82  ? 382  TYR A CA  1 
ATOM   3131  C  C   . TYR A 1 382  ? 36.054 41.607  13.550  1.00 6.75  ? 382  TYR A C   1 
ATOM   3132  O  O   . TYR A 1 382  ? 35.417 40.560  13.455  1.00 7.09  ? 382  TYR A O   1 
ATOM   3133  C  CB  . TYR A 1 382  ? 35.187 43.781  14.496  1.00 7.01  ? 382  TYR A CB  1 
ATOM   3134  C  CG  . TYR A 1 382  ? 33.912 43.495  13.764  1.00 7.21  ? 382  TYR A CG  1 
ATOM   3135  C  CD1 . TYR A 1 382  ? 32.826 42.905  14.426  1.00 8.25  ? 382  TYR A CD1 1 
ATOM   3136  C  CD2 . TYR A 1 382  ? 33.801 43.757  12.387  1.00 7.84  ? 382  TYR A CD2 1 
ATOM   3137  C  CE1 . TYR A 1 382  ? 31.685 42.572  13.753  1.00 8.56  ? 382  TYR A CE1 1 
ATOM   3138  C  CE2 . TYR A 1 382  ? 32.639 43.456  11.723  1.00 8.37  ? 382  TYR A CE2 1 
ATOM   3139  C  CZ  . TYR A 1 382  ? 31.576 42.844  12.408  1.00 8.66  ? 382  TYR A CZ  1 
ATOM   3140  O  OH  . TYR A 1 382  ? 30.369 42.517  11.804  1.00 9.55  ? 382  TYR A OH  1 
ATOM   3141  N  N   . PHE A 1 383  ? 36.797 42.072  12.553  1.00 6.94  ? 383  PHE A N   1 
ATOM   3142  C  CA  . PHE A 1 383  ? 36.834 41.328  11.315  1.00 6.74  ? 383  PHE A CA  1 
ATOM   3143  C  C   . PHE A 1 383  ? 37.425 39.935  11.513  1.00 7.18  ? 383  PHE A C   1 
ATOM   3144  O  O   . PHE A 1 383  ? 36.956 38.972  10.893  1.00 8.07  ? 383  PHE A O   1 
ATOM   3145  C  CB  . PHE A 1 383  ? 37.604 42.092  10.236  1.00 6.82  ? 383  PHE A CB  1 
ATOM   3146  C  CG  . PHE A 1 383  ? 36.817 43.240  9.628   1.00 7.03  ? 383  PHE A CG  1 
ATOM   3147  C  CD1 . PHE A 1 383  ? 35.611 43.011  8.985   1.00 7.11  ? 383  PHE A CD1 1 
ATOM   3148  C  CD2 . PHE A 1 383  ? 37.323 44.529  9.660   1.00 8.00  ? 383  PHE A CD2 1 
ATOM   3149  C  CE1 . PHE A 1 383  ? 34.907 44.051  8.386   1.00 7.50  ? 383  PHE A CE1 1 
ATOM   3150  C  CE2 . PHE A 1 383  ? 36.624 45.576  9.057   1.00 7.88  ? 383  PHE A CE2 1 
ATOM   3151  C  CZ  . PHE A 1 383  ? 35.416 45.342  8.435   1.00 7.16  ? 383  PHE A CZ  1 
ATOM   3152  N  N   . ASP A 1 384  ? 38.461 39.823  12.339  1.00 7.28  ? 384  ASP A N   1 
ATOM   3153  C  CA  . ASP A 1 384  ? 39.048 38.494  12.596  1.00 8.87  ? 384  ASP A CA  1 
ATOM   3154  C  C   . ASP A 1 384  ? 38.004 37.536  13.177  1.00 8.94  ? 384  ASP A C   1 
ATOM   3155  O  O   . ASP A 1 384  ? 37.911 36.355  12.776  1.00 9.78  ? 384  ASP A O   1 
ATOM   3156  C  CB  . ASP A 1 384  ? 40.214 38.593  13.580  1.00 9.98  ? 384  ASP A CB  1 
ATOM   3157  C  CG  . ASP A 1 384  ? 41.438 39.193  12.998  1.00 14.25 ? 384  ASP A CG  1 
ATOM   3158  O  OD1 . ASP A 1 384  ? 41.561 39.337  11.758  1.00 17.41 ? 384  ASP A OD1 1 
ATOM   3159  O  OD2 . ASP A 1 384  ? 42.360 39.572  13.762  1.00 19.23 ? 384  ASP A OD2 1 
ATOM   3160  N  N   . ALA A 1 385  ? 37.206 38.042  14.110  1.00 8.59  ? 385  ALA A N   1 
ATOM   3161  C  CA  . ALA A 1 385  ? 36.175 37.230  14.733  1.00 8.32  ? 385  ALA A CA  1 
ATOM   3162  C  C   . ALA A 1 385  ? 35.047 36.868  13.755  1.00 8.62  ? 385  ALA A C   1 
ATOM   3163  O  O   . ALA A 1 385  ? 34.552 35.761  13.739  1.00 8.64  ? 385  ALA A O   1 
ATOM   3164  C  CB  . ALA A 1 385  ? 35.625 37.928  15.996  1.00 8.77  ? 385  ALA A CB  1 
ATOM   3165  N  N   . VAL A 1 386  ? 34.663 37.791  12.864  1.00 7.33  ? 386  VAL A N   1 
ATOM   3166  C  CA  . VAL A 1 386  ? 33.672 37.479  11.855  1.00 9.13  ? 386  VAL A CA  1 
ATOM   3167  C  C   . VAL A 1 386  ? 34.170 36.379  10.949  1.00 9.44  ? 386  VAL A C   1 
ATOM   3168  O  O   . VAL A 1 386  ? 33.400 35.436  10.599  1.00 9.57  ? 386  VAL A O   1 
ATOM   3169  C  CB  . VAL A 1 386  ? 33.379 38.740  10.999  1.00 7.70  ? 386  VAL A CB  1 
ATOM   3170  C  CG1 . VAL A 1 386  ? 32.569 38.417  9.758   1.00 11.32 ? 386  VAL A CG1 1 
ATOM   3171  C  CG2 . VAL A 1 386  ? 32.665 39.748  11.838  1.00 9.75  ? 386  VAL A CG2 1 
ATOM   3172  N  N   . HIS A 1 387  ? 35.440 36.452  10.551  1.00 9.69  ? 387  HIS A N   1 
ATOM   3173  C  CA  . HIS A 1 387  ? 35.915 35.423  9.619   1.00 10.33 ? 387  HIS A CA  1 
ATOM   3174  C  C   . HIS A 1 387  ? 36.139 34.085  10.315  1.00 10.80 ? 387  HIS A C   1 
ATOM   3175  O  O   . HIS A 1 387  ? 35.986 33.033  9.675   1.00 10.77 ? 387  HIS A O   1 
ATOM   3176  C  CB  . HIS A 1 387  ? 37.135 35.859  8.819   1.00 10.20 ? 387  HIS A CB  1 
ATOM   3177  C  CG  . HIS A 1 387  ? 36.834 37.006  7.907   1.00 10.27 ? 387  HIS A CG  1 
ATOM   3178  N  ND1 . HIS A 1 387  ? 35.911 36.901  6.892   1.00 13.82 ? 387  HIS A ND1 1 
ATOM   3179  C  CD2 . HIS A 1 387  ? 37.297 38.276  7.881   1.00 10.39 ? 387  HIS A CD2 1 
ATOM   3180  C  CE1 . HIS A 1 387  ? 35.840 38.058  6.253   1.00 12.86 ? 387  HIS A CE1 1 
ATOM   3181  N  NE2 . HIS A 1 387  ? 36.677 38.906  6.826   1.00 11.83 ? 387  HIS A NE2 1 
ATOM   3182  N  N   . GLN A 1 388  ? 36.459 34.115  11.605  1.00 11.88 ? 388  GLN A N   1 
ATOM   3183  C  CA  . GLN A 1 388  ? 36.467 32.874  12.404  1.00 13.04 ? 388  GLN A CA  1 
ATOM   3184  C  C   . GLN A 1 388  ? 35.093 32.220  12.366  1.00 14.04 ? 388  GLN A C   1 
ATOM   3185  O  O   . GLN A 1 388  ? 34.986 30.986  12.214  1.00 14.82 ? 388  GLN A O   1 
ATOM   3186  C  CB  . GLN A 1 388  ? 36.919 33.172  13.820  1.00 14.16 ? 388  GLN A CB  1 
ATOM   3187  C  CG  . GLN A 1 388  ? 38.433 33.363  13.944  1.00 18.62 ? 388  GLN A CG  1 
ATOM   3188  C  CD  . GLN A 1 388  ? 38.874 34.149  15.184  1.00 23.00 ? 388  GLN A CD  1 
ATOM   3189  O  OE1 . GLN A 1 388  ? 38.089 34.354  16.118  1.00 26.88 ? 388  GLN A OE1 1 
ATOM   3190  N  NE2 . GLN A 1 388  ? 40.136 34.609  15.181  1.00 26.15 ? 388  GLN A NE2 1 
ATOM   3191  N  N   . ALA A 1 389  ? 34.041 33.021  12.492  1.00 13.71 ? 389  ALA A N   1 
ATOM   3192  C  CA  . ALA A 1 389  ? 32.659 32.533  12.464  1.00 15.36 ? 389  ALA A CA  1 
ATOM   3193  C  C   . ALA A 1 389  ? 32.324 31.951  11.100  1.00 16.82 ? 389  ALA A C   1 
ATOM   3194  O  O   . ALA A 1 389  ? 31.713 30.874  11.000  1.00 17.93 ? 389  ALA A O   1 
ATOM   3195  C  CB  . ALA A 1 389  ? 31.696 33.653  12.847  1.00 14.97 ? 389  ALA A CB  1 
ATOM   3196  N  N   . GLU A 1 390  ? 32.748 32.641  10.039  1.00 17.54 ? 390  GLU A N   1 
ATOM   3197  C  CA  . GLU A 1 390  ? 32.594 32.165  8.663   1.00 18.79 ? 390  GLU A CA  1 
ATOM   3198  C  C   . GLU A 1 390  ? 33.258 30.805  8.433   1.00 19.65 ? 390  GLU A C   1 
ATOM   3199  O  O   . GLU A 1 390  ? 32.669 29.918  7.807   1.00 20.54 ? 390  GLU A O   1 
ATOM   3200  C  CB  . GLU A 1 390  ? 33.186 33.207  7.709   1.00 18.56 ? 390  GLU A CB  1 
ATOM   3201  C  CG  . GLU A 1 390  ? 32.993 32.931  6.220   1.00 19.67 ? 390  GLU A CG  1 
ATOM   3202  C  CD  . GLU A 1 390  ? 33.728 33.938  5.356   1.00 21.19 ? 390  GLU A CD  1 
ATOM   3203  O  OE1 . GLU A 1 390  ? 34.615 34.656  5.897   1.00 23.12 ? 390  GLU A OE1 1 
ATOM   3204  O  OE2 . GLU A 1 390  ? 33.413 34.021  4.138   1.00 25.59 ? 390  GLU A OE2 1 
ATOM   3205  N  N   . ARG A 1 391  ? 34.485 30.653  8.922   1.00 19.54 ? 391  ARG A N   1 
ATOM   3206  C  CA  . ARG A 1 391  ? 35.224 29.400  8.754   1.00 21.66 ? 391  ARG A CA  1 
ATOM   3207  C  C   . ARG A 1 391  ? 34.581 28.284  9.588   1.00 21.62 ? 391  ARG A C   1 
ATOM   3208  O  O   . ARG A 1 391  ? 34.662 27.088  9.220   1.00 22.90 ? 391  ARG A O   1 
ATOM   3209  C  CB  . ARG A 1 391  ? 36.684 29.577  9.154   1.00 21.49 ? 391  ARG A CB  1 
ATOM   3210  C  CG  . ARG A 1 391  ? 37.508 30.485  8.248   1.00 23.60 ? 391  ARG A CG  1 
ATOM   3211  C  CD  . ARG A 1 391  ? 39.019 30.376  8.484   1.00 23.94 ? 391  ARG A CD  1 
ATOM   3212  N  NE  . ARG A 1 391  ? 39.428 30.833  9.815   1.00 27.74 ? 391  ARG A NE  1 
ATOM   3213  C  CZ  . ARG A 1 391  ? 39.668 32.105  10.134  1.00 26.56 ? 391  ARG A CZ  1 
ATOM   3214  N  NH1 . ARG A 1 391  ? 39.523 33.062  9.232   1.00 28.55 ? 391  ARG A NH1 1 
ATOM   3215  N  NH2 . ARG A 1 391  ? 40.036 32.417  11.362  1.00 28.21 ? 391  ARG A NH2 1 
ATOM   3216  N  N   . ALA A 1 392  ? 33.942 28.652  10.693  1.00 21.82 ? 392  ALA A N   1 
ATOM   3217  C  CA  . ALA A 1 392  ? 33.221 27.671  11.525  1.00 22.52 ? 392  ALA A CA  1 
ATOM   3218  C  C   . ALA A 1 392  ? 31.927 27.205  10.817  1.00 23.20 ? 392  ALA A C   1 
ATOM   3219  O  O   . ALA A 1 392  ? 31.219 26.302  11.312  1.00 24.30 ? 392  ALA A O   1 
ATOM   3220  C  CB  . ALA A 1 392  ? 32.916 28.241  12.903  1.00 23.12 ? 392  ALA A CB  1 
ATOM   3221  N  N   . GLY A 1 393  ? 31.633 27.818  9.664   1.00 22.80 ? 393  GLY A N   1 
ATOM   3222  C  CA  . GLY A 1 393  ? 30.450 27.497  8.881   1.00 22.67 ? 393  GLY A CA  1 
ATOM   3223  C  C   . GLY A 1 393  ? 29.194 28.153  9.410   1.00 22.08 ? 393  GLY A C   1 
ATOM   3224  O  O   . GLY A 1 393  ? 28.083 27.727  9.100   1.00 22.46 ? 393  GLY A O   1 
ATOM   3225  N  N   . GLN A 1 394  ? 29.349 29.216  10.179  1.00 21.82 ? 394  GLN A N   1 
ATOM   3226  C  CA  . GLN A 1 394  ? 28.240 29.855  10.838  1.00 22.22 ? 394  GLN A CA  1 
ATOM   3227  C  C   . GLN A 1 394  ? 27.487 30.774  9.866   1.00 20.97 ? 394  GLN A C   1 
ATOM   3228  O  O   . GLN A 1 394  ? 26.333 31.077  10.054  1.00 22.39 ? 394  GLN A O   1 
ATOM   3229  C  CB  . GLN A 1 394  ? 28.805 30.669  11.997  1.00 23.34 ? 394  GLN A CB  1 
ATOM   3230  C  CG  . GLN A 1 394  ? 27.873 30.963  13.090  1.00 25.68 ? 394  GLN A CG  1 
ATOM   3231  C  CD  . GLN A 1 394  ? 28.402 32.056  13.971  1.00 25.22 ? 394  GLN A CD  1 
ATOM   3232  O  OE1 . GLN A 1 394  ? 28.076 33.216  13.796  1.00 20.06 ? 394  GLN A OE1 1 
ATOM   3233  N  NE2 . GLN A 1 394  ? 29.257 31.687  14.902  1.00 24.78 ? 394  GLN A NE2 1 
ATOM   3234  N  N   . ALA A 1 395  ? 28.170 31.206  8.818   1.00 19.99 ? 395  ALA A N   1 
ATOM   3235  C  CA  . ALA A 1 395  ? 27.667 32.206  7.889   1.00 19.56 ? 395  ALA A CA  1 
ATOM   3236  C  C   . ALA A 1 395  ? 28.305 32.045  6.498   1.00 18.55 ? 395  ALA A C   1 
ATOM   3237  O  O   . ALA A 1 395  ? 29.480 31.657  6.384   1.00 17.67 ? 395  ALA A O   1 
ATOM   3238  C  CB  . ALA A 1 395  ? 27.949 33.600  8.453   1.00 19.88 ? 395  ALA A CB  1 
ATOM   3239  N  N   . GLU A 1 396  ? 27.529 32.322  5.449   1.00 17.72 ? 396  GLU A N   1 
ATOM   3240  C  CA  . GLU A 1 396  ? 28.071 32.558  4.105   1.00 18.60 ? 396  GLU A CA  1 
ATOM   3241  C  C   . GLU A 1 396  ? 27.681 33.979  3.728   1.00 16.32 ? 396  GLU A C   1 
ATOM   3242  O  O   . GLU A 1 396  ? 26.593 34.444  4.102   1.00 17.38 ? 396  GLU A O   1 
ATOM   3243  C  CB  . GLU A 1 396  ? 27.536 31.551  3.066   1.00 18.86 ? 396  GLU A CB  1 
ATOM   3244  C  CG  . GLU A 1 396  ? 26.013 31.429  3.014   1.00 23.43 ? 396  GLU A CG  1 
ATOM   3245  C  CD  . GLU A 1 396  ? 25.513 30.339  2.065   1.00 24.50 ? 396  GLU A CD  1 
ATOM   3246  O  OE1 . GLU A 1 396  ? 26.200 30.029  1.062   1.00 31.53 ? 396  GLU A OE1 1 
ATOM   3247  O  OE2 . GLU A 1 396  ? 24.404 29.790  2.310   1.00 32.43 ? 396  GLU A OE2 1 
ATOM   3248  N  N   . PHE A 1 397  ? 28.562 34.669  3.007   1.00 13.13 ? 397  PHE A N   1 
ATOM   3249  C  CA  . PHE A 1 397  ? 28.287 36.051  2.672   1.00 10.88 ? 397  PHE A CA  1 
ATOM   3250  C  C   . PHE A 1 397  ? 27.958 36.242  1.198   1.00 9.44  ? 397  PHE A C   1 
ATOM   3251  O  O   . PHE A 1 397  ? 28.522 35.569  0.346   1.00 10.40 ? 397  PHE A O   1 
ATOM   3252  C  CB  . PHE A 1 397  ? 29.518 36.892  3.031   1.00 10.95 ? 397  PHE A CB  1 
ATOM   3253  C  CG  . PHE A 1 397  ? 29.802 36.913  4.501   1.00 9.33  ? 397  PHE A CG  1 
ATOM   3254  C  CD1 . PHE A 1 397  ? 28.951 37.580  5.368   1.00 8.61  ? 397  PHE A CD1 1 
ATOM   3255  C  CD2 . PHE A 1 397  ? 30.901 36.241  5.002   1.00 11.65 ? 397  PHE A CD2 1 
ATOM   3256  C  CE1 . PHE A 1 397  ? 29.200 37.599  6.734   1.00 9.52  ? 397  PHE A CE1 1 
ATOM   3257  C  CE2 . PHE A 1 397  ? 31.158 36.242  6.364   1.00 13.19 ? 397  PHE A CE2 1 
ATOM   3258  C  CZ  . PHE A 1 397  ? 30.309 36.905  7.211   1.00 10.36 ? 397  PHE A CZ  1 
ATOM   3259  N  N   . PRO A 1 398  ? 27.061 37.158  0.906   1.00 8.36  ? 398  PRO A N   1 
ATOM   3260  C  CA  . PRO A 1 398  ? 26.696 37.442  -0.489  1.00 8.08  ? 398  PRO A CA  1 
ATOM   3261  C  C   . PRO A 1 398  ? 27.783 38.202  -1.224  1.00 7.98  ? 398  PRO A C   1 
ATOM   3262  O  O   . PRO A 1 398  ? 28.615 38.843  -0.609  1.00 8.25  ? 398  PRO A O   1 
ATOM   3263  C  CB  . PRO A 1 398  ? 25.464 38.324  -0.339  1.00 9.73  ? 398  PRO A CB  1 
ATOM   3264  C  CG  . PRO A 1 398  ? 25.678 39.048  0.973   1.00 8.77  ? 398  PRO A CG  1 
ATOM   3265  C  CD  . PRO A 1 398  ? 26.302 37.996  1.843   1.00 9.25  ? 398  PRO A CD  1 
ATOM   3266  N  N   . THR A 1 399  ? 27.757 38.083  -2.538  1.00 7.58  ? 399  THR A N   1 
ATOM   3267  C  CA  . THR A 1 399  ? 28.653 38.840  -3.417  1.00 6.90  ? 399  THR A CA  1 
ATOM   3268  C  C   . THR A 1 399  ? 27.906 40.053  -3.958  1.00 7.21  ? 399  THR A C   1 
ATOM   3269  O  O   . THR A 1 399  ? 26.693 40.016  -4.129  1.00 7.05  ? 399  THR A O   1 
ATOM   3270  C  CB  . THR A 1 399  ? 29.075 37.951  -4.554  1.00 7.72  ? 399  THR A CB  1 
ATOM   3271  O  OG1 . THR A 1 399  ? 27.894 37.477  -5.234  1.00 9.81  ? 399  THR A OG1 1 
ATOM   3272  C  CG2 . THR A 1 399  ? 29.845 36.725  -4.010  1.00 9.17  ? 399  THR A CG2 1 
ATOM   3273  N  N   . LEU A 1 400  ? 28.660 41.132  -4.205  1.00 5.94  ? 400  LEU A N   1 
ATOM   3274  C  CA  . LEU A 1 400  ? 28.028 42.370  -4.628  1.00 5.51  ? 400  LEU A CA  1 
ATOM   3275  C  C   . LEU A 1 400  ? 28.943 43.039  -5.639  1.00 4.71  ? 400  LEU A C   1 
ATOM   3276  O  O   . LEU A 1 400  ? 30.156 42.996  -5.502  1.00 5.61  ? 400  LEU A O   1 
ATOM   3277  C  CB  . LEU A 1 400  ? 27.826 43.301  -3.417  1.00 5.65  ? 400  LEU A CB  1 
ATOM   3278  C  CG  . LEU A 1 400  ? 27.123 44.641  -3.674  1.00 6.14  ? 400  LEU A CG  1 
ATOM   3279  C  CD1 . LEU A 1 400  ? 26.240 45.039  -2.477  1.00 8.00  ? 400  LEU A CD1 1 
ATOM   3280  C  CD2 . LEU A 1 400  ? 28.165 45.709  -3.942  1.00 7.51  ? 400  LEU A CD2 1 
ATOM   3281  N  N   . SER A 1 401  ? 28.343 43.664  -6.657  1.00 5.34  ? 401  SER A N   1 
ATOM   3282  C  CA  . SER A 1 401  ? 29.096 44.623  -7.449  1.00 5.31  ? 401  SER A CA  1 
ATOM   3283  C  C   . SER A 1 401  ? 28.259 45.865  -7.645  1.00 4.74  ? 401  SER A C   1 
ATOM   3284  O  O   . SER A 1 401  ? 27.044 45.850  -7.497  1.00 5.07  ? 401  SER A O   1 
ATOM   3285  C  CB  . SER A 1 401  ? 29.511 44.045  -8.787  1.00 5.94  ? 401  SER A CB  1 
ATOM   3286  O  OG  . SER A 1 401  ? 28.406 44.024  -9.697  1.00 6.34  ? 401  SER A OG  1 
ATOM   3287  N  N   . GLY A 1 402  ? 28.934 46.966  -7.989  1.00 4.92  ? 402  GLY A N   1 
ATOM   3288  C  CA  . GLY A 1 402  ? 28.263 48.236  -8.240  1.00 5.62  ? 402  GLY A CA  1 
ATOM   3289  C  C   . GLY A 1 402  ? 28.889 49.320  -7.392  1.00 5.59  ? 402  GLY A C   1 
ATOM   3290  O  O   . GLY A 1 402  ? 29.945 49.097  -6.769  1.00 7.23  ? 402  GLY A O   1 
ATOM   3291  N  N   . ASP A 1 403  ? 28.255 50.476  -7.334  1.00 4.92  ? 403  ASP A N   1 
ATOM   3292  C  CA  . ASP A 1 403  ? 28.740 51.595  -6.513  1.00 4.96  ? 403  ASP A CA  1 
ATOM   3293  C  C   . ASP A 1 403  ? 27.586 52.088  -5.644  1.00 5.99  ? 403  ASP A C   1 
ATOM   3294  O  O   . ASP A 1 403  ? 26.465 51.544  -5.677  1.00 7.00  ? 403  ASP A O   1 
ATOM   3295  C  CB  . ASP A 1 403  ? 29.311 52.710  -7.397  1.00 5.59  ? 403  ASP A CB  1 
ATOM   3296  C  CG  . ASP A 1 403  ? 28.274 53.500  -8.109  1.00 10.92 ? 403  ASP A CG  1 
ATOM   3297  O  OD1 . ASP A 1 403  ? 27.094 53.110  -8.154  1.00 13.75 ? 403  ASP A OD1 1 
ATOM   3298  O  OD2 . ASP A 1 403  ? 28.596 54.569  -8.643  1.00 13.36 ? 403  ASP A OD2 1 
ATOM   3299  N  N   . PHE A 1 404  ? 27.880 53.077  -4.821  1.00 4.38  ? 404  PHE A N   1 
ATOM   3300  C  CA  . PHE A 1 404  ? 26.950 53.627  -3.840  1.00 5.11  ? 404  PHE A CA  1 
ATOM   3301  C  C   . PHE A 1 404  ? 26.829 55.138  -4.002  1.00 5.60  ? 404  PHE A C   1 
ATOM   3302  O  O   . PHE A 1 404  ? 26.912 55.885  -3.049  1.00 6.75  ? 404  PHE A O   1 
ATOM   3303  C  CB  . PHE A 1 404  ? 27.316 53.175  -2.398  1.00 4.68  ? 404  PHE A CB  1 
ATOM   3304  C  CG  . PHE A 1 404  ? 27.274 51.681  -2.219  1.00 4.78  ? 404  PHE A CG  1 
ATOM   3305  C  CD1 . PHE A 1 404  ? 26.048 51.040  -2.070  1.00 5.60  ? 404  PHE A CD1 1 
ATOM   3306  C  CD2 . PHE A 1 404  ? 28.442 50.948  -2.209  1.00 5.24  ? 404  PHE A CD2 1 
ATOM   3307  C  CE1 . PHE A 1 404  ? 26.019 49.650  -1.925  1.00 5.56  ? 404  PHE A CE1 1 
ATOM   3308  C  CE2 . PHE A 1 404  ? 28.401 49.571  -2.058  1.00 6.62  ? 404  PHE A CE2 1 
ATOM   3309  C  CZ  . PHE A 1 404  ? 27.183 48.946  -1.897  1.00 6.20  ? 404  PHE A CZ  1 
ATOM   3310  N  N   . PHE A 1 405  ? 26.612 55.545  -5.248  1.00 6.00  ? 405  PHE A N   1 
ATOM   3311  C  CA  . PHE A 1 405  ? 26.230 56.920  -5.583  1.00 5.26  ? 405  PHE A CA  1 
ATOM   3312  C  C   . PHE A 1 405  ? 24.863 56.868  -6.243  1.00 5.54  ? 405  PHE A C   1 
ATOM   3313  O  O   . PHE A 1 405  ? 24.567 55.881  -6.915  1.00 6.62  ? 405  PHE A O   1 
ATOM   3314  C  CB  . PHE A 1 405  ? 27.224 57.519  -6.585  1.00 6.05  ? 405  PHE A CB  1 
ATOM   3315  C  CG  . PHE A 1 405  ? 28.622 57.621  -6.047  1.00 5.63  ? 405  PHE A CG  1 
ATOM   3316  C  CD1 . PHE A 1 405  ? 28.880 58.448  -4.971  1.00 7.08  ? 405  PHE A CD1 1 
ATOM   3317  C  CD2 . PHE A 1 405  ? 29.641 56.910  -6.621  1.00 5.60  ? 405  PHE A CD2 1 
ATOM   3318  C  CE1 . PHE A 1 405  ? 30.189 58.535  -4.425  1.00 7.33  ? 405  PHE A CE1 1 
ATOM   3319  C  CE2 . PHE A 1 405  ? 30.935 56.988  -6.095  1.00 6.73  ? 405  PHE A CE2 1 
ATOM   3320  C  CZ  . PHE A 1 405  ? 31.186 57.814  -4.979  1.00 6.11  ? 405  PHE A CZ  1 
ATOM   3321  N  N   . THR A 1 406  ? 24.065 57.939  -6.159  1.00 5.48  ? 406  THR A N   1 
ATOM   3322  C  CA  . THR A 1 406  ? 24.298 59.127  -5.349  1.00 5.04  ? 406  THR A CA  1 
ATOM   3323  C  C   . THR A 1 406  ? 23.647 58.991  -3.989  1.00 5.61  ? 406  THR A C   1 
ATOM   3324  O  O   . THR A 1 406  ? 22.487 58.578  -3.848  1.00 6.08  ? 406  THR A O   1 
ATOM   3325  C  CB  . THR A 1 406  ? 23.760 60.332  -6.142  1.00 5.63  ? 406  THR A CB  1 
ATOM   3326  O  OG1 . THR A 1 406  ? 24.700 60.552  -7.197  1.00 6.88  ? 406  THR A OG1 1 
ATOM   3327  C  CG2 . THR A 1 406  ? 23.677 61.619  -5.325  1.00 6.40  ? 406  THR A CG2 1 
ATOM   3328  N  N   . TYR A 1 407  ? 24.409 59.365  -2.980  1.00 6.44  ? 407  TYR A N   1 
ATOM   3329  C  CA  . TYR A 1 407  ? 23.985 59.267  -1.600  1.00 5.73  ? 407  TYR A CA  1 
ATOM   3330  C  C   . TYR A 1 407  ? 22.850 60.231  -1.273  1.00 6.45  ? 407  TYR A C   1 
ATOM   3331  O  O   . TYR A 1 407  ? 22.866 61.352  -1.701  1.00 6.87  ? 407  TYR A O   1 
ATOM   3332  C  CB  . TYR A 1 407  ? 25.193 59.557  -0.733  1.00 5.83  ? 407  TYR A CB  1 
ATOM   3333  C  CG  . TYR A 1 407  ? 24.968 59.669  0.754   1.00 4.86  ? 407  TYR A CG  1 
ATOM   3334  C  CD1 . TYR A 1 407  ? 24.520 58.594  1.506   1.00 6.77  ? 407  TYR A CD1 1 
ATOM   3335  C  CD2 . TYR A 1 407  ? 25.300 60.824  1.409   1.00 5.92  ? 407  TYR A CD2 1 
ATOM   3336  C  CE1 . TYR A 1 407  ? 24.390 58.697  2.859   1.00 6.44  ? 407  TYR A CE1 1 
ATOM   3337  C  CE2 . TYR A 1 407  ? 25.168 60.938  2.756   1.00 5.99  ? 407  TYR A CE2 1 
ATOM   3338  C  CZ  . TYR A 1 407  ? 24.713 59.867  3.480   1.00 5.39  ? 407  TYR A CZ  1 
ATOM   3339  O  OH  . TYR A 1 407  ? 24.601 59.948  4.831   1.00 7.19  ? 407  TYR A OH  1 
ATOM   3340  N  N   . ALA A 1 408  ? 21.880 59.751  -0.516  1.00 7.04  ? 408  ALA A N   1 
ATOM   3341  C  CA  . ALA A 1 408  ? 20.946 60.639  0.214   1.00 6.72  ? 408  ALA A CA  1 
ATOM   3342  C  C   . ALA A 1 408  ? 20.892 60.166  1.641   1.00 6.65  ? 408  ALA A C   1 
ATOM   3343  O  O   . ALA A 1 408  ? 20.781 58.948  1.897   1.00 6.65  ? 408  ALA A O   1 
ATOM   3344  C  CB  . ALA A 1 408  ? 19.530 60.579  -0.395  1.00 7.87  ? 408  ALA A CB  1 
ATOM   3345  N  N   . ASP A 1 409  ? 20.996 61.118  2.588   1.00 6.05  ? 409  ASP A N   1 
ATOM   3346  C  CA  . ASP A 1 409  ? 20.909 60.744  4.004   1.00 7.16  ? 409  ASP A CA  1 
ATOM   3347  C  C   . ASP A 1 409  ? 19.476 60.766  4.506   1.00 7.73  ? 409  ASP A C   1 
ATOM   3348  O  O   . ASP A 1 409  ? 19.191 60.123  5.521   1.00 8.51  ? 409  ASP A O   1 
ATOM   3349  C  CB  . ASP A 1 409  ? 21.798 61.595  4.928   1.00 8.34  ? 409  ASP A CB  1 
ATOM   3350  C  CG  . ASP A 1 409  ? 21.575 63.109  4.806   1.00 7.10  ? 409  ASP A CG  1 
ATOM   3351  O  OD1 . ASP A 1 409  ? 20.957 63.630  3.832   1.00 7.11  ? 409  ASP A OD1 1 
ATOM   3352  O  OD2 . ASP A 1 409  ? 22.103 63.867  5.680   1.00 8.40  ? 409  ASP A OD2 1 
ATOM   3353  N  N   . ARG A 1 410  ? 18.606 61.516  3.826   1.00 7.04  ? 410  ARG A N   1 
ATOM   3354  C  CA  . ARG A 1 410  ? 17.194 61.595  4.247   1.00 8.81  ? 410  ARG A CA  1 
ATOM   3355  C  C   . ARG A 1 410  ? 16.370 62.212  3.146   1.00 9.01  ? 410  ARG A C   1 
ATOM   3356  O  O   . ARG A 1 410  ? 16.877 62.984  2.316   1.00 9.32  ? 410  ARG A O   1 
ATOM   3357  C  CB  . ARG A 1 410  ? 17.032 62.360  5.569   1.00 8.90  ? 410  ARG A CB  1 
ATOM   3358  C  CG  . ARG A 1 410  ? 17.535 63.781  5.592   1.00 11.42 ? 410  ARG A CG  1 
ATOM   3359  C  CD  . ARG A 1 410  ? 17.493 64.383  6.998   1.00 11.82 ? 410  ARG A CD  1 
ATOM   3360  N  NE  . ARG A 1 410  ? 18.119 65.715  7.066   1.00 12.88 ? 410  ARG A NE  1 
ATOM   3361  C  CZ  . ARG A 1 410  ? 17.507 66.872  6.816   1.00 15.47 ? 410  ARG A CZ  1 
ATOM   3362  N  NH1 . ARG A 1 410  ? 16.230 66.898  6.412   1.00 16.89 ? 410  ARG A NH1 1 
ATOM   3363  N  NH2 . ARG A 1 410  ? 18.197 68.003  6.914   1.00 14.78 ? 410  ARG A NH2 1 
ATOM   3364  N  N   . SER A 1 411  ? 15.082 61.849  3.116   1.00 9.55  ? 411  SER A N   1 
ATOM   3365  C  CA  A SER A 1 411  ? 14.101 62.414  2.184   0.50 10.61 ? 411  SER A CA  1 
ATOM   3366  C  CA  B SER A 1 411  ? 14.138 62.491  2.213   0.50 10.10 ? 411  SER A CA  1 
ATOM   3367  C  C   . SER A 1 411  ? 14.659 62.528  0.761   1.00 9.63  ? 411  SER A C   1 
ATOM   3368  O  O   . SER A 1 411  ? 15.154 61.517  0.221   1.00 10.21 ? 411  SER A O   1 
ATOM   3369  C  CB  A SER A 1 411  ? 13.505 63.710  2.734   0.50 11.89 ? 411  SER A CB  1 
ATOM   3370  C  CB  B SER A 1 411  ? 13.848 63.889  2.748   0.50 11.18 ? 411  SER A CB  1 
ATOM   3371  O  OG  A SER A 1 411  ? 14.495 64.673  3.021   0.50 14.36 ? 411  SER A OG  1 
ATOM   3372  O  OG  B SER A 1 411  ? 12.807 64.497  2.020   0.50 11.24 ? 411  SER A OG  1 
ATOM   3373  N  N   . ASP A 1 412  ? 14.571 63.712  0.121   1.00 9.29  ? 412  ASP A N   1 
ATOM   3374  C  CA  . ASP A 1 412  ? 15.095 63.902  -1.240  1.00 7.83  ? 412  ASP A CA  1 
ATOM   3375  C  C   . ASP A 1 412  ? 16.439 64.641  -1.243  1.00 7.67  ? 412  ASP A C   1 
ATOM   3376  O  O   . ASP A 1 412  ? 16.810 65.261  -2.227  1.00 8.38  ? 412  ASP A O   1 
ATOM   3377  C  CB  . ASP A 1 412  ? 14.115 64.705  -2.103  1.00 9.87  ? 412  ASP A CB  1 
ATOM   3378  C  CG  . ASP A 1 412  ? 13.887 66.094  -1.561  1.00 9.98  ? 412  ASP A CG  1 
ATOM   3379  O  OD1 . ASP A 1 412  ? 14.347 66.432  -0.446  1.00 10.48 ? 412  ASP A OD1 1 
ATOM   3380  O  OD2 . ASP A 1 412  ? 13.240 66.930  -2.237  1.00 12.14 ? 412  ASP A OD2 1 
ATOM   3381  N  N   . ASN A 1 413  ? 17.124 64.622  -0.099  1.00 7.24  ? 413  ASN A N   1 
ATOM   3382  C  CA  . ASN A 1 413  ? 18.368 65.378  0.074   1.00 6.91  ? 413  ASN A CA  1 
ATOM   3383  C  C   . ASN A 1 413  ? 19.543 64.550  -0.469  1.00 6.99  ? 413  ASN A C   1 
ATOM   3384  O  O   . ASN A 1 413  ? 20.220 63.862  0.285   1.00 7.54  ? 413  ASN A O   1 
ATOM   3385  C  CB  . ASN A 1 413  ? 18.581 65.690  1.547   1.00 6.90  ? 413  ASN A CB  1 
ATOM   3386  C  CG  . ASN A 1 413  ? 17.641 66.760  2.133   1.00 7.76  ? 413  ASN A CG  1 
ATOM   3387  O  OD1 . ASN A 1 413  ? 17.940 67.274  3.207   1.00 9.76  ? 413  ASN A OD1 1 
ATOM   3388  N  ND2 . ASN A 1 413  ? 16.556 67.121  1.440   1.00 9.09  ? 413  ASN A ND2 1 
ATOM   3389  N  N   . TYR A 1 414  ? 19.724 64.601  -1.789  1.00 6.00  ? 414  TYR A N   1 
ATOM   3390  C  CA  . TYR A 1 414  ? 20.793 63.892  -2.485  1.00 6.51  ? 414  TYR A CA  1 
ATOM   3391  C  C   . TYR A 1 414  ? 22.036 64.763  -2.551  1.00 6.62  ? 414  TYR A C   1 
ATOM   3392  O  O   . TYR A 1 414  ? 21.952 65.943  -2.853  1.00 6.45  ? 414  TYR A O   1 
ATOM   3393  C  CB  . TYR A 1 414  ? 20.351 63.520  -3.905  1.00 6.61  ? 414  TYR A CB  1 
ATOM   3394  C  CG  . TYR A 1 414  ? 19.368 62.363  -3.911  1.00 6.28  ? 414  TYR A CG  1 
ATOM   3395  C  CD1 . TYR A 1 414  ? 18.012 62.580  -3.748  1.00 7.13  ? 414  TYR A CD1 1 
ATOM   3396  C  CD2 . TYR A 1 414  ? 19.814 61.072  -4.081  1.00 8.26  ? 414  TYR A CD2 1 
ATOM   3397  C  CE1 . TYR A 1 414  ? 17.127 61.502  -3.684  1.00 7.49  ? 414  TYR A CE1 1 
ATOM   3398  C  CE2 . TYR A 1 414  ? 18.937 59.997  -4.052  1.00 7.46  ? 414  TYR A CE2 1 
ATOM   3399  C  CZ  . TYR A 1 414  ? 17.600 60.222  -3.875  1.00 7.49  ? 414  TYR A CZ  1 
ATOM   3400  O  OH  . TYR A 1 414  ? 16.721 59.139  -3.847  1.00 8.04  ? 414  TYR A OH  1 
ATOM   3401  N  N   . TRP A 1 415  ? 23.168 64.132  -2.248  1.00 5.93  ? 415  TRP A N   1 
ATOM   3402  C  CA  . TRP A 1 415  ? 24.418 64.871  -2.120  1.00 5.82  ? 415  TRP A CA  1 
ATOM   3403  C  C   . TRP A 1 415  ? 25.135 64.916  -3.457  1.00 7.56  ? 415  TRP A C   1 
ATOM   3404  O  O   . TRP A 1 415  ? 26.256 64.410  -3.578  1.00 8.99  ? 415  TRP A O   1 
ATOM   3405  C  CB  . TRP A 1 415  ? 25.273 64.187  -1.066  1.00 6.27  ? 415  TRP A CB  1 
ATOM   3406  C  CG  . TRP A 1 415  ? 24.711 64.264  0.336   1.00 5.84  ? 415  TRP A CG  1 
ATOM   3407  C  CD1 . TRP A 1 415  ? 23.407 64.038  0.744   1.00 6.50  ? 415  TRP A CD1 1 
ATOM   3408  C  CD2 . TRP A 1 415  ? 25.451 64.533  1.525   1.00 6.12  ? 415  TRP A CD2 1 
ATOM   3409  N  NE1 . TRP A 1 415  ? 23.322 64.152  2.115   1.00 6.20  ? 415  TRP A NE1 1 
ATOM   3410  C  CE2 . TRP A 1 415  ? 24.569 64.434  2.624   1.00 6.99  ? 415  TRP A CE2 1 
ATOM   3411  C  CE3 . TRP A 1 415  ? 26.803 64.801  1.779   1.00 7.76  ? 415  TRP A CE3 1 
ATOM   3412  C  CZ2 . TRP A 1 415  ? 24.975 64.656  3.943   1.00 7.62  ? 415  TRP A CZ2 1 
ATOM   3413  C  CZ3 . TRP A 1 415  ? 27.212 65.009  3.091   1.00 6.96  ? 415  TRP A CZ3 1 
ATOM   3414  C  CH2 . TRP A 1 415  ? 26.307 64.931  4.166   1.00 8.21  ? 415  TRP A CH2 1 
ATOM   3415  N  N   . SER A 1 416  ? 24.510 65.518  -4.464  1.00 5.52  ? 416  SER A N   1 
ATOM   3416  C  CA  . SER A 1 416  ? 25.157 65.634  -5.750  1.00 5.83  ? 416  SER A CA  1 
ATOM   3417  C  C   . SER A 1 416  ? 25.695 67.026  -5.972  1.00 6.36  ? 416  SER A C   1 
ATOM   3418  O  O   . SER A 1 416  ? 26.383 67.248  -6.954  1.00 6.70  ? 416  SER A O   1 
ATOM   3419  C  CB  . SER A 1 416  ? 24.207 65.223  -6.879  1.00 6.00  ? 416  SER A CB  1 
ATOM   3420  O  OG  . SER A 1 416  ? 22.915 65.778  -6.689  1.00 7.00  ? 416  SER A OG  1 
ATOM   3421  N  N   . GLY A 1 417  ? 25.482 67.940  -5.035  1.00 4.81  ? 417  GLY A N   1 
ATOM   3422  C  CA  . GLY A 1 417  ? 26.066 69.262  -5.227  1.00 5.40  ? 417  GLY A CA  1 
ATOM   3423  C  C   . GLY A 1 417  ? 27.563 69.270  -5.140  1.00 4.16  ? 417  GLY A C   1 
ATOM   3424  O  O   . GLY A 1 417  ? 28.222 70.004  -5.881  1.00 5.14  ? 417  GLY A O   1 
ATOM   3425  N  N   . TYR A 1 418  ? 28.107 68.459  -4.231  1.00 4.05  ? 418  TYR A N   1 
ATOM   3426  C  CA  . TYR A 1 418  ? 29.559 68.504  -4.045  1.00 4.44  ? 418  TYR A CA  1 
ATOM   3427  C  C   . TYR A 1 418  ? 30.311 67.894  -5.235  1.00 4.87  ? 418  TYR A C   1 
ATOM   3428  O  O   . TYR A 1 418  ? 31.555 67.928  -5.277  1.00 6.03  ? 418  TYR A O   1 
ATOM   3429  C  CB  . TYR A 1 418  ? 29.952 67.806  -2.732  1.00 5.04  ? 418  TYR A CB  1 
ATOM   3430  C  CG  . TYR A 1 418  ? 30.074 66.302  -2.806  1.00 5.61  ? 418  TYR A CG  1 
ATOM   3431  C  CD1 . TYR A 1 418  ? 28.980 65.473  -2.628  1.00 5.92  ? 418  TYR A CD1 1 
ATOM   3432  C  CD2 . TYR A 1 418  ? 31.316 65.711  -3.000  1.00 5.64  ? 418  TYR A CD2 1 
ATOM   3433  C  CE1 . TYR A 1 418  ? 29.113 64.088  -2.679  1.00 4.50  ? 418  TYR A CE1 1 
ATOM   3434  C  CE2 . TYR A 1 418  ? 31.462 64.357  -3.031  1.00 4.35  ? 418  TYR A CE2 1 
ATOM   3435  C  CZ  . TYR A 1 418  ? 30.363 63.547  -2.869  1.00 4.40  ? 418  TYR A CZ  1 
ATOM   3436  O  OH  . TYR A 1 418  ? 30.539 62.176  -2.899  1.00 6.57  ? 418  TYR A OH  1 
ATOM   3437  N  N   . TYR A 1 419  ? 29.603 67.277  -6.192  1.00 4.65  ? 419  TYR A N   1 
ATOM   3438  C  CA  . TYR A 1 419  ? 30.273 66.865  -7.410  1.00 4.15  ? 419  TYR A CA  1 
ATOM   3439  C  C   . TYR A 1 419  ? 30.794 68.073  -8.205  1.00 4.89  ? 419  TYR A C   1 
ATOM   3440  O  O   . TYR A 1 419  ? 31.674 67.899  -9.063  1.00 5.41  ? 419  TYR A O   1 
ATOM   3441  C  CB  . TYR A 1 419  ? 29.373 66.041  -8.333  1.00 4.58  ? 419  TYR A CB  1 
ATOM   3442  C  CG  . TYR A 1 419  ? 28.723 64.854  -7.700  1.00 4.44  ? 419  TYR A CG  1 
ATOM   3443  C  CD1 . TYR A 1 419  ? 29.325 64.168  -6.644  1.00 4.71  ? 419  TYR A CD1 1 
ATOM   3444  C  CD2 . TYR A 1 419  ? 27.553 64.323  -8.245  1.00 3.78  ? 419  TYR A CD2 1 
ATOM   3445  C  CE1 . TYR A 1 419  ? 28.737 63.021  -6.087  1.00 4.93  ? 419  TYR A CE1 1 
ATOM   3446  C  CE2 . TYR A 1 419  ? 26.959 63.210  -7.696  1.00 4.20  ? 419  TYR A CE2 1 
ATOM   3447  C  CZ  . TYR A 1 419  ? 27.568 62.536  -6.658  1.00 4.33  ? 419  TYR A CZ  1 
ATOM   3448  O  OH  . TYR A 1 419  ? 26.986 61.415  -6.120  1.00 5.35  ? 419  TYR A OH  1 
ATOM   3449  N  N   . THR A 1 420  ? 30.297 69.279  -7.889  1.00 5.02  ? 420  THR A N   1 
ATOM   3450  C  CA  . THR A 1 420  ? 30.712 70.498  -8.599  1.00 4.77  ? 420  THR A CA  1 
ATOM   3451  C  C   . THR A 1 420  ? 31.250 71.571  -7.678  1.00 5.63  ? 420  THR A C   1 
ATOM   3452  O  O   . THR A 1 420  ? 32.030 72.401  -8.144  1.00 6.96  ? 420  THR A O   1 
ATOM   3453  C  CB  . THR A 1 420  ? 29.493 71.022  -9.375  1.00 5.63  ? 420  THR A CB  1 
ATOM   3454  O  OG1 . THR A 1 420  ? 29.057 69.981  -10.266 1.00 6.83  ? 420  THR A OG1 1 
ATOM   3455  C  CG2 . THR A 1 420  ? 29.837 72.205  -10.274 1.00 7.52  ? 420  THR A CG2 1 
ATOM   3456  N  N   . SER A 1 421  ? 30.882 71.586  -6.401  1.00 4.83  ? 421  SER A N   1 
ATOM   3457  C  CA  . SER A 1 421  ? 31.255 72.719  -5.565  1.00 4.89  ? 421  SER A CA  1 
ATOM   3458  C  C   . SER A 1 421  ? 32.738 73.069  -5.602  1.00 6.01  ? 421  SER A C   1 
ATOM   3459  O  O   . SER A 1 421  ? 33.588 72.180  -5.534  1.00 6.20  ? 421  SER A O   1 
ATOM   3460  C  CB  . SER A 1 421  ? 30.861 72.436  -4.125  1.00 5.46  ? 421  SER A CB  1 
ATOM   3461  O  OG  . SER A 1 421  ? 29.469 72.249  -4.011  1.00 5.95  ? 421  SER A OG  1 
ATOM   3462  N  N   . ARG A 1 422  ? 33.032 74.370  -5.657  1.00 5.55  ? 422  ARG A N   1 
ATOM   3463  C  CA  . ARG A 1 422  ? 34.423 74.862  -5.712  1.00 6.19  ? 422  ARG A CA  1 
ATOM   3464  C  C   . ARG A 1 422  ? 35.174 74.224  -6.888  1.00 6.19  ? 422  ARG A C   1 
ATOM   3465  O  O   . ARG A 1 422  ? 36.202 73.558  -6.731  1.00 6.11  ? 422  ARG A O   1 
ATOM   3466  C  CB  . ARG A 1 422  ? 35.160 74.628  -4.384  1.00 6.44  ? 422  ARG A CB  1 
ATOM   3467  C  CG  . ARG A 1 422  ? 34.886 75.678  -3.272  1.00 7.08  ? 422  ARG A CG  1 
ATOM   3468  C  CD  . ARG A 1 422  ? 33.420 75.816  -2.827  1.00 6.23  ? 422  ARG A CD  1 
ATOM   3469  N  NE  . ARG A 1 422  ? 33.417 76.809  -1.748  1.00 7.68  ? 422  ARG A NE  1 
ATOM   3470  C  CZ  . ARG A 1 422  ? 33.524 76.515  -0.463  1.00 7.09  ? 422  ARG A CZ  1 
ATOM   3471  N  NH1 . ARG A 1 422  ? 33.443 75.274  -0.049  1.00 7.40  ? 422  ARG A NH1 1 
ATOM   3472  N  NH2 . ARG A 1 422  ? 33.670 77.506  0.428   1.00 6.94  ? 422  ARG A NH2 1 
ATOM   3473  N  N   . PRO A 1 423  ? 34.677 74.438  -8.087  1.00 5.10  ? 423  PRO A N   1 
ATOM   3474  C  CA  . PRO A 1 423  ? 35.270 73.790  -9.258  1.00 5.51  ? 423  PRO A CA  1 
ATOM   3475  C  C   . PRO A 1 423  ? 36.679 74.296  -9.605  1.00 5.72  ? 423  PRO A C   1 
ATOM   3476  O  O   . PRO A 1 423  ? 37.407 73.596  -10.259 1.00 5.25  ? 423  PRO A O   1 
ATOM   3477  C  CB  . PRO A 1 423  ? 34.242 74.095  -10.381 1.00 6.45  ? 423  PRO A CB  1 
ATOM   3478  C  CG  . PRO A 1 423  ? 33.710 75.426  -9.968  1.00 6.34  ? 423  PRO A CG  1 
ATOM   3479  C  CD  . PRO A 1 423  ? 33.535 75.310  -8.447  1.00 5.71  ? 423  PRO A CD  1 
ATOM   3480  N  N   . TYR A 1 424  ? 37.064 75.506  -9.200  1.00 5.67  ? 424  TYR A N   1 
ATOM   3481  C  CA  . TYR A 1 424  ? 38.437 75.956  -9.445  1.00 4.84  ? 424  TYR A CA  1 
ATOM   3482  C  C   . TYR A 1 424  ? 39.405 74.957  -8.799  1.00 4.87  ? 424  TYR A C   1 
ATOM   3483  O  O   . TYR A 1 424  ? 40.406 74.580  -9.420  1.00 5.74  ? 424  TYR A O   1 
ATOM   3484  C  CB  . TYR A 1 424  ? 38.631 77.337  -8.832  1.00 6.44  ? 424  TYR A CB  1 
ATOM   3485  C  CG  . TYR A 1 424  ? 40.011 77.897  -9.038  1.00 5.97  ? 424  TYR A CG  1 
ATOM   3486  C  CD1 . TYR A 1 424  ? 41.043 77.650  -8.139  1.00 7.29  ? 424  TYR A CD1 1 
ATOM   3487  C  CD2 . TYR A 1 424  ? 40.279 78.657  -10.165 1.00 7.83  ? 424  TYR A CD2 1 
ATOM   3488  C  CE1 . TYR A 1 424  ? 42.322 78.208  -8.338  1.00 10.04 ? 424  TYR A CE1 1 
ATOM   3489  C  CE2 . TYR A 1 424  ? 41.528 79.185  -10.383 1.00 10.45 ? 424  TYR A CE2 1 
ATOM   3490  C  CZ  . TYR A 1 424  ? 42.546 78.968  -9.469  1.00 8.92  ? 424  TYR A CZ  1 
ATOM   3491  O  OH  . TYR A 1 424  ? 43.812 79.519  -9.726  1.00 12.86 ? 424  TYR A OH  1 
ATOM   3492  N  N   . HIS A 1 425  ? 39.075 74.522  -7.567  1.00 4.90  ? 425  HIS A N   1 
ATOM   3493  C  CA  . HIS A 1 425  ? 40.013 73.658  -6.842  1.00 4.78  ? 425  HIS A CA  1 
ATOM   3494  C  C   . HIS A 1 425  ? 39.953 72.231  -7.353  1.00 5.26  ? 425  HIS A C   1 
ATOM   3495  O  O   . HIS A 1 425  ? 40.950 71.481  -7.281  1.00 5.16  ? 425  HIS A O   1 
ATOM   3496  C  CB  . HIS A 1 425  ? 39.812 73.808  -5.332  1.00 6.65  ? 425  HIS A CB  1 
ATOM   3497  C  CG  . HIS A 1 425  ? 39.877 75.231  -4.910  1.00 8.18  ? 425  HIS A CG  1 
ATOM   3498  N  ND1 . HIS A 1 425  ? 38.778 76.059  -4.957  1.00 8.23  ? 425  HIS A ND1 1 
ATOM   3499  C  CD2 . HIS A 1 425  ? 40.943 76.022  -4.642  1.00 9.31  ? 425  HIS A CD2 1 
ATOM   3500  C  CE1 . HIS A 1 425  ? 39.152 77.289  -4.635  1.00 7.91  ? 425  HIS A CE1 1 
ATOM   3501  N  NE2 . HIS A 1 425  ? 40.459 77.289  -4.430  1.00 9.33  ? 425  HIS A NE2 1 
ATOM   3502  N  N   . LYS A 1 426  ? 38.766 71.830  -7.830  1.00 4.58  ? 426  LYS A N   1 
ATOM   3503  C  CA  . LYS A 1 426  ? 38.645 70.535  -8.502  1.00 4.89  ? 426  LYS A CA  1 
ATOM   3504  C  C   . LYS A 1 426  ? 39.530 70.447  -9.738  1.00 4.60  ? 426  LYS A C   1 
ATOM   3505  O  O   . LYS A 1 426  ? 40.190 69.440  -9.987  1.00 5.42  ? 426  LYS A O   1 
ATOM   3506  C  CB  . LYS A 1 426  ? 37.193 70.281  -8.867  1.00 5.13  ? 426  LYS A CB  1 
ATOM   3507  C  CG  . LYS A 1 426  ? 36.288 69.938  -7.679  1.00 4.92  ? 426  LYS A CG  1 
ATOM   3508  C  CD  . LYS A 1 426  ? 34.805 69.922  -8.053  1.00 6.09  ? 426  LYS A CD  1 
ATOM   3509  C  CE  . LYS A 1 426  ? 33.948 69.009  -7.177  1.00 7.02  ? 426  LYS A CE  1 
ATOM   3510  N  NZ  . LYS A 1 426  ? 33.886 69.477  -5.738  1.00 6.12  ? 426  LYS A NZ  1 
ATOM   3511  N  N   . ARG A 1 427  ? 39.566 71.526  -10.520 1.00 5.15  ? 427  ARG A N   1 
ATOM   3512  C  CA  . ARG A 1 427  ? 40.456 71.550  -11.646 1.00 5.74  ? 427  ARG A CA  1 
ATOM   3513  C  C   . ARG A 1 427  ? 41.925 71.584  -11.221 1.00 5.60  ? 427  ARG A C   1 
ATOM   3514  O  O   . ARG A 1 427  ? 42.756 70.881  -11.762 1.00 5.60  ? 427  ARG A O   1 
ATOM   3515  C  CB  . ARG A 1 427  ? 40.088 72.768  -12.521 1.00 5.81  ? 427  ARG A CB  1 
ATOM   3516  C  CG  . ARG A 1 427  ? 41.013 73.014  -13.699 1.00 6.55  ? 427  ARG A CG  1 
ATOM   3517  C  CD  . ARG A 1 427  ? 41.094 71.902  -14.741 1.00 8.02  ? 427  ARG A CD  1 
ATOM   3518  N  NE  . ARG A 1 427  ? 42.163 72.275  -15.675 1.00 8.75  ? 427  ARG A NE  1 
ATOM   3519  C  CZ  . ARG A 1 427  ? 42.986 71.433  -16.238 1.00 8.76  ? 427  ARG A CZ  1 
ATOM   3520  N  NH1 . ARG A 1 427  ? 42.897 70.132  -16.046 1.00 9.37  ? 427  ARG A NH1 1 
ATOM   3521  N  NH2 . ARG A 1 427  ? 43.962 71.916  -17.036 1.00 10.17 ? 427  ARG A NH2 1 
ATOM   3522  N  N   . MET A 1 428  ? 42.220 72.380  -10.197 1.00 5.65  ? 428  MET A N   1 
ATOM   3523  C  CA  . MET A 1 428  ? 43.586 72.439  -9.709  1.00 6.16  ? 428  MET A CA  1 
ATOM   3524  C  C   . MET A 1 428  ? 44.066 71.068  -9.247  1.00 6.03  ? 428  MET A C   1 
ATOM   3525  O  O   . MET A 1 428  ? 45.239 70.743  -9.433  1.00 5.99  ? 428  MET A O   1 
ATOM   3526  C  CB  . MET A 1 428  ? 43.653 73.459  -8.555  1.00 7.39  ? 428  MET A CB  1 
ATOM   3527  C  CG  . MET A 1 428  ? 45.062 73.856  -8.162  1.00 6.96  ? 428  MET A CG  1 
ATOM   3528  S  SD  . MET A 1 428  ? 44.956 75.144  -6.877  1.00 9.92  ? 428  MET A SD  1 
ATOM   3529  C  CE  . MET A 1 428  ? 46.668 75.696  -6.769  1.00 9.26  ? 428  MET A CE  1 
ATOM   3530  N  N   . ASP A 1 429  ? 43.188 70.245  -8.660  1.00 6.26  ? 429  ASP A N   1 
ATOM   3531  C  CA  . ASP A 1 429  ? 43.540 68.888  -8.263  1.00 5.79  ? 429  ASP A CA  1 
ATOM   3532  C  C   . ASP A 1 429  ? 44.125 68.108  -9.434  1.00 5.35  ? 429  ASP A C   1 
ATOM   3533  O  O   . ASP A 1 429  ? 45.129 67.392  -9.256  1.00 5.66  ? 429  ASP A O   1 
ATOM   3534  C  CB  . ASP A 1 429  ? 42.293 68.167  -7.744  1.00 6.78  ? 429  ASP A CB  1 
ATOM   3535  C  CG  . ASP A 1 429  ? 42.558 66.723  -7.467  1.00 6.97  ? 429  ASP A CG  1 
ATOM   3536  O  OD1 . ASP A 1 429  ? 43.054 66.459  -6.350  1.00 7.71  ? 429  ASP A OD1 1 
ATOM   3537  O  OD2 . ASP A 1 429  ? 42.266 65.805  -8.277  1.00 7.12  ? 429  ASP A OD2 1 
ATOM   3538  N  N   . ARG A 1 430  ? 43.489 68.217  -10.612 1.00 4.74  ? 430  ARG A N   1 
ATOM   3539  C  CA  . ARG A 1 430  ? 43.925 67.418  -11.737 1.00 5.05  ? 430  ARG A CA  1 
ATOM   3540  C  C   . ARG A 1 430  ? 45.220 67.973  -12.305 1.00 4.38  ? 430  ARG A C   1 
ATOM   3541  O  O   . ARG A 1 430  ? 46.072 67.228  -12.781 1.00 5.65  ? 430  ARG A O   1 
ATOM   3542  C  CB  . ARG A 1 430  ? 42.852 67.414  -12.819 1.00 5.34  ? 430  ARG A CB  1 
ATOM   3543  C  CG  . ARG A 1 430  ? 41.610 66.677  -12.413 1.00 5.25  ? 430  ARG A CG  1 
ATOM   3544  C  CD  . ARG A 1 430  ? 41.871 65.229  -12.002 1.00 5.64  ? 430  ARG A CD  1 
ATOM   3545  N  NE  . ARG A 1 430  ? 40.623 64.465  -12.039 1.00 6.06  ? 430  ARG A NE  1 
ATOM   3546  C  CZ  . ARG A 1 430  ? 39.941 64.094  -10.958 1.00 5.54  ? 430  ARG A CZ  1 
ATOM   3547  N  NH1 . ARG A 1 430  ? 40.329 64.441  -9.733  1.00 5.65  ? 430  ARG A NH1 1 
ATOM   3548  N  NH2 . ARG A 1 430  ? 38.820 63.374  -11.113 1.00 6.11  ? 430  ARG A NH2 1 
ATOM   3549  N  N   . VAL A 1 431  ? 45.411 69.284  -12.236 1.00 4.93  ? 431  VAL A N   1 
ATOM   3550  C  CA  . VAL A 1 431  ? 46.686 69.873  -12.686 1.00 5.06  ? 431  VAL A CA  1 
ATOM   3551  C  C   . VAL A 1 431  ? 47.823 69.399  -11.788 1.00 6.77  ? 431  VAL A C   1 
ATOM   3552  O  O   . VAL A 1 431  ? 48.855 68.947  -12.261 1.00 5.55  ? 431  VAL A O   1 
ATOM   3553  C  CB  . VAL A 1 431  ? 46.567 71.421  -12.694 1.00 5.48  ? 431  VAL A CB  1 
ATOM   3554  C  CG1 . VAL A 1 431  ? 47.920 72.047  -13.006 1.00 7.11  ? 431  VAL A CG1 1 
ATOM   3555  C  CG2 . VAL A 1 431  ? 45.495 71.877  -13.700 1.00 5.96  ? 431  VAL A CG2 1 
ATOM   3556  N  N   . LEU A 1 432  ? 47.618 69.467  -10.496 1.00 5.11  ? 432  LEU A N   1 
ATOM   3557  C  CA  . LEU A 1 432  ? 48.661 69.058  -9.575  1.00 5.07  ? 432  LEU A CA  1 
ATOM   3558  C  C   . LEU A 1 432  ? 48.884 67.554  -9.676  1.00 4.67  ? 432  LEU A C   1 
ATOM   3559  O  O   . LEU A 1 432  ? 50.032 67.085  -9.587  1.00 5.98  ? 432  LEU A O   1 
ATOM   3560  C  CB  . LEU A 1 432  ? 48.299 69.476  -8.162  1.00 5.91  ? 432  LEU A CB  1 
ATOM   3561  C  CG  . LEU A 1 432  ? 49.295 69.100  -7.077  1.00 5.93  ? 432  LEU A CG  1 
ATOM   3562  C  CD1 . LEU A 1 432  ? 50.701 69.679  -7.345  1.00 6.97  ? 432  LEU A CD1 1 
ATOM   3563  C  CD2 . LEU A 1 432  ? 48.802 69.653  -5.763  1.00 6.32  ? 432  LEU A CD2 1 
ATOM   3564  N  N   . MET A 1 433  ? 47.816 66.771  -9.877  1.00 4.78  ? 433  MET A N   1 
ATOM   3565  C  CA  . MET A 1 433  ? 47.992 65.326  -10.072 1.00 5.27  ? 433  MET A CA  1 
ATOM   3566  C  C   . MET A 1 433  ? 49.054 65.023  -11.137 1.00 4.51  ? 433  MET A C   1 
ATOM   3567  O  O   . MET A 1 433  ? 49.914 64.183  -10.986 1.00 5.34  ? 433  MET A O   1 
ATOM   3568  C  CB  . MET A 1 433  ? 46.656 64.730  -10.553 1.00 5.73  ? 433  MET A CB  1 
ATOM   3569  C  CG  . MET A 1 433  ? 46.727 63.235  -10.826 1.00 7.06  ? 433  MET A CG  1 
ATOM   3570  S  SD  . MET A 1 433  ? 45.175 62.552  -11.508 1.00 10.05 ? 433  MET A SD  1 
ATOM   3571  C  CE  . MET A 1 433  ? 45.204 63.264  -13.090 1.00 10.25 ? 433  MET A CE  1 
ATOM   3572  N  N   . HIS A 1 434  ? 48.903 65.703  -12.264 1.00 4.73  ? 434  HIS A N   1 
ATOM   3573  C  CA  . HIS A 1 434  ? 49.812 65.489  -13.367 1.00 5.09  ? 434  HIS A CA  1 
ATOM   3574  C  C   . HIS A 1 434  ? 51.224 65.976  -13.057 1.00 4.97  ? 434  HIS A C   1 
ATOM   3575  O  O   . HIS A 1 434  ? 52.215 65.321  -13.397 1.00 5.39  ? 434  HIS A O   1 
ATOM   3576  C  CB  . HIS A 1 434  ? 49.276 66.186  -14.621 1.00 6.26  ? 434  HIS A CB  1 
ATOM   3577  C  CG  . HIS A 1 434  ? 50.300 66.220  -15.720 1.00 6.53  ? 434  HIS A CG  1 
ATOM   3578  N  ND1 . HIS A 1 434  ? 50.637 65.103  -16.454 1.00 8.84  ? 434  HIS A ND1 1 
ATOM   3579  C  CD2 . HIS A 1 434  ? 51.155 67.201  -16.088 1.00 9.45  ? 434  HIS A CD2 1 
ATOM   3580  C  CE1 . HIS A 1 434  ? 51.637 65.412  -17.271 1.00 8.55  ? 434  HIS A CE1 1 
ATOM   3581  N  NE2 . HIS A 1 434  ? 51.956 66.680  -17.081 1.00 8.76  ? 434  HIS A NE2 1 
ATOM   3582  N  N   A TYR A 1 435  ? 51.298 67.144  -12.407 0.50 4.92  ? 435  TYR A N   1 
ATOM   3583  N  N   B TYR A 1 435  ? 51.325 67.121  -12.416 0.50 3.95  ? 435  TYR A N   1 
ATOM   3584  C  CA  A TYR A 1 435  ? 52.588 67.750  -12.019 0.60 5.65  ? 435  TYR A CA  1 
ATOM   3585  C  CA  B TYR A 1 435  ? 52.639 67.650  -12.110 0.40 3.81  ? 435  TYR A CA  1 
ATOM   3586  C  C   A TYR A 1 435  ? 53.370 66.875  -11.051 0.50 5.69  ? 435  TYR A C   1 
ATOM   3587  C  C   B TYR A 1 435  ? 53.390 66.827  -11.067 0.50 4.63  ? 435  TYR A C   1 
ATOM   3588  O  O   A TYR A 1 435  ? 54.598 66.820  -11.126 0.50 5.20  ? 435  TYR A O   1 
ATOM   3589  O  O   B TYR A 1 435  ? 54.583 66.708  -11.149 0.50 4.53  ? 435  TYR A O   1 
ATOM   3590  C  CB  A TYR A 1 435  ? 52.387 69.166  -11.409 0.60 7.44  ? 435  TYR A CB  1 
ATOM   3591  C  CB  B TYR A 1 435  ? 52.557 69.145  -11.794 0.40 4.03  ? 435  TYR A CB  1 
ATOM   3592  C  CG  A TYR A 1 435  ? 52.339 70.272  -12.437 0.60 9.39  ? 435  TYR A CG  1 
ATOM   3593  C  CG  B TYR A 1 435  ? 52.428 69.973  -13.062 0.40 4.08  ? 435  TYR A CG  1 
ATOM   3594  C  CD1 A TYR A 1 435  ? 51.510 70.164  -13.555 0.60 8.50  ? 435  TYR A CD1 1 
ATOM   3595  C  CD1 B TYR A 1 435  ? 53.351 69.863  -14.089 0.40 4.77  ? 435  TYR A CD1 1 
ATOM   3596  C  CD2 A TYR A 1 435  ? 53.099 71.437  -12.289 0.60 12.79 ? 435  TYR A CD2 1 
ATOM   3597  C  CD2 B TYR A 1 435  ? 51.380 70.809  -13.250 0.40 3.86  ? 435  TYR A CD2 1 
ATOM   3598  C  CE1 A TYR A 1 435  ? 51.458 71.159  -14.538 0.60 12.18 ? 435  TYR A CE1 1 
ATOM   3599  C  CE1 B TYR A 1 435  ? 53.242 70.625  -15.255 0.40 5.80  ? 435  TYR A CE1 1 
ATOM   3600  C  CE2 A TYR A 1 435  ? 53.056 72.448  -13.253 0.60 14.46 ? 435  TYR A CE2 1 
ATOM   3601  C  CE2 B TYR A 1 435  ? 51.266 71.577  -14.390 0.40 2.75  ? 435  TYR A CE2 1 
ATOM   3602  C  CZ  A TYR A 1 435  ? 52.231 72.299  -14.377 0.60 10.74 ? 435  TYR A CZ  1 
ATOM   3603  C  CZ  B TYR A 1 435  ? 52.189 71.472  -15.381 0.40 3.66  ? 435  TYR A CZ  1 
ATOM   3604  O  OH  A TYR A 1 435  ? 52.182 73.278  -15.356 0.60 14.33 ? 435  TYR A OH  1 
ATOM   3605  O  OH  B TYR A 1 435  ? 52.049 72.234  -16.520 0.40 4.90  ? 435  TYR A OH  1 
ATOM   3606  N  N   . VAL A 1 436  ? 52.666 66.194  -10.158 1.00 4.76  ? 436  VAL A N   1 
ATOM   3607  C  CA  . VAL A 1 436  ? 53.322 65.288  -9.211  1.00 4.65  ? 436  VAL A CA  1 
ATOM   3608  C  C   . VAL A 1 436  ? 53.836 64.074  -9.974  1.00 4.87  ? 436  VAL A C   1 
ATOM   3609  O  O   . VAL A 1 436  ? 55.001 63.678  -9.805  1.00 5.24  ? 436  VAL A O   1 
ATOM   3610  C  CB  . VAL A 1 436  ? 52.371 64.902  -8.086  1.00 4.66  ? 436  VAL A CB  1 
ATOM   3611  C  CG1 . VAL A 1 436  ? 52.869 63.664  -7.316  1.00 6.47  ? 436  VAL A CG1 1 
ATOM   3612  C  CG2 . VAL A 1 436  ? 52.169 66.087  -7.146  1.00 5.37  ? 436  VAL A CG2 1 
ATOM   3613  N  N   . ARG A 1 437  ? 53.016 63.514  -10.847 1.00 4.83  ? 437  ARG A N   1 
ATOM   3614  C  CA  . ARG A 1 437  ? 53.467 62.357  -11.619 1.00 5.07  ? 437  ARG A CA  1 
ATOM   3615  C  C   . ARG A 1 437  ? 54.706 62.728  -12.428 1.00 5.71  ? 437  ARG A C   1 
ATOM   3616  O  O   . ARG A 1 437  ? 55.696 61.969  -12.488 1.00 5.73  ? 437  ARG A O   1 
ATOM   3617  C  CB  . ARG A 1 437  ? 52.382 61.865  -12.559 1.00 5.43  ? 437  ARG A CB  1 
ATOM   3618  C  CG  . ARG A 1 437  ? 52.885 60.835  -13.582 1.00 8.20  ? 437  ARG A CG  1 
ATOM   3619  C  CD  . ARG A 1 437  ? 51.777 60.406  -14.489 1.00 9.35  ? 437  ARG A CD  1 
ATOM   3620  N  NE  . ARG A 1 437  ? 52.309 59.673  -15.627 1.00 7.85  ? 437  ARG A NE  1 
ATOM   3621  C  CZ  . ARG A 1 437  ? 51.587 58.849  -16.346 1.00 9.41  ? 437  ARG A CZ  1 
ATOM   3622  N  NH1 . ARG A 1 437  ? 50.310 58.584  -16.019 1.00 9.33  ? 437  ARG A NH1 1 
ATOM   3623  N  NH2 . ARG A 1 437  ? 52.148 58.253  -17.383 1.00 8.13  ? 437  ARG A NH2 1 
ATOM   3624  N  N   . ALA A 1 438  ? 54.656 63.877  -13.117 1.00 4.81  ? 438  ALA A N   1 
ATOM   3625  C  CA  . ALA A 1 438  ? 55.767 64.265  -13.978 1.00 5.73  ? 438  ALA A CA  1 
ATOM   3626  C  C   . ALA A 1 438  ? 57.034 64.548  -13.174 1.00 5.15  ? 438  ALA A C   1 
ATOM   3627  O  O   . ALA A 1 438  ? 58.129 64.192  -13.629 1.00 6.17  ? 438  ALA A O   1 
ATOM   3628  C  CB  . ALA A 1 438  ? 55.383 65.477  -14.819 1.00 6.33  ? 438  ALA A CB  1 
ATOM   3629  N  N   . ALA A 1 439  ? 56.913 65.237  -12.026 1.00 5.29  ? 439  ALA A N   1 
ATOM   3630  C  CA  . ALA A 1 439  ? 58.075 65.533  -11.198 1.00 5.80  ? 439  ALA A CA  1 
ATOM   3631  C  C   . ALA A 1 439  ? 58.691 64.249  -10.658 1.00 5.73  ? 439  ALA A C   1 
ATOM   3632  O  O   . ALA A 1 439  ? 59.923 64.112  -10.622 1.00 6.05  ? 439  ALA A O   1 
ATOM   3633  C  CB  . ALA A 1 439  ? 57.711 66.455  -10.086 1.00 5.71  ? 439  ALA A CB  1 
ATOM   3634  N  N   . GLU A 1 440  ? 57.858 63.312  -10.202 1.00 5.50  ? 440  GLU A N   1 
ATOM   3635  C  CA  . GLU A 1 440  ? 58.408 62.062  -9.686  1.00 6.17  ? 440  GLU A CA  1 
ATOM   3636  C  C   . GLU A 1 440  ? 59.081 61.275  -10.809 1.00 5.40  ? 440  GLU A C   1 
ATOM   3637  O  O   . GLU A 1 440  ? 60.133 60.663  -10.584 1.00 6.40  ? 440  GLU A O   1 
ATOM   3638  C  CB  . GLU A 1 440  ? 57.324 61.217  -8.986  1.00 7.14  ? 440  GLU A CB  1 
ATOM   3639  C  CG  . GLU A 1 440  ? 56.779 61.844  -7.724  1.00 8.15  ? 440  GLU A CG  1 
ATOM   3640  C  CD  . GLU A 1 440  ? 56.114 60.842  -6.819  1.00 12.60 ? 440  GLU A CD  1 
ATOM   3641  O  OE1 . GLU A 1 440  ? 55.006 60.369  -7.138  1.00 12.65 ? 440  GLU A OE1 1 
ATOM   3642  O  OE2 . GLU A 1 440  ? 56.717 60.550  -5.784  1.00 12.53 ? 440  GLU A OE2 1 
ATOM   3643  N  N   . MET A 1 441  ? 58.474 61.227  -11.988 1.00 5.16  ? 441  MET A N   1 
ATOM   3644  C  CA  . MET A 1 441  ? 59.041 60.472  -13.095 1.00 5.64  ? 441  MET A CA  1 
ATOM   3645  C  C   . MET A 1 441  ? 60.339 61.109  -13.621 1.00 5.81  ? 441  MET A C   1 
ATOM   3646  O  O   . MET A 1 441  ? 61.370 60.412  -13.724 1.00 6.58  ? 441  MET A O   1 
ATOM   3647  C  CB  . MET A 1 441  ? 58.003 60.340  -14.225 1.00 6.84  ? 441  MET A CB  1 
ATOM   3648  C  CG  . MET A 1 441  ? 58.542 59.604  -15.435 1.00 7.60  ? 441  MET A CG  1 
ATOM   3649  S  SD  . MET A 1 441  ? 57.272 59.410  -16.727 1.00 8.08  ? 441  MET A SD  1 
ATOM   3650  C  CE  . MET A 1 441  ? 56.147 58.221  -15.855 1.00 9.29  ? 441  MET A CE  1 
ATOM   3651  N  N   . LEU A 1 442  ? 60.315 62.412  -13.884 1.00 4.97  ? 442  LEU A N   1 
ATOM   3652  C  CA  . LEU A 1 442  ? 61.503 63.085  -14.395 1.00 6.85  ? 442  LEU A CA  1 
ATOM   3653  C  C   . LEU A 1 442  ? 62.683 62.961  -13.473 1.00 6.78  ? 442  LEU A C   1 
ATOM   3654  O  O   . LEU A 1 442  ? 63.836 62.814  -13.918 1.00 7.49  ? 442  LEU A O   1 
ATOM   3655  C  CB  . LEU A 1 442  ? 61.206 64.560  -14.659 1.00 6.46  ? 442  LEU A CB  1 
ATOM   3656  C  CG  . LEU A 1 442  ? 60.586 64.806  -16.045 1.00 6.87  ? 442  LEU A CG  1 
ATOM   3657  C  CD1 . LEU A 1 442  ? 59.917 66.158  -16.086 1.00 9.30  ? 442  LEU A CD1 1 
ATOM   3658  C  CD2 . LEU A 1 442  ? 61.685 64.729  -17.128 1.00 8.81  ? 442  LEU A CD2 1 
ATOM   3659  N  N   . SER A 1 443  ? 62.438 63.055  -12.170 1.00 4.82  ? 443  SER A N   1 
ATOM   3660  C  CA  . SER A 1 443  ? 63.540 62.992  -11.223 1.00 6.26  ? 443  SER A CA  1 
ATOM   3661  C  C   . SER A 1 443  ? 63.947 61.583  -10.876 1.00 7.18  ? 443  SER A C   1 
ATOM   3662  O  O   . SER A 1 443  ? 65.073 61.411  -10.370 1.00 8.08  ? 443  SER A O   1 
ATOM   3663  C  CB  . SER A 1 443  ? 63.267 63.801  -9.978  1.00 6.98  ? 443  SER A CB  1 
ATOM   3664  O  OG  . SER A 1 443  ? 62.176 63.257  -9.246  1.00 7.02  ? 443  SER A OG  1 
ATOM   3665  N  N   . ALA A 1 444  ? 63.136 60.581  -11.219 1.00 5.58  ? 444  ALA A N   1 
ATOM   3666  C  CA  . ALA A 1 444  ? 63.444 59.185  -10.903 1.00 7.56  ? 444  ALA A CA  1 
ATOM   3667  C  C   . ALA A 1 444  ? 64.628 58.667  -11.674 1.00 7.99  ? 444  ALA A C   1 
ATOM   3668  O  O   . ALA A 1 444  ? 65.251 57.673  -11.249 1.00 9.07  ? 444  ALA A O   1 
ATOM   3669  C  CB  . ALA A 1 444  ? 62.217 58.308  -11.214 1.00 7.10  ? 444  ALA A CB  1 
ATOM   3670  N  N   . TRP A 1 445  ? 64.889 59.243  -12.844 1.00 7.87  ? 445  TRP A N   1 
ATOM   3671  C  CA  . TRP A 1 445  ? 65.942 58.709  -13.717 1.00 8.51  ? 445  TRP A CA  1 
ATOM   3672  C  C   . TRP A 1 445  ? 67.344 58.769  -13.124 1.00 8.43  ? 445  TRP A C   1 
ATOM   3673  O  O   . TRP A 1 445  ? 68.195 57.961  -13.502 1.00 10.31 ? 445  TRP A O   1 
ATOM   3674  C  CB  . TRP A 1 445  ? 65.945 59.479  -15.045 1.00 8.68  ? 445  TRP A CB  1 
ATOM   3675  C  CG  . TRP A 1 445  ? 64.663 59.293  -15.844 1.00 6.23  ? 445  TRP A CG  1 
ATOM   3676  C  CD1 . TRP A 1 445  ? 63.660 60.233  -16.008 1.00 7.34  ? 445  TRP A CD1 1 
ATOM   3677  C  CD2 . TRP A 1 445  ? 64.216 58.114  -16.510 1.00 6.12  ? 445  TRP A CD2 1 
ATOM   3678  N  NE1 . TRP A 1 445  ? 62.642 59.695  -16.755 1.00 6.96  ? 445  TRP A NE1 1 
ATOM   3679  C  CE2 . TRP A 1 445  ? 62.950 58.396  -17.074 1.00 5.73  ? 445  TRP A CE2 1 
ATOM   3680  C  CE3 . TRP A 1 445  ? 64.760 56.839  -16.722 1.00 8.22  ? 445  TRP A CE3 1 
ATOM   3681  C  CZ2 . TRP A 1 445  ? 62.248 57.473  -17.832 1.00 7.48  ? 445  TRP A CZ2 1 
ATOM   3682  C  CZ3 . TRP A 1 445  ? 64.048 55.919  -17.489 1.00 9.00  ? 445  TRP A CZ3 1 
ATOM   3683  C  CH2 . TRP A 1 445  ? 62.811 56.235  -18.023 1.00 8.52  ? 445  TRP A CH2 1 
ATOM   3684  N  N   . HIS A 1 446  ? 67.546 59.705  -12.198 1.00 8.42  ? 446  HIS A N   1 
ATOM   3685  C  CA  . HIS A 1 446  ? 68.824 59.863  -11.535 1.00 10.77 ? 446  HIS A CA  1 
ATOM   3686  C  C   . HIS A 1 446  ? 68.675 59.752  -10.042 1.00 10.15 ? 446  HIS A C   1 
ATOM   3687  O  O   . HIS A 1 446  ? 67.621 60.001  -9.489  1.00 9.61  ? 446  HIS A O   1 
ATOM   3688  C  CB  . HIS A 1 446  ? 69.399 61.249  -11.788 1.00 11.10 ? 446  HIS A CB  1 
ATOM   3689  C  CG  . HIS A 1 446  ? 69.821 61.484  -13.199 1.00 13.74 ? 446  HIS A CG  1 
ATOM   3690  N  ND1 . HIS A 1 446  ? 69.032 62.158  -14.107 1.00 17.71 ? 446  HIS A ND1 1 
ATOM   3691  C  CD2 . HIS A 1 446  ? 70.959 61.150  -13.855 1.00 17.19 ? 446  HIS A CD2 1 
ATOM   3692  C  CE1 . HIS A 1 446  ? 69.659 62.222  -15.265 1.00 20.42 ? 446  HIS A CE1 1 
ATOM   3693  N  NE2 . HIS A 1 446  ? 70.825 61.615  -15.145 1.00 17.53 ? 446  HIS A NE2 1 
ATOM   3694  N  N   . SER A 1 447  ? 69.798 59.432  -9.394  1.00 11.47 ? 447  SER A N   1 
ATOM   3695  C  CA  A SER A 1 447  ? 69.985 59.642  -7.987  0.50 11.05 ? 447  SER A CA  1 
ATOM   3696  C  CA  B SER A 1 447  ? 69.971 59.663  -7.964  0.50 11.18 ? 447  SER A CA  1 
ATOM   3697  C  C   . SER A 1 447  ? 70.425 61.092  -7.762  1.00 11.49 ? 447  SER A C   1 
ATOM   3698  O  O   . SER A 1 447  ? 71.255 61.621  -8.545  1.00 12.65 ? 447  SER A O   1 
ATOM   3699  C  CB  A SER A 1 447  ? 71.076 58.695  -7.525  0.50 12.78 ? 447  SER A CB  1 
ATOM   3700  C  CB  B SER A 1 447  ? 71.022 58.734  -7.357  0.50 12.86 ? 447  SER A CB  1 
ATOM   3701  O  OG  A SER A 1 447  ? 71.006 58.543  -6.141  0.50 11.70 ? 447  SER A OG  1 
ATOM   3702  O  OG  B SER A 1 447  ? 70.433 57.594  -6.773  0.50 12.74 ? 447  SER A OG  1 
ATOM   3703  N  N   . TRP A 1 448  ? 69.893 61.743  -6.742  1.00 9.95  ? 448  TRP A N   1 
ATOM   3704  C  CA  . TRP A 1 448  ? 70.234 63.135  -6.528  1.00 11.23 ? 448  TRP A CA  1 
ATOM   3705  C  C   . TRP A 1 448  ? 70.940 63.336  -5.203  1.00 12.32 ? 448  TRP A C   1 
ATOM   3706  O  O   . TRP A 1 448  ? 70.538 62.764  -4.191  1.00 12.45 ? 448  TRP A O   1 
ATOM   3707  C  CB  . TRP A 1 448  ? 68.966 63.995  -6.559  1.00 9.66  ? 448  TRP A CB  1 
ATOM   3708  C  CG  . TRP A 1 448  ? 68.324 64.037  -7.905  1.00 9.62  ? 448  TRP A CG  1 
ATOM   3709  C  CD1 . TRP A 1 448  ? 67.459 63.123  -8.414  1.00 9.80  ? 448  TRP A CD1 1 
ATOM   3710  C  CD2 . TRP A 1 448  ? 68.495 65.045  -8.904  1.00 9.37  ? 448  TRP A CD2 1 
ATOM   3711  N  NE1 . TRP A 1 448  ? 67.077 63.486  -9.679  1.00 9.21  ? 448  TRP A NE1 1 
ATOM   3712  C  CE2 . TRP A 1 448  ? 67.672 64.685  -9.997  1.00 7.99  ? 448  TRP A CE2 1 
ATOM   3713  C  CE3 . TRP A 1 448  ? 69.242 66.237  -8.980  1.00 10.67 ? 448  TRP A CE3 1 
ATOM   3714  C  CZ2 . TRP A 1 448  ? 67.607 65.437  -11.159 1.00 10.27 ? 448  TRP A CZ2 1 
ATOM   3715  C  CZ3 . TRP A 1 448  ? 69.146 67.004  -10.133 1.00 9.15  ? 448  TRP A CZ3 1 
ATOM   3716  C  CH2 . TRP A 1 448  ? 68.337 66.584  -11.212 1.00 10.59 ? 448  TRP A CH2 1 
ATOM   3717  N  N   . ASP A 1 449  ? 71.989 64.166  -5.206  1.00 14.46 ? 449  ASP A N   1 
ATOM   3718  C  CA  . ASP A 1 449  ? 72.605 64.601  -3.970  1.00 15.82 ? 449  ASP A CA  1 
ATOM   3719  C  C   . ASP A 1 449  ? 71.548 65.222  -3.051  1.00 15.27 ? 449  ASP A C   1 
ATOM   3720  O  O   . ASP A 1 449  ? 70.641 65.898  -3.524  1.00 14.17 ? 449  ASP A O   1 
ATOM   3721  C  CB  . ASP A 1 449  ? 73.671 65.653  -4.274  1.00 17.75 ? 449  ASP A CB  1 
ATOM   3722  C  CG  . ASP A 1 449  ? 74.482 66.003  -3.058  1.00 21.17 ? 449  ASP A CG  1 
ATOM   3723  O  OD1 . ASP A 1 449  ? 75.432 65.244  -2.746  1.00 28.88 ? 449  ASP A OD1 1 
ATOM   3724  O  OD2 . ASP A 1 449  ? 74.234 66.984  -2.332  1.00 23.41 ? 449  ASP A OD2 1 
ATOM   3725  N  N   . GLY A 1 450  ? 71.697 65.060  -1.740  1.00 15.46 ? 450  GLY A N   1 
ATOM   3726  C  CA  . GLY A 1 450  ? 70.772 65.657  -0.788  1.00 16.18 ? 450  GLY A CA  1 
ATOM   3727  C  C   . GLY A 1 450  ? 70.653 67.166  -0.875  1.00 15.88 ? 450  GLY A C   1 
ATOM   3728  O  O   . GLY A 1 450  ? 69.604 67.747  -0.540  1.00 16.04 ? 450  GLY A O   1 
ATOM   3729  N  N   . MET A 1 451  ? 71.711 67.824  -1.359  1.00 15.75 ? 451  MET A N   1 
ATOM   3730  C  CA  . MET A 1 451  ? 71.688 69.273  -1.486  1.00 16.42 ? 451  MET A CA  1 
ATOM   3731  C  C   . MET A 1 451  ? 70.692 69.770  -2.535  1.00 15.04 ? 451  MET A C   1 
ATOM   3732  O  O   . MET A 1 451  ? 70.314 70.946  -2.534  1.00 16.07 ? 451  MET A O   1 
ATOM   3733  C  CB  . MET A 1 451  ? 73.091 69.818  -1.797  1.00 17.84 ? 451  MET A CB  1 
ATOM   3734  C  CG  . MET A 1 451  ? 74.078 69.681  -0.641  1.00 22.52 ? 451  MET A CG  1 
ATOM   3735  S  SD  . MET A 1 451  ? 73.514 70.562  0.840   1.00 35.43 ? 451  MET A SD  1 
ATOM   3736  C  CE  . MET A 1 451  ? 73.446 72.290  0.203   1.00 32.99 ? 451  MET A CE  1 
ATOM   3737  N  N   . ALA A 1 452  ? 70.258 68.871  -3.427  1.00 13.35 ? 452  ALA A N   1 
ATOM   3738  C  CA  . ALA A 1 452  ? 69.325 69.239  -4.489  1.00 13.07 ? 452  ALA A CA  1 
ATOM   3739  C  C   . ALA A 1 452  ? 67.897 69.362  -3.944  1.00 12.86 ? 452  ALA A C   1 
ATOM   3740  O  O   . ALA A 1 452  ? 67.046 69.975  -4.591  1.00 13.54 ? 452  ALA A O   1 
ATOM   3741  C  CB  . ALA A 1 452  ? 69.360 68.237  -5.631  1.00 12.93 ? 452  ALA A CB  1 
ATOM   3742  N  N   . ARG A 1 453  ? 67.666 68.794  -2.752  1.00 11.85 ? 453  ARG A N   1 
ATOM   3743  C  CA  . ARG A 1 453  ? 66.378 68.911  -2.046  1.00 11.92 ? 453  ARG A CA  1 
ATOM   3744  C  C   . ARG A 1 453  ? 65.245 68.311  -2.857  1.00 11.22 ? 453  ARG A C   1 
ATOM   3745  O  O   . ARG A 1 453  ? 64.095 68.740  -2.728  1.00 12.10 ? 453  ARG A O   1 
ATOM   3746  C  CB  . ARG A 1 453  ? 66.065 70.361  -1.695  1.00 12.59 ? 453  ARG A CB  1 
ATOM   3747  C  CG  . ARG A 1 453  ? 67.121 70.991  -0.821  1.00 15.09 ? 453  ARG A CG  1 
ATOM   3748  C  CD  . ARG A 1 453  ? 66.908 72.474  -0.619  1.00 18.97 ? 453  ARG A CD  1 
ATOM   3749  N  NE  . ARG A 1 453  ? 65.736 72.730  0.209   1.00 20.16 ? 453  ARG A NE  1 
ATOM   3750  C  CZ  . ARG A 1 453  ? 65.216 73.939  0.390   1.00 21.16 ? 453  ARG A CZ  1 
ATOM   3751  N  NH1 . ARG A 1 453  ? 65.757 75.006  -0.216  1.00 21.72 ? 453  ARG A NH1 1 
ATOM   3752  N  NH2 . ARG A 1 453  ? 64.148 74.080  1.156   1.00 23.05 ? 453  ARG A NH2 1 
ATOM   3753  N  N   . ILE A 1 454  ? 65.542 67.311  -3.675  1.00 9.12  ? 454  ILE A N   1 
ATOM   3754  C  CA  . ILE A 1 454  ? 64.520 66.701  -4.524  1.00 9.21  ? 454  ILE A CA  1 
ATOM   3755  C  C   . ILE A 1 454  ? 63.532 65.934  -3.650  1.00 9.53  ? 454  ILE A C   1 
ATOM   3756  O  O   . ILE A 1 454  ? 62.311 66.101  -3.797  1.00 9.10  ? 454  ILE A O   1 
ATOM   3757  C  CB  . ILE A 1 454  ? 65.183 65.769  -5.552  1.00 9.86  ? 454  ILE A CB  1 
ATOM   3758  C  CG1 . ILE A 1 454  ? 66.138 66.547  -6.479  1.00 11.14 ? 454  ILE A CG1 1 
ATOM   3759  C  CG2 . ILE A 1 454  ? 64.152 64.955  -6.320  1.00 10.89 ? 454  ILE A CG2 1 
ATOM   3760  C  CD1 . ILE A 1 454  ? 65.481 67.523  -7.395  1.00 12.01 ? 454  ILE A CD1 1 
ATOM   3761  N  N   . GLU A 1 455  ? 64.009 65.078  -2.764  1.00 9.33  ? 455  GLU A N   1 
ATOM   3762  C  CA  . GLU A 1 455  ? 63.092 64.292  -1.932  1.00 9.67  ? 455  GLU A CA  1 
ATOM   3763  C  C   . GLU A 1 455  ? 62.233 65.184  -1.065  1.00 9.55  ? 455  GLU A C   1 
ATOM   3764  O  O   . GLU A 1 455  ? 61.029 64.914  -0.913  1.00 8.91  ? 455  GLU A O   1 
ATOM   3765  C  CB  . GLU A 1 455  ? 63.867 63.309  -1.040  1.00 10.55 ? 455  GLU A CB  1 
ATOM   3766  C  CG  . GLU A 1 455  ? 64.471 62.137  -1.803  1.00 12.79 ? 455  GLU A CG  1 
ATOM   3767  C  CD  . GLU A 1 455  ? 65.856 62.434  -2.416  1.00 15.13 ? 455  GLU A CD  1 
ATOM   3768  O  OE1 . GLU A 1 455  ? 66.341 63.596  -2.281  1.00 14.70 ? 455  GLU A OE1 1 
ATOM   3769  O  OE2 . GLU A 1 455  ? 66.418 61.493  -3.013  1.00 12.83 ? 455  GLU A OE2 1 
ATOM   3770  N  N   . GLU A 1 456  ? 62.790 66.255  -0.518  1.00 9.78  ? 456  GLU A N   1 
ATOM   3771  C  CA  . GLU A 1 456  ? 62.047 67.204  0.280   1.00 11.15 ? 456  GLU A CA  1 
ATOM   3772  C  C   . GLU A 1 456  ? 60.915 67.824  -0.547  1.00 9.71  ? 456  GLU A C   1 
ATOM   3773  O  O   . GLU A 1 456  ? 59.770 67.918  -0.073  1.00 10.15 ? 456  GLU A O   1 
ATOM   3774  C  CB  . GLU A 1 456  ? 62.989 68.317  0.768   1.00 11.93 ? 456  GLU A CB  1 
ATOM   3775  C  CG  . GLU A 1 456  ? 62.354 69.443  1.541   1.00 15.58 ? 456  GLU A CG  1 
ATOM   3776  C  CD  . GLU A 1 456  ? 63.303 70.621  1.732   1.00 16.81 ? 456  GLU A CD  1 
ATOM   3777  O  OE1 . GLU A 1 456  ? 64.533 70.453  1.523   1.00 21.61 ? 456  GLU A OE1 1 
ATOM   3778  O  OE2 . GLU A 1 456  ? 62.817 71.716  2.099   1.00 22.76 ? 456  GLU A OE2 1 
ATOM   3779  N  N   . ARG A 1 457  ? 61.220 68.320  -1.743  1.00 7.90  ? 457  ARG A N   1 
ATOM   3780  C  CA  . ARG A 1 457  ? 60.182 68.994  -2.552  1.00 7.63  ? 457  ARG A CA  1 
ATOM   3781  C  C   . ARG A 1 457  ? 59.118 68.002  -2.999  1.00 7.95  ? 457  ARG A C   1 
ATOM   3782  O  O   . ARG A 1 457  ? 57.933 68.336  -2.997  1.00 7.36  ? 457  ARG A O   1 
ATOM   3783  C  CB  . ARG A 1 457  ? 60.804 69.714  -3.766  1.00 7.35  ? 457  ARG A CB  1 
ATOM   3784  C  CG  . ARG A 1 457  ? 61.152 71.156  -3.513  1.00 11.41 ? 457  ARG A CG  1 
ATOM   3785  C  CD  . ARG A 1 457  ? 62.149 71.412  -2.418  1.00 13.70 ? 457  ARG A CD  1 
ATOM   3786  N  NE  . ARG A 1 457  ? 62.392 72.842  -2.170  1.00 14.04 ? 457  ARG A NE  1 
ATOM   3787  C  CZ  . ARG A 1 457  ? 63.298 73.580  -2.798  1.00 18.53 ? 457  ARG A CZ  1 
ATOM   3788  N  NH1 . ARG A 1 457  ? 64.060 73.074  -3.774  1.00 17.16 ? 457  ARG A NH1 1 
ATOM   3789  N  NH2 . ARG A 1 457  ? 63.412 74.860  -2.458  1.00 20.43 ? 457  ARG A NH2 1 
ATOM   3790  N  N   . LEU A 1 458  ? 59.503 66.773  -3.332  1.00 6.65  ? 458  LEU A N   1 
ATOM   3791  C  CA  . LEU A 1 458  ? 58.510 65.786  -3.777  1.00 6.59  ? 458  LEU A CA  1 
ATOM   3792  C  C   . LEU A 1 458  ? 57.649 65.376  -2.620  1.00 7.74  ? 458  LEU A C   1 
ATOM   3793  O  O   . LEU A 1 458  ? 56.449 65.189  -2.812  1.00 8.19  ? 458  LEU A O   1 
ATOM   3794  C  CB  . LEU A 1 458  ? 59.186 64.559  -4.363  1.00 5.98  ? 458  LEU A CB  1 
ATOM   3795  C  CG  . LEU A 1 458  ? 59.886 64.827  -5.711  1.00 7.64  ? 458  LEU A CG  1 
ATOM   3796  C  CD1 . LEU A 1 458  ? 60.636 63.581  -6.112  1.00 9.73  ? 458  LEU A CD1 1 
ATOM   3797  C  CD2 . LEU A 1 458  ? 58.822 65.160  -6.773  1.00 9.57  ? 458  LEU A CD2 1 
ATOM   3798  N  N   . GLU A 1 459  ? 58.223 65.239  -1.432  1.00 7.08  ? 459  GLU A N   1 
ATOM   3799  C  CA  . GLU A 1 459  ? 57.398 64.828  -0.292  1.00 8.01  ? 459  GLU A CA  1 
ATOM   3800  C  C   . GLU A 1 459  ? 56.366 65.908  0.020   1.00 8.08  ? 459  GLU A C   1 
ATOM   3801  O  O   . GLU A 1 459  ? 55.191 65.620  0.260   1.00 7.37  ? 459  GLU A O   1 
ATOM   3802  C  CB  . GLU A 1 459  ? 58.279 64.577  0.931   1.00 9.18  ? 459  GLU A CB  1 
ATOM   3803  C  CG  . GLU A 1 459  ? 57.470 64.157  2.142   1.00 11.39 ? 459  GLU A CG  1 
ATOM   3804  C  CD  . GLU A 1 459  ? 58.365 63.560  3.212   1.00 16.30 ? 459  GLU A CD  1 
ATOM   3805  O  OE1 . GLU A 1 459  ? 58.891 64.372  4.002   1.00 20.72 ? 459  GLU A OE1 1 
ATOM   3806  O  OE2 . GLU A 1 459  ? 58.539 62.308  3.257   1.00 20.09 ? 459  GLU A OE2 1 
ATOM   3807  N  N   . GLN A 1 460  ? 56.766 67.173  -0.014  1.00 7.52  ? 460  GLN A N   1 
ATOM   3808  C  CA  . GLN A 1 460  ? 55.832 68.290  0.190   1.00 9.15  ? 460  GLN A CA  1 
ATOM   3809  C  C   . GLN A 1 460  ? 54.719 68.210  -0.854  1.00 7.97  ? 460  GLN A C   1 
ATOM   3810  O  O   . GLN A 1 460  ? 53.519 68.334  -0.529  1.00 8.41  ? 460  GLN A O   1 
ATOM   3811  C  CB  . GLN A 1 460  ? 56.582 69.621  0.053   1.00 10.59 ? 460  GLN A CB  1 
ATOM   3812  C  CG  . GLN A 1 460  ? 55.697 70.867  0.167   1.00 14.59 ? 460  GLN A CG  1 
ATOM   3813  C  CD  . GLN A 1 460  ? 56.444 72.156  -0.192  1.00 16.17 ? 460  GLN A CD  1 
ATOM   3814  O  OE1 . GLN A 1 460  ? 57.531 72.118  -0.769  1.00 26.13 ? 460  GLN A OE1 1 
ATOM   3815  N  NE2 . GLN A 1 460  ? 55.836 73.290  0.115   1.00 24.57 ? 460  GLN A NE2 1 
ATOM   3816  N  N   . ALA A 1 461  ? 55.085 68.055  -2.135  1.00 6.86  ? 461  ALA A N   1 
ATOM   3817  C  CA  . ALA A 1 461  ? 54.053 68.052  -3.165  1.00 6.35  ? 461  ALA A CA  1 
ATOM   3818  C  C   . ALA A 1 461  ? 53.127 66.836  -2.978  1.00 6.52  ? 461  ALA A C   1 
ATOM   3819  O  O   . ALA A 1 461  ? 51.914 67.001  -3.092  1.00 6.69  ? 461  ALA A O   1 
ATOM   3820  C  CB  . ALA A 1 461  ? 54.693 68.036  -4.520  1.00 6.88  ? 461  ALA A CB  1 
ATOM   3821  N  N   . ARG A 1 462  ? 53.663 65.642  -2.707  1.00 5.56  ? 462  ARG A N   1 
ATOM   3822  C  CA  . ARG A 1 462  ? 52.777 64.484  -2.505  1.00 5.49  ? 462  ARG A CA  1 
ATOM   3823  C  C   . ARG A 1 462  ? 51.841 64.720  -1.337  1.00 5.87  ? 462  ARG A C   1 
ATOM   3824  O  O   . ARG A 1 462  ? 50.666 64.300  -1.391  1.00 6.10  ? 462  ARG A O   1 
ATOM   3825  C  CB  . ARG A 1 462  ? 53.531 63.185  -2.225  1.00 5.81  ? 462  ARG A CB  1 
ATOM   3826  C  CG  . ARG A 1 462  ? 54.241 62.637  -3.471  1.00 7.94  ? 462  ARG A CG  1 
ATOM   3827  C  CD  . ARG A 1 462  ? 54.789 61.208  -3.239  1.00 6.74  ? 462  ARG A CD  1 
ATOM   3828  N  NE  . ARG A 1 462  ? 55.668 61.160  -2.057  1.00 7.53  ? 462  ARG A NE  1 
ATOM   3829  C  CZ  . ARG A 1 462  ? 56.986 61.318  -2.125  1.00 10.40 ? 462  ARG A CZ  1 
ATOM   3830  N  NH1 . ARG A 1 462  ? 57.575 61.477  -3.299  1.00 9.41  ? 462  ARG A NH1 1 
ATOM   3831  N  NH2 . ARG A 1 462  ? 57.712 61.284  -1.024  1.00 11.44 ? 462  ARG A NH2 1 
ATOM   3832  N  N   . ARG A 1 463  ? 52.351 65.330  -0.269  1.00 6.42  ? 463  ARG A N   1 
ATOM   3833  C  CA  . ARG A 1 463  ? 51.536 65.470  0.932   1.00 5.75  ? 463  ARG A CA  1 
ATOM   3834  C  C   . ARG A 1 463  ? 50.458 66.501  0.757   1.00 6.90  ? 463  ARG A C   1 
ATOM   3835  O  O   . ARG A 1 463  ? 49.345 66.313  1.260   1.00 7.07  ? 463  ARG A O   1 
ATOM   3836  C  CB  . ARG A 1 463  ? 52.396 65.716  2.165   1.00 6.15  ? 463  ARG A CB  1 
ATOM   3837  C  CG  . ARG A 1 463  ? 53.120 64.452  2.526   1.00 7.23  ? 463  ARG A CG  1 
ATOM   3838  C  CD  . ARG A 1 463  ? 54.127 64.623  3.644   1.00 9.73  ? 463  ARG A CD  1 
ATOM   3839  N  NE  . ARG A 1 463  ? 54.655 63.312  4.001   1.00 9.99  ? 463  ARG A NE  1 
ATOM   3840  C  CZ  . ARG A 1 463  ? 55.368 63.072  5.097   1.00 11.78 ? 463  ARG A CZ  1 
ATOM   3841  N  NH1 . ARG A 1 463  ? 55.675 64.069  5.916   1.00 12.53 ? 463  ARG A NH1 1 
ATOM   3842  N  NH2 . ARG A 1 463  ? 55.770 61.819  5.328   1.00 12.34 ? 463  ARG A NH2 1 
ATOM   3843  N  N   . GLU A 1 464  ? 50.736 67.586  0.021   1.00 6.62  ? 464  GLU A N   1 
ATOM   3844  C  CA  . GLU A 1 464  ? 49.701 68.581  -0.163  1.00 7.46  ? 464  GLU A CA  1 
ATOM   3845  C  C   . GLU A 1 464  ? 48.615 68.032  -1.081  1.00 6.48  ? 464  GLU A C   1 
ATOM   3846  O  O   . GLU A 1 464  ? 47.424 68.238  -0.815  1.00 6.24  ? 464  GLU A O   1 
ATOM   3847  C  CB  . GLU A 1 464  ? 50.235 69.889  -0.741  1.00 8.66  ? 464  GLU A CB  1 
ATOM   3848  C  CG  . GLU A 1 464  ? 51.380 70.562  0.044   1.00 11.66 ? 464  GLU A CG  1 
ATOM   3849  C  CD  . GLU A 1 464  ? 51.076 71.029  1.467   1.00 16.74 ? 464  GLU A CD  1 
ATOM   3850  O  OE1 . GLU A 1 464  ? 50.047 70.670  2.058   1.00 17.52 ? 464  GLU A OE1 1 
ATOM   3851  O  OE2 . GLU A 1 464  ? 51.921 71.796  2.005   1.00 20.20 ? 464  GLU A OE2 1 
ATOM   3852  N  N   . LEU A 1 465  ? 49.002 67.330  -2.143  1.00 5.75  ? 465  LEU A N   1 
ATOM   3853  C  CA  . LEU A 1 465  ? 47.992 66.733  -3.025  1.00 6.23  ? 465  LEU A CA  1 
ATOM   3854  C  C   . LEU A 1 465  ? 47.208 65.676  -2.243  1.00 5.06  ? 465  LEU A C   1 
ATOM   3855  O  O   . LEU A 1 465  ? 45.964 65.571  -2.395  1.00 5.73  ? 465  LEU A O   1 
ATOM   3856  C  CB  . LEU A 1 465  ? 48.637 66.092  -4.261  1.00 7.07  ? 465  LEU A CB  1 
ATOM   3857  C  CG  . LEU A 1 465  ? 47.668 65.440  -5.255  1.00 6.35  ? 465  LEU A CG  1 
ATOM   3858  C  CD1 . LEU A 1 465  ? 46.562 66.384  -5.771  1.00 8.38  ? 465  LEU A CD1 1 
ATOM   3859  C  CD2 . LEU A 1 465  ? 48.469 64.889  -6.441  1.00 7.78  ? 465  LEU A CD2 1 
ATOM   3860  N  N   . SER A 1 466  ? 47.905 64.893  -1.425  1.00 4.78  ? 466  SER A N   1 
ATOM   3861  C  CA  . SER A 1 466  ? 47.220 63.886  -0.650  1.00 3.92  ? 466  SER A CA  1 
ATOM   3862  C  C   . SER A 1 466  ? 46.223 64.489  0.322   1.00 4.98  ? 466  SER A C   1 
ATOM   3863  O  O   . SER A 1 466  ? 45.109 63.981  0.485   1.00 5.07  ? 466  SER A O   1 
ATOM   3864  C  CB  . SER A 1 466  ? 48.223 63.042  0.134   1.00 4.84  ? 466  SER A CB  1 
ATOM   3865  O  OG  . SER A 1 466  ? 49.022 62.248  -0.716  1.00 6.02  ? 466  SER A OG  1 
ATOM   3866  N  N   . LEU A 1 467  ? 46.614 65.571  0.974   1.00 4.41  ? 467  LEU A N   1 
ATOM   3867  C  CA  . LEU A 1 467  ? 45.737 66.231  1.906   1.00 4.81  ? 467  LEU A CA  1 
ATOM   3868  C  C   . LEU A 1 467  ? 44.420 66.631  1.215   1.00 4.65  ? 467  LEU A C   1 
ATOM   3869  O  O   . LEU A 1 467  ? 43.332 66.522  1.780   1.00 4.93  ? 467  LEU A O   1 
ATOM   3870  C  CB  . LEU A 1 467  ? 46.424 67.466  2.517   1.00 5.44  ? 467  LEU A CB  1 
ATOM   3871  C  CG  . LEU A 1 467  ? 45.577 68.156  3.564   1.00 8.54  ? 467  LEU A CG  1 
ATOM   3872  C  CD1 . LEU A 1 467  ? 45.548 67.330  4.827   1.00 14.60 ? 467  LEU A CD1 1 
ATOM   3873  C  CD2 . LEU A 1 467  ? 46.188 69.546  3.869   1.00 10.79 ? 467  LEU A CD2 1 
ATOM   3874  N  N   . PHE A 1 468  ? 44.539 67.138  -0.008  1.00 4.21  ? 468  PHE A N   1 
ATOM   3875  C  CA  . PHE A 1 468  ? 43.341 67.662  -0.697  1.00 4.71  ? 468  PHE A CA  1 
ATOM   3876  C  C   . PHE A 1 468  ? 42.405 66.557  -1.109  1.00 3.89  ? 468  PHE A C   1 
ATOM   3877  O  O   . PHE A 1 468  ? 41.240 66.838  -1.440  1.00 4.86  ? 468  PHE A O   1 
ATOM   3878  C  CB  . PHE A 1 468  ? 43.779 68.502  -1.894  1.00 4.84  ? 468  PHE A CB  1 
ATOM   3879  C  CG  . PHE A 1 468  ? 42.677 69.335  -2.468  1.00 4.73  ? 468  PHE A CG  1 
ATOM   3880  C  CD1 . PHE A 1 468  ? 42.047 70.296  -1.700  1.00 6.76  ? 468  PHE A CD1 1 
ATOM   3881  C  CD2 . PHE A 1 468  ? 42.245 69.147  -3.787  1.00 4.89  ? 468  PHE A CD2 1 
ATOM   3882  C  CE1 . PHE A 1 468  ? 40.997 71.067  -2.216  1.00 6.72  ? 468  PHE A CE1 1 
ATOM   3883  C  CE2 . PHE A 1 468  ? 41.166 69.932  -4.289  1.00 4.00  ? 468  PHE A CE2 1 
ATOM   3884  C  CZ  . PHE A 1 468  ? 40.559 70.867  -3.489  1.00 5.64  ? 468  PHE A CZ  1 
ATOM   3885  N  N   . GLN A 1 469  ? 42.834 65.294  -1.053  1.00 4.11  ? 469  GLN A N   1 
ATOM   3886  C  CA  . GLN A 1 469  ? 41.890 64.223  -1.356  1.00 3.97  ? 469  GLN A CA  1 
ATOM   3887  C  C   . GLN A 1 469  ? 40.887 64.011  -0.224  1.00 4.89  ? 469  GLN A C   1 
ATOM   3888  O  O   . GLN A 1 469  ? 39.932 63.237  -0.370  1.00 5.03  ? 469  GLN A O   1 
ATOM   3889  C  CB  . GLN A 1 469  ? 42.623 62.895  -1.583  1.00 4.44  ? 469  GLN A CB  1 
ATOM   3890  C  CG  . GLN A 1 469  ? 43.724 62.971  -2.682  1.00 5.27  ? 469  GLN A CG  1 
ATOM   3891  C  CD  . GLN A 1 469  ? 43.212 63.622  -3.933  1.00 6.08  ? 469  GLN A CD  1 
ATOM   3892  O  OE1 . GLN A 1 469  ? 42.224 63.174  -4.491  1.00 6.65  ? 469  GLN A OE1 1 
ATOM   3893  N  NE2 . GLN A 1 469  ? 43.847 64.702  -4.350  1.00 5.76  ? 469  GLN A NE2 1 
ATOM   3894  N  N   . HIS A 1 470  ? 41.104 64.668  0.911   1.00 4.12  ? 470  HIS A N   1 
ATOM   3895  C  CA  . HIS A 1 470  ? 40.168 64.595  2.022   1.00 3.65  ? 470  HIS A CA  1 
ATOM   3896  C  C   . HIS A 1 470  ? 38.749 64.848  1.541   1.00 4.75  ? 470  HIS A C   1 
ATOM   3897  O  O   . HIS A 1 470  ? 38.522 65.620  0.603   1.00 5.19  ? 470  HIS A O   1 
ATOM   3898  C  CB  . HIS A 1 470  ? 40.588 65.640  3.073   1.00 5.31  ? 470  HIS A CB  1 
ATOM   3899  C  CG  . HIS A 1 470  ? 39.574 65.905  4.141   1.00 5.30  ? 470  HIS A CG  1 
ATOM   3900  N  ND1 . HIS A 1 470  ? 38.950 64.892  4.849   1.00 7.70  ? 470  HIS A ND1 1 
ATOM   3901  C  CD2 . HIS A 1 470  ? 39.088 67.074  4.626   1.00 6.69  ? 470  HIS A CD2 1 
ATOM   3902  C  CE1 . HIS A 1 470  ? 38.128 65.440  5.733   1.00 6.86  ? 470  HIS A CE1 1 
ATOM   3903  N  NE2 . HIS A 1 470  ? 38.186 66.756  5.609   1.00 7.95  ? 470  HIS A NE2 1 
ATOM   3904  N  N   . HIS A 1 471  ? 37.785 64.219  2.212   1.00 4.88  ? 471  HIS A N   1 
ATOM   3905  C  CA  . HIS A 1 471  ? 36.375 64.377  1.856   1.00 4.91  ? 471  HIS A CA  1 
ATOM   3906  C  C   . HIS A 1 471  ? 35.760 65.740  2.195   1.00 5.47  ? 471  HIS A C   1 
ATOM   3907  O  O   . HIS A 1 471  ? 34.556 65.908  1.948   1.00 7.18  ? 471  HIS A O   1 
ATOM   3908  C  CB  . HIS A 1 471  ? 35.549 63.216  2.451   1.00 5.85  ? 471  HIS A CB  1 
ATOM   3909  C  CG  . HIS A 1 471  ? 35.630 63.131  3.938   1.00 5.38  ? 471  HIS A CG  1 
ATOM   3910  N  ND1 . HIS A 1 471  ? 36.595 62.402  4.597   1.00 6.51  ? 471  HIS A ND1 1 
ATOM   3911  C  CD2 . HIS A 1 471  ? 34.879 63.725  4.894   1.00 8.02  ? 471  HIS A CD2 1 
ATOM   3912  C  CE1 . HIS A 1 471  ? 36.422 62.550  5.905   1.00 5.84  ? 471  HIS A CE1 1 
ATOM   3913  N  NE2 . HIS A 1 471  ? 35.399 63.345  6.108   1.00 5.34  ? 471  HIS A NE2 1 
ATOM   3914  N  N   . ASP A 1 472  ? 36.545 66.716  2.657   1.00 6.29  ? 472  ASP A N   1 
ATOM   3915  C  CA  . ASP A 1 472  ? 36.123 68.128  2.601   1.00 7.44  ? 472  ASP A CA  1 
ATOM   3916  C  C   . ASP A 1 472  ? 37.064 69.009  1.819   1.00 7.64  ? 472  ASP A C   1 
ATOM   3917  O  O   . ASP A 1 472  ? 36.932 70.240  1.860   1.00 8.68  ? 472  ASP A O   1 
ATOM   3918  C  CB  . ASP A 1 472  ? 35.943 68.768  3.992   1.00 7.03  ? 472  ASP A CB  1 
ATOM   3919  C  CG  . ASP A 1 472  ? 34.936 68.042  4.837   1.00 8.91  ? 472  ASP A CG  1 
ATOM   3920  O  OD1 . ASP A 1 472  ? 33.748 68.042  4.432   1.00 9.17  ? 472  ASP A OD1 1 
ATOM   3921  O  OD2 . ASP A 1 472  ? 35.249 67.441  5.885   1.00 8.86  ? 472  ASP A OD2 1 
ATOM   3922  N  N   . GLY A 1 473  ? 38.018 68.408  1.103   1.00 5.98  ? 473  GLY A N   1 
ATOM   3923  C  CA  . GLY A 1 473  ? 38.983 69.153  0.300   1.00 5.03  ? 473  GLY A CA  1 
ATOM   3924  C  C   . GLY A 1 473  ? 38.429 69.217  -1.107  1.00 4.99  ? 473  GLY A C   1 
ATOM   3925  O  O   . GLY A 1 473  ? 37.707 70.151  -1.465  1.00 5.55  ? 473  GLY A O   1 
ATOM   3926  N  N   . ILE A 1 474  ? 38.750 68.198  -1.886  1.00 4.16  ? 474  ILE A N   1 
ATOM   3927  C  CA  . ILE A 1 474  ? 38.338 68.182  -3.293  1.00 4.97  ? 474  ILE A CA  1 
ATOM   3928  C  C   . ILE A 1 474  ? 36.814 68.306  -3.462  1.00 5.48  ? 474  ILE A C   1 
ATOM   3929  O  O   . ILE A 1 474  ? 36.350 68.841  -4.490  1.00 6.03  ? 474  ILE A O   1 
ATOM   3930  C  CB  . ILE A 1 474  ? 38.909 66.948  -4.000  1.00 5.15  ? 474  ILE A CB  1 
ATOM   3931  C  CG1 . ILE A 1 474  ? 38.679 67.032  -5.518  1.00 5.57  ? 474  ILE A CG1 1 
ATOM   3932  C  CG2 . ILE A 1 474  ? 38.397 65.661  -3.339  1.00 5.71  ? 474  ILE A CG2 1 
ATOM   3933  C  CD1 . ILE A 1 474  ? 39.423 65.948  -6.298  1.00 6.65  ? 474  ILE A CD1 1 
ATOM   3934  N  N   . THR A 1 475  ? 36.060 67.872  -2.453  1.00 3.73  ? 475  THR A N   1 
ATOM   3935  C  CA  . THR A 1 475  ? 34.615 67.961  -2.495  1.00 4.75  ? 475  THR A CA  1 
ATOM   3936  C  C   . THR A 1 475  ? 34.085 69.389  -2.488  1.00 4.87  ? 475  THR A C   1 
ATOM   3937  O  O   . THR A 1 475  ? 32.924 69.599  -2.851  1.00 6.26  ? 475  THR A O   1 
ATOM   3938  C  CB  . THR A 1 475  ? 34.031 67.287  -1.267  1.00 5.86  ? 475  THR A CB  1 
ATOM   3939  O  OG1 . THR A 1 475  ? 34.554 67.939  -0.104  1.00 6.14  ? 475  THR A OG1 1 
ATOM   3940  C  CG2 . THR A 1 475  ? 34.435 65.831  -1.166  1.00 6.25  ? 475  THR A CG2 1 
ATOM   3941  N  N   . GLY A 1 476  ? 34.877 70.362  -2.056  1.00 5.05  ? 476  GLY A N   1 
ATOM   3942  C  CA  . GLY A 1 476  ? 34.384 71.722  -2.067  1.00 6.22  ? 476  GLY A CA  1 
ATOM   3943  C  C   . GLY A 1 476  ? 33.421 72.018  -0.949  1.00 6.28  ? 476  GLY A C   1 
ATOM   3944  O  O   . GLY A 1 476  ? 32.525 72.867  -1.107  1.00 6.32  ? 476  GLY A O   1 
ATOM   3945  N  N   . THR A 1 477  ? 33.540 71.284  0.156   1.00 5.44  ? 477  THR A N   1 
ATOM   3946  C  CA  . THR A 1 477  ? 32.617 71.438  1.255   1.00 5.83  ? 477  THR A CA  1 
ATOM   3947  C  C   . THR A 1 477  ? 33.259 72.042  2.505   1.00 6.06  ? 477  THR A C   1 
ATOM   3948  O  O   . THR A 1 477  ? 32.723 71.854  3.607   1.00 7.46  ? 477  THR A O   1 
ATOM   3949  C  CB  . THR A 1 477  ? 31.962 70.091  1.625   1.00 6.99  ? 477  THR A CB  1 
ATOM   3950  O  OG1 . THR A 1 477  ? 32.982 69.092  1.860   1.00 6.48  ? 477  THR A OG1 1 
ATOM   3951  C  CG2 . THR A 1 477  ? 31.123 69.549  0.453   1.00 6.57  ? 477  THR A CG2 1 
ATOM   3952  N  N   . ALA A 1 478  ? 34.364 72.779  2.372   1.00 5.10  ? 478  ALA A N   1 
ATOM   3953  C  CA  . ALA A 1 478  ? 34.996 73.410  3.540   1.00 5.92  ? 478  ALA A CA  1 
ATOM   3954  C  C   . ALA A 1 478  ? 34.689 74.889  3.617   1.00 5.46  ? 478  ALA A C   1 
ATOM   3955  O  O   . ALA A 1 478  ? 34.220 75.515  2.646   1.00 6.25  ? 478  ALA A O   1 
ATOM   3956  C  CB  . ALA A 1 478  ? 36.520 73.191  3.485   1.00 6.39  ? 478  ALA A CB  1 
ATOM   3957  N  N   . LYS A 1 479  ? 34.926 75.476  4.786   1.00 5.68  ? 479  LYS A N   1 
ATOM   3958  C  CA  . LYS A 1 479  ? 34.742 76.936  4.896   1.00 7.17  ? 479  LYS A CA  1 
ATOM   3959  C  C   . LYS A 1 479  ? 35.695 77.668  3.962   1.00 7.39  ? 479  LYS A C   1 
ATOM   3960  O  O   . LYS A 1 479  ? 36.764 77.183  3.608   1.00 6.42  ? 479  LYS A O   1 
ATOM   3961  C  CB  . LYS A 1 479  ? 34.926 77.403  6.349   1.00 7.86  ? 479  LYS A CB  1 
ATOM   3962  C  CG  . LYS A 1 479  ? 33.705 77.064  7.210   1.00 10.36 ? 479  LYS A CG  1 
ATOM   3963  C  CD  . LYS A 1 479  ? 33.781 77.808  8.542   1.00 12.50 ? 479  LYS A CD  1 
ATOM   3964  C  CE  . LYS A 1 479  ? 32.510 77.692  9.381   1.00 15.29 ? 479  LYS A CE  1 
ATOM   3965  N  NZ  . LYS A 1 479  ? 31.315 78.303  8.727   1.00 15.33 ? 479  LYS A NZ  1 
ATOM   3966  N  N   . THR A 1 480  ? 35.301 78.886  3.618   1.00 8.36  ? 480  THR A N   1 
ATOM   3967  C  CA  . THR A 1 480  ? 36.110 79.703  2.717   1.00 8.99  ? 480  THR A CA  1 
ATOM   3968  C  C   . THR A 1 480  ? 37.575 79.789  3.116   1.00 8.71  ? 480  THR A C   1 
ATOM   3969  O  O   . THR A 1 480  ? 38.451 79.592  2.271   1.00 8.87  ? 480  THR A O   1 
ATOM   3970  C  CB  . THR A 1 480  ? 35.535 81.123  2.640   1.00 9.91  ? 480  THR A CB  1 
ATOM   3971  O  OG1 . THR A 1 480  ? 34.240 81.041  2.059   1.00 12.88 ? 480  THR A OG1 1 
ATOM   3972  C  CG2 . THR A 1 480  ? 36.323 82.038  1.682   1.00 12.66 ? 480  THR A CG2 1 
ATOM   3973  N  N   . HIS A 1 481  ? 37.864 80.060  4.393   1.00 7.99  ? 481  HIS A N   1 
ATOM   3974  C  CA  . HIS A 1 481  ? 39.271 80.208  4.733   1.00 8.22  ? 481  HIS A CA  1 
ATOM   3975  C  C   . HIS A 1 481  ? 40.036 78.907  4.687   1.00 8.05  ? 481  HIS A C   1 
ATOM   3976  O  O   . HIS A 1 481  ? 41.261 78.900  4.552   1.00 7.77  ? 481  HIS A O   1 
ATOM   3977  C  CB  . HIS A 1 481  ? 39.438 80.901  6.103   1.00 9.85  ? 481  HIS A CB  1 
ATOM   3978  C  CG  . HIS A 1 481  ? 39.283 79.994  7.286   1.00 8.90  ? 481  HIS A CG  1 
ATOM   3979  N  ND1 . HIS A 1 481  ? 38.054 79.562  7.740   1.00 11.49 ? 481  HIS A ND1 1 
ATOM   3980  C  CD2 . HIS A 1 481  ? 40.205 79.492  8.145   1.00 9.88  ? 481  HIS A CD2 1 
ATOM   3981  C  CE1 . HIS A 1 481  ? 38.234 78.792  8.804   1.00 11.81 ? 481  HIS A CE1 1 
ATOM   3982  N  NE2 . HIS A 1 481  ? 39.529 78.748  9.075   1.00 11.26 ? 481  HIS A NE2 1 
ATOM   3983  N  N   . VAL A 1 482  ? 39.301 77.799  4.779   1.00 6.92  ? 482  VAL A N   1 
ATOM   3984  C  CA  . VAL A 1 482  ? 39.947 76.490  4.683   1.00 7.03  ? 482  VAL A CA  1 
ATOM   3985  C  C   . VAL A 1 482  ? 40.244 76.166  3.210   1.00 6.85  ? 482  VAL A C   1 
ATOM   3986  O  O   . VAL A 1 482  ? 41.308 75.646  2.879   1.00 6.45  ? 482  VAL A O   1 
ATOM   3987  C  CB  . VAL A 1 482  ? 39.046 75.409  5.338   1.00 5.49  ? 482  VAL A CB  1 
ATOM   3988  C  CG1 . VAL A 1 482  ? 39.685 74.012  5.250   1.00 6.94  ? 482  VAL A CG1 1 
ATOM   3989  C  CG2 . VAL A 1 482  ? 38.767 75.723  6.804   1.00 7.06  ? 482  VAL A CG2 1 
ATOM   3990  N  N   . VAL A 1 483  ? 39.312 76.537  2.340   1.00 6.46  ? 483  VAL A N   1 
ATOM   3991  C  CA  . VAL A 1 483  ? 39.572 76.421  0.914   1.00 6.69  ? 483  VAL A CA  1 
ATOM   3992  C  C   . VAL A 1 483  ? 40.809 77.229  0.496   1.00 6.77  ? 483  VAL A C   1 
ATOM   3993  O  O   . VAL A 1 483  ? 41.652 76.743  -0.264  1.00 6.84  ? 483  VAL A O   1 
ATOM   3994  C  CB  . VAL A 1 483  ? 38.355 76.882  0.086   1.00 6.48  ? 483  VAL A CB  1 
ATOM   3995  C  CG1 . VAL A 1 483  ? 38.646 76.863  -1.406  1.00 9.18  ? 483  VAL A CG1 1 
ATOM   3996  C  CG2 . VAL A 1 483  ? 37.114 76.008  0.389   1.00 8.68  ? 483  VAL A CG2 1 
ATOM   3997  N  N   . VAL A 1 484  ? 40.944 78.429  1.066   1.00 8.29  ? 484  VAL A N   1 
ATOM   3998  C  CA  . VAL A 1 484  ? 42.132 79.245  0.814   1.00 8.81  ? 484  VAL A CA  1 
ATOM   3999  C  C   . VAL A 1 484  ? 43.392 78.523  1.273   1.00 8.07  ? 484  VAL A C   1 
ATOM   4000  O  O   . VAL A 1 484  ? 44.392 78.523  0.533   1.00 9.24  ? 484  VAL A O   1 
ATOM   4001  C  CB  . VAL A 1 484  ? 41.996 80.624  1.477   1.00 9.38  ? 484  VAL A CB  1 
ATOM   4002  C  CG1 . VAL A 1 484  ? 43.335 81.386  1.404   1.00 11.42 ? 484  VAL A CG1 1 
ATOM   4003  C  CG2 . VAL A 1 484  ? 40.888 81.406  0.785   1.00 10.99 ? 484  VAL A CG2 1 
ATOM   4004  N  N   . ASP A 1 485  ? 43.359 77.874  2.430   1.00 7.07  ? 485  ASP A N   1 
ATOM   4005  C  CA  . ASP A 1 485  ? 44.501 77.108  2.897   1.00 6.61  ? 485  ASP A CA  1 
ATOM   4006  C  C   . ASP A 1 485  ? 44.861 75.983  1.965   1.00 6.71  ? 485  ASP A C   1 
ATOM   4007  O  O   . ASP A 1 485  ? 46.041 75.786  1.653   1.00 7.18  ? 485  ASP A O   1 
ATOM   4008  C  CB  . ASP A 1 485  ? 44.240 76.575  4.307   1.00 7.89  ? 485  ASP A CB  1 
ATOM   4009  C  CG  . ASP A 1 485  ? 45.457 75.954  4.913   1.00 10.05 ? 485  ASP A CG  1 
ATOM   4010  O  OD1 . ASP A 1 485  ? 46.453 76.712  5.090   1.00 13.28 ? 485  ASP A OD1 1 
ATOM   4011  O  OD2 . ASP A 1 485  ? 45.502 74.776  5.279   1.00 9.56  ? 485  ASP A OD2 1 
ATOM   4012  N  N   . TYR A 1 486  ? 43.863 75.245  1.496   1.00 5.87  ? 486  TYR A N   1 
ATOM   4013  C  CA  . TYR A 1 486  ? 44.173 74.176  0.542   1.00 6.18  ? 486  TYR A CA  1 
ATOM   4014  C  C   . TYR A 1 486  ? 44.756 74.716  -0.742  1.00 6.48  ? 486  TYR A C   1 
ATOM   4015  O  O   . TYR A 1 486  ? 45.653 74.111  -1.290  1.00 7.19  ? 486  TYR A O   1 
ATOM   4016  C  CB  . TYR A 1 486  ? 42.913 73.384  0.219   1.00 6.93  ? 486  TYR A CB  1 
ATOM   4017  C  CG  . TYR A 1 486  ? 42.331 72.509  1.331   1.00 5.57  ? 486  TYR A CG  1 
ATOM   4018  C  CD1 . TYR A 1 486  ? 43.126 71.641  2.108   1.00 8.69  ? 486  TYR A CD1 1 
ATOM   4019  C  CD2 . TYR A 1 486  ? 40.951 72.499  1.533   1.00 7.16  ? 486  TYR A CD2 1 
ATOM   4020  C  CE1 . TYR A 1 486  ? 42.530 70.800  3.091   1.00 10.20 ? 486  TYR A CE1 1 
ATOM   4021  C  CE2 . TYR A 1 486  ? 40.369 71.671  2.499   1.00 6.79  ? 486  TYR A CE2 1 
ATOM   4022  C  CZ  . TYR A 1 486  ? 41.158 70.831  3.249   1.00 7.43  ? 486  TYR A CZ  1 
ATOM   4023  O  OH  . TYR A 1 486  ? 40.576 70.004  4.198   1.00 10.40 ? 486  TYR A OH  1 
ATOM   4024  N  N   . GLU A 1 487  ? 44.236 75.836  -1.219  1.00 7.24  ? 487  GLU A N   1 
ATOM   4025  C  CA  . GLU A 1 487  ? 44.731 76.412  -2.452  1.00 7.45  ? 487  GLU A CA  1 
ATOM   4026  C  C   . GLU A 1 487  ? 46.198 76.844  -2.289  1.00 8.09  ? 487  GLU A C   1 
ATOM   4027  O  O   . GLU A 1 487  ? 47.032 76.600  -3.187  1.00 8.92  ? 487  GLU A O   1 
ATOM   4028  C  CB  . GLU A 1 487  ? 43.905 77.621  -2.842  1.00 7.28  ? 487  GLU A CB  1 
ATOM   4029  C  CG  . GLU A 1 487  ? 44.306 78.181  -4.197  1.00 11.21 ? 487  GLU A CG  1 
ATOM   4030  C  CD  . GLU A 1 487  ? 43.407 79.303  -4.658  1.00 16.31 ? 487  GLU A CD  1 
ATOM   4031  O  OE1 . GLU A 1 487  ? 42.267 79.451  -4.152  1.00 17.38 ? 487  GLU A OE1 1 
ATOM   4032  O  OE2 . GLU A 1 487  ? 43.862 80.039  -5.577  1.00 20.65 ? 487  GLU A OE2 1 
ATOM   4033  N  N   . GLN A 1 488  ? 46.507 77.501  -1.173  1.00 7.85  ? 488  GLN A N   1 
ATOM   4034  C  CA  . GLN A 1 488  ? 47.880 77.950  -0.930  1.00 8.50  ? 488  GLN A CA  1 
ATOM   4035  C  C   . GLN A 1 488  ? 48.796 76.746  -0.833  1.00 7.98  ? 488  GLN A C   1 
ATOM   4036  O  O   . GLN A 1 488  ? 49.922 76.783  -1.355  1.00 8.48  ? 488  GLN A O   1 
ATOM   4037  C  CB  . GLN A 1 488  ? 47.960 78.727  0.394   1.00 10.88 ? 488  GLN A CB  1 
ATOM   4038  C  CG  . GLN A 1 488  ? 47.188 80.023  0.372   1.00 15.76 ? 488  GLN A CG  1 
ATOM   4039  C  CD  . GLN A 1 488  ? 47.232 80.719  1.728   1.00 21.00 ? 488  GLN A CD  1 
ATOM   4040  O  OE1 . GLN A 1 488  ? 47.325 80.070  2.782   1.00 25.00 ? 488  GLN A OE1 1 
ATOM   4041  N  NE2 . GLN A 1 488  ? 47.158 82.026  1.705   1.00 25.36 ? 488  GLN A NE2 1 
ATOM   4042  N  N   . ARG A 1 489  ? 48.362 75.671  -0.172  1.00 7.02  ? 489  ARG A N   1 
ATOM   4043  C  CA  . ARG A 1 489  ? 49.178 74.473  -0.091  1.00 7.79  ? 489  ARG A CA  1 
ATOM   4044  C  C   . ARG A 1 489  ? 49.386 73.885  -1.480  1.00 7.56  ? 489  ARG A C   1 
ATOM   4045  O  O   . ARG A 1 489  ? 50.504 73.489  -1.813  1.00 7.19  ? 489  ARG A O   1 
ATOM   4046  C  CB  . ARG A 1 489  ? 48.520 73.455  0.818   1.00 8.02  ? 489  ARG A CB  1 
ATOM   4047  C  CG  . ARG A 1 489  ? 48.539 73.819  2.282   1.00 6.95  ? 489  ARG A CG  1 
ATOM   4048  C  CD  . ARG A 1 489  ? 47.582 72.875  3.058   1.00 9.50  ? 489  ARG A CD  1 
ATOM   4049  N  NE  . ARG A 1 489  ? 47.687 73.026  4.508   1.00 8.60  ? 489  ARG A NE  1 
ATOM   4050  C  CZ  . ARG A 1 489  ? 48.563 72.374  5.294   1.00 11.06 ? 489  ARG A CZ  1 
ATOM   4051  N  NH1 . ARG A 1 489  ? 49.456 71.531  4.798   1.00 12.23 ? 489  ARG A NH1 1 
ATOM   4052  N  NH2 . ARG A 1 489  ? 48.543 72.594  6.607   1.00 11.35 ? 489  ARG A NH2 1 
ATOM   4053  N  N   . MET A 1 490  ? 48.345 73.836  -2.307  1.00 6.87  ? 490  MET A N   1 
ATOM   4054  C  CA  . MET A 1 490  ? 48.538 73.285  -3.646  1.00 7.82  ? 490  MET A CA  1 
ATOM   4055  C  C   . MET A 1 490  ? 49.413 74.176  -4.510  1.00 7.64  ? 490  MET A C   1 
ATOM   4056  O  O   . MET A 1 490  ? 50.170 73.657  -5.338  1.00 6.93  ? 490  MET A O   1 
ATOM   4057  C  CB  . MET A 1 490  ? 47.202 73.026  -4.343  1.00 8.26  ? 490  MET A CB  1 
ATOM   4058  C  CG  . MET A 1 490  ? 46.467 71.832  -3.686  1.00 9.07  ? 490  MET A CG  1 
ATOM   4059  S  SD  . MET A 1 490  ? 45.169 71.123  -4.802  1.00 12.55 ? 490  MET A SD  1 
ATOM   4060  C  CE  . MET A 1 490  ? 43.894 72.311  -4.547  1.00 14.39 ? 490  MET A CE  1 
ATOM   4061  N  N   . GLN A 1 491  ? 49.328 75.492  -4.329  1.00 7.07  ? 491  GLN A N   1 
ATOM   4062  C  CA  . GLN A 1 491  ? 50.234 76.358  -5.082  1.00 7.38  ? 491  GLN A CA  1 
ATOM   4063  C  C   . GLN A 1 491  ? 51.692 76.112  -4.728  1.00 7.98  ? 491  GLN A C   1 
ATOM   4064  O  O   . GLN A 1 491  ? 52.553 76.094  -5.607  1.00 8.57  ? 491  GLN A O   1 
ATOM   4065  C  CB  . GLN A 1 491  ? 49.875 77.823  -4.826  1.00 8.88  ? 491  GLN A CB  1 
ATOM   4066  C  CG  . GLN A 1 491  ? 50.617 78.795  -5.733  1.00 14.19 ? 491  GLN A CG  1 
ATOM   4067  C  CD  . GLN A 1 491  ? 50.484 78.441  -7.190  1.00 22.31 ? 491  GLN A CD  1 
ATOM   4068  O  OE1 . GLN A 1 491  ? 51.484 78.245  -7.883  1.00 27.45 ? 491  GLN A OE1 1 
ATOM   4069  N  NE2 . GLN A 1 491  ? 49.258 78.324  -7.650  1.00 25.86 ? 491  GLN A NE2 1 
ATOM   4070  N  N   . GLU A 1 492  ? 51.966 75.951  -3.438  1.00 7.63  ? 492  GLU A N   1 
ATOM   4071  C  CA  . GLU A 1 492  ? 53.313 75.612  -3.019  1.00 8.65  ? 492  GLU A CA  1 
ATOM   4072  C  C   . GLU A 1 492  ? 53.735 74.293  -3.621  1.00 8.43  ? 492  GLU A C   1 
ATOM   4073  O  O   . GLU A 1 492  ? 54.883 74.135  -4.055  1.00 9.06  ? 492  GLU A O   1 
ATOM   4074  C  CB  . GLU A 1 492  ? 53.429 75.590  -1.488  1.00 9.79  ? 492  GLU A CB  1 
ATOM   4075  C  CG  . GLU A 1 492  ? 53.360 76.991  -0.844  1.00 16.60 ? 492  GLU A CG  1 
ATOM   4076  C  CD  . GLU A 1 492  ? 54.257 78.035  -1.518  1.00 25.25 ? 492  GLU A CD  1 
ATOM   4077  O  OE1 . GLU A 1 492  ? 55.464 77.762  -1.763  1.00 28.53 ? 492  GLU A OE1 1 
ATOM   4078  O  OE2 . GLU A 1 492  ? 53.773 79.160  -1.801  1.00 29.95 ? 492  GLU A OE2 1 
ATOM   4079  N  N   . ALA A 1 493  ? 52.825 73.330  -3.676  1.00 7.02  ? 493  ALA A N   1 
ATOM   4080  C  CA  . ALA A 1 493  ? 53.143 72.043  -4.262  1.00 6.32  ? 493  ALA A CA  1 
ATOM   4081  C  C   . ALA A 1 493  ? 53.473 72.165  -5.758  1.00 6.64  ? 493  ALA A C   1 
ATOM   4082  O  O   . ALA A 1 493  ? 54.355 71.461  -6.254  1.00 6.06  ? 493  ALA A O   1 
ATOM   4083  C  CB  . ALA A 1 493  ? 51.970 71.070  -4.029  1.00 6.29  ? 493  ALA A CB  1 
ATOM   4084  N  N   . LEU A 1 494  ? 52.712 72.975  -6.492  1.00 6.03  ? 494  LEU A N   1 
ATOM   4085  C  CA  . LEU A 1 494  ? 52.996 73.187  -7.910  1.00 6.93  ? 494  LEU A CA  1 
ATOM   4086  C  C   . LEU A 1 494  ? 54.373 73.782  -8.093  1.00 6.73  ? 494  LEU A C   1 
ATOM   4087  O  O   . LEU A 1 494  ? 55.095 73.391  -8.993  1.00 7.46  ? 494  LEU A O   1 
ATOM   4088  C  CB  . LEU A 1 494  ? 51.955 74.081  -8.553  1.00 7.36  ? 494  LEU A CB  1 
ATOM   4089  C  CG  . LEU A 1 494  ? 50.592 73.431  -8.758  1.00 8.33  ? 494  LEU A CG  1 
ATOM   4090  C  CD1 . LEU A 1 494  ? 49.574 74.515  -9.102  1.00 9.76  ? 494  LEU A CD1 1 
ATOM   4091  C  CD2 . LEU A 1 494  ? 50.645 72.393  -9.847  1.00 7.87  ? 494  LEU A CD2 1 
ATOM   4092  N  N   . LYS A 1 495  ? 54.743 74.719  -7.229  1.00 7.24  ? 495  LYS A N   1 
ATOM   4093  C  CA  . LYS A 1 495  ? 56.084 75.340  -7.310  1.00 7.61  ? 495  LYS A CA  1 
ATOM   4094  C  C   . LYS A 1 495  ? 57.166 74.326  -7.024  1.00 7.84  ? 495  LYS A C   1 
ATOM   4095  O  O   . LYS A 1 495  ? 58.204 74.332  -7.704  1.00 8.59  ? 495  LYS A O   1 
ATOM   4096  C  CB  . LYS A 1 495  ? 56.192 76.500  -6.323  1.00 9.66  ? 495  LYS A CB  1 
ATOM   4097  C  CG  . LYS A 1 495  ? 55.354 77.700  -6.713  1.00 12.70 ? 495  LYS A CG  1 
ATOM   4098  C  CD  . LYS A 1 495  ? 55.732 78.901  -5.848  1.00 19.33 ? 495  LYS A CD  1 
ATOM   4099  C  CE  . LYS A 1 495  ? 54.725 79.188  -4.784  1.00 24.29 ? 495  LYS A CE  1 
ATOM   4100  N  NZ  . LYS A 1 495  ? 55.149 80.364  -3.944  1.00 28.15 ? 495  LYS A NZ  1 
ATOM   4101  N  N   . ALA A 1 496  ? 56.906 73.410  -6.085  1.00 6.03  ? 496  ALA A N   1 
ATOM   4102  C  CA  . ALA A 1 496  ? 57.861 72.353  -5.783  1.00 6.51  ? 496  ALA A CA  1 
ATOM   4103  C  C   . ALA A 1 496  ? 58.023 71.425  -6.979  1.00 7.31  ? 496  ALA A C   1 
ATOM   4104  O  O   . ALA A 1 496  ? 59.119 71.007  -7.358  1.00 6.81  ? 496  ALA A O   1 
ATOM   4105  C  CB  . ALA A 1 496  ? 57.374 71.571  -4.544  1.00 6.88  ? 496  ALA A CB  1 
ATOM   4106  N  N   . CYS A 1 497  ? 56.908 71.059  -7.591  1.00 6.19  ? 497  CYS A N   1 
ATOM   4107  C  CA  . CYS A 1 497  ? 56.992 70.191  -8.767  1.00 6.80  ? 497  CYS A CA  1 
ATOM   4108  C  C   . CYS A 1 497  ? 57.750 70.876  -9.887  1.00 6.93  ? 497  CYS A C   1 
ATOM   4109  O  O   . CYS A 1 497  ? 58.564 70.238  -10.542 1.00 7.06  ? 497  CYS A O   1 
ATOM   4110  C  CB  . CYS A 1 497  ? 55.592 69.859  -9.260  1.00 5.53  ? 497  CYS A CB  1 
ATOM   4111  S  SG  . CYS A 1 497  ? 54.678 68.714  -8.241  1.00 8.51  ? 497  CYS A SG  1 
ATOM   4112  N  N   . GLN A 1 498  ? 57.459 72.140  -10.154 1.00 6.52  ? 498  GLN A N   1 
ATOM   4113  C  CA  . GLN A 1 498  ? 58.185 72.856  -11.202 1.00 6.89  ? 498  GLN A CA  1 
ATOM   4114  C  C   . GLN A 1 498  ? 59.681 72.808  -10.934 1.00 7.01  ? 498  GLN A C   1 
ATOM   4115  O  O   . GLN A 1 498  ? 60.475 72.601  -11.867 1.00 6.99  ? 498  GLN A O   1 
ATOM   4116  C  CB  . GLN A 1 498  ? 57.699 74.290  -11.324 1.00 7.55  ? 498  GLN A CB  1 
ATOM   4117  C  CG  . GLN A 1 498  ? 58.562 75.137  -12.283 1.00 11.40 ? 498  GLN A CG  1 
ATOM   4118  C  CD  . GLN A 1 498  ? 58.043 76.543  -12.464 1.00 13.81 ? 498  GLN A CD  1 
ATOM   4119  O  OE1 . GLN A 1 498  ? 57.785 76.965  -13.589 1.00 14.28 ? 498  GLN A OE1 1 
ATOM   4120  N  NE2 . GLN A 1 498  ? 57.946 77.299  -11.365 1.00 14.27 ? 498  GLN A NE2 1 
ATOM   4121  N  N   . MET A 1 499  ? 60.083 73.073  -9.705  1.00 6.52  ? 499  MET A N   1 
ATOM   4122  C  CA  . MET A 1 499  ? 61.488 73.082  -9.367  1.00 6.66  ? 499  MET A CA  1 
ATOM   4123  C  C   . MET A 1 499  ? 62.132 71.740  -9.662  1.00 6.81  ? 499  MET A C   1 
ATOM   4124  O  O   . MET A 1 499  ? 63.166 71.688  -10.278 1.00 7.65  ? 499  MET A O   1 
ATOM   4125  C  CB  . MET A 1 499  ? 61.683 73.465  -7.900  1.00 7.93  ? 499  MET A CB  1 
ATOM   4126  C  CG  . MET A 1 499  ? 63.123 73.283  -7.366  1.00 9.88  ? 499  MET A CG  1 
ATOM   4127  S  SD  . MET A 1 499  ? 64.401 74.298  -8.195  1.00 18.05 ? 499  MET A SD  1 
ATOM   4128  C  CE  . MET A 1 499  ? 63.674 75.834  -7.857  1.00 13.37 ? 499  MET A CE  1 
ATOM   4129  N  N   . VAL A 1 500  ? 61.493 70.654  -9.246  1.00 5.96  ? 500  VAL A N   1 
ATOM   4130  C  CA  . VAL A 1 500  ? 62.069 69.350  -9.465  1.00 6.48  ? 500  VAL A CA  1 
ATOM   4131  C  C   . VAL A 1 500  ? 62.104 69.038  -10.953 1.00 6.57  ? 500  VAL A C   1 
ATOM   4132  O  O   . VAL A 1 500  ? 63.096 68.510  -11.450 1.00 6.73  ? 500  VAL A O   1 
ATOM   4133  C  CB  . VAL A 1 500  ? 61.298 68.262  -8.676  1.00 6.37  ? 500  VAL A CB  1 
ATOM   4134  C  CG1 . VAL A 1 500  ? 61.755 66.891  -9.064  1.00 6.53  ? 500  VAL A CG1 1 
ATOM   4135  C  CG2 . VAL A 1 500  ? 61.479 68.479  -7.189  1.00 8.01  ? 500  VAL A CG2 1 
ATOM   4136  N  N   . MET A 1 501  ? 61.034 69.351  -11.656 1.00 6.21  ? 501  MET A N   1 
ATOM   4137  C  CA  . MET A 1 501  ? 60.957 69.046  -13.080 1.00 7.21  ? 501  MET A CA  1 
ATOM   4138  C  C   . MET A 1 501  ? 62.041 69.786  -13.838 1.00 6.42  ? 501  MET A C   1 
ATOM   4139  O  O   . MET A 1 501  ? 62.726 69.192  -14.646 1.00 6.58  ? 501  MET A O   1 
ATOM   4140  C  CB  . MET A 1 501  ? 59.598 69.416  -13.652 1.00 6.92  ? 501  MET A CB  1 
ATOM   4141  C  CG  . MET A 1 501  ? 58.479 68.474  -13.178 1.00 7.15  ? 501  MET A CG  1 
ATOM   4142  S  SD  . MET A 1 501  ? 56.797 69.083  -13.489 1.00 11.67 ? 501  MET A SD  1 
ATOM   4143  C  CE  . MET A 1 501  ? 56.703 68.860  -15.256 1.00 13.28 ? 501  MET A CE  1 
ATOM   4144  N  N   . GLN A 1 502  ? 62.210 71.072  -13.567 1.00 6.31  ? 502  GLN A N   1 
ATOM   4145  C  CA  . GLN A 1 502  ? 63.139 71.835  -14.410 1.00 6.98  ? 502  GLN A CA  1 
ATOM   4146  C  C   . GLN A 1 502  ? 64.586 71.467  -14.094 1.00 7.65  ? 502  GLN A C   1 
ATOM   4147  O  O   . GLN A 1 502  ? 65.436 71.422  -15.009 1.00 7.52  ? 502  GLN A O   1 
ATOM   4148  C  CB  . GLN A 1 502  ? 62.860 73.317  -14.290 1.00 8.69  ? 502  GLN A CB  1 
ATOM   4149  C  CG  . GLN A 1 502  ? 63.067 73.945  -12.924 1.00 9.53  ? 502  GLN A CG  1 
ATOM   4150  C  CD  . GLN A 1 502  ? 64.489 74.479  -12.719 1.00 11.34 ? 502  GLN A CD  1 
ATOM   4151  O  OE1 . GLN A 1 502  ? 65.241 74.605  -13.697 1.00 11.15 ? 502  GLN A OE1 1 
ATOM   4152  N  NE2 . GLN A 1 502  ? 64.861 74.776  -11.482 1.00 11.82 ? 502  GLN A NE2 1 
ATOM   4153  N  N   . GLN A 1 503  ? 64.885 71.144  -12.835 1.00 6.15  ? 503  GLN A N   1 
ATOM   4154  C  CA  . GLN A 1 503  ? 66.257 70.651  -12.542 1.00 7.29  ? 503  GLN A CA  1 
ATOM   4155  C  C   . GLN A 1 503  ? 66.479 69.337  -13.260 1.00 6.92  ? 503  GLN A C   1 
ATOM   4156  O  O   . GLN A 1 503  ? 67.593 69.063  -13.750 1.00 7.92  ? 503  GLN A O   1 
ATOM   4157  C  CB  . GLN A 1 503  ? 66.503 70.440  -11.047 1.00 8.44  ? 503  GLN A CB  1 
ATOM   4158  C  CG  . GLN A 1 503  ? 66.605 71.722  -10.226 1.00 10.23 ? 503  GLN A CG  1 
ATOM   4159  C  CD  . GLN A 1 503  ? 67.965 72.396  -10.396 1.00 12.56 ? 503  GLN A CD  1 
ATOM   4160  O  OE1 . GLN A 1 503  ? 68.944 71.733  -10.706 1.00 12.84 ? 503  GLN A OE1 1 
ATOM   4161  N  NE2 . GLN A 1 503  ? 68.014 73.702  -10.204 1.00 14.32 ? 503  GLN A NE2 1 
ATOM   4162  N  N   . SER A 1 504  ? 65.437 68.501  -13.341 1.00 6.91  ? 504  SER A N   1 
ATOM   4163  C  CA  . SER A 1 504  ? 65.594 67.206  -13.965 1.00 6.77  ? 504  SER A CA  1 
ATOM   4164  C  C   . SER A 1 504  ? 65.796 67.337  -15.480 1.00 7.50  ? 504  SER A C   1 
ATOM   4165  O  O   . SER A 1 504  ? 66.627 66.610  -16.064 1.00 7.83  ? 504  SER A O   1 
ATOM   4166  C  CB  . SER A 1 504  ? 64.355 66.313  -13.706 1.00 7.40  ? 504  SER A CB  1 
ATOM   4167  O  OG  . SER A 1 504  ? 64.217 66.046  -12.314 1.00 8.36  ? 504  SER A OG  1 
ATOM   4168  N  N   . VAL A 1 505  ? 65.025 68.224  -16.116 1.00 7.23  ? 505  VAL A N   1 
ATOM   4169  C  CA  . VAL A 1 505  ? 65.183 68.424  -17.555 1.00 7.55  ? 505  VAL A CA  1 
ATOM   4170  C  C   . VAL A 1 505  ? 66.617 68.916  -17.867 1.00 8.24  ? 505  VAL A C   1 
ATOM   4171  O  O   . VAL A 1 505  ? 67.244 68.432  -18.809 1.00 8.08  ? 505  VAL A O   1 
ATOM   4172  C  CB  . VAL A 1 505  ? 64.138 69.417  -18.077 1.00 8.25  ? 505  VAL A CB  1 
ATOM   4173  C  CG1 . VAL A 1 505  ? 64.451 69.780  -19.549 1.00 8.76  ? 505  VAL A CG1 1 
ATOM   4174  C  CG2 . VAL A 1 505  ? 62.744 68.827  -17.973 1.00 8.43  ? 505  VAL A CG2 1 
ATOM   4175  N  N   A TYR A 1 506  ? 67.097 69.857  -17.089 0.50 8.15  ? 506  TYR A N   1 
ATOM   4176  N  N   B TYR A 1 506  ? 67.139 69.852  -17.068 0.50 8.32  ? 506  TYR A N   1 
ATOM   4177  C  CA  A TYR A 1 506  ? 68.424 70.350  -17.333 0.50 8.71  ? 506  TYR A CA  1 
ATOM   4178  C  CA  B TYR A 1 506  ? 68.511 70.371  -17.270 0.50 8.90  ? 506  TYR A CA  1 
ATOM   4179  C  C   A TYR A 1 506  ? 69.418 69.171  -17.279 0.50 8.45  ? 506  TYR A C   1 
ATOM   4180  C  C   B TYR A 1 506  ? 69.576 69.295  -17.111 0.50 8.69  ? 506  TYR A C   1 
ATOM   4181  O  O   A TYR A 1 506  ? 70.193 68.937  -18.234 0.50 8.10  ? 506  TYR A O   1 
ATOM   4182  O  O   B TYR A 1 506  ? 70.614 69.289  -17.767 0.50 8.64  ? 506  TYR A O   1 
ATOM   4183  C  CB  A TYR A 1 506  ? 68.724 71.483  -16.364 0.50 8.90  ? 506  TYR A CB  1 
ATOM   4184  C  CB  B TYR A 1 506  ? 68.836 71.565  -16.357 0.50 9.48  ? 506  TYR A CB  1 
ATOM   4185  C  CG  A TYR A 1 506  ? 69.939 72.269  -16.735 0.50 9.83  ? 506  TYR A CG  1 
ATOM   4186  C  CG  B TYR A 1 506  ? 70.320 71.970  -16.374 0.50 9.87  ? 506  TYR A CG  1 
ATOM   4187  C  CD1 A TYR A 1 506  ? 70.049 72.905  -17.985 0.50 8.86  ? 506  TYR A CD1 1 
ATOM   4188  C  CD1 B TYR A 1 506  ? 70.922 72.427  -17.545 0.50 13.41 ? 506  TYR A CD1 1 
ATOM   4189  C  CD2 A TYR A 1 506  ? 70.993 72.350  -15.850 0.50 10.08 ? 506  TYR A CD2 1 
ATOM   4190  C  CD2 B TYR A 1 506  ? 71.105 71.886  -15.226 0.50 11.22 ? 506  TYR A CD2 1 
ATOM   4191  C  CE1 A TYR A 1 506  ? 71.201 73.611  -18.310 0.50 9.79  ? 506  TYR A CE1 1 
ATOM   4192  C  CE1 B TYR A 1 506  ? 72.280 72.782  -17.581 0.50 10.37 ? 506  TYR A CE1 1 
ATOM   4193  C  CE2 A TYR A 1 506  ? 72.144 73.039  -16.176 0.50 8.44  ? 506  TYR A CE2 1 
ATOM   4194  C  CE2 B TYR A 1 506  ? 72.482 72.242  -15.251 0.50 9.52  ? 506  TYR A CE2 1 
ATOM   4195  C  CZ  A TYR A 1 506  ? 72.237 73.659  -17.392 0.50 9.33  ? 506  TYR A CZ  1 
ATOM   4196  C  CZ  B TYR A 1 506  ? 73.051 72.685  -16.436 0.50 10.51 ? 506  TYR A CZ  1 
ATOM   4197  O  OH  A TYR A 1 506  ? 73.405 74.328  -17.664 0.50 11.29 ? 506  TYR A OH  1 
ATOM   4198  O  OH  B TYR A 1 506  ? 74.396 73.046  -16.499 0.50 10.65 ? 506  TYR A OH  1 
ATOM   4199  N  N   . ARG A 1 507  ? 69.335 68.352  -16.228 1.00 7.85  ? 507  ARG A N   1 
ATOM   4200  C  CA  . ARG A 1 507  ? 70.260 67.227  -16.099 1.00 8.57  ? 507  ARG A CA  1 
ATOM   4201  C  C   . ARG A 1 507  ? 70.127 66.224  -17.260 1.00 8.55  ? 507  ARG A C   1 
ATOM   4202  O  O   . ARG A 1 507  ? 71.115 65.691  -17.762 1.00 10.22 ? 507  ARG A O   1 
ATOM   4203  C  CB  . ARG A 1 507  ? 70.042 66.504  -14.766 1.00 8.21  ? 507  ARG A CB  1 
ATOM   4204  C  CG  . ARG A 1 507  ? 71.138 65.502  -14.402 1.00 10.55 ? 507  ARG A CG  1 
ATOM   4205  C  CD  . ARG A 1 507  ? 71.022 65.071  -12.966 1.00 10.83 ? 507  ARG A CD  1 
ATOM   4206  N  NE  . ARG A 1 507  ? 72.029 64.073  -12.590 1.00 13.08 ? 507  ARG A NE  1 
ATOM   4207  C  CZ  . ARG A 1 507  ? 72.073 63.479  -11.381 1.00 13.29 ? 507  ARG A CZ  1 
ATOM   4208  N  NH1 . ARG A 1 507  ? 71.202 63.800  -10.432 1.00 14.14 ? 507  ARG A NH1 1 
ATOM   4209  N  NH2 . ARG A 1 507  ? 72.978 62.534  -11.139 1.00 15.58 ? 507  ARG A NH2 1 
ATOM   4210  N  N   . LEU A 1 508  ? 68.901 65.921  -17.661 1.00 7.95  ? 508  LEU A N   1 
ATOM   4211  C  CA  . LEU A 1 508  ? 68.681 64.886  -18.650 1.00 7.79  ? 508  LEU A CA  1 
ATOM   4212  C  C   . LEU A 1 508  ? 69.114 65.306  -20.055 1.00 8.13  ? 508  LEU A C   1 
ATOM   4213  O  O   . LEU A 1 508  ? 69.352 64.436  -20.920 1.00 9.41  ? 508  LEU A O   1 
ATOM   4214  C  CB  . LEU A 1 508  ? 67.191 64.521  -18.660 1.00 7.85  ? 508  LEU A CB  1 
ATOM   4215  C  CG  . LEU A 1 508  ? 66.731 63.704  -17.444 1.00 7.48  ? 508  LEU A CG  1 
ATOM   4216  C  CD1 . LEU A 1 508  ? 65.180 63.786  -17.374 1.00 8.55  ? 508  LEU A CD1 1 
ATOM   4217  C  CD2 . LEU A 1 508  ? 67.203 62.251  -17.591 1.00 9.68  ? 508  LEU A CD2 1 
ATOM   4218  N  N   . LEU A 1 509  ? 69.156 66.623  -20.307 1.00 8.64  ? 509  LEU A N   1 
ATOM   4219  C  CA  . LEU A 1 509  ? 69.428 67.147  -21.645 1.00 8.67  ? 509  LEU A CA  1 
ATOM   4220  C  C   . LEU A 1 509  ? 70.690 67.998  -21.714 1.00 9.87  ? 509  LEU A C   1 
ATOM   4221  O  O   . LEU A 1 509  ? 70.847 68.748  -22.680 1.00 10.62 ? 509  LEU A O   1 
ATOM   4222  C  CB  . LEU A 1 509  ? 68.222 67.959  -22.139 1.00 8.97  ? 509  LEU A CB  1 
ATOM   4223  C  CG  . LEU A 1 509  ? 66.985 67.125  -22.479 1.00 8.64  ? 509  LEU A CG  1 
ATOM   4224  C  CD1 . LEU A 1 509  ? 65.870 68.056  -22.898 1.00 8.96  ? 509  LEU A CD1 1 
ATOM   4225  C  CD2 . LEU A 1 509  ? 67.250 66.116  -23.593 1.00 10.19 ? 509  LEU A CD2 1 
ATOM   4226  N  N   . THR A 1 510  ? 71.596 67.851  -20.757 1.00 10.19 ? 510  THR A N   1 
ATOM   4227  C  CA  . THR A 1 510  ? 72.883 68.548  -20.879 1.00 10.57 ? 510  THR A CA  1 
ATOM   4228  C  C   . THR A 1 510  ? 74.013 67.521  -20.897 1.00 11.49 ? 510  THR A C   1 
ATOM   4229  O  O   . THR A 1 510  ? 73.994 66.521  -20.142 1.00 11.64 ? 510  THR A O   1 
ATOM   4230  C  CB  . THR A 1 510  ? 73.061 69.533  -19.720 1.00 10.90 ? 510  THR A CB  1 
ATOM   4231  O  OG1 . THR A 1 510  ? 71.995 70.497  -19.722 1.00 10.58 ? 510  THR A OG1 1 
ATOM   4232  C  CG2 . THR A 1 510  ? 74.318 70.410  -19.920 1.00 10.70 ? 510  THR A CG2 1 
ATOM   4233  N  N   . LYS A 1 511  ? 74.986 67.737  -21.787 1.00 12.84 ? 511  LYS A N   1 
ATOM   4234  C  CA  . LYS A 1 511  ? 76.126 66.819  -21.917 1.00 13.45 ? 511  LYS A CA  1 
ATOM   4235  C  C   . LYS A 1 511  ? 76.729 66.624  -20.528 1.00 13.35 ? 511  LYS A C   1 
ATOM   4236  O  O   . LYS A 1 511  ? 76.985 67.598  -19.843 1.00 12.11 ? 511  LYS A O   1 
ATOM   4237  C  CB  . LYS A 1 511  ? 77.150 67.446  -22.854 1.00 14.95 ? 511  LYS A CB  1 
ATOM   4238  C  CG  . LYS A 1 511  ? 78.410 66.606  -23.084 1.00 18.53 ? 511  LYS A CG  1 
ATOM   4239  C  CD  . LYS A 1 511  ? 79.219 67.232  -24.201 1.00 21.61 ? 511  LYS A CD  1 
ATOM   4240  C  CE  . LYS A 1 511  ? 80.479 66.462  -24.478 1.00 25.24 ? 511  LYS A CE  1 
ATOM   4241  N  NZ  . LYS A 1 511  ? 81.203 67.101  -25.612 1.00 29.55 ? 511  LYS A NZ  1 
ATOM   4242  N  N   . PRO A 1 512  ? 76.905 65.387  -20.063 1.00 14.69 ? 512  PRO A N   1 
ATOM   4243  C  CA  . PRO A 1 512  ? 77.302 65.166  -18.666 1.00 15.70 ? 512  PRO A CA  1 
ATOM   4244  C  C   . PRO A 1 512  ? 78.587 65.864  -18.221 1.00 15.23 ? 512  PRO A C   1 
ATOM   4245  O  O   . PRO A 1 512  ? 78.655 66.315  -17.077 1.00 15.42 ? 512  PRO A O   1 
ATOM   4246  C  CB  . PRO A 1 512  ? 77.453 63.648  -18.579 1.00 16.29 ? 512  PRO A CB  1 
ATOM   4247  C  CG  . PRO A 1 512  ? 76.541 63.145  -19.634 1.00 16.48 ? 512  PRO A CG  1 
ATOM   4248  C  CD  . PRO A 1 512  ? 76.628 64.119  -20.778 1.00 14.87 ? 512  PRO A CD  1 
ATOM   4249  N  N   . SER A 1 513  ? 79.578 65.995  -19.106 1.00 15.25 ? 513  SER A N   1 
ATOM   4250  C  CA  . SER A 1 513  ? 80.825 66.646  -18.696 1.00 15.24 ? 513  SER A CA  1 
ATOM   4251  C  C   . SER A 1 513  ? 80.733 68.176  -18.679 1.00 15.41 ? 513  SER A C   1 
ATOM   4252  O  O   . SER A 1 513  ? 81.678 68.855  -18.294 1.00 15.34 ? 513  SER A O   1 
ATOM   4253  C  CB  . SER A 1 513  ? 81.969 66.188  -19.595 1.00 15.34 ? 513  SER A CB  1 
ATOM   4254  O  OG  . SER A 1 513  ? 81.689 66.540  -20.922 1.00 15.81 ? 513  SER A OG  1 
ATOM   4255  N  N   . ILE A 1 514  ? 79.582 68.717  -19.081 1.00 14.85 ? 514  ILE A N   1 
ATOM   4256  C  CA  . ILE A 1 514  ? 79.313 70.152  -19.063 1.00 15.33 ? 514  ILE A CA  1 
ATOM   4257  C  C   . ILE A 1 514  ? 78.336 70.495  -17.932 1.00 13.88 ? 514  ILE A C   1 
ATOM   4258  O  O   . ILE A 1 514  ? 78.373 71.584  -17.372 1.00 14.06 ? 514  ILE A O   1 
ATOM   4259  C  CB  . ILE A 1 514  ? 78.728 70.619  -20.428 1.00 15.28 ? 514  ILE A CB  1 
ATOM   4260  C  CG1 . ILE A 1 514  ? 79.789 70.465  -21.528 1.00 18.13 ? 514  ILE A CG1 1 
ATOM   4261  C  CG2 . ILE A 1 514  ? 78.194 72.079  -20.331 1.00 15.92 ? 514  ILE A CG2 1 
ATOM   4262  C  CD1 . ILE A 1 514  ? 79.266 70.634  -22.938 1.00 19.25 ? 514  ILE A CD1 1 
ATOM   4263  N  N   . TYR A 1 515  ? 77.487 69.541  -17.581 1.00 12.66 ? 515  TYR A N   1 
ATOM   4264  C  CA  . TYR A 1 515  ? 76.430 69.780  -16.586 1.00 11.87 ? 515  TYR A CA  1 
ATOM   4265  C  C   . TYR A 1 515  ? 77.002 70.333  -15.290 1.00 11.83 ? 515  TYR A C   1 
ATOM   4266  O  O   . TYR A 1 515  ? 77.869 69.712  -14.663 1.00 11.64 ? 515  TYR A O   1 
ATOM   4267  C  CB  . TYR A 1 515  ? 75.734 68.452  -16.360 1.00 11.11 ? 515  TYR A CB  1 
ATOM   4268  C  CG  . TYR A 1 515  ? 74.713 68.432  -15.263 1.00 11.79 ? 515  TYR A CG  1 
ATOM   4269  C  CD1 . TYR A 1 515  ? 73.558 69.178  -15.339 1.00 9.58  ? 515  TYR A CD1 1 
ATOM   4270  C  CD2 . TYR A 1 515  ? 74.918 67.645  -14.155 1.00 11.14 ? 515  TYR A CD2 1 
ATOM   4271  C  CE1 . TYR A 1 515  ? 72.621 69.152  -14.309 1.00 10.26 ? 515  TYR A CE1 1 
ATOM   4272  C  CE2 . TYR A 1 515  ? 73.982 67.584  -13.139 1.00 9.10  ? 515  TYR A CE2 1 
ATOM   4273  C  CZ  . TYR A 1 515  ? 72.840 68.342  -13.221 1.00 11.72 ? 515  TYR A CZ  1 
ATOM   4274  O  OH  . TYR A 1 515  ? 71.921 68.298  -12.201 1.00 12.21 ? 515  TYR A OH  1 
ATOM   4275  N  N   . SER A 1 516  ? 76.524 71.507  -14.882 1.00 11.36 ? 516  SER A N   1 
ATOM   4276  C  CA  . SER A 1 516  ? 77.045 72.206  -13.709 1.00 12.47 ? 516  SER A CA  1 
ATOM   4277  C  C   . SER A 1 516  ? 75.919 72.885  -12.916 1.00 12.94 ? 516  SER A C   1 
ATOM   4278  O  O   . SER A 1 516  ? 75.738 74.110  -12.991 1.00 13.98 ? 516  SER A O   1 
ATOM   4279  C  CB  . SER A 1 516  ? 78.071 73.249  -14.168 1.00 13.39 ? 516  SER A CB  1 
ATOM   4280  O  OG  . SER A 1 516  ? 78.774 73.745  -13.043 1.00 16.40 ? 516  SER A OG  1 
ATOM   4281  N  N   . PRO A 1 517  ? 75.146 72.088  -12.173 1.00 12.76 ? 517  PRO A N   1 
ATOM   4282  C  CA  . PRO A 1 517  ? 73.918 72.608  -11.590 1.00 13.60 ? 517  PRO A CA  1 
ATOM   4283  C  C   . PRO A 1 517  ? 74.145 73.465  -10.358 1.00 14.36 ? 517  PRO A C   1 
ATOM   4284  O  O   . PRO A 1 517  ? 75.084 73.219  -9.603  1.00 16.39 ? 517  PRO A O   1 
ATOM   4285  C  CB  . PRO A 1 517  ? 73.163 71.338  -11.209 1.00 14.15 ? 517  PRO A CB  1 
ATOM   4286  C  CG  . PRO A 1 517  ? 74.211 70.395  -10.883 1.00 13.64 ? 517  PRO A CG  1 
ATOM   4287  C  CD  . PRO A 1 517  ? 75.358 70.667  -11.846 1.00 12.99 ? 517  PRO A CD  1 
ATOM   4288  N  N   . ASP A 1 518  ? 73.354 74.509  -10.250 1.00 14.25 ? 518  ASP A N   1 
ATOM   4289  C  CA  . ASP A 1 518  ? 73.057 75.192  -9.014  1.00 15.38 ? 518  ASP A CA  1 
ATOM   4290  C  C   . ASP A 1 518  ? 71.629 74.776  -8.690  1.00 13.75 ? 518  ASP A C   1 
ATOM   4291  O  O   . ASP A 1 518  ? 70.719 75.042  -9.432  1.00 13.38 ? 518  ASP A O   1 
ATOM   4292  C  CB  . ASP A 1 518  ? 73.140 76.691  -9.294  1.00 16.93 ? 518  ASP A CB  1 
ATOM   4293  C  CG  . ASP A 1 518  ? 72.588 77.568  -8.177  1.00 21.15 ? 518  ASP A CG  1 
ATOM   4294  O  OD1 . ASP A 1 518  ? 72.078 77.087  -7.145  1.00 21.83 ? 518  ASP A OD1 1 
ATOM   4295  O  OD2 . ASP A 1 518  ? 72.672 78.788  -8.376  1.00 23.24 ? 518  ASP A OD2 1 
ATOM   4296  N  N   . PHE A 1 519  ? 71.476 74.057  -7.601  1.00 13.65 ? 519  PHE A N   1 
ATOM   4297  C  CA  . PHE A 1 519  ? 70.183 73.420  -7.316  1.00 13.93 ? 519  PHE A CA  1 
ATOM   4298  C  C   . PHE A 1 519  ? 69.110 74.406  -6.913  1.00 14.80 ? 519  PHE A C   1 
ATOM   4299  O  O   . PHE A 1 519  ? 67.967 74.015  -6.740  1.00 15.29 ? 519  PHE A O   1 
ATOM   4300  C  CB  . PHE A 1 519  ? 70.341 72.333  -6.275  1.00 13.67 ? 519  PHE A CB  1 
ATOM   4301  C  CG  . PHE A 1 519  ? 71.189 71.188  -6.733  1.00 11.98 ? 519  PHE A CG  1 
ATOM   4302  C  CD1 . PHE A 1 519  ? 70.926 70.524  -7.946  1.00 10.70 ? 519  PHE A CD1 1 
ATOM   4303  C  CD2 . PHE A 1 519  ? 72.257 70.776  -5.973  1.00 13.31 ? 519  PHE A CD2 1 
ATOM   4304  C  CE1 . PHE A 1 519  ? 71.706 69.452  -8.363  1.00 13.32 ? 519  PHE A CE1 1 
ATOM   4305  C  CE2 . PHE A 1 519  ? 73.046 69.711  -6.390  1.00 14.10 ? 519  PHE A CE2 1 
ATOM   4306  C  CZ  . PHE A 1 519  ? 72.767 69.044  -7.585  1.00 14.39 ? 519  PHE A CZ  1 
ATOM   4307  N  N   . SER A 1 520  ? 69.472 75.677  -6.783  1.00 14.77 ? 520  SER A N   1 
ATOM   4308  C  CA  . SER A 1 520  ? 68.510 76.722  -6.467  1.00 15.92 ? 520  SER A CA  1 
ATOM   4309  C  C   . SER A 1 520  ? 68.105 77.545  -7.693  1.00 15.22 ? 520  SER A C   1 
ATOM   4310  O  O   . SER A 1 520  ? 67.187 78.341  -7.614  1.00 15.91 ? 520  SER A O   1 
ATOM   4311  C  CB  . SER A 1 520  ? 69.079 77.660  -5.401  1.00 16.92 ? 520  SER A CB  1 
ATOM   4312  O  OG  . SER A 1 520  ? 70.027 78.569  -5.953  1.00 19.48 ? 520  SER A OG  1 
ATOM   4313  N  N   . PHE A 1 521  ? 68.755 77.313  -8.837  1.00 14.72 ? 521  PHE A N   1 
ATOM   4314  C  CA  . PHE A 1 521  ? 68.553 78.143  -10.015 1.00 14.38 ? 521  PHE A CA  1 
ATOM   4315  C  C   . PHE A 1 521  ? 67.394 77.637  -10.873 1.00 14.14 ? 521  PHE A C   1 
ATOM   4316  O  O   . PHE A 1 521  ? 67.120 76.441  -10.900 1.00 14.58 ? 521  PHE A O   1 
ATOM   4317  C  CB  . PHE A 1 521  ? 69.843 78.172  -10.850 1.00 14.82 ? 521  PHE A CB  1 
ATOM   4318  C  CG  . PHE A 1 521  ? 69.797 79.109  -12.040 1.00 16.04 ? 521  PHE A CG  1 
ATOM   4319  C  CD1 . PHE A 1 521  ? 69.975 80.482  -11.868 1.00 19.94 ? 521  PHE A CD1 1 
ATOM   4320  C  CD2 . PHE A 1 521  ? 69.622 78.615  -13.340 1.00 18.47 ? 521  PHE A CD2 1 
ATOM   4321  C  CE1 . PHE A 1 521  ? 69.933 81.360  -12.969 1.00 21.80 ? 521  PHE A CE1 1 
ATOM   4322  C  CE2 . PHE A 1 521  ? 69.575 79.489  -14.441 1.00 20.22 ? 521  PHE A CE2 1 
ATOM   4323  C  CZ  . PHE A 1 521  ? 69.735 80.856  -14.253 1.00 20.56 ? 521  PHE A CZ  1 
ATOM   4324  N  N   . SER A 1 522  ? 66.736 78.551  -11.576 1.00 13.95 ? 522  SER A N   1 
ATOM   4325  C  CA  A SER A 1 522  ? 65.684 78.194  -12.519 0.50 13.84 ? 522  SER A CA  1 
ATOM   4326  C  CA  B SER A 1 522  ? 65.672 78.233  -12.517 0.50 13.68 ? 522  SER A CA  1 
ATOM   4327  C  C   . SER A 1 522  ? 66.243 78.140  -13.937 1.00 13.28 ? 522  SER A C   1 
ATOM   4328  O  O   . SER A 1 522  ? 66.390 79.166  -14.622 1.00 14.56 ? 522  SER A O   1 
ATOM   4329  C  CB  A SER A 1 522  ? 64.508 79.169  -12.438 0.50 14.32 ? 522  SER A CB  1 
ATOM   4330  C  CB  B SER A 1 522  ? 64.597 79.327  -12.461 0.50 14.07 ? 522  SER A CB  1 
ATOM   4331  O  OG  A SER A 1 522  ? 63.921 79.107  -11.151 0.50 16.53 ? 522  SER A OG  1 
ATOM   4332  O  OG  B SER A 1 522  ? 63.662 79.200  -13.509 0.50 15.51 ? 522  SER A OG  1 
ATOM   4333  N  N   . TYR A 1 523  ? 66.585 76.933  -14.377 1.00 10.72 ? 523  TYR A N   1 
ATOM   4334  C  CA  . TYR A 1 523  ? 67.043 76.718  -15.746 1.00 9.82  ? 523  TYR A CA  1 
ATOM   4335  C  C   . TYR A 1 523  ? 65.927 76.782  -16.755 1.00 10.55 ? 523  TYR A C   1 
ATOM   4336  O  O   . TYR A 1 523  ? 66.144 77.203  -17.901 1.00 9.97  ? 523  TYR A O   1 
ATOM   4337  C  CB  . TYR A 1 523  ? 67.740 75.363  -15.870 1.00 10.49 ? 523  TYR A CB  1 
ATOM   4338  C  CG  . TYR A 1 523  ? 68.996 75.351  -15.072 1.00 10.49 ? 523  TYR A CG  1 
ATOM   4339  C  CD1 . TYR A 1 523  ? 70.156 75.957  -15.573 1.00 13.51 ? 523  TYR A CD1 1 
ATOM   4340  C  CD2 . TYR A 1 523  ? 69.033 74.782  -13.805 1.00 10.62 ? 523  TYR A CD2 1 
ATOM   4341  C  CE1 . TYR A 1 523  ? 71.321 75.981  -14.832 1.00 15.73 ? 523  TYR A CE1 1 
ATOM   4342  C  CE2 . TYR A 1 523  ? 70.188 74.792  -13.055 1.00 13.73 ? 523  TYR A CE2 1 
ATOM   4343  C  CZ  . TYR A 1 523  ? 71.322 75.412  -13.571 1.00 14.37 ? 523  TYR A CZ  1 
ATOM   4344  O  OH  . TYR A 1 523  ? 72.469 75.422  -12.821 1.00 16.24 ? 523  TYR A OH  1 
ATOM   4345  N  N   . PHE A 1 524  ? 64.723 76.352  -16.354 1.00 8.61  ? 524  PHE A N   1 
ATOM   4346  C  CA  . PHE A 1 524  ? 63.535 76.397  -17.206 1.00 9.27  ? 524  PHE A CA  1 
ATOM   4347  C  C   . PHE A 1 524  ? 62.372 76.887  -16.385 1.00 10.63 ? 524  PHE A C   1 
ATOM   4348  O  O   . PHE A 1 524  ? 62.320 76.629  -15.167 1.00 11.77 ? 524  PHE A O   1 
ATOM   4349  C  CB  . PHE A 1 524  ? 63.143 75.011  -17.759 1.00 8.71  ? 524  PHE A CB  1 
ATOM   4350  C  CG  . PHE A 1 524  ? 64.193 74.371  -18.625 1.00 8.51  ? 524  PHE A CG  1 
ATOM   4351  C  CD1 . PHE A 1 524  ? 65.229 73.622  -18.056 1.00 9.54  ? 524  PHE A CD1 1 
ATOM   4352  C  CD2 . PHE A 1 524  ? 64.144 74.509  -20.009 1.00 8.34  ? 524  PHE A CD2 1 
ATOM   4353  C  CE1 . PHE A 1 524  ? 66.203 73.039  -18.852 1.00 10.45 ? 524  PHE A CE1 1 
ATOM   4354  C  CE2 . PHE A 1 524  ? 65.102 73.921  -20.811 1.00 9.58  ? 524  PHE A CE2 1 
ATOM   4355  C  CZ  . PHE A 1 524  ? 66.149 73.202  -20.231 1.00 9.82  ? 524  PHE A CZ  1 
ATOM   4356  N  N   . THR A 1 525  ? 61.426 77.526  -17.051 1.00 10.39 ? 525  THR A N   1 
ATOM   4357  C  CA  . THR A 1 525  ? 60.124 77.711  -16.424 1.00 12.58 ? 525  THR A CA  1 
ATOM   4358  C  C   . THR A 1 525  ? 59.088 76.926  -17.177 1.00 11.38 ? 525  THR A C   1 
ATOM   4359  O  O   . THR A 1 525  ? 59.180 76.764  -18.389 1.00 11.83 ? 525  THR A O   1 
ATOM   4360  C  CB  . THR A 1 525  ? 59.697 79.173  -16.394 1.00 13.85 ? 525  THR A CB  1 
ATOM   4361  O  OG1 . THR A 1 525  ? 59.719 79.670  -17.724 1.00 17.67 ? 525  THR A OG1 1 
ATOM   4362  C  CG2 . THR A 1 525  ? 60.698 80.065  -15.661 1.00 17.26 ? 525  THR A CG2 1 
ATOM   4363  N  N   . LEU A 1 526  ? 58.103 76.420  -16.460 1.00 9.99  ? 526  LEU A N   1 
ATOM   4364  C  CA  . LEU A 1 526  ? 57.006 75.734  -17.085 1.00 11.26 ? 526  LEU A CA  1 
ATOM   4365  C  C   . LEU A 1 526  ? 56.081 76.739  -17.739 1.00 11.81 ? 526  LEU A C   1 
ATOM   4366  O  O   . LEU A 1 526  ? 55.844 77.829  -17.208 1.00 13.92 ? 526  LEU A O   1 
ATOM   4367  C  CB  . LEU A 1 526  ? 56.247 74.883  -16.048 1.00 12.13 ? 526  LEU A CB  1 
ATOM   4368  C  CG  . LEU A 1 526  ? 56.802 73.502  -15.711 1.00 14.61 ? 526  LEU A CG  1 
ATOM   4369  C  CD1 . LEU A 1 526  ? 56.126 73.034  -14.422 1.00 16.54 ? 526  LEU A CD1 1 
ATOM   4370  C  CD2 . LEU A 1 526  ? 56.534 72.511  -16.835 1.00 17.11 ? 526  LEU A CD2 1 
ATOM   4371  N  N   . ASP A 1 527  ? 55.530 76.359  -18.879 1.00 9.72  ? 527  ASP A N   1 
ATOM   4372  C  CA  . ASP A 1 527  ? 54.524 77.160  -19.536 1.00 11.82 ? 527  ASP A CA  1 
ATOM   4373  C  C   . ASP A 1 527  ? 53.284 76.271  -19.628 1.00 11.59 ? 527  ASP A C   1 
ATOM   4374  O  O   . ASP A 1 527  ? 53.324 75.194  -20.180 1.00 14.85 ? 527  ASP A O   1 
ATOM   4375  C  CB  . ASP A 1 527  ? 55.001 77.546  -20.950 1.00 12.29 ? 527  ASP A CB  1 
ATOM   4376  C  CG  . ASP A 1 527  ? 53.984 78.395  -21.702 1.00 16.44 ? 527  ASP A CG  1 
ATOM   4377  O  OD1 . ASP A 1 527  ? 53.590 79.455  -21.178 1.00 21.44 ? 527  ASP A OD1 1 
ATOM   4378  O  OD2 . ASP A 1 527  ? 53.509 78.074  -22.813 1.00 20.79 ? 527  ASP A OD2 1 
ATOM   4379  N  N   . ASP A 1 528  ? 52.201 76.698  -19.013 1.00 12.16 ? 528  ASP A N   1 
ATOM   4380  C  CA  . ASP A 1 528  ? 50.990 75.911  -19.046 1.00 11.49 ? 528  ASP A CA  1 
ATOM   4381  C  C   . ASP A 1 528  ? 49.906 76.770  -19.649 1.00 11.90 ? 528  ASP A C   1 
ATOM   4382  O  O   . ASP A 1 528  ? 49.552 77.816  -19.119 1.00 11.84 ? 528  ASP A O   1 
ATOM   4383  C  CB  . ASP A 1 528  ? 50.654 75.459  -17.633 1.00 11.10 ? 528  ASP A CB  1 
ATOM   4384  C  CG  . ASP A 1 528  ? 49.638 74.354  -17.604 1.00 12.31 ? 528  ASP A CG  1 
ATOM   4385  O  OD1 . ASP A 1 528  ? 48.634 74.382  -18.357 1.00 14.08 ? 528  ASP A OD1 1 
ATOM   4386  O  OD2 . ASP A 1 528  ? 49.800 73.383  -16.842 1.00 14.53 ? 528  ASP A OD2 1 
ATOM   4387  N  N   . SER A 1 529  ? 49.392 76.316  -20.786 1.00 11.92 ? 529  SER A N   1 
ATOM   4388  C  CA  . SER A 1 529  ? 48.337 77.018  -21.526 1.00 13.98 ? 529  SER A CA  1 
ATOM   4389  C  C   . SER A 1 529  ? 46.977 76.917  -20.888 1.00 13.63 ? 529  SER A C   1 
ATOM   4390  O  O   . SER A 1 529  ? 46.096 77.688  -21.214 1.00 15.08 ? 529  SER A O   1 
ATOM   4391  C  CB  . SER A 1 529  ? 48.210 76.456  -22.938 1.00 15.52 ? 529  SER A CB  1 
ATOM   4392  O  OG  . SER A 1 529  ? 49.426 76.639  -23.617 1.00 19.69 ? 529  SER A OG  1 
ATOM   4393  N  N   . ARG A 1 530  ? 46.763 75.938  -20.014 1.00 11.72 ? 530  ARG A N   1 
ATOM   4394  C  CA  . ARG A 1 530  ? 45.409 75.683  -19.537 1.00 12.03 ? 530  ARG A CA  1 
ATOM   4395  C  C   . ARG A 1 530  ? 45.272 75.744  -18.062 1.00 12.96 ? 530  ARG A C   1 
ATOM   4396  O  O   . ARG A 1 530  ? 44.230 75.360  -17.540 1.00 15.13 ? 530  ARG A O   1 
ATOM   4397  C  CB  . ARG A 1 530  ? 44.917 74.313  -20.032 1.00 12.16 ? 530  ARG A CB  1 
ATOM   4398  C  CG  . ARG A 1 530  ? 44.914 74.243  -21.558 1.00 11.33 ? 530  ARG A CG  1 
ATOM   4399  C  CD  . ARG A 1 530  ? 44.239 73.025  -22.149 1.00 12.57 ? 530  ARG A CD  1 
ATOM   4400  N  NE  . ARG A 1 530  ? 44.893 71.816  -21.661 1.00 12.86 ? 530  ARG A NE  1 
ATOM   4401  C  CZ  . ARG A 1 530  ? 44.722 70.615  -22.210 1.00 13.94 ? 530  ARG A CZ  1 
ATOM   4402  N  NH1 . ARG A 1 530  ? 43.926 70.476  -23.266 1.00 15.28 ? 530  ARG A NH1 1 
ATOM   4403  N  NH2 . ARG A 1 530  ? 45.344 69.568  -21.686 1.00 14.01 ? 530  ARG A NH2 1 
ATOM   4404  N  N   . TRP A 1 531  ? 46.296 76.214  -17.368 1.00 10.85 ? 531  TRP A N   1 
ATOM   4405  C  CA  . TRP A 1 531  ? 46.174 76.462  -15.928 1.00 12.11 ? 531  TRP A CA  1 
ATOM   4406  C  C   . TRP A 1 531  ? 47.072 77.626  -15.489 1.00 13.21 ? 531  TRP A C   1 
ATOM   4407  O  O   . TRP A 1 531  ? 48.273 77.566  -15.724 1.00 12.39 ? 531  TRP A O   1 
ATOM   4408  C  CB  . TRP A 1 531  ? 46.529 75.228  -15.078 1.00 12.82 ? 531  TRP A CB  1 
ATOM   4409  C  CG  . TRP A 1 531  ? 46.433 75.610  -13.638 1.00 14.12 ? 531  TRP A CG  1 
ATOM   4410  C  CD1 . TRP A 1 531  ? 47.464 76.034  -12.812 1.00 15.56 ? 531  TRP A CD1 1 
ATOM   4411  C  CD2 . TRP A 1 531  ? 45.243 75.691  -12.874 1.00 15.38 ? 531  TRP A CD2 1 
ATOM   4412  N  NE1 . TRP A 1 531  ? 46.962 76.341  -11.571 1.00 18.20 ? 531  TRP A NE1 1 
ATOM   4413  C  CE2 . TRP A 1 531  ? 45.603 76.148  -11.580 1.00 13.78 ? 531  TRP A CE2 1 
ATOM   4414  C  CE3 . TRP A 1 531  ? 43.911 75.409  -13.139 1.00 16.20 ? 531  TRP A CE3 1 
ATOM   4415  C  CZ2 . TRP A 1 531  ? 44.671 76.318  -10.559 1.00 15.45 ? 531  TRP A CZ2 1 
ATOM   4416  C  CZ3 . TRP A 1 531  ? 42.970 75.605  -12.124 1.00 15.88 ? 531  TRP A CZ3 1 
ATOM   4417  C  CH2 . TRP A 1 531  ? 43.364 76.049  -10.850 1.00 16.77 ? 531  TRP A CH2 1 
ATOM   4418  N  N   . PRO A 1 532  ? 46.521 78.669  -14.883 1.00 14.04 ? 532  PRO A N   1 
ATOM   4419  C  CA  . PRO A 1 532  ? 45.122 78.751  -14.469 1.00 15.34 ? 532  PRO A CA  1 
ATOM   4420  C  C   . PRO A 1 532  ? 44.193 79.080  -15.618 1.00 17.67 ? 532  PRO A C   1 
ATOM   4421  O  O   . PRO A 1 532  ? 43.006 78.978  -15.471 1.00 18.28 ? 532  PRO A O   1 
ATOM   4422  C  CB  . PRO A 1 532  ? 45.126 79.931  -13.475 1.00 15.15 ? 532  PRO A CB  1 
ATOM   4423  C  CG  . PRO A 1 532  ? 46.475 79.982  -12.974 1.00 17.54 ? 532  PRO A CG  1 
ATOM   4424  C  CD  . PRO A 1 532  ? 47.354 79.627  -14.141 1.00 14.95 ? 532  PRO A CD  1 
ATOM   4425  N  N   . GLY A 1 533  ? 44.757 79.463  -16.750 1.00 19.69 ? 533  GLY A N   1 
ATOM   4426  C  CA  . GLY A 1 533  ? 43.981 79.610  -17.964 1.00 23.55 ? 533  GLY A CA  1 
ATOM   4427  C  C   . GLY A 1 533  ? 43.654 81.054  -18.293 1.00 27.34 ? 533  GLY A C   1 
ATOM   4428  O  O   . GLY A 1 533  ? 43.600 81.909  -17.407 1.00 27.12 ? 533  GLY A O   1 
ATOM   4429  N  N   . SER A 1 534  ? 43.469 81.305  -19.592 1.00 30.47 ? 534  SER A N   1 
ATOM   4430  C  CA  . SER A 1 534  ? 43.318 82.650  -20.164 1.00 33.59 ? 534  SER A CA  1 
ATOM   4431  C  C   . SER A 1 534  ? 42.150 83.200  -19.372 1.00 35.15 ? 534  SER A C   1 
ATOM   4432  O  O   . SER A 1 534  ? 41.121 82.540  -19.312 1.00 36.08 ? 534  SER A O   1 
ATOM   4433  C  CB  . SER A 1 534  ? 42.847 82.532  -21.632 1.00 34.03 ? 534  SER A CB  1 
ATOM   4434  O  OG  . SER A 1 534  ? 43.841 82.889  -22.581 1.00 35.99 ? 534  SER A OG  1 
ATOM   4435  N  N   . GLY A 1 535  ? 42.276 84.373  -18.771 1.00 36.55 ? 535  GLY A N   1 
ATOM   4436  C  CA  . GLY A 1 535  ? 41.141 84.979  -18.087 1.00 38.06 ? 535  GLY A CA  1 
ATOM   4437  C  C   . GLY A 1 535  ? 40.974 84.526  -16.646 1.00 39.23 ? 535  GLY A C   1 
ATOM   4438  O  O   . GLY A 1 535  ? 40.103 84.996  -15.887 1.00 39.06 ? 535  GLY A O   1 
ATOM   4439  N  N   . VAL A 1 536  ? 41.823 83.581  -16.261 1.00 40.29 ? 536  VAL A N   1 
ATOM   4440  C  CA  . VAL A 1 536  ? 41.930 83.184  -14.870 1.00 41.42 ? 536  VAL A CA  1 
ATOM   4441  C  C   . VAL A 1 536  ? 43.085 83.984  -14.253 1.00 42.40 ? 536  VAL A C   1 
ATOM   4442  O  O   . VAL A 1 536  ? 42.946 84.619  -13.208 1.00 42.48 ? 536  VAL A O   1 
ATOM   4443  C  CB  . VAL A 1 536  ? 42.207 81.676  -14.779 1.00 41.71 ? 536  VAL A CB  1 
ATOM   4444  C  CG1 . VAL A 1 536  ? 41.382 81.030  -13.681 1.00 40.82 ? 536  VAL A CG1 1 
ATOM   4445  C  CG2 . VAL A 1 536  ? 41.930 81.002  -16.113 1.00 41.81 ? 536  VAL A CG2 1 
ATOM   4446  N  N   . GLU A 1 537  ? 44.211 83.979  -14.950 1.00 42.95 ? 537  GLU A N   1 
ATOM   4447  C  CA  . GLU A 1 537  ? 45.448 84.589  -14.470 1.00 43.49 ? 537  GLU A CA  1 
ATOM   4448  C  C   . GLU A 1 537  ? 46.336 84.899  -15.664 1.00 43.09 ? 537  GLU A C   1 
ATOM   4449  O  O   . GLU A 1 537  ? 46.475 84.060  -16.562 1.00 43.27 ? 537  GLU A O   1 
ATOM   4450  C  CB  . GLU A 1 537  ? 46.179 83.617  -13.538 1.00 43.42 ? 537  GLU A CB  1 
ATOM   4451  C  CG  . GLU A 1 537  ? 47.485 84.129  -12.948 1.00 44.29 ? 537  GLU A CG  1 
ATOM   4452  C  CD  . GLU A 1 537  ? 47.938 83.317  -11.743 1.00 44.85 ? 537  GLU A CD  1 
ATOM   4453  O  OE1 . GLU A 1 537  ? 47.227 83.334  -10.708 1.00 45.82 ? 537  GLU A OE1 1 
ATOM   4454  O  OE2 . GLU A 1 537  ? 49.011 82.664  -11.823 1.00 46.84 ? 537  GLU A OE2 1 
ATOM   4455  N  N   . ASP A 1 538  ? 46.899 86.105  -15.739 1.00 42.74 ? 538  ASP A N   1 
ATOM   4456  C  CA  . ASP A 1 538  ? 48.089 86.266  -16.587 1.00 42.19 ? 538  ASP A CA  1 
ATOM   4457  C  C   . ASP A 1 538  ? 49.296 85.743  -15.856 1.00 41.09 ? 538  ASP A C   1 
ATOM   4458  O  O   . ASP A 1 538  ? 49.878 86.404  -15.010 1.00 41.42 ? 538  ASP A O   1 
ATOM   4459  C  CB  . ASP A 1 538  ? 48.327 87.678  -17.170 1.00 42.49 ? 538  ASP A CB  1 
ATOM   4460  C  CG  . ASP A 1 538  ? 49.138 87.634  -18.479 1.00 43.64 ? 538  ASP A CG  1 
ATOM   4461  O  OD1 . ASP A 1 538  ? 49.273 86.531  -19.035 1.00 43.81 ? 538  ASP A OD1 1 
ATOM   4462  O  OD2 . ASP A 1 538  ? 49.625 88.684  -18.981 1.00 44.77 ? 538  ASP A OD2 1 
ATOM   4463  N  N   . SER A 1 539  ? 49.692 84.527  -16.208 1.00 39.29 ? 539  SER A N   1 
ATOM   4464  C  CA  . SER A 1 539  ? 50.888 83.959  -15.630 1.00 37.41 ? 539  SER A CA  1 
ATOM   4465  C  C   . SER A 1 539  ? 51.819 83.478  -16.717 1.00 35.49 ? 539  SER A C   1 
ATOM   4466  O  O   . SER A 1 539  ? 52.942 83.081  -16.431 1.00 36.31 ? 539  SER A O   1 
ATOM   4467  C  CB  . SER A 1 539  ? 50.553 82.835  -14.670 1.00 37.80 ? 539  SER A CB  1 
ATOM   4468  O  OG  . SER A 1 539  ? 50.023 81.732  -15.370 1.00 38.03 ? 539  SER A OG  1 
ATOM   4469  N  N   . ARG A 1 540  ? 51.331 83.532  -17.956 1.00 32.53 ? 540  ARG A N   1 
ATOM   4470  C  CA  . ARG A 1 540  ? 52.053 82.996  -19.095 1.00 28.60 ? 540  ARG A CA  1 
ATOM   4471  C  C   . ARG A 1 540  ? 53.129 83.943  -19.525 1.00 26.38 ? 540  ARG A C   1 
ATOM   4472  O  O   . ARG A 1 540  ? 52.858 85.079  -19.871 1.00 26.31 ? 540  ARG A O   1 
ATOM   4473  C  CB  . ARG A 1 540  ? 51.136 82.672  -20.264 1.00 28.36 ? 540  ARG A CB  1 
ATOM   4474  C  CG  . ARG A 1 540  ? 50.493 81.311  -20.118 1.00 26.96 ? 540  ARG A CG  1 
ATOM   4475  C  CD  . ARG A 1 540  ? 49.841 80.860  -21.371 1.00 21.47 ? 540  ARG A CD  1 
ATOM   4476  N  NE  . ARG A 1 540  ? 50.781 80.119  -22.183 1.00 16.77 ? 540  ARG A NE  1 
ATOM   4477  C  CZ  . ARG A 1 540  ? 50.495 79.636  -23.375 1.00 16.48 ? 540  ARG A CZ  1 
ATOM   4478  N  NH1 . ARG A 1 540  ? 49.296 79.831  -23.892 1.00 13.86 ? 540  ARG A NH1 1 
ATOM   4479  N  NH2 . ARG A 1 540  ? 51.410 78.982  -24.042 1.00 16.80 ? 540  ARG A NH2 1 
ATOM   4480  N  N   . THR A 1 541  ? 54.350 83.438  -19.485 1.00 23.86 ? 541  THR A N   1 
ATOM   4481  C  CA  . THR A 1 541  ? 55.500 84.190  -19.893 1.00 21.94 ? 541  THR A CA  1 
ATOM   4482  C  C   . THR A 1 541  ? 55.549 84.261  -21.401 1.00 19.55 ? 541  THR A C   1 
ATOM   4483  O  O   . THR A 1 541  ? 55.192 83.328  -22.083 1.00 20.33 ? 541  THR A O   1 
ATOM   4484  C  CB  . THR A 1 541  ? 56.809 83.643  -19.285 1.00 23.03 ? 541  THR A CB  1 
ATOM   4485  O  OG1 . THR A 1 541  ? 57.517 82.861  -20.243 1.00 24.77 ? 541  THR A OG1 1 
ATOM   4486  C  CG2 . THR A 1 541  ? 56.538 82.807  -18.038 1.00 23.03 ? 541  THR A CG2 1 
ATOM   4487  N  N   . THR A 1 542  ? 55.946 85.417  -21.900 1.00 16.51 ? 542  THR A N   1 
ATOM   4488  C  CA  . THR A 1 542  ? 56.183 85.614  -23.308 1.00 14.20 ? 542  THR A CA  1 
ATOM   4489  C  C   . THR A 1 542  ? 57.655 85.358  -23.566 1.00 12.23 ? 542  THR A C   1 
ATOM   4490  O  O   . THR A 1 542  ? 58.517 85.836  -22.797 1.00 13.18 ? 542  THR A O   1 
ATOM   4491  C  CB  . THR A 1 542  ? 55.818 87.048  -23.663 1.00 14.87 ? 542  THR A CB  1 
ATOM   4492  O  OG1 . THR A 1 542  ? 54.419 87.228  -23.413 1.00 17.39 ? 542  THR A OG1 1 
ATOM   4493  C  CG2 . THR A 1 542  ? 55.984 87.309  -25.161 1.00 14.91 ? 542  THR A CG2 1 
ATOM   4494  N  N   . ILE A 1 543  ? 57.942 84.607  -24.623 1.00 10.82 ? 543  ILE A N   1 
ATOM   4495  C  CA  . ILE A 1 543  ? 59.324 84.436  -25.066 1.00 10.01 ? 543  ILE A CA  1 
ATOM   4496  C  C   . ILE A 1 543  ? 59.699 85.717  -25.827 1.00 10.88 ? 543  ILE A C   1 
ATOM   4497  O  O   . ILE A 1 543  ? 59.054 86.041  -26.827 1.00 11.46 ? 543  ILE A O   1 
ATOM   4498  C  CB  . ILE A 1 543  ? 59.433 83.223  -25.952 1.00 10.44 ? 543  ILE A CB  1 
ATOM   4499  C  CG1 . ILE A 1 543  ? 59.146 81.943  -25.129 1.00 9.94  ? 543  ILE A CG1 1 
ATOM   4500  C  CG2 . ILE A 1 543  ? 60.819 83.201  -26.687 1.00 10.62 ? 543  ILE A CG2 1 
ATOM   4501  C  CD1 . ILE A 1 543  ? 59.030 80.691  -25.972 1.00 10.49 ? 543  ILE A CD1 1 
ATOM   4502  N  N   . ILE A 1 544  ? 60.684 86.443  -25.291 1.00 11.41 ? 544  ILE A N   1 
ATOM   4503  C  CA  . ILE A 1 544  ? 61.072 87.736  -25.850 1.00 12.09 ? 544  ILE A CA  1 
ATOM   4504  C  C   . ILE A 1 544  ? 62.259 87.554  -26.782 1.00 12.83 ? 544  ILE A C   1 
ATOM   4505  O  O   . ILE A 1 544  ? 63.362 87.187  -26.365 1.00 12.99 ? 544  ILE A O   1 
ATOM   4506  C  CB  . ILE A 1 544  ? 61.329 88.738  -24.725 1.00 13.43 ? 544  ILE A CB  1 
ATOM   4507  C  CG1 . ILE A 1 544  ? 60.014 88.990  -23.983 1.00 15.95 ? 544  ILE A CG1 1 
ATOM   4508  C  CG2 . ILE A 1 544  ? 61.851 90.036  -25.297 1.00 14.28 ? 544  ILE A CG2 1 
ATOM   4509  C  CD1 . ILE A 1 544  ? 60.108 89.995  -22.847 1.00 20.80 ? 544  ILE A CD1 1 
ATOM   4510  N  N   . LEU A 1 545  ? 61.984 87.740  -28.063 1.00 12.33 ? 545  LEU A N   1 
ATOM   4511  C  CA  . LEU A 1 545  ? 63.001 87.642  -29.095 1.00 12.50 ? 545  LEU A CA  1 
ATOM   4512  C  C   . LEU A 1 545  ? 63.137 88.998  -29.767 1.00 12.44 ? 545  LEU A C   1 
ATOM   4513  O  O   . LEU A 1 545  ? 62.192 89.769  -29.796 1.00 13.18 ? 545  LEU A O   1 
ATOM   4514  C  CB  . LEU A 1 545  ? 62.620 86.572  -30.114 1.00 12.28 ? 545  LEU A CB  1 
ATOM   4515  C  CG  . LEU A 1 545  ? 62.430 85.145  -29.566 1.00 13.41 ? 545  LEU A CG  1 
ATOM   4516  C  CD1 . LEU A 1 545  ? 61.982 84.208  -30.664 1.00 14.86 ? 545  LEU A CD1 1 
ATOM   4517  C  CD2 . LEU A 1 545  ? 63.702 84.602  -28.922 1.00 13.13 ? 545  LEU A CD2 1 
ATOM   4518  N  N   . GLY A 1 546  ? 64.300 89.264  -30.336 1.00 12.95 ? 546  GLY A N   1 
ATOM   4519  C  CA  . GLY A 1 546  ? 64.494 90.525  -31.035 1.00 13.02 ? 546  GLY A CA  1 
ATOM   4520  C  C   . GLY A 1 546  ? 65.889 90.548  -31.581 1.00 13.50 ? 546  GLY A C   1 
ATOM   4521  O  O   . GLY A 1 546  ? 66.818 89.999  -30.993 1.00 12.06 ? 546  GLY A O   1 
ATOM   4522  N  N   . GLU A 1 547  ? 66.036 91.234  -32.706 1.00 14.99 ? 547  GLU A N   1 
ATOM   4523  C  CA  . GLU A 1 547  ? 67.343 91.387  -33.340 1.00 17.43 ? 547  GLU A CA  1 
ATOM   4524  C  C   . GLU A 1 547  ? 68.389 92.023  -32.422 1.00 17.37 ? 547  GLU A C   1 
ATOM   4525  O  O   . GLU A 1 547  ? 69.577 91.685  -32.479 1.00 18.54 ? 547  GLU A O   1 
ATOM   4526  C  CB  . GLU A 1 547  ? 67.169 92.247  -34.577 1.00 18.74 ? 547  GLU A CB  1 
ATOM   4527  C  CG  . GLU A 1 547  ? 68.410 92.455  -35.426 1.00 25.50 ? 547  GLU A CG  1 
ATOM   4528  C  CD  . GLU A 1 547  ? 68.088 93.224  -36.695 1.00 31.90 ? 547  GLU A CD  1 
ATOM   4529  O  OE1 . GLU A 1 547  ? 66.884 93.308  -37.035 1.00 34.67 ? 547  GLU A OE1 1 
ATOM   4530  O  OE2 . GLU A 1 547  ? 69.026 93.746  -37.351 1.00 35.90 ? 547  GLU A OE2 1 
ATOM   4531  N  N   . ASP A 1 548  ? 67.933 92.937  -31.571 1.00 16.27 ? 548  ASP A N   1 
ATOM   4532  C  CA  . ASP A 1 548  ? 68.834 93.612  -30.650 1.00 16.88 ? 548  ASP A CA  1 
ATOM   4533  C  C   . ASP A 1 548  ? 68.783 93.058  -29.241 1.00 17.50 ? 548  ASP A C   1 
ATOM   4534  O  O   . ASP A 1 548  ? 69.178 93.749  -28.290 1.00 19.22 ? 548  ASP A O   1 
ATOM   4535  C  CB  . ASP A 1 548  ? 68.538 95.111  -30.616 1.00 16.50 ? 548  ASP A CB  1 
ATOM   4536  C  CG  . ASP A 1 548  ? 68.648 95.750  -31.967 1.00 18.88 ? 548  ASP A CG  1 
ATOM   4537  O  OD1 . ASP A 1 548  ? 69.775 95.778  -32.506 1.00 23.41 ? 548  ASP A OD1 1 
ATOM   4538  O  OD2 . ASP A 1 548  ? 67.673 96.261  -32.567 1.00 22.31 ? 548  ASP A OD2 1 
ATOM   4539  N  N   . ILE A 1 549  ? 68.330 91.816  -29.079 1.00 16.11 ? 549  ILE A N   1 
ATOM   4540  C  CA  . ILE A 1 549  ? 68.321 91.217  -27.735 1.00 15.66 ? 549  ILE A CA  1 
ATOM   4541  C  C   . ILE A 1 549  ? 68.622 89.722  -27.705 1.00 14.75 ? 549  ILE A C   1 
ATOM   4542  O  O   . ILE A 1 549  ? 69.473 89.297  -26.940 1.00 14.72 ? 549  ILE A O   1 
ATOM   4543  C  CB  . ILE A 1 549  ? 67.019 91.555  -26.938 1.00 15.64 ? 549  ILE A CB  1 
ATOM   4544  C  CG1 . ILE A 1 549  ? 67.147 90.997  -25.497 1.00 16.19 ? 549  ILE A CG1 1 
ATOM   4545  C  CG2 . ILE A 1 549  ? 65.742 91.106  -27.692 1.00 14.44 ? 549  ILE A CG2 1 
ATOM   4546  C  CD1 . ILE A 1 549  ? 66.037 91.373  -24.524 1.00 17.90 ? 549  ILE A CD1 1 
ATOM   4547  N  N   . LEU A 1 550  ? 67.945 88.958  -28.556 1.00 13.49 ? 550  LEU A N   1 
ATOM   4548  C  CA  . LEU A 1 550  ? 68.007 87.499  -28.469 1.00 12.72 ? 550  LEU A CA  1 
ATOM   4549  C  C   . LEU A 1 550  ? 67.333 86.910  -29.688 1.00 11.75 ? 550  LEU A C   1 
ATOM   4550  O  O   . LEU A 1 550  ? 66.144 87.119  -29.883 1.00 12.43 ? 550  LEU A O   1 
ATOM   4551  C  CB  . LEU A 1 550  ? 67.273 87.019  -27.203 1.00 12.98 ? 550  LEU A CB  1 
ATOM   4552  C  CG  . LEU A 1 550  ? 67.411 85.512  -26.945 1.00 14.55 ? 550  LEU A CG  1 
ATOM   4553  C  CD1 . LEU A 1 550  ? 68.858 85.201  -26.612 1.00 14.89 ? 550  LEU A CD1 1 
ATOM   4554  C  CD2 . LEU A 1 550  ? 66.490 85.128  -25.821 1.00 14.34 ? 550  LEU A CD2 1 
ATOM   4555  N  N   . PRO A 1 551  ? 68.084 86.252  -30.569 1.00 11.13 ? 551  PRO A N   1 
ATOM   4556  C  CA  . PRO A 1 551  ? 67.475 85.703  -31.784 1.00 12.48 ? 551  PRO A CA  1 
ATOM   4557  C  C   . PRO A 1 551  ? 66.634 84.452  -31.614 1.00 11.31 ? 551  PRO A C   1 
ATOM   4558  O  O   . PRO A 1 551  ? 65.788 84.202  -32.466 1.00 12.80 ? 551  PRO A O   1 
ATOM   4559  C  CB  . PRO A 1 551  ? 68.679 85.392  -32.690 1.00 13.26 ? 551  PRO A CB  1 
ATOM   4560  C  CG  . PRO A 1 551  ? 69.815 85.264  -31.817 1.00 15.49 ? 551  PRO A CG  1 
ATOM   4561  C  CD  . PRO A 1 551  ? 69.558 86.175  -30.604 1.00 13.22 ? 551  PRO A CD  1 
ATOM   4562  N  N   . SER A 1 552  ? 66.928 83.649  -30.598 1.00 10.89 ? 552  SER A N   1 
ATOM   4563  C  CA  . SER A 1 552  ? 66.278 82.347  -30.559 1.00 10.43 ? 552  SER A CA  1 
ATOM   4564  C  C   . SER A 1 552  ? 66.171 81.858  -29.141 1.00 9.90  ? 552  SER A C   1 
ATOM   4565  O  O   . SER A 1 552  ? 66.816 82.386  -28.244 1.00 9.12  ? 552  SER A O   1 
ATOM   4566  C  CB  . SER A 1 552  ? 67.039 81.328  -31.397 1.00 12.25 ? 552  SER A CB  1 
ATOM   4567  O  OG  . SER A 1 552  ? 68.265 81.005  -30.797 1.00 15.97 ? 552  SER A OG  1 
ATOM   4568  N  N   . LYS A 1 553  ? 65.299 80.869  -28.959 1.00 8.79  ? 553  LYS A N   1 
ATOM   4569  C  CA  . LYS A 1 553  ? 65.019 80.307  -27.635 1.00 9.14  ? 553  LYS A CA  1 
ATOM   4570  C  C   . LYS A 1 553  ? 64.753 78.803  -27.730 1.00 8.37  ? 553  LYS A C   1 
ATOM   4571  O  O   . LYS A 1 553  ? 63.975 78.370  -28.569 1.00 8.31  ? 553  LYS A O   1 
ATOM   4572  C  CB  . LYS A 1 553  ? 63.772 80.986  -27.079 1.00 8.72  ? 553  LYS A CB  1 
ATOM   4573  C  CG  . LYS A 1 553  ? 63.267 80.414  -25.730 1.00 10.02 ? 553  LYS A CG  1 
ATOM   4574  C  CD  . LYS A 1 553  ? 64.297 80.578  -24.670 1.00 12.07 ? 553  LYS A CD  1 
ATOM   4575  C  CE  . LYS A 1 553  ? 64.539 82.034  -24.239 1.00 12.97 ? 553  LYS A CE  1 
ATOM   4576  N  NZ  . LYS A 1 553  ? 65.710 82.069  -23.274 1.00 12.80 ? 553  LYS A NZ  1 
ATOM   4577  N  N   . HIS A 1 554  ? 65.417 78.047  -26.862 1.00 8.49  ? 554  HIS A N   1 
ATOM   4578  C  CA  . HIS A 1 554  ? 65.113 76.620  -26.716 1.00 9.07  ? 554  HIS A CA  1 
ATOM   4579  C  C   . HIS A 1 554  ? 63.900 76.391  -25.828 1.00 8.72  ? 554  HIS A C   1 
ATOM   4580  O  O   . HIS A 1 554  ? 63.759 77.006  -24.779 1.00 9.34  ? 554  HIS A O   1 
ATOM   4581  C  CB  . HIS A 1 554  ? 66.304 75.910  -26.105 1.00 9.48  ? 554  HIS A CB  1 
ATOM   4582  C  CG  . HIS A 1 554  ? 67.459 75.714  -27.041 1.00 12.31 ? 554  HIS A CG  1 
ATOM   4583  N  ND1 . HIS A 1 554  ? 68.123 76.758  -27.655 1.00 19.56 ? 554  HIS A ND1 1 
ATOM   4584  C  CD2 . HIS A 1 554  ? 68.080 74.581  -27.453 1.00 16.15 ? 554  HIS A CD2 1 
ATOM   4585  C  CE1 . HIS A 1 554  ? 69.108 76.277  -28.396 1.00 19.74 ? 554  HIS A CE1 1 
ATOM   4586  N  NE2 . HIS A 1 554  ? 69.109 74.958  -28.286 1.00 15.70 ? 554  HIS A NE2 1 
ATOM   4587  N  N   . VAL A 1 555  ? 63.053 75.475  -26.285 1.00 7.54  ? 555  VAL A N   1 
ATOM   4588  C  CA  . VAL A 1 555  ? 61.932 74.969  -25.496 1.00 7.74  ? 555  VAL A CA  1 
ATOM   4589  C  C   . VAL A 1 555  ? 62.017 73.453  -25.486 1.00 7.70  ? 555  VAL A C   1 
ATOM   4590  O  O   . VAL A 1 555  ? 62.509 72.831  -26.431 1.00 7.89  ? 555  VAL A O   1 
ATOM   4591  C  CB  . VAL A 1 555  ? 60.588 75.457  -26.045 1.00 6.98  ? 555  VAL A CB  1 
ATOM   4592  C  CG1 . VAL A 1 555  ? 60.532 76.965  -25.968 1.00 9.15  ? 555  VAL A CG1 1 
ATOM   4593  C  CG2 . VAL A 1 555  ? 60.375 74.997  -27.473 1.00 8.23  ? 555  VAL A CG2 1 
ATOM   4594  N  N   . VAL A 1 556  ? 61.500 72.848  -24.416 1.00 6.80  ? 556  VAL A N   1 
ATOM   4595  C  CA  . VAL A 1 556  ? 61.565 71.402  -24.269 1.00 7.08  ? 556  VAL A CA  1 
ATOM   4596  C  C   . VAL A 1 556  ? 60.181 70.886  -23.863 1.00 5.96  ? 556  VAL A C   1 
ATOM   4597  O  O   . VAL A 1 556  ? 59.534 71.493  -23.006 1.00 5.75  ? 556  VAL A O   1 
ATOM   4598  C  CB  . VAL A 1 556  ? 62.561 71.017  -23.164 1.00 6.96  ? 556  VAL A CB  1 
ATOM   4599  C  CG1 . VAL A 1 556  ? 62.505 69.487  -22.887 1.00 7.75  ? 556  VAL A CG1 1 
ATOM   4600  C  CG2 . VAL A 1 556  ? 63.979 71.472  -23.519 1.00 9.07  ? 556  VAL A CG2 1 
ATOM   4601  N  N   . MET A 1 557  ? 59.771 69.792  -24.491 1.00 5.97  ? 557  MET A N   1 
ATOM   4602  C  CA  . MET A 1 557  ? 58.503 69.102  -24.130 1.00 6.55  ? 557  MET A CA  1 
ATOM   4603  C  C   . MET A 1 557  ? 58.804 67.776  -23.457 1.00 6.70  ? 557  MET A C   1 
ATOM   4604  O  O   . MET A 1 557  ? 59.677 67.044  -23.885 1.00 7.03  ? 557  MET A O   1 
ATOM   4605  C  CB  . MET A 1 557  ? 57.607 68.857  -25.355 1.00 7.28  ? 557  MET A CB  1 
ATOM   4606  C  CG  . MET A 1 557  ? 56.600 69.970  -25.656 1.00 8.40  ? 557  MET A CG  1 
ATOM   4607  S  SD  . MET A 1 557  ? 57.325 71.625  -25.859 1.00 10.70 ? 557  MET A SD  1 
ATOM   4608  C  CE  . MET A 1 557  ? 58.313 71.461  -27.311 1.00 13.40 ? 557  MET A CE  1 
ATOM   4609  N  N   . HIS A 1 558  ? 58.036 67.501  -22.403 1.00 6.17  ? 558  HIS A N   1 
ATOM   4610  C  CA  . HIS A 1 558  ? 58.092 66.207  -21.727 1.00 5.41  ? 558  HIS A CA  1 
ATOM   4611  C  C   . HIS A 1 558  ? 56.831 65.431  -21.954 1.00 5.69  ? 558  HIS A C   1 
ATOM   4612  O  O   . HIS A 1 558  ? 55.749 66.018  -21.955 1.00 6.77  ? 558  HIS A O   1 
ATOM   4613  C  CB  . HIS A 1 558  ? 58.278 66.411  -20.229 1.00 6.86  ? 558  HIS A CB  1 
ATOM   4614  C  CG  . HIS A 1 558  ? 58.215 65.143  -19.441 1.00 5.79  ? 558  HIS A CG  1 
ATOM   4615  N  ND1 . HIS A 1 558  ? 57.272 64.933  -18.459 1.00 6.29  ? 558  HIS A ND1 1 
ATOM   4616  C  CD2 . HIS A 1 558  ? 58.972 64.016  -19.489 1.00 6.14  ? 558  HIS A CD2 1 
ATOM   4617  C  CE1 . HIS A 1 558  ? 57.501 63.758  -17.893 1.00 6.24  ? 558  HIS A CE1 1 
ATOM   4618  N  NE2 . HIS A 1 558  ? 58.503 63.159  -18.509 1.00 6.96  ? 558  HIS A NE2 1 
ATOM   4619  N  N   . ASN A 1 559  ? 56.984 64.117  -22.169 1.00 5.49  ? 559  ASN A N   1 
ATOM   4620  C  CA  . ASN A 1 559  ? 55.841 63.232  -22.376 1.00 5.73  ? 559  ASN A CA  1 
ATOM   4621  C  C   . ASN A 1 559  ? 55.842 62.122  -21.331 1.00 5.99  ? 559  ASN A C   1 
ATOM   4622  O  O   . ASN A 1 559  ? 56.658 61.228  -21.410 1.00 6.70  ? 559  ASN A O   1 
ATOM   4623  C  CB  . ASN A 1 559  ? 55.949 62.592  -23.761 1.00 6.86  ? 559  ASN A CB  1 
ATOM   4624  C  CG  . ASN A 1 559  ? 54.970 61.479  -23.984 1.00 6.39  ? 559  ASN A CG  1 
ATOM   4625  O  OD1 . ASN A 1 559  ? 53.872 61.488  -23.427 1.00 6.70  ? 559  ASN A OD1 1 
ATOM   4626  N  ND2 . ASN A 1 559  ? 55.327 60.515  -24.868 1.00 7.29  ? 559  ASN A ND2 1 
ATOM   4627  N  N   . THR A 1 560  ? 54.943 62.209  -20.340 1.00 5.50  ? 560  THR A N   1 
ATOM   4628  C  CA  . THR A 1 560  ? 54.976 61.242  -19.242 1.00 5.96  ? 560  THR A CA  1 
ATOM   4629  C  C   . THR A 1 560  ? 54.407 59.868  -19.652 1.00 6.33  ? 560  THR A C   1 
ATOM   4630  O  O   . THR A 1 560  ? 54.609 58.887  -18.919 1.00 7.56  ? 560  THR A O   1 
ATOM   4631  C  CB  . THR A 1 560  ? 54.253 61.865  -18.047 1.00 6.77  ? 560  THR A CB  1 
ATOM   4632  O  OG1 . THR A 1 560  ? 54.548 61.127  -16.831 1.00 8.80  ? 560  THR A OG1 1 
ATOM   4633  C  CG2 . THR A 1 560  ? 52.746 61.890  -18.275 1.00 7.21  ? 560  THR A CG2 1 
ATOM   4634  N  N   . LEU A 1 561  ? 53.720 59.787  -20.805 1.00 5.88  ? 561  LEU A N   1 
ATOM   4635  C  CA  . LEU A 1 561  ? 53.100 58.518  -21.229 1.00 6.26  ? 561  LEU A CA  1 
ATOM   4636  C  C   . LEU A 1 561  ? 54.111 57.615  -21.907 1.00 6.90  ? 561  LEU A C   1 
ATOM   4637  O  O   . LEU A 1 561  ? 55.003 58.073  -22.592 1.00 6.68  ? 561  LEU A O   1 
ATOM   4638  C  CB  . LEU A 1 561  ? 51.937 58.776  -22.193 1.00 6.82  ? 561  LEU A CB  1 
ATOM   4639  C  CG  . LEU A 1 561  ? 50.827 59.683  -21.647 1.00 8.00  ? 561  LEU A CG  1 
ATOM   4640  C  CD1 . LEU A 1 561  ? 49.788 59.863  -22.717 1.00 10.74 ? 561  LEU A CD1 1 
ATOM   4641  C  CD2 . LEU A 1 561  ? 50.175 59.143  -20.384 1.00 9.70  ? 561  LEU A CD2 1 
ATOM   4642  N  N   . PRO A 1 562  ? 53.978 56.315  -21.738 1.00 6.76  ? 562  PRO A N   1 
ATOM   4643  C  CA  . PRO A 1 562  ? 54.954 55.376  -22.300 1.00 6.93  ? 562  PRO A CA  1 
ATOM   4644  C  C   . PRO A 1 562  ? 54.742 55.009  -23.759 1.00 7.38  ? 562  PRO A C   1 
ATOM   4645  O  O   . PRO A 1 562  ? 54.914 53.878  -24.157 1.00 7.40  ? 562  PRO A O   1 
ATOM   4646  C  CB  . PRO A 1 562  ? 54.801 54.134  -21.378 1.00 7.97  ? 562  PRO A CB  1 
ATOM   4647  C  CG  . PRO A 1 562  ? 53.307 54.138  -21.041 1.00 8.08  ? 562  PRO A CG  1 
ATOM   4648  C  CD  . PRO A 1 562  ? 52.996 55.625  -20.877 1.00 7.43  ? 562  PRO A CD  1 
ATOM   4649  N  N   . HIS A 1 563  ? 54.393 55.984  -24.578 1.00 6.57  ? 563  HIS A N   1 
ATOM   4650  C  CA  . HIS A 1 563  ? 54.358 55.766  -26.016 1.00 7.47  ? 563  HIS A CA  1 
ATOM   4651  C  C   . HIS A 1 563  ? 54.758 57.072  -26.687 1.00 7.35  ? 563  HIS A C   1 
ATOM   4652  O  O   . HIS A 1 563  ? 54.633 58.138  -26.091 1.00 7.31  ? 563  HIS A O   1 
ATOM   4653  C  CB  . HIS A 1 563  ? 52.987 55.291  -26.499 1.00 9.57  ? 563  HIS A CB  1 
ATOM   4654  C  CG  . HIS A 1 563  ? 51.843 56.141  -26.043 1.00 11.25 ? 563  HIS A CG  1 
ATOM   4655  N  ND1 . HIS A 1 563  ? 51.071 55.809  -24.951 1.00 10.36 ? 563  HIS A ND1 1 
ATOM   4656  C  CD2 . HIS A 1 563  ? 51.323 57.295  -26.532 1.00 12.51 ? 563  HIS A CD2 1 
ATOM   4657  C  CE1 . HIS A 1 563  ? 50.113 56.705  -24.793 1.00 11.36 ? 563  HIS A CE1 1 
ATOM   4658  N  NE2 . HIS A 1 563  ? 50.252 57.633  -25.728 1.00 12.90 ? 563  HIS A NE2 1 
ATOM   4659  N  N   . TRP A 1 564  ? 55.271 56.978  -27.914 1.00 8.15  ? 564  TRP A N   1 
ATOM   4660  C  CA  . TRP A 1 564  ? 55.546 58.180  -28.706 1.00 8.47  ? 564  TRP A CA  1 
ATOM   4661  C  C   . TRP A 1 564  ? 54.285 59.003  -28.836 1.00 8.95  ? 564  TRP A C   1 
ATOM   4662  O  O   . TRP A 1 564  ? 53.175 58.480  -29.016 1.00 9.41  ? 564  TRP A O   1 
ATOM   4663  C  CB  . TRP A 1 564  ? 56.026 57.808  -30.114 1.00 10.04 ? 564  TRP A CB  1 
ATOM   4664  C  CG  . TRP A 1 564  ? 57.460 57.404  -30.146 1.00 9.28  ? 564  TRP A CG  1 
ATOM   4665  C  CD1 . TRP A 1 564  ? 57.952 56.132  -29.987 1.00 11.04 ? 564  TRP A CD1 1 
ATOM   4666  C  CD2 . TRP A 1 564  ? 58.602 58.252  -30.310 1.00 10.05 ? 564  TRP A CD2 1 
ATOM   4667  N  NE1 . TRP A 1 564  ? 59.325 56.141  -30.043 1.00 11.88 ? 564  TRP A NE1 1 
ATOM   4668  C  CE2 . TRP A 1 564  ? 59.763 57.423  -30.244 1.00 9.71  ? 564  TRP A CE2 1 
ATOM   4669  C  CE3 . TRP A 1 564  ? 58.777 59.636  -30.503 1.00 10.27 ? 564  TRP A CE3 1 
ATOM   4670  C  CZ2 . TRP A 1 564  ? 61.067 57.933  -30.356 1.00 11.67 ? 564  TRP A CZ2 1 
ATOM   4671  C  CZ3 . TRP A 1 564  ? 60.066 60.142  -30.628 1.00 11.26 ? 564  TRP A CZ3 1 
ATOM   4672  C  CH2 . TRP A 1 564  ? 61.198 59.298  -30.538 1.00 12.32 ? 564  TRP A CH2 1 
ATOM   4673  N  N   . ARG A 1 565  ? 54.434 60.311  -28.645 1.00 9.00  ? 565  ARG A N   1 
ATOM   4674  C  CA  . ARG A 1 565  ? 53.256 61.140  -28.722 1.00 10.28 ? 565  ARG A CA  1 
ATOM   4675  C  C   . ARG A 1 565  ? 53.551 62.385  -29.511 1.00 9.42  ? 565  ARG A C   1 
ATOM   4676  O  O   . ARG A 1 565  ? 54.592 63.008  -29.326 1.00 10.32 ? 565  ARG A O   1 
ATOM   4677  C  CB  . ARG A 1 565  ? 52.752 61.503  -27.318 1.00 10.52 ? 565  ARG A CB  1 
ATOM   4678  C  CG  . ARG A 1 565  ? 51.369 62.175  -27.311 1.00 14.48 ? 565  ARG A CG  1 
ATOM   4679  C  CD  . ARG A 1 565  ? 50.549 61.910  -26.035 1.00 14.64 ? 565  ARG A CD  1 
ATOM   4680  N  NE  . ARG A 1 565  ? 51.314 62.294  -24.857 1.00 15.25 ? 565  ARG A NE  1 
ATOM   4681  C  CZ  . ARG A 1 565  ? 50.787 62.908  -23.792 1.00 10.29 ? 565  ARG A CZ  1 
ATOM   4682  N  NH1 . ARG A 1 565  ? 49.475 63.260  -23.779 1.00 11.26 ? 565  ARG A NH1 1 
ATOM   4683  N  NH2 . ARG A 1 565  ? 51.587 63.166  -22.765 1.00 10.12 ? 565  ARG A NH2 1 
ATOM   4684  N  N   . GLU A 1 566  ? 52.620 62.726  -30.397 1.00 11.14 ? 566  GLU A N   1 
ATOM   4685  C  CA  . GLU A 1 566  ? 52.567 64.070  -30.978 1.00 11.88 ? 566  GLU A CA  1 
ATOM   4686  C  C   . GLU A 1 566  ? 51.411 64.859  -30.375 1.00 12.61 ? 566  GLU A C   1 
ATOM   4687  O  O   . GLU A 1 566  ? 50.324 64.324  -30.152 1.00 12.98 ? 566  GLU A O   1 
ATOM   4688  C  CB  . GLU A 1 566  ? 52.341 64.001  -32.479 1.00 14.09 ? 566  GLU A CB  1 
ATOM   4689  C  CG  . GLU A 1 566  ? 53.418 63.260  -33.220 1.00 14.85 ? 566  GLU A CG  1 
ATOM   4690  C  CD  . GLU A 1 566  ? 53.195 63.245  -34.727 1.00 21.95 ? 566  GLU A CD  1 
ATOM   4691  O  OE1 . GLU A 1 566  ? 52.055 62.985  -35.184 1.00 25.77 ? 566  GLU A OE1 1 
ATOM   4692  O  OE2 . GLU A 1 566  ? 54.173 63.504  -35.453 1.00 25.83 ? 566  GLU A OE2 1 
ATOM   4693  N  N   . GLN A 1 567  ? 51.633 66.146  -30.150 1.00 10.60 ? 567  GLN A N   1 
ATOM   4694  C  CA  . GLN A 1 567  ? 50.576 67.015  -29.645 1.00 10.64 ? 567  GLN A CA  1 
ATOM   4695  C  C   . GLN A 1 567  ? 50.940 68.416  -30.106 1.00 9.61  ? 567  GLN A C   1 
ATOM   4696  O  O   . GLN A 1 567  ? 52.128 68.780  -30.106 1.00 8.19  ? 567  GLN A O   1 
ATOM   4697  C  CB  . GLN A 1 567  ? 50.558 66.998  -28.119 1.00 10.95 ? 567  GLN A CB  1 
ATOM   4698  C  CG  . GLN A 1 567  ? 49.420 67.787  -27.492 1.00 13.26 ? 567  GLN A CG  1 
ATOM   4699  C  CD  . GLN A 1 567  ? 49.765 68.262  -26.093 1.00 15.34 ? 567  GLN A CD  1 
ATOM   4700  O  OE1 . GLN A 1 567  ? 49.763 67.472  -25.144 1.00 12.90 ? 567  GLN A OE1 1 
ATOM   4701  N  NE2 . GLN A 1 567  ? 50.094 69.540  -25.954 1.00 15.91 ? 567  GLN A NE2 1 
ATOM   4702  N  N   . LEU A 1 568  ? 49.942 69.198  -30.509 1.00 9.45  ? 568  LEU A N   1 
ATOM   4703  C  CA  . LEU A 1 568  ? 50.232 70.620  -30.763 1.00 9.40  ? 568  LEU A CA  1 
ATOM   4704  C  C   . LEU A 1 568  ? 50.550 71.287  -29.446 1.00 9.17  ? 568  LEU A C   1 
ATOM   4705  O  O   . LEU A 1 568  ? 49.885 71.042  -28.413 1.00 10.28 ? 568  LEU A O   1 
ATOM   4706  C  CB  . LEU A 1 568  ? 49.065 71.369  -31.406 1.00 11.34 ? 568  LEU A CB  1 
ATOM   4707  C  CG  . LEU A 1 568  ? 48.658 70.946  -32.810 1.00 13.41 ? 568  LEU A CG  1 
ATOM   4708  C  CD1 . LEU A 1 568  ? 47.677 71.958  -33.339 1.00 14.58 ? 568  LEU A CD1 1 
ATOM   4709  C  CD2 . LEU A 1 568  ? 49.849 70.968  -33.720 1.00 14.81 ? 568  LEU A CD2 1 
ATOM   4710  N  N   . VAL A 1 569  ? 51.569 72.115  -29.459 1.00 7.15  ? 569  VAL A N   1 
ATOM   4711  C  CA  . VAL A 1 569  ? 51.927 72.945  -28.323 1.00 7.58  ? 569  VAL A CA  1 
ATOM   4712  C  C   . VAL A 1 569  ? 51.985 74.399  -28.736 1.00 8.86  ? 569  VAL A C   1 
ATOM   4713  O  O   . VAL A 1 569  ? 52.236 74.698  -29.900 1.00 8.81  ? 569  VAL A O   1 
ATOM   4714  C  CB  . VAL A 1 569  ? 53.293 72.538  -27.737 1.00 8.25  ? 569  VAL A CB  1 
ATOM   4715  C  CG1 . VAL A 1 569  ? 53.225 71.124  -27.085 1.00 8.94  ? 569  VAL A CG1 1 
ATOM   4716  C  CG2 . VAL A 1 569  ? 54.403 72.626  -28.804 1.00 8.95  ? 569  VAL A CG2 1 
ATOM   4717  N  N   . ASP A 1 570  ? 51.726 75.292  -27.790 1.00 8.63  ? 570  ASP A N   1 
ATOM   4718  C  CA  . ASP A 1 570  ? 51.775 76.714  -28.112 1.00 10.03 ? 570  ASP A CA  1 
ATOM   4719  C  C   . ASP A 1 570  ? 52.577 77.479  -27.090 1.00 10.32 ? 570  ASP A C   1 
ATOM   4720  O  O   . ASP A 1 570  ? 52.687 77.103  -25.911 1.00 11.26 ? 570  ASP A O   1 
ATOM   4721  C  CB  . ASP A 1 570  ? 50.371 77.294  -28.255 1.00 11.16 ? 570  ASP A CB  1 
ATOM   4722  C  CG  . ASP A 1 570  ? 49.675 77.481  -26.928 1.00 17.08 ? 570  ASP A CG  1 
ATOM   4723  O  OD1 . ASP A 1 570  ? 49.550 76.488  -26.190 1.00 22.13 ? 570  ASP A OD1 1 
ATOM   4724  O  OD2 . ASP A 1 570  ? 49.209 78.578  -26.545 1.00 22.78 ? 570  ASP A OD2 1 
ATOM   4725  N  N   . PHE A 1 571  ? 53.176 78.562  -27.570 1.00 7.83  ? 571  PHE A N   1 
ATOM   4726  C  CA  . PHE A 1 571  ? 53.949 79.457  -26.723 1.00 8.30  ? 571  PHE A CA  1 
ATOM   4727  C  C   . PHE A 1 571  ? 53.565 80.894  -27.104 1.00 8.79  ? 571  PHE A C   1 
ATOM   4728  O  O   . PHE A 1 571  ? 53.194 81.162  -28.247 1.00 9.75  ? 571  PHE A O   1 
ATOM   4729  C  CB  . PHE A 1 571  ? 55.451 79.269  -26.973 1.00 9.17  ? 571  PHE A CB  1 
ATOM   4730  C  CG  . PHE A 1 571  ? 55.973 77.934  -26.529 1.00 7.50  ? 571  PHE A CG  1 
ATOM   4731  C  CD1 . PHE A 1 571  ? 55.963 76.833  -27.396 1.00 8.52  ? 571  PHE A CD1 1 
ATOM   4732  C  CD2 . PHE A 1 571  ? 56.436 77.754  -25.239 1.00 8.50  ? 571  PHE A CD2 1 
ATOM   4733  C  CE1 . PHE A 1 571  ? 56.397 75.577  -26.955 1.00 8.57  ? 571  PHE A CE1 1 
ATOM   4734  C  CE2 . PHE A 1 571  ? 56.865 76.504  -24.807 1.00 8.35  ? 571  PHE A CE2 1 
ATOM   4735  C  CZ  . PHE A 1 571  ? 56.847 75.431  -25.678 1.00 9.78  ? 571  PHE A CZ  1 
ATOM   4736  N  N   . TYR A 1 572  ? 53.682 81.807  -26.163 1.00 8.31  ? 572  TYR A N   1 
ATOM   4737  C  CA  . TYR A 1 572  ? 53.581 83.237  -26.486 1.00 9.56  ? 572  TYR A CA  1 
ATOM   4738  C  C   . TYR A 1 572  ? 54.959 83.750  -26.860 1.00 9.19  ? 572  TYR A C   1 
ATOM   4739  O  O   . TYR A 1 572  ? 55.953 83.430  -26.195 1.00 9.17  ? 572  TYR A O   1 
ATOM   4740  C  CB  . TYR A 1 572  ? 53.104 84.029  -25.268 1.00 10.90 ? 572  TYR A CB  1 
ATOM   4741  C  CG  . TYR A 1 572  ? 51.619 83.920  -24.941 1.00 13.26 ? 572  TYR A CG  1 
ATOM   4742  C  CD1 . TYR A 1 572  ? 50.778 83.049  -25.632 1.00 14.02 ? 572  TYR A CD1 1 
ATOM   4743  C  CD2 . TYR A 1 572  ? 51.073 84.678  -23.911 1.00 18.48 ? 572  TYR A CD2 1 
ATOM   4744  C  CE1 . TYR A 1 572  ? 49.405 82.960  -25.316 1.00 16.35 ? 572  TYR A CE1 1 
ATOM   4745  C  CE2 . TYR A 1 572  ? 49.719 84.590  -23.587 1.00 18.75 ? 572  TYR A CE2 1 
ATOM   4746  C  CZ  . TYR A 1 572  ? 48.906 83.741  -24.293 1.00 17.70 ? 572  TYR A CZ  1 
ATOM   4747  O  OH  . TYR A 1 572  ? 47.560 83.658  -23.974 1.00 20.50 ? 572  TYR A OH  1 
ATOM   4748  N  N   . VAL A 1 573  ? 55.003 84.545  -27.934 1.00 8.96  ? 573  VAL A N   1 
ATOM   4749  C  CA  . VAL A 1 573  ? 56.263 85.098  -28.443 1.00 10.04 ? 573  VAL A CA  1 
ATOM   4750  C  C   . VAL A 1 573  ? 56.054 86.583  -28.740 1.00 9.35  ? 573  VAL A C   1 
ATOM   4751  O  O   . VAL A 1 573  ? 54.931 87.025  -28.992 1.00 9.74  ? 573  VAL A O   1 
ATOM   4752  C  CB  . VAL A 1 573  ? 56.715 84.357  -29.730 1.00 10.28 ? 573  VAL A CB  1 
ATOM   4753  C  CG1 . VAL A 1 573  ? 57.308 82.988  -29.405 1.00 11.81 ? 573  VAL A CG1 1 
ATOM   4754  C  CG2 . VAL A 1 573  ? 55.571 84.220  -30.719 1.00 10.56 ? 573  VAL A CG2 1 
ATOM   4755  N  N   . SER A 1 574  ? 57.142 87.331  -28.720 1.00 9.34  ? 574  SER A N   1 
ATOM   4756  C  CA  . SER A 1 574  ? 57.024 88.786  -28.886 1.00 10.64 ? 574  SER A CA  1 
ATOM   4757  C  C   . SER A 1 574  ? 57.058 89.282  -30.336 1.00 11.99 ? 574  SER A C   1 
ATOM   4758  O  O   . SER A 1 574  ? 57.054 90.505  -30.570 1.00 14.89 ? 574  SER A O   1 
ATOM   4759  C  CB  . SER A 1 574  ? 58.120 89.477  -28.090 1.00 10.55 ? 574  SER A CB  1 
ATOM   4760  O  OG  . SER A 1 574  ? 59.370 89.086  -28.600 1.00 12.24 ? 574  SER A OG  1 
ATOM   4761  N  N   . SER A 1 575  ? 57.066 88.370  -31.310 1.00 12.05 ? 575  SER A N   1 
ATOM   4762  C  CA  . SER A 1 575  ? 57.004 88.707  -32.738 1.00 13.29 ? 575  SER A CA  1 
ATOM   4763  C  C   . SER A 1 575  ? 56.166 87.672  -33.443 1.00 13.23 ? 575  SER A C   1 
ATOM   4764  O  O   . SER A 1 575  ? 56.151 86.511  -33.048 1.00 12.84 ? 575  SER A O   1 
ATOM   4765  C  CB  . SER A 1 575  ? 58.401 88.676  -33.354 1.00 14.45 ? 575  SER A CB  1 
ATOM   4766  O  OG  . SER A 1 575  ? 58.393 88.769  -34.780 1.00 14.91 ? 575  SER A OG  1 
ATOM   4767  N  N   . PRO A 1 576  ? 55.472 88.049  -34.503 1.00 12.69 ? 576  PRO A N   1 
ATOM   4768  C  CA  . PRO A 1 576  ? 54.793 87.038  -35.306 1.00 12.27 ? 576  PRO A CA  1 
ATOM   4769  C  C   . PRO A 1 576  ? 55.724 86.315  -36.285 1.00 12.12 ? 576  PRO A C   1 
ATOM   4770  O  O   . PRO A 1 576  ? 55.320 85.352  -36.920 1.00 12.82 ? 576  PRO A O   1 
ATOM   4771  C  CB  . PRO A 1 576  ? 53.731 87.835  -36.064 1.00 13.50 ? 576  PRO A CB  1 
ATOM   4772  C  CG  . PRO A 1 576  ? 54.266 89.229  -36.129 1.00 15.25 ? 576  PRO A CG  1 
ATOM   4773  C  CD  . PRO A 1 576  ? 55.240 89.418  -35.013 1.00 13.02 ? 576  PRO A CD  1 
ATOM   4774  N  N   . PHE A 1 577  ? 56.952 86.802  -36.435 1.00 11.82 ? 577  PHE A N   1 
ATOM   4775  C  CA  . PHE A 1 577  ? 57.837 86.264  -37.462 1.00 11.81 ? 577  PHE A CA  1 
ATOM   4776  C  C   . PHE A 1 577  ? 58.791 85.323  -36.796 1.00 12.15 ? 577  PHE A C   1 
ATOM   4777  O  O   . PHE A 1 577  ? 59.948 85.638  -36.544 1.00 11.61 ? 577  PHE A O   1 
ATOM   4778  C  CB  . PHE A 1 577  ? 58.575 87.403  -38.168 1.00 12.90 ? 577  PHE A CB  1 
ATOM   4779  C  CG  . PHE A 1 577  ? 57.647 88.425  -38.780 1.00 16.35 ? 577  PHE A CG  1 
ATOM   4780  C  CD1 . PHE A 1 577  ? 56.580 88.035  -39.570 1.00 17.95 ? 577  PHE A CD1 1 
ATOM   4781  C  CD2 . PHE A 1 577  ? 57.857 89.787  -38.552 1.00 18.84 ? 577  PHE A CD2 1 
ATOM   4782  C  CE1 . PHE A 1 577  ? 55.728 88.990  -40.153 1.00 19.53 ? 577  PHE A CE1 1 
ATOM   4783  C  CE2 . PHE A 1 577  ? 57.010 90.740  -39.120 1.00 21.83 ? 577  PHE A CE2 1 
ATOM   4784  C  CZ  . PHE A 1 577  ? 55.952 90.330  -39.920 1.00 20.20 ? 577  PHE A CZ  1 
ATOM   4785  N  N   . VAL A 1 578  ? 58.249 84.154  -36.453 1.00 11.40 ? 578  VAL A N   1 
ATOM   4786  C  CA  . VAL A 1 578  ? 59.011 83.170  -35.700 1.00 11.30 ? 578  VAL A CA  1 
ATOM   4787  C  C   . VAL A 1 578  ? 58.919 81.835  -36.416 1.00 11.10 ? 578  VAL A C   1 
ATOM   4788  O  O   . VAL A 1 578  ? 57.864 81.476  -36.891 1.00 11.43 ? 578  VAL A O   1 
ATOM   4789  C  CB  . VAL A 1 578  ? 58.489 83.064  -34.239 1.00 11.65 ? 578  VAL A CB  1 
ATOM   4790  C  CG1 . VAL A 1 578  ? 59.178 81.901  -33.462 1.00 11.61 ? 578  VAL A CG1 1 
ATOM   4791  C  CG2 . VAL A 1 578  ? 58.704 84.374  -33.519 1.00 12.44 ? 578  VAL A CG2 1 
ATOM   4792  N  N   . SER A 1 579  ? 60.044 81.139  -36.512 1.00 11.87 ? 579  SER A N   1 
ATOM   4793  C  CA  . SER A 1 579  ? 60.023 79.822  -37.110 1.00 12.56 ? 579  SER A CA  1 
ATOM   4794  C  C   . SER A 1 579  ? 60.541 78.817  -36.090 1.00 10.33 ? 579  SER A C   1 
ATOM   4795  O  O   . SER A 1 579  ? 61.286 79.165  -35.178 1.00 10.25 ? 579  SER A O   1 
ATOM   4796  C  CB  . SER A 1 579  ? 60.849 79.788  -38.384 1.00 15.62 ? 579  SER A CB  1 
ATOM   4797  O  OG  . SER A 1 579  ? 62.127 80.260  -38.108 1.00 21.03 ? 579  SER A OG  1 
ATOM   4798  N  N   . VAL A 1 580  ? 60.166 77.570  -36.308 1.00 8.86  ? 580  VAL A N   1 
ATOM   4799  C  CA  . VAL A 1 580  ? 60.482 76.470  -35.389 1.00 9.40  ? 580  VAL A CA  1 
ATOM   4800  C  C   . VAL A 1 580  ? 61.360 75.452  -36.089 1.00 10.08 ? 580  VAL A C   1 
ATOM   4801  O  O   . VAL A 1 580  ? 61.123 75.116  -37.246 1.00 10.78 ? 580  VAL A O   1 
ATOM   4802  C  CB  . VAL A 1 580  ? 59.189 75.787  -34.916 1.00 9.26  ? 580  VAL A CB  1 
ATOM   4803  C  CG1 . VAL A 1 580  ? 59.495 74.695  -33.876 1.00 10.59 ? 580  VAL A CG1 1 
ATOM   4804  C  CG2 . VAL A 1 580  ? 58.217 76.828  -34.309 1.00 10.94 ? 580  VAL A CG2 1 
ATOM   4805  N  N   . THR A 1 581  ? 62.345 74.964  -35.357 1.00 10.55 ? 581  THR A N   1 
ATOM   4806  C  CA  . THR A 1 581  ? 63.204 73.883  -35.833 1.00 10.60 ? 581  THR A CA  1 
ATOM   4807  C  C   . THR A 1 581  ? 63.342 72.869  -34.707 1.00 11.32 ? 581  THR A C   1 
ATOM   4808  O  O   . THR A 1 581  ? 63.233 73.204  -33.516 1.00 10.39 ? 581  THR A O   1 
ATOM   4809  C  CB  . THR A 1 581  ? 64.624 74.357  -36.228 1.00 10.83 ? 581  THR A CB  1 
ATOM   4810  O  OG1 . THR A 1 581  ? 65.126 75.294  -35.268 1.00 13.13 ? 581  THR A OG1 1 
ATOM   4811  C  CG2 . THR A 1 581  ? 64.593 75.170  -37.536 1.00 12.42 ? 581  THR A CG2 1 
ATOM   4812  N  N   . ASP A 1 582  ? 63.603 71.630  -35.082 1.00 12.09 ? 582  ASP A N   1 
ATOM   4813  C  CA  . ASP A 1 582  ? 63.970 70.585  -34.134 1.00 14.31 ? 582  ASP A CA  1 
ATOM   4814  C  C   . ASP A 1 582  ? 65.461 70.614  -33.841 1.00 15.84 ? 582  ASP A C   1 
ATOM   4815  O  O   . ASP A 1 582  ? 66.150 71.473  -34.315 1.00 14.56 ? 582  ASP A O   1 
ATOM   4816  C  CB  . ASP A 1 582  ? 63.454 69.225  -34.604 1.00 15.98 ? 582  ASP A CB  1 
ATOM   4817  C  CG  . ASP A 1 582  ? 64.192 68.679  -35.819 1.00 17.42 ? 582  ASP A CG  1 
ATOM   4818  O  OD1 . ASP A 1 582  ? 65.282 69.160  -36.132 1.00 16.74 ? 582  ASP A OD1 1 
ATOM   4819  O  OD2 . ASP A 1 582  ? 63.663 67.719  -36.396 1.00 21.89 ? 582  ASP A OD2 1 
ATOM   4820  N  N   . LEU A 1 583  ? 65.980 69.711  -33.025 1.00 18.55 ? 583  LEU A N   1 
ATOM   4821  C  CA  . LEU A 1 583  ? 67.405 69.866  -32.790 1.00 20.46 ? 583  LEU A CA  1 
ATOM   4822  C  C   . LEU A 1 583  ? 68.311 69.133  -33.771 1.00 19.87 ? 583  LEU A C   1 
ATOM   4823  O  O   . LEU A 1 583  ? 69.450 68.938  -33.475 1.00 21.65 ? 583  LEU A O   1 
ATOM   4824  C  CB  . LEU A 1 583  ? 67.857 69.711  -31.315 1.00 20.93 ? 583  LEU A CB  1 
ATOM   4825  C  CG  . LEU A 1 583  ? 68.734 70.817  -30.683 1.00 21.50 ? 583  LEU A CG  1 
ATOM   4826  C  CD1 . LEU A 1 583  ? 67.971 72.130  -30.637 1.00 24.73 ? 583  LEU A CD1 1 
ATOM   4827  C  CD2 . LEU A 1 583  ? 69.227 70.475  -29.264 1.00 21.46 ? 583  LEU A CD2 1 
ATOM   4828  N  N   . ALA A 1 584  ? 67.802 68.813  -34.957 1.00 18.17 ? 584  ALA A N   1 
ATOM   4829  C  CA  . ALA A 1 584  ? 68.667 68.610  -36.127 1.00 15.77 ? 584  ALA A CA  1 
ATOM   4830  C  C   . ALA A 1 584  ? 68.516 69.748  -37.121 1.00 14.51 ? 584  ALA A C   1 
ATOM   4831  O  O   . ALA A 1 584  ? 68.934 69.655  -38.247 1.00 13.87 ? 584  ALA A O   1 
ATOM   4832  C  CB  . ALA A 1 584  ? 68.348 67.307  -36.790 1.00 16.77 ? 584  ALA A CB  1 
ATOM   4833  N  N   A ASN A 1 585  ? 67.889 70.807  -36.641 0.50 13.47 ? 585  ASN A N   1 
ATOM   4834  N  N   B ASN A 1 585  ? 67.938 70.861  -36.691 0.50 14.07 ? 585  ASN A N   1 
ATOM   4835  C  CA  A ASN A 1 585  ? 67.674 72.008  -37.413 0.50 13.58 ? 585  ASN A CA  1 
ATOM   4836  C  CA  B ASN A 1 585  ? 67.764 72.025  -37.576 0.50 14.69 ? 585  ASN A CA  1 
ATOM   4837  C  C   A ASN A 1 585  ? 66.804 71.755  -38.638 0.50 13.62 ? 585  ASN A C   1 
ATOM   4838  C  C   B ASN A 1 585  ? 66.689 71.832  -38.645 0.50 14.42 ? 585  ASN A C   1 
ATOM   4839  O  O   A ASN A 1 585  ? 66.947 72.443  -39.646 0.50 14.77 ? 585  ASN A O   1 
ATOM   4840  O  O   B ASN A 1 585  ? 66.551 72.650  -39.563 0.50 15.39 ? 585  ASN A O   1 
ATOM   4841  C  CB  A ASN A 1 585  ? 69.014 72.657  -37.787 0.50 13.73 ? 585  ASN A CB  1 
ATOM   4842  C  CB  B ASN A 1 585  ? 69.085 72.416  -38.264 0.50 15.53 ? 585  ASN A CB  1 
ATOM   4843  C  CG  A ASN A 1 585  ? 68.852 74.060  -38.305 0.50 13.81 ? 585  ASN A CG  1 
ATOM   4844  C  CG  B ASN A 1 585  ? 69.718 73.665  -37.681 0.50 17.28 ? 585  ASN A CG  1 
ATOM   4845  O  OD1 A ASN A 1 585  ? 68.055 74.849  -37.771 0.50 14.13 ? 585  ASN A OD1 1 
ATOM   4846  O  OD1 B ASN A 1 585  ? 69.074 74.718  -37.556 0.50 20.48 ? 585  ASN A OD1 1 
ATOM   4847  N  ND2 A ASN A 1 585  ? 69.609 74.396  -39.348 0.50 14.14 ? 585  ASN A ND2 1 
ATOM   4848  N  ND2 B ASN A 1 585  ? 71.000 73.567  -37.349 0.50 20.53 ? 585  ASN A ND2 1 
ATOM   4849  N  N   . ASN A 1 586  ? 65.918 70.761  -38.527 1.00 13.49 ? 586  ASN A N   1 
ATOM   4850  C  CA  . ASN A 1 586  ? 64.853 70.488  -39.491 1.00 13.77 ? 586  ASN A CA  1 
ATOM   4851  C  C   . ASN A 1 586  ? 63.727 71.497  -39.233 1.00 14.51 ? 586  ASN A C   1 
ATOM   4852  O  O   . ASN A 1 586  ? 63.299 71.665  -38.081 1.00 12.99 ? 586  ASN A O   1 
ATOM   4853  C  CB  . ASN A 1 586  ? 64.271 69.091  -39.278 1.00 15.02 ? 586  ASN A CB  1 
ATOM   4854  C  CG  . ASN A 1 586  ? 65.289 67.980  -39.473 1.00 15.90 ? 586  ASN A CG  1 
ATOM   4855  O  OD1 . ASN A 1 586  ? 66.135 68.041  -40.380 1.00 17.02 ? 586  ASN A OD1 1 
ATOM   4856  N  ND2 . ASN A 1 586  ? 65.196 66.947  -38.639 1.00 17.43 ? 586  ASN A ND2 1 
ATOM   4857  N  N   . PRO A 1 587  ? 63.251 72.206  -40.249 1.00 13.44 ? 587  PRO A N   1 
ATOM   4858  C  CA  . PRO A 1 587  ? 62.069 73.056  -40.072 1.00 13.69 ? 587  PRO A CA  1 
ATOM   4859  C  C   . PRO A 1 587  ? 60.863 72.264  -39.590 1.00 12.72 ? 587  PRO A C   1 
ATOM   4860  O  O   . PRO A 1 587  ? 60.630 71.109  -39.957 1.00 13.48 ? 587  PRO A O   1 
ATOM   4861  C  CB  . PRO A 1 587  ? 61.786 73.616  -41.472 1.00 14.12 ? 587  PRO A CB  1 
ATOM   4862  C  CG  . PRO A 1 587  ? 62.874 73.134  -42.375 1.00 15.54 ? 587  PRO A CG  1 
ATOM   4863  C  CD  . PRO A 1 587  ? 63.849 72.313  -41.602 1.00 14.69 ? 587  PRO A CD  1 
ATOM   4864  N  N   . VAL A 1 588  ? 60.076 72.912  -38.729 1.00 11.82 ? 588  VAL A N   1 
ATOM   4865  C  CA  . VAL A 1 588  ? 58.844 72.330  -38.244 1.00 11.19 ? 588  VAL A CA  1 
ATOM   4866  C  C   . VAL A 1 588  ? 57.718 73.301  -38.632 1.00 10.01 ? 588  VAL A C   1 
ATOM   4867  O  O   . VAL A 1 588  ? 57.822 74.522  -38.372 1.00 11.30 ? 588  VAL A O   1 
ATOM   4868  C  CB  . VAL A 1 588  ? 58.881 72.156  -36.708 1.00 12.42 ? 588  VAL A CB  1 
ATOM   4869  C  CG1 . VAL A 1 588  ? 57.548 71.704  -36.177 1.00 12.48 ? 588  VAL A CG1 1 
ATOM   4870  C  CG2 . VAL A 1 588  ? 59.996 71.174  -36.303 1.00 12.77 ? 588  VAL A CG2 1 
ATOM   4871  N  N   . GLU A 1 589  ? 56.659 72.775  -39.234 1.00 9.95  ? 589  GLU A N   1 
ATOM   4872  C  CA  . GLU A 1 589  ? 55.527 73.596  -39.656 1.00 11.34 ? 589  GLU A CA  1 
ATOM   4873  C  C   . GLU A 1 589  ? 54.888 74.257  -38.429 1.00 11.05 ? 589  GLU A C   1 
ATOM   4874  O  O   . GLU A 1 589  ? 54.705 73.613  -37.383 1.00 11.08 ? 589  GLU A O   1 
ATOM   4875  C  CB  . GLU A 1 589  ? 54.491 72.747  -40.381 1.00 12.93 ? 589  GLU A CB  1 
ATOM   4876  C  CG  . GLU A 1 589  ? 53.308 73.572  -40.831 1.00 18.08 ? 589  GLU A CG  1 
ATOM   4877  C  CD  . GLU A 1 589  ? 52.335 72.847  -41.723 1.00 25.17 ? 589  GLU A CD  1 
ATOM   4878  O  OE1 . GLU A 1 589  ? 52.600 71.674  -42.084 1.00 28.63 ? 589  GLU A OE1 1 
ATOM   4879  O  OE2 . GLU A 1 589  ? 51.302 73.473  -42.076 1.00 28.58 ? 589  GLU A OE2 1 
ATOM   4880  N  N   . ALA A 1 590  ? 54.559 75.530  -38.523 1.00 9.89  ? 590  ALA A N   1 
ATOM   4881  C  CA  . ALA A 1 590  ? 54.051 76.263  -37.362 1.00 9.54  ? 590  ALA A CA  1 
ATOM   4882  C  C   . ALA A 1 590  ? 52.953 77.183  -37.797 1.00 9.81  ? 590  ALA A C   1 
ATOM   4883  O  O   . ALA A 1 590  ? 52.843 77.521  -38.995 1.00 9.99  ? 590  ALA A O   1 
ATOM   4884  C  CB  . ALA A 1 590  ? 55.118 77.029  -36.681 1.00 10.56 ? 590  ALA A CB  1 
ATOM   4885  N  N   . GLN A 1 591  ? 52.124 77.580  -36.849 1.00 8.34  ? 591  GLN A N   1 
ATOM   4886  C  CA  . GLN A 1 591  ? 51.056 78.518  -37.137 1.00 7.95  ? 591  GLN A CA  1 
ATOM   4887  C  C   . GLN A 1 591  ? 51.106 79.598  -36.095 1.00 8.22  ? 591  GLN A C   1 
ATOM   4888  O  O   . GLN A 1 591  ? 51.270 79.320  -34.906 1.00 10.02 ? 591  GLN A O   1 
ATOM   4889  C  CB  . GLN A 1 591  ? 49.696 77.825  -37.102 1.00 8.33  ? 591  GLN A CB  1 
ATOM   4890  C  CG  . GLN A 1 591  ? 48.496 78.815  -37.049 1.00 8.31  ? 591  GLN A CG  1 
ATOM   4891  C  CD  . GLN A 1 591  ? 47.167 78.091  -36.845 1.00 8.65  ? 591  GLN A CD  1 
ATOM   4892  O  OE1 . GLN A 1 591  ? 46.936 77.036  -37.475 1.00 9.76  ? 591  GLN A OE1 1 
ATOM   4893  N  NE2 . GLN A 1 591  ? 46.294 78.637  -36.023 1.00 10.20 ? 591  GLN A NE2 1 
ATOM   4894  N  N   . VAL A 1 592  ? 51.012 80.861  -36.528 1.00 9.14  ? 592  VAL A N   1 
ATOM   4895  C  CA  . VAL A 1 592  ? 50.944 81.960  -35.573 1.00 8.30  ? 592  VAL A CA  1 
ATOM   4896  C  C   . VAL A 1 592  ? 49.539 82.531  -35.560 1.00 9.16  ? 592  VAL A C   1 
ATOM   4897  O  O   . VAL A 1 592  ? 48.922 82.640  -36.608 1.00 9.90  ? 592  VAL A O   1 
ATOM   4898  C  CB  . VAL A 1 592  ? 51.976 83.043  -35.909 1.00 8.88  ? 592  VAL A CB  1 
ATOM   4899  C  CG1 . VAL A 1 592  ? 51.746 84.303  -35.063 1.00 9.35  ? 592  VAL A CG1 1 
ATOM   4900  C  CG2 . VAL A 1 592  ? 53.370 82.498  -35.624 1.00 9.28  ? 592  VAL A CG2 1 
ATOM   4901  N  N   . SER A 1 593  ? 49.039 82.827  -34.361 1.00 9.64  ? 593  SER A N   1 
ATOM   4902  C  CA  . SER A 1 593  ? 47.697 83.365  -34.171 1.00 10.02 ? 593  SER A CA  1 
ATOM   4903  C  C   . SER A 1 593  ? 47.840 84.536  -33.211 1.00 10.47 ? 593  SER A C   1 
ATOM   4904  O  O   . SER A 1 593  ? 48.825 84.632  -32.457 1.00 11.18 ? 593  SER A O   1 
ATOM   4905  C  CB  . SER A 1 593  ? 46.734 82.324  -33.519 1.00 10.80 ? 593  SER A CB  1 
ATOM   4906  O  OG  . SER A 1 593  ? 46.518 81.162  -34.320 1.00 13.98 ? 593  SER A OG  1 
ATOM   4907  N  N   . PRO A 1 594  ? 46.862 85.423  -33.165 1.00 10.60 ? 594  PRO A N   1 
ATOM   4908  C  CA  . PRO A 1 594  ? 46.918 86.482  -32.165 1.00 10.46 ? 594  PRO A CA  1 
ATOM   4909  C  C   . PRO A 1 594  ? 46.704 85.951  -30.742 1.00 10.54 ? 594  PRO A C   1 
ATOM   4910  O  O   . PRO A 1 594  ? 46.278 84.794  -30.538 1.00 10.74 ? 594  PRO A O   1 
ATOM   4911  C  CB  . PRO A 1 594  ? 45.763 87.419  -32.568 1.00 10.85 ? 594  PRO A CB  1 
ATOM   4912  C  CG  . PRO A 1 594  ? 45.344 86.967  -33.981 1.00 11.12 ? 594  PRO A CG  1 
ATOM   4913  C  CD  . PRO A 1 594  ? 45.629 85.500  -33.966 1.00 9.89  ? 594  PRO A CD  1 
ATOM   4914  N  N   . VAL A 1 595  ? 47.019 86.798  -29.752 1.00 10.47 ? 595  VAL A N   1 
ATOM   4915  C  CA  . VAL A 1 595  ? 46.651 86.525  -28.377 1.00 11.50 ? 595  VAL A CA  1 
ATOM   4916  C  C   . VAL A 1 595  ? 45.384 87.325  -28.111 1.00 12.21 ? 595  VAL A C   1 
ATOM   4917  O  O   . VAL A 1 595  ? 45.385 88.566  -28.146 1.00 12.87 ? 595  VAL A O   1 
ATOM   4918  C  CB  . VAL A 1 595  ? 47.768 86.903  -27.410 1.00 11.96 ? 595  VAL A CB  1 
ATOM   4919  C  CG1 . VAL A 1 595  ? 47.300 86.729  -25.984 1.00 12.82 ? 595  VAL A CG1 1 
ATOM   4920  C  CG2 . VAL A 1 595  ? 48.977 86.036  -27.674 1.00 11.27 ? 595  VAL A CG2 1 
ATOM   4921  N  N   . TRP A 1 596  ? 44.296 86.602  -27.942 1.00 11.67 ? 596  TRP A N   1 
ATOM   4922  C  CA  . TRP A 1 596  ? 42.988 87.170  -27.709 1.00 12.89 ? 596  TRP A CA  1 
ATOM   4923  C  C   . TRP A 1 596  ? 42.600 87.038  -26.254 1.00 14.63 ? 596  TRP A C   1 
ATOM   4924  O  O   . TRP A 1 596  ? 42.702 85.953  -25.672 1.00 15.47 ? 596  TRP A O   1 
ATOM   4925  C  CB  . TRP A 1 596  ? 41.938 86.418  -28.556 1.00 12.07 ? 596  TRP A CB  1 
ATOM   4926  C  CG  . TRP A 1 596  ? 42.074 86.600  -30.028 1.00 11.87 ? 596  TRP A CG  1 
ATOM   4927  C  CD1 . TRP A 1 596  ? 42.461 85.656  -30.959 1.00 10.05 ? 596  TRP A CD1 1 
ATOM   4928  C  CD2 . TRP A 1 596  ? 41.746 87.776  -30.768 1.00 10.97 ? 596  TRP A CD2 1 
ATOM   4929  N  NE1 . TRP A 1 596  ? 42.415 86.202  -32.220 1.00 11.45 ? 596  TRP A NE1 1 
ATOM   4930  C  CE2 . TRP A 1 596  ? 41.982 87.499  -32.130 1.00 11.23 ? 596  TRP A CE2 1 
ATOM   4931  C  CE3 . TRP A 1 596  ? 41.281 89.057  -30.414 1.00 10.27 ? 596  TRP A CE3 1 
ATOM   4932  C  CZ2 . TRP A 1 596  ? 41.777 88.449  -33.134 1.00 12.18 ? 596  TRP A CZ2 1 
ATOM   4933  C  CZ3 . TRP A 1 596  ? 41.080 90.005  -31.417 1.00 11.73 ? 596  TRP A CZ3 1 
ATOM   4934  C  CH2 . TRP A 1 596  ? 41.322 89.683  -32.751 1.00 12.10 ? 596  TRP A CH2 1 
ATOM   4935  N  N   . SER A 1 597  ? 42.165 88.141  -25.666 1.00 15.23 ? 597  SER A N   1 
ATOM   4936  C  CA  A SER A 1 597  ? 41.615 88.079  -24.322 0.50 15.48 ? 597  SER A CA  1 
ATOM   4937  C  CA  B SER A 1 597  ? 41.669 88.177  -24.296 0.50 16.06 ? 597  SER A CA  1 
ATOM   4938  C  C   . SER A 1 597  ? 40.229 88.689  -24.331 1.00 15.80 ? 597  SER A C   1 
ATOM   4939  O  O   . SER A 1 597  ? 39.920 89.575  -25.129 1.00 17.08 ? 597  SER A O   1 
ATOM   4940  C  CB  A SER A 1 597  ? 42.499 88.807  -23.324 0.50 16.19 ? 597  SER A CB  1 
ATOM   4941  C  CB  B SER A 1 597  ? 42.540 89.114  -23.449 0.50 16.81 ? 597  SER A CB  1 
ATOM   4942  O  OG  A SER A 1 597  ? 42.686 90.129  -23.769 0.50 14.33 ? 597  SER A OG  1 
ATOM   4943  O  OG  B SER A 1 597  ? 43.922 88.853  -23.654 0.50 18.47 ? 597  SER A OG  1 
ATOM   4944  N  N   . TRP A 1 598  ? 39.388 88.157  -23.463 1.00 14.97 ? 598  TRP A N   1 
ATOM   4945  C  CA  . TRP A 1 598  ? 37.999 88.568  -23.436 1.00 14.78 ? 598  TRP A CA  1 
ATOM   4946  C  C   . TRP A 1 598  ? 37.770 89.473  -22.250 1.00 16.19 ? 598  TRP A C   1 
ATOM   4947  O  O   . TRP A 1 598  ? 38.333 89.255  -21.189 1.00 17.01 ? 598  TRP A O   1 
ATOM   4948  C  CB  . TRP A 1 598  ? 37.102 87.340  -23.350 1.00 13.91 ? 598  TRP A CB  1 
ATOM   4949  C  CG  . TRP A 1 598  ? 37.024 86.608  -24.659 1.00 11.86 ? 598  TRP A CG  1 
ATOM   4950  C  CD1 . TRP A 1 598  ? 37.946 85.715  -25.159 1.00 11.41 ? 598  TRP A CD1 1 
ATOM   4951  C  CD2 . TRP A 1 598  ? 35.992 86.710  -25.634 1.00 11.38 ? 598  TRP A CD2 1 
ATOM   4952  N  NE1 . TRP A 1 598  ? 37.537 85.260  -26.393 1.00 11.45 ? 598  TRP A NE1 1 
ATOM   4953  C  CE2 . TRP A 1 598  ? 36.335 85.839  -26.702 1.00 8.82  ? 598  TRP A CE2 1 
ATOM   4954  C  CE3 . TRP A 1 598  ? 34.795 87.431  -25.722 1.00 9.18  ? 598  TRP A CE3 1 
ATOM   4955  C  CZ2 . TRP A 1 598  ? 35.529 85.682  -27.845 1.00 10.94 ? 598  TRP A CZ2 1 
ATOM   4956  C  CZ3 . TRP A 1 598  ? 33.982 87.260  -26.854 1.00 10.11 ? 598  TRP A CZ3 1 
ATOM   4957  C  CH2 . TRP A 1 598  ? 34.358 86.388  -27.895 1.00 10.78 ? 598  TRP A CH2 1 
ATOM   4958  N  N   . HIS A 1 599  ? 36.924 90.468  -22.459 1.00 18.15 ? 599  HIS A N   1 
ATOM   4959  C  CA  . HIS A 1 599  ? 36.711 91.514  -21.480 1.00 20.84 ? 599  HIS A CA  1 
ATOM   4960  C  C   . HIS A 1 599  ? 35.250 91.802  -21.365 1.00 21.14 ? 599  HIS A C   1 
ATOM   4961  O  O   . HIS A 1 599  ? 34.545 91.888  -22.377 1.00 20.44 ? 599  HIS A O   1 
ATOM   4962  C  CB  . HIS A 1 599  ? 37.451 92.780  -21.913 1.00 22.05 ? 599  HIS A CB  1 
ATOM   4963  C  CG  . HIS A 1 599  ? 38.942 92.613  -21.945 1.00 26.43 ? 599  HIS A CG  1 
ATOM   4964  N  ND1 . HIS A 1 599  ? 39.662 92.156  -20.858 1.00 29.36 ? 599  HIS A ND1 1 
ATOM   4965  C  CD2 . HIS A 1 599  ? 39.842 92.816  -22.936 1.00 30.54 ? 599  HIS A CD2 1 
ATOM   4966  C  CE1 . HIS A 1 599  ? 40.944 92.092  -21.177 1.00 31.10 ? 599  HIS A CE1 1 
ATOM   4967  N  NE2 . HIS A 1 599  ? 41.080 92.486  -22.433 1.00 30.74 ? 599  HIS A NE2 1 
ATOM   4968  N  N   . HIS A 1 600  ? 34.802 91.942  -20.125 1.00 22.80 ? 600  HIS A N   1 
ATOM   4969  C  CA  . HIS A 1 600  ? 33.464 92.450  -19.882 1.00 24.49 ? 600  HIS A CA  1 
ATOM   4970  C  C   . HIS A 1 600  ? 33.628 93.943  -19.891 1.00 24.69 ? 600  HIS A C   1 
ATOM   4971  O  O   . HIS A 1 600  ? 34.261 94.541  -18.998 1.00 25.39 ? 600  HIS A O   1 
ATOM   4972  C  CB  . HIS A 1 600  ? 32.838 91.935  -18.577 1.00 25.38 ? 600  HIS A CB  1 
ATOM   4973  C  CG  . HIS A 1 600  ? 31.490 92.533  -18.285 1.00 29.77 ? 600  HIS A CG  1 
ATOM   4974  N  ND1 . HIS A 1 600  ? 30.604 92.899  -19.279 1.00 32.66 ? 600  HIS A ND1 1 
ATOM   4975  C  CD2 . HIS A 1 600  ? 30.873 92.820  -17.112 1.00 33.17 ? 600  HIS A CD2 1 
ATOM   4976  C  CE1 . HIS A 1 600  ? 29.506 93.394  -18.734 1.00 34.27 ? 600  HIS A CE1 1 
ATOM   4977  N  NE2 . HIS A 1 600  ? 29.643 93.358  -17.420 1.00 34.78 ? 600  HIS A NE2 1 
ATOM   4978  N  N   . ASP A 1 601  ? 33.135 94.533  -20.965 1.00 24.47 ? 601  ASP A N   1 
ATOM   4979  C  CA  . ASP A 1 601  ? 33.238 95.953  -21.166 1.00 25.45 ? 601  ASP A CA  1 
ATOM   4980  C  C   . ASP A 1 601  ? 32.083 96.589  -20.393 1.00 25.93 ? 601  ASP A C   1 
ATOM   4981  O  O   . ASP A 1 601  ? 30.946 96.546  -20.841 1.00 25.33 ? 601  ASP A O   1 
ATOM   4982  C  CB  . ASP A 1 601  ? 33.136 96.239  -22.658 1.00 24.94 ? 601  ASP A CB  1 
ATOM   4983  C  CG  . ASP A 1 601  ? 33.516 97.650  -23.010 1.00 27.23 ? 601  ASP A CG  1 
ATOM   4984  O  OD1 . ASP A 1 601  ? 33.512 98.514  -22.102 1.00 25.74 ? 601  ASP A OD1 1 
ATOM   4985  O  OD2 . ASP A 1 601  ? 33.804 97.993  -24.184 1.00 29.09 ? 601  ASP A OD2 1 
ATOM   4986  N  N   . THR A 1 602  ? 32.378 97.148  -19.220 1.00 27.10 ? 602  THR A N   1 
ATOM   4987  C  CA  . THR A 1 602  ? 31.343 97.723  -18.351 1.00 28.79 ? 602  THR A CA  1 
ATOM   4988  C  C   . THR A 1 602  ? 30.756 98.994  -18.939 1.00 28.85 ? 602  THR A C   1 
ATOM   4989  O  O   . THR A 1 602  ? 29.738 99.495  -18.449 1.00 29.59 ? 602  THR A O   1 
ATOM   4990  C  CB  . THR A 1 602  ? 31.888 98.017  -16.928 1.00 28.92 ? 602  THR A CB  1 
ATOM   4991  O  OG1 . THR A 1 602  ? 33.050 98.862  -17.018 1.00 31.57 ? 602  THR A OG1 1 
ATOM   4992  C  CG2 . THR A 1 602  ? 32.385 96.732  -16.233 1.00 31.34 ? 602  THR A CG2 1 
ATOM   4993  N  N   . LEU A 1 603  ? 31.391 99.518  -19.985 1.00 28.45 ? 603  LEU A N   1 
ATOM   4994  C  CA  . LEU A 1 603  ? 30.905 100.712 -20.660 1.00 28.14 ? 603  LEU A CA  1 
ATOM   4995  C  C   . LEU A 1 603  ? 29.878 100.392 -21.750 1.00 27.21 ? 603  LEU A C   1 
ATOM   4996  O  O   . LEU A 1 603  ? 28.754 100.902 -21.687 1.00 26.77 ? 603  LEU A O   1 
ATOM   4997  C  CB  . LEU A 1 603  ? 32.064 101.594 -21.168 1.00 29.11 ? 603  LEU A CB  1 
ATOM   4998  C  CG  . LEU A 1 603  ? 32.755 102.551 -20.167 1.00 30.63 ? 603  LEU A CG  1 
ATOM   4999  C  CD1 . LEU A 1 603  ? 31.773 103.528 -19.497 1.00 32.34 ? 603  LEU A CD1 1 
ATOM   5000  C  CD2 . LEU A 1 603  ? 33.577 101.826 -19.099 1.00 33.01 ? 603  LEU A CD2 1 
ATOM   5001  N  N   . THR A 1 604  ? 30.242 99.526  -22.709 1.00 25.30 ? 604  THR A N   1 
ATOM   5002  C  CA  . THR A 1 604  ? 29.344 99.077  -23.786 1.00 23.44 ? 604  THR A CA  1 
ATOM   5003  C  C   . THR A 1 604  ? 28.380 97.956  -23.344 1.00 21.75 ? 604  THR A C   1 
ATOM   5004  O  O   . THR A 1 604  ? 27.453 97.606  -24.089 1.00 21.28 ? 604  THR A O   1 
ATOM   5005  C  CB  . THR A 1 604  ? 30.138 98.545  -24.999 1.00 23.92 ? 604  THR A CB  1 
ATOM   5006  O  OG1 . THR A 1 604  ? 30.974 97.454  -24.568 1.00 23.12 ? 604  THR A OG1 1 
ATOM   5007  C  CG2 . THR A 1 604  ? 31.126 99.598  -25.552 1.00 24.02 ? 604  THR A CG2 1 
ATOM   5008  N  N   . LYS A 1 605  ? 28.639 97.375  -22.171 1.00 20.58 ? 605  LYS A N   1 
ATOM   5009  C  CA  . LYS A 1 605  ? 27.836 96.262  -21.651 1.00 19.69 ? 605  LYS A CA  1 
ATOM   5010  C  C   . LYS A 1 605  ? 27.865 95.091  -22.634 1.00 19.76 ? 605  LYS A C   1 
ATOM   5011  O  O   . LYS A 1 605  ? 26.830 94.482  -22.936 1.00 20.64 ? 605  LYS A O   1 
ATOM   5012  C  CB  . LYS A 1 605  ? 26.381 96.706  -21.392 1.00 20.06 ? 605  LYS A CB  1 
ATOM   5013  C  CG  . LYS A 1 605  ? 26.273 97.873  -20.438 1.00 20.59 ? 605  LYS A CG  1 
ATOM   5014  C  CD  . LYS A 1 605  ? 26.672 97.431  -19.033 1.00 20.69 ? 605  LYS A CD  1 
ATOM   5015  C  CE  . LYS A 1 605  ? 26.612 98.574  -18.025 1.00 22.38 ? 605  LYS A CE  1 
ATOM   5016  N  NZ  . LYS A 1 605  ? 26.821 98.032  -16.642 1.00 26.64 ? 605  LYS A NZ  1 
ATOM   5017  N  N   . THR A 1 606  ? 29.054 94.819  -23.167 1.00 18.22 ? 606  THR A N   1 
ATOM   5018  C  CA  . THR A 1 606  ? 29.257 93.615  -23.984 1.00 18.00 ? 606  THR A CA  1 
ATOM   5019  C  C   . THR A 1 606  ? 30.471 92.878  -23.485 1.00 16.40 ? 606  THR A C   1 
ATOM   5020  O  O   . THR A 1 606  ? 31.330 93.434  -22.791 1.00 16.43 ? 606  THR A O   1 
ATOM   5021  C  CB  . THR A 1 606  ? 29.525 93.965  -25.445 1.00 18.77 ? 606  THR A CB  1 
ATOM   5022  O  OG1 . THR A 1 606  ? 30.678 94.819  -25.502 1.00 21.52 ? 606  THR A OG1 1 
ATOM   5023  C  CG2 . THR A 1 606  ? 28.331 94.738  -26.106 1.00 18.17 ? 606  THR A CG2 1 
ATOM   5024  N  N   . ILE A 1 607  ? 30.549 91.602  -23.857 1.00 15.05 ? 607  ILE A N   1 
ATOM   5025  C  CA  . ILE A 1 607  ? 31.732 90.774  -23.578 1.00 13.65 ? 607  ILE A CA  1 
ATOM   5026  C  C   . ILE A 1 607  ? 32.391 90.536  -24.935 1.00 13.28 ? 607  ILE A C   1 
ATOM   5027  O  O   . ILE A 1 607  ? 31.760 89.981  -25.855 1.00 12.54 ? 607  ILE A O   1 
ATOM   5028  C  CB  . ILE A 1 607  ? 31.283 89.450  -22.994 1.00 13.66 ? 607  ILE A CB  1 
ATOM   5029  C  CG1 . ILE A 1 607  ? 30.412 89.696  -21.759 1.00 15.56 ? 607  ILE A CG1 1 
ATOM   5030  C  CG2 . ILE A 1 607  ? 32.515 88.552  -22.652 1.00 13.36 ? 607  ILE A CG2 1 
ATOM   5031  C  CD1 . ILE A 1 607  ? 29.704 88.455  -21.257 1.00 18.38 ? 607  ILE A CD1 1 
ATOM   5032  N  N   . HIS A 1 608  ? 33.618 91.016  -25.101 1.00 13.95 ? 608  HIS A N   1 
ATOM   5033  C  CA  . HIS A 1 608  ? 34.222 91.024  -26.433 1.00 14.59 ? 608  HIS A CA  1 
ATOM   5034  C  C   . HIS A 1 608  ? 35.724 90.851  -26.335 1.00 13.58 ? 608  HIS A C   1 
ATOM   5035  O  O   . HIS A 1 608  ? 36.309 91.121  -25.287 1.00 14.06 ? 608  HIS A O   1 
ATOM   5036  C  CB  . HIS A 1 608  ? 33.865 92.297  -27.205 1.00 16.61 ? 608  HIS A CB  1 
ATOM   5037  C  CG  . HIS A 1 608  ? 34.397 93.553  -26.590 1.00 20.10 ? 608  HIS A CG  1 
ATOM   5038  N  ND1 . HIS A 1 608  ? 35.712 93.952  -26.718 1.00 25.88 ? 608  HIS A ND1 1 
ATOM   5039  C  CD2 . HIS A 1 608  ? 33.792 94.505  -25.837 1.00 23.26 ? 608  HIS A CD2 1 
ATOM   5040  C  CE1 . HIS A 1 608  ? 35.892 95.095  -26.078 1.00 25.81 ? 608  HIS A CE1 1 
ATOM   5041  N  NE2 . HIS A 1 608  ? 34.739 95.459  -25.546 1.00 25.37 ? 608  HIS A NE2 1 
ATOM   5042  N  N   . PRO A 1 609  ? 36.338 90.354  -27.394 1.00 12.83 ? 609  PRO A N   1 
ATOM   5043  C  CA  . PRO A 1 609  ? 37.772 90.084  -27.374 1.00 12.81 ? 609  PRO A CA  1 
ATOM   5044  C  C   . PRO A 1 609  ? 38.613 91.262  -27.809 1.00 13.66 ? 609  PRO A C   1 
ATOM   5045  O  O   . PRO A 1 609  ? 38.213 92.033  -28.694 1.00 15.32 ? 609  PRO A O   1 
ATOM   5046  C  CB  . PRO A 1 609  ? 37.913 88.962  -28.401 1.00 12.50 ? 609  PRO A CB  1 
ATOM   5047  C  CG  . PRO A 1 609  ? 36.819 89.197  -29.397 1.00 13.03 ? 609  PRO A CG  1 
ATOM   5048  C  CD  . PRO A 1 609  ? 35.727 89.929  -28.669 1.00 12.20 ? 609  PRO A CD  1 
ATOM   5049  N  N   . GLN A 1 610  ? 39.787 91.351  -27.198 1.00 13.44 ? 610  GLN A N   1 
ATOM   5050  C  CA  . GLN A 1 610  ? 40.791 92.310  -27.608 1.00 15.24 ? 610  GLN A CA  1 
ATOM   5051  C  C   . GLN A 1 610  ? 42.057 91.547  -27.976 1.00 13.25 ? 610  GLN A C   1 
ATOM   5052  O  O   . GLN A 1 610  ? 42.371 90.556  -27.338 1.00 14.33 ? 610  GLN A O   1 
ATOM   5053  C  CB  . GLN A 1 610  ? 41.043 93.326  -26.493 1.00 16.51 ? 610  GLN A CB  1 
ATOM   5054  C  CG  . GLN A 1 610  ? 39.825 94.250  -26.221 1.00 23.51 ? 610  GLN A CG  1 
ATOM   5055  C  CD  . GLN A 1 610  ? 39.578 95.277  -27.328 1.00 28.57 ? 610  GLN A CD  1 
ATOM   5056  O  OE1 . GLN A 1 610  ? 40.285 96.285  -27.406 1.00 33.14 ? 610  GLN A OE1 1 
ATOM   5057  N  NE2 . GLN A 1 610  ? 38.569 95.034  -28.171 1.00 30.18 ? 610  GLN A NE2 1 
ATOM   5058  N  N   . GLY A 1 611  ? 42.749 92.006  -29.006 1.00 13.94 ? 611  GLY A N   1 
ATOM   5059  C  CA  . GLY A 1 611  ? 43.953 91.331  -29.469 1.00 13.71 ? 611  GLY A CA  1 
ATOM   5060  C  C   . GLY A 1 611  ? 45.172 92.100  -28.996 1.00 14.74 ? 611  GLY A C   1 
ATOM   5061  O  O   . GLY A 1 611  ? 45.144 93.326  -28.883 1.00 14.72 ? 611  GLY A O   1 
ATOM   5062  N  N   . SER A 1 612  ? 46.235 91.372  -28.684 1.00 14.63 ? 612  SER A N   1 
ATOM   5063  C  CA  . SER A 1 612  ? 47.492 92.021  -28.341 1.00 14.33 ? 612  SER A CA  1 
ATOM   5064  C  C   . SER A 1 612  ? 48.165 92.547  -29.585 1.00 14.37 ? 612  SER A C   1 
ATOM   5065  O  O   . SER A 1 612  ? 48.106 91.924  -30.650 1.00 14.25 ? 612  SER A O   1 
ATOM   5066  C  CB  . SER A 1 612  ? 48.403 91.002  -27.661 1.00 14.39 ? 612  SER A CB  1 
ATOM   5067  O  OG  . SER A 1 612  ? 49.685 91.580  -27.466 1.00 15.01 ? 612  SER A OG  1 
ATOM   5068  N  N   . THR A 1 613  ? 48.846 93.695  -29.469 1.00 15.94 ? 613  THR A N   1 
ATOM   5069  C  CA  . THR A 1 613  ? 49.607 94.196  -30.605 1.00 16.85 ? 613  THR A CA  1 
ATOM   5070  C  C   . THR A 1 613  ? 51.111 93.961  -30.444 1.00 17.86 ? 613  THR A C   1 
ATOM   5071  O  O   . THR A 1 613  ? 51.902 94.442  -31.269 1.00 18.53 ? 613  THR A O   1 
ATOM   5072  C  CB  . THR A 1 613  ? 49.368 95.691  -30.854 1.00 17.55 ? 613  THR A CB  1 
ATOM   5073  O  OG1 . THR A 1 613  ? 49.857 96.411  -29.720 1.00 17.52 ? 613  THR A OG1 1 
ATOM   5074  C  CG2 . THR A 1 613  ? 47.868 96.017  -30.890 1.00 18.10 ? 613  THR A CG2 1 
ATOM   5075  N  N   . THR A 1 614  ? 51.507 93.226  -29.407 1.00 16.91 ? 614  THR A N   1 
ATOM   5076  C  CA  . THR A 1 614  ? 52.942 92.945  -29.203 1.00 17.95 ? 614  THR A CA  1 
ATOM   5077  C  C   . THR A 1 614  ? 53.240 91.506  -28.791 1.00 17.34 ? 614  THR A C   1 
ATOM   5078  O  O   . THR A 1 614  ? 54.401 91.164  -28.551 1.00 17.83 ? 614  THR A O   1 
ATOM   5079  C  CB  . THR A 1 614  ? 53.496 93.809  -28.079 1.00 18.27 ? 614  THR A CB  1 
ATOM   5080  O  OG1 . THR A 1 614  ? 52.645 93.667  -26.943 1.00 18.60 ? 614  THR A OG1 1 
ATOM   5081  C  CG2 . THR A 1 614  ? 53.489 95.317  -28.428 1.00 19.88 ? 614  THR A CG2 1 
ATOM   5082  N  N   . LYS A 1 615  ? 52.215 90.673  -28.631 1.00 16.16 ? 615  LYS A N   1 
ATOM   5083  C  CA  . LYS A 1 615  ? 52.492 89.288  -28.294 1.00 16.35 ? 615  LYS A CA  1 
ATOM   5084  C  C   . LYS A 1 615  ? 51.610 88.414  -29.142 1.00 14.05 ? 615  LYS A C   1 
ATOM   5085  O  O   . LYS A 1 615  ? 50.494 88.813  -29.500 1.00 13.62 ? 615  LYS A O   1 
ATOM   5086  C  CB  . LYS A 1 615  ? 52.428 89.006  -26.783 1.00 18.21 ? 615  LYS A CB  1 
ATOM   5087  C  CG  . LYS A 1 615  ? 51.177 88.556  -26.136 1.00 20.43 ? 615  LYS A CG  1 
ATOM   5088  C  CD  . LYS A 1 615  ? 51.478 88.516  -24.599 1.00 21.26 ? 615  LYS A CD  1 
ATOM   5089  C  CE  . LYS A 1 615  ? 50.303 88.025  -23.749 1.00 24.51 ? 615  LYS A CE  1 
ATOM   5090  N  NZ  . LYS A 1 615  ? 50.580 88.016  -22.249 1.00 23.77 ? 615  LYS A NZ  1 
ATOM   5091  N  N   . TYR A 1 616  ? 52.139 87.246  -29.497 1.00 11.48 ? 616  TYR A N   1 
ATOM   5092  C  CA  . TYR A 1 616  ? 51.502 86.369  -30.486 1.00 11.21 ? 616  TYR A CA  1 
ATOM   5093  C  C   . TYR A 1 616  ? 51.628 84.945  -30.017 1.00 10.29 ? 616  TYR A C   1 
ATOM   5094  O  O   . TYR A 1 616  ? 52.506 84.666  -29.205 1.00 11.06 ? 616  TYR A O   1 
ATOM   5095  C  CB  . TYR A 1 616  ? 52.177 86.534  -31.866 1.00 11.54 ? 616  TYR A CB  1 
ATOM   5096  C  CG  . TYR A 1 616  ? 52.097 87.975  -32.279 1.00 13.62 ? 616  TYR A CG  1 
ATOM   5097  C  CD1 . TYR A 1 616  ? 50.919 88.476  -32.835 1.00 15.44 ? 616  TYR A CD1 1 
ATOM   5098  C  CD2 . TYR A 1 616  ? 53.137 88.856  -31.997 1.00 13.72 ? 616  TYR A CD2 1 
ATOM   5099  C  CE1 . TYR A 1 616  ? 50.792 89.799  -33.137 1.00 16.78 ? 616  TYR A CE1 1 
ATOM   5100  C  CE2 . TYR A 1 616  ? 53.014 90.224  -32.304 1.00 15.81 ? 616  TYR A CE2 1 
ATOM   5101  C  CZ  . TYR A 1 616  ? 51.831 90.663  -32.872 1.00 15.25 ? 616  TYR A CZ  1 
ATOM   5102  O  OH  . TYR A 1 616  ? 51.666 91.991  -33.224 1.00 19.89 ? 616  TYR A OH  1 
ATOM   5103  N  N   . ARG A 1 617  ? 50.756 84.069  -30.502 1.00 9.66  ? 617  ARG A N   1 
ATOM   5104  C  CA  . ARG A 1 617  ? 50.830 82.655  -30.140 1.00 11.79 ? 617  ARG A CA  1 
ATOM   5105  C  C   . ARG A 1 617  ? 51.451 81.895  -31.284 1.00 10.97 ? 617  ARG A C   1 
ATOM   5106  O  O   . ARG A 1 617  ? 50.964 82.017  -32.413 1.00 11.23 ? 617  ARG A O   1 
ATOM   5107  C  CB  . ARG A 1 617  ? 49.434 82.077  -29.961 1.00 12.57 ? 617  ARG A CB  1 
ATOM   5108  C  CG  . ARG A 1 617  ? 48.720 82.422  -28.706 1.00 17.48 ? 617  ARG A CG  1 
ATOM   5109  C  CD  . ARG A 1 617  ? 47.363 81.719  -28.608 1.00 16.18 ? 617  ARG A CD  1 
ATOM   5110  N  NE  . ARG A 1 617  ? 47.429 80.251  -28.599 1.00 18.73 ? 617  ARG A NE  1 
ATOM   5111  C  CZ  . ARG A 1 617  ? 46.727 79.433  -29.389 1.00 21.65 ? 617  ARG A CZ  1 
ATOM   5112  N  NH1 . ARG A 1 617  ? 45.884 79.914  -30.310 1.00 21.17 ? 617  ARG A NH1 1 
ATOM   5113  N  NH2 . ARG A 1 617  ? 46.869 78.121  -29.266 1.00 22.50 ? 617  ARG A NH2 1 
ATOM   5114  N  N   . ILE A 1 618  ? 52.467 81.083  -31.038 1.00 8.86  ? 618  ILE A N   1 
ATOM   5115  C  CA  . ILE A 1 618  ? 52.970 80.184  -32.053 1.00 9.52  ? 618  ILE A CA  1 
ATOM   5116  C  C   . ILE A 1 618  ? 52.639 78.751  -31.657 1.00 9.66  ? 618  ILE A C   1 
ATOM   5117  O  O   . ILE A 1 618  ? 52.807 78.354  -30.487 1.00 10.23 ? 618  ILE A O   1 
ATOM   5118  C  CB  . ILE A 1 618  ? 54.449 80.375  -32.288 1.00 10.17 ? 618  ILE A CB  1 
ATOM   5119  C  CG1 . ILE A 1 618  ? 54.865 79.444  -33.411 1.00 11.03 ? 618  ILE A CG1 1 
ATOM   5120  C  CG2 . ILE A 1 618  ? 55.285 80.062  -31.028 1.00 10.91 ? 618  ILE A CG2 1 
ATOM   5121  C  CD1 . ILE A 1 618  ? 56.026 79.921  -34.194 1.00 13.27 ? 618  ILE A CD1 1 
ATOM   5122  N  N   . ILE A 1 619  ? 52.164 77.984  -32.627 1.00 9.09  ? 619  ILE A N   1 
ATOM   5123  C  CA  . ILE A 1 619  ? 51.660 76.629  -32.417 1.00 10.59 ? 619  ILE A CA  1 
ATOM   5124  C  C   . ILE A 1 619  ? 52.408 75.689  -33.349 1.00 10.17 ? 619  ILE A C   1 
ATOM   5125  O  O   . ILE A 1 619  ? 52.624 76.014  -34.520 1.00 9.80  ? 619  ILE A O   1 
ATOM   5126  C  CB  . ILE A 1 619  ? 50.154 76.582  -32.791 1.00 12.01 ? 619  ILE A CB  1 
ATOM   5127  C  CG1 . ILE A 1 619  ? 49.387 77.612  -31.962 1.00 15.44 ? 619  ILE A CG1 1 
ATOM   5128  C  CG2 . ILE A 1 619  ? 49.559 75.188  -32.601 1.00 15.56 ? 619  ILE A CG2 1 
ATOM   5129  C  CD1 . ILE A 1 619  ? 48.279 78.315  -32.723 1.00 18.47 ? 619  ILE A CD1 1 
ATOM   5130  N  N   . PHE A 1 620  ? 52.830 74.536  -32.865 1.00 7.97  ? 620  PHE A N   1 
ATOM   5131  C  CA  . PHE A 1 620  ? 53.469 73.561  -33.742 1.00 8.17  ? 620  PHE A CA  1 
ATOM   5132  C  C   . PHE A 1 620  ? 53.317 72.184  -33.117 1.00 8.88  ? 620  PHE A C   1 
ATOM   5133  O  O   . PHE A 1 620  ? 53.005 72.061  -31.925 1.00 8.91  ? 620  PHE A O   1 
ATOM   5134  C  CB  . PHE A 1 620  ? 54.943 73.866  -33.991 1.00 8.38  ? 620  PHE A CB  1 
ATOM   5135  C  CG  . PHE A 1 620  ? 55.795 73.819  -32.743 1.00 7.64  ? 620  PHE A CG  1 
ATOM   5136  C  CD1 . PHE A 1 620  ? 55.945 74.955  -31.942 1.00 8.95  ? 620  PHE A CD1 1 
ATOM   5137  C  CD2 . PHE A 1 620  ? 56.516 72.662  -32.395 1.00 7.91  ? 620  PHE A CD2 1 
ATOM   5138  C  CE1 . PHE A 1 620  ? 56.766 74.897  -30.792 1.00 9.94  ? 620  PHE A CE1 1 
ATOM   5139  C  CE2 . PHE A 1 620  ? 57.307 72.611  -31.254 1.00 8.74  ? 620  PHE A CE2 1 
ATOM   5140  C  CZ  . PHE A 1 620  ? 57.430 73.726  -30.459 1.00 9.48  ? 620  PHE A CZ  1 
ATOM   5141  N  N   . LYS A 1 621  ? 53.532 71.155  -33.923 1.00 8.69  ? 621  LYS A N   1 
ATOM   5142  C  CA  . LYS A 1 621  ? 53.373 69.798  -33.445 1.00 9.79  ? 621  LYS A CA  1 
ATOM   5143  C  C   . LYS A 1 621  ? 54.681 69.304  -32.846 1.00 10.14 ? 621  LYS A C   1 
ATOM   5144  O  O   . LYS A 1 621  ? 55.724 69.314  -33.496 1.00 10.80 ? 621  LYS A O   1 
ATOM   5145  C  CB  . LYS A 1 621  ? 52.944 68.909  -34.609 1.00 10.35 ? 621  LYS A CB  1 
ATOM   5146  C  CG  . LYS A 1 621  ? 52.555 67.485  -34.156 1.00 11.97 ? 621  LYS A CG  1 
ATOM   5147  C  CD  . LYS A 1 621  ? 51.743 66.746  -35.213 1.00 20.00 ? 621  LYS A CD  1 
ATOM   5148  C  CE  . LYS A 1 621  ? 52.371 66.873  -36.577 1.00 23.21 ? 621  LYS A CE  1 
ATOM   5149  N  NZ  . LYS A 1 621  ? 51.536 66.168  -37.603 1.00 26.89 ? 621  LYS A NZ  1 
ATOM   5150  N  N   . ALA A 1 622  ? 54.651 68.955  -31.558 1.00 10.10 ? 622  ALA A N   1 
ATOM   5151  C  CA  . ALA A 1 622  ? 55.826 68.417  -30.900 1.00 9.51  ? 622  ALA A CA  1 
ATOM   5152  C  C   . ALA A 1 622  ? 55.728 66.900  -30.913 1.00 10.00 ? 622  ALA A C   1 
ATOM   5153  O  O   . ALA A 1 622  ? 54.651 66.354  -30.720 1.00 11.31 ? 622  ALA A O   1 
ATOM   5154  C  CB  . ALA A 1 622  ? 55.877 68.904  -29.448 1.00 10.31 ? 622  ALA A CB  1 
ATOM   5155  N  N   . ARG A 1 623  ? 56.845 66.233  -31.175 1.00 8.91  ? 623  ARG A N   1 
ATOM   5156  C  CA  . ARG A 1 623  ? 56.898 64.761  -31.204 1.00 9.43  ? 623  ARG A CA  1 
ATOM   5157  C  C   . ARG A 1 623  ? 57.900 64.315  -30.162 1.00 8.99  ? 623  ARG A C   1 
ATOM   5158  O  O   . ARG A 1 623  ? 59.063 64.694  -30.210 1.00 10.45 ? 623  ARG A O   1 
ATOM   5159  C  CB  . ARG A 1 623  ? 57.338 64.258  -32.583 1.00 10.14 ? 623  ARG A CB  1 
ATOM   5160  C  CG  . ARG A 1 623  ? 57.333 62.718  -32.672 1.00 12.69 ? 623  ARG A CG  1 
ATOM   5161  C  CD  . ARG A 1 623  ? 57.417 62.142  -34.115 1.00 14.73 ? 623  ARG A CD  1 
ATOM   5162  N  NE  . ARG A 1 623  ? 57.589 60.680  -34.101 1.00 17.79 ? 623  ARG A NE  1 
ATOM   5163  C  CZ  . ARG A 1 623  ? 58.779 60.088  -34.055 1.00 21.16 ? 623  ARG A CZ  1 
ATOM   5164  N  NH1 . ARG A 1 623  ? 59.887 60.822  -34.047 1.00 23.81 ? 623  ARG A NH1 1 
ATOM   5165  N  NH2 . ARG A 1 623  ? 58.862 58.765  -34.002 1.00 21.44 ? 623  ARG A NH2 1 
ATOM   5166  N  N   . VAL A 1 624  ? 57.414 63.561  -29.174 1.00 7.42  ? 624  VAL A N   1 
ATOM   5167  C  CA  . VAL A 1 624  ? 58.193 63.330  -27.966 1.00 6.55  ? 624  VAL A CA  1 
ATOM   5168  C  C   . VAL A 1 624  ? 58.251 61.837  -27.665 1.00 6.04  ? 624  VAL A C   1 
ATOM   5169  O  O   . VAL A 1 624  ? 57.229 61.182  -27.777 1.00 6.41  ? 624  VAL A O   1 
ATOM   5170  C  CB  . VAL A 1 624  ? 57.553 64.084  -26.780 1.00 7.73  ? 624  VAL A CB  1 
ATOM   5171  C  CG1 . VAL A 1 624  ? 58.473 64.092  -25.571 1.00 8.19  ? 624  VAL A CG1 1 
ATOM   5172  C  CG2 . VAL A 1 624  ? 57.208 65.523  -27.171 1.00 9.27  ? 624  VAL A CG2 1 
ATOM   5173  N  N   . PRO A 1 625  ? 59.438 61.323  -27.314 1.00 7.22  ? 625  PRO A N   1 
ATOM   5174  C  CA  . PRO A 1 625  ? 59.562 59.878  -27.055 1.00 7.12  ? 625  PRO A CA  1 
ATOM   5175  C  C   . PRO A 1 625  ? 58.731 59.425  -25.856 1.00 6.91  ? 625  PRO A C   1 
ATOM   5176  O  O   . PRO A 1 625  ? 58.275 60.227  -25.025 1.00 6.47  ? 625  PRO A O   1 
ATOM   5177  C  CB  . PRO A 1 625  ? 61.050 59.685  -26.730 1.00 8.49  ? 625  PRO A CB  1 
ATOM   5178  C  CG  . PRO A 1 625  ? 61.760 60.905  -27.276 1.00 8.92  ? 625  PRO A CG  1 
ATOM   5179  C  CD  . PRO A 1 625  ? 60.730 62.014  -27.198 1.00 8.27  ? 625  PRO A CD  1 
ATOM   5180  N  N   . PRO A 1 626  ? 58.554 58.122  -25.720 1.00 7.13  ? 626  PRO A N   1 
ATOM   5181  C  CA  . PRO A 1 626  ? 57.920 57.564  -24.518 1.00 6.76  ? 626  PRO A CA  1 
ATOM   5182  C  C   . PRO A 1 626  ? 58.651 57.991  -23.256 1.00 7.27  ? 626  PRO A C   1 
ATOM   5183  O  O   . PRO A 1 626  ? 59.840 57.881  -23.156 1.00 6.88  ? 626  PRO A O   1 
ATOM   5184  C  CB  . PRO A 1 626  ? 58.036 56.046  -24.730 1.00 7.41  ? 626  PRO A CB  1 
ATOM   5185  C  CG  . PRO A 1 626  ? 58.336 55.877  -26.219 1.00 7.69  ? 626  PRO A CG  1 
ATOM   5186  C  CD  . PRO A 1 626  ? 59.157 57.074  -26.561 1.00 8.15  ? 626  PRO A CD  1 
ATOM   5187  N  N   . MET A 1 627  ? 57.909 58.491  -22.291 1.00 6.19  ? 627  MET A N   1 
ATOM   5188  C  CA  . MET A 1 627  ? 58.532 58.915  -21.024 1.00 6.46  ? 627  MET A CA  1 
ATOM   5189  C  C   . MET A 1 627  ? 59.800 59.724  -21.249 1.00 5.83  ? 627  MET A C   1 
ATOM   5190  O  O   . MET A 1 627  ? 60.800 59.554  -20.579 1.00 7.38  ? 627  MET A O   1 
ATOM   5191  C  CB  . MET A 1 627  ? 58.831 57.709  -20.111 1.00 7.19  ? 627  MET A CB  1 
ATOM   5192  C  CG  . MET A 1 627  ? 57.536 57.000  -19.771 1.00 6.50  ? 627  MET A CG  1 
ATOM   5193  S  SD  . MET A 1 627  ? 57.789 55.343  -19.054 1.00 11.22 ? 627  MET A SD  1 
ATOM   5194  C  CE  . MET A 1 627  ? 58.626 55.681  -17.524 1.00 12.00 ? 627  MET A CE  1 
ATOM   5195  N  N   . GLY A 1 628  ? 59.702 60.650  -22.215 1.00 6.48  ? 628  GLY A N   1 
ATOM   5196  C  CA  . GLY A 1 628  ? 60.895 61.305  -22.735 1.00 7.00  ? 628  GLY A CA  1 
ATOM   5197  C  C   . GLY A 1 628  ? 60.784 62.794  -22.941 1.00 6.50  ? 628  GLY A C   1 
ATOM   5198  O  O   . GLY A 1 628  ? 59.796 63.426  -22.546 1.00 6.53  ? 628  GLY A O   1 
ATOM   5199  N  N   . LEU A 1 629  ? 61.813 63.348  -23.568 1.00 6.64  ? 629  LEU A N   1 
ATOM   5200  C  CA  . LEU A 1 629  ? 61.916 64.802  -23.799 1.00 6.90  ? 629  LEU A CA  1 
ATOM   5201  C  C   . LEU A 1 629  ? 62.350 65.086  -25.203 1.00 7.18  ? 629  LEU A C   1 
ATOM   5202  O  O   . LEU A 1 629  ? 63.131 64.315  -25.796 1.00 7.07  ? 629  LEU A O   1 
ATOM   5203  C  CB  . LEU A 1 629  ? 62.965 65.429  -22.872 1.00 6.59  ? 629  LEU A CB  1 
ATOM   5204  C  CG  . LEU A 1 629  ? 62.748 65.259  -21.360 1.00 7.10  ? 629  LEU A CG  1 
ATOM   5205  C  CD1 . LEU A 1 629  ? 64.022 65.485  -20.580 1.00 7.45  ? 629  LEU A CD1 1 
ATOM   5206  C  CD2 . LEU A 1 629  ? 61.701 66.251  -20.907 1.00 8.12  ? 629  LEU A CD2 1 
ATOM   5207  N  N   . ALA A 1 630  ? 61.869 66.218  -25.734 1.00 6.68  ? 630  ALA A N   1 
ATOM   5208  C  CA  . ALA A 1 630  ? 62.248 66.665  -27.087 1.00 8.59  ? 630  ALA A CA  1 
ATOM   5209  C  C   . ALA A 1 630  ? 62.455 68.177  -27.057 1.00 8.50  ? 630  ALA A C   1 
ATOM   5210  O  O   . ALA A 1 630  ? 61.675 68.917  -26.462 1.00 8.68  ? 630  ALA A O   1 
ATOM   5211  C  CB  . ALA A 1 630  ? 61.184 66.316  -28.070 1.00 9.25  ? 630  ALA A CB  1 
ATOM   5212  N  N   . THR A 1 631  ? 63.536 68.623  -27.693 1.00 8.09  ? 631  THR A N   1 
ATOM   5213  C  CA  . THR A 1 631  ? 63.922 70.041  -27.687 1.00 8.38  ? 631  THR A CA  1 
ATOM   5214  C  C   . THR A 1 631  ? 63.639 70.643  -29.047 1.00 8.35  ? 631  THR A C   1 
ATOM   5215  O  O   . THR A 1 631  ? 63.923 70.023  -30.093 1.00 8.74  ? 631  THR A O   1 
ATOM   5216  C  CB  . THR A 1 631  ? 65.435 70.127  -27.441 1.00 8.39  ? 631  THR A CB  1 
ATOM   5217  O  OG1 . THR A 1 631  ? 65.740 69.495  -26.188 1.00 8.79  ? 631  THR A OG1 1 
ATOM   5218  C  CG2 . THR A 1 631  ? 65.932 71.563  -27.280 1.00 10.97 ? 631  THR A CG2 1 
ATOM   5219  N  N   . TYR A 1 632  ? 63.115 71.858  -29.018 1.00 7.52  ? 632  TYR A N   1 
ATOM   5220  C  CA  . TYR A 1 632  ? 62.904 72.611  -30.240 1.00 7.87  ? 632  TYR A CA  1 
ATOM   5221  C  C   . TYR A 1 632  ? 63.464 74.009  -30.040 1.00 8.36  ? 632  TYR A C   1 
ATOM   5222  O  O   . TYR A 1 632  ? 63.756 74.438  -28.922 1.00 8.06  ? 632  TYR A O   1 
ATOM   5223  C  CB  . TYR A 1 632  ? 61.421 72.715  -30.506 1.00 8.68  ? 632  TYR A CB  1 
ATOM   5224  C  CG  . TYR A 1 632  ? 60.810 71.408  -30.932 1.00 8.59  ? 632  TYR A CG  1 
ATOM   5225  C  CD1 . TYR A 1 632  ? 60.404 70.465  -29.980 1.00 8.64  ? 632  TYR A CD1 1 
ATOM   5226  C  CD2 . TYR A 1 632  ? 60.572 71.132  -32.289 1.00 11.13 ? 632  TYR A CD2 1 
ATOM   5227  C  CE1 . TYR A 1 632  ? 59.833 69.232  -30.364 1.00 9.89  ? 632  TYR A CE1 1 
ATOM   5228  C  CE2 . TYR A 1 632  ? 60.002 69.931  -32.696 1.00 11.05 ? 632  TYR A CE2 1 
ATOM   5229  C  CZ  . TYR A 1 632  ? 59.646 68.970  -31.719 1.00 9.89  ? 632  TYR A CZ  1 
ATOM   5230  O  OH  . TYR A 1 632  ? 59.073 67.772  -32.160 1.00 12.62 ? 632  TYR A OH  1 
ATOM   5231  N  N   . VAL A 1 633  ? 63.607 74.730  -31.163 1.00 7.59  ? 633  VAL A N   1 
ATOM   5232  C  CA  . VAL A 1 633  ? 64.151 76.088  -31.154 1.00 8.49  ? 633  VAL A CA  1 
ATOM   5233  C  C   . VAL A 1 633  ? 63.200 77.036  -31.886 1.00 7.52  ? 633  VAL A C   1 
ATOM   5234  O  O   . VAL A 1 633  ? 62.721 76.694  -32.963 1.00 8.43  ? 633  VAL A O   1 
ATOM   5235  C  CB  . VAL A 1 633  ? 65.536 76.156  -31.846 1.00 8.90  ? 633  VAL A CB  1 
ATOM   5236  C  CG1 . VAL A 1 633  ? 66.133 77.571  -31.716 1.00 11.36 ? 633  VAL A CG1 1 
ATOM   5237  C  CG2 . VAL A 1 633  ? 66.467 75.142  -31.207 1.00 11.23 ? 633  VAL A CG2 1 
ATOM   5238  N  N   . LEU A 1 634  ? 62.910 78.177  -31.244 1.00 7.84  ? 634  LEU A N   1 
ATOM   5239  C  CA  . LEU A 1 634  ? 62.106 79.239  -31.866 1.00 8.86  ? 634  LEU A CA  1 
ATOM   5240  C  C   . LEU A 1 634  ? 63.049 80.375  -32.231 1.00 9.09  ? 634  LEU A C   1 
ATOM   5241  O  O   . LEU A 1 634  ? 63.827 80.811  -31.392 1.00 9.55  ? 634  LEU A O   1 
ATOM   5242  C  CB  . LEU A 1 634  ? 61.068 79.775  -30.854 1.00 9.38  ? 634  LEU A CB  1 
ATOM   5243  C  CG  . LEU A 1 634  ? 60.163 78.777  -30.126 1.00 14.15 ? 634  LEU A CG  1 
ATOM   5244  C  CD1 . LEU A 1 634  ? 59.114 79.506  -29.326 1.00 15.16 ? 634  LEU A CD1 1 
ATOM   5245  C  CD2 . LEU A 1 634  ? 59.505 77.849  -31.074 1.00 16.48 ? 634  LEU A CD2 1 
ATOM   5246  N  N   . THR A 1 635  ? 62.992 80.803  -33.510 1.00 9.53  ? 635  THR A N   1 
ATOM   5247  C  CA  . THR A 1 635  ? 63.917 81.826  -34.018 1.00 9.20  ? 635  THR A CA  1 
ATOM   5248  C  C   . THR A 1 635  ? 63.136 82.949  -34.686 1.00 9.58  ? 635  THR A C   1 
ATOM   5249  O  O   . THR A 1 635  ? 62.218 82.692  -35.474 1.00 10.31 ? 635  THR A O   1 
ATOM   5250  C  CB  . THR A 1 635  ? 64.830 81.171  -35.055 1.00 10.30 ? 635  THR A CB  1 
ATOM   5251  O  OG1 . THR A 1 635  ? 65.587 80.124  -34.430 1.00 12.28 ? 635  THR A OG1 1 
ATOM   5252  C  CG2 . THR A 1 635  ? 65.881 82.168  -35.572 1.00 11.08 ? 635  THR A CG2 1 
ATOM   5253  N  N   . ILE A 1 636  ? 63.551 84.181  -34.380 1.00 11.35 ? 636  ILE A N   1 
ATOM   5254  C  CA  . ILE A 1 636  ? 62.892 85.331  -34.981 1.00 13.12 ? 636  ILE A CA  1 
ATOM   5255  C  C   . ILE A 1 636  ? 63.502 85.585  -36.368 1.00 14.37 ? 636  ILE A C   1 
ATOM   5256  O  O   . ILE A 1 636  ? 64.676 85.263  -36.610 1.00 14.52 ? 636  ILE A O   1 
ATOM   5257  C  CB  . ILE A 1 636  ? 63.010 86.568  -34.064 1.00 12.94 ? 636  ILE A CB  1 
ATOM   5258  C  CG1 . ILE A 1 636  ? 62.034 87.666  -34.502 1.00 13.37 ? 636  ILE A CG1 1 
ATOM   5259  C  CG2 . ILE A 1 636  ? 64.467 87.073  -34.000 1.00 14.14 ? 636  ILE A CG2 1 
ATOM   5260  C  CD1 . ILE A 1 636  ? 62.046 88.858  -33.581 1.00 15.22 ? 636  ILE A CD1 1 
ATOM   5261  N  N   . SER A 1 637  ? 62.686 86.112  -37.275 1.00 16.12 ? 637  SER A N   1 
ATOM   5262  C  CA  . SER A 1 637  ? 63.222 86.630  -38.544 1.00 19.42 ? 637  SER A CA  1 
ATOM   5263  C  C   . SER A 1 637  ? 62.600 87.991  -38.833 1.00 21.16 ? 637  SER A C   1 
ATOM   5264  O  O   . SER A 1 637  ? 61.716 88.408  -38.105 1.00 20.36 ? 637  SER A O   1 
ATOM   5265  C  CB  . SER A 1 637  ? 62.962 85.645  -39.683 1.00 20.99 ? 637  SER A CB  1 
ATOM   5266  O  OG  . SER A 1 637  ? 61.577 85.506  -39.920 1.00 22.92 ? 637  SER A OG  1 
ATOM   5267  N  N   . ASP A 1 638  ? 63.068 88.678  -39.886 1.00 23.33 ? 638  ASP A N   1 
ATOM   5268  C  CA  . ASP A 1 638  ? 62.555 90.020  -40.221 1.00 25.34 ? 638  ASP A CA  1 
ATOM   5269  C  C   . ASP A 1 638  ? 61.188 90.010  -40.913 1.00 25.15 ? 638  ASP A C   1 
ATOM   5270  O  O   . ASP A 1 638  ? 60.488 91.031  -40.950 1.00 26.66 ? 638  ASP A O   1 
ATOM   5271  C  CB  . ASP A 1 638  ? 63.547 90.778  -41.115 1.00 26.56 ? 638  ASP A CB  1 
ATOM   5272  C  CG  . ASP A 1 638  ? 64.909 90.978  -40.462 1.00 30.52 ? 638  ASP A CG  1 
ATOM   5273  O  OD1 . ASP A 1 638  ? 65.016 90.886  -39.214 1.00 35.58 ? 638  ASP A OD1 1 
ATOM   5274  O  OD2 . ASP A 1 638  ? 65.938 91.249  -41.124 1.00 36.49 ? 638  ASP A OD2 1 
ATOM   5275  N  N   . SER A 1 639  ? 60.806 88.862  -41.460 1.00 24.57 ? 639  SER A N   1 
ATOM   5276  C  CA  . SER A 1 639  ? 59.614 88.762  -42.285 1.00 24.45 ? 639  SER A CA  1 
ATOM   5277  C  C   . SER A 1 639  ? 59.026 87.365  -42.172 1.00 23.89 ? 639  SER A C   1 
ATOM   5278  O  O   . SER A 1 639  ? 59.613 86.503  -41.501 1.00 23.06 ? 639  SER A O   1 
ATOM   5279  C  CB  . SER A 1 639  ? 59.963 89.084  -43.744 1.00 24.32 ? 639  SER A CB  1 
ATOM   5280  O  OG  . SER A 1 639  ? 60.907 88.154  -44.261 1.00 26.32 ? 639  SER A OG  1 
ATOM   5281  N  N   . LYS A 1 640  ? 57.876 87.138  -42.816 1.00 23.12 ? 640  LYS A N   1 
ATOM   5282  C  CA  . LYS A 1 640  ? 57.216 85.820  -42.787 1.00 22.92 ? 640  LYS A CA  1 
ATOM   5283  C  C   . LYS A 1 640  ? 58.188 84.677  -43.078 1.00 21.88 ? 640  LYS A C   1 
ATOM   5284  O  O   . LYS A 1 640  ? 58.786 84.614  -44.155 1.00 22.23 ? 640  LYS A O   1 
ATOM   5285  C  CB  . LYS A 1 640  ? 56.043 85.738  -43.767 1.00 23.23 ? 640  LYS A CB  1 
ATOM   5286  C  CG  . LYS A 1 640  ? 54.791 86.512  -43.411 1.00 26.58 ? 640  LYS A CG  1 
ATOM   5287  C  CD  . LYS A 1 640  ? 53.618 85.954  -44.215 1.00 28.77 ? 640  LYS A CD  1 
ATOM   5288  C  CE  . LYS A 1 640  ? 52.663 87.045  -44.648 1.00 29.66 ? 640  LYS A CE  1 
ATOM   5289  N  NZ  . LYS A 1 640  ? 51.418 86.474  -45.236 1.00 30.91 ? 640  LYS A NZ  1 
ATOM   5290  N  N   . PRO A 1 641  ? 58.364 83.779  -42.114 1.00 20.41 ? 641  PRO A N   1 
ATOM   5291  C  CA  . PRO A 1 641  ? 59.155 82.568  -42.331 1.00 19.61 ? 641  PRO A CA  1 
ATOM   5292  C  C   . PRO A 1 641  ? 58.504 81.605  -43.307 1.00 18.74 ? 641  PRO A C   1 
ATOM   5293  O  O   . PRO A 1 641  ? 57.284 81.472  -43.331 1.00 19.55 ? 641  PRO A O   1 
ATOM   5294  C  CB  . PRO A 1 641  ? 59.161 81.912  -40.946 1.00 19.76 ? 641  PRO A CB  1 
ATOM   5295  C  CG  . PRO A 1 641  ? 58.876 83.006  -40.019 1.00 19.56 ? 641  PRO A CG  1 
ATOM   5296  C  CD  . PRO A 1 641  ? 57.882 83.872  -40.719 1.00 20.59 ? 641  PRO A CD  1 
ATOM   5297  N  N   . GLU A 1 642  ? 59.314 80.869  -44.051 1.00 19.26 ? 642  GLU A N   1 
ATOM   5298  C  CA  . GLU A 1 642  ? 58.796 79.904  -45.012 1.00 19.45 ? 642  GLU A CA  1 
ATOM   5299  C  C   . GLU A 1 642  ? 57.828 78.867  -44.437 1.00 18.32 ? 642  GLU A C   1 
ATOM   5300  O  O   . GLU A 1 642  ? 56.870 78.467  -45.099 1.00 18.62 ? 642  GLU A O   1 
ATOM   5301  C  CB  . GLU A 1 642  ? 59.964 79.176  -45.688 1.00 20.56 ? 642  GLU A CB  1 
ATOM   5302  C  CG  . GLU A 1 642  ? 59.537 78.153  -46.715 1.00 22.15 ? 642  GLU A CG  1 
ATOM   5303  C  CD  . GLU A 1 642  ? 60.704 77.582  -47.513 1.00 23.40 ? 642  GLU A CD  1 
ATOM   5304  O  OE1 . GLU A 1 642  ? 61.878 77.925  -47.236 1.00 29.17 ? 642  GLU A OE1 1 
ATOM   5305  O  OE2 . GLU A 1 642  ? 60.441 76.778  -48.426 1.00 30.33 ? 642  GLU A OE2 1 
ATOM   5306  N  N   . HIS A 1 643  ? 58.101 78.409  -43.215 1.00 16.32 ? 643  HIS A N   1 
ATOM   5307  C  CA  . HIS A 1 643  ? 57.334 77.272  -42.658 1.00 15.42 ? 643  HIS A CA  1 
ATOM   5308  C  C   . HIS A 1 643  ? 56.363 77.673  -41.554 1.00 14.24 ? 643  HIS A C   1 
ATOM   5309  O  O   . HIS A 1 643  ? 55.890 76.817  -40.799 1.00 13.32 ? 643  HIS A O   1 
ATOM   5310  C  CB  . HIS A 1 643  ? 58.279 76.169  -42.172 1.00 15.94 ? 643  HIS A CB  1 
ATOM   5311  C  CG  . HIS A 1 643  ? 59.114 75.601  -43.269 1.00 18.14 ? 643  HIS A CG  1 
ATOM   5312  N  ND1 . HIS A 1 643  ? 58.650 74.625  -44.119 1.00 23.84 ? 643  HIS A ND1 1 
ATOM   5313  C  CD2 . HIS A 1 643  ? 60.370 75.900  -43.674 1.00 21.31 ? 643  HIS A CD2 1 
ATOM   5314  C  CE1 . HIS A 1 643  ? 59.592 74.336  -45.001 1.00 22.89 ? 643  HIS A CE1 1 
ATOM   5315  N  NE2 . HIS A 1 643  ? 60.645 75.096  -44.751 1.00 22.57 ? 643  HIS A NE2 1 
ATOM   5316  N  N   . THR A 1 644  ? 56.037 78.955  -41.493 1.00 12.44 ? 644  THR A N   1 
ATOM   5317  C  CA  . THR A 1 644  ? 55.071 79.462  -40.524 1.00 12.66 ? 644  THR A CA  1 
ATOM   5318  C  C   . THR A 1 644  ? 53.908 80.072  -41.291 1.00 12.63 ? 644  THR A C   1 
ATOM   5319  O  O   . THR A 1 644  ? 54.134 80.895  -42.213 1.00 13.06 ? 644  THR A O   1 
ATOM   5320  C  CB  . THR A 1 644  ? 55.750 80.473  -39.586 1.00 12.08 ? 644  THR A CB  1 
ATOM   5321  O  OG1 . THR A 1 644  ? 56.764 79.783  -38.841 1.00 12.41 ? 644  THR A OG1 1 
ATOM   5322  C  CG2 . THR A 1 644  ? 54.776 81.035  -38.506 1.00 13.63 ? 644  THR A CG2 1 
ATOM   5323  N  N   . SER A 1 645  ? 52.682 79.654  -40.964 1.00 11.30 ? 645  SER A N   1 
ATOM   5324  C  CA  . SER A 1 645  ? 51.464 80.252  -41.528 1.00 11.34 ? 645  SER A CA  1 
ATOM   5325  C  C   . SER A 1 645  ? 50.770 81.104  -40.479 1.00 10.71 ? 645  SER A C   1 
ATOM   5326  O  O   . SER A 1 645  ? 51.088 81.027  -39.288 1.00 10.68 ? 645  SER A O   1 
ATOM   5327  C  CB  . SER A 1 645  ? 50.491 79.210  -42.050 1.00 12.14 ? 645  SER A CB  1 
ATOM   5328  O  OG  . SER A 1 645  ? 49.987 78.423  -40.974 1.00 15.65 ? 645  SER A OG  1 
ATOM   5329  N  N   . TYR A 1 646  ? 49.836 81.930  -40.926 1.00 11.00 ? 646  TYR A N   1 
ATOM   5330  C  CA  . TYR A 1 646  ? 49.129 82.865  -40.064 1.00 10.86 ? 646  TYR A CA  1 
ATOM   5331  C  C   . TYR A 1 646  ? 47.648 82.607  -40.147 1.00 11.36 ? 646  TYR A C   1 
ATOM   5332  O  O   . TYR A 1 646  ? 47.083 82.500  -41.227 1.00 13.56 ? 646  TYR A O   1 
ATOM   5333  C  CB  . TYR A 1 646  ? 49.454 84.299  -40.488 1.00 12.16 ? 646  TYR A CB  1 
ATOM   5334  C  CG  . TYR A 1 646  ? 50.910 84.519  -40.253 1.00 11.21 ? 646  TYR A CG  1 
ATOM   5335  C  CD1 . TYR A 1 646  ? 51.371 84.924  -39.002 1.00 9.76  ? 646  TYR A CD1 1 
ATOM   5336  C  CD2 . TYR A 1 646  ? 51.847 84.179  -41.223 1.00 12.85 ? 646  TYR A CD2 1 
ATOM   5337  C  CE1 . TYR A 1 646  ? 52.729 85.067  -38.751 1.00 12.23 ? 646  TYR A CE1 1 
ATOM   5338  C  CE2 . TYR A 1 646  ? 53.208 84.310  -40.983 1.00 14.35 ? 646  TYR A CE2 1 
ATOM   5339  C  CZ  . TYR A 1 646  ? 53.646 84.758  -39.744 1.00 13.09 ? 646  TYR A CZ  1 
ATOM   5340  O  OH  . TYR A 1 646  ? 54.991 84.877  -39.454 1.00 13.88 ? 646  TYR A OH  1 
ATOM   5341  N  N   . ALA A 1 647  ? 47.009 82.513  -38.976 1.00 10.00 ? 647  ALA A N   1 
ATOM   5342  C  CA  . ALA A 1 647  ? 45.570 82.323  -38.923 1.00 10.27 ? 647  ALA A CA  1 
ATOM   5343  C  C   . ALA A 1 647  ? 44.808 83.550  -39.425 1.00 10.04 ? 647  ALA A C   1 
ATOM   5344  O  O   . ALA A 1 647  ? 45.217 84.677  -39.200 1.00 10.62 ? 647  ALA A O   1 
ATOM   5345  C  CB  . ALA A 1 647  ? 45.135 82.018  -37.481 1.00 11.15 ? 647  ALA A CB  1 
ATOM   5346  N  N   . SER A 1 648  ? 43.673 83.299  -40.048 1.00 10.65 ? 648  SER A N   1 
ATOM   5347  C  CA  . SER A 1 648  ? 42.737 84.389  -40.308 1.00 10.98 ? 648  SER A CA  1 
ATOM   5348  C  C   . SER A 1 648  ? 41.818 84.535  -39.097 1.00 9.17  ? 648  SER A C   1 
ATOM   5349  O  O   . SER A 1 648  ? 41.647 83.571  -38.284 1.00 8.83  ? 648  SER A O   1 
ATOM   5350  C  CB  . SER A 1 648  ? 41.923 84.089  -41.553 1.00 12.62 ? 648  SER A CB  1 
ATOM   5351  O  OG  . SER A 1 648  ? 41.132 82.944  -41.384 1.00 17.44 ? 648  SER A OG  1 
ATOM   5352  N  N   . ASN A 1 649  ? 41.235 85.704  -38.914 1.00 8.89  ? 649  ASN A N   1 
ATOM   5353  C  CA  . ASN A 1 649  ? 40.356 85.994  -37.783 1.00 8.48  ? 649  ASN A CA  1 
ATOM   5354  C  C   . ASN A 1 649  ? 39.142 86.725  -38.247 1.00 9.79  ? 649  ASN A C   1 
ATOM   5355  O  O   . ASN A 1 649  ? 39.260 87.675  -39.036 1.00 9.70  ? 649  ASN A O   1 
ATOM   5356  C  CB  . ASN A 1 649  ? 41.067 86.812  -36.705 1.00 9.90  ? 649  ASN A CB  1 
ATOM   5357  C  CG  . ASN A 1 649  ? 42.273 86.087  -36.152 1.00 10.24 ? 649  ASN A CG  1 
ATOM   5358  O  OD1 . ASN A 1 649  ? 42.137 85.322  -35.182 1.00 12.12 ? 649  ASN A OD1 1 
ATOM   5359  N  ND2 . ASN A 1 649  ? 43.437 86.274  -36.763 1.00 11.95 ? 649  ASN A ND2 1 
ATOM   5360  N  N   . LEU A 1 650  ? 37.988 86.292  -37.776 1.00 8.36  ? 650  LEU A N   1 
ATOM   5361  C  CA  . LEU A 1 650  ? 36.720 86.880  -38.155 1.00 9.52  ? 650  LEU A CA  1 
ATOM   5362  C  C   . LEU A 1 650  ? 35.932 87.141  -36.892 1.00 10.51 ? 650  LEU A C   1 
ATOM   5363  O  O   . LEU A 1 650  ? 35.668 86.229  -36.100 1.00 10.71 ? 650  LEU A O   1 
ATOM   5364  C  CB  . LEU A 1 650  ? 35.952 85.926  -39.074 1.00 10.14 ? 650  LEU A CB  1 
ATOM   5365  C  CG  . LEU A 1 650  ? 34.504 86.248  -39.382 1.00 10.74 ? 650  LEU A CG  1 
ATOM   5366  C  CD1 . LEU A 1 650  ? 34.435 87.528  -40.251 1.00 12.01 ? 650  LEU A CD1 1 
ATOM   5367  C  CD2 . LEU A 1 650  ? 33.915 85.089  -40.157 1.00 13.27 ? 650  LEU A CD2 1 
ATOM   5368  N  N   . LEU A 1 651  ? 35.563 88.382  -36.669 1.00 10.40 ? 651  LEU A N   1 
ATOM   5369  C  CA  . LEU A 1 651  ? 34.771 88.778  -35.525 1.00 11.84 ? 651  LEU A CA  1 
ATOM   5370  C  C   . LEU A 1 651  ? 33.329 89.014  -35.958 1.00 12.35 ? 651  LEU A C   1 
ATOM   5371  O  O   . LEU A 1 651  ? 33.051 89.880  -36.806 1.00 12.51 ? 651  LEU A O   1 
ATOM   5372  C  CB  . LEU A 1 651  ? 35.366 90.042  -34.923 1.00 12.90 ? 651  LEU A CB  1 
ATOM   5373  C  CG  . LEU A 1 651  ? 35.069 90.392  -33.449 1.00 17.88 ? 651  LEU A CG  1 
ATOM   5374  C  CD1 . LEU A 1 651  ? 33.799 91.155  -33.319 1.00 24.33 ? 651  LEU A CD1 1 
ATOM   5375  C  CD2 . LEU A 1 651  ? 35.089 89.224  -32.475 1.00 17.66 ? 651  LEU A CD2 1 
ATOM   5376  N  N   . LEU A 1 652  ? 32.407 88.213  -35.449 1.00 11.85 ? 652  LEU A N   1 
ATOM   5377  C  CA  . LEU A 1 652  ? 31.009 88.303  -35.797 1.00 12.45 ? 652  LEU A CA  1 
ATOM   5378  C  C   . LEU A 1 652  ? 30.243 89.015  -34.694 1.00 13.73 ? 652  LEU A C   1 
ATOM   5379  O  O   . LEU A 1 652  ? 30.137 88.540  -33.567 1.00 13.94 ? 652  LEU A O   1 
ATOM   5380  C  CB  . LEU A 1 652  ? 30.429 86.920  -36.080 1.00 12.34 ? 652  LEU A CB  1 
ATOM   5381  C  CG  . LEU A 1 652  ? 31.147 86.176  -37.201 1.00 11.14 ? 652  LEU A CG  1 
ATOM   5382  C  CD1 . LEU A 1 652  ? 30.615 84.775  -37.332 1.00 12.36 ? 652  LEU A CD1 1 
ATOM   5383  C  CD2 . LEU A 1 652  ? 30.964 86.931  -38.523 1.00 13.52 ? 652  LEU A CD2 1 
ATOM   5384  N  N   . ARG A 1 653  ? 29.733 90.187  -35.037 1.00 14.36 ? 653  ARG A N   1 
ATOM   5385  C  CA  . ARG A 1 653  ? 28.963 90.989  -34.124 1.00 16.59 ? 653  ARG A CA  1 
ATOM   5386  C  C   . ARG A 1 653  ? 28.384 92.150  -34.927 1.00 17.09 ? 653  ARG A C   1 
ATOM   5387  O  O   . ARG A 1 653  ? 28.947 92.576  -35.897 1.00 17.96 ? 653  ARG A O   1 
ATOM   5388  C  CB  . ARG A 1 653  ? 29.840 91.539  -33.009 1.00 17.04 ? 653  ARG A CB  1 
ATOM   5389  C  CG  . ARG A 1 653  ? 30.435 92.845  -33.395 1.00 21.02 ? 653  ARG A CG  1 
ATOM   5390  C  CD  . ARG A 1 653  ? 31.284 93.457  -32.347 1.00 27.92 ? 653  ARG A CD  1 
ATOM   5391  N  NE  . ARG A 1 653  ? 30.667 93.569  -31.045 1.00 30.56 ? 653  ARG A NE  1 
ATOM   5392  C  CZ  . ARG A 1 653  ? 30.987 94.419  -30.091 1.00 32.91 ? 653  ARG A CZ  1 
ATOM   5393  N  NH1 . ARG A 1 653  ? 31.915 95.362  -30.286 1.00 34.95 ? 653  ARG A NH1 1 
ATOM   5394  N  NH2 . ARG A 1 653  ? 30.348 94.368  -28.936 1.00 36.22 ? 653  ARG A NH2 1 
ATOM   5395  N  N   . LYS A 1 654  ? 27.262 92.663  -34.483 1.00 18.92 ? 654  LYS A N   1 
ATOM   5396  C  CA  . LYS A 1 654  ? 26.794 93.903  -35.077 1.00 20.97 ? 654  LYS A CA  1 
ATOM   5397  C  C   . LYS A 1 654  ? 27.559 95.057  -34.423 1.00 21.66 ? 654  LYS A C   1 
ATOM   5398  O  O   . LYS A 1 654  ? 28.047 94.926  -33.303 1.00 21.97 ? 654  LYS A O   1 
ATOM   5399  C  CB  . LYS A 1 654  ? 25.273 94.026  -34.942 1.00 21.89 ? 654  LYS A CB  1 
ATOM   5400  C  CG  . LYS A 1 654  ? 24.511 92.998  -35.791 1.00 24.72 ? 654  LYS A CG  1 
ATOM   5401  C  CD  . LYS A 1 654  ? 23.267 93.587  -36.465 1.00 30.99 ? 654  LYS A CD  1 
ATOM   5402  C  CE  . LYS A 1 654  ? 23.644 94.439  -37.693 1.00 33.39 ? 654  LYS A CE  1 
ATOM   5403  N  NZ  . LYS A 1 654  ? 22.505 94.658  -38.642 1.00 35.47 ? 654  LYS A NZ  1 
ATOM   5404  N  N   . ASN A 1 655  ? 27.689 96.168  -35.132 1.00 22.96 ? 655  ASN A N   1 
ATOM   5405  C  CA  . ASN A 1 655  ? 28.385 97.329  -34.581 1.00 23.49 ? 655  ASN A CA  1 
ATOM   5406  C  C   . ASN A 1 655  ? 29.838 97.003  -34.195 1.00 22.41 ? 655  ASN A C   1 
ATOM   5407  O  O   . ASN A 1 655  ? 30.257 97.252  -33.061 1.00 22.62 ? 655  ASN A O   1 
ATOM   5408  C  CB  . ASN A 1 655  ? 27.619 97.854  -33.351 1.00 24.79 ? 655  ASN A CB  1 
ATOM   5409  C  CG  . ASN A 1 655  ? 27.980 99.279  -32.992 1.00 28.54 ? 655  ASN A CG  1 
ATOM   5410  O  OD1 . ASN A 1 655  ? 28.352 100.075 -33.860 1.00 32.39 ? 655  ASN A OD1 1 
ATOM   5411  N  ND2 . ASN A 1 655  ? 27.865 99.616  -31.700 1.00 31.24 ? 655  ASN A ND2 1 
ATOM   5412  N  N   . PRO A 1 656  ? 30.620 96.452  -35.119 1.00 20.96 ? 656  PRO A N   1 
ATOM   5413  C  CA  . PRO A 1 656  ? 32.003 96.130  -34.775 1.00 19.46 ? 656  PRO A CA  1 
ATOM   5414  C  C   . PRO A 1 656  ? 32.823 97.400  -34.710 1.00 18.18 ? 656  PRO A C   1 
ATOM   5415  O  O   . PRO A 1 656  ? 32.487 98.407  -35.357 1.00 17.57 ? 656  PRO A O   1 
ATOM   5416  C  CB  . PRO A 1 656  ? 32.477 95.291  -35.950 1.00 19.11 ? 656  PRO A CB  1 
ATOM   5417  C  CG  . PRO A 1 656  ? 31.657 95.769  -37.082 1.00 19.56 ? 656  PRO A CG  1 
ATOM   5418  C  CD  . PRO A 1 656  ? 30.297 96.078  -36.510 1.00 21.00 ? 656  PRO A CD  1 
ATOM   5419  N  N   . THR A 1 657  ? 33.873 97.337  -33.914 1.00 17.96 ? 657  THR A N   1 
ATOM   5420  C  CA  . THR A 1 657  ? 34.932 98.324  -33.974 1.00 17.94 ? 657  THR A CA  1 
ATOM   5421  C  C   . THR A 1 657  ? 36.217 97.606  -34.376 1.00 16.88 ? 657  THR A C   1 
ATOM   5422  O  O   . THR A 1 657  ? 36.309 96.377  -34.290 1.00 16.11 ? 657  THR A O   1 
ATOM   5423  C  CB  . THR A 1 657  ? 35.096 99.024  -32.634 1.00 19.28 ? 657  THR A CB  1 
ATOM   5424  O  OG1 . THR A 1 657  ? 35.072 98.057  -31.578 1.00 21.98 ? 657  THR A OG1 1 
ATOM   5425  C  CG2 . THR A 1 657  ? 33.881 99.898  -32.339 1.00 20.12 ? 657  THR A CG2 1 
ATOM   5426  N  N   . SER A 1 658  ? 37.212 98.370  -34.797 1.00 15.23 ? 658  SER A N   1 
ATOM   5427  C  CA  . SER A 1 658  ? 38.448 97.818  -35.332 1.00 15.30 ? 658  SER A CA  1 
ATOM   5428  C  C   . SER A 1 658  ? 39.238 97.016  -34.288 1.00 15.67 ? 658  SER A C   1 
ATOM   5429  O  O   . SER A 1 658  ? 39.050 97.194  -33.080 1.00 16.33 ? 658  SER A O   1 
ATOM   5430  C  CB  . SER A 1 658  ? 39.315 98.965  -35.809 1.00 16.26 ? 658  SER A CB  1 
ATOM   5431  O  OG  . SER A 1 658  ? 39.626 99.736  -34.672 1.00 17.94 ? 658  SER A OG  1 
ATOM   5432  N  N   . LEU A 1 659  ? 40.104 96.128  -34.780 1.00 14.75 ? 659  LEU A N   1 
ATOM   5433  C  CA  . LEU A 1 659  ? 40.913 95.253  -33.919 1.00 15.59 ? 659  LEU A CA  1 
ATOM   5434  C  C   . LEU A 1 659  ? 42.329 95.190  -34.493 1.00 15.50 ? 659  LEU A C   1 
ATOM   5435  O  O   . LEU A 1 659  ? 42.660 94.273  -35.250 1.00 15.52 ? 659  LEU A O   1 
ATOM   5436  C  CB  . LEU A 1 659  ? 40.308 93.837  -33.858 1.00 15.83 ? 659  LEU A CB  1 
ATOM   5437  C  CG  . LEU A 1 659  ? 39.010 93.637  -33.072 1.00 17.05 ? 659  LEU A CG  1 
ATOM   5438  C  CD1 . LEU A 1 659  ? 38.402 92.243  -33.363 1.00 19.39 ? 659  LEU A CD1 1 
ATOM   5439  C  CD2 . LEU A 1 659  ? 39.223 93.853  -31.584 1.00 17.39 ? 659  LEU A CD2 1 
ATOM   5440  N  N   . PRO A 1 660  ? 43.142 96.217  -34.215 1.00 15.64 ? 660  PRO A N   1 
ATOM   5441  C  CA  . PRO A 1 660  ? 44.538 96.238  -34.665 1.00 15.90 ? 660  PRO A CA  1 
ATOM   5442  C  C   . PRO A 1 660  ? 45.353 95.131  -33.983 1.00 15.14 ? 660  PRO A C   1 
ATOM   5443  O  O   . PRO A 1 660  ? 45.066 94.778  -32.836 1.00 14.67 ? 660  PRO A O   1 
ATOM   5444  C  CB  . PRO A 1 660  ? 45.031 97.626  -34.240 1.00 16.42 ? 660  PRO A CB  1 
ATOM   5445  C  CG  . PRO A 1 660  ? 44.086 98.112  -33.202 1.00 16.92 ? 660  PRO A CG  1 
ATOM   5446  C  CD  . PRO A 1 660  ? 42.764 97.435  -33.470 1.00 16.51 ? 660  PRO A CD  1 
ATOM   5447  N  N   . LEU A 1 661  ? 46.325 94.582  -34.697 1.00 15.76 ? 661  LEU A N   1 
ATOM   5448  C  CA  . LEU A 1 661  ? 47.114 93.470  -34.169 1.00 16.06 ? 661  LEU A CA  1 
ATOM   5449  C  C   . LEU A 1 661  ? 48.623 93.658  -34.365 1.00 17.35 ? 661  LEU A C   1 
ATOM   5450  O  O   . LEU A 1 661  ? 49.370 92.689  -34.479 1.00 16.19 ? 661  LEU A O   1 
ATOM   5451  C  CB  . LEU A 1 661  ? 46.658 92.179  -34.835 1.00 16.04 ? 661  LEU A CB  1 
ATOM   5452  C  CG  . LEU A 1 661  ? 45.250 91.661  -34.505 1.00 14.34 ? 661  LEU A CG  1 
ATOM   5453  C  CD1 . LEU A 1 661  ? 45.001 90.392  -35.316 1.00 13.65 ? 661  LEU A CD1 1 
ATOM   5454  C  CD2 . LEU A 1 661  ? 45.072 91.398  -33.008 1.00 14.15 ? 661  LEU A CD2 1 
ATOM   5455  N  N   . GLY A 1 662  ? 49.075 94.910  -34.414 1.00 18.12 ? 662  GLY A N   1 
ATOM   5456  C  CA  . GLY A 1 662  ? 50.505 95.183  -34.531 1.00 18.70 ? 662  GLY A CA  1 
ATOM   5457  C  C   . GLY A 1 662  ? 51.066 94.654  -35.830 1.00 19.39 ? 662  GLY A C   1 
ATOM   5458  O  O   . GLY A 1 662  ? 50.474 94.867  -36.887 1.00 19.32 ? 662  GLY A O   1 
ATOM   5459  N  N   . GLN A 1 663  ? 52.180 93.915  -35.756 1.00 19.31 ? 663  GLN A N   1 
ATOM   5460  C  CA  . GLN A 1 663  ? 52.819 93.399  -36.976 1.00 19.95 ? 663  GLN A CA  1 
ATOM   5461  C  C   . GLN A 1 663  ? 52.170 92.138  -37.530 1.00 18.25 ? 663  GLN A C   1 
ATOM   5462  O  O   . GLN A 1 663  ? 52.625 91.611  -38.540 1.00 19.27 ? 663  GLN A O   1 
ATOM   5463  C  CB  . GLN A 1 663  ? 54.325 93.122  -36.806 1.00 20.89 ? 663  GLN A CB  1 
ATOM   5464  C  CG  . GLN A 1 663  ? 55.123 94.044  -35.898 1.00 24.61 ? 663  GLN A CG  1 
ATOM   5465  C  CD  . GLN A 1 663  ? 56.279 93.272  -35.240 1.00 28.13 ? 663  GLN A CD  1 
ATOM   5466  O  OE1 . GLN A 1 663  ? 57.183 92.808  -35.938 1.00 28.41 ? 663  GLN A OE1 1 
ATOM   5467  N  NE2 . GLN A 1 663  ? 56.220 93.095  -33.917 1.00 30.57 ? 663  GLN A NE2 1 
ATOM   5468  N  N   . TYR A 1 664  ? 51.097 91.670  -36.896 1.00 18.52 ? 664  TYR A N   1 
ATOM   5469  C  CA  . TYR A 1 664  ? 50.404 90.471  -37.376 1.00 17.39 ? 664  TYR A CA  1 
ATOM   5470  C  C   . TYR A 1 664  ? 49.984 90.654  -38.829 1.00 17.69 ? 664  TYR A C   1 
ATOM   5471  O  O   . TYR A 1 664  ? 49.319 91.647  -39.146 1.00 19.02 ? 664  TYR A O   1 
ATOM   5472  C  CB  . TYR A 1 664  ? 49.190 90.200  -36.497 1.00 15.86 ? 664  TYR A CB  1 
ATOM   5473  C  CG  . TYR A 1 664  ? 48.593 88.828  -36.732 1.00 13.93 ? 664  TYR A CG  1 
ATOM   5474  C  CD1 . TYR A 1 664  ? 49.173 87.688  -36.170 1.00 12.98 ? 664  TYR A CD1 1 
ATOM   5475  C  CD2 . TYR A 1 664  ? 47.436 88.677  -37.483 1.00 13.23 ? 664  TYR A CD2 1 
ATOM   5476  C  CE1 . TYR A 1 664  ? 48.641 86.436  -36.394 1.00 12.24 ? 664  TYR A CE1 1 
ATOM   5477  C  CE2 . TYR A 1 664  ? 46.891 87.405  -37.728 1.00 12.14 ? 664  TYR A CE2 1 
ATOM   5478  C  CZ  . TYR A 1 664  ? 47.495 86.290  -37.149 1.00 11.71 ? 664  TYR A CZ  1 
ATOM   5479  O  OH  . TYR A 1 664  ? 46.906 85.067  -37.359 1.00 13.42 ? 664  TYR A OH  1 
ATOM   5480  N  N   . PRO A 1 665  ? 50.391 89.760  -39.732 1.00 18.66 ? 665  PRO A N   1 
ATOM   5481  C  CA  . PRO A 1 665  ? 50.233 90.033  -41.175 1.00 19.40 ? 665  PRO A CA  1 
ATOM   5482  C  C   . PRO A 1 665  ? 48.835 89.983  -41.793 1.00 20.31 ? 665  PRO A C   1 
ATOM   5483  O  O   . PRO A 1 665  ? 48.684 90.440  -42.930 1.00 21.59 ? 665  PRO A O   1 
ATOM   5484  C  CB  . PRO A 1 665  ? 51.162 89.014  -41.844 1.00 19.51 ? 665  PRO A CB  1 
ATOM   5485  C  CG  . PRO A 1 665  ? 51.309 87.919  -40.845 1.00 19.35 ? 665  PRO A CG  1 
ATOM   5486  C  CD  . PRO A 1 665  ? 51.133 88.512  -39.482 1.00 17.95 ? 665  PRO A CD  1 
ATOM   5487  N  N   . GLU A 1 666  ? 47.844 89.429  -41.094 1.00 20.27 ? 666  GLU A N   1 
ATOM   5488  C  CA  . GLU A 1 666  ? 46.490 89.309  -41.647 1.00 19.29 ? 666  GLU A CA  1 
ATOM   5489  C  C   . GLU A 1 666  ? 45.580 90.239  -40.878 1.00 18.56 ? 666  GLU A C   1 
ATOM   5490  O  O   . GLU A 1 666  ? 45.549 90.194  -39.648 1.00 18.27 ? 666  GLU A O   1 
ATOM   5491  C  CB  . GLU A 1 666  ? 45.963 87.877  -41.502 1.00 20.81 ? 666  GLU A CB  1 
ATOM   5492  C  CG  . GLU A 1 666  ? 46.674 86.849  -42.361 1.00 25.49 ? 666  GLU A CG  1 
ATOM   5493  C  CD  . GLU A 1 666  ? 46.624 87.203  -43.832 1.00 30.37 ? 666  GLU A CD  1 
ATOM   5494  O  OE1 . GLU A 1 666  ? 45.508 87.412  -44.354 1.00 33.57 ? 666  GLU A OE1 1 
ATOM   5495  O  OE2 . GLU A 1 666  ? 47.703 87.290  -44.459 1.00 34.35 ? 666  GLU A OE2 1 
ATOM   5496  N  N   . ASP A 1 667  ? 44.826 91.075  -41.597 1.00 16.26 ? 667  ASP A N   1 
ATOM   5497  C  CA  . ASP A 1 667  ? 43.873 91.964  -40.943 1.00 15.78 ? 667  ASP A CA  1 
ATOM   5498  C  C   . ASP A 1 667  ? 42.637 91.177  -40.460 1.00 12.73 ? 667  ASP A C   1 
ATOM   5499  O  O   . ASP A 1 667  ? 42.123 90.338  -41.193 1.00 12.51 ? 667  ASP A O   1 
ATOM   5500  C  CB  . ASP A 1 667  ? 43.360 93.013  -41.938 1.00 17.51 ? 667  ASP A CB  1 
ATOM   5501  C  CG  . ASP A 1 667  ? 44.405 94.033  -42.304 1.00 21.79 ? 667  ASP A CG  1 
ATOM   5502  O  OD1 . ASP A 1 667  ? 45.296 94.314  -41.463 1.00 26.40 ? 667  ASP A OD1 1 
ATOM   5503  O  OD2 . ASP A 1 667  ? 44.375 94.649  -43.395 1.00 26.87 ? 667  ASP A OD2 1 
ATOM   5504  N  N   . VAL A 1 668  ? 42.147 91.511  -39.282 1.00 11.54 ? 668  VAL A N   1 
ATOM   5505  C  CA  . VAL A 1 668  ? 40.872 90.941  -38.768 1.00 11.35 ? 668  VAL A CA  1 
ATOM   5506  C  C   . VAL A 1 668  ? 39.739 91.344  -39.688 1.00 11.73 ? 668  VAL A C   1 
ATOM   5507  O  O   . VAL A 1 668  ? 39.676 92.513  -40.144 1.00 12.43 ? 668  VAL A O   1 
ATOM   5508  C  CB  . VAL A 1 668  ? 40.549 91.376  -37.337 1.00 12.18 ? 668  VAL A CB  1 
ATOM   5509  C  CG1 . VAL A 1 668  ? 39.211 90.797  -36.850 1.00 11.77 ? 668  VAL A CG1 1 
ATOM   5510  C  CG2 . VAL A 1 668  ? 41.679 90.936  -36.405 1.00 13.33 ? 668  VAL A CG2 1 
ATOM   5511  N  N   . LYS A 1 669  ? 38.894 90.372  -39.997 1.00 9.88  ? 669  LYS A N   1 
ATOM   5512  C  CA  . LYS A 1 669  ? 37.648 90.563  -40.758 1.00 11.58 ? 669  LYS A CA  1 
ATOM   5513  C  C   . LYS A 1 669  ? 36.440 90.635  -39.836 1.00 11.39 ? 669  LYS A C   1 
ATOM   5514  O  O   . LYS A 1 669  ? 36.455 90.075  -38.721 1.00 11.01 ? 669  LYS A O   1 
ATOM   5515  C  CB  . LYS A 1 669  ? 37.458 89.419  -41.755 1.00 13.05 ? 669  LYS A CB  1 
ATOM   5516  C  CG  . LYS A 1 669  ? 38.200 89.575  -43.067 1.00 19.73 ? 669  LYS A CG  1 
ATOM   5517  C  CD  . LYS A 1 669  ? 39.686 89.358  -42.974 1.00 26.92 ? 669  LYS A CD  1 
ATOM   5518  C  CE  . LYS A 1 669  ? 40.395 90.061  -44.141 1.00 28.93 ? 669  LYS A CE  1 
ATOM   5519  N  NZ  . LYS A 1 669  ? 41.802 90.423  -43.772 1.00 31.05 ? 669  LYS A NZ  1 
ATOM   5520  N  N   . PHE A 1 670  ? 35.389 91.300  -40.304 1.00 10.74 ? 670  PHE A N   1 
ATOM   5521  C  CA  . PHE A 1 670  ? 34.170 91.521  -39.521 1.00 11.56 ? 670  PHE A CA  1 
ATOM   5522  C  C   . PHE A 1 670  ? 32.940 91.095  -40.281 1.00 13.17 ? 670  PHE A C   1 
ATOM   5523  O  O   . PHE A 1 670  ? 32.946 91.071  -41.493 1.00 13.28 ? 670  PHE A O   1 
ATOM   5524  C  CB  . PHE A 1 670  ? 34.028 92.991  -39.085 1.00 12.13 ? 670  PHE A CB  1 
ATOM   5525  C  CG  . PHE A 1 670  ? 35.196 93.476  -38.317 1.00 12.09 ? 670  PHE A CG  1 
ATOM   5526  C  CD1 . PHE A 1 670  ? 36.307 94.005  -38.983 1.00 14.09 ? 670  PHE A CD1 1 
ATOM   5527  C  CD2 . PHE A 1 670  ? 35.231 93.345  -36.925 1.00 15.64 ? 670  PHE A CD2 1 
ATOM   5528  C  CE1 . PHE A 1 670  ? 37.427 94.421  -38.275 1.00 14.50 ? 670  PHE A CE1 1 
ATOM   5529  C  CE2 . PHE A 1 670  ? 36.343 93.764  -36.212 1.00 16.30 ? 670  PHE A CE2 1 
ATOM   5530  C  CZ  . PHE A 1 670  ? 37.438 94.296  -36.888 1.00 14.85 ? 670  PHE A CZ  1 
ATOM   5531  N  N   . GLY A 1 671  ? 31.883 90.744  -39.559 1.00 13.15 ? 671  GLY A N   1 
ATOM   5532  C  CA  . GLY A 1 671  ? 30.646 90.317  -40.189 1.00 13.27 ? 671  GLY A CA  1 
ATOM   5533  C  C   . GLY A 1 671  ? 29.532 90.331  -39.166 1.00 13.53 ? 671  GLY A C   1 
ATOM   5534  O  O   . GLY A 1 671  ? 29.784 90.335  -37.959 1.00 12.11 ? 671  GLY A O   1 
ATOM   5535  N  N   . ASP A 1 672  ? 28.286 90.378  -39.633 1.00 14.29 ? 672  ASP A N   1 
ATOM   5536  C  CA  . ASP A 1 672  ? 27.161 90.174  -38.739 1.00 15.61 ? 672  ASP A CA  1 
ATOM   5537  C  C   . ASP A 1 672  ? 27.156 88.693  -38.330 1.00 15.12 ? 672  ASP A C   1 
ATOM   5538  O  O   . ASP A 1 672  ? 27.622 87.851  -39.090 1.00 14.37 ? 672  ASP A O   1 
ATOM   5539  C  CB  . ASP A 1 672  ? 25.849 90.454  -39.471 1.00 17.02 ? 672  ASP A CB  1 
ATOM   5540  C  CG  . ASP A 1 672  ? 25.562 91.937  -39.636 1.00 20.80 ? 672  ASP A CG  1 
ATOM   5541  O  OD1 . ASP A 1 672  ? 26.252 92.772  -39.026 1.00 24.20 ? 672  ASP A OD1 1 
ATOM   5542  O  OD2 . ASP A 1 672  ? 24.623 92.350  -40.370 1.00 27.67 ? 672  ASP A OD2 1 
ATOM   5543  N  N   . PRO A 1 673  ? 26.586 88.391  -37.155 1.00 15.15 ? 673  PRO A N   1 
ATOM   5544  C  CA  . PRO A 1 673  ? 26.442 86.997  -36.720 1.00 15.41 ? 673  PRO A CA  1 
ATOM   5545  C  C   . PRO A 1 673  ? 25.844 86.117  -37.815 1.00 15.20 ? 673  PRO A C   1 
ATOM   5546  O  O   . PRO A 1 673  ? 24.914 86.512  -38.526 1.00 14.88 ? 673  PRO A O   1 
ATOM   5547  C  CB  . PRO A 1 673  ? 25.495 87.111  -35.537 1.00 15.77 ? 673  PRO A CB  1 
ATOM   5548  C  CG  . PRO A 1 673  ? 25.778 88.452  -34.963 1.00 17.12 ? 673  PRO A CG  1 
ATOM   5549  C  CD  . PRO A 1 673  ? 26.043 89.334  -36.159 1.00 15.75 ? 673  PRO A CD  1 
ATOM   5550  N  N   . ARG A 1 674  ? 26.392 84.923  -37.961 1.00 13.86 ? 674  ARG A N   1 
ATOM   5551  C  CA  . ARG A 1 674  ? 25.952 83.991  -38.990 1.00 14.62 ? 674  ARG A CA  1 
ATOM   5552  C  C   . ARG A 1 674  ? 26.403 82.585  -38.627 1.00 13.96 ? 674  ARG A C   1 
ATOM   5553  O  O   . ARG A 1 674  ? 27.352 82.413  -37.867 1.00 14.28 ? 674  ARG A O   1 
ATOM   5554  C  CB  . ARG A 1 674  ? 26.518 84.388  -40.363 1.00 14.32 ? 674  ARG A CB  1 
ATOM   5555  C  CG  . ARG A 1 674  ? 28.012 84.317  -40.547 1.00 15.71 ? 674  ARG A CG  1 
ATOM   5556  C  CD  . ARG A 1 674  ? 28.351 84.442  -42.049 1.00 16.63 ? 674  ARG A CD  1 
ATOM   5557  N  NE  . ARG A 1 674  ? 29.714 84.111  -42.435 1.00 19.91 ? 674  ARG A NE  1 
ATOM   5558  C  CZ  . ARG A 1 674  ? 30.697 84.989  -42.577 1.00 21.04 ? 674  ARG A CZ  1 
ATOM   5559  N  NH1 . ARG A 1 674  ? 30.494 86.289  -42.331 1.00 22.91 ? 674  ARG A NH1 1 
ATOM   5560  N  NH2 . ARG A 1 674  ? 31.901 84.561  -42.966 1.00 22.21 ? 674  ARG A NH2 1 
ATOM   5561  N  N   . GLU A 1 675  ? 25.723 81.589  -39.165 1.00 13.86 ? 675  GLU A N   1 
ATOM   5562  C  CA  . GLU A 1 675  ? 26.188 80.217  -39.040 1.00 14.04 ? 675  GLU A CA  1 
ATOM   5563  C  C   . GLU A 1 675  ? 27.509 80.041  -39.760 1.00 14.73 ? 675  GLU A C   1 
ATOM   5564  O  O   . GLU A 1 675  ? 27.767 80.664  -40.801 1.00 16.43 ? 675  GLU A O   1 
ATOM   5565  C  CB  . GLU A 1 675  ? 25.114 79.241  -39.533 1.00 15.17 ? 675  GLU A CB  1 
ATOM   5566  C  CG  . GLU A 1 675  ? 23.858 79.379  -38.707 1.00 18.36 ? 675  GLU A CG  1 
ATOM   5567  C  CD  . GLU A 1 675  ? 23.068 78.092  -38.626 1.00 26.48 ? 675  GLU A CD  1 
ATOM   5568  O  OE1 . GLU A 1 675  ? 23.271 77.215  -39.519 1.00 28.59 ? 675  GLU A OE1 1 
ATOM   5569  O  OE2 . GLU A 1 675  ? 22.265 77.951  -37.655 1.00 29.23 ? 675  GLU A OE2 1 
ATOM   5570  N  N   . ILE A 1 676  ? 28.391 79.229  -39.197 1.00 14.87 ? 676  ILE A N   1 
ATOM   5571  C  CA  . ILE A 1 676  ? 29.662 78.973  -39.851 1.00 15.41 ? 676  ILE A CA  1 
ATOM   5572  C  C   . ILE A 1 676  ? 30.066 77.511  -39.729 1.00 14.98 ? 676  ILE A C   1 
ATOM   5573  O  O   . ILE A 1 676  ? 29.594 76.796  -38.840 1.00 15.00 ? 676  ILE A O   1 
ATOM   5574  C  CB  . ILE A 1 676  ? 30.796 79.830  -39.286 1.00 17.40 ? 676  ILE A CB  1 
ATOM   5575  C  CG1 . ILE A 1 676  ? 30.953 79.590  -37.807 1.00 17.05 ? 676  ILE A CG1 1 
ATOM   5576  C  CG2 . ILE A 1 676  ? 30.670 81.363  -39.649 1.00 20.28 ? 676  ILE A CG2 1 
ATOM   5577  C  CD1 . ILE A 1 676  ? 32.383 79.668  -37.359 1.00 22.72 ? 676  ILE A CD1 1 
ATOM   5578  N  N   . SER A 1 677  ? 30.950 77.091  -40.619 1.00 13.83 ? 677  SER A N   1 
ATOM   5579  C  CA  A SER A 1 677  ? 31.476 75.734  -40.649 0.50 14.67 ? 677  SER A CA  1 
ATOM   5580  C  CA  B SER A 1 677  ? 31.500 75.749  -40.553 0.50 14.55 ? 677  SER A CA  1 
ATOM   5581  C  C   . SER A 1 677  ? 32.995 75.778  -40.690 1.00 14.23 ? 677  SER A C   1 
ATOM   5582  O  O   . SER A 1 677  ? 33.560 76.639  -41.354 1.00 14.97 ? 677  SER A O   1 
ATOM   5583  C  CB  A SER A 1 677  ? 30.944 75.003  -41.890 0.50 14.87 ? 677  SER A CB  1 
ATOM   5584  C  CB  B SER A 1 677  ? 30.892 74.842  -41.619 0.50 14.49 ? 677  SER A CB  1 
ATOM   5585  O  OG  A SER A 1 677  ? 31.292 73.635  -41.871 0.50 17.95 ? 677  SER A OG  1 
ATOM   5586  O  OG  B SER A 1 677  ? 29.511 74.683  -41.391 0.50 17.61 ? 677  SER A OG  1 
ATOM   5587  N  N   . LEU A 1 678  ? 33.652 74.829  -40.029 1.00 13.07 ? 678  LEU A N   1 
ATOM   5588  C  CA  . LEU A 1 678  ? 35.092 74.752  -40.044 1.00 12.73 ? 678  LEU A CA  1 
ATOM   5589  C  C   . LEU A 1 678  ? 35.535 73.306  -40.145 1.00 12.85 ? 678  LEU A C   1 
ATOM   5590  O  O   . LEU A 1 678  ? 34.861 72.425  -39.601 1.00 12.33 ? 678  LEU A O   1 
ATOM   5591  C  CB  . LEU A 1 678  ? 35.643 75.284  -38.729 1.00 13.41 ? 678  LEU A CB  1 
ATOM   5592  C  CG  . LEU A 1 678  ? 35.690 76.778  -38.467 1.00 13.49 ? 678  LEU A CG  1 
ATOM   5593  C  CD1 . LEU A 1 678  ? 35.983 76.982  -36.995 1.00 16.36 ? 678  LEU A CD1 1 
ATOM   5594  C  CD2 . LEU A 1 678  ? 36.805 77.413  -39.297 1.00 17.83 ? 678  LEU A CD2 1 
ATOM   5595  N  N   . ARG A 1 679  ? 36.656 73.087  -40.812 1.00 12.82 ? 679  ARG A N   1 
ATOM   5596  C  CA  . ARG A 1 679  ? 37.293 71.777  -40.858 1.00 14.99 ? 679  ARG A CA  1 
ATOM   5597  C  C   . ARG A 1 679  ? 38.799 71.967  -40.798 1.00 14.74 ? 679  ARG A C   1 
ATOM   5598  O  O   . ARG A 1 679  ? 39.357 72.766  -41.566 1.00 15.02 ? 679  ARG A O   1 
ATOM   5599  C  CB  . ARG A 1 679  ? 36.899 71.029  -42.143 1.00 15.30 ? 679  ARG A CB  1 
ATOM   5600  C  CG  . ARG A 1 679  ? 37.533 69.649  -42.243 1.00 17.09 ? 679  ARG A CG  1 
ATOM   5601  C  CD  . ARG A 1 679  ? 37.276 68.943  -43.581 1.00 18.80 ? 679  ARG A CD  1 
ATOM   5602  N  NE  . ARG A 1 679  ? 37.444 67.505  -43.377 1.00 27.26 ? 679  ARG A NE  1 
ATOM   5603  C  CZ  . ARG A 1 679  ? 37.692 66.602  -44.319 1.00 30.10 ? 679  ARG A CZ  1 
ATOM   5604  N  NH1 . ARG A 1 679  ? 37.827 66.952  -45.588 1.00 32.81 ? 679  ARG A NH1 1 
ATOM   5605  N  NH2 . ARG A 1 679  ? 37.814 65.329  -43.972 1.00 31.84 ? 679  ARG A NH2 1 
ATOM   5606  N  N   . VAL A 1 680  ? 39.459 71.276  -39.876 1.00 13.51 ? 680  VAL A N   1 
ATOM   5607  C  CA  . VAL A 1 680  ? 40.915 71.278  -39.799 1.00 14.18 ? 680  VAL A CA  1 
ATOM   5608  C  C   . VAL A 1 680  ? 41.430 69.926  -40.239 1.00 16.12 ? 680  VAL A C   1 
ATOM   5609  O  O   . VAL A 1 680  ? 40.892 68.900  -39.821 1.00 15.63 ? 680  VAL A O   1 
ATOM   5610  C  CB  . VAL A 1 680  ? 41.426 71.576  -38.372 1.00 13.18 ? 680  VAL A CB  1 
ATOM   5611  C  CG1 . VAL A 1 680  ? 42.921 71.383  -38.282 1.00 14.15 ? 680  VAL A CG1 1 
ATOM   5612  C  CG2 . VAL A 1 680  ? 41.043 73.032  -37.967 1.00 12.27 ? 680  VAL A CG2 1 
ATOM   5613  N  N   . GLY A 1 681  ? 42.461 69.955  -41.078 1.00 17.58 ? 681  GLY A N   1 
ATOM   5614  C  CA  . GLY A 1 681  ? 43.048 68.735  -41.624 1.00 20.05 ? 681  GLY A CA  1 
ATOM   5615  C  C   . GLY A 1 681  ? 41.990 67.946  -42.378 1.00 21.54 ? 681  GLY A C   1 
ATOM   5616  O  O   . GLY A 1 681  ? 41.123 68.522  -43.059 1.00 21.97 ? 681  GLY A O   1 
ATOM   5617  N  N   . ASN A 1 682  ? 42.055 66.628  -42.257 1.00 24.27 ? 682  ASN A N   1 
ATOM   5618  C  CA  . ASN A 1 682  ? 41.013 65.791  -42.852 1.00 25.85 ? 682  ASN A CA  1 
ATOM   5619  C  C   . ASN A 1 682  ? 40.089 65.315  -41.730 1.00 25.43 ? 682  ASN A C   1 
ATOM   5620  O  O   . ASN A 1 682  ? 39.425 64.280  -41.833 1.00 26.95 ? 682  ASN A O   1 
ATOM   5621  C  CB  . ASN A 1 682  ? 41.615 64.646  -43.678 1.00 27.27 ? 682  ASN A CB  1 
ATOM   5622  C  CG  . ASN A 1 682  ? 42.616 63.817  -42.888 1.00 30.49 ? 682  ASN A CG  1 
ATOM   5623  O  OD1 . ASN A 1 682  ? 42.485 63.658  -41.671 1.00 34.95 ? 682  ASN A OD1 1 
ATOM   5624  N  ND2 . ASN A 1 682  ? 43.626 63.283  -43.579 1.00 34.25 ? 682  ASN A ND2 1 
ATOM   5625  N  N   . GLY A 1 683  ? 40.042 66.110  -40.662 1.00 24.18 ? 683  GLY A N   1 
ATOM   5626  C  CA  . GLY A 1 683  ? 39.296 65.776  -39.465 1.00 21.91 ? 683  GLY A CA  1 
ATOM   5627  C  C   . GLY A 1 683  ? 37.828 66.068  -39.652 1.00 19.91 ? 683  GLY A C   1 
ATOM   5628  O  O   . GLY A 1 683  ? 37.393 66.261  -40.783 1.00 20.21 ? 683  GLY A O   1 
ATOM   5629  N  N   . PRO A 1 684  ? 37.054 66.133  -38.566 1.00 17.40 ? 684  PRO A N   1 
ATOM   5630  C  CA  . PRO A 1 684  ? 35.613 66.390  -38.709 1.00 15.85 ? 684  PRO A CA  1 
ATOM   5631  C  C   . PRO A 1 684  ? 35.316 67.825  -39.164 1.00 14.37 ? 684  PRO A C   1 
ATOM   5632  O  O   . PRO A 1 684  ? 36.151 68.703  -38.964 1.00 13.92 ? 684  PRO A O   1 
ATOM   5633  C  CB  . PRO A 1 684  ? 35.057 66.147  -37.301 1.00 15.70 ? 684  PRO A CB  1 
ATOM   5634  C  CG  . PRO A 1 684  ? 36.261 66.322  -36.365 1.00 17.09 ? 684  PRO A CG  1 
ATOM   5635  C  CD  . PRO A 1 684  ? 37.457 65.979  -37.156 1.00 17.74 ? 684  PRO A CD  1 
ATOM   5636  N  N   . THR A 1 685  ? 34.152 68.019  -39.758 1.00 13.02 ? 685  THR A N   1 
ATOM   5637  C  CA  . THR A 1 685  ? 33.646 69.349  -40.062 1.00 12.46 ? 685  THR A CA  1 
ATOM   5638  C  C   . THR A 1 685  ? 32.619 69.661  -38.995 1.00 12.18 ? 685  THR A C   1 
ATOM   5639  O  O   . THR A 1 685  ? 31.675 68.897  -38.799 1.00 12.26 ? 685  THR A O   1 
ATOM   5640  C  CB  . THR A 1 685  ? 32.991 69.344  -41.443 1.00 13.31 ? 685  THR A CB  1 
ATOM   5641  O  OG1 . THR A 1 685  ? 33.999 69.084  -42.422 1.00 15.66 ? 685  THR A OG1 1 
ATOM   5642  C  CG2 . THR A 1 685  ? 32.485 70.739  -41.778 1.00 15.45 ? 685  THR A CG2 1 
ATOM   5643  N  N   . LEU A 1 686  ? 32.775 70.819  -38.355 1.00 10.50 ? 686  LEU A N   1 
ATOM   5644  C  CA  . LEU A 1 686  ? 31.884 71.260  -37.305 1.00 11.09 ? 686  LEU A CA  1 
ATOM   5645  C  C   . LEU A 1 686  ? 31.111 72.470  -37.796 1.00 10.55 ? 686  LEU A C   1 
ATOM   5646  O  O   . LEU A 1 686  ? 31.702 73.391  -38.400 1.00 11.36 ? 686  LEU A O   1 
ATOM   5647  C  CB  . LEU A 1 686  ? 32.689 71.679  -36.072 1.00 11.11 ? 686  LEU A CB  1 
ATOM   5648  C  CG  . LEU A 1 686  ? 33.559 70.661  -35.339 1.00 16.50 ? 686  LEU A CG  1 
ATOM   5649  C  CD1 . LEU A 1 686  ? 33.675 71.094  -33.865 1.00 15.88 ? 686  LEU A CD1 1 
ATOM   5650  C  CD2 . LEU A 1 686  ? 33.157 69.230  -35.484 1.00 16.65 ? 686  LEU A CD2 1 
ATOM   5651  N  N   . ALA A 1 687  ? 29.826 72.474  -37.492 1.00 10.41 ? 687  ALA A N   1 
ATOM   5652  C  CA  . ALA A 1 687  ? 28.960 73.595  -37.841 1.00 10.45 ? 687  ALA A CA  1 
ATOM   5653  C  C   . ALA A 1 687  ? 28.517 74.284  -36.573 1.00 10.98 ? 687  ALA A C   1 
ATOM   5654  O  O   . ALA A 1 687  ? 28.250 73.619  -35.567 1.00 10.04 ? 687  ALA A O   1 
ATOM   5655  C  CB  . ALA A 1 687  ? 27.756 73.127  -38.657 1.00 11.29 ? 687  ALA A CB  1 
ATOM   5656  N  N   . PHE A 1 688  ? 28.464 75.616  -36.607 1.00 9.61  ? 688  PHE A N   1 
ATOM   5657  C  CA  . PHE A 1 688  ? 28.129 76.410  -35.429 1.00 9.46  ? 688  PHE A CA  1 
ATOM   5658  C  C   . PHE A 1 688  ? 26.945 77.300  -35.703 1.00 10.48 ? 688  PHE A C   1 
ATOM   5659  O  O   . PHE A 1 688  ? 26.780 77.804  -36.823 1.00 11.36 ? 688  PHE A O   1 
ATOM   5660  C  CB  . PHE A 1 688  ? 29.321 77.281  -35.010 1.00 9.68  ? 688  PHE A CB  1 
ATOM   5661  C  CG  . PHE A 1 688  ? 30.536 76.491  -34.667 1.00 8.23  ? 688  PHE A CG  1 
ATOM   5662  C  CD1 . PHE A 1 688  ? 31.380 76.020  -35.640 1.00 8.89  ? 688  PHE A CD1 1 
ATOM   5663  C  CD2 . PHE A 1 688  ? 30.834 76.213  -33.343 1.00 9.60  ? 688  PHE A CD2 1 
ATOM   5664  C  CE1 . PHE A 1 688  ? 32.498 75.262  -35.322 1.00 9.18  ? 688  PHE A CE1 1 
ATOM   5665  C  CE2 . PHE A 1 688  ? 31.952 75.481  -33.038 1.00 8.74  ? 688  PHE A CE2 1 
ATOM   5666  C  CZ  . PHE A 1 688  ? 32.770 74.993  -34.004 1.00 9.19  ? 688  PHE A CZ  1 
ATOM   5667  N  N   . SER A 1 689  ? 26.145 77.539  -34.689 1.00 10.74 ? 689  SER A N   1 
ATOM   5668  C  CA  . SER A 1 689  ? 25.035 78.495  -34.787 1.00 11.49 ? 689  SER A CA  1 
ATOM   5669  C  C   . SER A 1 689  ? 25.563 79.933  -34.817 1.00 11.37 ? 689  SER A C   1 
ATOM   5670  O  O   . SER A 1 689  ? 26.738 80.209  -34.552 1.00 10.53 ? 689  SER A O   1 
ATOM   5671  C  CB  . SER A 1 689  ? 24.113 78.347  -33.598 1.00 11.78 ? 689  SER A CB  1 
ATOM   5672  O  OG  . SER A 1 689  ? 24.713 78.907  -32.442 1.00 12.08 ? 689  SER A OG  1 
ATOM   5673  N  N   . GLU A 1 690  ? 24.671 80.862  -35.126 1.00 12.55 ? 690  GLU A N   1 
ATOM   5674  C  CA  . GLU A 1 690  ? 25.049 82.268  -35.076 1.00 13.07 ? 690  GLU A CA  1 
ATOM   5675  C  C   . GLU A 1 690  ? 25.455 82.777  -33.692 1.00 13.12 ? 690  GLU A C   1 
ATOM   5676  O  O   . GLU A 1 690  ? 26.058 83.845  -33.588 1.00 13.28 ? 690  GLU A O   1 
ATOM   5677  C  CB  . GLU A 1 690  ? 23.954 83.143  -35.687 1.00 14.26 ? 690  GLU A CB  1 
ATOM   5678  C  CG  . GLU A 1 690  ? 22.800 83.491  -34.785 1.00 19.14 ? 690  GLU A CG  1 
ATOM   5679  C  CD  . GLU A 1 690  ? 21.943 84.556  -35.445 1.00 25.51 ? 690  GLU A CD  1 
ATOM   5680  O  OE1 . GLU A 1 690  ? 21.408 84.275  -36.545 1.00 28.67 ? 690  GLU A OE1 1 
ATOM   5681  O  OE2 . GLU A 1 690  ? 21.834 85.673  -34.888 1.00 30.29 ? 690  GLU A OE2 1 
ATOM   5682  N  N   . GLN A 1 691  ? 25.117 82.006  -32.642 1.00 13.21 ? 691  GLN A N   1 
ATOM   5683  C  CA  . GLN A 1 691  ? 25.594 82.311  -31.287 1.00 12.99 ? 691  GLN A CA  1 
ATOM   5684  C  C   . GLN A 1 691  ? 26.925 81.653  -30.934 1.00 12.36 ? 691  GLN A C   1 
ATOM   5685  O  O   . GLN A 1 691  ? 27.358 81.728  -29.788 1.00 13.77 ? 691  GLN A O   1 
ATOM   5686  C  CB  . GLN A 1 691  ? 24.556 81.948  -30.236 1.00 14.56 ? 691  GLN A CB  1 
ATOM   5687  C  CG  . GLN A 1 691  ? 23.337 82.789  -30.323 1.00 19.33 ? 691  GLN A CG  1 
ATOM   5688  C  CD  . GLN A 1 691  ? 22.187 81.917  -30.460 1.00 26.26 ? 691  GLN A CD  1 
ATOM   5689  O  OE1 . GLN A 1 691  ? 21.519 81.614  -29.470 1.00 27.37 ? 691  GLN A OE1 1 
ATOM   5690  N  NE2 . GLN A 1 691  ? 21.973 81.413  -31.678 1.00 26.44 ? 691  GLN A NE2 1 
ATOM   5691  N  N   . GLY A 1 692  ? 27.566 81.026  -31.909 1.00 11.17 ? 692  GLY A N   1 
ATOM   5692  C  CA  . GLY A 1 692  ? 28.906 80.477  -31.721 1.00 11.76 ? 692  GLY A CA  1 
ATOM   5693  C  C   . GLY A 1 692  ? 28.907 79.120  -31.050 1.00 11.00 ? 692  GLY A C   1 
ATOM   5694  O  O   . GLY A 1 692  ? 29.941 78.703  -30.565 1.00 11.95 ? 692  GLY A O   1 
ATOM   5695  N  N   . LEU A 1 693  ? 27.769 78.445  -30.995 1.00 10.94 ? 693  LEU A N   1 
ATOM   5696  C  CA  . LEU A 1 693  ? 27.667 77.152  -30.300 1.00 10.86 ? 693  LEU A CA  1 
ATOM   5697  C  C   . LEU A 1 693  ? 27.542 76.033  -31.310 1.00 10.15 ? 693  LEU A C   1 
ATOM   5698  O  O   . LEU A 1 693  ? 26.817 76.154  -32.312 1.00 10.05 ? 693  LEU A O   1 
ATOM   5699  C  CB  . LEU A 1 693  ? 26.445 77.152  -29.386 1.00 11.67 ? 693  LEU A CB  1 
ATOM   5700  C  CG  . LEU A 1 693  ? 26.522 78.137  -28.213 1.00 14.59 ? 693  LEU A CG  1 
ATOM   5701  C  CD1 . LEU A 1 693  ? 25.117 78.525  -27.785 1.00 18.67 ? 693  LEU A CD1 1 
ATOM   5702  C  CD2 . LEU A 1 693  ? 27.263 77.496  -27.066 1.00 17.22 ? 693  LEU A CD2 1 
ATOM   5703  N  N   . LEU A 1 694  ? 28.241 74.937  -31.060 1.00 9.09  ? 694  LEU A N   1 
ATOM   5704  C  CA  . LEU A 1 694  ? 28.173 73.777  -31.932 1.00 9.31  ? 694  LEU A CA  1 
ATOM   5705  C  C   . LEU A 1 694  ? 26.730 73.369  -32.207 1.00 9.17  ? 694  LEU A C   1 
ATOM   5706  O  O   . LEU A 1 694  ? 25.885 73.361  -31.310 1.00 9.34  ? 694  LEU A O   1 
ATOM   5707  C  CB  . LEU A 1 694  ? 28.896 72.590  -31.278 1.00 10.07 ? 694  LEU A CB  1 
ATOM   5708  C  CG  . LEU A 1 694  ? 29.120 71.376  -32.171 1.00 11.08 ? 694  LEU A CG  1 
ATOM   5709  C  CD1 . LEU A 1 694  ? 30.074 71.698  -33.268 1.00 11.75 ? 694  LEU A CD1 1 
ATOM   5710  C  CD2 . LEU A 1 694  ? 29.633 70.224  -31.309 1.00 12.34 ? 694  LEU A CD2 1 
ATOM   5711  N  N   . LYS A 1 695  ? 26.460 73.055  -33.477 1.00 9.84  ? 695  LYS A N   1 
ATOM   5712  C  CA  . LYS A 1 695  ? 25.178 72.482  -33.850 1.00 11.72 ? 695  LYS A CA  1 
ATOM   5713  C  C   . LYS A 1 695  ? 25.294 71.127  -34.539 1.00 11.23 ? 695  LYS A C   1 
ATOM   5714  O  O   . LYS A 1 695  ? 24.334 70.368  -34.478 1.00 12.78 ? 695  LYS A O   1 
ATOM   5715  C  CB  . LYS A 1 695  ? 24.348 73.459  -34.688 1.00 13.61 ? 695  LYS A CB  1 
ATOM   5716  C  CG  . LYS A 1 695  ? 24.996 73.931  -35.933 1.00 16.94 ? 695  LYS A CG  1 
ATOM   5717  C  CD  . LYS A 1 695  ? 24.075 74.940  -36.655 1.00 21.80 ? 695  LYS A CD  1 
ATOM   5718  C  CE  . LYS A 1 695  ? 22.809 74.267  -37.133 1.00 26.95 ? 695  LYS A CE  1 
ATOM   5719  N  NZ  . LYS A 1 695  ? 22.086 75.125  -38.129 1.00 29.58 ? 695  LYS A NZ  1 
ATOM   5720  N  N   . SER A 1 696  ? 26.417 70.810  -35.159 1.00 10.54 ? 696  SER A N   1 
ATOM   5721  C  CA  . SER A 1 696  ? 26.551 69.528  -35.862 1.00 11.03 ? 696  SER A CA  1 
ATOM   5722  C  C   . SER A 1 696  ? 27.995 69.154  -36.092 1.00 11.09 ? 696  SER A C   1 
ATOM   5723  O  O   . SER A 1 696  ? 28.883 70.024  -36.141 1.00 11.20 ? 696  SER A O   1 
ATOM   5724  C  CB  . SER A 1 696  ? 25.755 69.512  -37.188 1.00 12.63 ? 696  SER A CB  1 
ATOM   5725  O  OG  . SER A 1 696  ? 26.448 70.272  -38.159 1.00 15.53 ? 696  SER A OG  1 
ATOM   5726  N  N   . ILE A 1 697  ? 28.234 67.840  -36.248 1.00 10.87 ? 697  ILE A N   1 
ATOM   5727  C  CA  . ILE A 1 697  ? 29.538 67.281  -36.547 1.00 11.63 ? 697  ILE A CA  1 
ATOM   5728  C  C   . ILE A 1 697  ? 29.414 66.333  -37.721 1.00 12.33 ? 697  ILE A C   1 
ATOM   5729  O  O   . ILE A 1 697  ? 28.551 65.454  -37.694 1.00 13.43 ? 697  ILE A O   1 
ATOM   5730  C  CB  . ILE A 1 697  ? 30.113 66.490  -35.337 1.00 11.18 ? 697  ILE A CB  1 
ATOM   5731  C  CG1 . ILE A 1 697  ? 30.214 67.411  -34.113 1.00 10.74 ? 697  ILE A CG1 1 
ATOM   5732  C  CG2 . ILE A 1 697  ? 31.472 65.872  -35.719 1.00 12.63 ? 697  ILE A CG2 1 
ATOM   5733  C  CD1 . ILE A 1 697  ? 30.647 66.687  -32.831 1.00 12.48 ? 697  ILE A CD1 1 
ATOM   5734  N  N   . GLN A 1 698  ? 30.278 66.505  -38.709 1.00 12.29 ? 698  GLN A N   1 
ATOM   5735  C  CA  . GLN A 1 698  ? 30.322 65.599  -39.844 1.00 13.66 ? 698  GLN A CA  1 
ATOM   5736  C  C   . GLN A 1 698  ? 31.668 64.914  -39.814 1.00 14.16 ? 698  GLN A C   1 
ATOM   5737  O  O   . GLN A 1 698  ? 32.696 65.559  -39.985 1.00 14.59 ? 698  GLN A O   1 
ATOM   5738  C  CB  . GLN A 1 698  ? 30.144 66.395  -41.139 1.00 14.22 ? 698  GLN A CB  1 
ATOM   5739  C  CG  . GLN A 1 698  ? 30.138 65.478  -42.361 1.00 18.10 ? 698  GLN A CG  1 
ATOM   5740  C  CD  . GLN A 1 698  ? 30.295 66.245  -43.651 1.00 19.93 ? 698  GLN A CD  1 
ATOM   5741  O  OE1 . GLN A 1 698  ? 31.192 67.074  -43.780 1.00 22.57 ? 698  GLN A OE1 1 
ATOM   5742  N  NE2 . GLN A 1 698  ? 29.430 65.954  -44.618 1.00 24.07 ? 698  GLN A NE2 1 
ATOM   5743  N  N   . LEU A 1 699  ? 31.685 63.601  -39.565 1.00 16.41 ? 699  LEU A N   1 
ATOM   5744  C  CA  . LEU A 1 699  ? 32.957 62.916  -39.357 1.00 18.95 ? 699  LEU A CA  1 
ATOM   5745  C  C   . LEU A 1 699  ? 33.869 62.832  -40.591 1.00 21.30 ? 699  LEU A C   1 
ATOM   5746  O  O   . LEU A 1 699  ? 35.089 62.984  -40.466 1.00 22.74 ? 699  LEU A O   1 
ATOM   5747  C  CB  . LEU A 1 699  ? 32.729 61.528  -38.729 1.00 18.96 ? 699  LEU A CB  1 
ATOM   5748  C  CG  . LEU A 1 699  ? 32.056 61.510  -37.349 1.00 18.58 ? 699  LEU A CG  1 
ATOM   5749  C  CD1 . LEU A 1 699  ? 31.825 60.054  -36.891 1.00 21.47 ? 699  LEU A CD1 1 
ATOM   5750  C  CD2 . LEU A 1 699  ? 32.868 62.310  -36.321 1.00 17.56 ? 699  LEU A CD2 1 
ATOM   5751  N  N   . THR A 1 700  ? 33.278 62.615  -41.766 1.00 24.07 ? 700  THR A N   1 
ATOM   5752  C  CA  . THR A 1 700  ? 34.039 62.491  -43.017 1.00 27.30 ? 700  THR A CA  1 
ATOM   5753  C  C   . THR A 1 700  ? 33.311 63.225  -44.146 1.00 28.78 ? 700  THR A C   1 
ATOM   5754  O  O   . THR A 1 700  ? 32.138 63.543  -44.012 1.00 28.63 ? 700  THR A O   1 
ATOM   5755  C  CB  . THR A 1 700  ? 34.246 60.991  -43.403 1.00 27.35 ? 700  THR A CB  1 
ATOM   5756  O  OG1 . THR A 1 700  ? 32.973 60.342  -43.522 1.00 28.92 ? 700  THR A OG1 1 
ATOM   5757  C  CG2 . THR A 1 700  ? 34.963 60.199  -42.289 1.00 28.48 ? 700  THR A CG2 1 
ATOM   5758  N  N   . GLN A 1 701  ? 34.007 63.469  -45.260 1.00 31.20 ? 701  GLN A N   1 
ATOM   5759  C  CA  . GLN A 1 701  ? 33.474 64.258  -46.387 1.00 33.59 ? 701  GLN A CA  1 
ATOM   5760  C  C   . GLN A 1 701  ? 32.087 63.808  -46.867 1.00 34.32 ? 701  GLN A C   1 
ATOM   5761  O  O   . GLN A 1 701  ? 31.213 64.642  -47.137 1.00 35.32 ? 701  GLN A O   1 
ATOM   5762  C  CB  . GLN A 1 701  ? 34.452 64.239  -47.580 1.00 34.26 ? 701  GLN A CB  1 
ATOM   5763  C  CG  . GLN A 1 701  ? 35.668 65.148  -47.446 1.00 36.52 ? 701  GLN A CG  1 
ATOM   5764  C  CD  . GLN A 1 701  ? 35.391 66.605  -47.830 1.00 40.04 ? 701  GLN A CD  1 
ATOM   5765  O  OE1 . GLN A 1 701  ? 35.849 67.530  -47.150 1.00 40.42 ? 701  GLN A OE1 1 
ATOM   5766  N  NE2 . GLN A 1 701  ? 34.643 66.810  -48.915 1.00 41.02 ? 701  GLN A NE2 1 
ATOM   5767  N  N   . ASP A 1 702  ? 31.897 62.496  -46.968 1.00 34.85 ? 702  ASP A N   1 
ATOM   5768  C  CA  . ASP A 1 702  ? 30.670 61.921  -47.513 1.00 35.61 ? 702  ASP A CA  1 
ATOM   5769  C  C   . ASP A 1 702  ? 29.637 61.543  -46.442 1.00 35.07 ? 702  ASP A C   1 
ATOM   5770  O  O   . ASP A 1 702  ? 28.548 61.068  -46.770 1.00 35.70 ? 702  ASP A O   1 
ATOM   5771  C  CB  . ASP A 1 702  ? 31.018 60.673  -48.323 1.00 36.38 ? 702  ASP A CB  1 
ATOM   5772  C  CG  . ASP A 1 702  ? 31.605 59.578  -47.454 1.00 38.33 ? 702  ASP A CG  1 
ATOM   5773  O  OD1 . ASP A 1 702  ? 32.834 59.608  -47.205 1.00 40.92 ? 702  ASP A OD1 1 
ATOM   5774  O  OD2 . ASP A 1 702  ? 30.907 58.663  -46.952 1.00 41.04 ? 702  ASP A OD2 1 
ATOM   5775  N  N   . SER A 1 703  ? 29.978 61.745  -45.167 1.00 33.82 ? 703  SER A N   1 
ATOM   5776  C  CA  . SER A 1 703  ? 29.101 61.337  -44.068 1.00 31.94 ? 703  SER A CA  1 
ATOM   5777  C  C   . SER A 1 703  ? 28.066 62.417  -43.717 1.00 30.15 ? 703  SER A C   1 
ATOM   5778  O  O   . SER A 1 703  ? 28.203 63.561  -44.148 1.00 30.43 ? 703  SER A O   1 
ATOM   5779  C  CB  . SER A 1 703  ? 29.929 60.943  -42.840 1.00 31.99 ? 703  SER A CB  1 
ATOM   5780  O  OG  . SER A 1 703  ? 30.633 62.054  -42.312 1.00 32.45 ? 703  SER A OG  1 
ATOM   5781  N  N   . PRO A 1 704  ? 27.034 62.062  -42.947 1.00 28.84 ? 704  PRO A N   1 
ATOM   5782  C  CA  . PRO A 1 704  ? 25.993 63.021  -42.559 1.00 27.29 ? 704  PRO A CA  1 
ATOM   5783  C  C   . PRO A 1 704  ? 26.452 64.048  -41.512 1.00 25.59 ? 704  PRO A C   1 
ATOM   5784  O  O   . PRO A 1 704  ? 27.388 63.794  -40.745 1.00 25.23 ? 704  PRO A O   1 
ATOM   5785  C  CB  . PRO A 1 704  ? 24.897 62.131  -41.955 1.00 28.08 ? 704  PRO A CB  1 
ATOM   5786  C  CG  . PRO A 1 704  ? 25.284 60.738  -42.278 1.00 28.21 ? 704  PRO A CG  1 
ATOM   5787  C  CD  . PRO A 1 704  ? 26.774 60.724  -42.386 1.00 29.07 ? 704  PRO A CD  1 
ATOM   5788  N  N   . HIS A 1 705  ? 25.791 65.204  -41.505 1.00 23.91 ? 705  HIS A N   1 
ATOM   5789  C  CA  . HIS A 1 705  ? 25.963 66.194  -40.441 1.00 22.78 ? 705  HIS A CA  1 
ATOM   5790  C  C   . HIS A 1 705  ? 25.098 65.787  -39.256 1.00 21.19 ? 705  HIS A C   1 
ATOM   5791  O  O   . HIS A 1 705  ? 23.900 66.007  -39.237 1.00 22.18 ? 705  HIS A O   1 
ATOM   5792  C  CB  . HIS A 1 705  ? 25.609 67.596  -40.961 1.00 23.38 ? 705  HIS A CB  1 
ATOM   5793  C  CG  . HIS A 1 705  ? 26.492 68.039  -42.084 1.00 25.57 ? 705  HIS A CG  1 
ATOM   5794  N  ND1 . HIS A 1 705  ? 27.624 68.802  -41.890 1.00 26.34 ? 705  HIS A ND1 1 
ATOM   5795  C  CD2 . HIS A 1 705  ? 26.435 67.781  -43.414 1.00 27.42 ? 705  HIS A CD2 1 
ATOM   5796  C  CE1 . HIS A 1 705  ? 28.224 69.001  -43.051 1.00 27.42 ? 705  HIS A CE1 1 
ATOM   5797  N  NE2 . HIS A 1 705  ? 27.522 68.393  -43.992 1.00 27.84 ? 705  HIS A NE2 1 
ATOM   5798  N  N   . VAL A 1 706  ? 25.738 65.186  -38.249 1.00 18.18 ? 706  VAL A N   1 
ATOM   5799  C  CA  . VAL A 1 706  ? 25.044 64.677  -37.074 1.00 15.84 ? 706  VAL A CA  1 
ATOM   5800  C  C   . VAL A 1 706  ? 24.746 65.808  -36.094 1.00 14.86 ? 706  VAL A C   1 
ATOM   5801  O  O   . VAL A 1 706  ? 25.679 66.485  -35.668 1.00 13.23 ? 706  VAL A O   1 
ATOM   5802  C  CB  . VAL A 1 706  ? 25.955 63.648  -36.350 1.00 15.53 ? 706  VAL A CB  1 
ATOM   5803  C  CG1 . VAL A 1 706  ? 25.257 63.082  -35.129 1.00 14.89 ? 706  VAL A CG1 1 
ATOM   5804  C  CG2 . VAL A 1 706  ? 26.422 62.532  -37.314 1.00 15.72 ? 706  VAL A CG2 1 
ATOM   5805  N  N   . PRO A 1 707  ? 23.483 66.044  -35.737 1.00 14.20 ? 707  PRO A N   1 
ATOM   5806  C  CA  . PRO A 1 707  ? 23.132 67.083  -34.763 1.00 14.07 ? 707  PRO A CA  1 
ATOM   5807  C  C   . PRO A 1 707  ? 23.780 66.832  -33.401 1.00 13.50 ? 707  PRO A C   1 
ATOM   5808  O  O   . PRO A 1 707  ? 23.628 65.782  -32.790 1.00 13.44 ? 707  PRO A O   1 
ATOM   5809  C  CB  . PRO A 1 707  ? 21.603 66.986  -34.652 1.00 14.59 ? 707  PRO A CB  1 
ATOM   5810  C  CG  . PRO A 1 707  ? 21.166 66.281  -35.877 1.00 16.22 ? 707  PRO A CG  1 
ATOM   5811  C  CD  . PRO A 1 707  ? 22.277 65.372  -36.279 1.00 14.36 ? 707  PRO A CD  1 
ATOM   5812  N  N   . VAL A 1 708  ? 24.548 67.810  -32.957 1.00 12.56 ? 708  VAL A N   1 
ATOM   5813  C  CA  . VAL A 1 708  ? 25.152 67.818  -31.638 1.00 11.49 ? 708  VAL A CA  1 
ATOM   5814  C  C   . VAL A 1 708  ? 25.133 69.285  -31.220 1.00 11.21 ? 708  VAL A C   1 
ATOM   5815  O  O   . VAL A 1 708  ? 25.849 70.090  -31.775 1.00 11.81 ? 708  VAL A O   1 
ATOM   5816  C  CB  . VAL A 1 708  ? 26.617 67.303  -31.678 1.00 11.28 ? 708  VAL A CB  1 
ATOM   5817  C  CG1 . VAL A 1 708  ? 27.224 67.294  -30.279 1.00 11.77 ? 708  VAL A CG1 1 
ATOM   5818  C  CG2 . VAL A 1 708  ? 26.698 65.892  -32.307 1.00 12.41 ? 708  VAL A CG2 1 
ATOM   5819  N  N   A HIS A 1 709  ? 24.233 69.634  -30.314 0.50 10.17 ? 709  HIS A N   1 
ATOM   5820  N  N   B HIS A 1 709  ? 24.195 69.646  -30.368 0.50 10.62 ? 709  HIS A N   1 
ATOM   5821  C  CA  A HIS A 1 709  ? 23.920 71.034  -29.985 0.50 10.38 ? 709  HIS A CA  1 
ATOM   5822  C  CA  B HIS A 1 709  ? 24.054 71.048  -30.004 0.50 11.19 ? 709  HIS A CA  1 
ATOM   5823  C  C   A HIS A 1 709  ? 24.326 71.409  -28.556 0.50 10.31 ? 709  HIS A C   1 
ATOM   5824  C  C   B HIS A 1 709  ? 24.507 71.270  -28.581 0.50 10.78 ? 709  HIS A C   1 
ATOM   5825  O  O   A HIS A 1 709  ? 23.735 70.882  -27.605 0.50 10.46 ? 709  HIS A O   1 
ATOM   5826  O  O   B HIS A 1 709  ? 24.165 70.507  -27.683 0.50 10.58 ? 709  HIS A O   1 
ATOM   5827  C  CB  A HIS A 1 709  ? 22.421 71.258  -30.137 0.50 10.41 ? 709  HIS A CB  1 
ATOM   5828  C  CB  B HIS A 1 709  ? 22.629 71.548  -30.198 0.50 11.64 ? 709  HIS A CB  1 
ATOM   5829  C  CG  A HIS A 1 709  ? 21.972 71.409  -31.555 0.50 11.53 ? 709  HIS A CG  1 
ATOM   5830  C  CG  B HIS A 1 709  ? 22.469 73.025  -29.965 0.50 14.42 ? 709  HIS A CG  1 
ATOM   5831  N  ND1 A HIS A 1 709  ? 21.825 70.336  -32.406 0.50 15.74 ? 709  HIS A ND1 1 
ATOM   5832  N  ND1 B HIS A 1 709  ? 23.336 73.964  -30.489 0.50 17.18 ? 709  HIS A ND1 1 
ATOM   5833  C  CD2 A HIS A 1 709  ? 21.665 72.509  -32.279 0.50 14.16 ? 709  HIS A CD2 1 
ATOM   5834  C  CD2 B HIS A 1 709  ? 21.536 73.723  -29.275 0.50 18.42 ? 709  HIS A CD2 1 
ATOM   5835  C  CE1 A HIS A 1 709  ? 21.438 70.769  -33.592 0.50 13.11 ? 709  HIS A CE1 1 
ATOM   5836  C  CE1 B HIS A 1 709  ? 22.955 75.171  -30.117 0.50 18.45 ? 709  HIS A CE1 1 
ATOM   5837  N  NE2 A HIS A 1 709  ? 21.320 72.082  -33.538 0.50 17.06 ? 709  HIS A NE2 1 
ATOM   5838  N  NE2 B HIS A 1 709  ? 21.862 75.054  -29.385 0.50 18.63 ? 709  HIS A NE2 1 
ATOM   5839  N  N   . PHE A 1 710  ? 25.316 72.307  -28.405 1.00 9.63  ? 710  PHE A N   1 
ATOM   5840  C  CA  . PHE A 1 710  ? 25.686 72.798  -27.077 1.00 10.13 ? 710  PHE A CA  1 
ATOM   5841  C  C   . PHE A 1 710  ? 24.684 73.864  -26.643 1.00 11.04 ? 710  PHE A C   1 
ATOM   5842  O  O   . PHE A 1 710  ? 24.275 74.740  -27.448 1.00 10.78 ? 710  PHE A O   1 
ATOM   5843  C  CB  . PHE A 1 710  ? 27.092 73.418  -27.035 1.00 10.45 ? 710  PHE A CB  1 
ATOM   5844  C  CG  . PHE A 1 710  ? 28.198 72.467  -26.658 1.00 12.13 ? 710  PHE A CG  1 
ATOM   5845  C  CD1 . PHE A 1 710  ? 28.191 71.824  -25.428 1.00 15.52 ? 710  PHE A CD1 1 
ATOM   5846  C  CD2 . PHE A 1 710  ? 29.300 72.296  -27.479 1.00 17.07 ? 710  PHE A CD2 1 
ATOM   5847  C  CE1 . PHE A 1 710  ? 29.209 70.956  -25.049 1.00 18.03 ? 710  PHE A CE1 1 
ATOM   5848  C  CE2 . PHE A 1 710  ? 30.333 71.413  -27.087 1.00 15.25 ? 710  PHE A CE2 1 
ATOM   5849  C  CZ  . PHE A 1 710  ? 30.284 70.778  -25.870 1.00 14.90 ? 710  PHE A CZ  1 
ATOM   5850  N  N   . LYS A 1 711  ? 24.294 73.826  -25.383 1.00 9.77  ? 711  LYS A N   1 
ATOM   5851  C  CA  . LYS A 1 711  ? 23.368 74.797  -24.794 1.00 11.96 ? 711  LYS A CA  1 
ATOM   5852  C  C   . LYS A 1 711  ? 23.797 75.039  -23.371 1.00 10.70 ? 711  LYS A C   1 
ATOM   5853  O  O   . LYS A 1 711  ? 24.232 74.099  -22.703 1.00 11.52 ? 711  LYS A O   1 
ATOM   5854  C  CB  . LYS A 1 711  ? 21.937 74.227  -24.821 1.00 12.82 ? 711  LYS A CB  1 
ATOM   5855  C  CG  . LYS A 1 711  ? 20.824 75.188  -24.406 1.00 15.73 ? 711  LYS A CG  1 
ATOM   5856  C  CD  . LYS A 1 711  ? 19.441 74.538  -24.550 1.00 17.42 ? 711  LYS A CD  1 
ATOM   5857  C  CE  . LYS A 1 711  ? 18.911 74.668  -25.984 1.00 21.12 ? 711  LYS A CE  1 
ATOM   5858  N  NZ  . LYS A 1 711  ? 17.734 73.774  -26.193 1.00 24.70 ? 711  LYS A NZ  1 
ATOM   5859  N  N   . PHE A 1 712  ? 23.680 76.265  -22.887 1.00 8.54  ? 712  PHE A N   1 
ATOM   5860  C  CA  . PHE A 1 712  ? 23.876 76.589  -21.484 1.00 8.72  ? 712  PHE A CA  1 
ATOM   5861  C  C   . PHE A 1 712  ? 22.566 76.895  -20.794 1.00 8.62  ? 712  PHE A C   1 
ATOM   5862  O  O   . PHE A 1 712  ? 21.733 77.612  -21.344 1.00 8.95  ? 712  PHE A O   1 
ATOM   5863  C  CB  . PHE A 1 712  ? 24.872 77.756  -21.334 1.00 9.48  ? 712  PHE A CB  1 
ATOM   5864  C  CG  . PHE A 1 712  ? 26.281 77.356  -21.638 1.00 8.68  ? 712  PHE A CG  1 
ATOM   5865  C  CD1 . PHE A 1 712  ? 26.751 77.381  -22.950 1.00 9.59  ? 712  PHE A CD1 1 
ATOM   5866  C  CD2 . PHE A 1 712  ? 27.130 76.878  -20.635 1.00 9.20  ? 712  PHE A CD2 1 
ATOM   5867  C  CE1 . PHE A 1 712  ? 28.048 76.972  -23.255 1.00 9.73  ? 712  PHE A CE1 1 
ATOM   5868  C  CE2 . PHE A 1 712  ? 28.400 76.458  -20.937 1.00 9.53  ? 712  PHE A CE2 1 
ATOM   5869  C  CZ  . PHE A 1 712  ? 28.873 76.508  -22.240 1.00 8.71  ? 712  PHE A CZ  1 
ATOM   5870  N  N   . LEU A 1 713  ? 22.354 76.308  -19.627 1.00 8.24  ? 713  LEU A N   1 
ATOM   5871  C  CA  . LEU A 1 713  ? 21.135 76.516  -18.846 1.00 8.42  ? 713  LEU A CA  1 
ATOM   5872  C  C   . LEU A 1 713  ? 21.463 76.814  -17.404 1.00 8.93  ? 713  LEU A C   1 
ATOM   5873  O  O   . LEU A 1 713  ? 22.635 76.717  -16.993 1.00 9.34  ? 713  LEU A O   1 
ATOM   5874  C  CB  . LEU A 1 713  ? 20.194 75.292  -18.940 1.00 8.76  ? 713  LEU A CB  1 
ATOM   5875  C  CG  . LEU A 1 713  ? 19.880 74.849  -20.373 1.00 9.62  ? 713  LEU A CG  1 
ATOM   5876  C  CD1 . LEU A 1 713  ? 20.727 73.657  -20.784 1.00 11.99 ? 713  LEU A CD1 1 
ATOM   5877  C  CD2 . LEU A 1 713  ? 18.404 74.415  -20.474 1.00 11.98 ? 713  LEU A CD2 1 
ATOM   5878  N  N   . LYS A 1 714  ? 20.467 77.171  -16.621 1.00 9.84  ? 714  LYS A N   1 
ATOM   5879  C  CA  . LYS A 1 714  ? 20.690 77.451  -15.219 1.00 12.00 ? 714  LYS A CA  1 
ATOM   5880  C  C   . LYS A 1 714  ? 19.631 76.769  -14.398 1.00 10.70 ? 714  LYS A C   1 
ATOM   5881  O  O   . LYS A 1 714  ? 18.446 76.730  -14.780 1.00 11.28 ? 714  LYS A O   1 
ATOM   5882  C  CB  . LYS A 1 714  ? 20.708 78.950  -14.884 1.00 14.85 ? 714  LYS A CB  1 
ATOM   5883  C  CG  . LYS A 1 714  ? 19.634 79.760  -15.488 1.00 19.26 ? 714  LYS A CG  1 
ATOM   5884  C  CD  . LYS A 1 714  ? 19.779 81.242  -15.073 1.00 18.76 ? 714  LYS A CD  1 
ATOM   5885  C  CE  . LYS A 1 714  ? 21.123 81.842  -15.506 1.00 25.51 ? 714  LYS A CE  1 
ATOM   5886  N  NZ  . LYS A 1 714  ? 21.233 83.316  -15.225 1.00 26.48 ? 714  LYS A NZ  1 
ATOM   5887  N  N   . TYR A 1 715  ? 20.074 76.208  -13.277 1.00 8.09  ? 715  TYR A N   1 
ATOM   5888  C  CA  . TYR A 1 715  ? 19.197 75.756  -12.234 1.00 8.16  ? 715  TYR A CA  1 
ATOM   5889  C  C   . TYR A 1 715  ? 19.145 76.798  -11.125 1.00 9.54  ? 715  TYR A C   1 
ATOM   5890  O  O   . TYR A 1 715  ? 20.132 77.501  -10.900 1.00 10.28 ? 715  TYR A O   1 
ATOM   5891  C  CB  . TYR A 1 715  ? 19.751 74.462  -11.620 1.00 8.51  ? 715  TYR A CB  1 
ATOM   5892  C  CG  . TYR A 1 715  ? 19.681 73.240  -12.489 1.00 8.31  ? 715  TYR A CG  1 
ATOM   5893  C  CD1 . TYR A 1 715  ? 18.501 72.515  -12.575 1.00 6.22  ? 715  TYR A CD1 1 
ATOM   5894  C  CD2 . TYR A 1 715  ? 20.811 72.767  -13.191 1.00 8.58  ? 715  TYR A CD2 1 
ATOM   5895  C  CE1 . TYR A 1 715  ? 18.430 71.356  -13.337 1.00 8.09  ? 715  TYR A CE1 1 
ATOM   5896  C  CE2 . TYR A 1 715  ? 20.736 71.622  -13.966 1.00 7.66  ? 715  TYR A CE2 1 
ATOM   5897  C  CZ  . TYR A 1 715  ? 19.544 70.907  -14.042 1.00 7.56  ? 715  TYR A CZ  1 
ATOM   5898  O  OH  . TYR A 1 715  ? 19.481 69.732  -14.790 1.00 7.57  ? 715  TYR A OH  1 
ATOM   5899  N  N   . GLY A 1 716  ? 18.041 76.835  -10.401 1.00 9.60  ? 716  GLY A N   1 
ATOM   5900  C  CA  . GLY A 1 716  ? 17.892 77.738  -9.293  1.00 9.99  ? 716  GLY A CA  1 
ATOM   5901  C  C   . GLY A 1 716  ? 17.723 76.962  -8.005  1.00 10.33 ? 716  GLY A C   1 
ATOM   5902  O  O   . GLY A 1 716  ? 18.054 75.786  -7.922  1.00 11.19 ? 716  GLY A O   1 
ATOM   5903  N  N   . VAL A 1 717  ? 17.232 77.648  -6.991  1.00 10.94 ? 717  VAL A N   1 
ATOM   5904  C  CA  . VAL A 1 717  ? 17.103 77.104  -5.648  1.00 12.51 ? 717  VAL A CA  1 
ATOM   5905  C  C   . VAL A 1 717  ? 15.632 77.204  -5.250  1.00 13.54 ? 717  VAL A C   1 
ATOM   5906  O  O   . VAL A 1 717  ? 14.922 78.080  -5.742  1.00 15.12 ? 717  VAL A O   1 
ATOM   5907  C  CB  . VAL A 1 717  ? 18.060 77.902  -4.704  1.00 12.91 ? 717  VAL A CB  1 
ATOM   5908  C  CG1 . VAL A 1 717  ? 17.844 77.622  -3.232  1.00 16.84 ? 717  VAL A CG1 1 
ATOM   5909  C  CG2 . VAL A 1 717  ? 19.502 77.602  -5.072  1.00 12.30 ? 717  VAL A CG2 1 
ATOM   5910  N  N   . ARG A 1 718  ? 15.179 76.333  -4.361  1.00 12.90 ? 718  ARG A N   1 
ATOM   5911  C  CA  . ARG A 1 718  ? 13.787 76.335  -3.900  1.00 14.88 ? 718  ARG A CA  1 
ATOM   5912  C  C   . ARG A 1 718  ? 13.504 77.486  -2.961  1.00 16.90 ? 718  ARG A C   1 
ATOM   5913  O  O   . ARG A 1 718  ? 14.292 77.803  -2.081  1.00 17.85 ? 718  ARG A O   1 
ATOM   5914  C  CB  . ARG A 1 718  ? 13.461 75.005  -3.212  1.00 14.37 ? 718  ARG A CB  1 
ATOM   5915  C  CG  . ARG A 1 718  ? 13.527 73.862  -4.169  1.00 14.23 ? 718  ARG A CG  1 
ATOM   5916  C  CD  . ARG A 1 718  ? 13.540 72.508  -3.510  1.00 13.75 ? 718  ARG A CD  1 
ATOM   5917  N  NE  . ARG A 1 718  ? 13.812 71.495  -4.515  1.00 13.96 ? 718  ARG A NE  1 
ATOM   5918  C  CZ  . ARG A 1 718  ? 13.788 70.190  -4.281  1.00 13.16 ? 718  ARG A CZ  1 
ATOM   5919  N  NH1 . ARG A 1 718  ? 13.474 69.733  -3.067  1.00 13.35 ? 718  ARG A NH1 1 
ATOM   5920  N  NH2 . ARG A 1 718  ? 14.085 69.359  -5.265  1.00 14.28 ? 718  ARG A NH2 1 
ATOM   5921  N  N   . SER A 1 719  ? 12.342 78.106  -3.144  1.00 19.49 ? 719  SER A N   1 
ATOM   5922  C  CA  . SER A 1 719  ? 11.962 79.209  -2.274  1.00 21.84 ? 719  SER A CA  1 
ATOM   5923  C  C   . SER A 1 719  ? 11.264 78.668  -1.029  1.00 23.36 ? 719  SER A C   1 
ATOM   5924  O  O   . SER A 1 719  ? 11.174 79.355  -0.019  1.00 24.58 ? 719  SER A O   1 
ATOM   5925  C  CB  . SER A 1 719  ? 11.086 80.206  -3.037  1.00 21.94 ? 719  SER A CB  1 
ATOM   5926  O  OG  . SER A 1 719  ? 9.865  79.613  -3.409  1.00 25.00 ? 719  SER A OG  1 
ATOM   5927  N  N   . HIS A 1 720  ? 10.765 77.434  -1.113  1.00 24.54 ? 720  HIS A N   1 
ATOM   5928  C  CA  . HIS A 1 720  ? 10.182 76.741  0.031   1.00 25.69 ? 720  HIS A CA  1 
ATOM   5929  C  C   . HIS A 1 720  ? 10.917 75.424  0.239   1.00 24.71 ? 720  HIS A C   1 
ATOM   5930  O  O   . HIS A 1 720  ? 11.361 74.793  -0.725  1.00 25.31 ? 720  HIS A O   1 
ATOM   5931  C  CB  . HIS A 1 720  ? 8.697  76.451  -0.210  1.00 27.19 ? 720  HIS A CB  1 
ATOM   5932  C  CG  . HIS A 1 720  ? 7.941  77.613  -0.770  1.00 31.20 ? 720  HIS A CG  1 
ATOM   5933  N  ND1 . HIS A 1 720  ? 7.577  78.702  -0.007  1.00 35.48 ? 720  HIS A ND1 1 
ATOM   5934  C  CD2 . HIS A 1 720  ? 7.492  77.861  -2.024  1.00 34.92 ? 720  HIS A CD2 1 
ATOM   5935  C  CE1 . HIS A 1 720  ? 6.926  79.566  -0.765  1.00 36.19 ? 720  HIS A CE1 1 
ATOM   5936  N  NE2 . HIS A 1 720  ? 6.865  79.083  -1.993  1.00 37.04 ? 720  HIS A NE2 1 
ATOM   5937  N  N   . GLY A 1 721  ? 11.028 74.997  1.489   1.00 23.41 ? 721  GLY A N   1 
ATOM   5938  C  CA  . GLY A 1 721  ? 11.682 73.729  1.765   1.00 21.54 ? 721  GLY A CA  1 
ATOM   5939  C  C   . GLY A 1 721  ? 13.188 73.837  1.607   1.00 20.14 ? 721  GLY A C   1 
ATOM   5940  O  O   . GLY A 1 721  ? 13.763 74.929  1.616   1.00 20.67 ? 721  GLY A O   1 
ATOM   5941  N  N   . ASP A 1 722  ? 13.822 72.689  1.430   1.00 17.33 ? 722  ASP A N   1 
ATOM   5942  C  CA  . ASP A 1 722  ? 15.259 72.604  1.621   1.00 14.43 ? 722  ASP A CA  1 
ATOM   5943  C  C   . ASP A 1 722  ? 16.033 73.329  0.532   1.00 12.44 ? 722  ASP A C   1 
ATOM   5944  O  O   . ASP A 1 722  ? 15.706 73.268  -0.635  1.00 12.27 ? 722  ASP A O   1 
ATOM   5945  C  CB  . ASP A 1 722  ? 15.703 71.150  1.748   1.00 14.10 ? 722  ASP A CB  1 
ATOM   5946  C  CG  . ASP A 1 722  ? 15.070 70.427  2.940   1.00 14.61 ? 722  ASP A CG  1 
ATOM   5947  O  OD1 . ASP A 1 722  ? 14.848 71.073  4.014   1.00 17.27 ? 722  ASP A OD1 1 
ATOM   5948  O  OD2 . ASP A 1 722  ? 14.807 69.207  2.875   1.00 16.37 ? 722  ASP A OD2 1 
ATOM   5949  N  N   . ARG A 1 723  ? 17.108 73.979  0.949   1.00 12.25 ? 723  ARG A N   1 
ATOM   5950  C  CA  . ARG A 1 723  ? 17.931 74.745  0.028   1.00 12.46 ? 723  ARG A CA  1 
ATOM   5951  C  C   . ARG A 1 723  ? 19.221 74.015  -0.355  1.00 11.28 ? 723  ARG A C   1 
ATOM   5952  O  O   . ARG A 1 723  ? 19.827 73.337  0.491   1.00 11.16 ? 723  ARG A O   1 
ATOM   5953  C  CB  . ARG A 1 723  ? 18.281 76.069  0.678   1.00 14.00 ? 723  ARG A CB  1 
ATOM   5954  C  CG  . ARG A 1 723  ? 17.012 76.849  1.001   1.00 18.12 ? 723  ARG A CG  1 
ATOM   5955  C  CD  . ARG A 1 723  ? 17.183 78.321  1.160   1.00 26.65 ? 723  ARG A CD  1 
ATOM   5956  N  NE  . ARG A 1 723  ? 15.888 79.001  1.121   1.00 31.73 ? 723  ARG A NE  1 
ATOM   5957  C  CZ  . ARG A 1 723  ? 15.599 80.085  1.828   1.00 34.81 ? 723  ARG A CZ  1 
ATOM   5958  N  NH1 . ARG A 1 723  ? 16.501 80.605  2.654   1.00 36.56 ? 723  ARG A NH1 1 
ATOM   5959  N  NH2 . ARG A 1 723  ? 14.400 80.640  1.724   1.00 34.82 ? 723  ARG A NH2 1 
ATOM   5960  N  N   . SER A 1 724  ? 19.582 74.137  -1.636  1.00 10.21 ? 724  SER A N   1 
ATOM   5961  C  CA  . SER A 1 724  ? 20.879 73.709  -2.122  1.00 10.18 ? 724  SER A CA  1 
ATOM   5962  C  C   . SER A 1 724  ? 21.988 74.410  -1.352  1.00 9.48  ? 724  SER A C   1 
ATOM   5963  O  O   . SER A 1 724  ? 21.858 75.582  -0.967  1.00 11.03 ? 724  SER A O   1 
ATOM   5964  C  CB  . SER A 1 724  ? 21.031 74.047  -3.594  1.00 10.16 ? 724  SER A CB  1 
ATOM   5965  O  OG  . SER A 1 724  ? 19.993 73.393  -4.330  1.00 9.80  ? 724  SER A OG  1 
ATOM   5966  N  N   . GLY A 1 725  ? 23.099 73.708  -1.167  1.00 8.42  ? 725  GLY A N   1 
ATOM   5967  C  CA  . GLY A 1 725  ? 24.283 74.280  -0.552  1.00 8.31  ? 725  GLY A CA  1 
ATOM   5968  C  C   . GLY A 1 725  ? 25.483 73.531  -1.088  1.00 7.59  ? 725  GLY A C   1 
ATOM   5969  O  O   . GLY A 1 725  ? 25.403 72.868  -2.131  1.00 8.22  ? 725  GLY A O   1 
ATOM   5970  N  N   . ALA A 1 726  ? 26.607 73.614  -0.382  1.00 6.60  ? 726  ALA A N   1 
ATOM   5971  C  CA  . ALA A 1 726  ? 27.823 72.980  -0.860  1.00 7.10  ? 726  ALA A CA  1 
ATOM   5972  C  C   . ALA A 1 726  ? 27.680 71.486  -1.073  1.00 6.12  ? 726  ALA A C   1 
ATOM   5973  O  O   . ALA A 1 726  ? 28.343 70.908  -1.940  1.00 5.82  ? 726  ALA A O   1 
ATOM   5974  C  CB  . ALA A 1 726  ? 28.970 73.252  0.071   1.00 7.48  ? 726  ALA A CB  1 
ATOM   5975  N  N   . TYR A 1 727  ? 26.842 70.829  -0.277  1.00 6.22  ? 727  TYR A N   1 
ATOM   5976  C  CA  . TYR A 1 727  ? 26.643 69.370  -0.417  1.00 5.92  ? 727  TYR A CA  1 
ATOM   5977  C  C   . TYR A 1 727  ? 25.490 68.977  -1.298  1.00 6.42  ? 727  TYR A C   1 
ATOM   5978  O  O   . TYR A 1 727  ? 25.615 68.073  -2.136  1.00 6.37  ? 727  TYR A O   1 
ATOM   5979  C  CB  . TYR A 1 727  ? 26.379 68.719  0.943   1.00 6.16  ? 727  TYR A CB  1 
ATOM   5980  C  CG  . TYR A 1 727  ? 27.427 68.958  2.005   1.00 5.81  ? 727  TYR A CG  1 
ATOM   5981  C  CD1 . TYR A 1 727  ? 27.400 70.117  2.769   1.00 7.73  ? 727  TYR A CD1 1 
ATOM   5982  C  CD2 . TYR A 1 727  ? 28.403 67.996  2.288   1.00 8.82  ? 727  TYR A CD2 1 
ATOM   5983  C  CE1 . TYR A 1 727  ? 28.345 70.349  3.763   1.00 7.98  ? 727  TYR A CE1 1 
ATOM   5984  C  CE2 . TYR A 1 727  ? 29.350 68.219  3.293   1.00 8.29  ? 727  TYR A CE2 1 
ATOM   5985  C  CZ  . TYR A 1 727  ? 29.305 69.373  4.015   1.00 7.39  ? 727  TYR A CZ  1 
ATOM   5986  O  OH  . TYR A 1 727  ? 30.208 69.591  5.041   1.00 9.29  ? 727  TYR A OH  1 
ATOM   5987  N  N   . LEU A 1 728  ? 24.333 69.591  -1.029  1.00 6.51  ? 728  LEU A N   1 
ATOM   5988  C  CA  . LEU A 1 728  ? 23.064 69.144  -1.635  1.00 6.71  ? 728  LEU A CA  1 
ATOM   5989  C  C   . LEU A 1 728  ? 22.711 69.918  -2.883  1.00 6.48  ? 728  LEU A C   1 
ATOM   5990  O  O   . LEU A 1 728  ? 22.910 71.132  -2.961  1.00 7.96  ? 728  LEU A O   1 
ATOM   5991  C  CB  . LEU A 1 728  ? 21.928 69.408  -0.650  1.00 8.15  ? 728  LEU A CB  1 
ATOM   5992  C  CG  . LEU A 1 728  ? 22.080 68.799  0.734   1.00 7.48  ? 728  LEU A CG  1 
ATOM   5993  C  CD1 . LEU A 1 728  ? 20.779 69.039  1.484   1.00 10.11 ? 728  LEU A CD1 1 
ATOM   5994  C  CD2 . LEU A 1 728  ? 22.413 67.297  0.646   1.00 8.36  ? 728  LEU A CD2 1 
ATOM   5995  N  N   . PHE A 1 729  ? 22.167 69.211  -3.871  1.00 6.94  ? 729  PHE A N   1 
ATOM   5996  C  CA  . PHE A 1 729  ? 21.629 69.820  -5.071  1.00 7.46  ? 729  PHE A CA  1 
ATOM   5997  C  C   . PHE A 1 729  ? 20.115 69.639  -5.001  1.00 7.48  ? 729  PHE A C   1 
ATOM   5998  O  O   . PHE A 1 729  ? 19.624 68.512  -5.081  1.00 9.07  ? 729  PHE A O   1 
ATOM   5999  C  CB  . PHE A 1 729  ? 22.169 69.043  -6.267  1.00 6.77  ? 729  PHE A CB  1 
ATOM   6000  C  CG  . PHE A 1 729  ? 21.668 69.531  -7.608  1.00 6.71  ? 729  PHE A CG  1 
ATOM   6001  C  CD1 . PHE A 1 729  ? 21.344 70.874  -7.861  1.00 8.01  ? 729  PHE A CD1 1 
ATOM   6002  C  CD2 . PHE A 1 729  ? 21.591 68.615  -8.651  1.00 6.35  ? 729  PHE A CD2 1 
ATOM   6003  C  CE1 . PHE A 1 729  ? 20.928 71.287  -9.148  1.00 7.97  ? 729  PHE A CE1 1 
ATOM   6004  C  CE2 . PHE A 1 729  ? 21.166 69.026  -9.933  1.00 7.90  ? 729  PHE A CE2 1 
ATOM   6005  C  CZ  . PHE A 1 729  ? 20.846 70.360  -10.171 1.00 8.39  ? 729  PHE A CZ  1 
ATOM   6006  N  N   . LEU A 1 730  ? 19.408 70.759  -4.801  1.00 7.58  ? 730  LEU A N   1 
ATOM   6007  C  CA  . LEU A 1 730  ? 17.952 70.699  -4.629  1.00 8.50  ? 730  LEU A CA  1 
ATOM   6008  C  C   . LEU A 1 730  ? 17.320 71.685  -5.597  1.00 8.06  ? 730  LEU A C   1 
ATOM   6009  O  O   . LEU A 1 730  ? 16.884 72.762  -5.182  1.00 8.65  ? 730  LEU A O   1 
ATOM   6010  C  CB  . LEU A 1 730  ? 17.573 71.022  -3.177  1.00 8.32  ? 730  LEU A CB  1 
ATOM   6011  C  CG  . LEU A 1 730  ? 17.988 69.917  -2.211  1.00 9.29  ? 730  LEU A CG  1 
ATOM   6012  C  CD1 . LEU A 1 730  ? 17.999 70.391  -0.784  1.00 11.65 ? 730  LEU A CD1 1 
ATOM   6013  C  CD2 . LEU A 1 730  ? 17.026 68.716  -2.358  1.00 13.50 ? 730  LEU A CD2 1 
ATOM   6014  N  N   . PRO A 1 731  ? 17.316 71.361  -6.883  1.00 8.27  ? 731  PRO A N   1 
ATOM   6015  C  CA  . PRO A 1 731  ? 16.896 72.350  -7.890  1.00 9.41  ? 731  PRO A CA  1 
ATOM   6016  C  C   . PRO A 1 731  ? 15.413 72.664  -7.763  1.00 10.61 ? 731  PRO A C   1 
ATOM   6017  O  O   . PRO A 1 731  ? 14.627 71.822  -7.319  1.00 9.60  ? 731  PRO A O   1 
ATOM   6018  C  CB  . PRO A 1 731  ? 17.150 71.634  -9.207  1.00 10.11 ? 731  PRO A CB  1 
ATOM   6019  C  CG  . PRO A 1 731  ? 17.139 70.147  -8.907  1.00 10.45 ? 731  PRO A CG  1 
ATOM   6020  C  CD  . PRO A 1 731  ? 17.691 70.080  -7.507  1.00 8.62  ? 731  PRO A CD  1 
ATOM   6021  N  N   . ASN A 1 732  ? 15.044 73.871  -8.191  1.00 11.27 ? 732  ASN A N   1 
ATOM   6022  C  CA  . ASN A 1 732  ? 13.637 74.255  -8.267  1.00 13.47 ? 732  ASN A CA  1 
ATOM   6023  C  C   . ASN A 1 732  ? 13.126 73.912  -9.659  1.00 13.12 ? 732  ASN A C   1 
ATOM   6024  O  O   . ASN A 1 732  ? 12.726 74.794  -10.446 1.00 15.67 ? 732  ASN A O   1 
ATOM   6025  C  CB  . ASN A 1 732  ? 13.480 75.740  -7.946  1.00 14.82 ? 732  ASN A CB  1 
ATOM   6026  C  CG  . ASN A 1 732  ? 14.162 76.643  -8.957  1.00 17.05 ? 732  ASN A CG  1 
ATOM   6027  O  OD1 . ASN A 1 732  ? 15.134 76.262  -9.605  1.00 19.50 ? 732  ASN A OD1 1 
ATOM   6028  N  ND2 . ASN A 1 732  ? 13.642 77.875  -9.100  1.00 20.91 ? 732  ASN A ND2 1 
ATOM   6029  N  N   . GLY A 1 733  ? 13.198 72.642  -10.002 1.00 11.12 ? 733  GLY A N   1 
ATOM   6030  C  CA  . GLY A 1 733  ? 12.744 72.151  -11.286 1.00 12.11 ? 733  GLY A CA  1 
ATOM   6031  C  C   . GLY A 1 733  ? 13.862 72.063  -12.312 1.00 10.96 ? 733  GLY A C   1 
ATOM   6032  O  O   . GLY A 1 733  ? 15.023 72.409  -12.018 1.00 10.61 ? 733  GLY A O   1 
ATOM   6033  N  N   . PRO A 1 734  ? 13.535 71.579  -13.511 1.00 10.20 ? 734  PRO A N   1 
ATOM   6034  C  CA  . PRO A 1 734  ? 14.495 71.490  -14.618 1.00 11.24 ? 734  PRO A CA  1 
ATOM   6035  C  C   . PRO A 1 734  ? 15.105 72.845  -14.938 1.00 11.05 ? 734  PRO A C   1 
ATOM   6036  O  O   . PRO A 1 734  ? 14.532 73.903  -14.657 1.00 10.50 ? 734  PRO A O   1 
ATOM   6037  C  CB  . PRO A 1 734  ? 13.643 70.991  -15.797 1.00 12.23 ? 734  PRO A CB  1 
ATOM   6038  C  CG  . PRO A 1 734  ? 12.441 70.381  -15.161 1.00 12.79 ? 734  PRO A CG  1 
ATOM   6039  C  CD  . PRO A 1 734  ? 12.204 71.027  -13.852 1.00 11.20 ? 734  PRO A CD  1 
ATOM   6040  N  N   . ALA A 1 735  ? 16.298 72.783  -15.522 1.00 9.91  ? 735  ALA A N   1 
ATOM   6041  C  CA  . ALA A 1 735  ? 17.035 73.972  -15.882 1.00 10.21 ? 735  ALA A CA  1 
ATOM   6042  C  C   . ALA A 1 735  ? 16.338 74.798  -16.971 1.00 11.22 ? 735  ALA A C   1 
ATOM   6043  O  O   . ALA A 1 735  ? 15.615 74.252  -17.809 1.00 12.00 ? 735  ALA A O   1 
ATOM   6044  C  CB  . ALA A 1 735  ? 18.421 73.557  -16.327 1.00 10.28 ? 735  ALA A CB  1 
ATOM   6045  N  N   . SER A 1 736  ? 16.573 76.099  -16.911 1.00 12.68 ? 736  SER A N   1 
ATOM   6046  C  CA  . SER A 1 736  ? 16.017 77.076  -17.863 1.00 13.66 ? 736  SER A CA  1 
ATOM   6047  C  C   . SER A 1 736  ? 17.154 77.623  -18.721 1.00 13.51 ? 736  SER A C   1 
ATOM   6048  O  O   . SER A 1 736  ? 18.248 77.856  -18.201 1.00 11.99 ? 736  SER A O   1 
ATOM   6049  C  CB  . SER A 1 736  ? 15.403 78.248  -17.087 1.00 14.94 ? 736  SER A CB  1 
ATOM   6050  O  OG  . SER A 1 736  ? 14.484 77.791  -16.114 1.00 22.06 ? 736  SER A OG  1 
ATOM   6051  N  N   . PRO A 1 737  ? 16.932 77.869  -20.006 1.00 14.94 ? 737  PRO A N   1 
ATOM   6052  C  CA  . PRO A 1 737  ? 18.019 78.365  -20.868 1.00 15.49 ? 737  PRO A CA  1 
ATOM   6053  C  C   . PRO A 1 737  ? 18.582 79.691  -20.377 1.00 15.81 ? 737  PRO A C   1 
ATOM   6054  O  O   . PRO A 1 737  ? 17.826 80.549  -19.931 1.00 17.16 ? 737  PRO A O   1 
ATOM   6055  C  CB  . PRO A 1 737  ? 17.361 78.531  -22.251 1.00 16.02 ? 737  PRO A CB  1 
ATOM   6056  C  CG  . PRO A 1 737  ? 16.144 77.695  -22.186 1.00 16.87 ? 737  PRO A CG  1 
ATOM   6057  C  CD  . PRO A 1 737  ? 15.675 77.651  -20.749 1.00 15.69 ? 737  PRO A CD  1 
ATOM   6058  N  N   . VAL A 1 738  ? 19.907 79.837  -20.430 1.00 15.22 ? 738  VAL A N   1 
ATOM   6059  C  CA  . VAL A 1 738  ? 20.535 81.141  -20.215 1.00 15.38 ? 738  VAL A CA  1 
ATOM   6060  C  C   . VAL A 1 738  ? 20.139 82.033  -21.406 1.00 16.09 ? 738  VAL A C   1 
ATOM   6061  O  O   . VAL A 1 738  ? 20.242 81.620  -22.570 1.00 16.37 ? 738  VAL A O   1 
ATOM   6062  C  CB  . VAL A 1 738  ? 22.076 81.002  -20.087 1.00 13.79 ? 738  VAL A CB  1 
ATOM   6063  C  CG1 . VAL A 1 738  ? 22.753 82.384  -20.033 1.00 14.20 ? 738  VAL A CG1 1 
ATOM   6064  C  CG2 . VAL A 1 738  ? 22.460 80.142  -18.826 1.00 13.96 ? 738  VAL A CG2 1 
ATOM   6065  N  N   . GLU A 1 739  ? 19.696 83.248  -21.092 1.00 18.01 ? 739  GLU A N   1 
ATOM   6066  C  CA  . GLU A 1 739  ? 19.390 84.245  -22.115 1.00 18.97 ? 739  GLU A CA  1 
ATOM   6067  C  C   . GLU A 1 739  ? 20.699 84.792  -22.666 1.00 18.27 ? 739  GLU A C   1 
ATOM   6068  O  O   . GLU A 1 739  ? 21.485 85.371  -21.925 1.00 18.73 ? 739  GLU A O   1 
ATOM   6069  C  CB  . GLU A 1 739  ? 18.623 85.395  -21.491 1.00 20.28 ? 739  GLU A CB  1 
ATOM   6070  C  CG  . GLU A 1 739  ? 17.210 85.034  -21.084 1.00 24.92 ? 739  GLU A CG  1 
ATOM   6071  C  CD  . GLU A 1 739  ? 16.364 86.269  -20.848 1.00 32.04 ? 739  GLU A CD  1 
ATOM   6072  O  OE1 . GLU A 1 739  ? 16.292 87.120  -21.771 1.00 34.21 ? 739  GLU A OE1 1 
ATOM   6073  O  OE2 . GLU A 1 739  ? 15.775 86.384  -19.745 1.00 36.20 ? 739  GLU A OE2 1 
ATOM   6074  N  N   . LEU A 1 740  ? 20.944 84.558  -23.943 1.00 18.59 ? 740  LEU A N   1 
ATOM   6075  C  CA  . LEU A 1 740  ? 22.263 84.833  -24.527 1.00 18.00 ? 740  LEU A CA  1 
ATOM   6076  C  C   . LEU A 1 740  ? 22.418 86.203  -25.152 1.00 19.02 ? 740  LEU A C   1 
ATOM   6077  O  O   . LEU A 1 740  ? 23.529 86.604  -25.415 1.00 19.13 ? 740  LEU A O   1 
ATOM   6078  C  CB  . LEU A 1 740  ? 22.602 83.792  -25.588 1.00 17.92 ? 740  LEU A CB  1 
ATOM   6079  C  CG  . LEU A 1 740  ? 22.557 82.330  -25.168 1.00 17.35 ? 740  LEU A CG  1 
ATOM   6080  C  CD1 . LEU A 1 740  ? 23.097 81.475  -26.301 1.00 17.25 ? 740  LEU A CD1 1 
ATOM   6081  C  CD2 . LEU A 1 740  ? 23.358 82.105  -23.872 1.00 18.87 ? 740  LEU A CD2 1 
ATOM   6082  N  N   . GLY A 1 741  ? 21.310 86.898  -25.391 1.00 19.05 ? 741  GLY A N   1 
ATOM   6083  C  CA  . GLY A 1 741  ? 21.350 88.172  -26.092 1.00 19.12 ? 741  GLY A CA  1 
ATOM   6084  C  C   . GLY A 1 741  ? 21.896 87.945  -27.497 1.00 18.83 ? 741  GLY A C   1 
ATOM   6085  O  O   . GLY A 1 741  ? 21.539 86.973  -28.156 1.00 19.33 ? 741  GLY A O   1 
ATOM   6086  N  N   A GLN A 1 742  ? 22.799 88.829  -27.926 0.50 18.35 ? 742  GLN A N   1 
ATOM   6087  N  N   B GLN A 1 742  ? 22.730 88.862  -27.979 0.50 18.40 ? 742  GLN A N   1 
ATOM   6088  C  CA  A GLN A 1 742  ? 23.423 88.727  -29.244 0.50 17.27 ? 742  GLN A CA  1 
ATOM   6089  C  CA  B GLN A 1 742  ? 23.416 88.659  -29.254 0.50 17.38 ? 742  GLN A CA  1 
ATOM   6090  C  C   A GLN A 1 742  ? 24.952 88.646  -29.110 0.50 16.02 ? 742  GLN A C   1 
ATOM   6091  C  C   B GLN A 1 742  ? 24.908 88.680  -28.924 0.50 16.09 ? 742  GLN A C   1 
ATOM   6092  O  O   A GLN A 1 742  ? 25.655 89.607  -29.419 0.50 15.68 ? 742  GLN A O   1 
ATOM   6093  O  O   B GLN A 1 742  ? 25.520 89.753  -28.798 0.50 15.48 ? 742  GLN A O   1 
ATOM   6094  C  CB  A GLN A 1 742  ? 23.049 89.943  -30.097 0.50 18.22 ? 742  GLN A CB  1 
ATOM   6095  C  CB  B GLN A 1 742  ? 23.031 89.734  -30.285 0.50 17.99 ? 742  GLN A CB  1 
ATOM   6096  C  CG  A GLN A 1 742  ? 23.175 89.690  -31.585 0.50 19.79 ? 742  GLN A CG  1 
ATOM   6097  C  CG  B GLN A 1 742  ? 21.513 89.858  -30.482 0.50 18.27 ? 742  GLN A CG  1 
ATOM   6098  C  CD  A GLN A 1 742  ? 22.452 90.729  -32.436 0.50 23.55 ? 742  GLN A CD  1 
ATOM   6099  C  CD  B GLN A 1 742  ? 21.118 90.998  -31.385 0.50 19.19 ? 742  GLN A CD  1 
ATOM   6100  O  OE1 A GLN A 1 742  ? 22.094 91.813  -31.953 0.50 25.48 ? 742  GLN A OE1 1 
ATOM   6101  O  OE1 B GLN A 1 742  ? 21.316 90.939  -32.601 0.50 20.84 ? 742  GLN A OE1 1 
ATOM   6102  N  NE2 A GLN A 1 742  ? 22.233 90.398  -33.705 0.50 23.69 ? 742  GLN A NE2 1 
ATOM   6103  N  NE2 B GLN A 1 742  ? 20.536 92.034  -30.801 0.50 22.31 ? 742  GLN A NE2 1 
ATOM   6104  N  N   . PRO A 1 743  ? 25.480 87.503  -28.675 1.00 14.46 ? 743  PRO A N   1 
ATOM   6105  C  CA  . PRO A 1 743  ? 26.883 87.462  -28.237 1.00 12.78 ? 743  PRO A CA  1 
ATOM   6106  C  C   . PRO A 1 743  ? 27.893 87.656  -29.376 1.00 12.98 ? 743  PRO A C   1 
ATOM   6107  O  O   . PRO A 1 743  ? 27.603 87.413  -30.566 1.00 13.88 ? 743  PRO A O   1 
ATOM   6108  C  CB  . PRO A 1 743  ? 27.011 86.091  -27.569 1.00 13.09 ? 743  PRO A CB  1 
ATOM   6109  C  CG  . PRO A 1 743  ? 25.988 85.254  -28.226 1.00 12.94 ? 743  PRO A CG  1 
ATOM   6110  C  CD  . PRO A 1 743  ? 24.850 86.164  -28.678 1.00 14.37 ? 743  PRO A CD  1 
ATOM   6111  N  N   . VAL A 1 744  ? 29.074 88.136  -28.981 1.00 10.76 ? 744  VAL A N   1 
ATOM   6112  C  CA  . VAL A 1 744  ? 30.181 88.341  -29.897 1.00 9.97  ? 744  VAL A CA  1 
ATOM   6113  C  C   . VAL A 1 744  ? 30.865 87.003  -30.109 1.00 8.96  ? 744  VAL A C   1 
ATOM   6114  O  O   . VAL A 1 744  ? 31.189 86.291  -29.134 1.00 8.77  ? 744  VAL A O   1 
ATOM   6115  C  CB  . VAL A 1 744  ? 31.166 89.366  -29.331 1.00 10.59 ? 744  VAL A CB  1 
ATOM   6116  C  CG1 . VAL A 1 744  ? 32.339 89.547  -30.238 1.00 10.73 ? 744  VAL A CG1 1 
ATOM   6117  C  CG2 . VAL A 1 744  ? 30.437 90.736  -29.055 1.00 12.50 ? 744  VAL A CG2 1 
ATOM   6118  N  N   . VAL A 1 745  ? 31.067 86.662  -31.367 1.00 7.94  ? 745  VAL A N   1 
ATOM   6119  C  CA  . VAL A 1 745  ? 31.692 85.399  -31.752 1.00 7.43  ? 745  VAL A CA  1 
ATOM   6120  C  C   . VAL A 1 745  ? 32.974 85.652  -32.490 1.00 8.63  ? 745  VAL A C   1 
ATOM   6121  O  O   . VAL A 1 745  ? 33.009 86.472  -33.426 1.00 8.38  ? 745  VAL A O   1 
ATOM   6122  C  CB  . VAL A 1 745  ? 30.727 84.568  -32.646 1.00 7.74  ? 745  VAL A CB  1 
ATOM   6123  C  CG1 . VAL A 1 745  ? 31.447 83.292  -33.128 1.00 9.38  ? 745  VAL A CG1 1 
ATOM   6124  C  CG2 . VAL A 1 745  ? 29.407 84.280  -31.906 1.00 8.10  ? 745  VAL A CG2 1 
ATOM   6125  N  N   . LEU A 1 746  ? 34.049 84.985  -32.086 1.00 7.95  ? 746  LEU A N   1 
ATOM   6126  C  CA  . LEU A 1 746  ? 35.328 85.146  -32.717 1.00 7.85  ? 746  LEU A CA  1 
ATOM   6127  C  C   . LEU A 1 746  ? 35.758 83.832  -33.368 1.00 8.44  ? 746  LEU A C   1 
ATOM   6128  O  O   . LEU A 1 746  ? 35.867 82.812  -32.688 1.00 7.93  ? 746  LEU A O   1 
ATOM   6129  C  CB  . LEU A 1 746  ? 36.367 85.595  -31.679 1.00 8.56  ? 746  LEU A CB  1 
ATOM   6130  C  CG  . LEU A 1 746  ? 37.831 85.572  -32.108 1.00 11.21 ? 746  LEU A CG  1 
ATOM   6131  C  CD1 . LEU A 1 746  ? 38.137 86.636  -33.168 1.00 14.25 ? 746  LEU A CD1 1 
ATOM   6132  C  CD2 . LEU A 1 746  ? 38.743 85.695  -30.893 1.00 12.19 ? 746  LEU A CD2 1 
ATOM   6133  N  N   . VAL A 1 747  ? 36.035 83.847  -34.655 1.00 7.88  ? 747  VAL A N   1 
ATOM   6134  C  CA  . VAL A 1 747  ? 36.432 82.657  -35.401 1.00 7.94  ? 747  VAL A CA  1 
ATOM   6135  C  C   . VAL A 1 747  ? 37.886 82.812  -35.809 1.00 9.09  ? 747  VAL A C   1 
ATOM   6136  O  O   . VAL A 1 747  ? 38.255 83.807  -36.448 1.00 9.55  ? 747  VAL A O   1 
ATOM   6137  C  CB  . VAL A 1 747  ? 35.552 82.478  -36.661 1.00 8.75  ? 747  VAL A CB  1 
ATOM   6138  C  CG1 . VAL A 1 747  ? 35.942 81.198  -37.384 1.00 9.51  ? 747  VAL A CG1 1 
ATOM   6139  C  CG2 . VAL A 1 747  ? 34.098 82.520  -36.281 1.00 8.48  ? 747  VAL A CG2 1 
ATOM   6140  N  N   . THR A 1 748  ? 38.747 81.873  -35.445 1.00 8.64  ? 748  THR A N   1 
ATOM   6141  C  CA  . THR A 1 748  ? 40.122 81.899  -35.885 1.00 10.01 ? 748  THR A CA  1 
ATOM   6142  C  C   . THR A 1 748  ? 40.335 80.675  -36.745 1.00 10.18 ? 748  THR A C   1 
ATOM   6143  O  O   . THR A 1 748  ? 39.980 79.559  -36.328 1.00 11.53 ? 748  THR A O   1 
ATOM   6144  C  CB  . THR A 1 748  ? 41.053 81.942  -34.663 1.00 11.48 ? 748  THR A CB  1 
ATOM   6145  O  OG1 . THR A 1 748  ? 40.810 83.151  -33.910 1.00 13.47 ? 748  THR A OG1 1 
ATOM   6146  C  CG2 . THR A 1 748  ? 42.508 82.067  -35.076 1.00 13.47 ? 748  THR A CG2 1 
ATOM   6147  N  N   . LYS A 1 749  ? 40.862 80.862  -37.953 1.00 10.09 ? 749  LYS A N   1 
ATOM   6148  C  CA  . LYS A 1 749  ? 40.983 79.750  -38.874 1.00 10.20 ? 749  LYS A CA  1 
ATOM   6149  C  C   . LYS A 1 749  ? 42.421 79.598  -39.291 1.00 10.46 ? 749  LYS A C   1 
ATOM   6150  O  O   . LYS A 1 749  ? 43.017 80.533  -39.860 1.00 10.76 ? 749  LYS A O   1 
ATOM   6151  C  CB  . LYS A 1 749  ? 40.127 79.964  -40.118 1.00 11.10 ? 749  LYS A CB  1 
ATOM   6152  C  CG  . LYS A 1 749  ? 40.299 78.846  -41.127 1.00 15.01 ? 749  LYS A CG  1 
ATOM   6153  C  CD  . LYS A 1 749  ? 39.399 79.058  -42.329 1.00 19.98 ? 749  LYS A CD  1 
ATOM   6154  C  CE  . LYS A 1 749  ? 39.878 78.276  -43.536 1.00 24.31 ? 749  LYS A CE  1 
ATOM   6155  N  NZ  . LYS A 1 749  ? 39.199 78.829  -44.745 1.00 29.20 ? 749  LYS A NZ  1 
ATOM   6156  N  N   . GLY A 1 750  ? 42.985 78.428  -39.012 1.00 9.87  ? 750  GLY A N   1 
ATOM   6157  C  CA  . GLY A 1 750  ? 44.381 78.183  -39.263 1.00 11.31 ? 750  GLY A CA  1 
ATOM   6158  C  C   . GLY A 1 750  ? 44.585 76.807  -39.831 1.00 12.22 ? 750  GLY A C   1 
ATOM   6159  O  O   . GLY A 1 750  ? 43.692 75.951  -39.727 1.00 13.18 ? 750  GLY A O   1 
ATOM   6160  N  N   . LYS A 1 751  ? 45.765 76.595  -40.404 1.00 11.96 ? 751  LYS A N   1 
ATOM   6161  C  CA  . LYS A 1 751  ? 46.076 75.313  -41.018 1.00 12.48 ? 751  LYS A CA  1 
ATOM   6162  C  C   . LYS A 1 751  ? 46.159 74.221  -39.948 1.00 11.67 ? 751  LYS A C   1 
ATOM   6163  O  O   . LYS A 1 751  ? 45.766 73.076  -40.203 1.00 11.84 ? 751  LYS A O   1 
ATOM   6164  C  CB  . LYS A 1 751  ? 47.402 75.408  -41.761 1.00 13.90 ? 751  LYS A CB  1 
ATOM   6165  C  CG  . LYS A 1 751  ? 47.732 74.183  -42.588 1.00 18.97 ? 751  LYS A CG  1 
ATOM   6166  C  CD  . LYS A 1 751  ? 47.591 74.454  -44.089 1.00 25.76 ? 751  LYS A CD  1 
ATOM   6167  C  CE  . LYS A 1 751  ? 48.377 73.397  -44.843 1.00 30.03 ? 751  LYS A CE  1 
ATOM   6168  N  NZ  . LYS A 1 751  ? 49.725 73.204  -44.209 1.00 32.90 ? 751  LYS A NZ  1 
ATOM   6169  N  N   . LEU A 1 752  ? 46.721 74.577  -38.791 1.00 10.35 ? 752  LEU A N   1 
ATOM   6170  C  CA  . LEU A 1 752  ? 46.979 73.621  -37.703 1.00 9.88  ? 752  LEU A CA  1 
ATOM   6171  C  C   . LEU A 1 752  ? 45.905 73.630  -36.645 1.00 10.56 ? 752  LEU A C   1 
ATOM   6172  O  O   . LEU A 1 752  ? 45.659 72.592  -36.023 1.00 9.73  ? 752  LEU A O   1 
ATOM   6173  C  CB  . LEU A 1 752  ? 48.304 73.933  -37.022 1.00 9.83  ? 752  LEU A CB  1 
ATOM   6174  C  CG  . LEU A 1 752  ? 49.543 73.794  -37.924 1.00 11.82 ? 752  LEU A CG  1 
ATOM   6175  C  CD1 . LEU A 1 752  ? 50.809 73.945  -37.123 1.00 12.37 ? 752  LEU A CD1 1 
ATOM   6176  C  CD2 . LEU A 1 752  ? 49.573 72.523  -38.778 1.00 14.38 ? 752  LEU A CD2 1 
ATOM   6177  N  N   . GLU A 1 753  ? 45.281 74.788  -36.404 1.00 10.17 ? 753  GLU A N   1 
ATOM   6178  C  CA  . GLU A 1 753  ? 44.314 74.920  -35.335 1.00 10.55 ? 753  GLU A CA  1 
ATOM   6179  C  C   . GLU A 1 753  ? 43.329 76.008  -35.715 1.00 10.27 ? 753  GLU A C   1 
ATOM   6180  O  O   . GLU A 1 753  ? 43.728 77.108  -36.150 1.00 10.47 ? 753  GLU A O   1 
ATOM   6181  C  CB  . GLU A 1 753  ? 45.025 75.294  -34.029 1.00 10.49 ? 753  GLU A CB  1 
ATOM   6182  C  CG  . GLU A 1 753  ? 44.075 75.408  -32.838 1.00 13.01 ? 753  GLU A CG  1 
ATOM   6183  C  CD  . GLU A 1 753  ? 44.724 76.041  -31.617 1.00 15.17 ? 753  GLU A CD  1 
ATOM   6184  O  OE1 . GLU A 1 753  ? 44.869 77.285  -31.580 1.00 23.49 ? 753  GLU A OE1 1 
ATOM   6185  O  OE2 . GLU A 1 753  ? 45.070 75.287  -30.697 1.00 21.84 ? 753  GLU A OE2 1 
ATOM   6186  N  N   . SER A 1 754  ? 42.065 75.699  -35.552 1.00 8.16  ? 754  SER A N   1 
ATOM   6187  C  CA  . SER A 1 754  ? 40.990 76.666  -35.698 1.00 8.61  ? 754  SER A CA  1 
ATOM   6188  C  C   . SER A 1 754  ? 40.138 76.703  -34.468 1.00 8.35  ? 754  SER A C   1 
ATOM   6189  O  O   . SER A 1 754  ? 40.157 75.741  -33.687 1.00 8.95  ? 754  SER A O   1 
ATOM   6190  C  CB  . SER A 1 754  ? 40.127 76.324  -36.892 1.00 9.15  ? 754  SER A CB  1 
ATOM   6191  O  OG  . SER A 1 754  ? 40.906 76.463  -38.080 1.00 9.85  ? 754  SER A OG  1 
ATOM   6192  N  N   . SER A 1 755  ? 39.376 77.770  -34.253 1.00 8.27  ? 755  SER A N   1 
ATOM   6193  C  CA  A SER A 1 755  ? 38.540 77.879  -33.060 0.50 8.75  ? 755  SER A CA  1 
ATOM   6194  C  CA  B SER A 1 755  ? 38.487 77.819  -33.094 0.50 8.94  ? 755  SER A CA  1 
ATOM   6195  C  C   . SER A 1 755  ? 37.343 78.779  -33.273 1.00 8.40  ? 755  SER A C   1 
ATOM   6196  O  O   . SER A 1 755  ? 37.408 79.697  -34.109 1.00 8.59  ? 755  SER A O   1 
ATOM   6197  C  CB  A SER A 1 755  ? 39.362 78.440  -31.905 0.50 9.69  ? 755  SER A CB  1 
ATOM   6198  C  CB  B SER A 1 755  ? 39.247 78.182  -31.813 0.50 10.34 ? 755  SER A CB  1 
ATOM   6199  O  OG  A SER A 1 755  ? 40.003 79.637  -32.281 0.50 11.69 ? 755  SER A OG  1 
ATOM   6200  O  OG  B SER A 1 755  ? 39.658 79.530  -31.809 0.50 12.10 ? 755  SER A OG  1 
ATOM   6201  N  N   . VAL A 1 756  ? 36.309 78.563  -32.491 1.00 7.18  ? 756  VAL A N   1 
ATOM   6202  C  CA  . VAL A 1 756  ? 35.188 79.469  -32.398 1.00 7.48  ? 756  VAL A CA  1 
ATOM   6203  C  C   . VAL A 1 756  ? 35.048 79.785  -30.919 1.00 7.72  ? 756  VAL A C   1 
ATOM   6204  O  O   . VAL A 1 756  ? 34.889 78.856  -30.092 1.00 7.74  ? 756  VAL A O   1 
ATOM   6205  C  CB  . VAL A 1 756  ? 33.911 78.857  -32.956 1.00 8.12  ? 756  VAL A CB  1 
ATOM   6206  C  CG1 . VAL A 1 756  ? 32.762 79.835  -32.800 1.00 8.86  ? 756  VAL A CG1 1 
ATOM   6207  C  CG2 . VAL A 1 756  ? 34.147 78.463  -34.426 1.00 10.80 ? 756  VAL A CG2 1 
ATOM   6208  N  N   . SER A 1 757  ? 35.075 81.059  -30.566 1.00 7.36  ? 757  SER A N   1 
ATOM   6209  C  CA  . SER A 1 757  ? 34.921 81.478  -29.177 1.00 7.78  ? 757  SER A CA  1 
ATOM   6210  C  C   . SER A 1 757  ? 33.774 82.438  -29.066 1.00 7.57  ? 757  SER A C   1 
ATOM   6211  O  O   . SER A 1 757  ? 33.639 83.304  -29.945 1.00 8.63  ? 757  SER A O   1 
ATOM   6212  C  CB  . SER A 1 757  ? 36.180 82.197  -28.701 1.00 8.73  ? 757  SER A CB  1 
ATOM   6213  O  OG  . SER A 1 757  ? 37.289 81.328  -28.884 1.00 12.05 ? 757  SER A OG  1 
ATOM   6214  N  N   . VAL A 1 758  ? 32.979 82.352  -28.011 1.00 7.47  ? 758  VAL A N   1 
ATOM   6215  C  CA  . VAL A 1 758  ? 31.837 83.233  -27.834 1.00 7.94  ? 758  VAL A CA  1 
ATOM   6216  C  C   . VAL A 1 758  ? 31.744 83.719  -26.405 1.00 7.88  ? 758  VAL A C   1 
ATOM   6217  O  O   . VAL A 1 758  ? 31.898 82.913  -25.478 1.00 7.63  ? 758  VAL A O   1 
ATOM   6218  C  CB  . VAL A 1 758  ? 30.532 82.573  -28.345 1.00 8.62  ? 758  VAL A CB  1 
ATOM   6219  C  CG1 . VAL A 1 758  ? 30.234 81.263  -27.622 1.00 8.66  ? 758  VAL A CG1 1 
ATOM   6220  C  CG2 . VAL A 1 758  ? 29.382 83.540  -28.169 1.00 10.76 ? 758  VAL A CG2 1 
ATOM   6221  N  N   . GLY A 1 759  ? 31.467 85.005  -26.217 1.00 8.20  ? 759  GLY A N   1 
ATOM   6222  C  CA  . GLY A 1 759  ? 31.353 85.576  -24.877 1.00 8.35  ? 759  GLY A CA  1 
ATOM   6223  C  C   . GLY A 1 759  ? 29.903 85.504  -24.449 1.00 9.47  ? 759  GLY A C   1 
ATOM   6224  O  O   . GLY A 1 759  ? 29.090 86.329  -24.852 1.00 9.63  ? 759  GLY A O   1 
ATOM   6225  N  N   . LEU A 1 760  ? 29.551 84.487  -23.686 1.00 10.39 ? 760  LEU A N   1 
ATOM   6226  C  CA  . LEU A 1 760  ? 28.192 84.329  -23.153 1.00 11.02 ? 760  LEU A CA  1 
ATOM   6227  C  C   . LEU A 1 760  ? 28.114 84.899  -21.741 1.00 11.67 ? 760  LEU A C   1 
ATOM   6228  O  O   . LEU A 1 760  ? 29.154 85.080  -21.076 1.00 12.11 ? 760  LEU A O   1 
ATOM   6229  C  CB  . LEU A 1 760  ? 27.854 82.826  -23.114 1.00 11.72 ? 760  LEU A CB  1 
ATOM   6230  C  CG  . LEU A 1 760  ? 27.998 82.113  -24.449 1.00 11.08 ? 760  LEU A CG  1 
ATOM   6231  C  CD1 . LEU A 1 760  ? 27.753 80.629  -24.301 1.00 14.46 ? 760  LEU A CD1 1 
ATOM   6232  C  CD2 . LEU A 1 760  ? 27.049 82.699  -25.502 1.00 12.77 ? 760  LEU A CD2 1 
ATOM   6233  N  N   . PRO A 1 761  ? 26.914 85.153  -21.230 1.00 12.66 ? 761  PRO A N   1 
ATOM   6234  C  CA  . PRO A 1 761  ? 26.823 85.532  -19.816 1.00 12.39 ? 761  PRO A CA  1 
ATOM   6235  C  C   . PRO A 1 761  ? 27.405 84.408  -18.945 1.00 12.97 ? 761  PRO A C   1 
ATOM   6236  O  O   . PRO A 1 761  ? 26.968 83.246  -19.032 1.00 13.26 ? 761  PRO A O   1 
ATOM   6237  C  CB  . PRO A 1 761  ? 25.315 85.711  -19.585 1.00 13.57 ? 761  PRO A CB  1 
ATOM   6238  C  CG  . PRO A 1 761  ? 24.803 86.004  -20.969 1.00 14.09 ? 761  PRO A CG  1 
ATOM   6239  C  CD  . PRO A 1 761  ? 25.592 85.124  -21.893 1.00 12.52 ? 761  PRO A CD  1 
ATOM   6240  N  N   . SER A 1 762  ? 28.401 84.779  -18.147 1.00 12.18 ? 762  SER A N   1 
ATOM   6241  C  CA  . SER A 1 762  ? 29.093 83.896  -17.215 1.00 11.30 ? 762  SER A CA  1 
ATOM   6242  C  C   . SER A 1 762  ? 30.052 82.904  -17.845 1.00 10.08 ? 762  SER A C   1 
ATOM   6243  O  O   . SER A 1 762  ? 30.722 82.185  -17.099 1.00 9.82  ? 762  SER A O   1 
ATOM   6244  C  CB  . SER A 1 762  ? 28.113 83.083  -16.392 1.00 12.80 ? 762  SER A CB  1 
ATOM   6245  O  OG  . SER A 1 762  ? 27.235 83.923  -15.675 1.00 15.96 ? 762  SER A OG  1 
ATOM   6246  N  N   . VAL A 1 763  ? 30.119 82.802  -19.172 1.00 9.61  ? 763  VAL A N   1 
ATOM   6247  C  CA  . VAL A 1 763  ? 31.009 81.822  -19.765 1.00 9.19  ? 763  VAL A CA  1 
ATOM   6248  C  C   . VAL A 1 763  ? 31.617 82.308  -21.057 1.00 8.39  ? 763  VAL A C   1 
ATOM   6249  O  O   . VAL A 1 763  ? 30.875 82.673  -21.970 1.00 9.46  ? 763  VAL A O   1 
ATOM   6250  C  CB  . VAL A 1 763  ? 30.259 80.494  -20.090 1.00 9.94  ? 763  VAL A CB  1 
ATOM   6251  C  CG1 . VAL A 1 763  ? 31.225 79.462  -20.632 1.00 11.14 ? 763  VAL A CG1 1 
ATOM   6252  C  CG2 . VAL A 1 763  ? 29.553 79.887  -18.887 1.00 12.53 ? 763  VAL A CG2 1 
ATOM   6253  N  N   . VAL A 1 764  ? 32.929 82.261  -21.177 1.00 6.54  ? 764  VAL A N   1 
ATOM   6254  C  CA  . VAL A 1 764  ? 33.533 82.385  -22.497 1.00 7.19  ? 764  VAL A CA  1 
ATOM   6255  C  C   . VAL A 1 764  ? 33.729 80.942  -22.966 1.00 7.24  ? 764  VAL A C   1 
ATOM   6256  O  O   . VAL A 1 764  ? 34.500 80.174  -22.376 1.00 7.29  ? 764  VAL A O   1 
ATOM   6257  C  CB  . VAL A 1 764  ? 34.876 83.119  -22.513 1.00 7.29  ? 764  VAL A CB  1 
ATOM   6258  C  CG1 . VAL A 1 764  ? 35.424 83.215  -23.955 1.00 9.36  ? 764  VAL A CG1 1 
ATOM   6259  C  CG2 . VAL A 1 764  ? 34.715 84.516  -21.937 1.00 9.40  ? 764  VAL A CG2 1 
ATOM   6260  N  N   . HIS A 1 765  ? 33.018 80.578  -24.019 1.00 6.89  ? 765  HIS A N   1 
ATOM   6261  C  CA  . HIS A 1 765  ? 32.931 79.180  -24.482 1.00 6.49  ? 765  HIS A CA  1 
ATOM   6262  C  C   . HIS A 1 765  ? 33.738 79.088  -25.747 1.00 7.05  ? 765  HIS A C   1 
ATOM   6263  O  O   . HIS A 1 765  ? 33.558 79.919  -26.663 1.00 7.83  ? 765  HIS A O   1 
ATOM   6264  C  CB  . HIS A 1 765  ? 31.466 78.849  -24.714 1.00 7.82  ? 765  HIS A CB  1 
ATOM   6265  C  CG  . HIS A 1 765  ? 31.213 77.561  -25.416 1.00 8.47  ? 765  HIS A CG  1 
ATOM   6266  N  ND1 . HIS A 1 765  ? 31.395 76.337  -24.811 1.00 6.84  ? 765  HIS A ND1 1 
ATOM   6267  C  CD2 . HIS A 1 765  ? 30.697 77.304  -26.644 1.00 10.71 ? 765  HIS A CD2 1 
ATOM   6268  C  CE1 . HIS A 1 765  ? 31.049 75.376  -25.664 1.00 9.56  ? 765  HIS A CE1 1 
ATOM   6269  N  NE2 . HIS A 1 765  ? 30.631 75.943  -26.789 1.00 10.92 ? 765  HIS A NE2 1 
ATOM   6270  N  N   . GLN A 1 766  ? 34.618 78.113  -25.845 1.00 6.10  ? 766  GLN A N   1 
ATOM   6271  C  CA  A GLN A 1 766  ? 35.532 77.975  -26.970 0.50 6.67  ? 766  GLN A CA  1 
ATOM   6272  C  CA  B GLN A 1 766  ? 35.498 77.977  -26.981 0.50 6.73  ? 766  GLN A CA  1 
ATOM   6273  C  C   . GLN A 1 766  ? 35.516 76.538  -27.471 1.00 7.18  ? 766  GLN A C   1 
ATOM   6274  O  O   . GLN A 1 766  ? 35.632 75.600  -26.663 1.00 7.67  ? 766  GLN A O   1 
ATOM   6275  C  CB  A GLN A 1 766  ? 36.972 78.301  -26.568 0.50 7.28  ? 766  GLN A CB  1 
ATOM   6276  C  CB  B GLN A 1 766  ? 36.908 78.395  -26.602 0.50 7.20  ? 766  GLN A CB  1 
ATOM   6277  C  CG  A GLN A 1 766  ? 37.159 79.649  -25.866 0.50 7.29  ? 766  GLN A CG  1 
ATOM   6278  C  CG  B GLN A 1 766  ? 37.918 78.300  -27.713 0.50 7.85  ? 766  GLN A CG  1 
ATOM   6279  C  CD  A GLN A 1 766  ? 38.152 79.607  -24.670 0.50 13.80 ? 766  GLN A CD  1 
ATOM   6280  C  CD  B GLN A 1 766  ? 39.315 78.697  -27.280 0.50 10.39 ? 766  GLN A CD  1 
ATOM   6281  O  OE1 A GLN A 1 766  ? 39.308 79.241  -24.846 0.50 11.82 ? 766  GLN A OE1 1 
ATOM   6282  O  OE1 B GLN A 1 766  ? 39.684 78.510  -26.120 0.50 11.86 ? 766  GLN A OE1 1 
ATOM   6283  N  NE2 A GLN A 1 766  ? 37.684 79.983  -23.461 0.50 13.80 ? 766  GLN A NE2 1 
ATOM   6284  N  NE2 B GLN A 1 766  ? 40.097 79.249  -28.213 0.50 10.41 ? 766  GLN A NE2 1 
ATOM   6285  N  N   . THR A 1 767  ? 35.386 76.359  -28.776 1.00 6.89  ? 767  THR A N   1 
ATOM   6286  C  CA  . THR A 1 767  ? 35.548 75.051  -29.431 1.00 7.79  ? 767  THR A CA  1 
ATOM   6287  C  C   . THR A 1 767  ? 36.790 75.125  -30.261 1.00 8.17  ? 767  THR A C   1 
ATOM   6288  O  O   . THR A 1 767  ? 36.891 76.035  -31.106 1.00 8.69  ? 767  THR A O   1 
ATOM   6289  C  CB  . THR A 1 767  ? 34.356 74.769  -30.337 1.00 8.50  ? 767  THR A CB  1 
ATOM   6290  O  OG1 . THR A 1 767  ? 33.158 74.843  -29.557 1.00 11.90 ? 767  THR A OG1 1 
ATOM   6291  C  CG2 . THR A 1 767  ? 34.400 73.332  -30.877 1.00 9.95  ? 767  THR A CG2 1 
ATOM   6292  N  N   . ILE A 1 768  ? 37.747 74.229  -30.042 1.00 8.22  ? 768  ILE A N   1 
ATOM   6293  C  CA  . ILE A 1 768  ? 39.044 74.234  -30.698 1.00 8.15  ? 768  ILE A CA  1 
ATOM   6294  C  C   . ILE A 1 768  ? 39.202 72.968  -31.526 1.00 9.42  ? 768  ILE A C   1 
ATOM   6295  O  O   . ILE A 1 768  ? 38.931 71.868  -31.033 1.00 10.04 ? 768  ILE A O   1 
ATOM   6296  C  CB  . ILE A 1 768  ? 40.190 74.352  -29.666 1.00 8.04  ? 768  ILE A CB  1 
ATOM   6297  C  CG1 . ILE A 1 768  ? 40.019 75.589  -28.796 1.00 11.19 ? 768  ILE A CG1 1 
ATOM   6298  C  CG2 . ILE A 1 768  ? 41.549 74.419  -30.380 1.00 12.14 ? 768  ILE A CG2 1 
ATOM   6299  C  CD1 . ILE A 1 768  ? 40.870 75.503  -27.545 1.00 13.20 ? 768  ILE A CD1 1 
ATOM   6300  N  N   . MET A 1 769  ? 39.662 73.134  -32.748 1.00 8.56  ? 769  MET A N   1 
ATOM   6301  C  CA  A MET A 1 769  ? 39.812 72.034  -33.689 0.50 9.32  ? 769  MET A CA  1 
ATOM   6302  C  CA  B MET A 1 769  ? 39.790 72.043  -33.706 0.50 9.81  ? 769  MET A CA  1 
ATOM   6303  C  C   . MET A 1 769  ? 41.251 71.915  -34.127 1.00 9.82  ? 769  MET A C   1 
ATOM   6304  O  O   . MET A 1 769  ? 41.857 72.882  -34.607 1.00 8.92  ? 769  MET A O   1 
ATOM   6305  C  CB  A MET A 1 769  ? 38.956 72.303  -34.910 0.50 9.81  ? 769  MET A CB  1 
ATOM   6306  C  CB  B MET A 1 769  ? 38.894 72.324  -34.924 0.50 10.18 ? 769  MET A CB  1 
ATOM   6307  C  CG  A MET A 1 769  ? 37.527 72.482  -34.563 0.50 9.07  ? 769  MET A CG  1 
ATOM   6308  C  CG  B MET A 1 769  ? 37.413 72.149  -34.627 0.50 11.22 ? 769  MET A CG  1 
ATOM   6309  S  SD  A MET A 1 769  ? 36.646 72.866  -36.044 0.50 12.11 ? 769  MET A SD  1 
ATOM   6310  S  SD  B MET A 1 769  ? 36.292 73.218  -35.587 0.50 13.43 ? 769  MET A SD  1 
ATOM   6311  C  CE  A MET A 1 769  ? 36.953 71.496  -37.073 0.50 10.78 ? 769  MET A CE  1 
ATOM   6312  C  CE  B MET A 1 769  ? 36.541 74.809  -34.738 0.50 12.38 ? 769  MET A CE  1 
ATOM   6313  N  N   . ARG A 1 770  ? 41.803 70.722  -33.975 1.00 10.00 ? 770  ARG A N   1 
ATOM   6314  C  CA  . ARG A 1 770  ? 43.174 70.467  -34.382 1.00 11.22 ? 770  ARG A CA  1 
ATOM   6315  C  C   . ARG A 1 770  ? 43.279 69.269  -35.309 1.00 12.27 ? 770  ARG A C   1 
ATOM   6316  O  O   . ARG A 1 770  ? 44.381 68.795  -35.566 1.00 13.73 ? 770  ARG A O   1 
ATOM   6317  C  CB  . ARG A 1 770  ? 44.072 70.277  -33.169 1.00 11.89 ? 770  ARG A CB  1 
ATOM   6318  C  CG  . ARG A 1 770  ? 44.171 71.500  -32.303 1.00 13.48 ? 770  ARG A CG  1 
ATOM   6319  C  CD  . ARG A 1 770  ? 45.003 71.284  -31.046 1.00 17.16 ? 770  ARG A CD  1 
ATOM   6320  N  NE  . ARG A 1 770  ? 44.872 72.368  -30.067 1.00 24.39 ? 770  ARG A NE  1 
ATOM   6321  C  CZ  . ARG A 1 770  ? 44.172 72.269  -28.931 1.00 26.31 ? 770  ARG A CZ  1 
ATOM   6322  N  NH1 . ARG A 1 770  ? 43.545 71.132  -28.635 1.00 27.47 ? 770  ARG A NH1 1 
ATOM   6323  N  NH2 . ARG A 1 770  ? 44.107 73.300  -28.083 1.00 29.34 ? 770  ARG A NH2 1 
ATOM   6324  N  N   . GLY A 1 771  ? 42.139 68.815  -35.804 1.00 12.59 ? 771  GLY A N   1 
ATOM   6325  C  CA  . GLY A 1 771  ? 42.121 67.767  -36.810 1.00 15.76 ? 771  GLY A CA  1 
ATOM   6326  C  C   . GLY A 1 771  ? 41.557 66.442  -36.360 1.00 16.72 ? 771  GLY A C   1 
ATOM   6327  O  O   . GLY A 1 771  ? 41.494 65.498  -37.157 1.00 18.81 ? 771  GLY A O   1 
ATOM   6328  N  N   . GLY A 1 772  ? 41.169 66.347  -35.088 1.00 16.61 ? 772  GLY A N   1 
ATOM   6329  C  CA  . GLY A 1 772  ? 40.517 65.160  -34.513 1.00 15.93 ? 772  GLY A CA  1 
ATOM   6330  C  C   . GLY A 1 772  ? 39.342 65.636  -33.659 1.00 14.17 ? 772  GLY A C   1 
ATOM   6331  O  O   . GLY A 1 772  ? 38.738 66.644  -33.992 1.00 13.66 ? 772  GLY A O   1 
ATOM   6332  N  N   . ALA A 1 773  ? 39.002 64.941  -32.565 1.00 12.79 ? 773  ALA A N   1 
ATOM   6333  C  CA  . ALA A 1 773  ? 37.908 65.381  -31.704 1.00 11.13 ? 773  ALA A CA  1 
ATOM   6334  C  C   . ALA A 1 773  ? 38.147 66.810  -31.211 1.00 9.81  ? 773  ALA A C   1 
ATOM   6335  O  O   . ALA A 1 773  ? 39.256 67.138  -30.822 1.00 10.34 ? 773  ALA A O   1 
ATOM   6336  C  CB  . ALA A 1 773  ? 37.793 64.464  -30.511 1.00 11.32 ? 773  ALA A CB  1 
ATOM   6337  N  N   . PRO A 1 774  ? 37.126 67.656  -31.219 1.00 9.59  ? 774  PRO A N   1 
ATOM   6338  C  CA  . PRO A 1 774  ? 37.331 69.011  -30.702 1.00 9.41  ? 774  PRO A CA  1 
ATOM   6339  C  C   . PRO A 1 774  ? 37.657 69.051  -29.218 1.00 8.85  ? 774  PRO A C   1 
ATOM   6340  O  O   . PRO A 1 774  ? 37.364 68.103  -28.449 1.00 7.67  ? 774  PRO A O   1 
ATOM   6341  C  CB  . PRO A 1 774  ? 35.975 69.708  -30.932 1.00 10.89 ? 774  PRO A CB  1 
ATOM   6342  C  CG  . PRO A 1 774  ? 35.033 68.641  -31.297 1.00 13.93 ? 774  PRO A CG  1 
ATOM   6343  C  CD  . PRO A 1 774  ? 35.767 67.449  -31.756 1.00 10.48 ? 774  PRO A CD  1 
ATOM   6344  N  N   . GLU A 1 775  ? 38.322 70.127  -28.844 1.00 8.29  ? 775  GLU A N   1 
ATOM   6345  C  CA  A GLU A 1 775  ? 38.534 70.490  -27.454 0.50 8.48  ? 775  GLU A CA  1 
ATOM   6346  C  CA  B GLU A 1 775  ? 38.529 70.497  -27.447 0.50 8.21  ? 775  GLU A CA  1 
ATOM   6347  C  C   . GLU A 1 775  ? 37.560 71.617  -27.122 1.00 8.26  ? 775  GLU A C   1 
ATOM   6348  O  O   . GLU A 1 775  ? 37.357 72.537  -27.942 1.00 8.85  ? 775  GLU A O   1 
ATOM   6349  C  CB  A GLU A 1 775  ? 39.984 70.922  -27.237 0.50 8.99  ? 775  GLU A CB  1 
ATOM   6350  C  CB  B GLU A 1 775  ? 39.966 70.956  -27.181 0.50 8.85  ? 775  GLU A CB  1 
ATOM   6351  C  CG  A GLU A 1 775  ? 40.325 71.281  -25.789 0.50 9.53  ? 775  GLU A CG  1 
ATOM   6352  C  CG  B GLU A 1 775  ? 40.168 71.553  -25.776 0.50 8.84  ? 775  GLU A CG  1 
ATOM   6353  C  CD  A GLU A 1 775  ? 41.813 71.445  -25.533 0.50 11.80 ? 775  GLU A CD  1 
ATOM   6354  C  CD  B GLU A 1 775  ? 41.605 71.954  -25.450 0.50 10.74 ? 775  GLU A CD  1 
ATOM   6355  O  OE1 A GLU A 1 775  ? 42.593 70.582  -25.971 0.50 14.01 ? 775  GLU A OE1 1 
ATOM   6356  O  OE1 B GLU A 1 775  ? 42.460 71.963  -26.364 0.50 12.43 ? 775  GLU A OE1 1 
ATOM   6357  O  OE2 A GLU A 1 775  ? 42.212 72.443  -24.894 0.50 13.75 ? 775  GLU A OE2 1 
ATOM   6358  O  OE2 B GLU A 1 775  ? 41.899 72.243  -24.261 0.50 11.43 ? 775  GLU A OE2 1 
ATOM   6359  N  N   . ILE A 1 776  ? 36.921 71.550  -25.981 1.00 7.12  ? 776  ILE A N   1 
ATOM   6360  C  CA  . ILE A 1 776  ? 36.071 72.614  -25.510 1.00 6.75  ? 776  ILE A CA  1 
ATOM   6361  C  C   . ILE A 1 776  ? 36.723 73.232  -24.289 1.00 6.72  ? 776  ILE A C   1 
ATOM   6362  O  O   . ILE A 1 776  ? 37.194 72.504  -23.414 1.00 6.97  ? 776  ILE A O   1 
ATOM   6363  C  CB  . ILE A 1 776  ? 34.702 72.025  -25.108 1.00 8.04  ? 776  ILE A CB  1 
ATOM   6364  C  CG1 . ILE A 1 776  ? 34.114 71.106  -26.207 1.00 11.17 ? 776  ILE A CG1 1 
ATOM   6365  C  CG2 . ILE A 1 776  ? 33.757 73.133  -24.637 1.00 10.92 ? 776  ILE A CG2 1 
ATOM   6366  C  CD1 . ILE A 1 776  ? 33.943 71.753  -27.566 1.00 15.38 ? 776  ILE A CD1 1 
ATOM   6367  N  N   . ARG A 1 777  ? 36.731 74.550  -24.201 1.00 7.15  ? 777  ARG A N   1 
ATOM   6368  C  CA  . ARG A 1 777  ? 37.189 75.263  -23.009 1.00 6.67  ? 777  ARG A CA  1 
ATOM   6369  C  C   . ARG A 1 777  ? 36.138 76.245  -22.609 1.00 7.57  ? 777  ARG A C   1 
ATOM   6370  O  O   . ARG A 1 777  ? 35.654 77.012  -23.456 1.00 7.84  ? 777  ARG A O   1 
ATOM   6371  C  CB  . ARG A 1 777  ? 38.492 76.001  -23.231 1.00 7.53  ? 777  ARG A CB  1 
ATOM   6372  C  CG  . ARG A 1 777  ? 39.616 75.123  -23.651 1.00 9.07  ? 777  ARG A CG  1 
ATOM   6373  C  CD  . ARG A 1 777  ? 40.935 75.869  -23.756 1.00 11.51 ? 777  ARG A CD  1 
ATOM   6374  N  NE  . ARG A 1 777  ? 42.014 75.028  -24.288 1.00 12.85 ? 777  ARG A NE  1 
ATOM   6375  C  CZ  . ARG A 1 777  ? 43.205 75.478  -24.683 1.00 18.29 ? 777  ARG A CZ  1 
ATOM   6376  N  NH1 . ARG A 1 777  ? 43.503 76.768  -24.546 1.00 20.74 ? 777  ARG A NH1 1 
ATOM   6377  N  NH2 . ARG A 1 777  ? 44.113 74.639  -25.183 1.00 19.62 ? 777  ARG A NH2 1 
ATOM   6378  N  N   . ASN A 1 778  ? 35.755 76.245  -21.348 1.00 6.32  ? 778  ASN A N   1 
ATOM   6379  C  CA  . ASN A 1 778  ? 34.828 77.217  -20.822 1.00 6.39  ? 778  ASN A CA  1 
ATOM   6380  C  C   . ASN A 1 778  ? 35.540 77.987  -19.744 1.00 6.52  ? 778  ASN A C   1 
ATOM   6381  O  O   . ASN A 1 778  ? 35.972 77.406  -18.745 1.00 6.20  ? 778  ASN A O   1 
ATOM   6382  C  CB  . ASN A 1 778  ? 33.589 76.572  -20.160 1.00 6.85  ? 778  ASN A CB  1 
ATOM   6383  C  CG  . ASN A 1 778  ? 32.701 75.883  -21.127 1.00 7.96  ? 778  ASN A CG  1 
ATOM   6384  O  OD1 . ASN A 1 778  ? 32.693 76.228  -22.319 1.00 8.90  ? 778  ASN A OD1 1 
ATOM   6385  N  ND2 . ASN A 1 778  ? 31.928 74.920  -20.631 1.00 8.87  ? 778  ASN A ND2 1 
ATOM   6386  N  N   . LEU A 1 779  ? 35.633 79.297  -19.907 1.00 6.19  ? 779  LEU A N   1 
ATOM   6387  C  CA  . LEU A 1 779  ? 36.075 80.168  -18.809 1.00 6.11  ? 779  LEU A CA  1 
ATOM   6388  C  C   . LEU A 1 779  ? 34.838 80.628  -18.091 1.00 6.62  ? 779  LEU A C   1 
ATOM   6389  O  O   . LEU A 1 779  ? 34.042 81.408  -18.622 1.00 7.13  ? 779  LEU A O   1 
ATOM   6390  C  CB  . LEU A 1 779  ? 36.899 81.351  -19.342 1.00 7.52  ? 779  LEU A CB  1 
ATOM   6391  C  CG  . LEU A 1 779  ? 37.428 82.289  -18.248 1.00 10.14 ? 779  LEU A CG  1 
ATOM   6392  C  CD1 . LEU A 1 779  ? 38.403 81.553  -17.398 1.00 11.97 ? 779  LEU A CD1 1 
ATOM   6393  C  CD2 . LEU A 1 779  ? 38.038 83.507  -18.950 1.00 15.06 ? 779  LEU A CD2 1 
ATOM   6394  N  N   . VAL A 1 780  ? 34.617 80.023  -16.928 1.00 5.93  ? 780  VAL A N   1 
ATOM   6395  C  CA  . VAL A 1 780  ? 33.353 80.198  -16.202 1.00 7.13  ? 780  VAL A CA  1 
ATOM   6396  C  C   . VAL A 1 780  ? 33.526 81.189  -15.066 1.00 8.51  ? 780  VAL A C   1 
ATOM   6397  O  O   . VAL A 1 780  ? 34.339 80.982  -14.166 1.00 9.26  ? 780  VAL A O   1 
ATOM   6398  C  CB  . VAL A 1 780  ? 32.820 78.831  -15.647 1.00 7.04  ? 780  VAL A CB  1 
ATOM   6399  C  CG1 . VAL A 1 780  ? 31.474 78.991  -14.963 1.00 8.66  ? 780  VAL A CG1 1 
ATOM   6400  C  CG2 . VAL A 1 780  ? 32.749 77.798  -16.777 1.00 8.24  ? 780  VAL A CG2 1 
ATOM   6401  N  N   . ASP A 1 781  ? 32.761 82.275  -15.155 1.00 8.41  ? 781  ASP A N   1 
ATOM   6402  C  CA  . ASP A 1 781  ? 32.746 83.274  -14.106 1.00 8.75  ? 781  ASP A CA  1 
ATOM   6403  C  C   . ASP A 1 781  ? 31.328 83.622  -13.750 1.00 9.75  ? 781  ASP A C   1 
ATOM   6404  O  O   . ASP A 1 781  ? 30.686 84.481  -14.393 1.00 10.62 ? 781  ASP A O   1 
ATOM   6405  C  CB  . ASP A 1 781  ? 33.489 84.510  -14.583 1.00 10.37 ? 781  ASP A CB  1 
ATOM   6406  C  CG  . ASP A 1 781  ? 33.548 85.581  -13.522 1.00 14.23 ? 781  ASP A CG  1 
ATOM   6407  O  OD1 . ASP A 1 781  ? 33.094 85.368  -12.353 1.00 14.22 ? 781  ASP A OD1 1 
ATOM   6408  O  OD2 . ASP A 1 781  ? 34.092 86.685  -13.781 1.00 19.90 ? 781  ASP A OD2 1 
ATOM   6409  N  N   . ILE A 1 782  ? 30.813 82.919  -12.751 1.00 9.62  ? 782  ILE A N   1 
ATOM   6410  C  CA  . ILE A 1 782  ? 29.403 83.037  -12.325 1.00 11.98 ? 782  ILE A CA  1 
ATOM   6411  C  C   . ILE A 1 782  ? 29.151 84.389  -11.659 1.00 13.59 ? 782  ILE A C   1 
ATOM   6412  O  O   . ILE A 1 782  ? 27.990 84.798  -11.470 1.00 15.95 ? 782  ILE A O   1 
ATOM   6413  C  CB  . ILE A 1 782  ? 29.046 81.843  -11.398 1.00 12.11 ? 782  ILE A CB  1 
ATOM   6414  C  CG1 . ILE A 1 782  ? 27.551 81.678  -11.216 1.00 13.90 ? 782  ILE A CG1 1 
ATOM   6415  C  CG2 . ILE A 1 782  ? 29.734 81.973  -10.053 1.00 14.20 ? 782  ILE A CG2 1 
ATOM   6416  C  CD1 . ILE A 1 782  ? 27.272 80.276  -10.769 1.00 14.59 ? 782  ILE A CD1 1 
ATOM   6417  N  N   . GLY A 1 783  ? 30.225 85.115  -11.356 1.00 14.23 ? 783  GLY A N   1 
ATOM   6418  C  CA  . GLY A 1 783  ? 30.108 86.504  -10.898 1.00 15.57 ? 783  GLY A CA  1 
ATOM   6419  C  C   . GLY A 1 783  ? 29.252 86.613  -9.658  1.00 17.19 ? 783  GLY A C   1 
ATOM   6420  O  O   . GLY A 1 783  ? 29.479 85.875  -8.695  1.00 18.66 ? 783  GLY A O   1 
ATOM   6421  N  N   . SER A 1 784  ? 28.274 87.510  -9.681  1.00 19.61 ? 784  SER A N   1 
ATOM   6422  C  CA  . SER A 1 784  ? 27.446 87.737  -8.497  1.00 20.50 ? 784  SER A CA  1 
ATOM   6423  C  C   . SER A 1 784  ? 26.058 87.109  -8.648  1.00 20.61 ? 784  SER A C   1 
ATOM   6424  O  O   . SER A 1 784  ? 25.113 87.523  -7.957  1.00 20.23 ? 784  SER A O   1 
ATOM   6425  C  CB  . SER A 1 784  ? 27.352 89.236  -8.174  1.00 21.75 ? 784  SER A CB  1 
ATOM   6426  O  OG  . SER A 1 784  ? 26.867 89.957  -9.298  1.00 25.84 ? 784  SER A OG  1 
ATOM   6427  N  N   . LEU A 1 785  ? 25.926 86.122  -9.543  1.00 19.29 ? 785  LEU A N   1 
ATOM   6428  C  CA  . LEU A 1 785  ? 24.626 85.478  -9.763  1.00 19.63 ? 785  LEU A CA  1 
ATOM   6429  C  C   . LEU A 1 785  ? 24.245 84.535  -8.638  1.00 19.81 ? 785  LEU A C   1 
ATOM   6430  O  O   . LEU A 1 785  ? 24.535 83.322  -8.699  1.00 20.86 ? 785  LEU A O   1 
ATOM   6431  C  CB  . LEU A 1 785  ? 24.614 84.693  -11.071 1.00 19.65 ? 785  LEU A CB  1 
ATOM   6432  C  CG  . LEU A 1 785  ? 24.816 85.480  -12.366 1.00 20.45 ? 785  LEU A CG  1 
ATOM   6433  C  CD1 . LEU A 1 785  ? 24.779 84.514  -13.531 1.00 23.01 ? 785  LEU A CD1 1 
ATOM   6434  C  CD2 . LEU A 1 785  ? 23.766 86.570  -12.513 1.00 22.92 ? 785  LEU A CD2 1 
ATOM   6435  N  N   . ASP A 1 786  ? 23.530 85.045  -7.639  1.00 19.00 ? 786  ASP A N   1 
ATOM   6436  C  CA  . ASP A 1 786  ? 23.241 84.223  -6.476  1.00 17.97 ? 786  ASP A CA  1 
ATOM   6437  C  C   . ASP A 1 786  ? 22.216 83.121  -6.798  1.00 15.57 ? 786  ASP A C   1 
ATOM   6438  O  O   . ASP A 1 786  ? 21.352 83.254  -7.689  1.00 14.20 ? 786  ASP A O   1 
ATOM   6439  C  CB  . ASP A 1 786  ? 22.763 85.060  -5.270  1.00 20.02 ? 786  ASP A CB  1 
ATOM   6440  C  CG  . ASP A 1 786  ? 23.910 85.633  -4.421  1.00 22.91 ? 786  ASP A CG  1 
ATOM   6441  O  OD1 . ASP A 1 786  ? 25.011 85.975  -4.942  1.00 24.55 ? 786  ASP A OD1 1 
ATOM   6442  O  OD2 . ASP A 1 786  ? 23.771 85.777  -3.180  1.00 26.02 ? 786  ASP A OD2 1 
ATOM   6443  N  N   . ASN A 1 787  ? 22.341 82.030  -6.056  1.00 13.01 ? 787  ASN A N   1 
ATOM   6444  C  CA  . ASN A 1 787  ? 21.410 80.913  -6.135  1.00 11.88 ? 787  ASN A CA  1 
ATOM   6445  C  C   . ASN A 1 787  ? 21.217 80.404  -7.549  1.00 11.13 ? 787  ASN A C   1 
ATOM   6446  O  O   . ASN A 1 787  ? 20.101 80.248  -8.038  1.00 11.70 ? 787  ASN A O   1 
ATOM   6447  C  CB  . ASN A 1 787  ? 20.094 81.283  -5.439  1.00 11.75 ? 787  ASN A CB  1 
ATOM   6448  C  CG  . ASN A 1 787  ? 20.303 81.509  -3.982  1.00 15.08 ? 787  ASN A CG  1 
ATOM   6449  O  OD1 . ASN A 1 787  ? 21.043 80.748  -3.334  1.00 16.14 ? 787  ASN A OD1 1 
ATOM   6450  N  ND2 . ASN A 1 787  ? 19.671 82.563  -3.434  1.00 20.85 ? 787  ASN A ND2 1 
ATOM   6451  N  N   . THR A 1 788  ? 22.343 80.161  -8.207  1.00 10.57 ? 788  THR A N   1 
ATOM   6452  C  CA  . THR A 1 788  ? 22.375 79.765  -9.595  1.00 10.44 ? 788  THR A CA  1 
ATOM   6453  C  C   . THR A 1 788  ? 23.396 78.652  -9.790  1.00 8.80  ? 788  THR A C   1 
ATOM   6454  O  O   . THR A 1 788  ? 24.515 78.742  -9.262  1.00 9.45  ? 788  THR A O   1 
ATOM   6455  C  CB  . THR A 1 788  ? 22.792 80.981  -10.441 1.00 11.62 ? 788  THR A CB  1 
ATOM   6456  O  OG1 . THR A 1 788  ? 21.747 81.973  -10.369 1.00 14.81 ? 788  THR A OG1 1 
ATOM   6457  C  CG2 . THR A 1 788  ? 22.853 80.621  -11.898 1.00 13.18 ? 788  THR A CG2 1 
ATOM   6458  N  N   . GLU A 1 789  ? 23.013 77.657  -10.583 1.00 7.47  ? 789  GLU A N   1 
ATOM   6459  C  CA  . GLU A 1 789  ? 23.975 76.642  -11.016 1.00 7.89  ? 789  GLU A CA  1 
ATOM   6460  C  C   . GLU A 1 789  ? 23.972 76.648  -12.530 1.00 7.15  ? 789  GLU A C   1 
ATOM   6461  O  O   . GLU A 1 789  ? 22.891 76.550  -13.131 1.00 9.61  ? 789  GLU A O   1 
ATOM   6462  C  CB  . GLU A 1 789  ? 23.653 75.253  -10.430 1.00 8.08  ? 789  GLU A CB  1 
ATOM   6463  C  CG  . GLU A 1 789  ? 23.234 75.270  -8.958  1.00 8.80  ? 789  GLU A CG  1 
ATOM   6464  C  CD  . GLU A 1 789  ? 23.422 73.947  -8.245  1.00 8.72  ? 789  GLU A CD  1 
ATOM   6465  O  OE1 . GLU A 1 789  ? 24.261 73.128  -8.724  1.00 9.42  ? 789  GLU A OE1 1 
ATOM   6466  O  OE2 . GLU A 1 789  ? 22.798 73.785  -7.196  1.00 8.64  ? 789  GLU A OE2 1 
ATOM   6467  N  N   . ILE A 1 790  ? 25.124 76.794  -13.150 1.00 6.87  ? 790  ILE A N   1 
ATOM   6468  C  CA  A ILE A 1 790  ? 25.209 76.842  -14.613 0.50 8.12  ? 790  ILE A CA  1 
ATOM   6469  C  CA  B ILE A 1 790  ? 25.227 76.854  -14.613 0.50 7.79  ? 790  ILE A CA  1 
ATOM   6470  C  C   . ILE A 1 790  ? 25.568 75.469  -15.128 1.00 7.74  ? 790  ILE A C   1 
ATOM   6471  O  O   . ILE A 1 790  ? 26.547 74.865  -14.661 1.00 7.28  ? 790  ILE A O   1 
ATOM   6472  C  CB  A ILE A 1 790  ? 26.262 77.866  -15.101 0.50 8.64  ? 790  ILE A CB  1 
ATOM   6473  C  CB  B ILE A 1 790  ? 26.303 77.909  -15.067 0.50 8.75  ? 790  ILE A CB  1 
ATOM   6474  C  CG1 A ILE A 1 790  ? 26.013 79.247  -14.469 0.50 10.58 ? 790  ILE A CG1 1 
ATOM   6475  C  CG1 B ILE A 1 790  ? 25.839 79.356  -14.769 0.50 10.31 ? 790  ILE A CG1 1 
ATOM   6476  C  CG2 A ILE A 1 790  ? 26.275 77.951  -16.637 0.50 9.40  ? 790  ILE A CG2 1 
ATOM   6477  C  CG2 B ILE A 1 790  ? 26.715 77.751  -16.547 0.50 8.87  ? 790  ILE A CG2 1 
ATOM   6478  C  CD1 A ILE A 1 790  ? 27.066 80.280  -14.812 0.50 9.73  ? 790  ILE A CD1 1 
ATOM   6479  C  CD1 B ILE A 1 790  ? 24.441 79.718  -15.231 0.50 13.54 ? 790  ILE A CD1 1 
ATOM   6480  N  N   . VAL A 1 791  ? 24.772 74.975  -16.058 1.00 6.74  ? 791  VAL A N   1 
ATOM   6481  C  CA  . VAL A 1 791  ? 24.992 73.671  -16.673 1.00 7.28  ? 791  VAL A CA  1 
ATOM   6482  C  C   . VAL A 1 791  ? 25.265 73.798  -18.151 1.00 6.88  ? 791  VAL A C   1 
ATOM   6483  O  O   . VAL A 1 791  ? 24.688 74.681  -18.831 1.00 6.64  ? 791  VAL A O   1 
ATOM   6484  C  CB  . VAL A 1 791  ? 23.815 72.732  -16.393 1.00 7.02  ? 791  VAL A CB  1 
ATOM   6485  C  CG1 . VAL A 1 791  ? 22.579 73.128  -17.165 1.00 10.19 ? 791  VAL A CG1 1 
ATOM   6486  C  CG2 . VAL A 1 791  ? 24.159 71.316  -16.734 1.00 9.89  ? 791  VAL A CG2 1 
ATOM   6487  N  N   . MET A 1 792  ? 26.157 72.976  -18.653 1.00 6.01  ? 792  MET A N   1 
ATOM   6488  C  CA  . MET A 1 792  ? 26.396 72.844  -20.089 1.00 5.80  ? 792  MET A CA  1 
ATOM   6489  C  C   . MET A 1 792  ? 25.756 71.543  -20.564 1.00 6.94  ? 792  MET A C   1 
ATOM   6490  O  O   . MET A 1 792  ? 26.093 70.459  -20.043 1.00 6.86  ? 792  MET A O   1 
ATOM   6491  C  CB  . MET A 1 792  ? 27.897 72.849  -20.422 1.00 6.37  ? 792  MET A CB  1 
ATOM   6492  C  CG  . MET A 1 792  ? 28.192 72.748  -21.899 1.00 8.42  ? 792  MET A CG  1 
ATOM   6493  S  SD  . MET A 1 792  ? 29.972 72.748  -22.260 1.00 10.20 ? 792  MET A SD  1 
ATOM   6494  C  CE  . MET A 1 792  ? 30.504 71.279  -21.441 1.00 11.74 ? 792  MET A CE  1 
ATOM   6495  N  N   . ARG A 1 793  ? 24.833 71.633  -21.520 1.00 7.10  ? 793  ARG A N   1 
ATOM   6496  C  CA  . ARG A 1 793  ? 24.120 70.466  -22.030 1.00 7.51  ? 793  ARG A CA  1 
ATOM   6497  C  C   . ARG A 1 793  ? 24.461 70.248  -23.485 1.00 8.10  ? 793  ARG A C   1 
ATOM   6498  O  O   . ARG A 1 793  ? 24.637 71.214  -24.254 1.00 8.03  ? 793  ARG A O   1 
ATOM   6499  C  CB  . ARG A 1 793  ? 22.625 70.671  -21.836 1.00 8.15  ? 793  ARG A CB  1 
ATOM   6500  C  CG  . ARG A 1 793  ? 21.790 69.491  -22.320 1.00 7.15  ? 793  ARG A CG  1 
ATOM   6501  C  CD  . ARG A 1 793  ? 20.298 69.652  -21.997 1.00 9.63  ? 793  ARG A CD  1 
ATOM   6502  N  NE  . ARG A 1 793  ? 20.066 69.782  -20.556 1.00 9.44  ? 793  ARG A NE  1 
ATOM   6503  C  CZ  . ARG A 1 793  ? 18.970 70.296  -19.998 1.00 11.30 ? 793  ARG A CZ  1 
ATOM   6504  N  NH1 . ARG A 1 793  ? 17.984 70.752  -20.789 1.00 11.29 ? 793  ARG A NH1 1 
ATOM   6505  N  NH2 . ARG A 1 793  ? 18.873 70.408  -18.684 1.00 10.41 ? 793  ARG A NH2 1 
ATOM   6506  N  N   . LEU A 1 794  ? 24.515 68.981  -23.878 1.00 7.72  ? 794  LEU A N   1 
ATOM   6507  C  CA  . LEU A 1 794  ? 24.646 68.541  -25.264 1.00 7.96  ? 794  LEU A CA  1 
ATOM   6508  C  C   . LEU A 1 794  ? 23.353 67.834  -25.636 1.00 8.74  ? 794  LEU A C   1 
ATOM   6509  O  O   . LEU A 1 794  ? 22.916 66.944  -24.922 1.00 8.66  ? 794  LEU A O   1 
ATOM   6510  C  CB  . LEU A 1 794  ? 25.786 67.537  -25.433 1.00 9.81  ? 794  LEU A CB  1 
ATOM   6511  C  CG  . LEU A 1 794  ? 27.127 68.231  -25.541 1.00 10.96 ? 794  LEU A CG  1 
ATOM   6512  C  CD1 . LEU A 1 794  ? 28.232 67.227  -25.248 1.00 14.45 ? 794  LEU A CD1 1 
ATOM   6513  C  CD2 . LEU A 1 794  ? 27.289 68.742  -26.966 1.00 16.82 ? 794  LEU A CD2 1 
ATOM   6514  N  N   . GLU A 1 795  ? 22.753 68.241  -26.744 1.00 8.85  ? 795  GLU A N   1 
ATOM   6515  C  CA  . GLU A 1 795  ? 21.512 67.618  -27.247 1.00 10.65 ? 795  GLU A CA  1 
ATOM   6516  C  C   . GLU A 1 795  ? 21.827 66.912  -28.553 1.00 10.04 ? 795  GLU A C   1 
ATOM   6517  O  O   . GLU A 1 795  ? 22.407 67.504  -29.459 1.00 10.21 ? 795  GLU A O   1 
ATOM   6518  C  CB  . GLU A 1 795  ? 20.438 68.681  -27.493 1.00 11.52 ? 795  GLU A CB  1 
ATOM   6519  C  CG  . GLU A 1 795  ? 20.082 69.443  -26.232 1.00 14.78 ? 795  GLU A CG  1 
ATOM   6520  C  CD  . GLU A 1 795  ? 19.200 70.681  -26.438 1.00 15.99 ? 795  GLU A CD  1 
ATOM   6521  O  OE1 . GLU A 1 795  ? 19.193 71.268  -27.541 1.00 24.83 ? 795  GLU A OE1 1 
ATOM   6522  O  OE2 . GLU A 1 795  ? 18.532 71.099  -25.466 1.00 22.84 ? 795  GLU A OE2 1 
ATOM   6523  N  N   . THR A 1 796  ? 21.462 65.636  -28.651 1.00 9.74  ? 796  THR A N   1 
ATOM   6524  C  CA  . THR A 1 796  ? 21.731 64.862  -29.837 1.00 9.66  ? 796  THR A CA  1 
ATOM   6525  C  C   . THR A 1 796  ? 20.484 64.046  -30.186 1.00 9.79  ? 796  THR A C   1 
ATOM   6526  O  O   . THR A 1 796  ? 19.513 64.056  -29.426 1.00 11.72 ? 796  THR A O   1 
ATOM   6527  C  CB  . THR A 1 796  ? 22.900 63.859  -29.655 1.00 10.61 ? 796  THR A CB  1 
ATOM   6528  O  OG1 . THR A 1 796  ? 22.466 62.709  -28.901 1.00 10.09 ? 796  THR A OG1 1 
ATOM   6529  C  CG2 . THR A 1 796  ? 24.076 64.441  -28.886 1.00 11.65 ? 796  THR A CG2 1 
ATOM   6530  N  N   A HIS A 1 797  ? 20.607 63.330  -31.304 0.50 9.29  ? 797  HIS A N   1 
ATOM   6531  N  N   B HIS A 1 797  ? 20.525 63.328  -31.310 0.50 10.16 ? 797  HIS A N   1 
ATOM   6532  C  CA  A HIS A 1 797  ? 19.576 62.410  -31.771 0.50 10.26 ? 797  HIS A CA  1 
ATOM   6533  C  CA  B HIS A 1 797  ? 19.447 62.369  -31.649 0.50 11.31 ? 797  HIS A CA  1 
ATOM   6534  C  C   A HIS A 1 797  ? 19.731 61.029  -31.205 0.50 10.40 ? 797  HIS A C   1 
ATOM   6535  C  C   B HIS A 1 797  ? 19.956 60.918  -31.483 0.50 10.98 ? 797  HIS A C   1 
ATOM   6536  O  O   A HIS A 1 797  ? 18.801 60.231  -31.375 0.50 9.59  ? 797  HIS A O   1 
ATOM   6537  O  O   B HIS A 1 797  ? 19.510 59.949  -32.133 0.50 8.76  ? 797  HIS A O   1 
ATOM   6538  C  CB  A HIS A 1 797  ? 19.502 62.370  -33.312 0.50 9.34  ? 797  HIS A CB  1 
ATOM   6539  C  CB  B HIS A 1 797  ? 18.858 62.635  -33.049 0.50 11.76 ? 797  HIS A CB  1 
ATOM   6540  C  CG  A HIS A 1 797  ? 18.776 63.543  -33.885 0.50 8.68  ? 797  HIS A CG  1 
ATOM   6541  C  CG  B HIS A 1 797  ? 18.346 64.032  -33.261 0.50 14.24 ? 797  HIS A CG  1 
ATOM   6542  N  ND1 A HIS A 1 797  ? 18.059 64.422  -33.094 0.50 10.58 ? 797  HIS A ND1 1 
ATOM   6543  N  ND1 B HIS A 1 797  ? 18.023 64.894  -32.232 0.50 14.72 ? 797  HIS A ND1 1 
ATOM   6544  C  CD2 A HIS A 1 797  ? 18.679 64.006  -35.150 0.50 11.06 ? 797  HIS A CD2 1 
ATOM   6545  C  CD2 B HIS A 1 797  ? 18.068 64.702  -34.407 0.50 13.49 ? 797  HIS A CD2 1 
ATOM   6546  C  CE1 A HIS A 1 797  ? 17.539 65.365  -33.857 0.50 6.79  ? 797  HIS A CE1 1 
ATOM   6547  C  CE1 B HIS A 1 797  ? 17.592 66.038  -32.736 0.50 15.90 ? 797  HIS A CE1 1 
ATOM   6548  N  NE2 A HIS A 1 797  ? 17.905 65.141  -35.104 0.50 11.26 ? 797  HIS A NE2 1 
ATOM   6549  N  NE2 B HIS A 1 797  ? 17.615 65.948  -34.052 0.50 15.04 ? 797  HIS A NE2 1 
ATOM   6550  N  N   . ILE A 1 798  ? 20.883 60.742  -30.550 1.00 9.79  ? 798  ILE A N   1 
ATOM   6551  C  CA  . ILE A 1 798  ? 21.281 59.390  -30.166 1.00 9.63  ? 798  ILE A CA  1 
ATOM   6552  C  C   . ILE A 1 798  ? 20.182 58.761  -29.329 1.00 9.45  ? 798  ILE A C   1 
ATOM   6553  O  O   . ILE A 1 798  ? 19.657 59.366  -28.436 1.00 10.15 ? 798  ILE A O   1 
ATOM   6554  C  CB  . ILE A 1 798  ? 22.597 59.452  -29.392 1.00 8.53  ? 798  ILE A CB  1 
ATOM   6555  C  CG1 . ILE A 1 798  ? 23.718 59.884  -30.312 1.00 9.99  ? 798  ILE A CG1 1 
ATOM   6556  C  CG2 . ILE A 1 798  ? 22.889 58.076  -28.778 1.00 10.03 ? 798  ILE A CG2 1 
ATOM   6557  C  CD1 . ILE A 1 798  ? 25.052 60.194  -29.579 1.00 10.80 ? 798  ILE A CD1 1 
ATOM   6558  N  N   . ASP A 1 799  ? 19.813 57.533  -29.683 1.00 11.33 ? 799  ASP A N   1 
ATOM   6559  C  CA  . ASP A 1 799  ? 18.670 56.921  -29.053 1.00 10.66 ? 799  ASP A CA  1 
ATOM   6560  C  C   . ASP A 1 799  ? 19.111 56.145  -27.804 1.00 11.07 ? 799  ASP A C   1 
ATOM   6561  O  O   . ASP A 1 799  ? 19.062 54.921  -27.740 1.00 9.88  ? 799  ASP A O   1 
ATOM   6562  C  CB  . ASP A 1 799  ? 17.976 55.976  -30.061 1.00 13.20 ? 799  ASP A CB  1 
ATOM   6563  C  CG  . ASP A 1 799  ? 16.640 55.456  -29.570 1.00 15.53 ? 799  ASP A CG  1 
ATOM   6564  O  OD1 . ASP A 1 799  ? 16.010 56.053  -28.681 1.00 20.51 ? 799  ASP A OD1 1 
ATOM   6565  O  OD2 . ASP A 1 799  ? 16.163 54.392  -30.017 1.00 20.93 ? 799  ASP A OD2 1 
ATOM   6566  N  N   . SER A 1 800  ? 19.540 56.896  -26.790 1.00 10.43 ? 800  SER A N   1 
ATOM   6567  C  CA  . SER A 1 800  ? 20.098 56.296  -25.584 1.00 9.74  ? 800  SER A CA  1 
ATOM   6568  C  C   . SER A 1 800  ? 19.052 55.897  -24.574 1.00 9.29  ? 800  SER A C   1 
ATOM   6569  O  O   . SER A 1 800  ? 19.326 55.102  -23.655 1.00 9.09  ? 800  SER A O   1 
ATOM   6570  C  CB  . SER A 1 800  ? 21.074 57.285  -24.930 1.00 9.33  ? 800  SER A CB  1 
ATOM   6571  O  OG  . SER A 1 800  ? 20.446 58.514  -24.647 1.00 7.92  ? 800  SER A OG  1 
ATOM   6572  N  N   . GLY A 1 801  ? 17.838 56.424  -24.691 1.00 9.49  ? 801  GLY A N   1 
ATOM   6573  C  CA  . GLY A 1 801  ? 16.798 56.022  -23.780 1.00 9.39  ? 801  GLY A CA  1 
ATOM   6574  C  C   . GLY A 1 801  ? 17.072 56.565  -22.409 1.00 9.28  ? 801  GLY A C   1 
ATOM   6575  O  O   . GLY A 1 801  ? 17.132 57.776  -22.234 1.00 10.36 ? 801  GLY A O   1 
ATOM   6576  N  N   . ASP A 1 802  ? 17.197 55.658  -21.448 1.00 8.98  ? 802  ASP A N   1 
ATOM   6577  C  CA  . ASP A 1 802  ? 17.472 56.066  -20.087 1.00 9.40  ? 802  ASP A CA  1 
ATOM   6578  C  C   . ASP A 1 802  ? 18.866 55.659  -19.637 1.00 9.58  ? 802  ASP A C   1 
ATOM   6579  O  O   . ASP A 1 802  ? 19.152 55.753  -18.454 1.00 8.97  ? 802  ASP A O   1 
ATOM   6580  C  CB  . ASP A 1 802  ? 16.417 55.509  -19.114 1.00 11.26 ? 802  ASP A CB  1 
ATOM   6581  C  CG  . ASP A 1 802  ? 16.248 54.012  -19.202 1.00 13.72 ? 802  ASP A CG  1 
ATOM   6582  O  OD1 . ASP A 1 802  ? 17.025 53.303  -19.894 1.00 17.64 ? 802  ASP A OD1 1 
ATOM   6583  O  OD2 . ASP A 1 802  ? 15.327 53.439  -18.541 1.00 17.93 ? 802  ASP A OD2 1 
ATOM   6584  N  N   . ILE A 1 803  ? 19.695 55.211  -20.558 1.00 7.44  ? 803  ILE A N   1 
ATOM   6585  C  CA  . ILE A 1 803  ? 21.033 54.713  -20.207 1.00 7.24  ? 803  ILE A CA  1 
ATOM   6586  C  C   . ILE A 1 803  ? 22.101 55.749  -20.501 1.00 7.11  ? 803  ILE A C   1 
ATOM   6587  O  O   . ILE A 1 803  ? 22.058 56.436  -21.525 1.00 6.82  ? 803  ILE A O   1 
ATOM   6588  C  CB  . ILE A 1 803  ? 21.347 53.415  -21.001 1.00 7.59  ? 803  ILE A CB  1 
ATOM   6589  C  CG1 . ILE A 1 803  ? 20.309 52.332  -20.675 1.00 10.50 ? 803  ILE A CG1 1 
ATOM   6590  C  CG2 . ILE A 1 803  ? 22.778 52.929  -20.775 1.00 7.77  ? 803  ILE A CG2 1 
ATOM   6591  C  CD1 . ILE A 1 803  ? 20.247 52.013  -19.198 1.00 11.38 ? 803  ILE A CD1 1 
ATOM   6592  N  N   . PHE A 1 804  ? 23.102 55.820  -19.622 1.00 5.56  ? 804  PHE A N   1 
ATOM   6593  C  CA  . PHE A 1 804  ? 24.283 56.634  -19.854 1.00 5.78  ? 804  PHE A CA  1 
ATOM   6594  C  C   . PHE A 1 804  ? 25.418 56.035  -19.052 1.00 4.82  ? 804  PHE A C   1 
ATOM   6595  O  O   . PHE A 1 804  ? 25.179 55.154  -18.214 1.00 7.91  ? 804  PHE A O   1 
ATOM   6596  C  CB  . PHE A 1 804  ? 24.065 58.144  -19.553 1.00 4.87  ? 804  PHE A CB  1 
ATOM   6597  C  CG  . PHE A 1 804  ? 23.650 58.481  -18.143 1.00 6.05  ? 804  PHE A CG  1 
ATOM   6598  C  CD1 . PHE A 1 804  ? 22.366 58.287  -17.694 1.00 4.70  ? 804  PHE A CD1 1 
ATOM   6599  C  CD2 . PHE A 1 804  ? 24.570 59.095  -17.278 1.00 6.90  ? 804  PHE A CD2 1 
ATOM   6600  C  CE1 . PHE A 1 804  ? 21.970 58.644  -16.424 1.00 7.09  ? 804  PHE A CE1 1 
ATOM   6601  C  CE2 . PHE A 1 804  ? 24.194 59.473  -16.030 1.00 5.27  ? 804  PHE A CE2 1 
ATOM   6602  C  CZ  . PHE A 1 804  ? 22.905 59.252  -15.575 1.00 6.81  ? 804  PHE A CZ  1 
ATOM   6603  N  N   . TYR A 1 805  ? 26.626 56.484  -19.306 1.00 4.52  ? 805  TYR A N   1 
ATOM   6604  C  CA  . TYR A 1 805  ? 27.790 55.929  -18.624 1.00 4.40  ? 805  TYR A CA  1 
ATOM   6605  C  C   . TYR A 1 805  ? 28.609 57.034  -18.042 1.00 5.48  ? 805  TYR A C   1 
ATOM   6606  O  O   . TYR A 1 805  ? 28.780 58.051  -18.697 1.00 5.50  ? 805  TYR A O   1 
ATOM   6607  C  CB  . TYR A 1 805  ? 28.651 55.162  -19.610 1.00 5.73  ? 805  TYR A CB  1 
ATOM   6608  C  CG  . TYR A 1 805  ? 27.976 53.929  -20.192 1.00 5.10  ? 805  TYR A CG  1 
ATOM   6609  C  CD1 . TYR A 1 805  ? 26.989 54.027  -21.189 1.00 7.66  ? 805  TYR A CD1 1 
ATOM   6610  C  CD2 . TYR A 1 805  ? 28.271 52.676  -19.666 1.00 6.29  ? 805  TYR A CD2 1 
ATOM   6611  C  CE1 . TYR A 1 805  ? 26.376 52.875  -21.662 1.00 6.62  ? 805  TYR A CE1 1 
ATOM   6612  C  CE2 . TYR A 1 805  ? 27.663 51.500  -20.187 1.00 6.62  ? 805  TYR A CE2 1 
ATOM   6613  C  CZ  . TYR A 1 805  ? 26.692 51.643  -21.150 1.00 6.81  ? 805  TYR A CZ  1 
ATOM   6614  O  OH  . TYR A 1 805  ? 26.043 50.538  -21.704 1.00 8.26  ? 805  TYR A OH  1 
ATOM   6615  N  N   . THR A 1 806  ? 29.126 56.816  -16.833 1.00 5.16  ? 806  THR A N   1 
ATOM   6616  C  CA  . THR A 1 806  ? 29.967 57.836  -16.180 1.00 4.97  ? 806  THR A CA  1 
ATOM   6617  C  C   . THR A 1 806  ? 31.141 57.100  -15.617 1.00 5.91  ? 806  THR A C   1 
ATOM   6618  O  O   . THR A 1 806  ? 31.090 55.902  -15.331 1.00 6.32  ? 806  THR A O   1 
ATOM   6619  C  CB  . THR A 1 806  ? 29.240 58.620  -15.106 1.00 5.98  ? 806  THR A CB  1 
ATOM   6620  O  OG1 . THR A 1 806  ? 28.852 57.723  -14.070 1.00 5.72  ? 806  THR A OG1 1 
ATOM   6621  C  CG2 . THR A 1 806  ? 27.964 59.288  -15.634 1.00 6.01  ? 806  THR A CG2 1 
ATOM   6622  N  N   . ASP A 1 807  ? 32.240 57.788  -15.427 1.00 5.55  ? 807  ASP A N   1 
ATOM   6623  C  CA  . ASP A 1 807  ? 33.380 57.105  -14.856 1.00 6.92  ? 807  ASP A CA  1 
ATOM   6624  C  C   . ASP A 1 807  ? 33.432 57.148  -13.342 1.00 5.20  ? 807  ASP A C   1 
ATOM   6625  O  O   . ASP A 1 807  ? 32.794 57.954  -12.728 1.00 6.30  ? 807  ASP A O   1 
ATOM   6626  C  CB  . ASP A 1 807  ? 34.670 57.566  -15.483 1.00 9.29  ? 807  ASP A CB  1 
ATOM   6627  C  CG  . ASP A 1 807  ? 35.124 58.836  -14.948 1.00 11.73 ? 807  ASP A CG  1 
ATOM   6628  O  OD1 . ASP A 1 807  ? 34.362 59.804  -14.968 1.00 12.98 ? 807  ASP A OD1 1 
ATOM   6629  O  OD2 . ASP A 1 807  ? 36.269 58.880  -14.468 1.00 14.71 ? 807  ASP A OD2 1 
ATOM   6630  N  N   . LEU A 1 808  ? 34.197 56.221  -12.791 1.00 5.41  ? 808  LEU A N   1 
ATOM   6631  C  CA  . LEU A 1 808  ? 34.461 56.170  -11.362 1.00 5.02  ? 808  LEU A CA  1 
ATOM   6632  C  C   . LEU A 1 808  ? 35.951 56.388  -11.189 1.00 4.14  ? 808  LEU A C   1 
ATOM   6633  O  O   . LEU A 1 808  ? 36.746 55.553  -11.603 1.00 5.26  ? 808  LEU A O   1 
ATOM   6634  C  CB  . LEU A 1 808  ? 34.077 54.825  -10.759 1.00 6.13  ? 808  LEU A CB  1 
ATOM   6635  C  CG  . LEU A 1 808  ? 32.545 54.692  -10.622 1.00 5.96  ? 808  LEU A CG  1 
ATOM   6636  C  CD1 . LEU A 1 808  ? 32.255 53.221  -10.361 1.00 7.78  ? 808  LEU A CD1 1 
ATOM   6637  C  CD2 . LEU A 1 808  ? 32.009 55.553  -9.495  1.00 9.40  ? 808  LEU A CD2 1 
ATOM   6638  N  N   . ASN A 1 809  ? 36.306 57.539  -10.632 1.00 4.36  ? 809  ASN A N   1 
ATOM   6639  C  CA  . ASN A 1 809  ? 37.697 57.847  -10.273 1.00 4.46  ? 809  ASN A CA  1 
ATOM   6640  C  C   . ASN A 1 809  ? 38.649 57.750  -11.434 1.00 4.71  ? 809  ASN A C   1 
ATOM   6641  O  O   . ASN A 1 809  ? 39.837 57.505  -11.237 1.00 4.84  ? 809  ASN A O   1 
ATOM   6642  C  CB  . ASN A 1 809  ? 38.175 56.957  -9.120  1.00 4.51  ? 809  ASN A CB  1 
ATOM   6643  C  CG  . ASN A 1 809  ? 37.146 56.879  -8.049  1.00 4.81  ? 809  ASN A CG  1 
ATOM   6644  O  OD1 . ASN A 1 809  ? 36.317 55.968  -8.023  1.00 5.68  ? 809  ASN A OD1 1 
ATOM   6645  N  ND2 . ASN A 1 809  ? 37.162 57.851  -7.145  1.00 5.53  ? 809  ASN A ND2 1 
ATOM   6646  N  N   . GLY A 1 810  ? 38.168 57.937  -12.667 1.00 5.30  ? 810  GLY A N   1 
ATOM   6647  C  CA  . GLY A 1 810  ? 39.128 57.878  -13.771 1.00 6.12  ? 810  GLY A CA  1 
ATOM   6648  C  C   . GLY A 1 810  ? 39.611 56.490  -14.093 1.00 6.96  ? 810  GLY A C   1 
ATOM   6649  O  O   . GLY A 1 810  ? 40.555 56.329  -14.883 1.00 9.21  ? 810  GLY A O   1 
ATOM   6650  N  N   . LEU A 1 811  ? 38.980 55.478  -13.485 1.00 6.36  ? 811  LEU A N   1 
ATOM   6651  C  CA  . LEU A 1 811  ? 39.431 54.107  -13.577 1.00 7.64  ? 811  LEU A CA  1 
ATOM   6652  C  C   . LEU A 1 811  ? 38.538 53.199  -14.450 1.00 7.58  ? 811  LEU A C   1 
ATOM   6653  O  O   . LEU A 1 811  ? 39.047 52.298  -15.139 1.00 9.53  ? 811  LEU A O   1 
ATOM   6654  C  CB  . LEU A 1 811  ? 39.518 53.534  -12.147 1.00 8.09  ? 811  LEU A CB  1 
ATOM   6655  C  CG  . LEU A 1 811  ? 39.995 52.096  -12.000 1.00 9.83  ? 811  LEU A CG  1 
ATOM   6656  C  CD1 . LEU A 1 811  ? 41.419 51.929  -12.524 1.00 10.79 ? 811  LEU A CD1 1 
ATOM   6657  C  CD2 . LEU A 1 811  ? 39.877 51.603  -10.538 1.00 10.62 ? 811  LEU A CD2 1 
ATOM   6658  N  N   . GLN A 1 812  ? 37.232 53.402  -14.358 1.00 5.94  ? 812  GLN A N   1 
ATOM   6659  C  CA  . GLN A 1 812  ? 36.270 52.481  -14.996 1.00 6.57  ? 812  GLN A CA  1 
ATOM   6660  C  C   . GLN A 1 812  ? 35.035 53.270  -15.341 1.00 6.60  ? 812  GLN A C   1 
ATOM   6661  O  O   . GLN A 1 812  ? 34.764 54.328  -14.749 1.00 6.99  ? 812  GLN A O   1 
ATOM   6662  C  CB  . GLN A 1 812  ? 35.947 51.339  -14.040 1.00 7.66  ? 812  GLN A CB  1 
ATOM   6663  C  CG  . GLN A 1 812  ? 35.391 51.844  -12.709 1.00 9.37  ? 812  GLN A CG  1 
ATOM   6664  C  CD  . GLN A 1 812  ? 35.132 50.706  -11.745 1.00 11.97 ? 812  GLN A CD  1 
ATOM   6665  O  OE1 . GLN A 1 812  ? 34.180 49.979  -11.904 1.00 11.15 ? 812  GLN A OE1 1 
ATOM   6666  N  NE2 . GLN A 1 812  ? 35.967 50.590  -10.727 1.00 13.42 ? 812  GLN A NE2 1 
ATOM   6667  N  N   . PHE A 1 813  ? 34.284 52.803  -16.316 1.00 6.56  ? 813  PHE A N   1 
ATOM   6668  C  CA  . PHE A 1 813  ? 33.017 53.432  -16.674 1.00 5.79  ? 813  PHE A CA  1 
ATOM   6669  C  C   . PHE A 1 813  ? 31.901 52.528  -16.246 1.00 6.22  ? 813  PHE A C   1 
ATOM   6670  O  O   . PHE A 1 813  ? 31.908 51.301  -16.536 1.00 8.28  ? 813  PHE A O   1 
ATOM   6671  C  CB  . PHE A 1 813  ? 32.926 53.737  -18.171 1.00 5.58  ? 813  PHE A CB  1 
ATOM   6672  C  CG  . PHE A 1 813  ? 33.665 54.967  -18.543 1.00 6.34  ? 813  PHE A CG  1 
ATOM   6673  C  CD1 . PHE A 1 813  ? 35.036 54.968  -18.661 1.00 7.00  ? 813  PHE A CD1 1 
ATOM   6674  C  CD2 . PHE A 1 813  ? 32.965 56.159  -18.742 1.00 7.16  ? 813  PHE A CD2 1 
ATOM   6675  C  CE1 . PHE A 1 813  ? 35.725 56.174  -18.929 1.00 9.10  ? 813  PHE A CE1 1 
ATOM   6676  C  CE2 . PHE A 1 813  ? 33.649 57.329  -19.038 1.00 8.63  ? 813  PHE A CE2 1 
ATOM   6677  C  CZ  . PHE A 1 813  ? 35.005 57.323  -19.131 1.00 7.89  ? 813  PHE A CZ  1 
ATOM   6678  N  N   . ILE A 1 814  ? 30.929 53.087  -15.565 1.00 4.90  ? 814  ILE A N   1 
ATOM   6679  C  CA  . ILE A 1 814  ? 29.826 52.302  -15.044 1.00 5.12  ? 814  ILE A CA  1 
ATOM   6680  C  C   . ILE A 1 814  ? 28.526 52.722  -15.711 1.00 5.87  ? 814  ILE A C   1 
ATOM   6681  O  O   . ILE A 1 814  ? 28.299 53.929  -15.984 1.00 5.54  ? 814  ILE A O   1 
ATOM   6682  C  CB  . ILE A 1 814  ? 29.762 52.446  -13.492 1.00 6.33  ? 814  ILE A CB  1 
ATOM   6683  C  CG1 . ILE A 1 814  ? 28.719 51.502  -12.883 1.00 6.89  ? 814  ILE A CG1 1 
ATOM   6684  C  CG2 . ILE A 1 814  ? 29.514 53.864  -13.067 1.00 6.66  ? 814  ILE A CG2 1 
ATOM   6685  C  CD1 . ILE A 1 814  ? 28.841 51.349  -11.364 1.00 6.64  ? 814  ILE A CD1 1 
ATOM   6686  N  N   . LYS A 1 815  ? 27.683 51.736  -16.023 1.00 5.52  ? 815  LYS A N   1 
ATOM   6687  C  CA  A LYS A 1 815  ? 26.372 52.000  -16.567 0.50 5.64  ? 815  LYS A CA  1 
ATOM   6688  C  CA  B LYS A 1 815  ? 26.373 52.027  -16.567 0.50 6.08  ? 815  LYS A CA  1 
ATOM   6689  C  C   . LYS A 1 815  ? 25.467 52.634  -15.540 1.00 5.76  ? 815  LYS A C   1 
ATOM   6690  O  O   . LYS A 1 815  ? 25.350 52.135  -14.414 1.00 5.87  ? 815  LYS A O   1 
ATOM   6691  C  CB  A LYS A 1 815  ? 25.779 50.669  -17.038 0.50 6.35  ? 815  LYS A CB  1 
ATOM   6692  C  CB  B LYS A 1 815  ? 25.718 50.757  -17.110 0.50 6.62  ? 815  LYS A CB  1 
ATOM   6693  C  CG  A LYS A 1 815  ? 24.545 50.781  -17.911 0.50 7.27  ? 815  LYS A CG  1 
ATOM   6694  C  CG  B LYS A 1 815  ? 24.374 51.033  -17.811 0.50 6.71  ? 815  LYS A CG  1 
ATOM   6695  C  CD  A LYS A 1 815  ? 24.236 49.401  -18.495 0.50 8.47  ? 815  LYS A CD  1 
ATOM   6696  C  CD  B LYS A 1 815  ? 23.681 49.746  -18.230 0.50 8.72  ? 815  LYS A CD  1 
ATOM   6697  C  CE  A LYS A 1 815  ? 22.993 49.416  -19.346 0.50 13.55 ? 815  LYS A CE  1 
ATOM   6698  C  CE  B LYS A 1 815  ? 24.549 48.976  -19.191 0.50 9.46  ? 815  LYS A CE  1 
ATOM   6699  N  NZ  A LYS A 1 815  ? 22.665 48.010  -19.751 0.50 14.96 ? 815  LYS A NZ  1 
ATOM   6700  N  NZ  B LYS A 1 815  ? 23.864 47.698  -19.598 0.50 14.53 ? 815  LYS A NZ  1 
ATOM   6701  N  N   . ARG A 1 816  ? 24.811 53.710  -15.945 1.00 5.78  ? 816  ARG A N   1 
ATOM   6702  C  CA  . ARG A 1 816  ? 23.808 54.378  -15.161 1.00 5.97  ? 816  ARG A CA  1 
ATOM   6703  C  C   . ARG A 1 816  ? 22.477 54.266  -15.863 1.00 5.59  ? 816  ARG A C   1 
ATOM   6704  O  O   . ARG A 1 816  ? 22.416 54.231  -17.109 1.00 6.20  ? 816  ARG A O   1 
ATOM   6705  C  CB  . ARG A 1 816  ? 24.121 55.890  -15.038 1.00 7.33  ? 816  ARG A CB  1 
ATOM   6706  C  CG  . ARG A 1 816  ? 25.526 56.213  -14.526 1.00 6.33  ? 816  ARG A CG  1 
ATOM   6707  C  CD  . ARG A 1 816  ? 25.732 55.629  -13.182 1.00 6.97  ? 816  ARG A CD  1 
ATOM   6708  N  NE  . ARG A 1 816  ? 26.904 56.219  -12.546 1.00 5.48  ? 816  ARG A NE  1 
ATOM   6709  C  CZ  . ARG A 1 816  ? 27.292 55.825  -11.330 1.00 5.58  ? 816  ARG A CZ  1 
ATOM   6710  N  NH1 . ARG A 1 816  ? 26.619 54.882  -10.706 1.00 6.21  ? 816  ARG A NH1 1 
ATOM   6711  N  NH2 . ARG A 1 816  ? 28.331 56.419  -10.732 1.00 5.96  ? 816  ARG A NH2 1 
ATOM   6712  N  N   . ARG A 1 817  ? 21.426 54.276  -15.071 1.00 6.02  ? 817  ARG A N   1 
ATOM   6713  C  CA  . ARG A 1 817  ? 20.094 54.345  -15.661 1.00 7.04  ? 817  ARG A CA  1 
ATOM   6714  C  C   . ARG A 1 817  ? 19.348 55.461  -14.961 1.00 7.29  ? 817  ARG A C   1 
ATOM   6715  O  O   . ARG A 1 817  ? 19.215 55.485  -13.721 1.00 7.48  ? 817  ARG A O   1 
ATOM   6716  C  CB  . ARG A 1 817  ? 19.351 53.004  -15.470 1.00 6.91  ? 817  ARG A CB  1 
ATOM   6717  C  CG  . ARG A 1 817  ? 17.913 53.010  -15.976 1.00 8.55  ? 817  ARG A CG  1 
ATOM   6718  C  CD  . ARG A 1 817  ? 17.162 51.693  -15.723 1.00 9.88  ? 817  ARG A CD  1 
ATOM   6719  N  NE  . ARG A 1 817  ? 17.685 50.633  -16.572 1.00 11.37 ? 817  ARG A NE  1 
ATOM   6720  C  CZ  . ARG A 1 817  ? 18.427 49.617  -16.171 1.00 12.38 ? 817  ARG A CZ  1 
ATOM   6721  N  NH1 . ARG A 1 817  ? 18.792 49.488  -14.900 1.00 11.80 ? 817  ARG A NH1 1 
ATOM   6722  N  NH2 . ARG A 1 817  ? 18.821 48.722  -17.063 1.00 14.68 ? 817  ARG A NH2 1 
ATOM   6723  N  N   A ARG A 1 818  ? 18.885 56.404  -15.764 0.50 6.64  ? 818  ARG A N   1 
ATOM   6724  N  N   B ARG A 1 818  ? 18.885 56.404  -15.766 0.50 7.15  ? 818  ARG A N   1 
ATOM   6725  C  CA  A ARG A 1 818  ? 18.043 57.478  -15.273 0.50 7.88  ? 818  ARG A CA  1 
ATOM   6726  C  CA  B ARG A 1 818  ? 18.043 57.476  -15.275 0.50 8.90  ? 818  ARG A CA  1 
ATOM   6727  C  C   A ARG A 1 818  ? 16.748 56.862  -14.786 0.50 8.30  ? 818  ARG A C   1 
ATOM   6728  C  C   B ARG A 1 818  ? 16.748 56.861  -14.785 0.50 8.89  ? 818  ARG A C   1 
ATOM   6729  O  O   A ARG A 1 818  ? 16.146 56.084  -15.480 0.50 9.05  ? 818  ARG A O   1 
ATOM   6730  O  O   B ARG A 1 818  ? 16.146 56.083  -15.479 0.50 10.07 ? 818  ARG A O   1 
ATOM   6731  C  CB  A ARG A 1 818  ? 17.732 58.452  -16.415 0.50 7.40  ? 818  ARG A CB  1 
ATOM   6732  C  CB  B ARG A 1 818  ? 17.728 58.455  -16.414 0.50 8.69  ? 818  ARG A CB  1 
ATOM   6733  C  CG  A ARG A 1 818  ? 16.982 59.711  -15.990 0.50 7.53  ? 818  ARG A CG  1 
ATOM   6734  C  CG  B ARG A 1 818  ? 16.903 59.660  -15.977 0.50 9.81  ? 818  ARG A CG  1 
ATOM   6735  C  CD  A ARG A 1 818  ? 16.386 60.445  -17.201 0.50 7.76  ? 818  ARG A CD  1 
ATOM   6736  C  CD  B ARG A 1 818  ? 16.477 60.558  -17.143 0.50 9.88  ? 818  ARG A CD  1 
ATOM   6737  N  NE  A ARG A 1 818  ? 15.149 59.782  -17.589 0.50 10.14 ? 818  ARG A NE  1 
ATOM   6738  N  NE  B ARG A 1 818  ? 15.778 59.858  -18.209 0.50 14.67 ? 818  ARG A NE  1 
ATOM   6739  C  CZ  A ARG A 1 818  ? 14.912 59.200  -18.759 0.50 10.24 ? 818  ARG A CZ  1 
ATOM   6740  C  CZ  B ARG A 1 818  ? 16.322 59.540  -19.386 0.50 11.26 ? 818  ARG A CZ  1 
ATOM   6741  N  NH1 A ARG A 1 818  ? 15.797 59.218  -19.746 0.50 9.03  ? 818  ARG A NH1 1 
ATOM   6742  N  NH1 B ARG A 1 818  ? 17.602 59.831  -19.691 0.50 9.20  ? 818  ARG A NH1 1 
ATOM   6743  N  NH2 A ARG A 1 818  ? 13.732 58.599  -18.926 0.50 11.65 ? 818  ARG A NH2 1 
ATOM   6744  N  NH2 B ARG A 1 818  ? 15.583 58.914  -20.253 0.50 13.54 ? 818  ARG A NH2 1 
ATOM   6745  N  N   . LEU A 1 819  ? 16.335 57.225  -13.586 1.00 8.85  ? 819  LEU A N   1 
ATOM   6746  C  CA  . LEU A 1 819  ? 15.136 56.661  -12.990 1.00 9.83  ? 819  LEU A CA  1 
ATOM   6747  C  C   . LEU A 1 819  ? 14.151 57.763  -12.709 1.00 10.32 ? 819  LEU A C   1 
ATOM   6748  O  O   . LEU A 1 819  ? 14.394 58.648  -11.908 1.00 11.07 ? 819  LEU A O   1 
ATOM   6749  C  CB  . LEU A 1 819  ? 15.473 55.936  -11.687 1.00 10.27 ? 819  LEU A CB  1 
ATOM   6750  C  CG  . LEU A 1 819  ? 16.320 54.653  -11.870 1.00 11.34 ? 819  LEU A CG  1 
ATOM   6751  C  CD1 . LEU A 1 819  ? 16.765 54.129  -10.484 1.00 14.48 ? 819  LEU A CD1 1 
ATOM   6752  C  CD2 . LEU A 1 819  ? 15.631 53.562  -12.677 1.00 12.91 ? 819  LEU A CD2 1 
ATOM   6753  N  N   . ASP A 1 820  ? 13.015 57.684  -13.379 1.00 12.50 ? 820  ASP A N   1 
ATOM   6754  C  CA  . ASP A 1 820  ? 12.022 58.711  -13.123 1.00 13.25 ? 820  ASP A CA  1 
ATOM   6755  C  C   . ASP A 1 820  ? 11.322 58.584  -11.768 1.00 11.77 ? 820  ASP A C   1 
ATOM   6756  O  O   . ASP A 1 820  ? 10.691 59.539  -11.315 1.00 13.06 ? 820  ASP A O   1 
ATOM   6757  C  CB  . ASP A 1 820  ? 11.070 58.815  -14.305 1.00 15.08 ? 820  ASP A CB  1 
ATOM   6758  C  CG  . ASP A 1 820  ? 11.809 59.203  -15.600 1.00 19.69 ? 820  ASP A CG  1 
ATOM   6759  O  OD1 . ASP A 1 820  ? 12.850 59.952  -15.576 1.00 21.37 ? 820  ASP A OD1 1 
ATOM   6760  O  OD2 . ASP A 1 820  ? 11.429 58.780  -16.702 1.00 24.25 ? 820  ASP A OD2 1 
ATOM   6761  N  N   . LYS A 1 821  ? 11.495 57.442  -11.084 1.00 10.72 ? 821  LYS A N   1 
ATOM   6762  C  CA  . LYS A 1 821  ? 10.999 57.291  -9.713  1.00 11.24 ? 821  LYS A CA  1 
ATOM   6763  C  C   . LYS A 1 821  ? 11.870 58.070  -8.721  1.00 12.30 ? 821  LYS A C   1 
ATOM   6764  O  O   . LYS A 1 821  ? 11.488 58.206  -7.569  1.00 13.70 ? 821  LYS A O   1 
ATOM   6765  C  CB  . LYS A 1 821  ? 10.875 55.816  -9.276  1.00 11.41 ? 821  LYS A CB  1 
ATOM   6766  C  CG  . LYS A 1 821  ? 12.220 55.076  -9.161  1.00 10.40 ? 821  LYS A CG  1 
ATOM   6767  C  CD  . LYS A 1 821  ? 12.021 53.574  -9.019  1.00 11.87 ? 821  LYS A CD  1 
ATOM   6768  C  CE  . LYS A 1 821  ? 13.355 52.855  -9.140  1.00 11.65 ? 821  LYS A CE  1 
ATOM   6769  N  NZ  . LYS A 1 821  ? 13.220 51.388  -9.099  1.00 12.12 ? 821  LYS A NZ  1 
ATOM   6770  N  N   . LEU A 1 822  ? 13.019 58.597  -9.190  1.00 10.91 ? 822  LEU A N   1 
ATOM   6771  C  CA  . LEU A 1 822  ? 13.909 59.410  -8.335  1.00 11.31 ? 822  LEU A CA  1 
ATOM   6772  C  C   . LEU A 1 822  ? 13.895 60.839  -8.856  1.00 10.51 ? 822  LEU A C   1 
ATOM   6773  O  O   . LEU A 1 822  ? 13.712 61.038  -10.056 1.00 10.99 ? 822  LEU A O   1 
ATOM   6774  C  CB  . LEU A 1 822  ? 15.339 58.889  -8.378  1.00 11.86 ? 822  LEU A CB  1 
ATOM   6775  C  CG  . LEU A 1 822  ? 15.552 57.470  -7.843  1.00 13.13 ? 822  LEU A CG  1 
ATOM   6776  C  CD1 . LEU A 1 822  ? 17.026 57.153  -7.939  1.00 15.66 ? 822  LEU A CD1 1 
ATOM   6777  C  CD2 . LEU A 1 822  ? 15.014 57.292  -6.429  1.00 16.52 ? 822  LEU A CD2 1 
ATOM   6778  N  N   . PRO A 1 823  ? 14.098 61.805  -7.956  1.00 9.94  ? 823  PRO A N   1 
ATOM   6779  C  CA  . PRO A 1 823  ? 14.123 63.215  -8.367  1.00 9.96  ? 823  PRO A CA  1 
ATOM   6780  C  C   . PRO A 1 823  ? 15.359 63.519  -9.209  1.00 9.91  ? 823  PRO A C   1 
ATOM   6781  O  O   . PRO A 1 823  ? 16.333 62.766  -9.240  1.00 8.89  ? 823  PRO A O   1 
ATOM   6782  C  CB  . PRO A 1 823  ? 14.132 63.982  -7.049  1.00 11.49 ? 823  PRO A CB  1 
ATOM   6783  C  CG  . PRO A 1 823  ? 14.732 63.031  -6.034  1.00 12.59 ? 823  PRO A CG  1 
ATOM   6784  C  CD  . PRO A 1 823  ? 14.304 61.628  -6.500  1.00 10.65 ? 823  PRO A CD  1 
ATOM   6785  N  N   . LEU A 1 824  ? 15.317 64.660  -9.903  1.00 9.30  ? 824  LEU A N   1 
ATOM   6786  C  CA  . LEU A 1 824  ? 16.378 65.072  -10.796 1.00 9.76  ? 824  LEU A CA  1 
ATOM   6787  C  C   . LEU A 1 824  ? 17.786 64.926  -10.174 1.00 8.83  ? 824  LEU A C   1 
ATOM   6788  O  O   . LEU A 1 824  ? 18.703 64.392  -10.801 1.00 8.52  ? 824  LEU A O   1 
ATOM   6789  C  CB  . LEU A 1 824  ? 16.079 66.533  -11.216 1.00 10.61 ? 824  LEU A CB  1 
ATOM   6790  C  CG  . LEU A 1 824  ? 16.869 67.198  -12.323 1.00 10.79 ? 824  LEU A CG  1 
ATOM   6791  C  CD1 . LEU A 1 824  ? 16.073 68.393  -12.891 1.00 12.39 ? 824  LEU A CD1 1 
ATOM   6792  C  CD2 . LEU A 1 824  ? 18.260 67.655  -11.856 1.00 9.96  ? 824  LEU A CD2 1 
ATOM   6793  N  N   . GLN A 1 825  ? 17.925 65.404  -8.952  1.00 7.93  ? 825  GLN A N   1 
ATOM   6794  C  CA  . GLN A 1 825  ? 19.244 65.465  -8.328  1.00 7.78  ? 825  GLN A CA  1 
ATOM   6795  C  C   . GLN A 1 825  ? 19.791 64.105  -7.984  1.00 7.54  ? 825  GLN A C   1 
ATOM   6796  O  O   . GLN A 1 825  ? 21.016 63.971  -7.774  1.00 7.27  ? 825  GLN A O   1 
ATOM   6797  C  CB  . GLN A 1 825  ? 19.186 66.364  -7.109  1.00 8.69  ? 825  GLN A CB  1 
ATOM   6798  C  CG  . GLN A 1 825  ? 18.251 65.856  -5.993  1.00 7.64  ? 825  GLN A CG  1 
ATOM   6799  C  CD  . GLN A 1 825  ? 16.794 66.323  -6.095  1.00 8.90  ? 825  GLN A CD  1 
ATOM   6800  O  OE1 . GLN A 1 825  ? 16.331 66.769  -7.148  1.00 9.50  ? 825  GLN A OE1 1 
ATOM   6801  N  NE2 . GLN A 1 825  ? 16.098 66.244  -4.984  1.00 9.33  ? 825  GLN A NE2 1 
ATOM   6802  N  N   . ALA A 1 826  ? 18.926 63.088  -7.934  1.00 6.89  ? 826  ALA A N   1 
ATOM   6803  C  CA  . ALA A 1 826  ? 19.391 61.721  -7.690  1.00 6.75  ? 826  ALA A CA  1 
ATOM   6804  C  C   . ALA A 1 826  ? 19.957 61.127  -8.946  1.00 6.93  ? 826  ALA A C   1 
ATOM   6805  O  O   . ALA A 1 826  ? 20.667 60.128  -8.890  1.00 8.49  ? 826  ALA A O   1 
ATOM   6806  C  CB  . ALA A 1 826  ? 18.206 60.853  -7.244  1.00 7.64  ? 826  ALA A CB  1 
ATOM   6807  N  N   . ASN A 1 827  ? 19.598 61.698  -10.096 1.00 6.65  ? 827  ASN A N   1 
ATOM   6808  C  CA  . ASN A 1 827  ? 20.081 61.220  -11.399 1.00 6.73  ? 827  ASN A CA  1 
ATOM   6809  C  C   . ASN A 1 827  ? 21.394 61.864  -11.845 1.00 6.02  ? 827  ASN A C   1 
ATOM   6810  O  O   . ASN A 1 827  ? 21.903 61.588  -12.897 1.00 7.69  ? 827  ASN A O   1 
ATOM   6811  C  CB  . ASN A 1 827  ? 18.971 61.329  -12.464 1.00 8.38  ? 827  ASN A CB  1 
ATOM   6812  C  CG  . ASN A 1 827  ? 17.852 60.323  -12.200 1.00 11.44 ? 827  ASN A CG  1 
ATOM   6813  O  OD1 . ASN A 1 827  ? 18.061 59.128  -12.220 1.00 10.13 ? 827  ASN A OD1 1 
ATOM   6814  N  ND2 . ASN A 1 827  ? 16.663 60.824  -11.922 1.00 13.84 ? 827  ASN A ND2 1 
ATOM   6815  N  N   . TYR A 1 828  ? 21.911 62.709  -10.949 1.00 6.07  ? 828  TYR A N   1 
ATOM   6816  C  CA  . TYR A 1 828  ? 23.235 63.302  -11.100 1.00 5.76  ? 828  TYR A CA  1 
ATOM   6817  C  C   . TYR A 1 828  ? 24.266 62.397  -10.502 1.00 5.87  ? 828  TYR A C   1 
ATOM   6818  O  O   . TYR A 1 828  ? 24.028 61.814  -9.431  1.00 6.49  ? 828  TYR A O   1 
ATOM   6819  C  CB  . TYR A 1 828  ? 23.300 64.676  -10.411 1.00 6.75  ? 828  TYR A CB  1 
ATOM   6820  C  CG  . TYR A 1 828  ? 23.277 65.810  -11.407 1.00 5.94  ? 828  TYR A CG  1 
ATOM   6821  C  CD1 . TYR A 1 828  ? 22.190 66.042  -12.251 1.00 6.52  ? 828  TYR A CD1 1 
ATOM   6822  C  CD2 . TYR A 1 828  ? 24.372 66.643  -11.501 1.00 7.38  ? 828  TYR A CD2 1 
ATOM   6823  C  CE1 . TYR A 1 828  ? 22.240 67.090  -13.206 1.00 9.01  ? 828  TYR A CE1 1 
ATOM   6824  C  CE2 . TYR A 1 828  ? 24.426 67.660  -12.396 1.00 8.92  ? 828  TYR A CE2 1 
ATOM   6825  C  CZ  . TYR A 1 828  ? 23.374 67.879  -13.254 1.00 6.95  ? 828  TYR A CZ  1 
ATOM   6826  O  OH  . TYR A 1 828  ? 23.522 68.919  -14.133 1.00 9.74  ? 828  TYR A OH  1 
ATOM   6827  N  N   . TYR A 1 829  ? 25.391 62.273  -11.195 1.00 4.65  ? 829  TYR A N   1 
ATOM   6828  C  CA  . TYR A 1 829  ? 26.472 61.389  -10.755 1.00 5.73  ? 829  TYR A CA  1 
ATOM   6829  C  C   . TYR A 1 829  ? 27.785 62.104  -10.897 1.00 6.17  ? 829  TYR A C   1 
ATOM   6830  O  O   . TYR A 1 829  ? 27.871 63.100  -11.606 1.00 6.11  ? 829  TYR A O   1 
ATOM   6831  C  CB  . TYR A 1 829  ? 26.529 60.107  -11.610 1.00 5.43  ? 829  TYR A CB  1 
ATOM   6832  C  CG  . TYR A 1 829  ? 25.345 59.216  -11.341 1.00 5.26  ? 829  TYR A CG  1 
ATOM   6833  C  CD1 . TYR A 1 829  ? 25.364 58.339  -10.264 1.00 6.30  ? 829  TYR A CD1 1 
ATOM   6834  C  CD2 . TYR A 1 829  ? 24.181 59.265  -12.135 1.00 7.51  ? 829  TYR A CD2 1 
ATOM   6835  C  CE1 . TYR A 1 829  ? 24.275 57.525  -9.966  1.00 6.95  ? 829  TYR A CE1 1 
ATOM   6836  C  CE2 . TYR A 1 829  ? 23.107 58.447  -11.833 1.00 7.15  ? 829  TYR A CE2 1 
ATOM   6837  C  CZ  . TYR A 1 829  ? 23.157 57.586  -10.764 1.00 6.90  ? 829  TYR A CZ  1 
ATOM   6838  O  OH  . TYR A 1 829  ? 22.077 56.753  -10.465 1.00 7.58  ? 829  TYR A OH  1 
ATOM   6839  N  N   . PRO A 1 830  ? 28.824 61.631  -10.232 1.00 5.65  ? 830  PRO A N   1 
ATOM   6840  C  CA  . PRO A 1 830  ? 30.115 62.273  -10.418 1.00 5.56  ? 830  PRO A CA  1 
ATOM   6841  C  C   . PRO A 1 830  ? 30.610 61.997  -11.823 1.00 5.86  ? 830  PRO A C   1 
ATOM   6842  O  O   . PRO A 1 830  ? 30.397 60.882  -12.368 1.00 6.78  ? 830  PRO A O   1 
ATOM   6843  C  CB  . PRO A 1 830  ? 31.024 61.597  -9.353  1.00 8.07  ? 830  PRO A CB  1 
ATOM   6844  C  CG  . PRO A 1 830  ? 30.199 60.610  -8.635  1.00 9.10  ? 830  PRO A CG  1 
ATOM   6845  C  CD  . PRO A 1 830  ? 28.843 60.489  -9.293  1.00 6.18  ? 830  PRO A CD  1 
ATOM   6846  N  N   . ILE A 1 831  ? 31.223 63.019  -12.433 1.00 5.13  ? 831  ILE A N   1 
ATOM   6847  C  CA  . ILE A 1 831  ? 31.898 62.866  -13.720 1.00 5.66  ? 831  ILE A CA  1 
ATOM   6848  C  C   . ILE A 1 831  ? 33.348 63.190  -13.498 1.00 7.07  ? 831  ILE A C   1 
ATOM   6849  O  O   . ILE A 1 831  ? 33.812 64.285  -13.814 1.00 6.11  ? 831  ILE A O   1 
ATOM   6850  C  CB  . ILE A 1 831  ? 31.304 63.796  -14.822 1.00 5.20  ? 831  ILE A CB  1 
ATOM   6851  C  CG1 . ILE A 1 831  ? 29.778 63.830  -14.795 1.00 6.59  ? 831  ILE A CG1 1 
ATOM   6852  C  CG2 . ILE A 1 831  ? 31.847 63.384  -16.185 1.00 6.68  ? 831  ILE A CG2 1 
ATOM   6853  C  CD1 . ILE A 1 831  ? 29.087 62.557  -15.144 1.00 6.33  ? 831  ILE A CD1 1 
ATOM   6854  N  N   . PRO A 1 832  ? 34.070 62.262  -12.894 1.00 5.95  ? 832  PRO A N   1 
ATOM   6855  C  CA  . PRO A 1 832  ? 35.474 62.516  -12.578 1.00 6.24  ? 832  PRO A CA  1 
ATOM   6856  C  C   . PRO A 1 832  ? 36.361 62.575  -13.766 1.00 7.41  ? 832  PRO A C   1 
ATOM   6857  O  O   . PRO A 1 832  ? 37.403 63.196  -13.615 1.00 11.42 ? 832  PRO A O   1 
ATOM   6858  C  CB  . PRO A 1 832  ? 35.867 61.409  -11.558 1.00 6.91  ? 832  PRO A CB  1 
ATOM   6859  C  CG  . PRO A 1 832  ? 34.834 60.389  -11.715 1.00 8.26  ? 832  PRO A CG  1 
ATOM   6860  C  CD  . PRO A 1 832  ? 33.596 60.980  -12.342 1.00 7.84  ? 832  PRO A CD  1 
ATOM   6861  N  N   A SER A 1 833  ? 35.998 62.010  -14.915 0.50 6.43  ? 833  SER A N   1 
ATOM   6862  N  N   B SER A 1 833  ? 36.008 61.967  -14.897 0.50 7.06  ? 833  SER A N   1 
ATOM   6863  C  CA  A SER A 1 833  ? 36.847 62.131  -16.106 0.50 5.50  ? 833  SER A CA  1 
ATOM   6864  C  CA  B SER A 1 833  ? 36.869 61.987  -16.085 0.50 6.79  ? 833  SER A CA  1 
ATOM   6865  C  C   A SER A 1 833  ? 36.124 61.908  -17.431 0.50 4.89  ? 833  SER A C   1 
ATOM   6866  C  C   B SER A 1 833  ? 36.089 61.981  -17.387 0.50 5.52  ? 833  SER A C   1 
ATOM   6867  O  O   A SER A 1 833  ? 36.689 62.147  -18.502 0.50 4.25  ? 833  SER A O   1 
ATOM   6868  O  O   B SER A 1 833  ? 36.573 62.447  -18.400 0.50 4.25  ? 833  SER A O   1 
ATOM   6869  C  CB  A SER A 1 833  ? 38.076 61.209  -16.039 0.50 5.72  ? 833  SER A CB  1 
ATOM   6870  C  CB  B SER A 1 833  ? 37.842 60.797  -16.118 0.50 7.40  ? 833  SER A CB  1 
ATOM   6871  O  OG  A SER A 1 833  ? 37.738 59.858  -16.309 0.50 5.44  ? 833  SER A OG  1 
ATOM   6872  O  OG  B SER A 1 833  ? 38.680 60.753  -14.985 0.50 11.25 ? 833  SER A OG  1 
ATOM   6873  N  N   . GLY A 1 834  ? 34.889 61.439  -17.369 1.00 5.22  ? 834  GLY A N   1 
ATOM   6874  C  CA  . GLY A 1 834  ? 34.118 61.416  -18.598 1.00 5.36  ? 834  GLY A CA  1 
ATOM   6875  C  C   . GLY A 1 834  ? 32.767 60.779  -18.470 1.00 4.97  ? 834  GLY A C   1 
ATOM   6876  O  O   . GLY A 1 834  ? 32.414 60.136  -17.468 1.00 5.30  ? 834  GLY A O   1 
ATOM   6877  N  N   . MET A 1 835  ? 32.014 60.867  -19.550 1.00 5.33  ? 835  MET A N   1 
ATOM   6878  C  CA  . MET A 1 835  ? 30.680 60.300  -19.590 1.00 5.69  ? 835  MET A CA  1 
ATOM   6879  C  C   . MET A 1 835  ? 30.341 60.072  -21.055 1.00 5.42  ? 835  MET A C   1 
ATOM   6880  O  O   . MET A 1 835  ? 30.900 60.714  -21.920 1.00 6.06  ? 835  MET A O   1 
ATOM   6881  C  CB  . MET A 1 835  ? 29.668 61.266  -18.958 1.00 5.85  ? 835  MET A CB  1 
ATOM   6882  C  CG  . MET A 1 835  ? 29.555 62.586  -19.716 1.00 7.37  ? 835  MET A CG  1 
ATOM   6883  S  SD  . MET A 1 835  ? 28.646 63.887  -18.835 1.00 11.50 ? 835  MET A SD  1 
ATOM   6884  C  CE  . MET A 1 835  ? 27.178 63.006  -18.362 1.00 11.84 ? 835  MET A CE  1 
ATOM   6885  N  N   . PHE A 1 836  ? 29.425 59.143  -21.311 1.00 4.82  ? 836  PHE A N   1 
ATOM   6886  C  CA  . PHE A 1 836  ? 29.014 58.894  -22.703 1.00 5.54  ? 836  PHE A CA  1 
ATOM   6887  C  C   . PHE A 1 836  ? 27.588 58.401  -22.766 1.00 6.15  ? 836  PHE A C   1 
ATOM   6888  O  O   . PHE A 1 836  ? 27.049 57.839  -21.800 1.00 5.54  ? 836  PHE A O   1 
ATOM   6889  C  CB  . PHE A 1 836  ? 29.977 58.030  -23.512 1.00 5.63  ? 836  PHE A CB  1 
ATOM   6890  C  CG  . PHE A 1 836  ? 30.176 56.599  -23.053 1.00 6.55  ? 836  PHE A CG  1 
ATOM   6891  C  CD1 . PHE A 1 836  ? 29.369 55.572  -23.554 1.00 7.57  ? 836  PHE A CD1 1 
ATOM   6892  C  CD2 . PHE A 1 836  ? 31.281 56.257  -22.305 1.00 7.18  ? 836  PHE A CD2 1 
ATOM   6893  C  CE1 . PHE A 1 836  ? 29.613 54.234  -23.189 1.00 8.41  ? 836  PHE A CE1 1 
ATOM   6894  C  CE2 . PHE A 1 836  ? 31.528 54.895  -21.949 1.00 6.77  ? 836  PHE A CE2 1 
ATOM   6895  C  CZ  . PHE A 1 836  ? 30.690 53.899  -22.417 1.00 8.02  ? 836  PHE A CZ  1 
ATOM   6896  N  N   . ILE A 1 837  ? 26.979 58.638  -23.947 1.00 5.68  ? 837  ILE A N   1 
ATOM   6897  C  CA  . ILE A 1 837  ? 25.692 58.010  -24.299 1.00 7.16  ? 837  ILE A CA  1 
ATOM   6898  C  C   . ILE A 1 837  ? 25.898 57.325  -25.624 1.00 6.60  ? 837  ILE A C   1 
ATOM   6899  O  O   . ILE A 1 837  ? 26.748 57.732  -26.424 1.00 6.88  ? 837  ILE A O   1 
ATOM   6900  C  CB  . ILE A 1 837  ? 24.526 59.013  -24.373 1.00 6.95  ? 837  ILE A CB  1 
ATOM   6901  C  CG1 . ILE A 1 837  ? 24.914 60.237  -25.197 1.00 8.02  ? 837  ILE A CG1 1 
ATOM   6902  C  CG2 . ILE A 1 837  ? 24.067 59.403  -22.991 1.00 6.83  ? 837  ILE A CG2 1 
ATOM   6903  C  CD1 . ILE A 1 837  ? 23.715 61.157  -25.584 1.00 7.91  ? 837  ILE A CD1 1 
ATOM   6904  N  N   . GLU A 1 838  ? 25.128 56.263  -25.850 1.00 7.00  ? 838  GLU A N   1 
ATOM   6905  C  CA  . GLU A 1 838  ? 25.239 55.561  -27.127 1.00 7.52  ? 838  GLU A CA  1 
ATOM   6906  C  C   . GLU A 1 838  ? 23.933 54.905  -27.487 1.00 8.36  ? 838  GLU A C   1 
ATOM   6907  O  O   . GLU A 1 838  ? 23.089 54.647  -26.645 1.00 7.64  ? 838  GLU A O   1 
ATOM   6908  C  CB  . GLU A 1 838  ? 26.339 54.512  -27.119 1.00 7.93  ? 838  GLU A CB  1 
ATOM   6909  C  CG  . GLU A 1 838  ? 26.139 53.441  -26.079 1.00 9.33  ? 838  GLU A CG  1 
ATOM   6910  C  CD  . GLU A 1 838  ? 27.233 52.402  -26.091 1.00 13.39 ? 838  GLU A CD  1 
ATOM   6911  O  OE1 . GLU A 1 838  ? 28.261 52.559  -26.798 1.00 14.09 ? 838  GLU A OE1 1 
ATOM   6912  O  OE2 . GLU A 1 838  ? 27.054 51.373  -25.403 1.00 14.07 ? 838  GLU A OE2 1 
ATOM   6913  N  N   . ASP A 1 839  ? 23.833 54.602  -28.782 1.00 8.48  ? 839  ASP A N   1 
ATOM   6914  C  CA  . ASP A 1 839  ? 22.791 53.680  -29.250 1.00 8.53  ? 839  ASP A CA  1 
ATOM   6915  C  C   . ASP A 1 839  ? 23.466 52.605  -30.079 1.00 8.53  ? 839  ASP A C   1 
ATOM   6916  O  O   . ASP A 1 839  ? 24.660 52.376  -29.954 1.00 10.06 ? 839  ASP A O   1 
ATOM   6917  C  CB  . ASP A 1 839  ? 21.638 54.389  -29.970 1.00 8.82  ? 839  ASP A CB  1 
ATOM   6918  C  CG  . ASP A 1 839  ? 22.060 55.140  -31.231 1.00 10.33 ? 839  ASP A CG  1 
ATOM   6919  O  OD1 . ASP A 1 839  ? 23.101 54.802  -31.816 1.00 11.58 ? 839  ASP A OD1 1 
ATOM   6920  O  OD2 . ASP A 1 839  ? 21.350 56.085  -31.672 1.00 15.57 ? 839  ASP A OD2 1 
ATOM   6921  N  N   . ALA A 1 840  ? 22.691 51.881  -30.899 1.00 9.97  ? 840  ALA A N   1 
ATOM   6922  C  CA  . ALA A 1 840  ? 23.291 50.815  -31.687 1.00 11.69 ? 840  ALA A CA  1 
ATOM   6923  C  C   . ALA A 1 840  ? 24.400 51.305  -32.606 1.00 10.99 ? 840  ALA A C   1 
ATOM   6924  O  O   . ALA A 1 840  ? 25.338 50.586  -32.893 1.00 12.84 ? 840  ALA A O   1 
ATOM   6925  C  CB  . ALA A 1 840  ? 22.227 50.079  -32.513 1.00 12.48 ? 840  ALA A CB  1 
ATOM   6926  N  N   . ASN A 1 841  ? 24.269 52.538  -33.086 1.00 10.12 ? 841  ASN A N   1 
ATOM   6927  C  CA  . ASN A 1 841  ? 25.147 53.054  -34.140 1.00 9.62  ? 841  ASN A CA  1 
ATOM   6928  C  C   . ASN A 1 841  ? 26.131 54.150  -33.778 1.00 8.48  ? 841  ASN A C   1 
ATOM   6929  O  O   . ASN A 1 841  ? 27.188 54.234  -34.378 1.00 9.81  ? 841  ASN A O   1 
ATOM   6930  C  CB  . ASN A 1 841  ? 24.305 53.523  -35.328 1.00 10.16 ? 841  ASN A CB  1 
ATOM   6931  C  CG  . ASN A 1 841  ? 23.542 52.390  -35.954 1.00 12.16 ? 841  ASN A CG  1 
ATOM   6932  O  OD1 . ASN A 1 841  ? 24.070 51.297  -36.101 1.00 14.82 ? 841  ASN A OD1 1 
ATOM   6933  N  ND2 . ASN A 1 841  ? 22.282 52.640  -36.278 1.00 16.00 ? 841  ASN A ND2 1 
ATOM   6934  N  N   . THR A 1 842  ? 25.748 54.974  -32.801 1.00 8.80  ? 842  THR A N   1 
ATOM   6935  C  CA  . THR A 1 842  ? 26.464 56.222  -32.518 1.00 8.83  ? 842  THR A CA  1 
ATOM   6936  C  C   . THR A 1 842  ? 26.761 56.331  -31.026 1.00 7.31  ? 842  THR A C   1 
ATOM   6937  O  O   . THR A 1 842  ? 25.915 55.967  -30.221 1.00 9.02  ? 842  THR A O   1 
ATOM   6938  C  CB  . THR A 1 842  ? 25.572 57.391  -32.938 1.00 9.52  ? 842  THR A CB  1 
ATOM   6939  O  OG1 . THR A 1 842  ? 25.217 57.223  -34.329 1.00 12.57 ? 842  THR A OG1 1 
ATOM   6940  C  CG2 . THR A 1 842  ? 26.322 58.741  -32.898 1.00 11.80 ? 842  THR A CG2 1 
ATOM   6941  N  N   . ARG A 1 843  ? 27.939 56.895  -30.710 1.00 7.58  ? 843  ARG A N   1 
ATOM   6942  C  CA  . ARG A 1 843  ? 28.268 57.243  -29.310 1.00 7.08  ? 843  ARG A CA  1 
ATOM   6943  C  C   . ARG A 1 843  ? 28.774 58.671  -29.275 1.00 6.87  ? 843  ARG A C   1 
ATOM   6944  O  O   . ARG A 1 843  ? 29.497 59.094  -30.188 1.00 7.95  ? 843  ARG A O   1 
ATOM   6945  C  CB  . ARG A 1 843  ? 29.337 56.295  -28.774 1.00 7.41  ? 843  ARG A CB  1 
ATOM   6946  C  CG  . ARG A 1 843  ? 29.762 56.546  -27.327 1.00 7.27  ? 843  ARG A CG  1 
ATOM   6947  C  CD  . ARG A 1 843  ? 30.928 55.711  -26.943 1.00 7.45  ? 843  ARG A CD  1 
ATOM   6948  N  NE  . ARG A 1 843  ? 30.537 54.328  -26.655 1.00 8.22  ? 843  ARG A NE  1 
ATOM   6949  C  CZ  . ARG A 1 843  ? 31.357 53.479  -26.061 1.00 8.41  ? 843  ARG A CZ  1 
ATOM   6950  N  NH1 . ARG A 1 843  ? 32.585 53.865  -25.728 1.00 7.34  ? 843  ARG A NH1 1 
ATOM   6951  N  NH2 . ARG A 1 843  ? 30.939 52.256  -25.753 1.00 8.89  ? 843  ARG A NH2 1 
ATOM   6952  N  N   . LEU A 1 844  ? 28.397 59.378  -28.206 1.00 6.20  ? 844  LEU A N   1 
ATOM   6953  C  CA  . LEU A 1 844  ? 28.979 60.697  -27.919 1.00 6.88  ? 844  LEU A CA  1 
ATOM   6954  C  C   . LEU A 1 844  ? 29.628 60.624  -26.530 1.00 6.30  ? 844  LEU A C   1 
ATOM   6955  O  O   . LEU A 1 844  ? 28.935 60.310  -25.556 1.00 7.09  ? 844  LEU A O   1 
ATOM   6956  C  CB  . LEU A 1 844  ? 27.933 61.801  -27.948 1.00 8.04  ? 844  LEU A CB  1 
ATOM   6957  C  CG  . LEU A 1 844  ? 28.532 63.235  -27.830 1.00 8.86  ? 844  LEU A CG  1 
ATOM   6958  C  CD1 . LEU A 1 844  ? 29.416 63.601  -29.019 1.00 12.10 ? 844  LEU A CD1 1 
ATOM   6959  C  CD2 . LEU A 1 844  ? 27.390 64.235  -27.663 1.00 11.65 ? 844  LEU A CD2 1 
ATOM   6960  N  N   . THR A 1 845  ? 30.936 60.862  -26.503 1.00 5.92  ? 845  THR A N   1 
ATOM   6961  C  CA  . THR A 1 845  ? 31.706 60.813  -25.250 1.00 5.85  ? 845  THR A CA  1 
ATOM   6962  C  C   . THR A 1 845  ? 32.230 62.221  -24.969 1.00 5.40  ? 845  THR A C   1 
ATOM   6963  O  O   . THR A 1 845  ? 32.823 62.862  -25.844 1.00 6.50  ? 845  THR A O   1 
ATOM   6964  C  CB  . THR A 1 845  ? 32.900 59.889  -25.384 1.00 5.27  ? 845  THR A CB  1 
ATOM   6965  O  OG1 . THR A 1 845  ? 32.461 58.573  -25.814 1.00 7.87  ? 845  THR A OG1 1 
ATOM   6966  C  CG2 . THR A 1 845  ? 33.603 59.647  -24.020 1.00 7.74  ? 845  THR A CG2 1 
ATOM   6967  N  N   . LEU A 1 846  ? 32.005 62.672  -23.746 1.00 6.25  ? 846  LEU A N   1 
ATOM   6968  C  CA  . LEU A 1 846  ? 32.561 63.940  -23.267 1.00 6.05  ? 846  LEU A CA  1 
ATOM   6969  C  C   . LEU A 1 846  ? 33.634 63.608  -22.222 1.00 5.63  ? 846  LEU A C   1 
ATOM   6970  O  O   . LEU A 1 846  ? 33.292 63.002  -21.191 1.00 5.93  ? 846  LEU A O   1 
ATOM   6971  C  CB  . LEU A 1 846  ? 31.472 64.825  -22.677 1.00 7.83  ? 846  LEU A CB  1 
ATOM   6972  C  CG  . LEU A 1 846  ? 31.934 66.197  -22.187 1.00 8.23  ? 846  LEU A CG  1 
ATOM   6973  C  CD1 . LEU A 1 846  ? 32.409 67.043  -23.373 1.00 11.32 ? 846  LEU A CD1 1 
ATOM   6974  C  CD2 . LEU A 1 846  ? 30.790 66.910  -21.496 1.00 12.08 ? 846  LEU A CD2 1 
ATOM   6975  N  N   . LEU A 1 847  ? 34.889 63.924  -22.490 1.00 5.65  ? 847  LEU A N   1 
ATOM   6976  C  CA  . LEU A 1 847  ? 35.977 63.716  -21.509 1.00 4.43  ? 847  LEU A CA  1 
ATOM   6977  C  C   . LEU A 1 847  ? 36.201 65.029  -20.790 1.00 6.16  ? 847  LEU A C   1 
ATOM   6978  O  O   . LEU A 1 847  ? 36.094 66.097  -21.409 1.00 5.60  ? 847  LEU A O   1 
ATOM   6979  C  CB  . LEU A 1 847  ? 37.277 63.277  -22.172 1.00 5.09  ? 847  LEU A CB  1 
ATOM   6980  C  CG  . LEU A 1 847  ? 37.237 61.924  -22.876 1.00 5.45  ? 847  LEU A CG  1 
ATOM   6981  C  CD1 . LEU A 1 847  ? 36.624 60.779  -22.046 1.00 6.40  ? 847  LEU A CD1 1 
ATOM   6982  C  CD2 . LEU A 1 847  ? 36.580 62.017  -24.271 1.00 6.12  ? 847  LEU A CD2 1 
ATOM   6983  N  N   . THR A 1 848  ? 36.570 64.965  -19.509 1.00 4.90  ? 848  THR A N   1 
ATOM   6984  C  CA  A THR A 1 848  ? 36.770 66.200  -18.711 0.50 5.40  ? 848  THR A CA  1 
ATOM   6985  C  CA  B THR A 1 848  ? 36.735 66.168  -18.708 0.50 5.36  ? 848  THR A CA  1 
ATOM   6986  C  C   . THR A 1 848  ? 38.156 66.271  -18.115 1.00 6.76  ? 848  THR A C   1 
ATOM   6987  O  O   . THR A 1 848  ? 38.794 65.240  -17.809 1.00 7.11  ? 848  THR A O   1 
ATOM   6988  C  CB  A THR A 1 848  ? 35.860 66.322  -17.508 0.50 7.03  ? 848  THR A CB  1 
ATOM   6989  C  CB  B THR A 1 848  ? 35.679 66.158  -17.623 0.50 6.53  ? 848  THR A CB  1 
ATOM   6990  O  OG1 A THR A 1 848  ? 36.166 65.244  -16.605 0.50 6.37  ? 848  THR A OG1 1 
ATOM   6991  O  OG1 B THR A 1 848  ? 34.389 65.862  -18.177 0.50 12.02 ? 848  THR A OG1 1 
ATOM   6992  C  CG2 A THR A 1 848  ? 34.410 66.173  -17.815 0.50 8.77  ? 848  THR A CG2 1 
ATOM   6993  C  CG2 B THR A 1 848  ? 35.546 67.512  -16.998 0.50 3.79  ? 848  THR A CG2 1 
ATOM   6994  N  N   . GLY A 1 849  ? 38.632 67.499  -17.939 1.00 5.87  ? 849  GLY A N   1 
ATOM   6995  C  CA  . GLY A 1 849  ? 39.893 67.725  -17.281 1.00 5.33  ? 849  GLY A CA  1 
ATOM   6996  C  C   . GLY A 1 849  ? 39.729 68.091  -15.809 1.00 5.04  ? 849  GLY A C   1 
ATOM   6997  O  O   . GLY A 1 849  ? 40.682 68.528  -15.186 1.00 5.03  ? 849  GLY A O   1 
ATOM   6998  N  N   . GLN A 1 850  ? 38.522 67.957  -15.285 1.00 4.57  ? 850  GLN A N   1 
ATOM   6999  C  CA  . GLN A 1 850  ? 38.206 68.264  -13.889 1.00 4.41  ? 850  GLN A CA  1 
ATOM   7000  C  C   . GLN A 1 850  ? 36.954 67.490  -13.513 1.00 4.35  ? 850  GLN A C   1 
ATOM   7001  O  O   . GLN A 1 850  ? 36.072 67.286  -14.353 1.00 5.18  ? 850  GLN A O   1 
ATOM   7002  C  CB  . GLN A 1 850  ? 37.955 69.779  -13.727 1.00 5.73  ? 850  GLN A CB  1 
ATOM   7003  C  CG  . GLN A 1 850  ? 36.827 70.389  -14.636 1.00 5.31  ? 850  GLN A CG  1 
ATOM   7004  C  CD  . GLN A 1 850  ? 37.225 70.507  -16.116 1.00 5.21  ? 850  GLN A CD  1 
ATOM   7005  O  OE1 . GLN A 1 850  ? 38.336 70.921  -16.443 1.00 6.48  ? 850  GLN A OE1 1 
ATOM   7006  N  NE2 . GLN A 1 850  ? 36.300 70.158  -16.994 1.00 5.12  ? 850  GLN A NE2 1 
ATOM   7007  N  N   . PRO A 1 851  ? 36.831 67.061  -12.266 1.00 4.06  ? 851  PRO A N   1 
ATOM   7008  C  CA  . PRO A 1 851  ? 35.604 66.367  -11.837 1.00 4.33  ? 851  PRO A CA  1 
ATOM   7009  C  C   . PRO A 1 851  ? 34.482 67.345  -11.650 1.00 4.32  ? 851  PRO A C   1 
ATOM   7010  O  O   . PRO A 1 851  ? 34.650 68.387  -10.999 1.00 4.85  ? 851  PRO A O   1 
ATOM   7011  C  CB  . PRO A 1 851  ? 36.003 65.732  -10.478 1.00 5.45  ? 851  PRO A CB  1 
ATOM   7012  C  CG  . PRO A 1 851  ? 37.104 66.664  -9.940  1.00 4.21  ? 851  PRO A CG  1 
ATOM   7013  C  CD  . PRO A 1 851  ? 37.824 67.147  -11.183 1.00 4.65  ? 851  PRO A CD  1 
ATOM   7014  N  N   . LEU A 1 852  ? 33.328 66.999  -12.211 1.00 4.77  ? 852  LEU A N   1 
ATOM   7015  C  CA  . LEU A 1 852  ? 32.129 67.808  -12.096 1.00 5.69  ? 852  LEU A CA  1 
ATOM   7016  C  C   . LEU A 1 852  ? 30.906 66.896  -12.006 1.00 7.15  ? 852  LEU A C   1 
ATOM   7017  O  O   . LEU A 1 852  ? 31.037 65.699  -12.159 1.00 10.79 ? 852  LEU A O   1 
ATOM   7018  C  CB  . LEU A 1 852  ? 31.994 68.709  -13.334 1.00 6.31  ? 852  LEU A CB  1 
ATOM   7019  C  CG  . LEU A 1 852  ? 33.106 69.764  -13.503 1.00 5.68  ? 852  LEU A CG  1 
ATOM   7020  C  CD1 . LEU A 1 852  ? 33.104 70.358  -14.927 1.00 8.05  ? 852  LEU A CD1 1 
ATOM   7021  C  CD2 . LEU A 1 852  ? 33.069 70.880  -12.484 1.00 7.29  ? 852  LEU A CD2 1 
ATOM   7022  N  N   . GLY A 1 853  ? 29.746 67.435  -11.710 1.00 5.70  ? 853  GLY A N   1 
ATOM   7023  C  CA  . GLY A 1 853  ? 28.545 66.603  -11.644 1.00 5.73  ? 853  GLY A CA  1 
ATOM   7024  C  C   . GLY A 1 853  ? 27.828 66.600  -12.972 1.00 4.43  ? 853  GLY A C   1 
ATOM   7025  O  O   . GLY A 1 853  ? 27.894 67.593  -13.734 1.00 5.13  ? 853  GLY A O   1 
ATOM   7026  N  N   . GLY A 1 854  ? 27.158 65.511  -13.289 1.00 4.76  ? 854  GLY A N   1 
ATOM   7027  C  CA  . GLY A 1 854  ? 26.454 65.488  -14.548 1.00 5.27  ? 854  GLY A CA  1 
ATOM   7028  C  C   . GLY A 1 854  ? 25.461 64.368  -14.663 1.00 4.92  ? 854  GLY A C   1 
ATOM   7029  O  O   . GLY A 1 854  ? 25.275 63.551  -13.764 1.00 5.87  ? 854  GLY A O   1 
ATOM   7030  N  N   . SER A 1 855  ? 24.778 64.357  -15.809 1.00 6.36  ? 855  SER A N   1 
ATOM   7031  C  CA  . SER A 1 855  ? 23.713 63.375  -15.982 1.00 6.73  ? 855  SER A CA  1 
ATOM   7032  C  C   . SER A 1 855  ? 23.327 63.320  -17.447 1.00 7.62  ? 855  SER A C   1 
ATOM   7033  O  O   . SER A 1 855  ? 23.868 64.001  -18.306 1.00 7.52  ? 855  SER A O   1 
ATOM   7034  C  CB  . SER A 1 855  ? 22.472 63.791  -15.196 1.00 7.57  ? 855  SER A CB  1 
ATOM   7035  O  OG  . SER A 1 855  ? 21.479 62.765  -15.189 1.00 9.23  ? 855  SER A OG  1 
ATOM   7036  N  N   . SER A 1 856  ? 22.383 62.425  -17.726 1.00 7.15  ? 856  SER A N   1 
ATOM   7037  C  CA  . SER A 1 856  ? 21.631 62.427  -18.996 1.00 7.64  ? 856  SER A CA  1 
ATOM   7038  C  C   . SER A 1 856  ? 20.165 62.431  -18.601 1.00 7.66  ? 856  SER A C   1 
ATOM   7039  O  O   . SER A 1 856  ? 19.632 61.384  -18.194 1.00 8.37  ? 856  SER A O   1 
ATOM   7040  C  CB  . SER A 1 856  ? 22.006 61.192  -19.817 1.00 6.75  ? 856  SER A CB  1 
ATOM   7041  O  OG  . SER A 1 856  ? 21.124 61.057  -20.937 1.00 7.84  ? 856  SER A OG  1 
ATOM   7042  N  N   . LEU A 1 857  ? 19.496 63.591  -18.667 1.00 8.52  ? 857  LEU A N   1 
ATOM   7043  C  CA  . LEU A 1 857  ? 18.143 63.710  -18.126 1.00 8.85  ? 857  LEU A CA  1 
ATOM   7044  C  C   . LEU A 1 857  ? 17.057 63.430  -19.149 1.00 9.67  ? 857  LEU A C   1 
ATOM   7045  O  O   . LEU A 1 857  ? 15.884 63.375  -18.810 1.00 10.25 ? 857  LEU A O   1 
ATOM   7046  C  CB  . LEU A 1 857  ? 17.916 65.081  -17.456 1.00 9.29  ? 857  LEU A CB  1 
ATOM   7047  C  CG  . LEU A 1 857  ? 18.729 65.321  -16.192 1.00 10.22 ? 857  LEU A CG  1 
ATOM   7048  C  CD1 . LEU A 1 857  ? 18.557 66.775  -15.758 1.00 12.85 ? 857  LEU A CD1 1 
ATOM   7049  C  CD2 . LEU A 1 857  ? 18.292 64.375  -15.094 1.00 11.94 ? 857  LEU A CD2 1 
ATOM   7050  N  N   . ALA A 1 858  ? 17.494 63.213  -20.372 1.00 7.96  ? 858  ALA A N   1 
ATOM   7051  C  CA  . ALA A 1 858  ? 16.602 62.763  -21.473 1.00 8.85  ? 858  ALA A CA  1 
ATOM   7052  C  C   . ALA A 1 858  ? 17.410 62.041  -22.511 1.00 9.72  ? 858  ALA A C   1 
ATOM   7053  O  O   . ALA A 1 858  ? 18.611 62.245  -22.625 1.00 8.96  ? 858  ALA A O   1 
ATOM   7054  C  CB  . ALA A 1 858  ? 15.871 63.941  -22.123 1.00 9.56  ? 858  ALA A CB  1 
ATOM   7055  N  N   . SER A 1 859  ? 16.762 61.164  -23.279 1.00 9.13  ? 859  SER A N   1 
ATOM   7056  C  CA  . SER A 1 859  ? 17.404 60.400  -24.301 1.00 9.30  ? 859  SER A CA  1 
ATOM   7057  C  C   . SER A 1 859  ? 18.141 61.358  -25.210 1.00 9.25  ? 859  SER A C   1 
ATOM   7058  O  O   . SER A 1 859  ? 17.601 62.422  -25.588 1.00 10.59 ? 859  SER A O   1 
ATOM   7059  C  CB  . SER A 1 859  ? 16.342 59.576  -25.063 1.00 9.75  ? 859  SER A CB  1 
ATOM   7060  O  OG  . SER A 1 859  ? 16.921 58.815  -26.062 1.00 10.59 ? 859  SER A OG  1 
ATOM   7061  N  N   . GLY A 1 860  ? 19.363 60.994  -25.544 1.00 8.55  ? 860  GLY A N   1 
ATOM   7062  C  CA  . GLY A 1 860  ? 20.196 61.781  -26.434 1.00 8.83  ? 860  GLY A CA  1 
ATOM   7063  C  C   . GLY A 1 860  ? 20.899 62.984  -25.787 1.00 8.75  ? 860  GLY A C   1 
ATOM   7064  O  O   . GLY A 1 860  ? 21.638 63.696  -26.476 1.00 8.86  ? 860  GLY A O   1 
ATOM   7065  N  N   . GLU A 1 861  ? 20.713 63.193  -24.483 1.00 9.12  ? 861  GLU A N   1 
ATOM   7066  C  CA  . GLU A 1 861  ? 21.349 64.342  -23.812 1.00 9.20  ? 861  GLU A CA  1 
ATOM   7067  C  C   . GLU A 1 861  ? 22.513 63.958  -22.924 1.00 8.05  ? 861  GLU A C   1 
ATOM   7068  O  O   . GLU A 1 861  ? 22.526 62.870  -22.341 1.00 9.04  ? 861  GLU A O   1 
ATOM   7069  C  CB  . GLU A 1 861  ? 20.380 65.112  -22.942 1.00 9.80  ? 861  GLU A CB  1 
ATOM   7070  C  CG  . GLU A 1 861  ? 19.250 65.777  -23.704 1.00 12.90 ? 861  GLU A CG  1 
ATOM   7071  C  CD  . GLU A 1 861  ? 18.343 66.603  -22.773 1.00 13.33 ? 861  GLU A CD  1 
ATOM   7072  O  OE1 . GLU A 1 861  ? 18.526 66.642  -21.506 1.00 15.57 ? 861  GLU A OE1 1 
ATOM   7073  O  OE2 . GLU A 1 861  ? 17.382 67.253  -23.287 1.00 18.28 ? 861  GLU A OE2 1 
ATOM   7074  N  N   . LEU A 1 862  ? 23.462 64.869  -22.801 1.00 7.35  ? 862  LEU A N   1 
ATOM   7075  C  CA  . LEU A 1 862  ? 24.498 64.798  -21.743 1.00 7.22  ? 862  LEU A CA  1 
ATOM   7076  C  C   . LEU A 1 862  ? 24.496 66.175  -21.127 1.00 7.32  ? 862  LEU A C   1 
ATOM   7077  O  O   . LEU A 1 862  ? 24.320 67.168  -21.829 1.00 6.88  ? 862  LEU A O   1 
ATOM   7078  C  CB  . LEU A 1 862  ? 25.871 64.551  -22.363 1.00 8.05  ? 862  LEU A CB  1 
ATOM   7079  C  CG  . LEU A 1 862  ? 26.230 63.169  -22.925 1.00 8.92  ? 862  LEU A CG  1 
ATOM   7080  C  CD1 . LEU A 1 862  ? 27.612 63.172  -23.568 1.00 12.04 ? 862  LEU A CD1 1 
ATOM   7081  C  CD2 . LEU A 1 862  ? 26.079 62.100  -21.825 1.00 10.78 ? 862  LEU A CD2 1 
ATOM   7082  N  N   . GLU A 1 863  ? 24.720 66.291  -19.830 1.00 5.85  ? 863  GLU A N   1 
ATOM   7083  C  CA  . GLU A 1 863  ? 24.946 67.601  -19.232 1.00 6.22  ? 863  GLU A CA  1 
ATOM   7084  C  C   . GLU A 1 863  ? 25.926 67.487  -18.101 1.00 5.72  ? 863  GLU A C   1 
ATOM   7085  O  O   . GLU A 1 863  ? 26.046 66.453  -17.411 1.00 5.54  ? 863  GLU A O   1 
ATOM   7086  C  CB  . GLU A 1 863  ? 23.661 68.251  -18.768 1.00 7.34  ? 863  GLU A CB  1 
ATOM   7087  C  CG  . GLU A 1 863  ? 23.033 67.645  -17.518 1.00 9.28  ? 863  GLU A CG  1 
ATOM   7088  C  CD  . GLU A 1 863  ? 21.740 68.355  -17.157 1.00 9.25  ? 863  GLU A CD  1 
ATOM   7089  O  OE1 . GLU A 1 863  ? 20.812 68.381  -18.036 1.00 10.44 ? 863  GLU A OE1 1 
ATOM   7090  O  OE2 . GLU A 1 863  ? 21.621 68.871  -16.032 1.00 9.07  ? 863  GLU A OE2 1 
ATOM   7091  N  N   . ILE A 1 864  ? 26.604 68.607  -17.900 1.00 5.87  ? 864  ILE A N   1 
ATOM   7092  C  CA  A ILE A 1 864  ? 27.615 68.674  -16.862 0.50 5.09  ? 864  ILE A CA  1 
ATOM   7093  C  CA  B ILE A 1 864  ? 27.668 68.701  -16.883 0.50 6.21  ? 864  ILE A CA  1 
ATOM   7094  C  C   . ILE A 1 864  ? 27.631 70.068  -16.239 1.00 5.85  ? 864  ILE A C   1 
ATOM   7095  O  O   . ILE A 1 864  ? 27.644 71.089  -16.958 1.00 5.69  ? 864  ILE A O   1 
ATOM   7096  C  CB  A ILE A 1 864  ? 28.977 68.232  -17.460 0.50 5.09  ? 864  ILE A CB  1 
ATOM   7097  C  CB  B ILE A 1 864  ? 29.074 68.520  -17.500 0.50 6.58  ? 864  ILE A CB  1 
ATOM   7098  C  CG1 A ILE A 1 864  ? 30.009 67.912  -16.355 0.50 5.85  ? 864  ILE A CG1 1 
ATOM   7099  C  CG1 B ILE A 1 864  ? 29.251 67.138  -18.109 0.50 6.86  ? 864  ILE A CG1 1 
ATOM   7100  C  CG2 A ILE A 1 864  ? 29.431 69.205  -18.588 0.50 2.63  ? 864  ILE A CG2 1 
ATOM   7101  C  CG2 B ILE A 1 864  ? 30.154 68.784  -16.464 0.50 7.62  ? 864  ILE A CG2 1 
ATOM   7102  C  CD1 A ILE A 1 864  ? 31.225 67.189  -16.901 0.50 5.60  ? 864  ILE A CD1 1 
ATOM   7103  C  CD1 B ILE A 1 864  ? 30.728 66.824  -18.522 0.50 8.19  ? 864  ILE A CD1 1 
ATOM   7104  N  N   . MET A 1 865  ? 27.575 70.104  -14.925 1.00 5.81  ? 865  MET A N   1 
ATOM   7105  C  CA  . MET A 1 865  ? 27.503 71.372  -14.233 1.00 6.22  ? 865  MET A CA  1 
ATOM   7106  C  C   . MET A 1 865  ? 28.858 72.068  -14.264 1.00 7.29  ? 865  MET A C   1 
ATOM   7107  O  O   . MET A 1 865  ? 29.900 71.423  -14.132 1.00 8.10  ? 865  MET A O   1 
ATOM   7108  C  CB  . MET A 1 865  ? 27.057 71.112  -12.802 1.00 7.50  ? 865  MET A CB  1 
ATOM   7109  C  CG  . MET A 1 865  ? 26.503 72.326  -12.102 1.00 7.87  ? 865  MET A CG  1 
ATOM   7110  S  SD  . MET A 1 865  ? 24.867 72.795  -12.793 1.00 10.24 ? 865  MET A SD  1 
ATOM   7111  C  CE  . MET A 1 865  ? 23.875 71.449  -11.998 1.00 13.04 ? 865  MET A CE  1 
ATOM   7112  N  N   . GLN A 1 866  ? 28.843 73.393  -14.430 1.00 6.11  ? 866  GLN A N   1 
ATOM   7113  C  CA  . GLN A 1 866  ? 30.062 74.193  -14.563 1.00 5.89  ? 866  GLN A CA  1 
ATOM   7114  C  C   . GLN A 1 866  ? 30.456 74.898  -13.264 1.00 6.20  ? 866  GLN A C   1 
ATOM   7115  O  O   . GLN A 1 866  ? 31.625 74.908  -12.896 1.00 6.97  ? 866  GLN A O   1 
ATOM   7116  C  CB  . GLN A 1 866  ? 29.889 75.248  -15.671 1.00 6.27  ? 866  GLN A CB  1 
ATOM   7117  C  CG  . GLN A 1 866  ? 29.558 74.621  -17.043 1.00 8.11  ? 866  GLN A CG  1 
ATOM   7118  C  CD  . GLN A 1 866  ? 30.604 73.658  -17.505 1.00 8.88  ? 866  GLN A CD  1 
ATOM   7119  O  OE1 . GLN A 1 866  ? 31.733 74.041  -17.842 1.00 9.35  ? 866  GLN A OE1 1 
ATOM   7120  N  NE2 . GLN A 1 866  ? 30.255 72.388  -17.520 1.00 8.70  ? 866  GLN A NE2 1 
ATOM   7121  N  N   . ASP A 1 867  ? 29.486 75.496  -12.579 1.00 6.49  ? 867  ASP A N   1 
ATOM   7122  C  CA  . ASP A 1 867  ? 29.739 76.148  -11.288 1.00 6.45  ? 867  ASP A CA  1 
ATOM   7123  C  C   . ASP A 1 867  ? 28.402 76.363  -10.642 1.00 5.99  ? 867  ASP A C   1 
ATOM   7124  O  O   . ASP A 1 867  ? 27.333 76.252  -11.309 1.00 6.29  ? 867  ASP A O   1 
ATOM   7125  C  CB  . ASP A 1 867  ? 30.520 77.465  -11.418 1.00 7.31  ? 867  ASP A CB  1 
ATOM   7126  C  CG  . ASP A 1 867  ? 31.227 77.861  -10.132 1.00 7.95  ? 867  ASP A CG  1 
ATOM   7127  O  OD1 . ASP A 1 867  ? 31.107 77.185  -9.077  1.00 7.81  ? 867  ASP A OD1 1 
ATOM   7128  O  OD2 . ASP A 1 867  ? 31.967 78.869  -10.172 1.00 10.08 ? 867  ASP A OD2 1 
ATOM   7129  N  N   . ARG A 1 868  ? 28.461 76.641  -9.357  1.00 6.67  ? 868  ARG A N   1 
ATOM   7130  C  CA  . ARG A 1 868  ? 27.262 76.870  -8.579  1.00 6.68  ? 868  ARG A CA  1 
ATOM   7131  C  C   . ARG A 1 868  ? 27.578 77.898  -7.500  1.00 7.15  ? 868  ARG A C   1 
ATOM   7132  O  O   . ARG A 1 868  ? 28.640 77.858  -6.879  1.00 7.62  ? 868  ARG A O   1 
ATOM   7133  C  CB  . ARG A 1 868  ? 26.714 75.565  -8.008  1.00 7.40  ? 868  ARG A CB  1 
ATOM   7134  C  CG  . ARG A 1 868  ? 27.673 74.758  -7.141  1.00 8.71  ? 868  ARG A CG  1 
ATOM   7135  C  CD  . ARG A 1 868  ? 27.411 73.249  -7.182  1.00 8.60  ? 868  ARG A CD  1 
ATOM   7136  N  NE  . ARG A 1 868  ? 26.046 72.980  -6.756  1.00 7.45  ? 868  ARG A NE  1 
ATOM   7137  C  CZ  . ARG A 1 868  ? 25.707 72.723  -5.496  1.00 6.90  ? 868  ARG A CZ  1 
ATOM   7138  N  NH1 . ARG A 1 868  ? 26.643 72.608  -4.532  1.00 6.75  ? 868  ARG A NH1 1 
ATOM   7139  N  NH2 . ARG A 1 868  ? 24.426 72.552  -5.200  1.00 7.85  ? 868  ARG A NH2 1 
ATOM   7140  N  N   . ARG A 1 869  ? 26.636 78.826  -7.291  1.00 6.55  ? 869  ARG A N   1 
ATOM   7141  C  CA  . ARG A 1 869  ? 26.818 79.910  -6.322  1.00 7.66  ? 869  ARG A CA  1 
ATOM   7142  C  C   . ARG A 1 869  ? 25.537 79.929  -5.533  1.00 8.07  ? 869  ARG A C   1 
ATOM   7143  O  O   . ARG A 1 869  ? 24.447 80.106  -6.098  1.00 8.67  ? 869  ARG A O   1 
ATOM   7144  C  CB  . ARG A 1 869  ? 27.067 81.218  -7.055  1.00 8.40  ? 869  ARG A CB  1 
ATOM   7145  C  CG  . ARG A 1 869  ? 27.231 82.372  -6.118  1.00 9.55  ? 869  ARG A CG  1 
ATOM   7146  C  CD  . ARG A 1 869  ? 27.637 83.636  -6.857  1.00 12.42 ? 869  ARG A CD  1 
ATOM   7147  N  NE  . ARG A 1 869  ? 27.744 84.801  -5.976  1.00 14.47 ? 869  ARG A NE  1 
ATOM   7148  C  CZ  . ARG A 1 869  ? 28.850 85.148  -5.351  1.00 13.76 ? 869  ARG A CZ  1 
ATOM   7149  N  NH1 . ARG A 1 869  ? 29.944 84.418  -5.472  1.00 14.40 ? 869  ARG A NH1 1 
ATOM   7150  N  NH2 . ARG A 1 869  ? 28.862 86.242  -4.588  1.00 18.25 ? 869  ARG A NH2 1 
ATOM   7151  N  N   . LEU A 1 870  ? 25.679 79.658  -4.243  1.00 8.85  ? 870  LEU A N   1 
ATOM   7152  C  CA  . LEU A 1 870  ? 24.529 79.365  -3.376  1.00 9.39  ? 870  LEU A CA  1 
ATOM   7153  C  C   . LEU A 1 870  ? 24.593 80.187  -2.119  1.00 10.60 ? 870  LEU A C   1 
ATOM   7154  O  O   . LEU A 1 870  ? 25.568 80.139  -1.367  1.00 10.74 ? 870  LEU A O   1 
ATOM   7155  C  CB  . LEU A 1 870  ? 24.543 77.886  -2.972  1.00 9.38  ? 870  LEU A CB  1 
ATOM   7156  C  CG  . LEU A 1 870  ? 24.441 77.039  -4.244  1.00 13.73 ? 870  LEU A CG  1 
ATOM   7157  C  CD1 . LEU A 1 870  ? 24.927 75.656  -4.029  1.00 17.18 ? 870  LEU A CD1 1 
ATOM   7158  C  CD2 . LEU A 1 870  ? 23.104 77.077  -4.956  1.00 12.62 ? 870  LEU A CD2 1 
ATOM   7159  N  N   . ALA A 1 871  ? 23.508 80.905  -1.864  1.00 10.76 ? 871  ALA A N   1 
ATOM   7160  C  CA  . ALA A 1 871  ? 23.526 81.781  -0.717  1.00 12.90 ? 871  ALA A CA  1 
ATOM   7161  C  C   . ALA A 1 871  ? 23.334 81.078  0.636   1.00 14.05 ? 871  ALA A C   1 
ATOM   7162  O  O   . ALA A 1 871  ? 23.752 81.588  1.677   1.00 17.21 ? 871  ALA A O   1 
ATOM   7163  C  CB  . ALA A 1 871  ? 22.474 82.900  -0.879  1.00 13.75 ? 871  ALA A CB  1 
ATOM   7164  N  N   . SER A 1 872  ? 22.714 79.907  0.619   1.00 14.06 ? 872  SER A N   1 
ATOM   7165  C  CA  . SER A 1 872  ? 22.264 79.282  1.855   1.00 14.80 ? 872  SER A CA  1 
ATOM   7166  C  C   . SER A 1 872  ? 23.159 78.135  2.287   1.00 13.70 ? 872  SER A C   1 
ATOM   7167  O  O   . SER A 1 872  ? 23.812 77.479  1.453   1.00 13.78 ? 872  SER A O   1 
ATOM   7168  C  CB  . SER A 1 872  ? 20.836 78.751  1.673   1.00 15.79 ? 872  SER A CB  1 
ATOM   7169  O  OG  . SER A 1 872  ? 19.963 79.845  1.432   1.00 20.93 ? 872  SER A OG  1 
ATOM   7170  N  N   . ASP A 1 873  ? 23.210 77.924  3.600   1.00 13.76 ? 873  ASP A N   1 
ATOM   7171  C  CA  . ASP A 1 873  ? 23.747 76.697  4.183   1.00 13.75 ? 873  ASP A CA  1 
ATOM   7172  C  C   . ASP A 1 873  ? 22.734 75.553  4.017   1.00 14.43 ? 873  ASP A C   1 
ATOM   7173  O  O   . ASP A 1 873  ? 21.528 75.782  4.084   1.00 15.64 ? 873  ASP A O   1 
ATOM   7174  C  CB  . ASP A 1 873  ? 24.040 76.925  5.657   1.00 13.49 ? 873  ASP A CB  1 
ATOM   7175  C  CG  . ASP A 1 873  ? 24.476 75.662  6.357   1.00 15.73 ? 873  ASP A CG  1 
ATOM   7176  O  OD1 . ASP A 1 873  ? 25.587 75.169  6.040   1.00 15.82 ? 873  ASP A OD1 1 
ATOM   7177  O  OD2 . ASP A 1 873  ? 23.767 75.099  7.219   1.00 15.74 ? 873  ASP A OD2 1 
ATOM   7178  N  N   . ASP A 1 874  ? 23.219 74.333  3.795   1.00 12.64 ? 874  ASP A N   1 
ATOM   7179  C  CA  . ASP A 1 874  ? 22.331 73.199  3.586   1.00 10.72 ? 874  ASP A CA  1 
ATOM   7180  C  C   . ASP A 1 874  ? 22.333 72.234  4.793   1.00 10.28 ? 874  ASP A C   1 
ATOM   7181  O  O   . ASP A 1 874  ? 22.113 71.027  4.627   1.00 11.69 ? 874  ASP A O   1 
ATOM   7182  C  CB  . ASP A 1 874  ? 22.686 72.499  2.270   1.00 10.47 ? 874  ASP A CB  1 
ATOM   7183  C  CG  . ASP A 1 874  ? 24.159 72.170  2.153   1.00 10.71 ? 874  ASP A CG  1 
ATOM   7184  O  OD1 . ASP A 1 874  ? 25.003 72.518  3.028   1.00 12.59 ? 874  ASP A OD1 1 
ATOM   7185  O  OD2 . ASP A 1 874  ? 24.531 71.538  1.156   1.00 9.84  ? 874  ASP A OD2 1 
ATOM   7186  N  N   . GLU A 1 875  ? 22.590 72.759  5.991   1.00 10.32 ? 875  GLU A N   1 
ATOM   7187  C  CA  . GLU A 1 875  ? 22.281 72.031  7.240   1.00 13.03 ? 875  GLU A CA  1 
ATOM   7188  C  C   . GLU A 1 875  ? 23.081 70.769  7.443   1.00 12.57 ? 875  GLU A C   1 
ATOM   7189  O  O   . GLU A 1 875  ? 22.608 69.820  8.106   1.00 12.78 ? 875  GLU A O   1 
ATOM   7190  C  CB  . GLU A 1 875  ? 20.781 71.669  7.370   1.00 13.99 ? 875  GLU A CB  1 
ATOM   7191  C  CG  . GLU A 1 875  ? 19.783 72.758  7.031   1.00 17.03 ? 875  GLU A CG  1 
ATOM   7192  C  CD  . GLU A 1 875  ? 18.332 72.276  7.082   1.00 19.28 ? 875  GLU A CD  1 
ATOM   7193  O  OE1 . GLU A 1 875  ? 18.020 71.098  6.713   1.00 24.00 ? 875  GLU A OE1 1 
ATOM   7194  O  OE2 . GLU A 1 875  ? 17.486 73.105  7.483   1.00 27.03 ? 875  GLU A OE2 1 
ATOM   7195  N  N   . ARG A 1 876  ? 24.290 70.740  6.885   1.00 9.99  ? 876  ARG A N   1 
ATOM   7196  C  CA  . ARG A 1 876  ? 25.179 69.592  7.084   1.00 11.08 ? 876  ARG A CA  1 
ATOM   7197  C  C   . ARG A 1 876  ? 26.436 69.968  7.869   1.00 10.89 ? 876  ARG A C   1 
ATOM   7198  O  O   . ARG A 1 876  ? 27.410 69.195  7.881   1.00 12.93 ? 876  ARG A O   1 
ATOM   7199  C  CB  . ARG A 1 876  ? 25.555 68.935  5.753   1.00 9.60  ? 876  ARG A CB  1 
ATOM   7200  C  CG  . ARG A 1 876  ? 24.355 68.313  4.974   1.00 10.81 ? 876  ARG A CG  1 
ATOM   7201  C  CD  . ARG A 1 876  ? 23.539 67.383  5.840   1.00 11.91 ? 876  ARG A CD  1 
ATOM   7202  N  NE  . ARG A 1 876  ? 22.442 66.667  5.174   1.00 10.42 ? 876  ARG A NE  1 
ATOM   7203  C  CZ  . ARG A 1 876  ? 21.250 67.191  4.886   1.00 10.00 ? 876  ARG A CZ  1 
ATOM   7204  N  NH1 . ARG A 1 876  ? 20.992 68.489  5.080   1.00 8.96  ? 876  ARG A NH1 1 
ATOM   7205  N  NH2 . ARG A 1 876  ? 20.326 66.396  4.353   1.00 9.08  ? 876  ARG A NH2 1 
ATOM   7206  N  N   . GLY A 1 877  ? 26.415 71.125  8.532   1.00 11.45 ? 877  GLY A N   1 
ATOM   7207  C  CA  . GLY A 1 877  ? 27.502 71.508  9.426   1.00 11.89 ? 877  GLY A CA  1 
ATOM   7208  C  C   . GLY A 1 877  ? 28.495 72.513  8.886   1.00 11.10 ? 877  GLY A C   1 
ATOM   7209  O  O   . GLY A 1 877  ? 29.327 73.015  9.662   1.00 11.96 ? 877  GLY A O   1 
ATOM   7210  N  N   . LEU A 1 878  ? 28.395 72.859  7.601   1.00 10.34 ? 878  LEU A N   1 
ATOM   7211  C  CA  . LEU A 1 878  ? 29.369 73.787  7.030   1.00 11.45 ? 878  LEU A CA  1 
ATOM   7212  C  C   . LEU A 1 878  ? 29.169 75.207  7.540   1.00 11.14 ? 878  LEU A C   1 
ATOM   7213  O  O   . LEU A 1 878  ? 30.140 75.925  7.773   1.00 11.21 ? 878  LEU A O   1 
ATOM   7214  C  CB  . LEU A 1 878  ? 29.335 73.719  5.501   1.00 10.87 ? 878  LEU A CB  1 
ATOM   7215  C  CG  . LEU A 1 878  ? 30.141 74.759  4.718   1.00 11.30 ? 878  LEU A CG  1 
ATOM   7216  C  CD1 . LEU A 1 878  ? 31.621 74.727  5.166   1.00 11.90 ? 878  LEU A CD1 1 
ATOM   7217  C  CD2 . LEU A 1 878  ? 30.025 74.568  3.223   1.00 13.26 ? 878  LEU A CD2 1 
ATOM   7218  N  N   . GLY A 1 879  ? 27.902 75.609  7.685   1.00 10.80 ? 879  GLY A N   1 
ATOM   7219  C  CA  . GLY A 1 879  ? 27.561 76.900  8.255   1.00 11.20 ? 879  GLY A CA  1 
ATOM   7220  C  C   . GLY A 1 879  ? 27.832 78.068  7.335   1.00 11.58 ? 879  GLY A C   1 
ATOM   7221  O  O   . GLY A 1 879  ? 28.018 79.188  7.801   1.00 12.91 ? 879  GLY A O   1 
ATOM   7222  N  N   . GLN A 1 880  ? 27.826 77.819  6.029   1.00 10.90 ? 880  GLN A N   1 
ATOM   7223  C  CA  . GLN A 1 880  ? 27.902 78.899  5.049   1.00 10.92 ? 880  GLN A CA  1 
ATOM   7224  C  C   . GLN A 1 880  ? 27.409 78.372  3.722   1.00 11.70 ? 880  GLN A C   1 
ATOM   7225  O  O   . GLN A 1 880  ? 27.348 77.156  3.525   1.00 11.99 ? 880  GLN A O   1 
ATOM   7226  C  CB  . GLN A 1 880  ? 29.342 79.450  4.918   1.00 10.61 ? 880  GLN A CB  1 
ATOM   7227  C  CG  . GLN A 1 880  ? 30.340 78.418  4.397   1.00 11.45 ? 880  GLN A CG  1 
ATOM   7228  C  CD  . GLN A 1 880  ? 31.634 79.034  3.880   1.00 11.35 ? 880  GLN A CD  1 
ATOM   7229  O  OE1 . GLN A 1 880  ? 32.526 79.382  4.648   1.00 11.27 ? 880  GLN A OE1 1 
ATOM   7230  N  NE2 . GLN A 1 880  ? 31.716 79.195  2.579   1.00 12.04 ? 880  GLN A NE2 1 
ATOM   7231  N  N   . GLY A 1 881  ? 27.080 79.303  2.832   1.00 13.21 ? 881  GLY A N   1 
ATOM   7232  C  CA  . GLY A 1 881  ? 26.813 78.978  1.448   1.00 12.99 ? 881  GLY A CA  1 
ATOM   7233  C  C   . GLY A 1 881  ? 28.097 78.845  0.645   1.00 12.60 ? 881  GLY A C   1 
ATOM   7234  O  O   . GLY A 1 881  ? 29.220 78.686  1.181   1.00 13.27 ? 881  GLY A O   1 
ATOM   7235  N  N   . VAL A 1 882  ? 27.925 78.906  -0.668  1.00 10.89 ? 882  VAL A N   1 
ATOM   7236  C  CA  . VAL A 1 882  ? 29.056 78.889  -1.576  1.00 11.34 ? 882  VAL A CA  1 
ATOM   7237  C  C   . VAL A 1 882  ? 29.013 80.210  -2.332  1.00 11.27 ? 882  VAL A C   1 
ATOM   7238  O  O   . VAL A 1 882  ? 28.267 80.368  -3.291  1.00 10.31 ? 882  VAL A O   1 
ATOM   7239  C  CB  . VAL A 1 882  ? 29.023 77.687  -2.508  1.00 11.15 ? 882  VAL A CB  1 
ATOM   7240  C  CG1 . VAL A 1 882  ? 30.158 77.778  -3.512  1.00 12.38 ? 882  VAL A CG1 1 
ATOM   7241  C  CG2 . VAL A 1 882  ? 29.167 76.430  -1.665  1.00 11.94 ? 882  VAL A CG2 1 
ATOM   7242  N  N   . LEU A 1 883  ? 29.785 81.182  -1.841  1.00 11.22 ? 883  LEU A N   1 
ATOM   7243  C  CA  . LEU A 1 883  ? 29.767 82.522  -2.432  1.00 11.97 ? 883  LEU A CA  1 
ATOM   7244  C  C   . LEU A 1 883  ? 31.167 83.013  -2.750  1.00 12.43 ? 883  LEU A C   1 
ATOM   7245  O  O   . LEU A 1 883  ? 31.356 84.212  -2.923  1.00 15.20 ? 883  LEU A O   1 
ATOM   7246  C  CB  . LEU A 1 883  ? 29.074 83.520  -1.492  1.00 12.61 ? 883  LEU A CB  1 
ATOM   7247  C  CG  . LEU A 1 883  ? 27.574 83.278  -1.245  1.00 12.70 ? 883  LEU A CG  1 
ATOM   7248  C  CD1 . LEU A 1 883  ? 27.006 84.179  -0.114  1.00 13.07 ? 883  LEU A CD1 1 
ATOM   7249  C  CD2 . LEU A 1 883  ? 26.769 83.507  -2.508  1.00 12.67 ? 883  LEU A CD2 1 
ATOM   7250  N  N   . ASP A 1 884  ? 32.131 82.104  -2.817  1.00 11.30 ? 884  ASP A N   1 
ATOM   7251  C  CA  . ASP A 1 884  ? 33.549 82.438  -3.040  1.00 10.80 ? 884  ASP A CA  1 
ATOM   7252  C  C   . ASP A 1 884  ? 34.060 81.991  -4.419  1.00 11.15 ? 884  ASP A C   1 
ATOM   7253  O  O   . ASP A 1 884  ? 35.248 81.708  -4.623  1.00 10.64 ? 884  ASP A O   1 
ATOM   7254  C  CB  . ASP A 1 884  ? 34.419 81.842  -1.921  1.00 11.61 ? 884  ASP A CB  1 
ATOM   7255  C  CG  . ASP A 1 884  ? 34.204 80.340  -1.712  1.00 13.92 ? 884  ASP A CG  1 
ATOM   7256  O  OD1 . ASP A 1 884  ? 33.388 79.675  -2.430  1.00 12.20 ? 884  ASP A OD1 1 
ATOM   7257  O  OD2 . ASP A 1 884  ? 34.834 79.758  -0.775  1.00 15.63 ? 884  ASP A OD2 1 
ATOM   7258  N  N   . ASN A 1 885  ? 33.142 81.942  -5.373  1.00 9.69  ? 885  ASN A N   1 
ATOM   7259  C  CA  . ASN A 1 885  ? 33.479 81.558  -6.729  1.00 10.80 ? 885  ASN A CA  1 
ATOM   7260  C  C   . ASN A 1 885  ? 34.556 82.405  -7.305  1.00 10.86 ? 885  ASN A C   1 
ATOM   7261  O  O   . ASN A 1 885  ? 34.652 83.601  -7.001  1.00 11.82 ? 885  ASN A O   1 
ATOM   7262  C  CB  . ASN A 1 885  ? 32.239 81.657  -7.615  1.00 9.62  ? 885  ASN A CB  1 
ATOM   7263  C  CG  . ASN A 1 885  ? 31.043 80.985  -6.991  1.00 10.40 ? 885  ASN A CG  1 
ATOM   7264  O  OD1 . ASN A 1 885  ? 30.392 81.538  -6.104  1.00 11.51 ? 885  ASN A OD1 1 
ATOM   7265  N  ND2 . ASN A 1 885  ? 30.714 79.800  -7.492  1.00 9.43  ? 885  ASN A ND2 1 
ATOM   7266  N  N   . LYS A 1 886  ? 35.342 81.803  -8.174  1.00 11.23 ? 886  LYS A N   1 
ATOM   7267  C  CA  . LYS A 1 886  ? 36.313 82.561  -8.955  1.00 11.42 ? 886  LYS A CA  1 
ATOM   7268  C  C   . LYS A 1 886  ? 36.426 81.944  -10.327 1.00 10.60 ? 886  LYS A C   1 
ATOM   7269  O  O   . LYS A 1 886  ? 36.055 80.781  -10.546 1.00 10.36 ? 886  LYS A O   1 
ATOM   7270  C  CB  . LYS A 1 886  ? 37.661 82.587  -8.245  1.00 13.81 ? 886  LYS A CB  1 
ATOM   7271  C  CG  . LYS A 1 886  ? 38.198 81.208  -7.926  1.00 14.36 ? 886  LYS A CG  1 
ATOM   7272  C  CD  . LYS A 1 886  ? 39.251 81.225  -6.797  1.00 20.38 ? 886  LYS A CD  1 
ATOM   7273  C  CE  . LYS A 1 886  ? 40.603 81.581  -7.369  1.00 20.84 ? 886  LYS A CE  1 
ATOM   7274  N  NZ  . LYS A 1 886  ? 41.702 81.564  -6.354  1.00 22.26 ? 886  LYS A NZ  1 
ATOM   7275  N  N   . PRO A 1 887  ? 36.869 82.729  -11.290 1.00 9.06  ? 887  PRO A N   1 
ATOM   7276  C  CA  . PRO A 1 887  ? 36.939 82.240  -12.662 1.00 9.39  ? 887  PRO A CA  1 
ATOM   7277  C  C   . PRO A 1 887  ? 37.736 80.966  -12.774 1.00 8.87  ? 887  PRO A C   1 
ATOM   7278  O  O   . PRO A 1 887  ? 38.803 80.854  -12.189 1.00 9.93  ? 887  PRO A O   1 
ATOM   7279  C  CB  . PRO A 1 887  ? 37.584 83.401  -13.417 1.00 10.16 ? 887  PRO A CB  1 
ATOM   7280  C  CG  . PRO A 1 887  ? 37.089 84.608  -12.613 1.00 10.84 ? 887  PRO A CG  1 
ATOM   7281  C  CD  . PRO A 1 887  ? 37.173 84.177  -11.197 1.00 11.11 ? 887  PRO A CD  1 
ATOM   7282  N  N   . VAL A 1 888  ? 37.186 80.003  -13.510 1.00 7.67  ? 888  VAL A N   1 
ATOM   7283  C  CA  . VAL A 1 888  ? 37.857 78.732  -13.694 1.00 6.55  ? 888  VAL A CA  1 
ATOM   7284  C  C   . VAL A 1 888  ? 37.787 78.364  -15.170 1.00 6.45  ? 888  VAL A C   1 
ATOM   7285  O  O   . VAL A 1 888  ? 36.739 78.577  -15.823 1.00 6.46  ? 888  VAL A O   1 
ATOM   7286  C  CB  . VAL A 1 888  ? 37.237 77.612  -12.778 1.00 8.19  ? 888  VAL A CB  1 
ATOM   7287  C  CG1 . VAL A 1 888  ? 35.740 77.549  -12.971 1.00 8.38  ? 888  VAL A CG1 1 
ATOM   7288  C  CG2 . VAL A 1 888  ? 37.894 76.285  -13.077 1.00 8.26  ? 888  VAL A CG2 1 
ATOM   7289  N  N   . LEU A 1 889  ? 38.891 77.838  -15.696 1.00 5.57  ? 889  LEU A N   1 
ATOM   7290  C  CA  . LEU A 1 889  ? 38.907 77.340  -17.055 1.00 6.42  ? 889  LEU A CA  1 
ATOM   7291  C  C   . LEU A 1 889  ? 38.700 75.827  -17.092 1.00 6.61  ? 889  LEU A C   1 
ATOM   7292  O  O   . LEU A 1 889  ? 39.600 75.044  -16.766 1.00 7.55  ? 889  LEU A O   1 
ATOM   7293  C  CB  . LEU A 1 889  ? 40.209 77.721  -17.755 1.00 6.82  ? 889  LEU A CB  1 
ATOM   7294  C  CG  . LEU A 1 889  ? 40.278 77.270  -19.222 1.00 7.56  ? 889  LEU A CG  1 
ATOM   7295  C  CD1 . LEU A 1 889  ? 39.429 78.156  -20.125 1.00 9.87  ? 889  LEU A CD1 1 
ATOM   7296  C  CD2 . LEU A 1 889  ? 41.729 77.249  -19.727 1.00 12.43 ? 889  LEU A CD2 1 
ATOM   7297  N  N   . HIS A 1 890  ? 37.503 75.425  -17.452 1.00 5.28  ? 890  HIS A N   1 
ATOM   7298  C  CA  . HIS A 1 890  ? 37.199 73.993  -17.581 1.00 5.13  ? 890  HIS A CA  1 
ATOM   7299  C  C   . HIS A 1 890  ? 37.573 73.529  -18.949 1.00 5.33  ? 890  HIS A C   1 
ATOM   7300  O  O   . HIS A 1 890  ? 37.329 74.256  -19.939 1.00 6.24  ? 890  HIS A O   1 
ATOM   7301  C  CB  . HIS A 1 890  ? 35.704 73.769  -17.394 1.00 5.84  ? 890  HIS A CB  1 
ATOM   7302  C  CG  . HIS A 1 890  ? 35.250 73.914  -15.975 1.00 6.69  ? 890  HIS A CG  1 
ATOM   7303  N  ND1 . HIS A 1 890  ? 36.048 73.551  -14.899 1.00 8.65  ? 890  HIS A ND1 1 
ATOM   7304  C  CD2 . HIS A 1 890  ? 34.075 74.333  -15.445 1.00 7.84  ? 890  HIS A CD2 1 
ATOM   7305  C  CE1 . HIS A 1 890  ? 35.373 73.737  -13.775 1.00 9.83  ? 890  HIS A CE1 1 
ATOM   7306  N  NE2 . HIS A 1 890  ? 34.176 74.212  -14.078 1.00 8.74  ? 890  HIS A NE2 1 
ATOM   7307  N  N   . ILE A 1 891  ? 38.084 72.312  -19.059 1.00 5.20  ? 891  ILE A N   1 
ATOM   7308  C  CA  . ILE A 1 891  ? 38.519 71.783  -20.342 1.00 5.36  ? 891  ILE A CA  1 
ATOM   7309  C  C   . ILE A 1 891  ? 37.880 70.426  -20.618 1.00 4.80  ? 891  ILE A C   1 
ATOM   7310  O  O   . ILE A 1 891  ? 37.623 69.641  -19.660 1.00 4.96  ? 891  ILE A O   1 
ATOM   7311  C  CB  . ILE A 1 891  ? 40.076 71.746  -20.427 1.00 5.57  ? 891  ILE A CB  1 
ATOM   7312  C  CG1 . ILE A 1 891  ? 40.659 70.702  -19.467 1.00 6.85  ? 891  ILE A CG1 1 
ATOM   7313  C  CG2 . ILE A 1 891  ? 40.658 73.172  -20.202 1.00 8.22  ? 891  ILE A CG2 1 
ATOM   7314  C  CD1 . ILE A 1 891  ? 42.176 70.502  -19.594 1.00 8.44  ? 891  ILE A CD1 1 
ATOM   7315  N  N   . TYR A 1 892  ? 37.613 70.161  -21.889 1.00 5.01  ? 892  TYR A N   1 
ATOM   7316  C  CA  . TYR A 1 892  ? 36.954 68.934  -22.318 1.00 4.92  ? 892  TYR A CA  1 
ATOM   7317  C  C   . TYR A 1 892  ? 37.407 68.501  -23.678 1.00 5.11  ? 892  TYR A C   1 
ATOM   7318  O  O   . TYR A 1 892  ? 37.953 69.296  -24.440 1.00 5.10  ? 892  TYR A O   1 
ATOM   7319  C  CB  . TYR A 1 892  ? 35.432 69.150  -22.448 1.00 5.21  ? 892  TYR A CB  1 
ATOM   7320  C  CG  . TYR A 1 892  ? 34.757 69.811  -21.264 1.00 4.99  ? 892  TYR A CG  1 
ATOM   7321  C  CD1 . TYR A 1 892  ? 34.698 71.195  -21.135 1.00 6.35  ? 892  TYR A CD1 1 
ATOM   7322  C  CD2 . TYR A 1 892  ? 34.196 69.032  -20.253 1.00 6.79  ? 892  TYR A CD2 1 
ATOM   7323  C  CE1 . TYR A 1 892  ? 34.097 71.791  -20.059 1.00 6.03  ? 892  TYR A CE1 1 
ATOM   7324  C  CE2 . TYR A 1 892  ? 33.614 69.619  -19.154 1.00 6.22  ? 892  TYR A CE2 1 
ATOM   7325  C  CZ  . TYR A 1 892  ? 33.552 70.987  -19.055 1.00 5.70  ? 892  TYR A CZ  1 
ATOM   7326  O  OH  . TYR A 1 892  ? 32.922 71.529  -17.965 1.00 7.07  ? 892  TYR A OH  1 
ATOM   7327  N  N   . ARG A 1 893  ? 37.145 67.228  -23.996 1.00 4.91  ? 893  ARG A N   1 
ATOM   7328  C  CA  . ARG A 1 893  ? 37.210 66.775  -25.390 1.00 5.96  ? 893  ARG A CA  1 
ATOM   7329  C  C   . ARG A 1 893  ? 35.870 66.129  -25.696 1.00 6.17  ? 893  ARG A C   1 
ATOM   7330  O  O   . ARG A 1 893  ? 35.274 65.497  -24.858 1.00 6.48  ? 893  ARG A O   1 
ATOM   7331  C  CB  . ARG A 1 893  ? 38.296 65.736  -25.599 1.00 6.97  ? 893  ARG A CB  1 
ATOM   7332  C  CG  . ARG A 1 893  ? 39.719 66.212  -25.415 1.00 7.95  ? 893  ARG A CG  1 
ATOM   7333  C  CD  . ARG A 1 893  ? 40.179 67.235  -26.474 1.00 7.61  ? 893  ARG A CD  1 
ATOM   7334  N  NE  . ARG A 1 893  ? 40.246 66.704  -27.834 1.00 8.86  ? 893  ARG A NE  1 
ATOM   7335  C  CZ  . ARG A 1 893  ? 41.232 65.956  -28.331 1.00 8.36  ? 893  ARG A CZ  1 
ATOM   7336  N  NH1 . ARG A 1 893  ? 42.252 65.588  -27.547 1.00 11.21 ? 893  ARG A NH1 1 
ATOM   7337  N  NH2 . ARG A 1 893  ? 41.211 65.547  -29.608 1.00 12.75 ? 893  ARG A NH2 1 
ATOM   7338  N  N   . LEU A 1 894  ? 35.425 66.287  -26.944 1.00 7.31  ? 894  LEU A N   1 
ATOM   7339  C  CA  . LEU A 1 894  ? 34.123 65.805  -27.376 1.00 7.81  ? 894  LEU A CA  1 
ATOM   7340  C  C   . LEU A 1 894  ? 34.326 64.840  -28.519 1.00 7.29  ? 894  LEU A C   1 
ATOM   7341  O  O   . LEU A 1 894  ? 34.807 65.247  -29.576 1.00 9.04  ? 894  LEU A O   1 
ATOM   7342  C  CB  . LEU A 1 894  ? 33.291 67.001  -27.860 1.00 8.72  ? 894  LEU A CB  1 
ATOM   7343  C  CG  . LEU A 1 894  ? 31.835 66.655  -28.206 1.00 10.82 ? 894  LEU A CG  1 
ATOM   7344  C  CD1 . LEU A 1 894  ? 31.079 66.121  -26.995 1.00 13.57 ? 894  LEU A CD1 1 
ATOM   7345  C  CD2 . LEU A 1 894  ? 31.150 67.871  -28.788 1.00 13.90 ? 894  LEU A CD2 1 
ATOM   7346  N  N   . VAL A 1 895  ? 33.997 63.561  -28.306 1.00 6.90  ? 895  VAL A N   1 
ATOM   7347  C  CA  . VAL A 1 895  ? 34.282 62.535  -29.292 1.00 8.09  ? 895  VAL A CA  1 
ATOM   7348  C  C   . VAL A 1 895  ? 32.980 61.898  -29.779 1.00 8.66  ? 895  VAL A C   1 
ATOM   7349  O  O   . VAL A 1 895  ? 32.295 61.219  -29.018 1.00 8.77  ? 895  VAL A O   1 
ATOM   7350  C  CB  . VAL A 1 895  ? 35.167 61.448  -28.677 1.00 8.27  ? 895  VAL A CB  1 
ATOM   7351  C  CG1 . VAL A 1 895  ? 35.598 60.485  -29.756 1.00 10.93 ? 895  VAL A CG1 1 
ATOM   7352  C  CG2 . VAL A 1 895  ? 36.424 62.073  -28.026 1.00 10.14 ? 895  VAL A CG2 1 
ATOM   7353  N  N   . LEU A 1 896  ? 32.628 62.158  -31.036 1.00 8.49  ? 896  LEU A N   1 
ATOM   7354  C  CA  . LEU A 1 896  ? 31.483 61.520  -31.680 1.00 8.59  ? 896  LEU A CA  1 
ATOM   7355  C  C   . LEU A 1 896  ? 32.022 60.383  -32.530 1.00 9.17  ? 896  LEU A C   1 
ATOM   7356  O  O   . LEU A 1 896  ? 32.975 60.566  -33.294 1.00 9.89  ? 896  LEU A O   1 
ATOM   7357  C  CB  . LEU A 1 896  ? 30.752 62.528  -32.578 1.00 8.96  ? 896  LEU A CB  1 
ATOM   7358  C  CG  . LEU A 1 896  ? 29.578 61.937  -33.375 1.00 10.96 ? 896  LEU A CG  1 
ATOM   7359  C  CD1 . LEU A 1 896  ? 28.407 61.755  -32.455 1.00 12.80 ? 896  LEU A CD1 1 
ATOM   7360  C  CD2 . LEU A 1 896  ? 29.217 62.864  -34.533 1.00 12.03 ? 896  LEU A CD2 1 
ATOM   7361  N  N   . GLU A 1 897  ? 31.435 59.197  -32.382 1.00 8.98  ? 897  GLU A N   1 
ATOM   7362  C  CA  . GLU A 1 897  ? 31.984 58.013  -33.050 1.00 9.60  ? 897  GLU A CA  1 
ATOM   7363  C  C   . GLU A 1 897  ? 30.877 57.106  -33.531 1.00 9.43  ? 897  GLU A C   1 
ATOM   7364  O  O   . GLU A 1 897  ? 29.839 57.026  -32.892 1.00 9.13  ? 897  GLU A O   1 
ATOM   7365  C  CB  . GLU A 1 897  ? 32.889 57.220  -32.104 1.00 12.43 ? 897  GLU A CB  1 
ATOM   7366  C  CG  . GLU A 1 897  ? 34.021 58.022  -31.508 1.00 16.02 ? 897  GLU A CG  1 
ATOM   7367  C  CD  . GLU A 1 897  ? 34.764 57.227  -30.445 1.00 18.58 ? 897  GLU A CD  1 
ATOM   7368  O  OE1 . GLU A 1 897  ? 34.189 56.985  -29.325 1.00 21.21 ? 897  GLU A OE1 1 
ATOM   7369  O  OE2 . GLU A 1 897  ? 35.930 56.896  -30.758 1.00 20.55 ? 897  GLU A OE2 1 
ATOM   7370  N  N   . LYS A 1 898  ? 31.135 56.415  -34.640 1.00 11.52 ? 898  LYS A N   1 
ATOM   7371  C  CA  . LYS A 1 898  ? 30.308 55.296  -35.079 1.00 13.27 ? 898  LYS A CA  1 
ATOM   7372  C  C   . LYS A 1 898  ? 30.727 54.043  -34.322 1.00 13.56 ? 898  LYS A C   1 
ATOM   7373  O  O   . LYS A 1 898  ? 31.911 53.699  -34.275 1.00 15.82 ? 898  LYS A O   1 
ATOM   7374  C  CB  . LYS A 1 898  ? 30.431 55.094  -36.586 1.00 14.32 ? 898  LYS A CB  1 
ATOM   7375  C  CG  . LYS A 1 898  ? 29.815 56.223  -37.403 1.00 18.81 ? 898  LYS A CG  1 
ATOM   7376  C  CD  . LYS A 1 898  ? 28.568 56.858  -36.724 1.00 24.14 ? 898  LYS A CD  1 
ATOM   7377  C  CE  . LYS A 1 898  ? 27.216 56.255  -37.159 1.00 25.51 ? 898  LYS A CE  1 
ATOM   7378  N  NZ  . LYS A 1 898  ? 27.137 54.743  -37.244 1.00 26.43 ? 898  LYS A NZ  1 
ATOM   7379  N  N   . VAL A 1 899  ? 29.762 53.379  -33.699 1.00 12.38 ? 899  VAL A N   1 
ATOM   7380  C  CA  . VAL A 1 899  ? 30.086 52.232  -32.853 1.00 12.33 ? 899  VAL A CA  1 
ATOM   7381  C  C   . VAL A 1 899  ? 29.368 50.959  -33.273 1.00 13.12 ? 899  VAL A C   1 
ATOM   7382  O  O   . VAL A 1 899  ? 29.396 49.975  -32.553 1.00 12.00 ? 899  VAL A O   1 
ATOM   7383  C  CB  . VAL A 1 899  ? 29.816 52.522  -31.360 1.00 12.46 ? 899  VAL A CB  1 
ATOM   7384  C  CG1 . VAL A 1 899  ? 30.826 53.545  -30.836 1.00 15.25 ? 899  VAL A CG1 1 
ATOM   7385  C  CG2 . VAL A 1 899  ? 28.389 52.981  -31.133 1.00 10.71 ? 899  VAL A CG2 1 
ATOM   7386  N  N   . ASN A 1 900  ? 28.736 50.975  -34.443 1.00 13.01 ? 900  ASN A N   1 
ATOM   7387  C  CA  . ASN A 1 900  ? 27.969 49.807  -34.873 1.00 14.23 ? 900  ASN A CA  1 
ATOM   7388  C  C   . ASN A 1 900  ? 28.834 48.569  -35.066 1.00 14.09 ? 900  ASN A C   1 
ATOM   7389  O  O   . ASN A 1 900  ? 28.313 47.449  -34.952 1.00 15.49 ? 900  ASN A O   1 
ATOM   7390  C  CB  . ASN A 1 900  ? 27.193 50.100  -36.164 1.00 13.99 ? 900  ASN A CB  1 
ATOM   7391  C  CG  . ASN A 1 900  ? 28.064 50.635  -37.267 1.00 17.19 ? 900  ASN A CG  1 
ATOM   7392  O  OD1 . ASN A 1 900  ? 28.623 51.735  -37.181 1.00 22.98 ? 900  ASN A OD1 1 
ATOM   7393  N  ND2 . ASN A 1 900  ? 28.166 49.865  -38.351 1.00 21.25 ? 900  ASN A ND2 1 
ATOM   7394  N  N   . ASN A 1 901  ? 30.129 48.774  -35.314 1.00 12.88 ? 901  ASN A N   1 
ATOM   7395  C  CA  . ASN A 1 901  ? 31.109 47.675  -35.507 1.00 13.64 ? 901  ASN A CA  1 
ATOM   7396  C  C   . ASN A 1 901  ? 31.858 47.269  -34.258 1.00 13.46 ? 901  ASN A C   1 
ATOM   7397  O  O   . ASN A 1 901  ? 32.601 46.294  -34.285 1.00 13.21 ? 901  ASN A O   1 
ATOM   7398  C  CB  . ASN A 1 901  ? 32.129 48.049  -36.572 1.00 15.29 ? 901  ASN A CB  1 
ATOM   7399  C  CG  . ASN A 1 901  ? 31.558 48.000  -37.953 1.00 18.85 ? 901  ASN A CG  1 
ATOM   7400  O  OD1 . ASN A 1 901  ? 30.761 47.119  -38.281 1.00 23.10 ? 901  ASN A OD1 1 
ATOM   7401  N  ND2 . ASN A 1 901  ? 31.970 48.947  -38.794 1.00 24.06 ? 901  ASN A ND2 1 
ATOM   7402  N  N   . CYS A 1 902  ? 31.631 47.971  -33.155 1.00 12.91 ? 902  CYS A N   1 
ATOM   7403  C  CA  . CYS A 1 902  ? 32.367 47.706  -31.919 1.00 13.32 ? 902  CYS A CA  1 
ATOM   7404  C  C   . CYS A 1 902  ? 31.832 46.499  -31.192 1.00 12.61 ? 902  CYS A C   1 
ATOM   7405  O  O   . CYS A 1 902  ? 30.625 46.307  -31.095 1.00 13.41 ? 902  CYS A O   1 
ATOM   7406  C  CB  . CYS A 1 902  ? 32.287 48.895  -30.975 1.00 13.92 ? 902  CYS A CB  1 
ATOM   7407  S  SG  . CYS A 1 902  ? 33.096 50.355  -31.633 1.00 19.13 ? 902  CYS A SG  1 
ATOM   7408  N  N   . VAL A 1 903  ? 32.734 45.716  -30.620 1.00 11.60 ? 903  VAL A N   1 
ATOM   7409  C  CA  . VAL A 1 903  ? 32.328 44.607  -29.761 1.00 12.03 ? 903  VAL A CA  1 
ATOM   7410  C  C   . VAL A 1 903  ? 32.083 45.171  -28.352 1.00 12.02 ? 903  VAL A C   1 
ATOM   7411  O  O   . VAL A 1 903  ? 33.028 45.512  -27.616 1.00 12.53 ? 903  VAL A O   1 
ATOM   7412  C  CB  . VAL A 1 903  ? 33.401 43.518  -29.731 1.00 10.95 ? 903  VAL A CB  1 
ATOM   7413  C  CG1 . VAL A 1 903  ? 33.044 42.415  -28.745 1.00 13.16 ? 903  VAL A CG1 1 
ATOM   7414  C  CG2 . VAL A 1 903  ? 33.595 42.935  -31.131 1.00 11.78 ? 903  VAL A CG2 1 
ATOM   7415  N  N   . ARG A 1 904  ? 30.823 45.294  -28.002 1.00 11.32 ? 904  ARG A N   1 
ATOM   7416  C  CA  . ARG A 1 904  ? 30.440 45.876  -26.721 1.00 11.06 ? 904  ARG A CA  1 
ATOM   7417  C  C   . ARG A 1 904  ? 29.894 44.834  -25.791 1.00 11.33 ? 904  ARG A C   1 
ATOM   7418  O  O   . ARG A 1 904  ? 29.524 43.740  -26.220 1.00 10.87 ? 904  ARG A O   1 
ATOM   7419  C  CB  . ARG A 1 904  ? 29.365 46.917  -26.952 1.00 12.04 ? 904  ARG A CB  1 
ATOM   7420  C  CG  . ARG A 1 904  ? 29.925 48.161  -27.623 1.00 13.98 ? 904  ARG A CG  1 
ATOM   7421  C  CD  . ARG A 1 904  ? 28.907 49.244  -27.909 1.00 15.89 ? 904  ARG A CD  1 
ATOM   7422  N  NE  . ARG A 1 904  ? 28.122 48.903  -29.093 1.00 14.10 ? 904  ARG A NE  1 
ATOM   7423  C  CZ  . ARG A 1 904  ? 27.183 49.696  -29.602 1.00 17.12 ? 904  ARG A CZ  1 
ATOM   7424  N  NH1 . ARG A 1 904  ? 26.897 50.861  -29.018 1.00 16.70 ? 904  ARG A NH1 1 
ATOM   7425  N  NH2 . ARG A 1 904  ? 26.526 49.301  -30.687 1.00 18.31 ? 904  ARG A NH2 1 
ATOM   7426  N  N   . PRO A 1 905  ? 29.857 45.145  -24.503 1.00 9.71  ? 905  PRO A N   1 
ATOM   7427  C  CA  . PRO A 1 905  ? 29.229 44.230  -23.542 1.00 10.03 ? 905  PRO A CA  1 
ATOM   7428  C  C   . PRO A 1 905  ? 27.766 44.008  -23.884 1.00 10.15 ? 905  PRO A C   1 
ATOM   7429  O  O   . PRO A 1 905  ? 27.150 44.841  -24.549 1.00 11.17 ? 905  PRO A O   1 
ATOM   7430  C  CB  . PRO A 1 905  ? 29.359 44.979  -22.209 1.00 9.99  ? 905  PRO A CB  1 
ATOM   7431  C  CG  . PRO A 1 905  ? 30.551 45.920  -22.413 1.00 10.31 ? 905  PRO A CG  1 
ATOM   7432  C  CD  . PRO A 1 905  ? 30.427 46.353  -23.856 1.00 10.15 ? 905  PRO A CD  1 
ATOM   7433  N  N   . SER A 1 906  ? 27.221 42.882  -23.431 1.00 11.07 ? 906  SER A N   1 
ATOM   7434  C  CA  . SER A 1 906  ? 25.804 42.644  -23.618 1.00 13.80 ? 906  SER A CA  1 
ATOM   7435  C  C   . SER A 1 906  ? 24.954 43.607  -22.794 1.00 14.30 ? 906  SER A C   1 
ATOM   7436  O  O   . SER A 1 906  ? 25.462 44.311  -21.912 1.00 13.74 ? 906  SER A O   1 
ATOM   7437  C  CB  . SER A 1 906  ? 25.500 41.220  -23.231 1.00 16.02 ? 906  SER A CB  1 
ATOM   7438  O  OG  . SER A 1 906  ? 25.290 41.169  -21.851 1.00 19.90 ? 906  SER A OG  1 
ATOM   7439  N  N   . LYS A 1 907  ? 23.651 43.638  -23.065 1.00 15.18 ? 907  LYS A N   1 
ATOM   7440  C  CA  . LYS A 1 907  ? 22.760 44.604  -22.420 1.00 17.37 ? 907  LYS A CA  1 
ATOM   7441  C  C   . LYS A 1 907  ? 22.719 44.470  -20.887 1.00 15.90 ? 907  LYS A C   1 
ATOM   7442  O  O   . LYS A 1 907  ? 22.442 45.434  -20.165 1.00 17.84 ? 907  LYS A O   1 
ATOM   7443  C  CB  . LYS A 1 907  ? 21.351 44.504  -23.037 1.00 18.33 ? 907  LYS A CB  1 
ATOM   7444  C  CG  . LYS A 1 907  ? 21.304 45.036  -24.480 1.00 21.11 ? 907  LYS A CG  1 
ATOM   7445  C  CD  . LYS A 1 907  ? 19.889 45.033  -25.123 1.00 21.86 ? 907  LYS A CD  1 
ATOM   7446  C  CE  . LYS A 1 907  ? 18.746 44.873  -24.115 1.00 27.51 ? 907  LYS A CE  1 
ATOM   7447  N  NZ  . LYS A 1 907  ? 18.450 46.096  -23.300 1.00 29.96 ? 907  LYS A NZ  1 
ATOM   7448  N  N   . LEU A 1 908  ? 23.024 43.287  -20.380 1.00 14.91 ? 908  LEU A N   1 
ATOM   7449  C  CA  . LEU A 1 908  ? 22.968 43.087  -18.928 1.00 15.39 ? 908  LEU A CA  1 
ATOM   7450  C  C   . LEU A 1 908  ? 24.293 43.375  -18.220 1.00 13.66 ? 908  LEU A C   1 
ATOM   7451  O  O   . LEU A 1 908  ? 24.366 43.326  -17.000 1.00 14.68 ? 908  LEU A O   1 
ATOM   7452  C  CB  . LEU A 1 908  ? 22.474 41.672  -18.581 1.00 16.96 ? 908  LEU A CB  1 
ATOM   7453  C  CG  . LEU A 1 908  ? 21.009 41.402  -18.974 1.00 19.28 ? 908  LEU A CG  1 
ATOM   7454  C  CD1 . LEU A 1 908  ? 20.662 39.947  -18.744 1.00 21.58 ? 908  LEU A CD1 1 
ATOM   7455  C  CD2 . LEU A 1 908  ? 20.007 42.317  -18.255 1.00 23.41 ? 908  LEU A CD2 1 
ATOM   7456  N  N   . HIS A 1 909  ? 25.350 43.681  -18.973 1.00 11.52 ? 909  HIS A N   1 
ATOM   7457  C  CA  . HIS A 1 909  ? 26.645 43.974  -18.356 1.00 9.90  ? 909  HIS A CA  1 
ATOM   7458  C  C   . HIS A 1 909  ? 26.636 45.356  -17.676 1.00 9.30  ? 909  HIS A C   1 
ATOM   7459  O  O   . HIS A 1 909  ? 26.124 46.322  -18.252 1.00 9.85  ? 909  HIS A O   1 
ATOM   7460  C  CB  . HIS A 1 909  ? 27.733 43.935  -19.402 1.00 9.15  ? 909  HIS A CB  1 
ATOM   7461  C  CG  . HIS A 1 909  ? 29.086 43.672  -18.847 1.00 10.05 ? 909  HIS A CG  1 
ATOM   7462  N  ND1 . HIS A 1 909  ? 29.788 44.633  -18.139 1.00 11.38 ? 909  HIS A ND1 1 
ATOM   7463  C  CD2 . HIS A 1 909  ? 29.884 42.579  -18.906 1.00 9.53  ? 909  HIS A CD2 1 
ATOM   7464  C  CE1 . HIS A 1 909  ? 30.957 44.130  -17.783 1.00 11.58 ? 909  HIS A CE1 1 
ATOM   7465  N  NE2 . HIS A 1 909  ? 31.054 42.898  -18.266 1.00 11.60 ? 909  HIS A NE2 1 
ATOM   7466  N  N   . PRO A 1 910  ? 27.162 45.463  -16.461 1.00 7.96  ? 910  PRO A N   1 
ATOM   7467  C  CA  . PRO A 1 910  ? 27.140 46.762  -15.763 1.00 7.93  ? 910  PRO A CA  1 
ATOM   7468  C  C   . PRO A 1 910  ? 28.219 47.773  -16.167 1.00 6.89  ? 910  PRO A C   1 
ATOM   7469  O  O   . PRO A 1 910  ? 28.161 48.893  -15.632 1.00 7.03  ? 910  PRO A O   1 
ATOM   7470  C  CB  . PRO A 1 910  ? 27.273 46.382  -14.276 1.00 10.02 ? 910  PRO A CB  1 
ATOM   7471  C  CG  . PRO A 1 910  ? 27.680 44.994  -14.234 1.00 11.42 ? 910  PRO A CG  1 
ATOM   7472  C  CD  . PRO A 1 910  ? 27.599 44.347  -15.583 1.00 8.98  ? 910  PRO A CD  1 
ATOM   7473  N  N   . ALA A 1 911  ? 29.153 47.391  -17.021 1.00 7.11  ? 911  ALA A N   1 
ATOM   7474  C  CA  . ALA A 1 911  ? 30.247 48.282  -17.406 1.00 7.21  ? 911  ALA A CA  1 
ATOM   7475  C  C   . ALA A 1 911  ? 30.133 48.775  -18.821 1.00 7.74  ? 911  ALA A C   1 
ATOM   7476  O  O   . ALA A 1 911  ? 29.402 48.204  -19.653 1.00 8.04  ? 911  ALA A O   1 
ATOM   7477  C  CB  . ALA A 1 911  ? 31.581 47.575  -17.241 1.00 8.01  ? 911  ALA A CB  1 
ATOM   7478  N  N   . GLY A 1 912  ? 30.878 49.824  -19.106 1.00 7.17  ? 912  GLY A N   1 
ATOM   7479  C  CA  . GLY A 1 912  ? 31.155 50.237  -20.463 1.00 7.46  ? 912  GLY A CA  1 
ATOM   7480  C  C   . GLY A 1 912  ? 32.609 50.554  -20.600 1.00 6.30  ? 912  GLY A C   1 
ATOM   7481  O  O   . GLY A 1 912  ? 33.319 50.677  -19.602 1.00 7.07  ? 912  GLY A O   1 
ATOM   7482  N  N   . TYR A 1 913  ? 33.055 50.735  -21.833 1.00 6.32  ? 913  TYR A N   1 
ATOM   7483  C  CA  . TYR A 1 913  ? 34.463 50.908  -22.125 1.00 6.46  ? 913  TYR A CA  1 
ATOM   7484  C  C   . TYR A 1 913  ? 34.652 51.961  -23.191 1.00 6.69  ? 913  TYR A C   1 
ATOM   7485  O  O   . TYR A 1 913  ? 33.859 52.021  -24.152 1.00 8.24  ? 913  TYR A O   1 
ATOM   7486  C  CB  . TYR A 1 913  ? 35.153 49.592  -22.585 1.00 7.43  ? 913  TYR A CB  1 
ATOM   7487  C  CG  . TYR A 1 913  ? 35.067 48.551  -21.489 1.00 7.07  ? 913  TYR A CG  1 
ATOM   7488  C  CD1 . TYR A 1 913  ? 35.946 48.610  -20.409 1.00 7.91  ? 913  TYR A CD1 1 
ATOM   7489  C  CD2 . TYR A 1 913  ? 34.085 47.575  -21.493 1.00 6.74  ? 913  TYR A CD2 1 
ATOM   7490  C  CE1 . TYR A 1 913  ? 35.863 47.726  -19.379 1.00 6.88  ? 913  TYR A CE1 1 
ATOM   7491  C  CE2 . TYR A 1 913  ? 34.009 46.653  -20.435 1.00 7.49  ? 913  TYR A CE2 1 
ATOM   7492  C  CZ  . TYR A 1 913  ? 34.903 46.756  -19.391 1.00 8.52  ? 913  TYR A CZ  1 
ATOM   7493  O  OH  . TYR A 1 913  ? 34.785 45.871  -18.343 1.00 9.77  ? 913  TYR A OH  1 
ATOM   7494  N  N   . LEU A 1 914  ? 35.744 52.701  -23.081 1.00 7.25  ? 914  LEU A N   1 
ATOM   7495  C  CA  . LEU A 1 914  ? 36.058 53.719  -24.069 1.00 6.96  ? 914  LEU A CA  1 
ATOM   7496  C  C   . LEU A 1 914  ? 36.629 53.114  -25.341 1.00 8.07  ? 914  LEU A C   1 
ATOM   7497  O  O   . LEU A 1 914  ? 37.188 52.026  -25.329 1.00 8.89  ? 914  LEU A O   1 
ATOM   7498  C  CB  . LEU A 1 914  ? 37.090 54.695  -23.505 1.00 6.65  ? 914  LEU A CB  1 
ATOM   7499  C  CG  . LEU A 1 914  ? 36.619 55.594  -22.360 1.00 7.53  ? 914  LEU A CG  1 
ATOM   7500  C  CD1 . LEU A 1 914  ? 37.742 56.596  -22.053 1.00 8.72  ? 914  LEU A CD1 1 
ATOM   7501  C  CD2 . LEU A 1 914  ? 35.312 56.321  -22.710 1.00 8.24  ? 914  LEU A CD2 1 
ATOM   7502  N  N   . THR A 1 915  ? 36.505 53.865  -26.440 1.00 8.93  ? 915  THR A N   1 
ATOM   7503  C  CA  . THR A 1 915  ? 37.279 53.587  -27.633 1.00 9.55  ? 915  THR A CA  1 
ATOM   7504  C  C   . THR A 1 915  ? 38.698 54.141  -27.504 1.00 9.85  ? 915  THR A C   1 
ATOM   7505  O  O   . THR A 1 915  ? 38.962 54.999  -26.646 1.00 8.76  ? 915  THR A O   1 
ATOM   7506  C  CB  . THR A 1 915  ? 36.672 54.280  -28.824 1.00 10.86 ? 915  THR A CB  1 
ATOM   7507  O  OG1 . THR A 1 915  ? 36.591 55.703  -28.541 1.00 12.81 ? 915  THR A OG1 1 
ATOM   7508  C  CG2 . THR A 1 915  ? 35.264 53.789  -29.082 1.00 13.30 ? 915  THR A CG2 1 
ATOM   7509  N  N   . SER A 1 916  ? 39.600 53.743  -28.385 1.00 9.89  ? 916  SER A N   1 
ATOM   7510  C  CA  . SER A 1 916  ? 40.942 54.284  -28.417 1.00 10.66 ? 916  SER A CA  1 
ATOM   7511  C  C   . SER A 1 916  ? 40.921 55.798  -28.511 1.00 9.57  ? 916  SER A C   1 
ATOM   7512  O  O   . SER A 1 916  ? 41.627 56.460  -27.772 1.00 9.90  ? 916  SER A O   1 
ATOM   7513  C  CB  . SER A 1 916  ? 41.701 53.721  -29.634 1.00 12.19 ? 916  SER A CB  1 
ATOM   7514  O  OG  . SER A 1 916  ? 42.878 54.455  -29.895 1.00 18.99 ? 916  SER A OG  1 
ATOM   7515  N  N   . ALA A 1 917  ? 40.107 56.368  -29.399 1.00 8.99  ? 917  ALA A N   1 
ATOM   7516  C  CA  . ALA A 1 917  ? 40.179 57.829  -29.573 1.00 9.30  ? 917  ALA A CA  1 
ATOM   7517  C  C   . ALA A 1 917  ? 39.701 58.543  -28.321 1.00 8.72  ? 917  ALA A C   1 
ATOM   7518  O  O   . ALA A 1 917  ? 40.250 59.589  -27.954 1.00 8.89  ? 917  ALA A O   1 
ATOM   7519  C  CB  . ALA A 1 917  ? 39.369 58.287  -30.772 1.00 10.82 ? 917  ALA A CB  1 
ATOM   7520  N  N   . ALA A 1 918  ? 38.700 57.991  -27.629 1.00 7.79  ? 918  ALA A N   1 
ATOM   7521  C  CA  . ALA A 1 918  ? 38.222 58.653  -26.403 1.00 7.48  ? 918  ALA A CA  1 
ATOM   7522  C  C   . ALA A 1 918  ? 39.234 58.523  -25.279 1.00 7.12  ? 918  ALA A C   1 
ATOM   7523  O  O   . ALA A 1 918  ? 39.430 59.456  -24.503 1.00 6.93  ? 918  ALA A O   1 
ATOM   7524  C  CB  . ALA A 1 918  ? 36.851 58.134  -25.984 1.00 7.68  ? 918  ALA A CB  1 
ATOM   7525  N  N   . HIS A 1 919  ? 39.864 57.366  -25.154 1.00 6.78  ? 919  HIS A N   1 
ATOM   7526  C  CA  . HIS A 1 919  ? 40.897 57.224  -24.135 1.00 6.80  ? 919  HIS A CA  1 
ATOM   7527  C  C   . HIS A 1 919  ? 42.054 58.179  -24.415 1.00 6.34  ? 919  HIS A C   1 
ATOM   7528  O  O   . HIS A 1 919  ? 42.568 58.831  -23.487 1.00 7.80  ? 919  HIS A O   1 
ATOM   7529  C  CB  . HIS A 1 919  ? 41.344 55.746  -24.107 1.00 8.48  ? 919  HIS A CB  1 
ATOM   7530  C  CG  . HIS A 1 919  ? 42.537 55.480  -23.248 1.00 8.64  ? 919  HIS A CG  1 
ATOM   7531  N  ND1 . HIS A 1 919  ? 42.514 55.588  -21.875 1.00 13.51 ? 919  HIS A ND1 1 
ATOM   7532  C  CD2 . HIS A 1 919  ? 43.796 55.114  -23.582 1.00 10.31 ? 919  HIS A CD2 1 
ATOM   7533  C  CE1 . HIS A 1 919  ? 43.716 55.278  -21.399 1.00 9.53  ? 919  HIS A CE1 1 
ATOM   7534  N  NE2 . HIS A 1 919  ? 44.502 54.987  -22.411 1.00 13.75 ? 919  HIS A NE2 1 
ATOM   7535  N  N   . LYS A 1 920  ? 42.510 58.267  -25.669 1.00 7.06  ? 920  LYS A N   1 
ATOM   7536  C  CA  . LYS A 1 920  ? 43.589 59.195  -25.982 1.00 7.63  ? 920  LYS A CA  1 
ATOM   7537  C  C   . LYS A 1 920  ? 43.164 60.627  -25.688 1.00 6.62  ? 920  LYS A C   1 
ATOM   7538  O  O   . LYS A 1 920  ? 43.962 61.430  -25.204 1.00 6.74  ? 920  LYS A O   1 
ATOM   7539  C  CB  . LYS A 1 920  ? 44.082 59.030  -27.421 1.00 9.15  ? 920  LYS A CB  1 
ATOM   7540  C  CG  . LYS A 1 920  ? 44.944 57.786  -27.523 1.00 13.33 ? 920  LYS A CG  1 
ATOM   7541  C  CD  . LYS A 1 920  ? 45.746 57.749  -28.790 1.00 16.50 ? 920  LYS A CD  1 
ATOM   7542  C  CE  . LYS A 1 920  ? 46.617 56.503  -28.819 1.00 16.94 ? 920  LYS A CE  1 
ATOM   7543  N  NZ  . LYS A 1 920  ? 47.875 56.609  -27.981 1.00 18.12 ? 920  LYS A NZ  1 
ATOM   7544  N  N   . ALA A 1 921  ? 41.907 60.939  -25.982 1.00 6.68  ? 921  ALA A N   1 
ATOM   7545  C  CA  . ALA A 1 921  ? 41.424 62.286  -25.673 1.00 6.93  ? 921  ALA A CA  1 
ATOM   7546  C  C   . ALA A 1 921  ? 41.464 62.553  -24.167 1.00 6.94  ? 921  ALA A C   1 
ATOM   7547  O  O   . ALA A 1 921  ? 41.832 63.652  -23.711 1.00 6.92  ? 921  ALA A O   1 
ATOM   7548  C  CB  . ALA A 1 921  ? 39.993 62.467  -26.213 1.00 6.63  ? 921  ALA A CB  1 
ATOM   7549  N  N   . SER A 1 922  ? 41.078 61.548  -23.388 1.00 5.71  ? 922  SER A N   1 
ATOM   7550  C  CA  . SER A 1 922  ? 41.157 61.736  -21.933 1.00 5.63  ? 922  SER A CA  1 
ATOM   7551  C  C   . SER A 1 922  ? 42.621 61.977  -21.499 1.00 5.82  ? 922  SER A C   1 
ATOM   7552  O  O   . SER A 1 922  ? 42.925 62.851  -20.683 1.00 5.93  ? 922  SER A O   1 
ATOM   7553  C  CB  . SER A 1 922  ? 40.591 60.517  -21.213 1.00 6.57  ? 922  SER A CB  1 
ATOM   7554  O  OG  . SER A 1 922  ? 40.745 60.673  -19.804 1.00 7.15  ? 922  SER A OG  1 
ATOM   7555  N  N   . GLN A 1 923  ? 43.543 61.213  -22.052 1.00 6.33  ? 923  GLN A N   1 
ATOM   7556  C  CA  . GLN A 1 923  ? 44.960 61.394  -21.737 1.00 7.09  ? 923  GLN A CA  1 
ATOM   7557  C  C   . GLN A 1 923  ? 45.437 62.791  -22.146 1.00 7.13  ? 923  GLN A C   1 
ATOM   7558  O  O   . GLN A 1 923  ? 46.287 63.374  -21.461 1.00 8.18  ? 923  GLN A O   1 
ATOM   7559  C  CB  . GLN A 1 923  ? 45.836 60.303  -22.376 1.00 7.27  ? 923  GLN A CB  1 
ATOM   7560  C  CG  . GLN A 1 923  ? 45.543 58.939  -21.849 1.00 6.57  ? 923  GLN A CG  1 
ATOM   7561  C  CD  . GLN A 1 923  ? 46.448 57.897  -22.464 1.00 9.29  ? 923  GLN A CD  1 
ATOM   7562  O  OE1 . GLN A 1 923  ? 46.557 57.850  -23.696 1.00 10.22 ? 923  GLN A OE1 1 
ATOM   7563  N  NE2 . GLN A 1 923  ? 47.076 57.046  -21.623 1.00 9.69  ? 923  GLN A NE2 1 
ATOM   7564  N  N   . SER A 1 924  ? 44.912 63.360  -23.238 1.00 7.06  ? 924  SER A N   1 
ATOM   7565  C  CA  . SER A 1 924  ? 45.344 64.698  -23.668 1.00 8.32  ? 924  SER A CA  1 
ATOM   7566  C  C   . SER A 1 924  ? 44.934 65.740  -22.646 1.00 8.79  ? 924  SER A C   1 
ATOM   7567  O  O   . SER A 1 924  ? 45.527 66.833  -22.560 1.00 9.11  ? 924  SER A O   1 
ATOM   7568  C  CB  . SER A 1 924  ? 44.722 65.042  -25.029 1.00 9.18  ? 924  SER A CB  1 
ATOM   7569  O  OG  . SER A 1 924  ? 43.351 65.424  -24.928 1.00 9.77  ? 924  SER A OG  1 
ATOM   7570  N  N   . LEU A 1 925  ? 43.853 65.462  -21.921 1.00 7.47  ? 925  LEU A N   1 
ATOM   7571  C  CA  . LEU A 1 925  ? 43.380 66.384  -20.881 1.00 6.65  ? 925  LEU A CA  1 
ATOM   7572  C  C   . LEU A 1 925  ? 44.108 66.199  -19.558 1.00 7.52  ? 925  LEU A C   1 
ATOM   7573  O  O   . LEU A 1 925  ? 44.472 67.184  -18.906 1.00 9.17  ? 925  LEU A O   1 
ATOM   7574  C  CB  . LEU A 1 925  ? 41.864 66.222  -20.608 1.00 6.36  ? 925  LEU A CB  1 
ATOM   7575  C  CG  . LEU A 1 925  ? 40.982 66.497  -21.824 1.00 7.47  ? 925  LEU A CG  1 
ATOM   7576  C  CD1 . LEU A 1 925  ? 39.548 66.142  -21.473 1.00 8.23  ? 925  LEU A CD1 1 
ATOM   7577  C  CD2 . LEU A 1 925  ? 41.123 67.963  -22.264 1.00 10.51 ? 925  LEU A CD2 1 
ATOM   7578  N  N   . LEU A 1 926  ? 44.297 64.960  -19.140 1.00 7.21  ? 926  LEU A N   1 
ATOM   7579  C  CA  . LEU A 1 926  ? 44.848 64.710  -17.823 1.00 7.93  ? 926  LEU A CA  1 
ATOM   7580  C  C   . LEU A 1 926  ? 46.353 64.691  -17.802 1.00 8.03  ? 926  LEU A C   1 
ATOM   7581  O  O   . LEU A 1 926  ? 46.926 65.111  -16.781 1.00 8.54  ? 926  LEU A O   1 
ATOM   7582  C  CB  . LEU A 1 926  ? 44.277 63.428  -17.249 1.00 8.50  ? 926  LEU A CB  1 
ATOM   7583  C  CG  . LEU A 1 926  ? 42.768 63.544  -16.981 1.00 10.96 ? 926  LEU A CG  1 
ATOM   7584  C  CD1 . LEU A 1 926  ? 42.281 62.190  -16.454 1.00 14.29 ? 926  LEU A CD1 1 
ATOM   7585  C  CD2 . LEU A 1 926  ? 42.444 64.680  -16.013 1.00 12.50 ? 926  LEU A CD2 1 
ATOM   7586  N  N   . ASP A 1 927  ? 46.989 64.212  -18.870 1.00 7.06  ? 927  ASP A N   1 
ATOM   7587  C  CA  . ASP A 1 927  ? 48.458 64.153  -18.886 1.00 7.30  ? 927  ASP A CA  1 
ATOM   7588  C  C   . ASP A 1 927  ? 48.977 64.715  -20.199 1.00 6.99  ? 927  ASP A C   1 
ATOM   7589  O  O   . ASP A 1 927  ? 49.548 63.982  -20.998 1.00 7.33  ? 927  ASP A O   1 
ATOM   7590  C  CB  . ASP A 1 927  ? 48.972 62.735  -18.631 1.00 8.87  ? 927  ASP A CB  1 
ATOM   7591  C  CG  . ASP A 1 927  ? 48.636 62.256  -17.198 1.00 11.08 ? 927  ASP A CG  1 
ATOM   7592  O  OD1 . ASP A 1 927  ? 49.315 62.673  -16.181 1.00 10.20 ? 927  ASP A OD1 1 
ATOM   7593  O  OD2 . ASP A 1 927  ? 47.660 61.490  -17.018 1.00 12.53 ? 927  ASP A OD2 1 
ATOM   7594  N  N   . PRO A 1 928  ? 48.836 66.025  -20.383 1.00 7.29  ? 928  PRO A N   1 
ATOM   7595  C  CA  . PRO A 1 928  ? 49.332 66.692  -21.597 1.00 7.47  ? 928  PRO A CA  1 
ATOM   7596  C  C   . PRO A 1 928  ? 50.852 66.677  -21.615 1.00 7.79  ? 928  PRO A C   1 
ATOM   7597  O  O   . PRO A 1 928  ? 51.496 66.419  -20.593 1.00 8.27  ? 928  PRO A O   1 
ATOM   7598  C  CB  . PRO A 1 928  ? 48.814 68.129  -21.432 1.00 8.91  ? 928  PRO A CB  1 
ATOM   7599  C  CG  . PRO A 1 928  ? 48.708 68.314  -20.012 1.00 10.53 ? 928  PRO A CG  1 
ATOM   7600  C  CD  . PRO A 1 928  ? 48.265 66.976  -19.410 1.00 8.99  ? 928  PRO A CD  1 
ATOM   7601  N  N   . LEU A 1 929  ? 51.448 66.991  -22.763 1.00 7.54  ? 929  LEU A N   1 
ATOM   7602  C  CA  . LEU A 1 929  ? 52.872 67.316  -22.750 1.00 8.25  ? 929  LEU A CA  1 
ATOM   7603  C  C   . LEU A 1 929  ? 53.142 68.473  -21.818 1.00 8.34  ? 929  LEU A C   1 
ATOM   7604  O  O   . LEU A 1 929  ? 52.335 69.393  -21.725 1.00 9.92  ? 929  LEU A O   1 
ATOM   7605  C  CB  . LEU A 1 929  ? 53.342 67.707  -24.155 1.00 8.38  ? 929  LEU A CB  1 
ATOM   7606  C  CG  . LEU A 1 929  ? 53.234 66.661  -25.249 1.00 8.77  ? 929  LEU A CG  1 
ATOM   7607  C  CD1 . LEU A 1 929  ? 53.792 67.232  -26.575 1.00 8.97  ? 929  LEU A CD1 1 
ATOM   7608  C  CD2 . LEU A 1 929  ? 53.964 65.361  -24.848 1.00 8.60  ? 929  LEU A CD2 1 
ATOM   7609  N  N   . ASP A 1 930  ? 54.250 68.416  -21.101 1.00 7.29  ? 930  ASP A N   1 
ATOM   7610  C  CA  . ASP A 1 930  ? 54.758 69.541  -20.323 1.00 7.45  ? 930  ASP A CA  1 
ATOM   7611  C  C   . ASP A 1 930  ? 55.685 70.389  -21.178 1.00 8.14  ? 930  ASP A C   1 
ATOM   7612  O  O   . ASP A 1 930  ? 56.406 69.865  -21.957 1.00 8.35  ? 930  ASP A O   1 
ATOM   7613  C  CB  . ASP A 1 930  ? 55.493 69.018  -19.089 1.00 7.46  ? 930  ASP A CB  1 
ATOM   7614  C  CG  . ASP A 1 930  ? 54.703 67.956  -18.378 1.00 11.18 ? 930  ASP A CG  1 
ATOM   7615  O  OD1 . ASP A 1 930  ? 53.642 68.334  -17.893 1.00 14.02 ? 930  ASP A OD1 1 
ATOM   7616  O  OD2 . ASP A 1 930  ? 55.100 66.776  -18.346 1.00 11.09 ? 930  ASP A OD2 1 
ATOM   7617  N  N   . LYS A 1 931  ? 55.640 71.694  -20.996 1.00 7.96  ? 931  LYS A N   1 
ATOM   7618  C  CA  . LYS A 1 931  ? 56.401 72.629  -21.828 1.00 8.02  ? 931  LYS A CA  1 
ATOM   7619  C  C   . LYS A 1 931  ? 57.323 73.425  -20.943 1.00 8.51  ? 931  LYS A C   1 
ATOM   7620  O  O   . LYS A 1 931  ? 56.897 74.025  -19.951 1.00 8.92  ? 931  LYS A O   1 
ATOM   7621  C  CB  . LYS A 1 931  ? 55.432 73.590  -22.546 1.00 8.43  ? 931  LYS A CB  1 
ATOM   7622  C  CG  . LYS A 1 931  ? 54.455 72.968  -23.539 1.00 11.63 ? 931  LYS A CG  1 
ATOM   7623  C  CD  . LYS A 1 931  ? 53.592 74.057  -24.217 1.00 12.36 ? 931  LYS A CD  1 
ATOM   7624  C  CE  . LYS A 1 931  ? 52.626 74.734  -23.247 1.00 17.34 ? 931  LYS A CE  1 
ATOM   7625  N  NZ  . LYS A 1 931  ? 51.822 75.818  -23.873 1.00 18.31 ? 931  LYS A NZ  1 
ATOM   7626  N  N   . PHE A 1 932  ? 58.604 73.429  -21.284 1.00 7.32  ? 932  PHE A N   1 
ATOM   7627  C  CA  . PHE A 1 932  ? 59.618 74.153  -20.548 1.00 7.21  ? 932  PHE A CA  1 
ATOM   7628  C  C   . PHE A 1 932  ? 60.277 75.202  -21.459 1.00 7.52  ? 932  PHE A C   1 
ATOM   7629  O  O   . PHE A 1 932  ? 60.599 74.883  -22.608 1.00 8.45  ? 932  PHE A O   1 
ATOM   7630  C  CB  . PHE A 1 932  ? 60.699 73.216  -20.071 1.00 7.64  ? 932  PHE A CB  1 
ATOM   7631  C  CG  . PHE A 1 932  ? 60.214 72.124  -19.162 1.00 7.69  ? 932  PHE A CG  1 
ATOM   7632  C  CD1 . PHE A 1 932  ? 59.679 70.963  -19.686 1.00 7.64  ? 932  PHE A CD1 1 
ATOM   7633  C  CD2 . PHE A 1 932  ? 60.314 72.279  -17.777 1.00 9.44  ? 932  PHE A CD2 1 
ATOM   7634  C  CE1 . PHE A 1 932  ? 59.259 69.905  -18.831 1.00 8.76  ? 932  PHE A CE1 1 
ATOM   7635  C  CE2 . PHE A 1 932  ? 59.907 71.253  -16.900 1.00 10.67 ? 932  PHE A CE2 1 
ATOM   7636  C  CZ  . PHE A 1 932  ? 59.366 70.085  -17.422 1.00 9.71  ? 932  PHE A CZ  1 
ATOM   7637  N  N   . ILE A 1 933  ? 60.525 76.392  -20.916 1.00 7.07  ? 933  ILE A N   1 
ATOM   7638  C  CA  . ILE A 1 933  ? 61.195 77.442  -21.687 1.00 7.13  ? 933  ILE A CA  1 
ATOM   7639  C  C   . ILE A 1 933  ? 62.529 77.668  -21.029 1.00 7.83  ? 933  ILE A C   1 
ATOM   7640  O  O   . ILE A 1 933  ? 62.586 77.949  -19.836 1.00 8.10  ? 933  ILE A O   1 
ATOM   7641  C  CB  . ILE A 1 933  ? 60.385 78.740  -21.682 1.00 7.15  ? 933  ILE A CB  1 
ATOM   7642  C  CG1 . ILE A 1 933  ? 58.982 78.524  -22.215 1.00 7.59  ? 933  ILE A CG1 1 
ATOM   7643  C  CG2 . ILE A 1 933  ? 61.101 79.837  -22.497 1.00 8.74  ? 933  ILE A CG2 1 
ATOM   7644  C  CD1 . ILE A 1 933  ? 58.057 79.730  -22.010 1.00 9.46  ? 933  ILE A CD1 1 
ATOM   7645  N  N   . PHE A 1 934  ? 63.628 77.539  -21.786 1.00 7.83  ? 934  PHE A N   1 
ATOM   7646  C  CA  . PHE A 1 934  ? 64.945 77.778  -21.204 1.00 9.37  ? 934  PHE A CA  1 
ATOM   7647  C  C   . PHE A 1 934  ? 65.071 79.237  -20.723 1.00 9.75  ? 934  PHE A C   1 
ATOM   7648  O  O   . PHE A 1 934  ? 64.710 80.169  -21.447 1.00 10.02 ? 934  PHE A O   1 
ATOM   7649  C  CB  . PHE A 1 934  ? 66.071 77.407  -22.174 1.00 9.74  ? 934  PHE A CB  1 
ATOM   7650  C  CG  . PHE A 1 934  ? 67.416 77.472  -21.545 1.00 9.93  ? 934  PHE A CG  1 
ATOM   7651  C  CD1 . PHE A 1 934  ? 67.825 76.503  -20.636 1.00 10.73 ? 934  PHE A CD1 1 
ATOM   7652  C  CD2 . PHE A 1 934  ? 68.257 78.566  -21.787 1.00 12.53 ? 934  PHE A CD2 1 
ATOM   7653  C  CE1 . PHE A 1 934  ? 69.078 76.585  -20.016 1.00 15.47 ? 934  PHE A CE1 1 
ATOM   7654  C  CE2 . PHE A 1 934  ? 69.489 78.664  -21.178 1.00 15.04 ? 934  PHE A CE2 1 
ATOM   7655  C  CZ  . PHE A 1 934  ? 69.912 77.689  -20.283 1.00 14.84 ? 934  PHE A CZ  1 
ATOM   7656  N  N   . ALA A 1 935  ? 65.540 79.427  -19.489 1.00 10.52 ? 935  ALA A N   1 
ATOM   7657  C  CA  . ALA A 1 935  ? 65.414 80.741  -18.861 1.00 13.39 ? 935  ALA A CA  1 
ATOM   7658  C  C   . ALA A 1 935  ? 66.498 81.725  -19.259 1.00 16.06 ? 935  ALA A C   1 
ATOM   7659  O  O   . ALA A 1 935  ? 66.249 82.943  -19.267 1.00 19.19 ? 935  ALA A O   1 
ATOM   7660  C  CB  . ALA A 1 935  ? 65.377 80.609  -17.352 1.00 14.99 ? 935  ALA A CB  1 
ATOM   7661  N  N   . GLU A 1 936  ? 67.684 81.228  -19.572 1.00 16.32 ? 936  GLU A N   1 
ATOM   7662  C  CA  . GLU A 1 936  ? 68.796 82.137  -19.841 1.00 17.41 ? 936  GLU A CA  1 
ATOM   7663  C  C   . GLU A 1 936  ? 69.047 82.254  -21.336 1.00 16.50 ? 936  GLU A C   1 
ATOM   7664  O  O   . GLU A 1 936  ? 68.336 81.672  -22.148 1.00 16.38 ? 936  GLU A O   1 
ATOM   7665  C  CB  . GLU A 1 936  ? 70.042 81.729  -19.054 1.00 19.22 ? 936  GLU A CB  1 
ATOM   7666  C  CG  . GLU A 1 936  ? 69.866 81.920  -17.550 1.00 24.17 ? 936  GLU A CG  1 
ATOM   7667  C  CD  . GLU A 1 936  ? 69.479 83.346  -17.153 1.00 31.40 ? 936  GLU A CD  1 
ATOM   7668  O  OE1 . GLU A 1 936  ? 69.984 84.316  -17.777 1.00 34.60 ? 936  GLU A OE1 1 
ATOM   7669  O  OE2 . GLU A 1 936  ? 68.665 83.512  -16.206 1.00 34.95 ? 936  GLU A OE2 1 
ATOM   7670  N  N   . ASN A 1 937  ? 70.066 83.012  -21.720 1.00 16.25 ? 937  ASN A N   1 
ATOM   7671  C  CA  . ASN A 1 937  ? 70.203 83.266  -23.142 1.00 15.98 ? 937  ASN A CA  1 
ATOM   7672  C  C   . ASN A 1 937  ? 70.746 82.102  -23.953 1.00 15.00 ? 937  ASN A C   1 
ATOM   7673  O  O   . ASN A 1 937  ? 70.339 81.906  -25.088 1.00 15.67 ? 937  ASN A O   1 
ATOM   7674  C  CB  . ASN A 1 937  ? 71.085 84.489  -23.368 1.00 15.33 ? 937  ASN A CB  1 
ATOM   7675  C  CG  . ASN A 1 937  ? 70.359 85.790  -23.071 1.00 18.13 ? 937  ASN A CG  1 
ATOM   7676  O  OD1 . ASN A 1 937  ? 69.128 85.826  -22.959 1.00 19.43 ? 937  ASN A OD1 1 
ATOM   7677  N  ND2 . ASN A 1 937  ? 71.119 86.876  -22.970 1.00 20.64 ? 937  ASN A ND2 1 
ATOM   7678  N  N   . GLU A 1 938  ? 71.685 81.352  -23.373 1.00 15.87 ? 938  GLU A N   1 
ATOM   7679  C  CA  . GLU A 1 938  ? 72.325 80.266  -24.084 1.00 16.32 ? 938  GLU A CA  1 
ATOM   7680  C  C   . GLU A 1 938  ? 72.406 79.040  -23.200 1.00 15.31 ? 938  GLU A C   1 
ATOM   7681  O  O   . GLU A 1 938  ? 72.805 79.132  -22.050 1.00 16.31 ? 938  GLU A O   1 
ATOM   7682  C  CB  . GLU A 1 938  ? 73.741 80.640  -24.548 1.00 17.71 ? 938  GLU A CB  1 
ATOM   7683  C  CG  . GLU A 1 938  ? 74.435 79.440  -25.170 1.00 22.45 ? 938  GLU A CG  1 
ATOM   7684  C  CD  . GLU A 1 938  ? 75.721 79.761  -25.902 1.00 29.58 ? 938  GLU A CD  1 
ATOM   7685  O  OE1 . GLU A 1 938  ? 76.409 80.753  -25.543 1.00 31.90 ? 938  GLU A OE1 1 
ATOM   7686  O  OE2 . GLU A 1 938  ? 76.045 78.989  -26.842 1.00 32.61 ? 938  GLU A OE2 1 
ATOM   7687  N  N   . TRP A 1 939  ? 72.046 77.899  -23.774 1.00 16.20 ? 939  TRP A N   1 
ATOM   7688  C  CA  . TRP A 1 939  ? 72.123 76.631  -23.070 1.00 15.98 ? 939  TRP A CA  1 
ATOM   7689  C  C   . TRP A 1 939  ? 73.314 75.852  -23.622 1.00 16.67 ? 939  TRP A C   1 
ATOM   7690  O  O   . TRP A 1 939  ? 73.223 75.236  -24.682 1.00 18.06 ? 939  TRP A O   1 
ATOM   7691  C  CB  . TRP A 1 939  ? 70.803 75.898  -23.289 1.00 14.54 ? 939  TRP A CB  1 
ATOM   7692  C  CG  . TRP A 1 939  ? 70.668 74.545  -22.663 1.00 12.03 ? 939  TRP A CG  1 
ATOM   7693  C  CD1 . TRP A 1 939  ? 71.518 73.920  -21.797 1.00 13.94 ? 939  TRP A CD1 1 
ATOM   7694  C  CD2 . TRP A 1 939  ? 69.565 73.658  -22.866 1.00 10.94 ? 939  TRP A CD2 1 
ATOM   7695  N  NE1 . TRP A 1 939  ? 71.013 72.686  -21.455 1.00 12.06 ? 939  TRP A NE1 1 
ATOM   7696  C  CE2 . TRP A 1 939  ? 69.819 72.500  -22.108 1.00 9.89  ? 939  TRP A CE2 1 
ATOM   7697  C  CE3 . TRP A 1 939  ? 68.386 73.721  -23.635 1.00 11.29 ? 939  TRP A CE3 1 
ATOM   7698  C  CZ2 . TRP A 1 939  ? 68.934 71.422  -22.075 1.00 11.35 ? 939  TRP A CZ2 1 
ATOM   7699  C  CZ3 . TRP A 1 939  ? 67.519 72.659  -23.621 1.00 11.78 ? 939  TRP A CZ3 1 
ATOM   7700  C  CH2 . TRP A 1 939  ? 67.799 71.521  -22.839 1.00 11.30 ? 939  TRP A CH2 1 
ATOM   7701  N  N   . ILE A 1 940  ? 74.435 75.905  -22.895 1.00 18.70 ? 940  ILE A N   1 
ATOM   7702  C  CA  . ILE A 1 940  ? 75.645 75.203  -23.326 1.00 19.30 ? 940  ILE A CA  1 
ATOM   7703  C  C   . ILE A 1 940  ? 75.491 73.703  -23.017 1.00 17.40 ? 940  ILE A C   1 
ATOM   7704  O  O   . ILE A 1 940  ? 75.063 73.340  -21.930 1.00 17.97 ? 940  ILE A O   1 
ATOM   7705  C  CB  . ILE A 1 940  ? 76.899 75.820  -22.669 1.00 20.12 ? 940  ILE A CB  1 
ATOM   7706  C  CG1 . ILE A 1 940  ? 77.043 77.289  -23.102 1.00 20.97 ? 940  ILE A CG1 1 
ATOM   7707  C  CG2 . ILE A 1 940  ? 78.164 75.017  -23.026 1.00 21.40 ? 940  ILE A CG2 1 
ATOM   7708  C  CD1 . ILE A 1 940  ? 78.291 77.985  -22.597 1.00 21.90 ? 940  ILE A CD1 1 
ATOM   7709  N  N   . GLY A 1 941  ? 75.795 72.849  -23.985 1.00 16.97 ? 941  GLY A N   1 
ATOM   7710  C  CA  . GLY A 1 941  ? 75.698 71.408  -23.773 1.00 15.87 ? 941  GLY A CA  1 
ATOM   7711  C  C   . GLY A 1 941  ? 74.314 70.819  -24.053 1.00 15.48 ? 941  GLY A C   1 
ATOM   7712  O  O   . GLY A 1 941  ? 74.087 69.632  -23.802 1.00 13.93 ? 941  GLY A O   1 
ATOM   7713  N  N   . ALA A 1 942  ? 73.409 71.632  -24.600 1.00 14.41 ? 942  ALA A N   1 
ATOM   7714  C  CA  . ALA A 1 942  ? 72.029 71.199  -24.861 1.00 14.23 ? 942  ALA A CA  1 
ATOM   7715  C  C   . ALA A 1 942  ? 71.988 69.982  -25.748 1.00 14.87 ? 942  ALA A C   1 
ATOM   7716  O  O   . ALA A 1 942  ? 72.754 69.901  -26.717 1.00 15.15 ? 942  ALA A O   1 
ATOM   7717  C  CB  . ALA A 1 942  ? 71.218 72.320  -25.504 1.00 14.90 ? 942  ALA A CB  1 
ATOM   7718  N  N   . GLN A 1 943  ? 71.104 69.039  -25.415 1.00 14.46 ? 943  GLN A N   1 
ATOM   7719  C  CA  . GLN A 1 943  ? 70.844 67.881  -26.243 1.00 14.39 ? 943  GLN A CA  1 
ATOM   7720  C  C   . GLN A 1 943  ? 69.416 67.874  -26.787 1.00 12.97 ? 943  GLN A C   1 
ATOM   7721  O  O   . GLN A 1 943  ? 68.527 68.516  -26.205 1.00 14.22 ? 943  GLN A O   1 
ATOM   7722  C  CB  . GLN A 1 943  ? 71.118 66.589  -25.459 1.00 16.01 ? 943  GLN A CB  1 
ATOM   7723  C  CG  . GLN A 1 943  ? 72.494 66.589  -24.810 1.00 20.65 ? 943  GLN A CG  1 
ATOM   7724  C  CD  . GLN A 1 943  ? 72.721 65.365  -23.975 1.00 26.62 ? 943  GLN A CD  1 
ATOM   7725  O  OE1 . GLN A 1 943  ? 71.780 64.849  -23.356 1.00 29.47 ? 943  GLN A OE1 1 
ATOM   7726  N  NE2 . GLN A 1 943  ? 73.965 64.894  -23.937 1.00 29.30 ? 943  GLN A NE2 1 
ATOM   7727  N  N   . GLY A 1 944  ? 69.188 67.127  -27.855 1.00 13.41 ? 944  GLY A N   1 
ATOM   7728  C  CA  . GLY A 1 944  ? 67.962 67.209  -28.603 1.00 12.95 ? 944  GLY A CA  1 
ATOM   7729  C  C   . GLY A 1 944  ? 66.836 66.349  -28.089 1.00 13.04 ? 944  GLY A C   1 
ATOM   7730  O  O   . GLY A 1 944  ? 65.645 66.580  -28.367 1.00 12.47 ? 944  GLY A O   1 
ATOM   7731  N  N   . GLN A 1 945  ? 67.198 65.317  -27.355 1.00 11.74 ? 945  GLN A N   1 
ATOM   7732  C  CA  . GLN A 1 945  ? 66.190 64.322  -27.023 1.00 12.90 ? 945  GLN A CA  1 
ATOM   7733  C  C   . GLN A 1 945  ? 66.642 63.488  -25.846 1.00 11.42 ? 945  GLN A C   1 
ATOM   7734  O  O   . GLN A 1 945  ? 67.843 63.326  -25.584 1.00 11.95 ? 945  GLN A O   1 
ATOM   7735  C  CB  . GLN A 1 945  ? 65.989 63.405  -28.232 1.00 12.51 ? 945  GLN A CB  1 
ATOM   7736  C  CG  . GLN A 1 945  ? 64.709 62.588  -28.261 1.00 15.66 ? 945  GLN A CG  1 
ATOM   7737  C  CD  . GLN A 1 945  ? 64.658 61.650  -29.467 1.00 15.93 ? 945  GLN A CD  1 
ATOM   7738  O  OE1 . GLN A 1 945  ? 63.779 61.767  -30.323 1.00 21.60 ? 945  GLN A OE1 1 
ATOM   7739  N  NE2 . GLN A 1 945  ? 65.598 60.725  -29.529 1.00 20.70 ? 945  GLN A NE2 1 
ATOM   7740  N  N   . PHE A 1 946  ? 65.650 63.008  -25.100 1.00 9.82  ? 946  PHE A N   1 
ATOM   7741  C  CA  . PHE A 1 946  ? 65.876 61.978  -24.089 1.00 8.77  ? 946  PHE A CA  1 
ATOM   7742  C  C   . PHE A 1 946  ? 64.804 60.945  -24.238 1.00 8.38  ? 946  PHE A C   1 
ATOM   7743  O  O   . PHE A 1 946  ? 63.652 61.273  -24.446 1.00 8.00  ? 946  PHE A O   1 
ATOM   7744  C  CB  . PHE A 1 946  ? 65.855 62.567  -22.681 1.00 8.18  ? 946  PHE A CB  1 
ATOM   7745  C  CG  . PHE A 1 946  ? 65.759 61.526  -21.597 1.00 8.65  ? 946  PHE A CG  1 
ATOM   7746  C  CD1 . PHE A 1 946  ? 66.844 60.719  -21.286 1.00 9.76  ? 946  PHE A CD1 1 
ATOM   7747  C  CD2 . PHE A 1 946  ? 64.569 61.357  -20.898 1.00 9.92  ? 946  PHE A CD2 1 
ATOM   7748  C  CE1 . PHE A 1 946  ? 66.713 59.730  -20.284 1.00 10.19 ? 946  PHE A CE1 1 
ATOM   7749  C  CE2 . PHE A 1 946  ? 64.454 60.372  -19.929 1.00 9.48  ? 946  PHE A CE2 1 
ATOM   7750  C  CZ  . PHE A 1 946  ? 65.502 59.557  -19.622 1.00 10.85 ? 946  PHE A CZ  1 
ATOM   7751  N  N   . GLY A 1 947  ? 65.183 59.663  -24.148 1.00 9.04  ? 947  GLY A N   1 
ATOM   7752  C  CA  . GLY A 1 947  ? 64.216 58.583  -24.159 1.00 9.89  ? 947  GLY A CA  1 
ATOM   7753  C  C   . GLY A 1 947  ? 63.865 57.991  -25.512 1.00 9.71  ? 947  GLY A C   1 
ATOM   7754  O  O   . GLY A 1 947  ? 62.921 57.213  -25.643 1.00 10.38 ? 947  GLY A O   1 
ATOM   7755  N  N   . GLY A 1 948  ? 64.649 58.338  -26.543 1.00 12.60 ? 948  GLY A N   1 
ATOM   7756  C  CA  . GLY A 1 948  ? 64.411 57.787  -27.851 1.00 13.58 ? 948  GLY A CA  1 
ATOM   7757  C  C   . GLY A 1 948  ? 64.469 56.266  -27.886 1.00 14.70 ? 948  GLY A C   1 
ATOM   7758  O  O   . GLY A 1 948  ? 63.860 55.667  -28.777 1.00 16.99 ? 948  GLY A O   1 
ATOM   7759  N  N   . ASP A 1 949  ? 65.164 55.649  -26.923 1.00 14.63 ? 949  ASP A N   1 
ATOM   7760  C  CA  . ASP A 1 949  ? 65.255 54.181  -26.877 1.00 16.66 ? 949  ASP A CA  1 
ATOM   7761  C  C   . ASP A 1 949  ? 64.283 53.535  -25.888 1.00 16.11 ? 949  ASP A C   1 
ATOM   7762  O  O   . ASP A 1 949  ? 64.310 52.320  -25.648 1.00 17.37 ? 949  ASP A O   1 
ATOM   7763  C  CB  . ASP A 1 949  ? 66.697 53.733  -26.602 1.00 17.47 ? 949  ASP A CB  1 
ATOM   7764  C  CG  . ASP A 1 949  ? 67.248 54.261  -25.276 1.00 22.13 ? 949  ASP A CG  1 
ATOM   7765  O  OD1 . ASP A 1 949  ? 66.625 55.149  -24.629 1.00 25.76 ? 949  ASP A OD1 1 
ATOM   7766  O  OD2 . ASP A 1 949  ? 68.330 53.844  -24.784 1.00 27.71 ? 949  ASP A OD2 1 
ATOM   7767  N  N   . HIS A 1 950  ? 63.401 54.348  -25.300 1.00 13.94 ? 950  HIS A N   1 
ATOM   7768  C  CA  . HIS A 1 950  ? 62.363 53.799  -24.414 1.00 12.70 ? 950  HIS A CA  1 
ATOM   7769  C  C   . HIS A 1 950  ? 61.324 53.057  -25.241 1.00 12.92 ? 950  HIS A C   1 
ATOM   7770  O  O   . HIS A 1 950  ? 60.911 53.531  -26.282 1.00 12.76 ? 950  HIS A O   1 
ATOM   7771  C  CB  . HIS A 1 950  ? 61.643 54.921  -23.645 1.00 11.86 ? 950  HIS A CB  1 
ATOM   7772  C  CG  . HIS A 1 950  ? 62.500 55.641  -22.655 1.00 9.90  ? 950  HIS A CG  1 
ATOM   7773  N  ND1 . HIS A 1 950  ? 62.117 56.820  -22.057 1.00 9.53  ? 950  HIS A ND1 1 
ATOM   7774  C  CD2 . HIS A 1 950  ? 63.729 55.356  -22.152 1.00 10.52 ? 950  HIS A CD2 1 
ATOM   7775  C  CE1 . HIS A 1 950  ? 63.063 57.233  -21.232 1.00 11.14 ? 950  HIS A CE1 1 
ATOM   7776  N  NE2 . HIS A 1 950  ? 64.060 56.366  -21.275 1.00 11.10 ? 950  HIS A NE2 1 
ATOM   7777  N  N   . PRO A 1 951  ? 60.880 51.893  -24.777 1.00 13.74 ? 951  PRO A N   1 
ATOM   7778  C  CA  . PRO A 1 951  ? 59.849 51.126  -25.483 1.00 14.13 ? 951  PRO A CA  1 
ATOM   7779  C  C   . PRO A 1 951  ? 58.562 51.924  -25.623 1.00 13.49 ? 951  PRO A C   1 
ATOM   7780  O  O   . PRO A 1 951  ? 58.202 52.623  -24.664 1.00 14.09 ? 951  PRO A O   1 
ATOM   7781  C  CB  . PRO A 1 951  ? 59.622 49.912  -24.564 1.00 14.59 ? 951  PRO A CB  1 
ATOM   7782  C  CG  . PRO A 1 951  ? 60.874 49.819  -23.762 1.00 17.45 ? 951  PRO A CG  1 
ATOM   7783  C  CD  . PRO A 1 951  ? 61.348 51.231  -23.542 1.00 14.10 ? 951  PRO A CD  1 
ATOM   7784  N  N   . SER A 1 952  ? 57.903 51.842  -26.772 1.00 12.52 ? 952  SER A N   1 
ATOM   7785  C  CA  . SER A 1 952  ? 56.636 52.522  -27.009 1.00 11.16 ? 952  SER A CA  1 
ATOM   7786  C  C   . SER A 1 952  ? 55.548 51.481  -26.813 1.00 11.67 ? 952  SER A C   1 
ATOM   7787  O  O   . SER A 1 952  ? 55.299 50.634  -27.686 1.00 11.95 ? 952  SER A O   1 
ATOM   7788  C  CB  . SER A 1 952  ? 56.595 53.153  -28.415 1.00 12.29 ? 952  SER A CB  1 
ATOM   7789  O  OG  . SER A 1 952  ? 55.501 54.056  -28.537 1.00 11.72 ? 952  SER A OG  1 
ATOM   7790  N  N   . ALA A 1 953  ? 54.923 51.524  -25.635 1.00 11.27 ? 953  ALA A N   1 
ATOM   7791  C  CA  . ALA A 1 953  ? 53.990 50.475  -25.208 1.00 10.63 ? 953  ALA A CA  1 
ATOM   7792  C  C   . ALA A 1 953  ? 52.639 50.567  -25.900 1.00 10.35 ? 953  ALA A C   1 
ATOM   7793  O  O   . ALA A 1 953  ? 52.252 51.638  -26.416 1.00 9.79  ? 953  ALA A O   1 
ATOM   7794  C  CB  . ALA A 1 953  ? 53.821 50.535  -23.684 1.00 11.62 ? 953  ALA A CB  1 
ATOM   7795  N  N   A ARG A 1 954  ? 51.920 49.450  -25.923 0.50 10.01 ? 954  ARG A N   1 
ATOM   7796  N  N   B ARG A 1 954  ? 51.921 49.450  -25.918 0.50 9.43  ? 954  ARG A N   1 
ATOM   7797  C  CA  A ARG A 1 954  ? 50.563 49.423  -26.428 0.50 10.92 ? 954  ARG A CA  1 
ATOM   7798  C  CA  B ARG A 1 954  ? 50.571 49.437  -26.426 0.50 9.75  ? 954  ARG A CA  1 
ATOM   7799  C  C   A ARG A 1 954  ? 49.717 50.530  -25.791 0.50 10.14 ? 954  ARG A C   1 
ATOM   7800  C  C   B ARG A 1 954  ? 49.719 50.535  -25.789 0.50 9.57  ? 954  ARG A C   1 
ATOM   7801  O  O   A ARG A 1 954  ? 49.854 50.827  -24.623 0.50 10.15 ? 954  ARG A O   1 
ATOM   7802  O  O   B ARG A 1 954  ? 49.852 50.830  -24.621 0.50 9.72  ? 954  ARG A O   1 
ATOM   7803  C  CB  A ARG A 1 954  ? 49.915 48.052  -26.187 0.50 11.18 ? 954  ARG A CB  1 
ATOM   7804  C  CB  B ARG A 1 954  ? 49.898 48.072  -26.256 0.50 9.85  ? 954  ARG A CB  1 
ATOM   7805  C  CG  A ARG A 1 954  ? 48.772 47.699  -27.149 0.50 14.02 ? 954  ARG A CG  1 
ATOM   7806  C  CG  B ARG A 1 954  ? 48.705 47.918  -27.205 0.50 11.32 ? 954  ARG A CG  1 
ATOM   7807  C  CD  A ARG A 1 954  ? 48.170 46.320  -26.781 0.50 13.58 ? 954  ARG A CD  1 
ATOM   7808  C  CD  B ARG A 1 954  ? 48.203 46.492  -27.324 0.50 10.30 ? 954  ARG A CD  1 
ATOM   7809  N  NE  A ARG A 1 954  ? 48.027 46.233  -25.329 0.50 19.63 ? 954  ARG A NE  1 
ATOM   7810  N  NE  B ARG A 1 954  ? 47.256 46.186  -26.278 0.50 10.34 ? 954  ARG A NE  1 
ATOM   7811  C  CZ  A ARG A 1 954  ? 48.933 45.757  -24.459 0.50 19.15 ? 954  ARG A CZ  1 
ATOM   7812  C  CZ  B ARG A 1 954  ? 46.635 45.025  -26.153 0.50 12.95 ? 954  ARG A CZ  1 
ATOM   7813  N  NH1 A ARG A 1 954  ? 50.115 45.231  -24.850 0.50 15.00 ? 954  ARG A NH1 1 
ATOM   7814  N  NH1 B ARG A 1 954  ? 46.865 44.045  -27.021 0.50 13.22 ? 954  ARG A NH1 1 
ATOM   7815  N  NH2 A ARG A 1 954  ? 48.618 45.787  -23.166 0.50 20.49 ? 954  ARG A NH2 1 
ATOM   7816  N  NH2 B ARG A 1 954  ? 45.791 44.824  -25.171 0.50 12.77 ? 954  ARG A NH2 1 
ATOM   7817  N  N   . GLU A 1 955  ? 48.814 51.095  -26.582 1.00 9.24  ? 955  GLU A N   1 
ATOM   7818  C  CA  . GLU A 1 955  ? 48.107 52.307  -26.181 1.00 10.60 ? 955  GLU A CA  1 
ATOM   7819  C  C   . GLU A 1 955  ? 47.266 52.190  -24.914 1.00 9.53  ? 955  GLU A C   1 
ATOM   7820  O  O   . GLU A 1 955  ? 46.983 53.209  -24.278 1.00 10.42 ? 955  GLU A O   1 
ATOM   7821  C  CB  . GLU A 1 955  ? 47.222 52.800  -27.308 1.00 11.87 ? 955  GLU A CB  1 
ATOM   7822  C  CG  . GLU A 1 955  ? 46.206 51.751  -27.738 1.00 14.35 ? 955  GLU A CG  1 
ATOM   7823  C  CD  . GLU A 1 955  ? 45.214 52.265  -28.750 1.00 19.59 ? 955  GLU A CD  1 
ATOM   7824  O  OE1 . GLU A 1 955  ? 45.023 53.501  -28.827 1.00 24.32 ? 955  GLU A OE1 1 
ATOM   7825  O  OE2 . GLU A 1 955  ? 44.657 51.428  -29.488 1.00 22.25 ? 955  GLU A OE2 1 
ATOM   7826  N  N   . ASP A 1 956  ? 46.839 50.975  -24.566 1.00 8.28  ? 956  ASP A N   1 
ATOM   7827  C  CA  . ASP A 1 956  ? 46.026 50.790  -23.369 1.00 8.42  ? 956  ASP A CA  1 
ATOM   7828  C  C   . ASP A 1 956  ? 46.843 50.647  -22.095 1.00 8.02  ? 956  ASP A C   1 
ATOM   7829  O  O   . ASP A 1 956  ? 46.253 50.581  -21.019 1.00 8.77  ? 956  ASP A O   1 
ATOM   7830  C  CB  . ASP A 1 956  ? 45.037 49.638  -23.515 1.00 9.08  ? 956  ASP A CB  1 
ATOM   7831  C  CG  . ASP A 1 956  ? 45.680 48.332  -23.907 1.00 11.39 ? 956  ASP A CG  1 
ATOM   7832  O  OD1 . ASP A 1 956  ? 46.919 48.256  -24.093 1.00 13.76 ? 956  ASP A OD1 1 
ATOM   7833  O  OD2 . ASP A 1 956  ? 44.965 47.298  -24.022 1.00 13.45 ? 956  ASP A OD2 1 
ATOM   7834  N  N   . LEU A 1 957  ? 48.161 50.673  -22.190 1.00 7.86  ? 957  LEU A N   1 
ATOM   7835  C  CA  . LEU A 1 957  ? 49.011 50.541  -21.013 1.00 9.31  ? 957  LEU A CA  1 
ATOM   7836  C  C   . LEU A 1 957  ? 49.566 51.883  -20.574 1.00 8.28  ? 957  LEU A C   1 
ATOM   7837  O  O   . LEU A 1 957  ? 49.994 52.673  -21.430 1.00 9.51  ? 957  LEU A O   1 
ATOM   7838  C  CB  . LEU A 1 957  ? 50.165 49.590  -21.334 1.00 9.74  ? 957  LEU A CB  1 
ATOM   7839  C  CG  . LEU A 1 957  ? 51.054 49.095  -20.201 1.00 13.28 ? 957  LEU A CG  1 
ATOM   7840  C  CD1 . LEU A 1 957  ? 50.196 48.312  -19.234 1.00 14.72 ? 957  LEU A CD1 1 
ATOM   7841  C  CD2 . LEU A 1 957  ? 52.144 48.198  -20.773 1.00 13.23 ? 957  LEU A CD2 1 
ATOM   7842  N  N   . ASP A 1 958  ? 49.567 52.139  -19.268 1.00 7.70  ? 958  ASP A N   1 
ATOM   7843  C  CA  . ASP A 1 958  ? 50.192 53.317  -18.743 1.00 7.42  ? 958  ASP A CA  1 
ATOM   7844  C  C   . ASP A 1 958  ? 51.150 52.981  -17.611 1.00 7.11  ? 958  ASP A C   1 
ATOM   7845  O  O   . ASP A 1 958  ? 50.924 52.013  -16.881 1.00 7.90  ? 958  ASP A O   1 
ATOM   7846  C  CB  . ASP A 1 958  ? 49.132 54.284  -18.244 1.00 7.60  ? 958  ASP A CB  1 
ATOM   7847  C  CG  . ASP A 1 958  ? 49.662 55.704  -18.066 1.00 9.00  ? 958  ASP A CG  1 
ATOM   7848  O  OD1 . ASP A 1 958  ? 50.785 56.047  -18.550 1.00 8.23  ? 958  ASP A OD1 1 
ATOM   7849  O  OD2 . ASP A 1 958  ? 48.991 56.549  -17.426 1.00 10.12 ? 958  ASP A OD2 1 
ATOM   7850  N  N   . VAL A 1 959  ? 52.208 53.779  -17.492 1.00 6.53  ? 959  VAL A N   1 
ATOM   7851  C  CA  . VAL A 1 959  ? 53.043 53.797  -16.314 1.00 6.22  ? 959  VAL A CA  1 
ATOM   7852  C  C   . VAL A 1 959  ? 52.487 54.894  -15.417 1.00 6.89  ? 959  VAL A C   1 
ATOM   7853  O  O   . VAL A 1 959  ? 52.902 56.056  -15.499 1.00 7.44  ? 959  VAL A O   1 
ATOM   7854  C  CB  . VAL A 1 959  ? 54.535 54.046  -16.677 1.00 7.52  ? 959  VAL A CB  1 
ATOM   7855  C  CG1 . VAL A 1 959  ? 55.364 54.190  -15.404 1.00 7.74  ? 959  VAL A CG1 1 
ATOM   7856  C  CG2 . VAL A 1 959  ? 55.064 52.852  -17.513 1.00 7.59  ? 959  VAL A CG2 1 
ATOM   7857  N  N   . SER A 1 960  ? 51.532 54.531  -14.569 1.00 6.51  ? 960  SER A N   1 
ATOM   7858  C  CA  . SER A 1 960  ? 50.794 55.489  -13.742 1.00 7.17  ? 960  SER A CA  1 
ATOM   7859  C  C   . SER A 1 960  ? 51.698 56.219  -12.750 1.00 7.95  ? 960  SER A C   1 
ATOM   7860  O  O   . SER A 1 960  ? 51.500 57.419  -12.457 1.00 9.61  ? 960  SER A O   1 
ATOM   7861  C  CB  . SER A 1 960  ? 49.674 54.766  -13.006 1.00 7.72  ? 960  SER A CB  1 
ATOM   7862  O  OG  . SER A 1 960  ? 48.855 54.038  -13.931 1.00 9.99  ? 960  SER A OG  1 
ATOM   7863  N  N   . VAL A 1 961  ? 52.677 55.470  -12.224 1.00 6.73  ? 961  VAL A N   1 
ATOM   7864  C  CA  . VAL A 1 961  ? 53.638 55.968  -11.251 1.00 6.90  ? 961  VAL A CA  1 
ATOM   7865  C  C   . VAL A 1 961  ? 55.003 55.433  -11.642 1.00 6.36  ? 961  VAL A C   1 
ATOM   7866  O  O   . VAL A 1 961  ? 55.158 54.248  -11.942 1.00 6.19  ? 961  VAL A O   1 
ATOM   7867  C  CB  . VAL A 1 961  ? 53.314 55.466  -9.817  1.00 7.66  ? 961  VAL A CB  1 
ATOM   7868  C  CG1 . VAL A 1 961  ? 54.406 55.912  -8.832  1.00 9.86  ? 961  VAL A CG1 1 
ATOM   7869  C  CG2 . VAL A 1 961  ? 51.916 55.982  -9.344  1.00 9.56  ? 961  VAL A CG2 1 
ATOM   7870  N  N   . MET A 1 962  ? 56.002 56.320  -11.597 1.00 6.67  ? 962  MET A N   1 
ATOM   7871  C  CA  . MET A 1 962  ? 57.393 55.921  -11.559 1.00 6.15  ? 962  MET A CA  1 
ATOM   7872  C  C   . MET A 1 962  ? 57.992 56.777  -10.451 1.00 6.91  ? 962  MET A C   1 
ATOM   7873  O  O   . MET A 1 962  ? 57.906 58.004  -10.481 1.00 7.48  ? 962  MET A O   1 
ATOM   7874  C  CB  . MET A 1 962  ? 58.084 56.201  -12.918 1.00 7.37  ? 962  MET A CB  1 
ATOM   7875  C  CG  . MET A 1 962  ? 59.596 55.911  -12.856 1.00 7.52  ? 962  MET A CG  1 
ATOM   7876  S  SD  . MET A 1 962  ? 60.299 56.249  -14.486 1.00 9.62  ? 962  MET A SD  1 
ATOM   7877  C  CE  . MET A 1 962  ? 62.074 55.946  -14.170 1.00 9.99  ? 962  MET A CE  1 
ATOM   7878  N  N   . ARG A 1 963  ? 58.541 56.120  -9.443  1.00 6.03  ? 963  ARG A N   1 
ATOM   7879  C  CA  . ARG A 1 963  ? 59.045 56.784  -8.250  1.00 6.56  ? 963  ARG A CA  1 
ATOM   7880  C  C   . ARG A 1 963  ? 60.311 56.113  -7.741  1.00 6.40  ? 963  ARG A C   1 
ATOM   7881  O  O   . ARG A 1 963  ? 60.277 54.937  -7.429  1.00 6.52  ? 963  ARG A O   1 
ATOM   7882  C  CB  . ARG A 1 963  ? 57.982 56.746  -7.140  1.00 6.71  ? 963  ARG A CB  1 
ATOM   7883  C  CG  . ARG A 1 963  ? 58.423 57.393  -5.816  1.00 8.18  ? 963  ARG A CG  1 
ATOM   7884  C  CD  . ARG A 1 963  ? 57.339 57.243  -4.716  1.00 9.70  ? 963  ARG A CD  1 
ATOM   7885  N  NE  . ARG A 1 963  ? 56.121 57.867  -5.199  1.00 9.38  ? 963  ARG A NE  1 
ATOM   7886  C  CZ  . ARG A 1 963  ? 54.915 57.333  -5.159  1.00 10.19 ? 963  ARG A CZ  1 
ATOM   7887  N  NH1 . ARG A 1 963  ? 54.681 56.166  -4.585  1.00 9.73  ? 963  ARG A NH1 1 
ATOM   7888  N  NH2 . ARG A 1 963  ? 53.926 57.999  -5.692  1.00 9.88  ? 963  ARG A NH2 1 
ATOM   7889  N  N   . ARG A 1 964  ? 61.401 56.878  -7.615  1.00 6.24  ? 964  ARG A N   1 
ATOM   7890  C  CA  . ARG A 1 964  ? 62.576 56.293  -6.974  1.00 7.52  ? 964  ARG A CA  1 
ATOM   7891  C  C   . ARG A 1 964  ? 62.291 56.260  -5.490  1.00 7.44  ? 964  ARG A C   1 
ATOM   7892  O  O   . ARG A 1 964  ? 61.830 57.224  -4.897  1.00 8.28  ? 964  ARG A O   1 
ATOM   7893  C  CB  . ARG A 1 964  ? 63.811 57.127  -7.290  1.00 7.44  ? 964  ARG A CB  1 
ATOM   7894  C  CG  . ARG A 1 964  ? 65.057 56.516  -6.695  1.00 8.88  ? 964  ARG A CG  1 
ATOM   7895  C  CD  . ARG A 1 964  ? 66.345 57.165  -7.162  1.00 9.18  ? 964  ARG A CD  1 
ATOM   7896  N  NE  . ARG A 1 964  ? 66.519 56.999  -8.591  1.00 9.54  ? 964  ARG A NE  1 
ATOM   7897  C  CZ  . ARG A 1 964  ? 67.440 56.247  -9.156  1.00 9.68  ? 964  ARG A CZ  1 
ATOM   7898  N  NH1 . ARG A 1 964  ? 68.286 55.536  -8.397  1.00 12.28 ? 964  ARG A NH1 1 
ATOM   7899  N  NH2 . ARG A 1 964  ? 67.546 56.184  -10.463 1.00 11.13 ? 964  ARG A NH2 1 
ATOM   7900  N  N   . LEU A 1 965  ? 62.558 55.104  -4.902  1.00 6.69  ? 965  LEU A N   1 
ATOM   7901  C  CA  . LEU A 1 965  ? 62.179 54.811  -3.522  1.00 7.57  ? 965  LEU A CA  1 
ATOM   7902  C  C   . LEU A 1 965  ? 63.302 54.974  -2.508  1.00 8.82  ? 965  LEU A C   1 
ATOM   7903  O  O   . LEU A 1 965  ? 63.066 54.911  -1.302  1.00 10.10 ? 965  LEU A O   1 
ATOM   7904  C  CB  . LEU A 1 965  ? 61.627 53.391  -3.418  1.00 8.17  ? 965  LEU A CB  1 
ATOM   7905  C  CG  . LEU A 1 965  ? 60.403 53.140  -4.314  1.00 7.75  ? 965  LEU A CG  1 
ATOM   7906  C  CD1 . LEU A 1 965  ? 59.999 51.664  -4.312  1.00 9.68  ? 965  LEU A CD1 1 
ATOM   7907  C  CD2 . LEU A 1 965  ? 59.231 54.010  -3.908  1.00 10.70 ? 965  LEU A CD2 1 
ATOM   7908  N  N   . THR A 1 966  ? 64.524 55.146  -3.019  1.00 8.87  ? 966  THR A N   1 
ATOM   7909  C  CA  . THR A 1 966  ? 65.732 55.223  -2.198  1.00 9.57  ? 966  THR A CA  1 
ATOM   7910  C  C   . THR A 1 966  ? 66.435 56.538  -2.376  1.00 9.55  ? 966  THR A C   1 
ATOM   7911  O  O   . THR A 1 966  ? 66.435 57.092  -3.473  1.00 9.56  ? 966  THR A O   1 
ATOM   7912  C  CB  . THR A 1 966  ? 66.725 54.123  -2.602  1.00 9.30  ? 966  THR A CB  1 
ATOM   7913  O  OG1 . THR A 1 966  ? 66.758 54.022  -4.022  1.00 10.01 ? 966  THR A OG1 1 
ATOM   7914  C  CG2 . THR A 1 966  ? 66.267 52.737  -2.101  1.00 10.80 ? 966  THR A CG2 1 
ATOM   7915  N  N   . LYS A 1 967  ? 67.062 57.002  -1.311  1.00 10.72 ? 967  LYS A N   1 
ATOM   7916  C  CA  . LYS A 1 967  ? 67.902 58.199  -1.353  1.00 11.77 ? 967  LYS A CA  1 
ATOM   7917  C  C   . LYS A 1 967  ? 69.293 57.817  -1.859  1.00 12.38 ? 967  LYS A C   1 
ATOM   7918  O  O   . LYS A 1 967  ? 69.583 56.628  -2.024  1.00 11.11 ? 967  LYS A O   1 
ATOM   7919  C  CB  . LYS A 1 967  ? 68.023 58.807  0.033   1.00 12.58 ? 967  LYS A CB  1 
ATOM   7920  C  CG  . LYS A 1 967  ? 66.679 59.320  0.562   1.00 17.05 ? 967  LYS A CG  1 
ATOM   7921  C  CD  . LYS A 1 967  ? 66.865 60.397  1.621   1.00 22.22 ? 967  LYS A CD  1 
ATOM   7922  C  CE  . LYS A 1 967  ? 65.581 60.670  2.398   1.00 28.35 ? 967  LYS A CE  1 
ATOM   7923  N  NZ  . LYS A 1 967  ? 64.589 61.441  1.602   1.00 32.02 ? 967  LYS A NZ  1 
ATOM   7924  N  N   . SER A 1 968  ? 70.120 58.826  -2.143  1.00 12.94 ? 968  SER A N   1 
ATOM   7925  C  CA  . SER A 1 968  ? 71.344 58.577  -2.897  1.00 14.97 ? 968  SER A CA  1 
ATOM   7926  C  C   . SER A 1 968  ? 72.369 57.754  -2.136  1.00 15.12 ? 968  SER A C   1 
ATOM   7927  O  O   . SER A 1 968  ? 73.204 57.122  -2.780  1.00 16.55 ? 968  SER A O   1 
ATOM   7928  C  CB  . SER A 1 968  ? 71.990 59.881  -3.347  1.00 16.04 ? 968  SER A CB  1 
ATOM   7929  O  OG  . SER A 1 968  ? 72.274 60.680  -2.231  1.00 19.53 ? 968  SER A OG  1 
ATOM   7930  N  N   . SER A 1 969  ? 72.306 57.746  -0.810  1.00 15.31 ? 969  SER A N   1 
ATOM   7931  C  CA  . SER A 1 969  ? 73.312 56.980  -0.037  1.00 16.71 ? 969  SER A CA  1 
ATOM   7932  C  C   . SER A 1 969  ? 73.047 55.469  0.000   1.00 16.53 ? 969  SER A C   1 
ATOM   7933  O  O   . SER A 1 969  ? 73.887 54.693  0.472   1.00 16.98 ? 969  SER A O   1 
ATOM   7934  C  CB  . SER A 1 969  ? 73.444 57.535  1.367   1.00 18.42 ? 969  SER A CB  1 
ATOM   7935  O  OG  . SER A 1 969  ? 72.329 57.138  2.145   1.00 23.03 ? 969  SER A OG  1 
ATOM   7936  N  N   . ALA A 1 970  ? 71.897 55.026  -0.504  1.00 14.31 ? 970  ALA A N   1 
ATOM   7937  C  CA  . ALA A 1 970  ? 71.618 53.604  -0.525  1.00 14.54 ? 970  ALA A CA  1 
ATOM   7938  C  C   . ALA A 1 970  ? 72.425 52.852  -1.577  1.00 15.19 ? 970  ALA A C   1 
ATOM   7939  O  O   . ALA A 1 970  ? 72.418 53.192  -2.768  1.00 15.26 ? 970  ALA A O   1 
ATOM   7940  C  CB  . ALA A 1 970  ? 70.109 53.320  -0.662  1.00 15.59 ? 970  ALA A CB  1 
ATOM   7941  N  N   A LYS A 1 971  ? 73.146 51.844  -1.092  0.50 15.29 ? 971  LYS A N   1 
ATOM   7942  N  N   B LYS A 1 971  ? 73.135 51.798  -1.157  0.50 15.05 ? 971  LYS A N   1 
ATOM   7943  C  CA  A LYS A 1 971  ? 73.880 50.921  -1.934  0.50 16.01 ? 971  LYS A CA  1 
ATOM   7944  C  CA  B LYS A 1 971  ? 73.914 50.976  -2.095  0.50 15.58 ? 971  LYS A CA  1 
ATOM   7945  C  C   A LYS A 1 971  ? 73.001 50.395  -3.064  0.50 15.26 ? 971  LYS A C   1 
ATOM   7946  C  C   B LYS A 1 971  ? 73.039 50.246  -3.119  0.50 15.02 ? 971  LYS A C   1 
ATOM   7947  O  O   A LYS A 1 971  ? 73.359 50.526  -4.233  0.50 15.23 ? 971  LYS A O   1 
ATOM   7948  O  O   B LYS A 1 971  ? 73.450 50.035  -4.271  0.50 14.97 ? 971  LYS A O   1 
ATOM   7949  C  CB  A LYS A 1 971  ? 74.412 49.772  -1.066  0.50 15.90 ? 971  LYS A CB  1 
ATOM   7950  C  CB  B LYS A 1 971  ? 74.793 49.964  -1.339  0.50 15.21 ? 971  LYS A CB  1 
ATOM   7951  C  CG  A LYS A 1 971  ? 75.132 48.673  -1.816  0.50 17.40 ? 971  LYS A CG  1 
ATOM   7952  C  CG  B LYS A 1 971  ? 75.685 49.119  -2.239  0.50 17.43 ? 971  LYS A CG  1 
ATOM   7953  C  CD  A LYS A 1 971  ? 75.939 47.765  -0.862  0.50 17.81 ? 971  LYS A CD  1 
ATOM   7954  C  CD  B LYS A 1 971  ? 76.579 48.187  -1.414  0.50 16.74 ? 971  LYS A CD  1 
ATOM   7955  C  CE  A LYS A 1 971  ? 76.660 48.540  0.219   0.50 21.21 ? 971  LYS A CE  1 
ATOM   7956  C  CE  B LYS A 1 971  ? 77.009 46.951  -2.194  0.50 19.48 ? 971  LYS A CE  1 
ATOM   7957  N  NZ  A LYS A 1 971  ? 77.563 49.591  -0.319  0.50 23.51 ? 971  LYS A NZ  1 
ATOM   7958  N  NZ  B LYS A 1 971  ? 77.452 47.248  -3.574  0.50 20.72 ? 971  LYS A NZ  1 
ATOM   7959  N  N   . THR A 1 972  ? 71.844 49.839  -2.698  1.00 14.86 ? 972  THR A N   1 
ATOM   7960  C  CA  . THR A 1 972  ? 70.922 49.243  -3.648  1.00 14.50 ? 972  THR A CA  1 
ATOM   7961  C  C   . THR A 1 972  ? 69.811 50.257  -3.909  1.00 12.26 ? 972  THR A C   1 
ATOM   7962  O  O   . THR A 1 972  ? 69.020 50.535  -3.021  1.00 13.36 ? 972  THR A O   1 
ATOM   7963  C  CB  . THR A 1 972  ? 70.335 47.945  -3.120  1.00 16.21 ? 972  THR A CB  1 
ATOM   7964  O  OG1 . THR A 1 972  ? 71.413 47.021  -2.897  1.00 18.84 ? 972  THR A OG1 1 
ATOM   7965  C  CG2 . THR A 1 972  ? 69.523 47.258  -4.212  1.00 16.77 ? 972  THR A CG2 1 
ATOM   7966  N  N   . GLN A 1 973  ? 69.797 50.829  -5.108  1.00 10.30 ? 973  GLN A N   1 
ATOM   7967  C  CA  . GLN A 1 973  ? 68.733 51.773  -5.479  1.00 10.94 ? 973  GLN A CA  1 
ATOM   7968  C  C   . GLN A 1 973  ? 67.504 50.989  -5.842  1.00 10.23 ? 973  GLN A C   1 
ATOM   7969  O  O   . GLN A 1 973  ? 67.594 49.912  -6.416  1.00 10.61 ? 973  GLN A O   1 
ATOM   7970  C  CB  . GLN A 1 973  ? 69.185 52.644  -6.641  1.00 10.77 ? 973  GLN A CB  1 
ATOM   7971  C  CG  . GLN A 1 973  ? 70.273 53.628  -6.199  1.00 10.15 ? 973  GLN A CG  1 
ATOM   7972  C  CD  . GLN A 1 973  ? 69.790 54.692  -5.233  1.00 11.90 ? 973  GLN A CD  1 
ATOM   7973  O  OE1 . GLN A 1 973  ? 68.790 55.364  -5.514  1.00 10.80 ? 973  GLN A OE1 1 
ATOM   7974  N  NE2 . GLN A 1 973  ? 70.485 54.875  -4.114  1.00 10.14 ? 973  GLN A NE2 1 
ATOM   7975  N  N   . ARG A 1 974  ? 66.340 51.565  -5.527  1.00 10.34 ? 974  ARG A N   1 
ATOM   7976  C  CA  A ARG A 1 974  ? 65.086 50.929  -5.888  0.50 9.44  ? 974  ARG A CA  1 
ATOM   7977  C  CA  B ARG A 1 974  ? 65.052 50.937  -5.790  0.50 9.92  ? 974  ARG A CA  1 
ATOM   7978  C  C   . ARG A 1 974  ? 64.143 51.920  -6.540  1.00 8.95  ? 974  ARG A C   1 
ATOM   7979  O  O   . ARG A 1 974  ? 64.036 53.053  -6.098  1.00 9.31  ? 974  ARG A O   1 
ATOM   7980  C  CB  A ARG A 1 974  ? 64.412 50.300  -4.683  0.50 10.22 ? 974  ARG A CB  1 
ATOM   7981  C  CB  B ARG A 1 974  ? 64.393 50.529  -4.468  0.50 10.53 ? 974  ARG A CB  1 
ATOM   7982  C  CG  A ARG A 1 974  ? 65.259 49.243  -3.991  0.50 10.59 ? 974  ARG A CG  1 
ATOM   7983  C  CG  B ARG A 1 974  ? 65.067 49.333  -3.758  0.50 11.37 ? 974  ARG A CG  1 
ATOM   7984  C  CD  A ARG A 1 974  ? 64.758 48.875  -2.606  0.50 13.01 ? 974  ARG A CD  1 
ATOM   7985  C  CD  B ARG A 1 974  ? 64.690 49.148  -2.273  0.50 12.14 ? 974  ARG A CD  1 
ATOM   7986  N  NE  A ARG A 1 974  ? 63.530 48.098  -2.679  0.50 12.71 ? 974  ARG A NE  1 
ATOM   7987  N  NE  B ARG A 1 974  ? 63.256 49.225  -2.014  0.50 15.38 ? 974  ARG A NE  1 
ATOM   7988  C  CZ  A ARG A 1 974  ? 62.337 48.455  -2.189  0.50 13.94 ? 974  ARG A CZ  1 
ATOM   7989  C  CZ  B ARG A 1 974  ? 62.379 48.228  -2.134  0.50 18.38 ? 974  ARG A CZ  1 
ATOM   7990  N  NH1 A ARG A 1 974  ? 62.160 49.596  -1.524  0.50 10.68 ? 974  ARG A NH1 1 
ATOM   7991  N  NH1 B ARG A 1 974  ? 62.754 47.004  -2.512  0.50 18.28 ? 974  ARG A NH1 1 
ATOM   7992  N  NH2 A ARG A 1 974  ? 61.314 47.623  -2.345  0.50 10.82 ? 974  ARG A NH2 1 
ATOM   7993  N  NH2 B ARG A 1 974  ? 61.103 48.462  -1.865  0.50 16.54 ? 974  ARG A NH2 1 
ATOM   7994  N  N   . VAL A 1 975  ? 63.484 51.456  -7.598  1.00 8.35  ? 975  VAL A N   1 
ATOM   7995  C  CA  . VAL A 1 975  ? 62.530 52.319  -8.313  1.00 8.90  ? 975  VAL A CA  1 
ATOM   7996  C  C   . VAL A 1 975  ? 61.234 51.543  -8.412  1.00 7.22  ? 975  VAL A C   1 
ATOM   7997  O  O   . VAL A 1 975  ? 61.200 50.381  -8.853  1.00 8.20  ? 975  VAL A O   1 
ATOM   7998  C  CB  . VAL A 1 975  ? 63.062 52.728  -9.710  1.00 9.21  ? 975  VAL A CB  1 
ATOM   7999  C  CG1 . VAL A 1 975  ? 62.075 53.663  -10.466 1.00 8.85  ? 975  VAL A CG1 1 
ATOM   8000  C  CG2 . VAL A 1 975  ? 64.411 53.460  -9.583  1.00 11.56 ? 975  VAL A CG2 1 
ATOM   8001  N  N   . GLY A 1 976  ? 60.159 52.225  -8.041  1.00 6.73  ? 976  GLY A N   1 
ATOM   8002  C  CA  . GLY A 1 976  ? 58.838 51.623  -8.071  1.00 6.40  ? 976  GLY A CA  1 
ATOM   8003  C  C   . GLY A 1 976  ? 58.020 52.107  -9.255  1.00 6.89  ? 976  GLY A C   1 
ATOM   8004  O  O   . GLY A 1 976  ? 58.102 53.282  -9.619  1.00 6.72  ? 976  GLY A O   1 
ATOM   8005  N  N   . TYR A 1 977  ? 57.272 51.186  -9.851  1.00 6.12  ? 977  TYR A N   1 
ATOM   8006  C  CA  . TYR A 1 977  ? 56.397 51.475  -10.974 1.00 5.84  ? 977  TYR A CA  1 
ATOM   8007  C  C   . TYR A 1 977  ? 55.016 50.940  -10.702 1.00 7.01  ? 977  TYR A C   1 
ATOM   8008  O  O   . TYR A 1 977  ? 54.878 49.819  -10.174 1.00 6.51  ? 977  TYR A O   1 
ATOM   8009  C  CB  . TYR A 1 977  ? 56.878 50.755  -12.228 1.00 6.65  ? 977  TYR A CB  1 
ATOM   8010  C  CG  . TYR A 1 977  ? 58.263 51.136  -12.645 1.00 6.42  ? 977  TYR A CG  1 
ATOM   8011  C  CD1 . TYR A 1 977  ? 58.483 52.223  -13.506 1.00 7.45  ? 977  TYR A CD1 1 
ATOM   8012  C  CD2 . TYR A 1 977  ? 59.362 50.421  -12.159 1.00 7.14  ? 977  TYR A CD2 1 
ATOM   8013  C  CE1 . TYR A 1 977  ? 59.754 52.566  -13.907 1.00 9.50  ? 977  TYR A CE1 1 
ATOM   8014  C  CE2 . TYR A 1 977  ? 60.662 50.782  -12.545 1.00 9.78  ? 977  TYR A CE2 1 
ATOM   8015  C  CZ  . TYR A 1 977  ? 60.833 51.864  -13.419 1.00 7.47  ? 977  TYR A CZ  1 
ATOM   8016  O  OH  . TYR A 1 977  ? 62.096 52.296  -13.856 1.00 10.10 ? 977  TYR A OH  1 
ATOM   8017  N  N   . VAL A 1 978  ? 54.000 51.731  -11.039 1.00 6.64  ? 978  VAL A N   1 
ATOM   8018  C  CA  . VAL A 1 978  ? 52.629 51.222  -11.047 1.00 6.42  ? 978  VAL A CA  1 
ATOM   8019  C  C   . VAL A 1 978  ? 52.182 51.173  -12.514 1.00 6.75  ? 978  VAL A C   1 
ATOM   8020  O  O   . VAL A 1 978  ? 52.281 52.223  -13.206 1.00 6.65  ? 978  VAL A O   1 
ATOM   8021  C  CB  . VAL A 1 978  ? 51.662 52.063  -10.210 1.00 6.68  ? 978  VAL A CB  1 
ATOM   8022  C  CG1 . VAL A 1 978  ? 50.219 51.572  -10.396 1.00 8.20  ? 978  VAL A CG1 1 
ATOM   8023  C  CG2 . VAL A 1 978  ? 52.049 52.010  -8.761  1.00 7.57  ? 978  VAL A CG2 1 
ATOM   8024  N  N   A LEU A 1 979  ? 51.824 49.985  -13.001 0.50 6.07  ? 979  LEU A N   1 
ATOM   8025  N  N   B LEU A 1 979  ? 51.747 50.001  -12.983 0.50 6.57  ? 979  LEU A N   1 
ATOM   8026  C  CA  A LEU A 1 979  ? 51.327 49.820  -14.350 0.50 6.74  ? 979  LEU A CA  1 
ATOM   8027  C  CA  B LEU A 1 979  ? 51.406 49.757  -14.375 0.50 8.00  ? 979  LEU A CA  1 
ATOM   8028  C  C   A LEU A 1 979  ? 49.857 49.649  -14.282 0.50 6.89  ? 979  LEU A C   1 
ATOM   8029  C  C   B LEU A 1 979  ? 49.933 49.452  -14.466 0.50 7.30  ? 979  LEU A C   1 
ATOM   8030  O  O   A LEU A 1 979  ? 49.331 48.978  -13.405 0.50 6.73  ? 979  LEU A O   1 
ATOM   8031  O  O   B LEU A 1 979  ? 49.480 48.481  -13.846 0.50 7.00  ? 979  LEU A O   1 
ATOM   8032  C  CB  A LEU A 1 979  ? 51.915 48.583  -15.030 0.50 7.33  ? 979  LEU A CB  1 
ATOM   8033  C  CB  B LEU A 1 979  ? 52.177 48.523  -14.860 0.50 8.37  ? 979  LEU A CB  1 
ATOM   8034  C  CG  A LEU A 1 979  ? 53.426 48.602  -15.254 0.50 8.75  ? 979  LEU A CG  1 
ATOM   8035  C  CG  B LEU A 1 979  ? 52.281 48.276  -16.359 0.50 11.00 ? 979  LEU A CG  1 
ATOM   8036  C  CD1 A LEU A 1 979  ? 53.826 47.530  -16.242 0.50 12.08 ? 979  LEU A CD1 1 
ATOM   8037  C  CD1 B LEU A 1 979  ? 53.181 49.339  -16.944 0.50 13.28 ? 979  LEU A CD1 1 
ATOM   8038  C  CD2 A LEU A 1 979  ? 53.894 49.956  -15.741 0.50 11.17 ? 979  LEU A CD2 1 
ATOM   8039  C  CD2 B LEU A 1 979  ? 52.829 46.884  -16.651 0.50 10.74 ? 979  LEU A CD2 1 
ATOM   8040  N  N   . HIS A 1 980  ? 49.190 50.267  -15.223 1.00 7.17  ? 980  HIS A N   1 
ATOM   8041  C  CA  . HIS A 1 980  ? 47.752 50.083  -15.358 1.00 7.02  ? 980  HIS A CA  1 
ATOM   8042  C  C   . HIS A 1 980  ? 47.391 49.840  -16.806 1.00 8.08  ? 980  HIS A C   1 
ATOM   8043  O  O   . HIS A 1 980  ? 47.822 50.609  -17.664 1.00 8.78  ? 980  HIS A O   1 
ATOM   8044  C  CB  . HIS A 1 980  ? 46.986 51.325  -14.896 1.00 8.21  ? 980  HIS A CB  1 
ATOM   8045  C  CG  . HIS A 1 980  ? 45.513 51.185  -15.104 1.00 8.97  ? 980  HIS A CG  1 
ATOM   8046  N  ND1 . HIS A 1 980  ? 44.766 50.290  -14.375 1.00 10.10 ? 980  HIS A ND1 1 
ATOM   8047  C  CD2 . HIS A 1 980  ? 44.660 51.757  -15.990 1.00 9.45  ? 980  HIS A CD2 1 
ATOM   8048  C  CE1 . HIS A 1 980  ? 43.509 50.316  -14.802 1.00 10.23 ? 980  HIS A CE1 1 
ATOM   8049  N  NE2 . HIS A 1 980  ? 43.416 51.213  -15.771 1.00 9.55  ? 980  HIS A NE2 1 
ATOM   8050  N  N   A ARG A 1 981  ? 46.565 48.833  -17.058 0.50 7.71  ? 981  ARG A N   1 
ATOM   8051  N  N   B ARG A 1 981  ? 46.647 48.775  -17.107 0.50 7.41  ? 981  ARG A N   1 
ATOM   8052  C  CA  A ARG A 1 981  ? 46.099 48.597  -18.401 0.50 8.02  ? 981  ARG A CA  1 
ATOM   8053  C  CA  B ARG A 1 981  ? 46.110 48.656  -18.457 0.50 7.35  ? 981  ARG A CA  1 
ATOM   8054  C  C   A ARG A 1 981  ? 44.614 48.772  -18.423 0.50 7.47  ? 981  ARG A C   1 
ATOM   8055  C  C   B ARG A 1 981  ? 44.641 48.843  -18.368 0.50 6.97  ? 981  ARG A C   1 
ATOM   8056  O  O   A ARG A 1 981  ? 43.905 48.051  -17.737 0.50 7.92  ? 981  ARG A O   1 
ATOM   8057  O  O   B ARG A 1 981  ? 43.983 48.217  -17.541 0.50 7.31  ? 981  ARG A O   1 
ATOM   8058  C  CB  A ARG A 1 981  ? 46.487 47.190  -18.829 0.50 8.87  ? 981  ARG A CB  1 
ATOM   8059  C  CB  B ARG A 1 981  ? 46.428 47.310  -19.109 0.50 8.03  ? 981  ARG A CB  1 
ATOM   8060  C  CG  A ARG A 1 981  ? 45.977 46.826  -20.184 0.50 11.14 ? 981  ARG A CG  1 
ATOM   8061  C  CG  B ARG A 1 981  ? 46.144 47.276  -20.637 0.50 7.23  ? 981  ARG A CG  1 
ATOM   8062  C  CD  A ARG A 1 981  ? 46.815 45.793  -20.894 0.50 15.34 ? 981  ARG A CD  1 
ATOM   8063  C  CD  B ARG A 1 981  ? 46.177 45.859  -21.245 0.50 8.38  ? 981  ARG A CD  1 
ATOM   8064  N  NE  A ARG A 1 981  ? 46.173 45.358  -22.125 0.50 17.47 ? 981  ARG A NE  1 
ATOM   8065  N  NE  B ARG A 1 981  ? 47.472 45.226  -21.034 0.50 10.15 ? 981  ARG A NE  1 
ATOM   8066  C  CZ  A ARG A 1 981  ? 46.327 44.154  -22.658 0.50 20.06 ? 981  ARG A CZ  1 
ATOM   8067  C  CZ  B ARG A 1 981  ? 48.473 45.264  -21.895 0.50 8.75  ? 981  ARG A CZ  1 
ATOM   8068  N  NH1 A ARG A 1 981  ? 47.101 43.252  -22.067 0.50 19.50 ? 981  ARG A NH1 1 
ATOM   8069  N  NH1 B ARG A 1 981  ? 48.349 45.887  -23.071 0.50 9.49  ? 981  ARG A NH1 1 
ATOM   8070  N  NH2 A ARG A 1 981  ? 45.698 43.849  -23.780 0.50 20.81 ? 981  ARG A NH2 1 
ATOM   8071  N  NH2 B ARG A 1 981  ? 49.608 44.649  -21.594 0.50 11.08 ? 981  ARG A NH2 1 
ATOM   8072  N  N   . THR A 1 982  ? 44.149 49.731  -19.216 1.00 7.76  ? 982  THR A N   1 
ATOM   8073  C  CA  . THR A 1 982  ? 42.715 49.905  -19.355 1.00 7.86  ? 982  THR A CA  1 
ATOM   8074  C  C   . THR A 1 982  ? 42.166 48.874  -20.334 1.00 9.03  ? 982  THR A C   1 
ATOM   8075  O  O   . THR A 1 982  ? 42.876 47.970  -20.725 1.00 10.71 ? 982  THR A O   1 
ATOM   8076  C  CB  . THR A 1 982  ? 42.405 51.377  -19.700 1.00 8.12  ? 982  THR A CB  1 
ATOM   8077  O  OG1 . THR A 1 982  ? 41.001 51.613  -19.562 1.00 8.88  ? 982  THR A OG1 1 
ATOM   8078  C  CG2 . THR A 1 982  ? 42.804 51.741  -21.124 1.00 8.97  ? 982  THR A CG2 1 
ATOM   8079  N  N   . ASN A 1 983  ? 40.884 48.944  -20.605 1.00 7.40  ? 983  ASN A N   1 
ATOM   8080  C  CA  . ASN A 1 983  ? 40.314 48.073  -21.627 1.00 8.01  ? 983  ASN A CA  1 
ATOM   8081  C  C   . ASN A 1 983  ? 39.591 48.949  -22.627 1.00 8.46  ? 983  ASN A C   1 
ATOM   8082  O  O   . ASN A 1 983  ? 38.702 49.735  -22.257 1.00 8.87  ? 983  ASN A O   1 
ATOM   8083  C  CB  . ASN A 1 983  ? 39.336 47.062  -21.025 1.00 7.28  ? 983  ASN A CB  1 
ATOM   8084  C  CG  . ASN A 1 983  ? 38.827 46.103  -22.056 1.00 8.66  ? 983  ASN A CG  1 
ATOM   8085  O  OD1 . ASN A 1 983  ? 39.542 45.203  -22.461 1.00 9.60  ? 983  ASN A OD1 1 
ATOM   8086  N  ND2 . ASN A 1 983  ? 37.611 46.320  -22.520 1.00 9.57  ? 983  ASN A ND2 1 
ATOM   8087  N  N   . LEU A 1 984  ? 40.031 48.843  -23.869 1.00 9.18  ? 984  LEU A N   1 
ATOM   8088  C  CA  . LEU A 1 984  ? 39.457 49.651  -24.940 1.00 10.12 ? 984  LEU A CA  1 
ATOM   8089  C  C   . LEU A 1 984  ? 38.607 48.789  -25.841 1.00 12.44 ? 984  LEU A C   1 
ATOM   8090  O  O   . LEU A 1 984  ? 38.903 47.606  -26.031 1.00 11.99 ? 984  LEU A O   1 
ATOM   8091  C  CB  . LEU A 1 984  ? 40.569 50.280  -25.768 1.00 9.51  ? 984  LEU A CB  1 
ATOM   8092  C  CG  . LEU A 1 984  ? 41.516 51.158  -24.943 1.00 10.27 ? 984  LEU A CG  1 
ATOM   8093  C  CD1 . LEU A 1 984  ? 42.715 51.602  -25.824 1.00 12.41 ? 984  LEU A CD1 1 
ATOM   8094  C  CD2 . LEU A 1 984  ? 40.777 52.310  -24.239 1.00 9.79  ? 984  LEU A CD2 1 
ATOM   8095  N  N   A MET A 1 985  ? 37.562 49.373  -26.386 0.50 13.63 ? 985  MET A N   1 
ATOM   8096  N  N   B MET A 1 985  ? 37.552 49.374  -26.382 0.50 13.32 ? 985  MET A N   1 
ATOM   8097  C  CA  A MET A 1 985  ? 36.696 48.664  -27.311 0.50 16.20 ? 985  MET A CA  1 
ATOM   8098  C  CA  B MET A 1 985  ? 36.676 48.688  -27.332 0.50 15.47 ? 985  MET A CA  1 
ATOM   8099  C  C   A MET A 1 985  ? 37.384 48.270  -28.578 0.50 17.02 ? 985  MET A C   1 
ATOM   8100  C  C   B MET A 1 985  ? 37.395 48.266  -28.574 0.50 16.74 ? 985  MET A C   1 
ATOM   8101  O  O   A MET A 1 985  ? 38.144 49.018  -29.141 0.50 17.22 ? 985  MET A O   1 
ATOM   8102  O  O   B MET A 1 985  ? 38.162 49.006  -29.136 0.50 17.01 ? 985  MET A O   1 
ATOM   8103  C  CB  A MET A 1 985  ? 35.517 49.532  -27.647 0.50 16.24 ? 985  MET A CB  1 
ATOM   8104  C  CB  B MET A 1 985  ? 35.576 49.618  -27.783 0.50 15.65 ? 985  MET A CB  1 
ATOM   8105  C  CG  A MET A 1 985  ? 34.625 49.711  -26.488 0.50 17.20 ? 985  MET A CG  1 
ATOM   8106  C  CG  B MET A 1 985  ? 34.650 50.036  -26.720 0.50 16.08 ? 985  MET A CG  1 
ATOM   8107  S  SD  A MET A 1 985  ? 32.968 49.348  -27.011 0.50 18.31 ? 985  MET A SD  1 
ATOM   8108  S  SD  B MET A 1 985  ? 33.024 49.327  -26.982 0.50 17.41 ? 985  MET A SD  1 
ATOM   8109  C  CE  A MET A 1 985  ? 32.785 50.768  -28.039 0.50 18.57 ? 985  MET A CE  1 
ATOM   8110  C  CE  B MET A 1 985  ? 33.283 48.056  -25.754 0.50 11.97 ? 985  MET A CE  1 
ATOM   8111  N  N   . GLN A 1 986  ? 37.094 47.058  -29.015 1.00 17.63 ? 986  GLN A N   1 
ATOM   8112  C  CA  . GLN A 1 986  ? 37.587 46.545  -30.299 1.00 19.45 ? 986  GLN A CA  1 
ATOM   8113  C  C   . GLN A 1 986  ? 36.597 47.014  -31.329 1.00 20.32 ? 986  GLN A C   1 
ATOM   8114  O  O   . GLN A 1 986  ? 35.427 46.642  -31.247 1.00 19.67 ? 986  GLN A O   1 
ATOM   8115  C  CB  . GLN A 1 986  ? 37.542 45.008  -30.306 1.00 21.04 ? 986  GLN A CB  1 
ATOM   8116  C  CG  . GLN A 1 986  ? 38.466 44.309  -29.348 1.00 25.13 ? 986  GLN A CG  1 
ATOM   8117  C  CD  . GLN A 1 986  ? 39.885 44.252  -29.844 1.00 29.93 ? 986  GLN A CD  1 
ATOM   8118  O  OE1 . GLN A 1 986  ? 40.138 44.213  -31.063 1.00 33.50 ? 986  GLN A OE1 1 
ATOM   8119  N  NE2 . GLN A 1 986  ? 40.824 44.245  -28.914 1.00 31.73 ? 986  GLN A NE2 1 
ATOM   8120  N  N   . CYS A 1 987  ? 37.047 47.835  -32.286 1.00 20.52 ? 987  CYS A N   1 
ATOM   8121  C  CA  . CYS A 1 987  ? 36.144 48.340  -33.320 1.00 23.61 ? 987  CYS A CA  1 
ATOM   8122  C  C   . CYS A 1 987  ? 36.648 48.059  -34.739 1.00 24.62 ? 987  CYS A C   1 
ATOM   8123  O  O   . CYS A 1 987  ? 36.278 48.771  -35.675 1.00 25.50 ? 987  CYS A O   1 
ATOM   8124  C  CB  . CYS A 1 987  ? 35.861 49.832  -33.110 1.00 23.54 ? 987  CYS A CB  1 
ATOM   8125  S  SG  . CYS A 1 987  ? 35.125 50.198  -31.492 1.00 26.96 ? 987  CYS A SG  1 
ATOM   8126  N  N   . GLY A 1 988  ? 37.486 47.038  -34.892 1.00 26.23 ? 988  GLY A N   1 
ATOM   8127  C  CA  . GLY A 1 988  ? 37.945 46.634  -36.211 1.00 29.18 ? 988  GLY A CA  1 
ATOM   8128  C  C   . GLY A 1 988  ? 39.169 47.345  -36.749 1.00 31.35 ? 988  GLY A C   1 
ATOM   8129  O  O   . GLY A 1 988  ? 39.540 47.139  -37.918 1.00 31.52 ? 988  GLY A O   1 
ATOM   8130  N  N   . THR A 1 989  ? 39.811 48.163  -35.916 1.00 32.73 ? 989  THR A N   1 
ATOM   8131  C  CA  . THR A 1 989  ? 41.070 48.796  -36.304 1.00 34.67 ? 989  THR A CA  1 
ATOM   8132  C  C   . THR A 1 989  ? 42.210 47.845  -35.994 1.00 36.02 ? 989  THR A C   1 
ATOM   8133  O  O   . THR A 1 989  ? 42.391 47.446  -34.842 1.00 36.26 ? 989  THR A O   1 
ATOM   8134  C  CB  . THR A 1 989  ? 41.282 50.128  -35.575 1.00 34.51 ? 989  THR A CB  1 
ATOM   8135  O  OG1 . THR A 1 989  ? 40.158 50.981  -35.811 1.00 35.25 ? 989  THR A OG1 1 
ATOM   8136  C  CG2 . THR A 1 989  ? 42.451 50.893  -36.189 1.00 34.63 ? 989  THR A CG2 1 
ATOM   8137  N  N   . PRO A 1 990  ? 42.963 47.458  -37.022 1.00 37.29 ? 990  PRO A N   1 
ATOM   8138  C  CA  . PRO A 1 990  ? 44.109 46.562  -36.830 1.00 38.28 ? 990  PRO A CA  1 
ATOM   8139  C  C   . PRO A 1 990  ? 45.151 47.095  -35.822 1.00 39.24 ? 990  PRO A C   1 
ATOM   8140  O  O   . PRO A 1 990  ? 45.635 46.280  -35.026 1.00 39.60 ? 990  PRO A O   1 
ATOM   8141  C  CB  . PRO A 1 990  ? 44.678 46.424  -38.245 1.00 38.50 ? 990  PRO A CB  1 
ATOM   8142  C  CG  . PRO A 1 990  ? 43.486 46.666  -39.127 1.00 37.96 ? 990  PRO A CG  1 
ATOM   8143  C  CD  . PRO A 1 990  ? 42.772 47.810  -38.443 1.00 37.45 ? 990  PRO A CD  1 
ATOM   8144  N  N   . GLU A 1 991  ? 45.442 48.404  -35.826 1.00 40.13 ? 991  GLU A N   1 
ATOM   8145  C  CA  . GLU A 1 991  ? 46.416 49.040  -34.905 1.00 41.13 ? 991  GLU A CA  1 
ATOM   8146  C  C   . GLU A 1 991  ? 47.370 48.047  -34.200 1.00 41.04 ? 991  GLU A C   1 
ATOM   8147  O  O   . GLU A 1 991  ? 47.147 47.697  -33.039 1.00 41.79 ? 991  GLU A O   1 
ATOM   8148  C  CB  . GLU A 1 991  ? 45.680 49.893  -33.849 1.00 41.19 ? 991  GLU A CB  1 
ATOM   8149  C  CG  . GLU A 1 991  ? 45.619 51.393  -34.133 1.00 41.94 ? 991  GLU A CG  1 
ATOM   8150  C  CD  . GLU A 1 991  ? 44.654 52.150  -33.212 1.00 42.38 ? 991  GLU A CD  1 
ATOM   8151  O  OE1 . GLU A 1 991  ? 44.108 51.549  -32.248 1.00 43.43 ? 991  GLU A OE1 1 
ATOM   8152  O  OE2 . GLU A 1 991  ? 44.427 53.360  -33.455 1.00 43.25 ? 991  GLU A OE2 1 
ATOM   8153  N  N   . GLU A 1 992  ? 48.425 47.599  -34.886 1.00 40.48 ? 992  GLU A N   1 
ATOM   8154  C  CA  . GLU A 1 992  ? 49.168 46.407  -34.426 1.00 40.22 ? 992  GLU A CA  1 
ATOM   8155  C  C   . GLU A 1 992  ? 50.557 46.578  -33.755 1.00 39.08 ? 992  GLU A C   1 
ATOM   8156  O  O   . GLU A 1 992  ? 50.620 46.931  -32.580 1.00 39.19 ? 992  GLU A O   1 
ATOM   8157  C  CB  . GLU A 1 992  ? 49.180 45.322  -35.515 1.00 40.78 ? 992  GLU A CB  1 
ATOM   8158  C  CG  . GLU A 1 992  ? 48.015 44.350  -35.380 1.00 42.33 ? 992  GLU A CG  1 
ATOM   8159  C  CD  . GLU A 1 992  ? 47.554 43.770  -36.704 1.00 44.81 ? 992  GLU A CD  1 
ATOM   8160  O  OE1 . GLU A 1 992  ? 47.263 44.552  -37.635 1.00 46.62 ? 992  GLU A OE1 1 
ATOM   8161  O  OE2 . GLU A 1 992  ? 47.464 42.527  -36.809 1.00 46.39 ? 992  GLU A OE2 1 
ATOM   8162  N  N   . HIS A 1 993  ? 51.641 46.306  -34.489 1.00 37.59 ? 993  HIS A N   1 
ATOM   8163  C  CA  . HIS A 1 993  ? 53.029 46.291  -33.962 1.00 36.03 ? 993  HIS A CA  1 
ATOM   8164  C  C   . HIS A 1 993  ? 53.372 47.284  -32.825 1.00 33.99 ? 993  HIS A C   1 
ATOM   8165  O  O   . HIS A 1 993  ? 53.483 48.496  -33.075 1.00 34.08 ? 993  HIS A O   1 
ATOM   8166  C  CB  . HIS A 1 993  ? 53.998 46.559  -35.123 1.00 37.00 ? 993  HIS A CB  1 
ATOM   8167  C  CG  . HIS A 1 993  ? 53.869 47.940  -35.693 1.00 38.07 ? 993  HIS A CG  1 
ATOM   8168  N  ND1 . HIS A 1 993  ? 54.580 49.014  -35.203 1.00 40.33 ? 993  HIS A ND1 1 
ATOM   8169  C  CD2 . HIS A 1 993  ? 53.067 48.433  -36.666 1.00 40.54 ? 993  HIS A CD2 1 
ATOM   8170  C  CE1 . HIS A 1 993  ? 54.242 50.105  -35.866 1.00 40.26 ? 993  HIS A CE1 1 
ATOM   8171  N  NE2 . HIS A 1 993  ? 53.326 49.780  -36.761 1.00 41.54 ? 993  HIS A NE2 1 
ATOM   8172  N  N   . THR A 1 994  ? 53.541 46.792  -31.591 1.00 30.97 ? 994  THR A N   1 
ATOM   8173  C  CA  . THR A 1 994  ? 54.142 47.621  -30.519 1.00 28.14 ? 994  THR A CA  1 
ATOM   8174  C  C   . THR A 1 994  ? 55.198 46.857  -29.715 1.00 26.24 ? 994  THR A C   1 
ATOM   8175  O  O   . THR A 1 994  ? 55.276 45.632  -29.782 1.00 27.12 ? 994  THR A O   1 
ATOM   8176  C  CB  . THR A 1 994  ? 53.082 48.236  -29.540 1.00 27.93 ? 994  THR A CB  1 
ATOM   8177  O  OG1 . THR A 1 994  ? 52.256 47.199  -28.997 1.00 26.92 ? 994  THR A OG1 1 
ATOM   8178  C  CG2 . THR A 1 994  ? 52.107 49.187  -30.258 1.00 27.20 ? 994  THR A CG2 1 
ATOM   8179  N  N   . GLN A 1 995  ? 55.968 47.582  -28.907 1.00 23.39 ? 995  GLN A N   1 
ATOM   8180  C  CA  . GLN A 1 995  ? 57.022 46.965  -28.122 1.00 21.49 ? 995  GLN A CA  1 
ATOM   8181  C  C   . GLN A 1 995  ? 56.560 46.620  -26.711 1.00 19.58 ? 995  GLN A C   1 
ATOM   8182  O  O   . GLN A 1 995  ? 55.787 47.368  -26.089 1.00 18.85 ? 995  GLN A O   1 
ATOM   8183  C  CB  . GLN A 1 995  ? 58.229 47.887  -28.047 1.00 21.51 ? 995  GLN A CB  1 
ATOM   8184  C  CG  . GLN A 1 995  ? 58.796 48.266  -29.407 1.00 23.69 ? 995  GLN A CG  1 
ATOM   8185  C  CD  . GLN A 1 995  ? 59.598 49.548  -29.367 1.00 28.32 ? 995  GLN A CD  1 
ATOM   8186  O  OE1 . GLN A 1 995  ? 59.058 50.623  -29.088 1.00 22.08 ? 995  GLN A OE1 1 
ATOM   8187  N  NE2 . GLN A 1 995  ? 60.892 49.444  -29.665 1.00 30.85 ? 995  GLN A NE2 1 
ATOM   8188  N  N   . LYS A 1 996  ? 57.045 45.490  -26.206 1.00 18.00 ? 996  LYS A N   1 
ATOM   8189  C  CA  . LYS A 1 996  ? 56.841 45.124  -24.819 1.00 17.95 ? 996  LYS A CA  1 
ATOM   8190  C  C   . LYS A 1 996  ? 57.519 46.139  -23.926 1.00 16.85 ? 996  LYS A C   1 
ATOM   8191  O  O   . LYS A 1 996  ? 58.656 46.535  -24.156 1.00 17.06 ? 996  LYS A O   1 
ATOM   8192  C  CB  . LYS A 1 996  ? 57.438 43.735  -24.553 1.00 19.00 ? 996  LYS A CB  1 
ATOM   8193  C  CG  . LYS A 1 996  ? 56.576 42.615  -25.065 1.00 22.62 ? 996  LYS A CG  1 
ATOM   8194  C  CD  . LYS A 1 996  ? 55.161 42.723  -24.502 1.00 28.26 ? 996  LYS A CD  1 
ATOM   8195  C  CE  . LYS A 1 996  ? 54.437 41.399  -24.592 1.00 29.46 ? 996  LYS A CE  1 
ATOM   8196  N  NZ  . LYS A 1 996  ? 54.166 41.045  -26.013 1.00 32.09 ? 996  LYS A NZ  1 
ATOM   8197  N  N   . LEU A 1 997  ? 56.793 46.572  -22.907 1.00 15.34 ? 997  LEU A N   1 
ATOM   8198  C  CA  . LEU A 1 997  ? 57.376 47.410  -21.889 1.00 15.38 ? 997  LEU A CA  1 
ATOM   8199  C  C   . LEU A 1 997  ? 57.722 46.553  -20.681 1.00 14.64 ? 997  LEU A C   1 
ATOM   8200  O  O   . LEU A 1 997  ? 56.834 45.960  -20.050 1.00 15.76 ? 997  LEU A O   1 
ATOM   8201  C  CB  . LEU A 1 997  ? 56.393 48.522  -21.503 1.00 16.57 ? 997  LEU A CB  1 
ATOM   8202  C  CG  . LEU A 1 997  ? 56.808 49.356  -20.291 1.00 17.60 ? 997  LEU A CG  1 
ATOM   8203  C  CD1 . LEU A 1 997  ? 58.021 50.246  -20.576 1.00 20.47 ? 997  LEU A CD1 1 
ATOM   8204  C  CD2 . LEU A 1 997  ? 55.621 50.172  -19.871 1.00 19.05 ? 997  LEU A CD2 1 
ATOM   8205  N  N   . ASP A 1 998  ? 59.010 46.509  -20.366 1.00 13.94 ? 998  ASP A N   1 
ATOM   8206  C  CA  . ASP A 1 998  ? 59.506 45.887  -19.147 1.00 13.84 ? 998  ASP A CA  1 
ATOM   8207  C  C   . ASP A 1 998  ? 60.077 46.973  -18.259 1.00 13.70 ? 998  ASP A C   1 
ATOM   8208  O  O   . ASP A 1 998  ? 61.215 47.439  -18.435 1.00 13.50 ? 998  ASP A O   1 
ATOM   8209  C  CB  . ASP A 1 998  ? 60.562 44.822  -19.493 1.00 14.20 ? 998  ASP A CB  1 
ATOM   8210  C  CG  . ASP A 1 998  ? 61.266 44.287  -18.277 1.00 16.57 ? 998  ASP A CG  1 
ATOM   8211  O  OD1 . ASP A 1 998  ? 60.792 44.516  -17.136 1.00 16.23 ? 998  ASP A OD1 1 
ATOM   8212  O  OD2 . ASP A 1 998  ? 62.328 43.622  -18.398 1.00 17.90 ? 998  ASP A OD2 1 
ATOM   8213  N  N   . VAL A 1 999  ? 59.277 47.401  -17.280 1.00 13.26 ? 999  VAL A N   1 
ATOM   8214  C  CA  . VAL A 1 999  ? 59.722 48.523  -16.474 1.00 12.36 ? 999  VAL A CA  1 
ATOM   8215  C  C   . VAL A 1 999  ? 60.995 48.239  -15.687 1.00 13.13 ? 999  VAL A C   1 
ATOM   8216  O  O   . VAL A 1 999  ? 61.754 49.142  -15.362 1.00 12.73 ? 999  VAL A O   1 
ATOM   8217  C  CB  . VAL A 1 999  ? 58.633 49.041  -15.516 1.00 12.45 ? 999  VAL A CB  1 
ATOM   8218  C  CG1 . VAL A 1 999  ? 57.500 49.660  -16.317 1.00 12.12 ? 999  VAL A CG1 1 
ATOM   8219  C  CG2 . VAL A 1 999  ? 58.146 47.939  -14.553 1.00 12.24 ? 999  VAL A CG2 1 
ATOM   8220  N  N   . CYS A 1 1000 ? 61.249 46.968  -15.398 1.00 13.49 ? 1000 CYS A N   1 
ATOM   8221  C  CA  . CYS A 1 1000 ? 62.448 46.653  -14.630 1.00 15.54 ? 1000 CYS A CA  1 
ATOM   8222  C  C   . CYS A 1 1000 ? 63.781 46.884  -15.356 1.00 14.85 ? 1000 CYS A C   1 
ATOM   8223  O  O   . CYS A 1 1000 ? 64.807 47.007  -14.712 1.00 16.84 ? 1000 CYS A O   1 
ATOM   8224  C  CB  . CYS A 1 1000 ? 62.348 45.244  -14.037 1.00 15.97 ? 1000 CYS A CB  1 
ATOM   8225  S  SG  . CYS A 1 1000 ? 61.297 45.214  -12.543 1.00 18.95 ? 1000 CYS A SG  1 
ATOM   8226  N  N   . HIS A 1 1001 ? 63.728 47.027  -16.681 1.00 15.03 ? 1001 HIS A N   1 
ATOM   8227  C  CA  . HIS A 1 1001 ? 64.935 47.295  -17.467 1.00 15.74 ? 1001 HIS A CA  1 
ATOM   8228  C  C   . HIS A 1 1001 ? 64.983 48.733  -18.014 1.00 16.38 ? 1001 HIS A C   1 
ATOM   8229  O  O   . HIS A 1 1001 ? 65.770 49.063  -18.907 1.00 16.70 ? 1001 HIS A O   1 
ATOM   8230  C  CB  . HIS A 1 1001 ? 65.094 46.238  -18.572 1.00 16.30 ? 1001 HIS A CB  1 
ATOM   8231  C  CG  . HIS A 1 1001 ? 65.661 44.941  -18.085 1.00 17.74 ? 1001 HIS A CG  1 
ATOM   8232  N  ND1 . HIS A 1 1001 ? 64.871 43.873  -17.729 1.00 18.34 ? 1001 HIS A ND1 1 
ATOM   8233  C  CD2 . HIS A 1 1001 ? 66.943 44.547  -17.888 1.00 19.92 ? 1001 HIS A CD2 1 
ATOM   8234  C  CE1 . HIS A 1 1001 ? 65.639 42.868  -17.339 1.00 19.70 ? 1001 HIS A CE1 1 
ATOM   8235  N  NE2 . HIS A 1 1001 ? 66.902 43.252  -17.426 1.00 20.87 ? 1001 HIS A NE2 1 
ATOM   8236  N  N   . LEU A 1 1002 ? 64.141 49.604  -17.475 1.00 15.41 ? 1002 LEU A N   1 
ATOM   8237  C  CA  . LEU A 1 1002 ? 64.186 50.998  -17.883 1.00 15.97 ? 1002 LEU A CA  1 
ATOM   8238  C  C   . LEU A 1 1002 ? 65.435 51.688  -17.358 1.00 16.25 ? 1002 LEU A C   1 
ATOM   8239  O  O   . LEU A 1 1002 ? 65.924 52.657  -17.967 1.00 17.11 ? 1002 LEU A O   1 
ATOM   8240  C  CB  . LEU A 1 1002 ? 62.945 51.750  -17.406 1.00 15.69 ? 1002 LEU A CB  1 
ATOM   8241  C  CG  . LEU A 1 1002 ? 61.737 51.552  -18.291 1.00 15.29 ? 1002 LEU A CG  1 
ATOM   8242  C  CD1 . LEU A 1 1002 ? 60.510 52.134  -17.612 1.00 14.74 ? 1002 LEU A CD1 1 
ATOM   8243  C  CD2 . LEU A 1 1002 ? 61.932 52.237  -19.635 1.00 15.93 ? 1002 LEU A CD2 1 
ATOM   8244  N  N   . LEU A 1 1003 ? 65.934 51.240  -16.211 1.00 16.60 ? 1003 LEU A N   1 
ATOM   8245  C  CA  . LEU A 1 1003 ? 67.157 51.786  -15.628 1.00 17.39 ? 1003 LEU A CA  1 
ATOM   8246  C  C   . LEU A 1 1003 ? 68.235 50.703  -15.704 1.00 18.23 ? 1003 LEU A C   1 
ATOM   8247  O  O   . LEU A 1 1003 ? 67.939 49.509  -15.614 1.00 18.48 ? 1003 LEU A O   1 
ATOM   8248  C  CB  . LEU A 1 1003 ? 66.942 52.224  -14.181 1.00 17.53 ? 1003 LEU A CB  1 
ATOM   8249  C  CG  . LEU A 1 1003 ? 66.252 53.575  -13.948 1.00 19.83 ? 1003 LEU A CG  1 
ATOM   8250  C  CD1 . LEU A 1 1003 ? 64.810 53.612  -14.404 1.00 25.60 ? 1003 LEU A CD1 1 
ATOM   8251  C  CD2 . LEU A 1 1003 ? 66.309 53.913  -12.494 1.00 24.51 ? 1003 LEU A CD2 1 
ATOM   8252  N  N   . PRO A 1 1004 ? 69.487 51.107  -15.884 1.00 18.87 ? 1004 PRO A N   1 
ATOM   8253  C  CA  . PRO A 1 1004 ? 70.555 50.125  -16.074 1.00 18.73 ? 1004 PRO A CA  1 
ATOM   8254  C  C   . PRO A 1 1004 ? 70.934 49.408  -14.772 1.00 18.84 ? 1004 PRO A C   1 
ATOM   8255  O  O   . PRO A 1 1004 ? 70.486 49.759  -13.663 1.00 17.15 ? 1004 PRO A O   1 
ATOM   8256  C  CB  . PRO A 1 1004 ? 71.705 50.983  -16.620 1.00 19.23 ? 1004 PRO A CB  1 
ATOM   8257  C  CG  . PRO A 1 1004 ? 71.474 52.316  -16.028 1.00 19.73 ? 1004 PRO A CG  1 
ATOM   8258  C  CD  . PRO A 1 1004 ? 69.984 52.495  -15.930 1.00 19.06 ? 1004 PRO A CD  1 
ATOM   8259  N  N   . ASN A 1 1005 ? 71.749 48.365  -14.917 1.00 18.96 ? 1005 ASN A N   1 
ATOM   8260  C  CA  . ASN A 1 1005 ? 72.276 47.601  -13.787 1.00 19.57 ? 1005 ASN A CA  1 
ATOM   8261  C  C   . ASN A 1 1005 ? 71.205 47.003  -12.858 1.00 18.64 ? 1005 ASN A C   1 
ATOM   8262  O  O   . ASN A 1 1005 ? 71.357 47.032  -11.636 1.00 18.87 ? 1005 ASN A O   1 
ATOM   8263  C  CB  . ASN A 1 1005 ? 73.245 48.452  -12.957 1.00 20.83 ? 1005 ASN A CB  1 
ATOM   8264  C  CG  . ASN A 1 1005 ? 74.291 49.148  -13.806 1.00 24.01 ? 1005 ASN A CG  1 
ATOM   8265  O  OD1 . ASN A 1 1005 ? 74.436 50.374  -13.748 1.00 29.22 ? 1005 ASN A OD1 1 
ATOM   8266  N  ND2 . ASN A 1 1005 ? 75.012 48.375  -14.608 1.00 25.65 ? 1005 ASN A ND2 1 
ATOM   8267  N  N   . VAL A 1 1006 ? 70.141 46.457  -13.442 1.00 18.44 ? 1006 VAL A N   1 
ATOM   8268  C  CA  . VAL A 1 1006 ? 69.082 45.855  -12.617 1.00 17.99 ? 1006 VAL A CA  1 
ATOM   8269  C  C   . VAL A 1 1006 ? 69.636 44.578  -11.984 1.00 18.44 ? 1006 VAL A C   1 
ATOM   8270  O  O   . VAL A 1 1006 ? 70.320 43.810  -12.649 1.00 19.29 ? 1006 VAL A O   1 
ATOM   8271  C  CB  . VAL A 1 1006 ? 67.751 45.627  -13.411 1.00 18.40 ? 1006 VAL A CB  1 
ATOM   8272  C  CG1 . VAL A 1 1006 ? 67.932 44.679  -14.568 1.00 17.80 ? 1006 VAL A CG1 1 
ATOM   8273  C  CG2 . VAL A 1 1006 ? 66.609 45.150  -12.477 1.00 16.88 ? 1006 VAL A CG2 1 
ATOM   8274  N  N   . ALA A 1 1007 ? 69.369 44.397  -10.694 1.00 16.71 ? 1007 ALA A N   1 
ATOM   8275  C  CA  . ALA A 1 1007 ? 69.831 43.234  -9.930  1.00 17.03 ? 1007 ALA A CA  1 
ATOM   8276  C  C   . ALA A 1 1007 ? 68.663 42.381  -9.459  1.00 17.17 ? 1007 ALA A C   1 
ATOM   8277  O  O   . ALA A 1 1007 ? 68.852 41.215  -9.094  1.00 18.42 ? 1007 ALA A O   1 
ATOM   8278  C  CB  . ALA A 1 1007 ? 70.650 43.697  -8.737  1.00 16.94 ? 1007 ALA A CB  1 
ATOM   8279  N  N   . ARG A 1 1008 ? 67.451 42.953  -9.436  1.00 15.92 ? 1008 ARG A N   1 
ATOM   8280  C  CA  . ARG A 1 1008 ? 66.269 42.233  -8.965  1.00 15.74 ? 1008 ARG A CA  1 
ATOM   8281  C  C   . ARG A 1 1008 ? 65.032 42.967  -9.448  1.00 15.11 ? 1008 ARG A C   1 
ATOM   8282  O  O   . ARG A 1 1008 ? 65.061 44.182  -9.599  1.00 13.47 ? 1008 ARG A O   1 
ATOM   8283  C  CB  . ARG A 1 1008 ? 66.260 42.207  -7.445  1.00 16.14 ? 1008 ARG A CB  1 
ATOM   8284  C  CG  . ARG A 1 1008 ? 65.242 41.296  -6.824  1.00 19.77 ? 1008 ARG A CG  1 
ATOM   8285  C  CD  . ARG A 1 1008 ? 65.347 41.303  -5.316  1.00 22.99 ? 1008 ARG A CD  1 
ATOM   8286  N  NE  . ARG A 1 1008 ? 64.581 40.215  -4.716  1.00 29.45 ? 1008 ARG A NE  1 
ATOM   8287  C  CZ  . ARG A 1 1008 ? 65.042 38.981  -4.516  1.00 31.91 ? 1008 ARG A CZ  1 
ATOM   8288  N  NH1 . ARG A 1 1008 ? 66.285 38.659  -4.862  1.00 31.32 ? 1008 ARG A NH1 1 
ATOM   8289  N  NH2 . ARG A 1 1008 ? 64.250 38.064  -3.966  1.00 33.21 ? 1008 ARG A NH2 1 
ATOM   8290  N  N   . CYS A 1 1009 ? 63.976 42.212  -9.712  1.00 14.03 ? 1009 CYS A N   1 
ATOM   8291  C  CA  . CYS A 1 1009 ? 62.663 42.775  -10.062 1.00 13.90 ? 1009 CYS A CA  1 
ATOM   8292  C  C   . CYS A 1 1009 ? 61.653 42.033  -9.221  1.00 13.40 ? 1009 CYS A C   1 
ATOM   8293  O  O   . CYS A 1 1009 ? 61.617 40.797  -9.227  1.00 13.48 ? 1009 CYS A O   1 
ATOM   8294  C  CB  . CYS A 1 1009 ? 62.374 42.542  -11.540 1.00 14.76 ? 1009 CYS A CB  1 
ATOM   8295  S  SG  . CYS A 1 1009 ? 60.850 43.288  -12.174 1.00 18.68 ? 1009 CYS A SG  1 
ATOM   8296  N  N   . GLU A 1 1010 ? 60.830 42.783  -8.489  1.00 11.24 ? 1010 GLU A N   1 
ATOM   8297  C  CA  . GLU A 1 1010 ? 59.803 42.183  -7.663  1.00 11.21 ? 1010 GLU A CA  1 
ATOM   8298  C  C   . GLU A 1 1010 ? 58.429 42.772  -7.978  1.00 10.26 ? 1010 GLU A C   1 
ATOM   8299  O  O   . GLU A 1 1010 ? 58.317 43.976  -8.189  1.00 10.81 ? 1010 GLU A O   1 
ATOM   8300  C  CB  . GLU A 1 1010 ? 60.110 42.429  -6.193  1.00 12.25 ? 1010 GLU A CB  1 
ATOM   8301  C  CG  . GLU A 1 1010 ? 61.276 41.564  -5.717  1.00 17.21 ? 1010 GLU A CG  1 
ATOM   8302  C  CD  . GLU A 1 1010 ? 62.099 42.175  -4.596  1.00 22.23 ? 1010 GLU A CD  1 
ATOM   8303  O  OE1 . GLU A 1 1010 ? 62.467 43.379  -4.643  1.00 24.36 ? 1010 GLU A OE1 1 
ATOM   8304  O  OE2 . GLU A 1 1010 ? 62.412 41.410  -3.651  1.00 25.54 ? 1010 GLU A OE2 1 
ATOM   8305  N  N   . ARG A 1 1011 ? 57.405 41.942  -7.950  1.00 8.55  ? 1011 ARG A N   1 
ATOM   8306  C  CA  . ARG A 1 1011 ? 56.032 42.460  -7.953  1.00 8.93  ? 1011 ARG A CA  1 
ATOM   8307  C  C   . ARG A 1 1011 ? 55.692 42.781  -6.510  1.00 8.99  ? 1011 ARG A C   1 
ATOM   8308  O  O   . ARG A 1 1011 ? 56.011 42.000  -5.616  1.00 8.81  ? 1011 ARG A O   1 
ATOM   8309  C  CB  . ARG A 1 1011 ? 55.073 41.443  -8.589  1.00 10.47 ? 1011 ARG A CB  1 
ATOM   8310  C  CG  . ARG A 1 1011 ? 53.701 42.043  -8.902  1.00 12.63 ? 1011 ARG A CG  1 
ATOM   8311  C  CD  . ARG A 1 1011 ? 52.758 41.089  -9.570  1.00 12.43 ? 1011 ARG A CD  1 
ATOM   8312  N  NE  . ARG A 1 1011 ? 52.475 39.961  -8.698  1.00 20.15 ? 1011 ARG A NE  1 
ATOM   8313  C  CZ  . ARG A 1 1011 ? 51.516 39.951  -7.772  1.00 24.08 ? 1011 ARG A CZ  1 
ATOM   8314  N  NH1 . ARG A 1 1011 ? 50.746 41.022  -7.590  1.00 27.28 ? 1011 ARG A NH1 1 
ATOM   8315  N  NH2 . ARG A 1 1011 ? 51.325 38.870  -7.023  1.00 25.69 ? 1011 ARG A NH2 1 
ATOM   8316  N  N   . THR A 1 1012 ? 55.062 43.931  -6.270  1.00 6.89  ? 1012 THR A N   1 
ATOM   8317  C  CA  . THR A 1 1012 ? 54.733 44.356  -4.924  1.00 6.78  ? 1012 THR A CA  1 
ATOM   8318  C  C   . THR A 1 1012 ? 53.266 44.742  -4.826  1.00 6.47  ? 1012 THR A C   1 
ATOM   8319  O  O   . THR A 1 1012 ? 52.601 44.938  -5.855  1.00 7.35  ? 1012 THR A O   1 
ATOM   8320  C  CB  . THR A 1 1012 ? 55.599 45.580  -4.499  1.00 8.05  ? 1012 THR A CB  1 
ATOM   8321  O  OG1 . THR A 1 1012 ? 55.294 46.711  -5.340  1.00 9.23  ? 1012 THR A OG1 1 
ATOM   8322  C  CG2 . THR A 1 1012 ? 57.074 45.364  -4.708  1.00 7.95  ? 1012 THR A CG2 1 
ATOM   8323  N  N   . THR A 1 1013 ? 52.816 44.991  -3.599  1.00 6.18  ? 1013 THR A N   1 
ATOM   8324  C  CA  . THR A 1 1013 ? 51.564 45.702  -3.416  1.00 6.20  ? 1013 THR A CA  1 
ATOM   8325  C  C   . THR A 1 1013 ? 51.668 47.113  -4.054  1.00 5.95  ? 1013 THR A C   1 
ATOM   8326  O  O   . THR A 1 1013 ? 52.741 47.625  -4.314  1.00 6.34  ? 1013 THR A O   1 
ATOM   8327  C  CB  . THR A 1 1013 ? 51.232 45.825  -1.942  1.00 7.24  ? 1013 THR A CB  1 
ATOM   8328  O  OG1 . THR A 1 1013 ? 52.399 46.264  -1.220  1.00 8.00  ? 1013 THR A OG1 1 
ATOM   8329  C  CG2 . THR A 1 1013 ? 50.778 44.431  -1.351  1.00 8.37  ? 1013 THR A CG2 1 
ATOM   8330  N  N   . LEU A 1 1014 ? 50.515 47.761  -4.255  1.00 5.79  ? 1014 LEU A N   1 
ATOM   8331  C  CA  . LEU A 1 1014 ? 50.535 49.014  -5.022  1.00 5.81  ? 1014 LEU A CA  1 
ATOM   8332  C  C   . LEU A 1 1014 ? 51.190 50.155  -4.305  1.00 5.31  ? 1014 LEU A C   1 
ATOM   8333  O  O   . LEU A 1 1014 ? 51.551 51.153  -4.928  1.00 6.06  ? 1014 LEU A O   1 
ATOM   8334  C  CB  . LEU A 1 1014 ? 49.123 49.424  -5.417  1.00 6.74  ? 1014 LEU A CB  1 
ATOM   8335  C  CG  . LEU A 1 1014 ? 48.381 48.485  -6.348  1.00 5.62  ? 1014 LEU A CG  1 
ATOM   8336  C  CD1 . LEU A 1 1014 ? 47.036 49.194  -6.671  1.00 7.91  ? 1014 LEU A CD1 1 
ATOM   8337  C  CD2 . LEU A 1 1014 ? 49.158 48.149  -7.645  1.00 7.39  ? 1014 LEU A CD2 1 
ATOM   8338  N  N   . THR A 1 1015 ? 51.350 49.998  -2.990  1.00 5.34  ? 1015 THR A N   1 
ATOM   8339  C  CA  . THR A 1 1015 ? 52.017 50.984  -2.149  1.00 5.49  ? 1015 THR A CA  1 
ATOM   8340  C  C   . THR A 1 1015 ? 53.526 50.749  -2.097  1.00 5.93  ? 1015 THR A C   1 
ATOM   8341  O  O   . THR A 1 1015 ? 54.229 51.522  -1.430  1.00 7.03  ? 1015 THR A O   1 
ATOM   8342  C  CB  . THR A 1 1015 ? 51.509 50.884  -0.721  1.00 6.28  ? 1015 THR A CB  1 
ATOM   8343  O  OG1 . THR A 1 1015 ? 51.636 49.498  -0.342  1.00 6.80  ? 1015 THR A OG1 1 
ATOM   8344  C  CG2 . THR A 1 1015 ? 50.018 51.218  -0.652  1.00 6.49  ? 1015 THR A CG2 1 
ATOM   8345  N  N   . PHE A 1 1016 ? 53.988 49.673  -2.737  1.00 5.71  ? 1016 PHE A N   1 
ATOM   8346  C  CA  . PHE A 1 1016 ? 55.395 49.264  -2.753  1.00 7.08  ? 1016 PHE A CA  1 
ATOM   8347  C  C   . PHE A 1 1016 ? 55.862 48.670  -1.434  1.00 8.39  ? 1016 PHE A C   1 
ATOM   8348  O  O   . PHE A 1 1016 ? 57.050 48.405  -1.292  1.00 9.93  ? 1016 PHE A O   1 
ATOM   8349  C  CB  . PHE A 1 1016 ? 56.334 50.389  -3.192  1.00 7.75  ? 1016 PHE A CB  1 
ATOM   8350  C  CG  . PHE A 1 1016 ? 55.980 51.026  -4.516  1.00 6.24  ? 1016 PHE A CG  1 
ATOM   8351  C  CD1 . PHE A 1 1016 ? 55.846 50.261  -5.669  1.00 7.08  ? 1016 PHE A CD1 1 
ATOM   8352  C  CD2 . PHE A 1 1016 ? 55.820 52.410  -4.605  1.00 7.51  ? 1016 PHE A CD2 1 
ATOM   8353  C  CE1 . PHE A 1 1016 ? 55.546 50.887  -6.898  1.00 6.66  ? 1016 PHE A CE1 1 
ATOM   8354  C  CE2 . PHE A 1 1016 ? 55.521 53.021  -5.825  1.00 7.54  ? 1016 PHE A CE2 1 
ATOM   8355  C  CZ  . PHE A 1 1016 ? 55.407 52.243  -6.961  1.00 7.18  ? 1016 PHE A CZ  1 
ATOM   8356  N  N   . LEU A 1 1017 ? 54.958 48.392  -0.509  1.00 7.19  ? 1017 LEU A N   1 
ATOM   8357  C  CA  . LEU A 1 1017 ? 55.385 48.060  0.855   1.00 8.98  ? 1017 LEU A CA  1 
ATOM   8358  C  C   . LEU A 1 1017 ? 55.564 46.571  1.131   1.00 9.75  ? 1017 LEU A C   1 
ATOM   8359  O  O   . LEU A 1 1017 ? 56.149 46.213  2.174   1.00 12.01 ? 1017 LEU A O   1 
ATOM   8360  C  CB  . LEU A 1 1017 ? 54.424 48.679  1.865   1.00 8.68  ? 1017 LEU A CB  1 
ATOM   8361  C  CG  . LEU A 1 1017 ? 54.448 50.210  1.859   1.00 8.08  ? 1017 LEU A CG  1 
ATOM   8362  C  CD1 . LEU A 1 1017 ? 53.360 50.697  2.777   1.00 9.49  ? 1017 LEU A CD1 1 
ATOM   8363  C  CD2 . LEU A 1 1017 ? 55.780 50.813  2.217   1.00 10.06 ? 1017 LEU A CD2 1 
ATOM   8364  N  N   . GLN A 1 1018 ? 55.095 45.693  0.246   1.00 8.88  ? 1018 GLN A N   1 
ATOM   8365  C  CA  . GLN A 1 1018 ? 55.283 44.242  0.471   1.00 10.11 ? 1018 GLN A CA  1 
ATOM   8366  C  C   . GLN A 1 1018 ? 55.651 43.577  -0.827  1.00 10.54 ? 1018 GLN A C   1 
ATOM   8367  O  O   . GLN A 1 1018 ? 55.006 43.811  -1.845  1.00 10.06 ? 1018 GLN A O   1 
ATOM   8368  C  CB  . GLN A 1 1018 ? 54.002 43.608  1.009   1.00 10.88 ? 1018 GLN A CB  1 
ATOM   8369  C  CG  . GLN A 1 1018 ? 54.200 42.096  1.302   1.00 14.68 ? 1018 GLN A CG  1 
ATOM   8370  C  CD  . GLN A 1 1018 ? 52.903 41.342  1.501   1.00 19.87 ? 1018 GLN A CD  1 
ATOM   8371  O  OE1 . GLN A 1 1018 ? 51.823 41.944  1.588   1.00 18.93 ? 1018 GLN A OE1 1 
ATOM   8372  N  NE2 . GLN A 1 1018 ? 53.004 40.009  1.589   1.00 22.42 ? 1018 GLN A NE2 1 
ATOM   8373  N  N   . ASN A 1 1019 ? 56.701 42.767  -0.810  1.00 11.55 ? 1019 ASN A N   1 
ATOM   8374  C  CA  . ASN A 1 1019 ? 57.073 41.981  -1.973  1.00 13.88 ? 1019 ASN A CA  1 
ATOM   8375  C  C   . ASN A 1 1019 ? 56.178 40.780  -2.115  1.00 14.74 ? 1019 ASN A C   1 
ATOM   8376  O  O   . ASN A 1 1019 ? 55.998 40.028  -1.141  1.00 16.25 ? 1019 ASN A O   1 
ATOM   8377  C  CB  . ASN A 1 1019 ? 58.543 41.552  -1.855  1.00 14.04 ? 1019 ASN A CB  1 
ATOM   8378  C  CG  . ASN A 1 1019 ? 59.486 42.753  -1.766  1.00 16.41 ? 1019 ASN A CG  1 
ATOM   8379  O  OD1 . ASN A 1 1019 ? 59.251 43.792  -2.394  1.00 16.51 ? 1019 ASN A OD1 1 
ATOM   8380  N  ND2 . ASN A 1 1019 ? 60.572 42.616  -0.985  1.00 19.91 ? 1019 ASN A ND2 1 
ATOM   8381  N  N   . LEU A 1 1020 ? 55.614 40.603  -3.302  1.00 13.99 ? 1020 LEU A N   1 
ATOM   8382  C  CA  . LEU A 1 1020 ? 54.679 39.525  -3.580  1.00 14.91 ? 1020 LEU A CA  1 
ATOM   8383  C  C   . LEU A 1 1020 ? 55.271 38.423  -4.435  1.00 15.69 ? 1020 LEU A C   1 
ATOM   8384  O  O   . LEU A 1 1020 ? 54.852 37.267  -4.302  1.00 16.71 ? 1020 LEU A O   1 
ATOM   8385  C  CB  . LEU A 1 1020 ? 53.403 40.044  -4.259  1.00 15.08 ? 1020 LEU A CB  1 
ATOM   8386  C  CG  . LEU A 1 1020 ? 52.601 41.109  -3.486  1.00 14.68 ? 1020 LEU A CG  1 
ATOM   8387  C  CD1 . LEU A 1 1020 ? 51.511 41.647  -4.377  1.00 17.23 ? 1020 LEU A CD1 1 
ATOM   8388  C  CD2 . LEU A 1 1020 ? 52.010 40.501  -2.222  1.00 16.36 ? 1020 LEU A CD2 1 
ATOM   8389  N  N   . GLU A 1 1021 ? 56.231 38.760  -5.296  1.00 15.94 ? 1021 GLU A N   1 
ATOM   8390  C  CA  . GLU A 1 1021 ? 56.820 37.783  -6.221  1.00 18.10 ? 1021 GLU A CA  1 
ATOM   8391  C  C   . GLU A 1 1021 ? 58.189 38.235  -6.655  1.00 17.29 ? 1021 GLU A C   1 
ATOM   8392  O  O   . GLU A 1 1021 ? 58.389 39.395  -6.967  1.00 15.41 ? 1021 GLU A O   1 
ATOM   8393  C  CB  . GLU A 1 1021 ? 55.932 37.650  -7.459  1.00 17.75 ? 1021 GLU A CB  1 
ATOM   8394  C  CG  . GLU A 1 1021 ? 56.279 36.536  -8.442  1.00 22.26 ? 1021 GLU A CG  1 
ATOM   8395  C  CD  . GLU A 1 1021 ? 55.421 36.576  -9.698  1.00 23.27 ? 1021 GLU A CD  1 
ATOM   8396  O  OE1 . GLU A 1 1021 ? 54.473 37.404  -9.769  1.00 29.61 ? 1021 GLU A OE1 1 
ATOM   8397  O  OE2 . GLU A 1 1021 ? 55.703 35.776  -10.628 1.00 28.59 ? 1021 GLU A OE2 1 
ATOM   8398  N  N   . HIS A 1 1022 ? 59.135 37.304  -6.716  1.00 17.37 ? 1022 HIS A N   1 
ATOM   8399  C  CA  . HIS A 1 1022 ? 60.470 37.580  -7.194  1.00 18.29 ? 1022 HIS A CA  1 
ATOM   8400  C  C   . HIS A 1 1022 ? 60.486 37.141  -8.636  1.00 18.19 ? 1022 HIS A C   1 
ATOM   8401  O  O   . HIS A 1 1022 ? 60.209 35.977  -8.931  1.00 18.79 ? 1022 HIS A O   1 
ATOM   8402  C  CB  . HIS A 1 1022 ? 61.477 36.771  -6.371  1.00 18.72 ? 1022 HIS A CB  1 
ATOM   8403  C  CG  . HIS A 1 1022 ? 62.883 36.888  -6.855  1.00 23.90 ? 1022 HIS A CG  1 
ATOM   8404  N  ND1 . HIS A 1 1022 ? 63.759 35.824  -6.850  1.00 29.10 ? 1022 HIS A ND1 1 
ATOM   8405  C  CD2 . HIS A 1 1022 ? 63.572 37.943  -7.352  1.00 25.81 ? 1022 HIS A CD2 1 
ATOM   8406  C  CE1 . HIS A 1 1022 ? 64.926 36.216  -7.335  1.00 29.13 ? 1022 HIS A CE1 1 
ATOM   8407  N  NE2 . HIS A 1 1022 ? 64.841 37.499  -7.641  1.00 29.27 ? 1022 HIS A NE2 1 
ATOM   8408  N  N   . LEU A 1 1023 ? 60.749 38.076  -9.546  1.00 17.34 ? 1023 LEU A N   1 
ATOM   8409  C  CA  . LEU A 1 1023 ? 60.460 37.844  -10.953 1.00 18.32 ? 1023 LEU A CA  1 
ATOM   8410  C  C   . LEU A 1 1023 ? 61.617 37.252  -11.762 1.00 19.16 ? 1023 LEU A C   1 
ATOM   8411  O  O   . LEU A 1 1023 ? 62.731 37.789  -11.770 1.00 18.85 ? 1023 LEU A O   1 
ATOM   8412  C  CB  . LEU A 1 1023 ? 59.956 39.135  -11.598 1.00 17.85 ? 1023 LEU A CB  1 
ATOM   8413  C  CG  . LEU A 1 1023 ? 58.548 39.488  -11.100 1.00 18.01 ? 1023 LEU A CG  1 
ATOM   8414  C  CD1 . LEU A 1 1023 ? 58.275 40.949  -11.295 1.00 21.64 ? 1023 LEU A CD1 1 
ATOM   8415  C  CD2 . LEU A 1 1023 ? 57.497 38.659  -11.823 1.00 21.55 ? 1023 LEU A CD2 1 
ATOM   8416  N  N   . ASP A 1 1024 ? 61.324 36.159  -12.459 1.00 20.96 ? 1024 ASP A N   1 
ATOM   8417  C  CA  . ASP A 1 1024 ? 62.327 35.465  -13.263 1.00 22.72 ? 1024 ASP A CA  1 
ATOM   8418  C  C   . ASP A 1 1024 ? 62.949 36.371  -14.308 1.00 22.45 ? 1024 ASP A C   1 
ATOM   8419  O  O   . ASP A 1 1024 ? 62.240 37.110  -15.015 1.00 23.01 ? 1024 ASP A O   1 
ATOM   8420  C  CB  . ASP A 1 1024 ? 61.701 34.255  -13.947 1.00 23.80 ? 1024 ASP A CB  1 
ATOM   8421  C  CG  . ASP A 1 1024 ? 61.232 33.202  -12.954 1.00 27.76 ? 1024 ASP A CG  1 
ATOM   8422  O  OD1 . ASP A 1 1024 ? 61.672 33.261  -11.775 1.00 32.71 ? 1024 ASP A OD1 1 
ATOM   8423  O  OD2 . ASP A 1 1024 ? 60.427 32.283  -13.265 1.00 33.51 ? 1024 ASP A OD2 1 
ATOM   8424  N  N   . GLY A 1 1025 ? 64.276 36.331  -14.378 1.00 22.23 ? 1025 GLY A N   1 
ATOM   8425  C  CA  . GLY A 1 1025 ? 65.025 37.072  -15.377 1.00 22.15 ? 1025 GLY A CA  1 
ATOM   8426  C  C   . GLY A 1 1025 ? 64.927 38.569  -15.212 1.00 21.86 ? 1025 GLY A C   1 
ATOM   8427  O  O   . GLY A 1 1025 ? 65.305 39.322  -16.106 1.00 22.45 ? 1025 GLY A O   1 
ATOM   8428  N  N   . MET A 1 1026 ? 64.452 38.994  -14.039 1.00 20.74 ? 1026 MET A N   1 
ATOM   8429  C  CA  . MET A 1 1026 ? 64.312 40.414  -13.704 1.00 21.60 ? 1026 MET A CA  1 
ATOM   8430  C  C   . MET A 1 1026 ? 63.390 41.117  -14.684 1.00 20.04 ? 1026 MET A C   1 
ATOM   8431  O  O   . MET A 1 1026 ? 63.568 42.318  -14.938 1.00 19.97 ? 1026 MET A O   1 
ATOM   8432  C  CB  . MET A 1 1026 ? 65.670 41.121  -13.644 1.00 21.28 ? 1026 MET A CB  1 
ATOM   8433  C  CG  . MET A 1 1026 ? 66.610 40.460  -12.657 1.00 23.00 ? 1026 MET A CG  1 
ATOM   8434  S  SD  . MET A 1 1026 ? 68.245 41.181  -12.656 1.00 26.56 ? 1026 MET A SD  1 
ATOM   8435  C  CE  . MET A 1 1026 ? 68.845 40.754  -14.342 1.00 29.17 ? 1026 MET A CE  1 
ATOM   8436  N  N   . VAL A 1 1027 ? 62.418 40.379  -15.221 1.00 18.98 ? 1027 VAL A N   1 
ATOM   8437  C  CA  . VAL A 1 1027 ? 61.454 40.927  -16.179 1.00 19.07 ? 1027 VAL A CA  1 
ATOM   8438  C  C   . VAL A 1 1027 ? 60.093 41.124  -15.527 1.00 18.90 ? 1027 VAL A C   1 
ATOM   8439  O  O   . VAL A 1 1027 ? 59.516 40.190  -14.952 1.00 18.20 ? 1027 VAL A O   1 
ATOM   8440  C  CB  . VAL A 1 1027 ? 61.295 40.050  -17.455 1.00 18.72 ? 1027 VAL A CB  1 
ATOM   8441  C  CG1 . VAL A 1 1027 ? 60.110 40.536  -18.311 1.00 20.05 ? 1027 VAL A CG1 1 
ATOM   8442  C  CG2 . VAL A 1 1027 ? 62.587 40.033  -18.286 1.00 19.82 ? 1027 VAL A CG2 1 
ATOM   8443  N  N   . ALA A 1 1028 ? 59.574 42.347  -15.641 1.00 17.97 ? 1028 ALA A N   1 
ATOM   8444  C  CA  . ALA A 1 1028 ? 58.239 42.680  -15.131 1.00 18.29 ? 1028 ALA A CA  1 
ATOM   8445  C  C   . ALA A 1 1028 ? 57.232 42.495  -16.241 1.00 18.25 ? 1028 ALA A C   1 
ATOM   8446  O  O   . ALA A 1 1028 ? 57.224 43.278  -17.189 1.00 18.62 ? 1028 ALA A O   1 
ATOM   8447  C  CB  . ALA A 1 1028 ? 58.194 44.113  -14.652 1.00 18.14 ? 1028 ALA A CB  1 
ATOM   8448  N  N   . PRO A 1 1029 ? 56.350 41.514  -16.106 1.00 18.01 ? 1029 PRO A N   1 
ATOM   8449  C  CA  . PRO A 1 1029 ? 55.331 41.241  -17.128 1.00 18.65 ? 1029 PRO A CA  1 
ATOM   8450  C  C   . PRO A 1 1029 ? 54.345 42.401  -17.238 1.00 18.81 ? 1029 PRO A C   1 
ATOM   8451  O  O   . PRO A 1 1029 ? 54.151 43.125  -16.272 1.00 20.00 ? 1029 PRO A O   1 
ATOM   8452  C  CB  . PRO A 1 1029 ? 54.592 40.015  -16.582 1.00 18.57 ? 1029 PRO A CB  1 
ATOM   8453  C  CG  . PRO A 1 1029 ? 55.437 39.487  -15.451 1.00 19.58 ? 1029 PRO A CG  1 
ATOM   8454  C  CD  . PRO A 1 1029 ? 56.223 40.641  -14.925 1.00 17.96 ? 1029 PRO A CD  1 
ATOM   8455  N  N   . GLU A 1 1030 ? 53.778 42.603  -18.411 1.00 18.37 ? 1030 GLU A N   1 
ATOM   8456  C  CA  . GLU A 1 1030 ? 52.678 43.548  -18.544 1.00 19.57 ? 1030 GLU A CA  1 
ATOM   8457  C  C   . GLU A 1 1030 ? 51.419 42.963  -17.897 1.00 19.62 ? 1030 GLU A C   1 
ATOM   8458  O  O   . GLU A 1 1030 ? 51.301 41.731  -17.673 1.00 21.02 ? 1030 GLU A O   1 
ATOM   8459  C  CB  . GLU A 1 1030 ? 52.422 43.853  -20.016 1.00 19.94 ? 1030 GLU A CB  1 
ATOM   8460  C  CG  . GLU A 1 1030 ? 53.558 44.612  -20.698 1.00 19.98 ? 1030 GLU A CG  1 
ATOM   8461  C  CD  . GLU A 1 1030 ? 53.263 44.919  -22.153 1.00 20.67 ? 1030 GLU A CD  1 
ATOM   8462  O  OE1 . GLU A 1 1030 ? 52.289 44.335  -22.703 1.00 23.20 ? 1030 GLU A OE1 1 
ATOM   8463  O  OE2 . GLU A 1 1030 ? 54.012 45.749  -22.748 1.00 18.30 ? 1030 GLU A OE2 1 
ATOM   8464  N  N   . VAL A 1 1031 ? 50.487 43.852  -17.583 1.00 17.57 ? 1031 VAL A N   1 
ATOM   8465  C  CA  . VAL A 1 1031 ? 49.280 43.495  -16.859 1.00 15.87 ? 1031 VAL A CA  1 
ATOM   8466  C  C   . VAL A 1 1031 ? 48.118 43.251  -17.824 1.00 14.96 ? 1031 VAL A C   1 
ATOM   8467  O  O   . VAL A 1 1031 ? 48.167 43.676  -18.983 1.00 15.42 ? 1031 VAL A O   1 
ATOM   8468  C  CB  . VAL A 1 1031 ? 48.931 44.572  -15.799 1.00 16.22 ? 1031 VAL A CB  1 
ATOM   8469  C  CG1 . VAL A 1 1031 ? 50.066 44.673  -14.786 1.00 17.55 ? 1031 VAL A CG1 1 
ATOM   8470  C  CG2 . VAL A 1 1031 ? 48.638 45.934  -16.417 1.00 16.44 ? 1031 VAL A CG2 1 
ATOM   8471  N  N   . CYS A 1 1032 ? 47.085 42.559  -17.356 1.00 13.70 ? 1032 CYS A N   1 
ATOM   8472  C  CA  . CYS A 1 1032 ? 45.866 42.299  -18.125 1.00 13.83 ? 1032 CYS A CA  1 
ATOM   8473  C  C   . CYS A 1 1032 ? 44.941 43.514  -18.198 1.00 11.32 ? 1032 CYS A C   1 
ATOM   8474  O  O   . CYS A 1 1032 ? 45.063 44.417  -17.376 1.00 9.99  ? 1032 CYS A O   1 
ATOM   8475  C  CB  . CYS A 1 1032 ? 45.092 41.195  -17.434 1.00 14.24 ? 1032 CYS A CB  1 
ATOM   8476  S  SG  . CYS A 1 1032 ? 45.936 39.618  -17.660 1.00 22.69 ? 1032 CYS A SG  1 
ATOM   8477  N  N   . PRO A 1 1033 ? 44.000 43.552  -19.146 1.00 10.41 ? 1033 PRO A N   1 
ATOM   8478  C  CA  . PRO A 1 1033 ? 43.013 44.639  -19.176 1.00 10.07 ? 1033 PRO A CA  1 
ATOM   8479  C  C   . PRO A 1 1033 ? 42.294 44.768  -17.845 1.00 8.40  ? 1033 PRO A C   1 
ATOM   8480  O  O   . PRO A 1 1033 ? 41.837 43.782  -17.264 1.00 8.90  ? 1033 PRO A O   1 
ATOM   8481  C  CB  . PRO A 1 1033 ? 42.028 44.191  -20.263 1.00 9.53  ? 1033 PRO A CB  1 
ATOM   8482  C  CG  . PRO A 1 1033 ? 42.877 43.336  -21.166 1.00 11.91 ? 1033 PRO A CG  1 
ATOM   8483  C  CD  . PRO A 1 1033 ? 43.802 42.589  -20.262 1.00 11.75 ? 1033 PRO A CD  1 
ATOM   8484  N  N   . MET A 1 1034 ? 42.203 46.017  -17.402 1.00 8.01  ? 1034 MET A N   1 
ATOM   8485  C  CA  . MET A 1 1034 ? 41.571 46.432  -16.161 1.00 9.29  ? 1034 MET A CA  1 
ATOM   8486  C  C   . MET A 1 1034 ? 42.373 46.064  -14.931 1.00 9.92  ? 1034 MET A C   1 
ATOM   8487  O  O   . MET A 1 1034 ? 41.911 46.298  -13.811 1.00 13.17 ? 1034 MET A O   1 
ATOM   8488  C  CB  . MET A 1 1034 ? 40.100 46.010  -16.022 1.00 8.66  ? 1034 MET A CB  1 
ATOM   8489  C  CG  . MET A 1 1034 ? 39.220 46.529  -17.150 1.00 11.30 ? 1034 MET A CG  1 
ATOM   8490  S  SD  . MET A 1 1034 ? 39.276 48.299  -17.359 1.00 11.93 ? 1034 MET A SD  1 
ATOM   8491  C  CE  . MET A 1 1034 ? 38.445 48.916  -15.832 1.00 12.70 ? 1034 MET A CE  1 
ATOM   8492  N  N   . GLU A 1 1035 ? 43.593 45.596  -15.116 1.00 9.04  ? 1035 GLU A N   1 
ATOM   8493  C  CA  . GLU A 1 1035 ? 44.418 45.302  -13.963 1.00 10.33 ? 1035 GLU A CA  1 
ATOM   8494  C  C   . GLU A 1 1035 ? 45.468 46.376  -13.731 1.00 8.77  ? 1035 GLU A C   1 
ATOM   8495  O  O   . GLU A 1 1035 ? 45.829 47.126  -14.637 1.00 7.91  ? 1035 GLU A O   1 
ATOM   8496  C  CB  . GLU A 1 1035 ? 45.042 43.915  -14.098 1.00 13.04 ? 1035 GLU A CB  1 
ATOM   8497  C  CG  . GLU A 1 1035 ? 43.993 42.774  -14.045 1.00 18.19 ? 1035 GLU A CG  1 
ATOM   8498  C  CD  . GLU A 1 1035 ? 43.268 42.590  -12.697 1.00 27.68 ? 1035 GLU A CD  1 
ATOM   8499  O  OE1 . GLU A 1 1035 ? 43.026 43.574  -11.954 1.00 29.62 ? 1035 GLU A OE1 1 
ATOM   8500  O  OE2 . GLU A 1 1035 ? 42.904 41.429  -12.377 1.00 31.66 ? 1035 GLU A OE2 1 
ATOM   8501  N  N   . THR A 1 1036 ? 45.936 46.455  -12.489 1.00 7.41  ? 1036 THR A N   1 
ATOM   8502  C  CA  . THR A 1 1036 ? 47.004 47.351  -12.089 1.00 8.86  ? 1036 THR A CA  1 
ATOM   8503  C  C   . THR A 1 1036 ? 47.956 46.525  -11.261 1.00 8.72  ? 1036 THR A C   1 
ATOM   8504  O  O   . THR A 1 1036 ? 47.519 45.723  -10.418 1.00 10.36 ? 1036 THR A O   1 
ATOM   8505  C  CB  . THR A 1 1036 ? 46.410 48.450  -11.213 1.00 8.24  ? 1036 THR A CB  1 
ATOM   8506  O  OG1 . THR A 1 1036 ? 45.329 49.090  -11.900 1.00 8.81  ? 1036 THR A OG1 1 
ATOM   8507  C  CG2 . THR A 1 1036 ? 47.371 49.572  -10.899 1.00 9.66  ? 1036 THR A CG2 1 
ATOM   8508  N  N   . ALA A 1 1037 ? 49.247 46.698  -11.512 1.00 8.24  ? 1037 ALA A N   1 
ATOM   8509  C  CA  . ALA A 1 1037 ? 50.284 45.990  -10.782 1.00 8.38  ? 1037 ALA A CA  1 
ATOM   8510  C  C   . ALA A 1 1037 ? 51.394 46.931  -10.441 1.00 8.11  ? 1037 ALA A C   1 
ATOM   8511  O  O   . ALA A 1 1037 ? 51.548 47.952  -11.109 1.00 9.21  ? 1037 ALA A O   1 
ATOM   8512  C  CB  . ALA A 1 1037 ? 50.816 44.869  -11.621 1.00 10.67 ? 1037 ALA A CB  1 
ATOM   8513  N  N   . ALA A 1 1038 ? 52.155 46.595  -9.419  1.00 6.96  ? 1038 ALA A N   1 
ATOM   8514  C  CA  . ALA A 1 1038 ? 53.304 47.383  -9.050  1.00 6.90  ? 1038 ALA A CA  1 
ATOM   8515  C  C   . ALA A 1 1038 ? 54.546 46.519  -9.079  1.00 7.25  ? 1038 ALA A C   1 
ATOM   8516  O  O   . ALA A 1 1038 ? 54.480 45.334  -8.714  1.00 7.68  ? 1038 ALA A O   1 
ATOM   8517  C  CB  . ALA A 1 1038 ? 53.129 48.014  -7.684  1.00 6.70  ? 1038 ALA A CB  1 
ATOM   8518  N  N   . TYR A 1 1039 ? 55.654 47.135  -9.481  1.00 7.45  ? 1039 TYR A N   1 
ATOM   8519  C  CA  . TYR A 1 1039 ? 56.931 46.444  -9.561  1.00 7.69  ? 1039 TYR A CA  1 
ATOM   8520  C  C   . TYR A 1 1039 ? 57.985 47.338  -8.972  1.00 9.58  ? 1039 TYR A C   1 
ATOM   8521  O  O   . TYR A 1 1039 ? 57.875 48.561  -9.062  1.00 9.76  ? 1039 TYR A O   1 
ATOM   8522  C  CB  . TYR A 1 1039 ? 57.285 46.158  -11.005 1.00 9.54  ? 1039 TYR A CB  1 
ATOM   8523  C  CG  . TYR A 1 1039 ? 56.318 45.280  -11.702 1.00 8.70  ? 1039 TYR A CG  1 
ATOM   8524  C  CD1 . TYR A 1 1039 ? 56.310 43.911  -11.468 1.00 9.62  ? 1039 TYR A CD1 1 
ATOM   8525  C  CD2 . TYR A 1 1039 ? 55.397 45.807  -12.623 1.00 11.56 ? 1039 TYR A CD2 1 
ATOM   8526  C  CE1 . TYR A 1 1039 ? 55.403 43.077  -12.142 1.00 10.06 ? 1039 TYR A CE1 1 
ATOM   8527  C  CE2 . TYR A 1 1039 ? 54.512 44.987  -13.278 1.00 11.25 ? 1039 TYR A CE2 1 
ATOM   8528  C  CZ  . TYR A 1 1039 ? 54.512 43.641  -13.029 1.00 12.63 ? 1039 TYR A CZ  1 
ATOM   8529  O  OH  . TYR A 1 1039 ? 53.641 42.839  -13.720 1.00 15.36 ? 1039 TYR A OH  1 
ATOM   8530  N  N   . VAL A 1 1040 ? 58.987 46.735  -8.331  1.00 9.37  ? 1040 VAL A N   1 
ATOM   8531  C  CA  . VAL A 1 1040 ? 60.132 47.492  -7.854  1.00 9.40  ? 1040 VAL A CA  1 
ATOM   8532  C  C   . VAL A 1 1040 ? 61.356 46.862  -8.455  1.00 10.61 ? 1040 VAL A C   1 
ATOM   8533  O  O   . VAL A 1 1040 ? 61.537 45.638  -8.343  1.00 9.67  ? 1040 VAL A O   1 
ATOM   8534  C  CB  . VAL A 1 1040 ? 60.223 47.475  -6.330  1.00 9.70  ? 1040 VAL A CB  1 
ATOM   8535  C  CG1 . VAL A 1 1040 ? 61.537 48.113  -5.845  1.00 9.65  ? 1040 VAL A CG1 1 
ATOM   8536  C  CG2 . VAL A 1 1040 ? 59.031 48.253  -5.756  1.00 10.05 ? 1040 VAL A CG2 1 
ATOM   8537  N  N   . SER A 1 1041 ? 62.149 47.666  -9.150  1.00 9.59  ? 1041 SER A N   1 
ATOM   8538  C  CA  . SER A 1 1041 ? 63.447 47.218  -9.632  1.00 9.95  ? 1041 SER A CA  1 
ATOM   8539  C  C   . SER A 1 1041 ? 64.530 47.682  -8.673  1.00 9.72  ? 1041 SER A C   1 
ATOM   8540  O  O   . SER A 1 1041 ? 64.469 48.790  -8.148  1.00 9.95  ? 1041 SER A O   1 
ATOM   8541  C  CB  . SER A 1 1041 ? 63.696 47.714  -11.062 1.00 11.17 ? 1041 SER A CB  1 
ATOM   8542  O  OG  . SER A 1 1041 ? 63.707 49.124  -11.104 1.00 11.91 ? 1041 SER A OG  1 
ATOM   8543  N  N   . SER A 1 1042 ? 65.533 46.816  -8.433  1.00 10.25 ? 1042 SER A N   1 
ATOM   8544  C  CA  . SER A 1 1042 ? 66.647 47.135  -7.545  1.00 11.60 ? 1042 SER A CA  1 
ATOM   8545  C  C   . SER A 1 1042 ? 67.896 47.193  -8.430  1.00 11.96 ? 1042 SER A C   1 
ATOM   8546  O  O   . SER A 1 1042 ? 68.047 46.365  -9.319  1.00 12.67 ? 1042 SER A O   1 
ATOM   8547  C  CB  . SER A 1 1042 ? 66.836 46.048  -6.478  1.00 12.66 ? 1042 SER A CB  1 
ATOM   8548  O  OG  . SER A 1 1042 ? 65.672 45.937  -5.691  1.00 13.62 ? 1042 SER A OG  1 
ATOM   8549  N  N   . HIS A 1 1043 ? 68.776 48.137  -8.139  1.00 13.33 ? 1043 HIS A N   1 
ATOM   8550  C  CA  . HIS A 1 1043 ? 69.900 48.437  -9.013  1.00 14.71 ? 1043 HIS A CA  1 
ATOM   8551  C  C   . HIS A 1 1043 ? 71.127 48.595  -8.167  1.00 15.91 ? 1043 HIS A C   1 
ATOM   8552  O  O   . HIS A 1 1043 ? 71.124 49.274  -7.177  1.00 15.27 ? 1043 HIS A O   1 
ATOM   8553  C  CB  . HIS A 1 1043 ? 69.633 49.715  -9.827  1.00 14.77 ? 1043 HIS A CB  1 
ATOM   8554  C  CG  . HIS A 1 1043 ? 68.357 49.662  -10.598 1.00 14.82 ? 1043 HIS A CG  1 
ATOM   8555  N  ND1 . HIS A 1 1043 ? 68.293 49.263  -11.909 1.00 13.76 ? 1043 HIS A ND1 1 
ATOM   8556  C  CD2 . HIS A 1 1043 ? 67.081 49.881  -10.208 1.00 14.26 ? 1043 HIS A CD2 1 
ATOM   8557  C  CE1 . HIS A 1 1043 ? 67.033 49.263  -12.306 1.00 14.90 ? 1043 HIS A CE1 1 
ATOM   8558  N  NE2 . HIS A 1 1043 ? 66.280 49.636  -11.286 1.00 12.65 ? 1043 HIS A NE2 1 
ATOM   8559  N  N   . SER A 1 1044 ? 72.204 47.965  -8.595  1.00 19.52 ? 1044 SER A N   1 
ATOM   8560  C  CA  . SER A 1 1044 ? 73.438 48.131  -7.866  1.00 22.44 ? 1044 SER A CA  1 
ATOM   8561  C  C   . SER A 1 1044 ? 74.037 49.507  -8.189  1.00 23.25 ? 1044 SER A C   1 
ATOM   8562  O  O   . SER A 1 1044 ? 74.187 49.842  -9.339  1.00 23.92 ? 1044 SER A O   1 
ATOM   8563  C  CB  . SER A 1 1044 ? 74.403 46.992  -8.205  1.00 23.15 ? 1044 SER A CB  1 
ATOM   8564  O  OG  . SER A 1 1044 ? 73.901 46.168  -9.252  1.00 27.23 ? 1044 SER A OG  1 
ATOM   8565  N  N   . SER A 1 1045 ? 74.346 50.293  -7.157  1.00 24.56 ? 1045 SER A N   1 
ATOM   8566  C  CA  . SER A 1 1045 ? 74.815 51.671  -7.333  1.00 25.53 ? 1045 SER A CA  1 
ATOM   8567  C  C   . SER A 1 1045 ? 76.096 51.993  -6.571  1.00 26.68 ? 1045 SER A C   1 
ATOM   8568  O  O   . SER A 1 1045 ? 76.763 52.965  -6.887  1.00 27.51 ? 1045 SER A O   1 
ATOM   8569  C  CB  . SER A 1 1045 ? 73.734 52.694  -6.982  1.00 25.31 ? 1045 SER A CB  1 
ATOM   8570  O  OG  . SER A 1 1045 ? 73.690 52.984  -5.609  1.00 24.89 ? 1045 SER A OG  1 
HETATM 8571  C  C1  . NAG B 2 .    ? 58.100 44.816  12.795  1.00 26.58 ? 1046 NAG A C1  1 
HETATM 8572  C  C2  . NAG B 2 .    ? 59.145 44.493  13.850  1.00 33.03 ? 1046 NAG A C2  1 
HETATM 8573  C  C3  . NAG B 2 .    ? 59.694 43.099  13.692  1.00 38.25 ? 1046 NAG A C3  1 
HETATM 8574  C  C4  . NAG B 2 .    ? 58.554 42.184  14.078  1.00 46.11 ? 1046 NAG A C4  1 
HETATM 8575  C  C5  . NAG B 2 .    ? 57.288 42.623  13.337  1.00 44.63 ? 1046 NAG A C5  1 
HETATM 8576  C  C6  . NAG B 2 .    ? 57.177 42.022  11.957  1.00 53.75 ? 1046 NAG A C6  1 
HETATM 8577  C  C7  . NAG B 2 .    ? 60.530 46.054  14.987  1.00 49.69 ? 1046 NAG A C7  1 
HETATM 8578  C  C8  . NAG B 2 .    ? 59.799 45.522  16.227  1.00 51.28 ? 1046 NAG A C8  1 
HETATM 8579  N  N2  . NAG B 2 .    ? 60.192 45.479  13.859  1.00 42.52 ? 1046 NAG A N2  1 
HETATM 8580  O  O3  . NAG B 2 .    ? 60.776 42.967  14.612  1.00 57.93 ? 1046 NAG A O3  1 
HETATM 8581  O  O4  . NAG B 2 .    ? 58.861 40.807  13.802  1.00 56.49 ? 1046 NAG A O4  1 
HETATM 8582  O  O5  . NAG B 2 .    ? 57.007 44.068  13.230  1.00 36.51 ? 1046 NAG A O5  1 
HETATM 8583  O  O6  . NAG B 2 .    ? 55.816 42.100  11.546  1.00 71.81 ? 1046 NAG A O6  1 
HETATM 8584  O  O7  . NAG B 2 .    ? 61.356 46.955  15.054  1.00 66.78 ? 1046 NAG A O7  1 
HETATM 8585  ZN ZN  . ZN  C 3 .    ? 34.643 63.904  7.901   1.00 8.23  ? 1047 ZN  A ZN  1 
HETATM 8586  C  C1  . MPD D 4 .    ? 16.699 62.412  10.235  1.00 20.36 ? 1048 MPD A C1  1 
HETATM 8587  C  C2  . MPD D 4 .    ? 16.224 60.980  10.507  1.00 18.36 ? 1048 MPD A C2  1 
HETATM 8588  O  O2  . MPD D 4 .    ? 14.815 60.941  10.164  1.00 17.35 ? 1048 MPD A O2  1 
HETATM 8589  C  CM  . MPD D 4 .    ? 16.892 59.994  9.562   1.00 18.53 ? 1048 MPD A CM  1 
HETATM 8590  C  C3  . MPD D 4 .    ? 16.198 60.485  11.958  1.00 17.15 ? 1048 MPD A C3  1 
HETATM 8591  C  C4  . MPD D 4 .    ? 17.191 60.752  13.111  1.00 22.95 ? 1048 MPD A C4  1 
HETATM 8592  O  O4  . MPD D 4 .    ? 17.577 59.520  13.741  1.00 12.17 ? 1048 MPD A O4  1 
HETATM 8593  C  C5  . MPD D 4 .    ? 18.366 61.704  12.922  1.00 20.68 ? 1048 MPD A C5  1 
HETATM 8594  C  C1  . MPD E 4 .    ? 54.178 78.392  -12.278 1.00 38.09 ? 1049 MPD A C1  1 
HETATM 8595  C  C2  . MPD E 4 .    ? 53.599 77.258  -11.437 1.00 38.24 ? 1049 MPD A C2  1 
HETATM 8596  O  O2  . MPD E 4 .    ? 54.624 76.749  -10.540 1.00 37.14 ? 1049 MPD A O2  1 
HETATM 8597  C  CM  . MPD E 4 .    ? 52.451 77.796  -10.597 1.00 37.55 ? 1049 MPD A CM  1 
HETATM 8598  C  C3  . MPD E 4 .    ? 53.123 76.077  -12.282 1.00 38.11 ? 1049 MPD A C3  1 
HETATM 8599  C  C4  . MPD E 4 .    ? 52.306 76.482  -13.507 1.00 38.63 ? 1049 MPD A C4  1 
HETATM 8600  O  O4  . MPD E 4 .    ? 53.139 76.424  -14.648 1.00 39.00 ? 1049 MPD A O4  1 
HETATM 8601  C  C5  . MPD E 4 .    ? 51.092 75.576  -13.666 1.00 36.63 ? 1049 MPD A C5  1 
HETATM 8602  C  C1  . MPD F 4 .    ? 25.672 84.923  5.260   1.00 35.21 ? 1050 MPD A C1  1 
HETATM 8603  C  C2  . MPD F 4 .    ? 26.905 85.797  5.050   1.00 35.89 ? 1050 MPD A C2  1 
HETATM 8604  O  O2  . MPD F 4 .    ? 27.881 85.404  6.057   1.00 36.31 ? 1050 MPD A O2  1 
HETATM 8605  C  CM  . MPD F 4 .    ? 27.489 85.550  3.658   1.00 35.81 ? 1050 MPD A CM  1 
HETATM 8606  C  C3  . MPD F 4 .    ? 26.600 87.276  5.288   1.00 33.88 ? 1050 MPD A C3  1 
HETATM 8607  C  C4  . MPD F 4 .    ? 25.909 87.986  4.129   1.00 32.10 ? 1050 MPD A C4  1 
HETATM 8608  O  O4  . MPD F 4 .    ? 24.576 87.523  4.015   1.00 31.96 ? 1050 MPD A O4  1 
HETATM 8609  C  C5  . MPD F 4 .    ? 25.907 89.483  4.394   1.00 30.26 ? 1050 MPD A C5  1 
HETATM 8610  O  O   . HOH G 5 .    ? 33.764 65.900  7.339   1.00 19.92 ? 1051 HOH A O   1 
HETATM 8611  O  O   . HOH G 5 .    ? 31.623 67.415  5.939   1.00 12.26 ? 1052 HOH A O   1 
HETATM 8612  O  O   . HOH G 5 .    ? 32.548 65.310  10.068  1.00 22.84 ? 1053 HOH A O   1 
HETATM 8613  O  O   . HOH G 5 .    ? 30.826 64.038  9.113   1.00 16.88 ? 1054 HOH A O   1 
HETATM 8614  O  O   . HOH G 5 .    ? 30.186 65.263  6.877   1.00 24.53 ? 1055 HOH A O   1 
HETATM 8615  O  O   . HOH G 5 .    ? 27.849 66.551  7.751   1.00 23.83 ? 1056 HOH A O   1 
HETATM 8616  O  O   . HOH G 5 .    ? 26.072 64.790  8.296   1.00 25.17 ? 1057 HOH A O   1 
HETATM 8617  O  O   . HOH G 5 .    ? 24.180 63.306  7.340   1.00 10.67 ? 1058 HOH A O   1 
HETATM 8618  O  O   . HOH G 5 .    ? 24.643 61.249  9.016   1.00 13.12 ? 1059 HOH A O   1 
HETATM 8619  O  O   . HOH G 5 .    ? 27.154 61.045  10.126  1.00 26.84 ? 1060 HOH A O   1 
HETATM 8620  O  O   . HOH G 5 .    ? 27.259 59.262  8.321   1.00 26.54 ? 1061 HOH A O   1 
HETATM 8621  O  O   . HOH G 5 .    ? 23.810 57.978  6.231   1.00 10.98 ? 1062 HOH A O   1 
HETATM 8622  O  O   . HOH G 5 .    ? 21.684 56.994  4.986   1.00 11.53 ? 1063 HOH A O   1 
HETATM 8623  O  O   . HOH G 5 .    ? 20.085 55.876  7.086   1.00 9.85  ? 1064 HOH A O   1 
HETATM 8624  O  O   . HOH G 5 .    ? 17.575 52.638  6.257   1.00 8.21  ? 1065 HOH A O   1 
HETATM 8625  O  O   . HOH G 5 .    ? 19.321 53.421  8.123   1.00 8.26  ? 1066 HOH A O   1 
HETATM 8626  O  O   . HOH G 5 .    ? 20.088 54.636  16.059  1.00 9.32  ? 1067 HOH A O   1 
HETATM 8627  O  O   . HOH G 5 .    ? 18.295 54.765  14.060  1.00 9.28  ? 1068 HOH A O   1 
HETATM 8628  O  O   . HOH G 5 .    ? 19.308 55.095  11.466  1.00 11.40 ? 1069 HOH A O   1 
HETATM 8629  O  O   . HOH G 5 .    ? 17.019 56.134  10.187  1.00 9.49  ? 1070 HOH A O   1 
HETATM 8630  O  O   . HOH G 5 .    ? 16.666 56.920  12.917  1.00 10.61 ? 1071 HOH A O   1 
HETATM 8631  O  O   . HOH G 5 .    ? 15.438 60.222  15.376  1.00 11.99 ? 1072 HOH A O   1 
HETATM 8632  O  O   . HOH G 5 .    ? 13.768 62.231  14.566  1.00 21.77 ? 1073 HOH A O   1 
HETATM 8633  O  O   . HOH G 5 .    ? 11.468 61.651  15.966  1.00 32.22 ? 1074 HOH A O   1 
HETATM 8634  O  O   . HOH G 5 .    ? 8.627  61.369  18.922  1.00 42.55 ? 1075 HOH A O   1 
HETATM 8635  O  O   . HOH G 5 .    ? 11.864 62.193  23.250  1.00 36.42 ? 1076 HOH A O   1 
HETATM 8636  O  O   . HOH G 5 .    ? 12.117 60.745  20.293  1.00 34.97 ? 1077 HOH A O   1 
HETATM 8637  O  O   . HOH G 5 .    ? 11.489 58.223  19.966  1.00 28.40 ? 1078 HOH A O   1 
HETATM 8638  O  O   . HOH G 5 .    ? 13.884 57.501  18.923  1.00 16.90 ? 1079 HOH A O   1 
HETATM 8639  O  O   . HOH G 5 .    ? 13.931 58.076  16.244  1.00 12.33 ? 1080 HOH A O   1 
HETATM 8640  O  O   . HOH G 5 .    ? 11.338 58.536  16.070  1.00 27.80 ? 1081 HOH A O   1 
HETATM 8641  O  O   . HOH G 5 .    ? 28.524 63.593  10.292  1.00 36.50 ? 1082 HOH A O   1 
HETATM 8642  O  O   . HOH G 5 .    ? 29.414 65.323  12.214  1.00 35.04 ? 1083 HOH A O   1 
HETATM 8643  O  O   . HOH G 5 .    ? 28.542 68.900  12.338  1.00 32.97 ? 1084 HOH A O   1 
HETATM 8644  O  O   . HOH G 5 .    ? 29.705 71.831  12.140  1.00 19.43 ? 1085 HOH A O   1 
HETATM 8645  O  O   . HOH G 5 .    ? 31.858 70.725  13.371  1.00 24.51 ? 1086 HOH A O   1 
HETATM 8646  O  O   . HOH G 5 .    ? 31.006 68.068  13.940  1.00 24.04 ? 1087 HOH A O   1 
HETATM 8647  O  O   . HOH G 5 .    ? 29.228 66.851  15.492  1.00 35.82 ? 1088 HOH A O   1 
HETATM 8648  O  O   . HOH G 5 .    ? 29.848 66.824  18.016  1.00 27.14 ? 1089 HOH A O   1 
HETATM 8649  O  O   . HOH G 5 .    ? 31.873 65.473  18.949  1.00 14.67 ? 1090 HOH A O   1 
HETATM 8650  O  O   . HOH G 5 .    ? 33.413 68.466  17.000  1.00 34.81 ? 1091 HOH A O   1 
HETATM 8651  O  O   . HOH G 5 .    ? 35.269 70.784  16.013  1.00 43.53 ? 1092 HOH A O   1 
HETATM 8652  O  O   . HOH G 5 .    ? 35.371 73.366  15.209  1.00 37.07 ? 1093 HOH A O   1 
HETATM 8653  O  O   . HOH G 5 .    ? 34.962 76.217  14.933  1.00 34.72 ? 1094 HOH A O   1 
HETATM 8654  O  O   . HOH G 5 .    ? 22.844 48.903  -36.303 1.00 30.85 ? 1095 HOH A O   1 
HETATM 8655  O  O   . HOH G 5 .    ? 21.798 47.156  -34.727 1.00 30.45 ? 1096 HOH A O   1 
HETATM 8656  O  O   . HOH G 5 .    ? 20.534 50.966  -37.948 1.00 28.54 ? 1097 HOH A O   1 
HETATM 8657  O  O   . HOH G 5 .    ? 20.985 55.167  -35.936 1.00 30.44 ? 1098 HOH A O   1 
HETATM 8658  O  O   . HOH G 5 .    ? 19.662 54.929  -33.540 1.00 33.64 ? 1099 HOH A O   1 
HETATM 8659  O  O   . HOH G 5 .    ? 19.168 57.708  -32.905 1.00 32.50 ? 1100 HOH A O   1 
HETATM 8660  O  O   . HOH G 5 .    ? 20.843 58.999  -34.512 1.00 16.11 ? 1101 HOH A O   1 
HETATM 8661  O  O   . HOH G 5 .    ? 22.222 61.302  -35.034 1.00 28.38 ? 1102 HOH A O   1 
HETATM 8662  O  O   . HOH G 5 .    ? 22.724 63.196  -33.139 1.00 15.38 ? 1103 HOH A O   1 
HETATM 8663  O  O   . HOH G 5 .    ? 24.917 59.271  -36.270 1.00 34.85 ? 1104 HOH A O   1 
HETATM 8664  O  O   . HOH G 5 .    ? 26.224 58.936  -38.974 1.00 41.29 ? 1105 HOH A O   1 
HETATM 8665  O  O   . HOH G 5 .    ? 28.609 59.791  -39.157 1.00 29.98 ? 1106 HOH A O   1 
HETATM 8666  O  O   . HOH G 5 .    ? 29.142 62.140  -39.763 1.00 19.95 ? 1107 HOH A O   1 
HETATM 8667  O  O   . HOH G 5 .    ? 31.336 58.325  -40.234 1.00 31.33 ? 1108 HOH A O   1 
HETATM 8668  O  O   . HOH G 5 .    ? 33.717 57.604  -38.999 1.00 34.35 ? 1109 HOH A O   1 
HETATM 8669  O  O   . HOH G 5 .    ? 33.691 56.993  -35.900 1.00 16.63 ? 1110 HOH A O   1 
HETATM 8670  O  O   . HOH G 5 .    ? 34.857 59.338  -34.869 1.00 17.61 ? 1111 HOH A O   1 
HETATM 8671  O  O   . HOH G 5 .    ? 37.035 58.775  -33.259 1.00 23.95 ? 1112 HOH A O   1 
HETATM 8672  O  O   . HOH G 5 .    ? 39.354 58.367  -34.535 1.00 34.80 ? 1113 HOH A O   1 
HETATM 8673  O  O   . HOH G 5 .    ? 40.835 56.010  -33.248 1.00 25.27 ? 1114 HOH A O   1 
HETATM 8674  O  O   . HOH G 5 .    ? 38.778 55.135  -31.676 1.00 17.67 ? 1115 HOH A O   1 
HETATM 8675  O  O   . HOH G 5 .    ? 36.987 52.616  -32.177 1.00 38.30 ? 1116 HOH A O   1 
HETATM 8676  O  O   . HOH G 5 .    ? 34.650 53.760  -33.014 1.00 34.99 ? 1117 HOH A O   1 
HETATM 8677  O  O   . HOH G 5 .    ? 35.665 55.270  -34.712 1.00 34.49 ? 1118 HOH A O   1 
HETATM 8678  O  O   . HOH G 5 .    ? 35.747 59.724  -37.726 1.00 34.95 ? 1119 HOH A O   1 
HETATM 8679  O  O   . HOH G 5 .    ? 36.551 62.584  -38.276 1.00 29.60 ? 1120 HOH A O   1 
HETATM 8680  O  O   A HOH G 5 .    ? 36.269 63.455  -33.909 0.50 24.28 ? 1121 HOH A O   1 
HETATM 8681  O  O   B HOH G 5 .    ? 35.253 62.385  -33.129 0.50 19.99 ? 1121 HOH A O   1 
HETATM 8682  O  O   . HOH G 5 .    ? 34.056 64.340  -32.291 1.00 13.61 ? 1122 HOH A O   1 
HETATM 8683  O  O   . HOH G 5 .    ? 37.667 61.343  -32.432 1.00 22.78 ? 1123 HOH A O   1 
HETATM 8684  O  O   . HOH G 5 .    ? 40.351 62.381  -31.971 1.00 18.69 ? 1124 HOH A O   1 
HETATM 8685  O  O   . HOH G 5 .    ? 42.395 62.137  -34.028 1.00 40.08 ? 1125 HOH A O   1 
HETATM 8686  O  O   . HOH G 5 .    ? 42.967 64.098  -31.401 1.00 37.55 ? 1126 HOH A O   1 
HETATM 8687  O  O   . HOH G 5 .    ? 43.442 66.654  -31.958 1.00 26.03 ? 1127 HOH A O   1 
HETATM 8688  O  O   . HOH G 5 .    ? 41.219 68.251  -32.516 1.00 15.47 ? 1128 HOH A O   1 
HETATM 8689  O  O   . HOH G 5 .    ? 42.621 68.856  -29.850 1.00 34.23 ? 1129 HOH A O   1 
HETATM 8690  O  O   . HOH G 5 .    ? 45.777 68.002  -27.093 1.00 25.33 ? 1130 HOH A O   1 
HETATM 8691  O  O   . HOH G 5 .    ? 45.595 65.972  -28.561 1.00 33.26 ? 1131 HOH A O   1 
HETATM 8692  O  O   . HOH G 5 .    ? 48.147 64.344  -28.488 1.00 23.53 ? 1132 HOH A O   1 
HETATM 8693  O  O   . HOH G 5 .    ? 46.192 62.706  -28.223 1.00 26.10 ? 1133 HOH A O   1 
HETATM 8694  O  O   . HOH G 5 .    ? 43.582 63.008  -28.606 1.00 22.29 ? 1134 HOH A O   1 
HETATM 8695  O  O   . HOH G 5 .    ? 41.732 61.184  -29.698 1.00 16.67 ? 1135 HOH A O   1 
HETATM 8696  O  O   . HOH G 5 .    ? 42.998 59.466  -31.459 1.00 23.25 ? 1136 HOH A O   1 
HETATM 8697  O  O   . HOH G 5 .    ? 42.945 56.662  -31.441 1.00 22.11 ? 1137 HOH A O   1 
HETATM 8698  O  O   . HOH G 5 .    ? 45.568 56.317  -32.516 1.00 43.02 ? 1138 HOH A O   1 
HETATM 8699  O  O   . HOH G 5 .    ? 47.638 57.898  -32.278 1.00 39.38 ? 1139 HOH A O   1 
HETATM 8700  O  O   . HOH G 5 .    ? 49.041 59.362  -28.456 1.00 35.47 ? 1140 HOH A O   1 
HETATM 8701  O  O   . HOH G 5 .    ? 47.906 59.248  -25.572 1.00 14.22 ? 1141 HOH A O   1 
HETATM 8702  O  O   . HOH G 5 .    ? 46.815 61.811  -25.677 1.00 20.06 ? 1142 HOH A O   1 
HETATM 8703  O  O   . HOH G 5 .    ? 48.265 64.996  -25.575 1.00 33.44 ? 1143 HOH A O   1 
HETATM 8704  O  O   . HOH G 5 .    ? 47.040 68.125  -24.432 1.00 21.68 ? 1144 HOH A O   1 
HETATM 8705  O  O   . HOH G 5 .    ? 47.256 70.916  -24.390 1.00 31.46 ? 1145 HOH A O   1 
HETATM 8706  O  O   . HOH G 5 .    ? 48.393 72.366  -26.247 1.00 32.83 ? 1146 HOH A O   1 
HETATM 8707  O  O   . HOH G 5 .    ? 50.296 73.920  -25.388 1.00 24.06 ? 1147 HOH A O   1 
HETATM 8708  O  O   . HOH G 5 .    ? 47.120 74.870  -25.484 1.00 41.17 ? 1148 HOH A O   1 
HETATM 8709  O  O   . HOH G 5 .    ? 46.325 77.512  -26.086 1.00 32.99 ? 1149 HOH A O   1 
HETATM 8710  O  O   . HOH G 5 .    ? 46.699 80.421  -22.747 1.00 33.46 ? 1150 HOH A O   1 
HETATM 8711  O  O   . HOH G 5 .    ? 45.929 82.398  -26.096 1.00 42.15 ? 1151 HOH A O   1 
HETATM 8712  O  O   . HOH G 5 .    ? 44.349 83.668  -27.754 1.00 26.25 ? 1152 HOH A O   1 
HETATM 8713  O  O   . HOH G 5 .    ? 44.718 82.513  -30.786 1.00 25.62 ? 1153 HOH A O   1 
HETATM 8714  O  O   . HOH G 5 .    ? 42.464 79.691  -31.681 1.00 36.99 ? 1154 HOH A O   1 
HETATM 8715  O  O   . HOH G 5 .    ? 44.544 79.190  -33.349 1.00 24.71 ? 1155 HOH A O   1 
HETATM 8716  O  O   . HOH G 5 .    ? 42.779 79.844  -28.291 1.00 43.12 ? 1156 HOH A O   1 
HETATM 8717  O  O   . HOH G 5 .    ? 41.270 82.664  -28.960 1.00 35.54 ? 1157 HOH A O   1 
HETATM 8718  O  O   . HOH G 5 .    ? 40.547 82.903  -31.272 1.00 22.24 ? 1158 HOH A O   1 
HETATM 8719  O  O   . HOH G 5 .    ? 38.163 81.662  -31.391 1.00 11.69 ? 1159 HOH A O   1 
HETATM 8720  O  O   . HOH G 5 .    ? 39.068 83.209  -27.479 1.00 22.06 ? 1160 HOH A O   1 
HETATM 8721  O  O   . HOH G 5 .    ? 41.350 83.352  -26.411 1.00 26.83 ? 1161 HOH A O   1 
HETATM 8722  O  O   . HOH G 5 .    ? 40.384 85.790  -22.211 1.00 26.88 ? 1162 HOH A O   1 
HETATM 8723  O  O   . HOH G 5 .    ? 42.517 86.475  -20.964 1.00 34.71 ? 1163 HOH A O   1 
HETATM 8724  O  O   . HOH G 5 .    ? 47.164 84.376  -18.756 1.00 36.65 ? 1164 HOH A O   1 
HETATM 8725  O  O   . HOH G 5 .    ? 47.391 79.699  -18.197 1.00 19.57 ? 1165 HOH A O   1 
HETATM 8726  O  O   . HOH G 5 .    ? 50.484 79.081  -15.510 1.00 23.62 ? 1166 HOH A O   1 
HETATM 8727  O  O   . HOH G 5 .    ? 52.238 79.124  -17.603 1.00 22.38 ? 1167 HOH A O   1 
HETATM 8728  O  O   . HOH G 5 .    ? 54.061 80.501  -19.005 1.00 36.87 ? 1168 HOH A O   1 
HETATM 8729  O  O   . HOH G 5 .    ? 57.002 80.049  -18.168 1.00 29.65 ? 1169 HOH A O   1 
HETATM 8730  O  O   . HOH G 5 .    ? 56.169 78.815  -14.605 1.00 23.33 ? 1170 HOH A O   1 
HETATM 8731  O  O   . HOH G 5 .    ? 56.923 80.054  -11.185 1.00 29.91 ? 1171 HOH A O   1 
HETATM 8732  O  O   . HOH G 5 .    ? 60.648 80.088  -12.109 1.00 31.97 ? 1172 HOH A O   1 
HETATM 8733  O  O   . HOH G 5 .    ? 61.320 77.432  -12.780 1.00 18.41 ? 1173 HOH A O   1 
HETATM 8734  O  O   . HOH G 5 .    ? 61.709 76.374  -10.377 1.00 14.80 ? 1174 HOH A O   1 
HETATM 8735  O  O   . HOH G 5 .    ? 59.421 76.542  -8.859  1.00 12.03 ? 1175 HOH A O   1 
HETATM 8736  O  O   . HOH G 5 .    ? 65.226 79.792  -8.820  1.00 25.49 ? 1176 HOH A O   1 
HETATM 8737  O  O   . HOH G 5 .    ? 65.307 78.554  -5.657  1.00 28.08 ? 1177 HOH A O   1 
HETATM 8738  O  O   . HOH G 5 .    ? 65.101 76.742  -3.729  1.00 32.80 ? 1178 HOH A O   1 
HETATM 8739  O  O   . HOH G 5 .    ? 66.845 74.113  -4.310  1.00 24.12 ? 1179 HOH A O   1 
HETATM 8740  O  O   . HOH G 5 .    ? 69.147 73.864  -3.297  1.00 37.13 ? 1180 HOH A O   1 
HETATM 8741  O  O   . HOH G 5 .    ? 70.728 73.264  -1.727  1.00 34.41 ? 1181 HOH A O   1 
HETATM 8742  O  O   . HOH G 5 .    ? 73.701 73.986  -5.693  1.00 24.94 ? 1182 HOH A O   1 
HETATM 8743  O  O   . HOH G 5 .    ? 75.648 72.142  -5.864  1.00 37.83 ? 1183 HOH A O   1 
HETATM 8744  O  O   . HOH G 5 .    ? 75.415 76.120  -5.791  1.00 40.94 ? 1184 HOH A O   1 
HETATM 8745  O  O   . HOH G 5 .    ? 73.664 81.021  -3.977  1.00 27.75 ? 1185 HOH A O   1 
HETATM 8746  O  O   . HOH G 5 .    ? 71.476 80.506  -4.684  1.00 46.92 ? 1186 HOH A O   1 
HETATM 8747  O  O   . HOH G 5 .    ? 70.519 83.223  -10.079 1.00 37.67 ? 1187 HOH A O   1 
HETATM 8748  O  O   . HOH G 5 .    ? 67.988 82.777  -9.870  1.00 33.56 ? 1188 HOH A O   1 
HETATM 8749  O  O   . HOH G 5 .    ? 66.839 81.434  -11.336 1.00 30.93 ? 1189 HOH A O   1 
HETATM 8750  O  O   . HOH G 5 .    ? 66.266 81.756  -14.237 1.00 26.65 ? 1190 HOH A O   1 
HETATM 8751  O  O   . HOH G 5 .    ? 63.446 81.924  -14.373 1.00 38.11 ? 1191 HOH A O   1 
HETATM 8752  O  O   . HOH G 5 .    ? 62.544 82.612  -16.935 1.00 39.41 ? 1192 HOH A O   1 
HETATM 8753  O  O   . HOH G 5 .    ? 61.837 80.707  -18.781 1.00 21.53 ? 1193 HOH A O   1 
HETATM 8754  O  O   . HOH G 5 .    ? 62.684 82.884  -20.536 1.00 42.34 ? 1194 HOH A O   1 
HETATM 8755  O  O   . HOH G 5 .    ? 62.069 85.446  -22.864 1.00 25.57 ? 1195 HOH A O   1 
HETATM 8756  O  O   . HOH G 5 .    ? 62.387 87.267  -20.872 1.00 37.72 ? 1196 HOH A O   1 
HETATM 8757  O  O   . HOH G 5 .    ? 63.964 89.463  -22.207 1.00 23.68 ? 1197 HOH A O   1 
HETATM 8758  O  O   . HOH G 5 .    ? 65.057 87.949  -24.169 1.00 22.43 ? 1198 HOH A O   1 
HETATM 8759  O  O   . HOH G 5 .    ? 67.514 88.045  -23.430 1.00 24.77 ? 1199 HOH A O   1 
HETATM 8760  O  O   . HOH G 5 .    ? 66.409 89.147  -21.010 1.00 33.21 ? 1200 HOH A O   1 
HETATM 8761  O  O   . HOH G 5 .    ? 66.598 84.558  -22.179 1.00 26.79 ? 1201 HOH A O   1 
HETATM 8762  O  O   . HOH G 5 .    ? 67.649 81.700  -25.592 1.00 12.33 ? 1202 HOH A O   1 
HETATM 8763  O  O   . HOH G 5 .    ? 67.579 78.963  -25.258 1.00 12.63 ? 1203 HOH A O   1 
HETATM 8764  O  O   . HOH G 5 .    ? 70.255 78.046  -25.854 1.00 23.91 ? 1204 HOH A O   1 
HETATM 8765  O  O   . HOH G 5 .    ? 72.410 75.988  -27.070 1.00 39.54 ? 1205 HOH A O   1 
HETATM 8766  O  O   . HOH G 5 .    ? 71.494 73.905  -28.978 1.00 26.36 ? 1206 HOH A O   1 
HETATM 8767  O  O   . HOH G 5 .    ? 72.723 71.335  -29.677 1.00 41.13 ? 1207 HOH A O   1 
HETATM 8768  O  O   . HOH G 5 .    ? 71.707 69.237  -31.325 1.00 38.95 ? 1208 HOH A O   1 
HETATM 8769  O  O   . HOH G 5 .    ? 71.356 69.698  -35.077 1.00 34.60 ? 1209 HOH A O   1 
HETATM 8770  O  O   . HOH G 5 .    ? 70.925 72.150  -34.298 1.00 41.12 ? 1210 HOH A O   1 
HETATM 8771  O  O   . HOH G 5 .    ? 68.322 72.842  -33.747 1.00 34.14 ? 1211 HOH A O   1 
HETATM 8772  O  O   . HOH G 5 .    ? 67.853 75.105  -35.064 1.00 24.32 ? 1212 HOH A O   1 
HETATM 8773  O  O   . HOH G 5 .    ? 68.965 77.024  -34.246 1.00 27.71 ? 1213 HOH A O   1 
HETATM 8774  O  O   . HOH G 5 .    ? 68.245 79.503  -34.665 1.00 26.67 ? 1214 HOH A O   1 
HETATM 8775  O  O   . HOH G 5 .    ? 68.445 79.574  -37.403 1.00 34.36 ? 1215 HOH A O   1 
HETATM 8776  O  O   . HOH G 5 .    ? 67.715 77.290  -38.680 1.00 32.44 ? 1216 HOH A O   1 
HETATM 8777  O  O   . HOH G 5 .    ? 64.079 78.559  -37.720 1.00 28.68 ? 1217 HOH A O   1 
HETATM 8778  O  O   . HOH G 5 .    ? 64.246 77.879  -35.226 1.00 11.87 ? 1218 HOH A O   1 
HETATM 8779  O  O   . HOH G 5 .    ? 63.870 76.939  -40.275 1.00 33.97 ? 1219 HOH A O   1 
HETATM 8780  O  O   . HOH G 5 .    ? 61.171 76.592  -39.760 1.00 19.74 ? 1220 HOH A O   1 
HETATM 8781  O  O   . HOH G 5 .    ? 60.606 78.679  -41.435 1.00 31.66 ? 1221 HOH A O   1 
HETATM 8782  O  O   . HOH G 5 .    ? 62.833 80.576  -42.288 1.00 37.10 ? 1222 HOH A O   1 
HETATM 8783  O  O   . HOH G 5 .    ? 61.934 81.430  -44.441 1.00 36.42 ? 1223 HOH A O   1 
HETATM 8784  O  O   . HOH G 5 .    ? 61.818 83.173  -38.232 1.00 25.61 ? 1224 HOH A O   1 
HETATM 8785  O  O   . HOH G 5 .    ? 66.217 84.141  -38.691 1.00 39.03 ? 1225 HOH A O   1 
HETATM 8786  O  O   . HOH G 5 .    ? 68.283 82.256  -38.249 1.00 38.16 ? 1226 HOH A O   1 
HETATM 8787  O  O   . HOH G 5 .    ? 69.156 83.711  -35.936 1.00 23.90 ? 1227 HOH A O   1 
HETATM 8788  O  O   . HOH G 5 .    ? 69.562 81.916  -33.962 1.00 34.54 ? 1228 HOH A O   1 
HETATM 8789  O  O   . HOH G 5 .    ? 71.614 82.363  -31.937 1.00 40.17 ? 1229 HOH A O   1 
HETATM 8790  O  O   . HOH G 5 .    ? 69.838 83.079  -29.471 1.00 23.87 ? 1230 HOH A O   1 
HETATM 8791  O  O   . HOH G 5 .    ? 71.155 82.248  -27.563 1.00 40.89 ? 1231 HOH A O   1 
HETATM 8792  O  O   . HOH G 5 .    ? 68.261 79.285  -28.566 1.00 24.03 ? 1232 HOH A O   1 
HETATM 8793  O  O   . HOH G 5 .    ? 71.206 76.541  -35.784 1.00 34.94 ? 1233 HOH A O   1 
HETATM 8794  O  O   . HOH G 5 .    ? 65.870 74.627  -41.237 1.00 37.36 ? 1234 HOH A O   1 
HETATM 8795  O  O   . HOH G 5 .    ? 64.406 72.595  -45.486 1.00 42.22 ? 1235 HOH A O   1 
HETATM 8796  O  O   . HOH G 5 .    ? 63.032 74.683  -45.932 1.00 33.04 ? 1236 HOH A O   1 
HETATM 8797  O  O   . HOH G 5 .    ? 55.367 73.157  -43.467 1.00 52.39 ? 1237 HOH A O   1 
HETATM 8798  O  O   . HOH G 5 .    ? 53.271 76.694  -43.922 1.00 34.56 ? 1238 HOH A O   1 
HETATM 8799  O  O   . HOH G 5 .    ? 53.004 79.033  -44.921 1.00 47.14 ? 1239 HOH A O   1 
HETATM 8800  O  O   . HOH G 5 .    ? 50.592 80.062  -45.523 1.00 39.12 ? 1240 HOH A O   1 
HETATM 8801  O  O   . HOH G 5 .    ? 49.709 82.184  -43.880 1.00 17.25 ? 1241 HOH A O   1 
HETATM 8802  O  O   . HOH G 5 .    ? 47.263 83.936  -43.985 1.00 40.04 ? 1242 HOH A O   1 
HETATM 8803  O  O   . HOH G 5 .    ? 44.991 83.215  -43.215 1.00 40.58 ? 1243 HOH A O   1 
HETATM 8804  O  O   . HOH G 5 .    ? 46.481 80.126  -42.521 1.00 23.69 ? 1244 HOH A O   1 
HETATM 8805  O  O   . HOH G 5 .    ? 47.440 78.850  -40.490 1.00 18.93 ? 1245 HOH A O   1 
HETATM 8806  O  O   . HOH G 5 .    ? 43.772 79.903  -42.557 1.00 27.19 ? 1246 HOH A O   1 
HETATM 8807  O  O   . HOH G 5 .    ? 43.504 77.262  -43.445 1.00 37.04 ? 1247 HOH A O   1 
HETATM 8808  O  O   . HOH G 5 .    ? 42.137 74.620  -41.426 1.00 21.50 ? 1248 HOH A O   1 
HETATM 8809  O  O   . HOH G 5 .    ? 43.756 72.427  -41.946 1.00 16.96 ? 1249 HOH A O   1 
HETATM 8810  O  O   . HOH G 5 .    ? 44.564 71.974  -44.364 1.00 29.42 ? 1250 HOH A O   1 
HETATM 8811  O  O   . HOH G 5 .    ? 46.154 70.172  -39.651 1.00 26.30 ? 1251 HOH A O   1 
HETATM 8812  O  O   . HOH G 5 .    ? 48.882 69.857  -40.553 1.00 35.38 ? 1252 HOH A O   1 
HETATM 8813  O  O   . HOH G 5 .    ? 51.544 69.989  -40.451 1.00 33.69 ? 1253 HOH A O   1 
HETATM 8814  O  O   . HOH G 5 .    ? 51.579 70.076  -37.946 1.00 22.10 ? 1254 HOH A O   1 
HETATM 8815  O  O   . HOH G 5 .    ? 53.871 71.175  -36.788 1.00 11.43 ? 1255 HOH A O   1 
HETATM 8816  O  O   . HOH G 5 .    ? 55.250 69.046  -37.710 1.00 23.93 ? 1256 HOH A O   1 
HETATM 8817  O  O   . HOH G 5 .    ? 56.783 69.959  -39.704 1.00 23.18 ? 1257 HOH A O   1 
HETATM 8818  O  O   . HOH G 5 .    ? 59.890 68.593  -38.918 1.00 28.82 ? 1258 HOH A O   1 
HETATM 8819  O  O   . HOH G 5 .    ? 60.981 67.529  -36.589 1.00 33.50 ? 1259 HOH A O   1 
HETATM 8820  O  O   . HOH G 5 .    ? 59.134 67.238  -34.679 1.00 27.92 ? 1260 HOH A O   1 
HETATM 8821  O  O   . HOH G 5 .    ? 56.605 67.637  -35.421 1.00 24.39 ? 1261 HOH A O   1 
HETATM 8822  O  O   . HOH G 5 .    ? 56.081 65.229  -36.058 1.00 25.95 ? 1262 HOH A O   1 
HETATM 8823  O  O   . HOH G 5 .    ? 58.585 64.625  -36.630 1.00 33.33 ? 1263 HOH A O   1 
HETATM 8824  O  O   . HOH G 5 .    ? 53.800 64.103  -38.205 1.00 31.82 ? 1264 HOH A O   1 
HETATM 8825  O  O   . HOH G 5 .    ? 49.918 61.669  -33.952 1.00 36.71 ? 1265 HOH A O   1 
HETATM 8826  O  O   . HOH G 5 .    ? 50.469 61.086  -30.979 1.00 24.31 ? 1266 HOH A O   1 
HETATM 8827  O  O   . HOH G 5 .    ? 53.673 59.685  -32.458 1.00 30.38 ? 1267 HOH A O   1 
HETATM 8828  O  O   . HOH G 5 .    ? 55.178 58.924  -34.146 1.00 33.90 ? 1268 HOH A O   1 
HETATM 8829  O  O   . HOH G 5 .    ? 53.090 57.499  -33.656 1.00 47.01 ? 1269 HOH A O   1 
HETATM 8830  O  O   . HOH G 5 .    ? 53.315 54.974  -31.961 1.00 36.92 ? 1270 HOH A O   1 
HETATM 8831  O  O   . HOH G 5 .    ? 52.092 56.315  -30.233 1.00 20.77 ? 1271 HOH A O   1 
HETATM 8832  O  O   . HOH G 5 .    ? 49.825 55.049  -29.083 1.00 15.42 ? 1272 HOH A O   1 
HETATM 8833  O  O   . HOH G 5 .    ? 51.215 52.729  -28.632 1.00 18.32 ? 1273 HOH A O   1 
HETATM 8834  O  O   . HOH G 5 .    ? 53.499 53.211  -30.003 1.00 25.90 ? 1274 HOH A O   1 
HETATM 8835  O  O   . HOH G 5 .    ? 56.576 53.890  -32.780 1.00 45.49 ? 1275 HOH A O   1 
HETATM 8836  O  O   . HOH G 5 .    ? 58.973 54.108  -33.272 1.00 32.45 ? 1276 HOH A O   1 
HETATM 8837  O  O   . HOH G 5 .    ? 58.210 52.308  -31.664 1.00 36.91 ? 1277 HOH A O   1 
HETATM 8838  O  O   . HOH G 5 .    ? 60.088 52.817  -30.332 1.00 32.13 ? 1278 HOH A O   1 
HETATM 8839  O  O   . HOH G 5 .    ? 61.355 54.425  -28.956 1.00 21.13 ? 1279 HOH A O   1 
HETATM 8840  O  O   . HOH G 5 .    ? 62.976 50.879  -29.195 1.00 38.73 ? 1280 HOH A O   1 
HETATM 8841  O  O   . HOH G 5 .    ? 62.167 51.947  -32.163 1.00 41.07 ? 1281 HOH A O   1 
HETATM 8842  O  O   . HOH G 5 .    ? 64.745 55.347  -31.302 1.00 35.43 ? 1282 HOH A O   1 
HETATM 8843  O  O   . HOH G 5 .    ? 66.918 59.974  -27.009 1.00 23.05 ? 1283 HOH A O   1 
HETATM 8844  O  O   . HOH G 5 .    ? 67.903 58.728  -23.976 1.00 17.30 ? 1284 HOH A O   1 
HETATM 8845  O  O   . HOH G 5 .    ? 68.175 56.973  -22.115 1.00 36.66 ? 1285 HOH A O   1 
HETATM 8846  O  O   . HOH G 5 .    ? 66.525 56.204  -20.135 1.00 17.13 ? 1286 HOH A O   1 
HETATM 8847  O  O   . HOH G 5 .    ? 67.638 54.701  -18.087 1.00 25.42 ? 1287 HOH A O   1 
HETATM 8848  O  O   . HOH G 5 .    ? 69.959 53.771  -19.506 1.00 40.21 ? 1288 HOH A O   1 
HETATM 8849  O  O   . HOH G 5 .    ? 66.053 53.368  -20.379 1.00 36.13 ? 1289 HOH A O   1 
HETATM 8850  O  O   . HOH G 5 .    ? 65.010 51.942  -22.374 1.00 42.30 ? 1290 HOH A O   1 
HETATM 8851  O  O   . HOH G 5 .    ? 64.507 49.417  -21.460 1.00 39.15 ? 1291 HOH A O   1 
HETATM 8852  O  O   . HOH G 5 .    ? 62.024 48.265  -20.867 1.00 34.25 ? 1292 HOH A O   1 
HETATM 8853  O  O   . HOH G 5 .    ? 60.931 46.775  -22.377 1.00 31.68 ? 1293 HOH A O   1 
HETATM 8854  O  O   . HOH G 5 .    ? 60.888 45.608  -24.627 1.00 35.67 ? 1294 HOH A O   1 
HETATM 8855  O  O   . HOH G 5 .    ? 61.319 43.925  -22.848 1.00 40.68 ? 1295 HOH A O   1 
HETATM 8856  O  O   . HOH G 5 .    ? 62.947 42.752  -20.858 1.00 30.68 ? 1296 HOH A O   1 
HETATM 8857  O  O   . HOH G 5 .    ? 58.164 41.144  -21.475 1.00 36.10 ? 1297 HOH A O   1 
HETATM 8858  O  O   . HOH G 5 .    ? 57.176 43.086  -19.965 1.00 21.32 ? 1298 HOH A O   1 
HETATM 8859  O  O   . HOH G 5 .    ? 54.532 40.833  -20.417 1.00 35.49 ? 1299 HOH A O   1 
HETATM 8860  O  O   . HOH G 5 .    ? 54.357 38.224  -20.084 1.00 41.93 ? 1300 HOH A O   1 
HETATM 8861  O  O   . HOH G 5 .    ? 57.061 39.016  -19.283 1.00 32.04 ? 1301 HOH A O   1 
HETATM 8862  O  O   . HOH G 5 .    ? 58.310 37.322  -17.767 1.00 39.00 ? 1302 HOH A O   1 
HETATM 8863  O  O   . HOH G 5 .    ? 59.286 37.633  -15.284 1.00 24.27 ? 1303 HOH A O   1 
HETATM 8864  O  O   . HOH G 5 .    ? 57.177 36.028  -14.274 1.00 31.04 ? 1304 HOH A O   1 
HETATM 8865  O  O   . HOH G 5 .    ? 58.604 34.853  -12.276 1.00 29.76 ? 1305 HOH A O   1 
HETATM 8866  O  O   . HOH G 5 .    ? 57.719 34.262  -10.024 1.00 38.88 ? 1306 HOH A O   1 
HETATM 8867  O  O   . HOH G 5 .    ? 58.218 34.739  -6.249  1.00 30.67 ? 1307 HOH A O   1 
HETATM 8868  O  O   . HOH G 5 .    ? 55.663 34.393  -4.748  1.00 35.29 ? 1308 HOH A O   1 
HETATM 8869  O  O   . HOH G 5 .    ? 52.450 36.730  -3.015  1.00 34.33 ? 1309 HOH A O   1 
HETATM 8870  O  O   . HOH G 5 .    ? 48.768 39.227  -3.483  1.00 33.16 ? 1310 HOH A O   1 
HETATM 8871  O  O   . HOH G 5 .    ? 48.481 40.829  -1.044  1.00 25.28 ? 1311 HOH A O   1 
HETATM 8872  O  O   . HOH G 5 .    ? 47.480 42.853  -2.292  1.00 15.29 ? 1312 HOH A O   1 
HETATM 8873  O  O   . HOH G 5 .    ? 47.987 41.752  -5.286  1.00 26.64 ? 1313 HOH A O   1 
HETATM 8874  O  O   . HOH G 5 .    ? 45.471 41.465  -6.049  1.00 30.10 ? 1314 HOH A O   1 
HETATM 8875  O  O   . HOH G 5 .    ? 43.551 41.761  -7.538  1.00 23.86 ? 1315 HOH A O   1 
HETATM 8876  O  O   . HOH G 5 .    ? 45.713 42.168  -8.991  1.00 37.77 ? 1316 HOH A O   1 
HETATM 8877  O  O   . HOH G 5 .    ? 48.045 43.920  -8.546  1.00 17.18 ? 1317 HOH A O   1 
HETATM 8878  O  O   . HOH G 5 .    ? 48.777 44.181  -6.118  1.00 13.47 ? 1318 HOH A O   1 
HETATM 8879  O  O   . HOH G 5 .    ? 51.045 44.219  -7.929  1.00 9.33  ? 1319 HOH A O   1 
HETATM 8880  O  O   . HOH G 5 .    ? 49.516 41.499  -10.581 1.00 43.08 ? 1320 HOH A O   1 
HETATM 8881  O  O   . HOH G 5 .    ? 48.097 41.658  -12.524 1.00 41.50 ? 1321 HOH A O   1 
HETATM 8882  O  O   . HOH G 5 .    ? 47.467 41.248  -14.815 1.00 22.73 ? 1322 HOH A O   1 
HETATM 8883  O  O   . HOH G 5 .    ? 45.186 39.267  -14.090 1.00 39.72 ? 1323 HOH A O   1 
HETATM 8884  O  O   . HOH G 5 .    ? 42.664 39.329  -15.826 1.00 23.59 ? 1324 HOH A O   1 
HETATM 8885  O  O   . HOH G 5 .    ? 41.669 41.132  -17.620 1.00 18.52 ? 1325 HOH A O   1 
HETATM 8886  O  O   . HOH G 5 .    ? 41.008 40.692  -21.503 1.00 25.07 ? 1326 HOH A O   1 
HETATM 8887  O  O   . HOH G 5 .    ? 43.321 40.540  -22.933 1.00 30.75 ? 1327 HOH A O   1 
HETATM 8888  O  O   . HOH G 5 .    ? 43.598 42.854  -24.747 1.00 24.44 ? 1328 HOH A O   1 
HETATM 8889  O  O   . HOH G 5 .    ? 41.501 44.684  -24.245 1.00 22.26 ? 1329 HOH A O   1 
HETATM 8890  O  O   . HOH G 5 .    ? 40.128 45.380  -26.503 1.00 35.28 ? 1330 HOH A O   1 
HETATM 8891  O  O   . HOH G 5 .    ? 37.392 45.261  -25.389 1.00 20.21 ? 1331 HOH A O   1 
HETATM 8892  O  O   . HOH G 5 .    ? 35.646 45.142  -27.384 1.00 15.74 ? 1332 HOH A O   1 
HETATM 8893  O  O   . HOH G 5 .    ? 36.134 41.663  -26.736 1.00 34.45 ? 1333 HOH A O   1 
HETATM 8894  O  O   . HOH G 5 .    ? 37.141 41.166  -24.357 1.00 29.21 ? 1334 HOH A O   1 
HETATM 8895  O  O   . HOH G 5 .    ? 38.715 42.095  -22.090 1.00 22.35 ? 1335 HOH A O   1 
HETATM 8896  O  O   . HOH G 5 .    ? 43.387 46.092  -22.688 1.00 32.70 ? 1336 HOH A O   1 
HETATM 8897  O  O   . HOH G 5 .    ? 42.226 47.328  -24.548 1.00 14.52 ? 1337 HOH A O   1 
HETATM 8898  O  O   . HOH G 5 .    ? 42.810 47.299  -27.209 1.00 33.99 ? 1338 HOH A O   1 
HETATM 8899  O  O   . HOH G 5 .    ? 45.151 48.566  -27.095 1.00 72.54 ? 1339 HOH A O   1 
HETATM 8900  O  O   . HOH G 5 .    ? 41.132 48.389  -29.278 1.00 36.13 ? 1340 HOH A O   1 
HETATM 8901  O  O   . HOH G 5 .    ? 38.862 51.323  -29.794 1.00 25.75 ? 1341 HOH A O   1 
HETATM 8902  O  O   . HOH G 5 .    ? 39.514 48.583  -32.813 1.00 26.82 ? 1342 HOH A O   1 
HETATM 8903  O  O   . HOH G 5 .    ? 38.638 45.110  -33.605 1.00 25.98 ? 1343 HOH A O   1 
HETATM 8904  O  O   . HOH G 5 .    ? 42.202 45.223  -33.009 1.00 43.65 ? 1344 HOH A O   1 
HETATM 8905  O  O   . HOH G 5 .    ? 48.035 48.970  -31.196 1.00 32.13 ? 1345 HOH A O   1 
HETATM 8906  O  O   . HOH G 5 .    ? 49.091 50.680  -29.464 1.00 20.57 ? 1346 HOH A O   1 
HETATM 8907  O  O   . HOH G 5 .    ? 49.907 46.602  -30.330 1.00 34.08 ? 1347 HOH A O   1 
HETATM 8908  O  O   . HOH G 5 .    ? 52.506 45.272  -27.149 1.00 31.91 ? 1348 HOH A O   1 
HETATM 8909  O  O   . HOH G 5 .    ? 53.317 47.097  -24.990 1.00 17.21 ? 1349 HOH A O   1 
HETATM 8910  O  O   . HOH G 5 .    ? 56.318 50.026  -30.038 1.00 31.48 ? 1350 HOH A O   1 
HETATM 8911  O  O   . HOH G 5 .    ? 59.426 44.628  -30.538 1.00 34.59 ? 1351 HOH A O   1 
HETATM 8912  O  O   . HOH G 5 .    ? 58.587 43.866  -27.960 1.00 37.95 ? 1352 HOH A O   1 
HETATM 8913  O  O   . HOH G 5 .    ? 61.361 47.328  -26.702 1.00 41.87 ? 1353 HOH A O   1 
HETATM 8914  O  O   . HOH G 5 .    ? 58.648 53.785  -22.080 1.00 21.79 ? 1354 HOH A O   1 
HETATM 8915  O  O   . HOH G 5 .    ? 51.331 53.266  -23.816 1.00 12.60 ? 1355 HOH A O   1 
HETATM 8916  O  O   . HOH G 5 .    ? 48.717 54.907  -22.606 1.00 22.54 ? 1356 HOH A O   1 
HETATM 8917  O  O   . HOH G 5 .    ? 46.746 53.843  -21.211 1.00 27.05 ? 1357 HOH A O   1 
HETATM 8918  O  O   . HOH G 5 .    ? 46.005 52.708  -19.056 1.00 16.52 ? 1358 HOH A O   1 
HETATM 8919  O  O   . HOH G 5 .    ? 45.202 54.993  -18.088 1.00 24.14 ? 1359 HOH A O   1 
HETATM 8920  O  O   A HOH G 5 .    ? 42.497 54.578  -17.501 0.50 17.73 ? 1360 HOH A O   1 
HETATM 8921  O  O   B HOH G 5 .    ? 41.146 54.711  -17.172 0.50 12.69 ? 1360 HOH A O   1 
HETATM 8922  O  O   . HOH G 5 .    ? 41.089 52.192  -16.880 1.00 10.82 ? 1361 HOH A O   1 
HETATM 8923  O  O   . HOH G 5 .    ? 38.503 54.225  -17.451 1.00 28.52 ? 1362 HOH A O   1 
HETATM 8924  O  O   . HOH G 5 .    ? 37.651 56.635  -16.501 1.00 43.44 ? 1363 HOH A O   1 
HETATM 8925  O  O   A HOH G 5 .    ? 39.747 58.750  -17.986 0.50 14.42 ? 1364 HOH A O   1 
HETATM 8926  O  O   B HOH G 5 .    ? 38.609 58.425  -18.868 0.50 14.48 ? 1364 HOH A O   1 
HETATM 8927  O  O   . HOH G 5 .    ? 41.733 58.577  -15.973 1.00 17.38 ? 1365 HOH A O   1 
HETATM 8928  O  O   . HOH G 5 .    ? 44.566 58.582  -15.929 1.00 20.41 ? 1366 HOH A O   1 
HETATM 8929  O  O   . HOH G 5 .    ? 44.524 56.076  -15.350 1.00 18.16 ? 1367 HOH A O   1 
HETATM 8930  O  O   . HOH G 5 .    ? 47.312 55.662  -15.416 1.00 16.40 ? 1368 HOH A O   1 
HETATM 8931  O  O   . HOH G 5 .    ? 46.710 57.317  -18.759 1.00 13.56 ? 1369 HOH A O   1 
HETATM 8932  O  O   . HOH G 5 .    ? 45.695 59.896  -18.221 1.00 16.74 ? 1370 HOH A O   1 
HETATM 8933  O  O   . HOH G 5 .    ? 42.863 59.273  -18.679 1.00 22.56 ? 1371 HOH A O   1 
HETATM 8934  O  O   . HOH G 5 .    ? 40.339 56.073  -19.282 1.00 24.48 ? 1372 HOH A O   1 
HETATM 8935  O  O   . HOH G 5 .    ? 39.675 53.874  -20.683 1.00 13.47 ? 1373 HOH A O   1 
HETATM 8936  O  O   . HOH G 5 .    ? 37.686 52.059  -21.087 1.00 9.62  ? 1374 HOH A O   1 
HETATM 8937  O  O   . HOH G 5 .    ? 37.622 51.392  -18.557 1.00 14.54 ? 1375 HOH A O   1 
HETATM 8938  O  O   . HOH G 5 .    ? 35.190 50.518  -17.606 1.00 11.17 ? 1376 HOH A O   1 
HETATM 8939  O  O   . HOH G 5 .    ? 35.102 48.178  -16.416 1.00 22.03 ? 1377 HOH A O   1 
HETATM 8940  O  O   . HOH G 5 .    ? 33.561 48.018  -10.136 1.00 6.55  ? 1378 HOH A O   1 
HETATM 8941  O  O   . HOH G 5 .    ? 31.766 46.924  -8.096  1.00 5.67  ? 1379 HOH A O   1 
HETATM 8942  O  O   . HOH G 5 .    ? 36.710 44.809  -5.500  1.00 9.63  ? 1380 HOH A O   1 
HETATM 8943  O  O   . HOH G 5 .    ? 41.499 44.610  -6.802  1.00 13.20 ? 1381 HOH A O   1 
HETATM 8944  O  O   . HOH G 5 .    ? 42.024 40.332  -9.886  1.00 38.49 ? 1382 HOH A O   1 
HETATM 8945  O  O   . HOH G 5 .    ? 39.283 37.991  -10.870 1.00 33.52 ? 1383 HOH A O   1 
HETATM 8946  O  O   . HOH G 5 .    ? 41.112 36.375  -12.813 1.00 41.51 ? 1384 HOH A O   1 
HETATM 8947  O  O   . HOH G 5 .    ? 36.692 35.013  -15.927 1.00 30.37 ? 1385 HOH A O   1 
HETATM 8948  O  O   . HOH G 5 .    ? 37.291 35.425  -18.805 1.00 37.64 ? 1386 HOH A O   1 
HETATM 8949  O  O   . HOH G 5 .    ? 34.567 35.402  -22.353 1.00 38.78 ? 1387 HOH A O   1 
HETATM 8950  O  O   . HOH G 5 .    ? 33.559 38.913  -19.534 1.00 23.89 ? 1388 HOH A O   1 
HETATM 8951  O  O   . HOH G 5 .    ? 33.012 40.895  -17.757 1.00 19.60 ? 1389 HOH A O   1 
HETATM 8952  O  O   . HOH G 5 .    ? 35.873 39.047  -16.055 1.00 23.71 ? 1390 HOH A O   1 
HETATM 8953  O  O   . HOH G 5 .    ? 39.939 42.946  -12.736 1.00 41.38 ? 1391 HOH A O   1 
HETATM 8954  O  O   . HOH G 5 .    ? 43.147 38.255  -5.866  1.00 32.78 ? 1392 HOH A O   1 
HETATM 8955  O  O   . HOH G 5 .    ? 39.887 38.648  -3.419  1.00 23.38 ? 1393 HOH A O   1 
HETATM 8956  O  O   . HOH G 5 .    ? 38.985 36.283  -3.711  1.00 33.34 ? 1394 HOH A O   1 
HETATM 8957  O  O   . HOH G 5 .    ? 36.480 35.872  -1.984  1.00 42.37 ? 1395 HOH A O   1 
HETATM 8958  O  O   . HOH G 5 .    ? 35.996 35.960  -4.636  1.00 22.30 ? 1396 HOH A O   1 
HETATM 8959  O  O   . HOH G 5 .    ? 33.297 36.561  -4.458  1.00 14.45 ? 1397 HOH A O   1 
HETATM 8960  O  O   . HOH G 5 .    ? 32.294 39.045  -4.925  1.00 8.59  ? 1398 HOH A O   1 
HETATM 8961  O  O   . HOH G 5 .    ? 32.175 34.326  -3.202  1.00 22.43 ? 1399 HOH A O   1 
HETATM 8962  O  O   . HOH G 5 .    ? 30.165 34.061  -1.353  1.00 29.37 ? 1400 HOH A O   1 
HETATM 8963  O  O   . HOH G 5 .    ? 31.227 33.541  2.694   1.00 21.28 ? 1401 HOH A O   1 
HETATM 8964  O  O   . HOH G 5 .    ? 31.108 29.884  5.546   1.00 35.15 ? 1402 HOH A O   1 
HETATM 8965  O  O   . HOH G 5 .    ? 24.710 32.880  6.300   1.00 24.64 ? 1403 HOH A O   1 
HETATM 8966  O  O   . HOH G 5 .    ? 23.084 31.549  3.947   1.00 38.50 ? 1404 HOH A O   1 
HETATM 8967  O  O   . HOH G 5 .    ? 22.552 34.174  1.174   1.00 35.38 ? 1405 HOH A O   1 
HETATM 8968  O  O   . HOH G 5 .    ? 22.084 36.691  0.119   1.00 22.05 ? 1406 HOH A O   1 
HETATM 8969  O  O   . HOH G 5 .    ? 19.671 37.198  1.451   1.00 37.08 ? 1407 HOH A O   1 
HETATM 8970  O  O   . HOH G 5 .    ? 17.914 37.439  -0.136  1.00 35.92 ? 1408 HOH A O   1 
HETATM 8971  O  O   . HOH G 5 .    ? 18.032 39.671  -2.902  1.00 40.95 ? 1409 HOH A O   1 
HETATM 8972  O  O   . HOH G 5 .    ? 20.074 38.885  -3.664  1.00 27.51 ? 1410 HOH A O   1 
HETATM 8973  O  O   . HOH G 5 .    ? 19.752 41.421  -4.972  1.00 27.07 ? 1411 HOH A O   1 
HETATM 8974  O  O   . HOH G 5 .    ? 20.879 42.418  -7.507  1.00 23.90 ? 1412 HOH A O   1 
HETATM 8975  O  O   . HOH G 5 .    ? 19.755 40.948  -9.710  1.00 30.11 ? 1413 HOH A O   1 
HETATM 8976  O  O   . HOH G 5 .    ? 22.440 40.005  -9.639  1.00 40.00 ? 1414 HOH A O   1 
HETATM 8977  O  O   . HOH G 5 .    ? 24.120 39.069  -11.290 1.00 21.71 ? 1415 HOH A O   1 
HETATM 8978  O  O   . HOH G 5 .    ? 21.900 38.211  -12.132 1.00 38.42 ? 1416 HOH A O   1 
HETATM 8979  O  O   . HOH G 5 .    ? 19.689 39.872  -12.886 1.00 46.49 ? 1417 HOH A O   1 
HETATM 8980  O  O   . HOH G 5 .    ? 17.581 39.868  -15.283 1.00 38.08 ? 1418 HOH A O   1 
HETATM 8981  O  O   . HOH G 5 .    ? 20.168 42.144  -15.222 1.00 43.38 ? 1419 HOH A O   1 
HETATM 8982  O  O   . HOH G 5 .    ? 21.329 44.937  -15.557 1.00 39.69 ? 1420 HOH A O   1 
HETATM 8983  O  O   . HOH G 5 .    ? 21.096 46.485  -17.552 1.00 36.21 ? 1421 HOH A O   1 
HETATM 8984  O  O   . HOH G 5 .    ? 23.609 45.997  -16.012 1.00 27.05 ? 1422 HOH A O   1 
HETATM 8985  O  O   . HOH G 5 .    ? 22.989 45.189  -13.565 1.00 28.42 ? 1423 HOH A O   1 
HETATM 8986  O  O   . HOH G 5 .    ? 24.433 42.352  -14.337 1.00 19.00 ? 1424 HOH A O   1 
HETATM 8987  O  O   . HOH G 5 .    ? 26.819 41.539  -13.270 1.00 11.30 ? 1425 HOH A O   1 
HETATM 8988  O  O   . HOH G 5 .    ? 28.953 42.642  -11.960 1.00 9.05  ? 1426 HOH A O   1 
HETATM 8989  O  O   . HOH G 5 .    ? 26.331 48.818  -11.006 1.00 8.06  ? 1427 HOH A O   1 
HETATM 8990  O  O   . HOH G 5 .    ? 26.188 49.487  -13.731 1.00 7.04  ? 1428 HOH A O   1 
HETATM 8991  O  O   . HOH G 5 .    ? 24.740 52.821  -11.801 1.00 8.41  ? 1429 HOH A O   1 
HETATM 8992  O  O   . HOH G 5 .    ? 22.361 54.371  -12.039 1.00 8.13  ? 1430 HOH A O   1 
HETATM 8993  O  O   . HOH G 5 .    ? 19.715 53.399  -11.818 1.00 10.38 ? 1431 HOH A O   1 
HETATM 8994  O  O   . HOH G 5 .    ? 18.703 50.933  -12.512 1.00 10.00 ? 1432 HOH A O   1 
HETATM 8995  O  O   . HOH G 5 .    ? 19.753 46.832  -14.449 1.00 18.31 ? 1433 HOH A O   1 
HETATM 8996  O  O   . HOH G 5 .    ? 17.576 45.385  -14.314 1.00 28.27 ? 1434 HOH A O   1 
HETATM 8997  O  O   . HOH G 5 .    ? 16.236 44.601  -11.691 1.00 23.98 ? 1435 HOH A O   1 
HETATM 8998  O  O   . HOH G 5 .    ? 13.728 45.896  -12.457 1.00 33.47 ? 1436 HOH A O   1 
HETATM 8999  O  O   . HOH G 5 .    ? 11.577 45.628  -11.949 1.00 42.94 ? 1437 HOH A O   1 
HETATM 9000  O  O   . HOH G 5 .    ? 12.893 51.446  -12.105 1.00 27.18 ? 1438 HOH A O   1 
HETATM 9001  O  O   . HOH G 5 .    ? 13.157 52.052  -15.068 1.00 29.97 ? 1439 HOH A O   1 
HETATM 9002  O  O   . HOH G 5 .    ? 14.380 54.094  -16.306 1.00 16.89 ? 1440 HOH A O   1 
HETATM 9003  O  O   . HOH G 5 .    ? 12.284 55.371  -15.113 1.00 17.47 ? 1441 HOH A O   1 
HETATM 9004  O  O   . HOH G 5 .    ? 11.828 54.714  -12.377 1.00 16.78 ? 1442 HOH A O   1 
HETATM 9005  O  O   . HOH G 5 .    ? 9.344  53.804  -12.189 1.00 37.20 ? 1443 HOH A O   1 
HETATM 9006  O  O   . HOH G 5 .    ? 7.996  57.231  -11.511 1.00 43.09 ? 1444 HOH A O   1 
HETATM 9007  O  O   . HOH G 5 .    ? 7.246  56.716  -9.065  1.00 37.12 ? 1445 HOH A O   1 
HETATM 9008  O  O   A HOH G 5 .    ? 8.653  57.670  -6.934  0.50 17.38 ? 1446 HOH A O   1 
HETATM 9009  O  O   B HOH G 5 .    ? 9.938  56.892  -5.788  0.50 14.35 ? 1446 HOH A O   1 
HETATM 9010  O  O   . HOH G 5 .    ? 8.789  54.992  -6.125  1.00 28.66 ? 1447 HOH A O   1 
HETATM 9011  O  O   . HOH G 5 .    ? 10.185 58.047  -3.376  1.00 31.25 ? 1448 HOH A O   1 
HETATM 9012  O  O   . HOH G 5 .    ? 11.987 59.267  -5.008  1.00 18.81 ? 1449 HOH A O   1 
HETATM 9013  O  O   . HOH G 5 .    ? 14.186 59.569  -3.438  1.00 12.44 ? 1450 HOH A O   1 
HETATM 9014  O  O   . HOH G 5 .    ? 13.000 61.794  -2.552  1.00 27.25 ? 1451 HOH A O   1 
HETATM 9015  O  O   . HOH G 5 .    ? 11.385 62.478  -4.519  1.00 33.41 ? 1452 HOH A O   1 
HETATM 9016  O  O   . HOH G 5 .    ? 10.979 65.030  -5.491  1.00 34.65 ? 1453 HOH A O   1 
HETATM 9017  O  O   . HOH G 5 .    ? 13.158 66.575  -4.890  1.00 12.40 ? 1454 HOH A O   1 
HETATM 9018  O  O   . HOH G 5 .    ? 14.122 68.030  -7.866  1.00 18.60 ? 1455 HOH A O   1 
HETATM 9019  O  O   . HOH G 5 .    ? 13.563 69.664  -9.679  1.00 28.27 ? 1456 HOH A O   1 
HETATM 9020  O  O   . HOH G 5 .    ? 12.423 68.138  -11.538 1.00 23.74 ? 1457 HOH A O   1 
HETATM 9021  O  O   . HOH G 5 .    ? 12.782 66.835  -13.721 1.00 23.16 ? 1458 HOH A O   1 
HETATM 9022  O  O   . HOH G 5 .    ? 14.623 66.202  -15.493 1.00 19.46 ? 1459 HOH A O   1 
HETATM 9023  O  O   . HOH G 5 .    ? 14.435 63.834  -16.437 1.00 16.92 ? 1460 HOH A O   1 
HETATM 9024  O  O   . HOH G 5 .    ? 14.620 61.847  -14.490 1.00 24.54 ? 1461 HOH A O   1 
HETATM 9025  O  O   . HOH G 5 .    ? 14.296 62.636  -12.250 1.00 25.84 ? 1462 HOH A O   1 
HETATM 9026  O  O   . HOH G 5 .    ? 10.771 62.235  -11.986 1.00 30.84 ? 1463 HOH A O   1 
HETATM 9027  O  O   . HOH G 5 .    ? 10.582 64.274  -10.448 1.00 36.19 ? 1464 HOH A O   1 
HETATM 9028  O  O   . HOH G 5 .    ? 12.733 66.062  -9.866  1.00 18.25 ? 1465 HOH A O   1 
HETATM 9029  O  O   . HOH G 5 .    ? 10.323 69.956  -10.182 1.00 32.75 ? 1466 HOH A O   1 
HETATM 9030  O  O   . HOH G 5 .    ? 12.454 74.987  -13.222 1.00 25.39 ? 1467 HOH A O   1 
HETATM 9031  O  O   . HOH G 5 .    ? 15.854 75.066  -11.729 1.00 15.70 ? 1468 HOH A O   1 
HETATM 9032  O  O   . HOH G 5 .    ? 15.646 77.090  -13.725 1.00 29.94 ? 1469 HOH A O   1 
HETATM 9033  O  O   . HOH G 5 .    ? 15.297 79.604  -11.561 1.00 38.43 ? 1470 HOH A O   1 
HETATM 9034  O  O   . HOH G 5 .    ? 15.590 81.006  -9.516  1.00 49.83 ? 1471 HOH A O   1 
HETATM 9035  O  O   . HOH G 5 .    ? 17.221 80.624  -7.394  1.00 21.25 ? 1472 HOH A O   1 
HETATM 9036  O  O   . HOH G 5 .    ? 16.743 81.915  -4.976  1.00 31.16 ? 1473 HOH A O   1 
HETATM 9037  O  O   . HOH G 5 .    ? 18.047 84.255  -5.129  1.00 30.08 ? 1474 HOH A O   1 
HETATM 9038  O  O   . HOH G 5 .    ? 19.608 84.284  -1.014  1.00 39.27 ? 1475 HOH A O   1 
HETATM 9039  O  O   . HOH G 5 .    ? 21.060 86.274  -2.366  1.00 39.20 ? 1476 HOH A O   1 
HETATM 9040  O  O   . HOH G 5 .    ? 24.512 86.865  -1.035  1.00 32.38 ? 1477 HOH A O   1 
HETATM 9041  O  O   . HOH G 5 .    ? 26.334 88.117  0.796   1.00 38.67 ? 1478 HOH A O   1 
HETATM 9042  O  O   . HOH G 5 .    ? 22.628 88.967  2.789   1.00 29.22 ? 1479 HOH A O   1 
HETATM 9043  O  O   . HOH G 5 .    ? 24.704 83.827  2.510   1.00 25.82 ? 1480 HOH A O   1 
HETATM 9044  O  O   . HOH G 5 .    ? 27.311 82.134  3.151   1.00 26.25 ? 1481 HOH A O   1 
HETATM 9045  O  O   . HOH G 5 .    ? 29.773 82.977  2.416   1.00 18.09 ? 1482 HOH A O   1 
HETATM 9046  O  O   . HOH G 5 .    ? 30.679 83.235  4.787   1.00 30.61 ? 1483 HOH A O   1 
HETATM 9047  O  O   . HOH G 5 .    ? 30.164 82.576  7.071   1.00 28.73 ? 1484 HOH A O   1 
HETATM 9048  O  O   . HOH G 5 .    ? 31.990 80.334  7.237   1.00 24.35 ? 1485 HOH A O   1 
HETATM 9049  O  O   . HOH G 5 .    ? 35.895 80.908  6.322   1.00 15.48 ? 1486 HOH A O   1 
HETATM 9050  O  O   . HOH G 5 .    ? 33.555 83.661  3.326   1.00 36.22 ? 1487 HOH A O   1 
HETATM 9051  O  O   . HOH G 5 .    ? 32.639 84.202  0.379   1.00 30.50 ? 1488 HOH A O   1 
HETATM 9052  O  O   . HOH G 5 .    ? 35.329 84.870  -0.649  1.00 34.72 ? 1489 HOH A O   1 
HETATM 9053  O  O   . HOH G 5 .    ? 38.080 83.086  -1.058  1.00 26.02 ? 1490 HOH A O   1 
HETATM 9054  O  O   . HOH G 5 .    ? 37.570 80.476  -0.614  1.00 21.35 ? 1491 HOH A O   1 
HETATM 9055  O  O   . HOH G 5 .    ? 38.876 80.204  -2.976  1.00 32.56 ? 1492 HOH A O   1 
HETATM 9056  O  O   . HOH G 5 .    ? 40.942 81.847  -3.709  1.00 28.50 ? 1493 HOH A O   1 
HETATM 9057  O  O   . HOH G 5 .    ? 37.294 83.377  -4.103  1.00 26.93 ? 1494 HOH A O   1 
HETATM 9058  O  O   . HOH G 5 .    ? 36.232 79.160  -5.029  1.00 23.74 ? 1495 HOH A O   1 
HETATM 9059  O  O   . HOH G 5 .    ? 35.718 77.543  -7.357  1.00 13.10 ? 1496 HOH A O   1 
HETATM 9060  O  O   . HOH G 5 .    ? 34.513 79.024  -9.193  1.00 10.81 ? 1497 HOH A O   1 
HETATM 9061  O  O   . HOH G 5 .    ? 32.738 80.947  -11.695 1.00 9.96  ? 1498 HOH A O   1 
HETATM 9062  O  O   . HOH G 5 .    ? 33.535 83.440  -10.418 1.00 14.11 ? 1499 HOH A O   1 
HETATM 9063  O  O   . HOH G 5 .    ? 32.057 85.163  -8.624  1.00 21.83 ? 1500 HOH A O   1 
HETATM 9064  O  O   . HOH G 5 .    ? 32.853 85.242  -5.639  1.00 17.67 ? 1501 HOH A O   1 
HETATM 9065  O  O   . HOH G 5 .    ? 31.064 86.875  -2.829  1.00 29.83 ? 1502 HOH A O   1 
HETATM 9066  O  O   . HOH G 5 .    ? 26.699 87.736  -4.017  1.00 39.16 ? 1503 HOH A O   1 
HETATM 9067  O  O   . HOH G 5 .    ? 24.150 82.739  -4.144  1.00 31.99 ? 1504 HOH A O   1 
HETATM 9068  O  O   . HOH G 5 .    ? 21.296 78.385  -1.326  1.00 16.36 ? 1505 HOH A O   1 
HETATM 9069  O  O   . HOH G 5 .    ? 19.472 80.189  -1.061  1.00 34.48 ? 1506 HOH A O   1 
HETATM 9070  O  O   . HOH G 5 .    ? 16.093 80.365  -1.308  1.00 42.12 ? 1507 HOH A O   1 
HETATM 9071  O  O   . HOH G 5 .    ? 13.688 77.484  0.714   1.00 29.40 ? 1508 HOH A O   1 
HETATM 9072  O  O   . HOH G 5 .    ? 10.294 76.405  3.873   1.00 35.64 ? 1509 HOH A O   1 
HETATM 9073  O  O   . HOH G 5 .    ? 6.769  80.177  2.189   1.00 34.81 ? 1510 HOH A O   1 
HETATM 9074  O  O   . HOH G 5 .    ? 8.972  81.386  -5.284  1.00 32.65 ? 1511 HOH A O   1 
HETATM 9075  O  O   . HOH G 5 .    ? 10.559 77.206  -5.272  1.00 31.05 ? 1512 HOH A O   1 
HETATM 9076  O  O   . HOH G 5 .    ? 9.862  75.367  -3.268  1.00 32.23 ? 1513 HOH A O   1 
HETATM 9077  O  O   . HOH G 5 .    ? 12.564 70.807  -0.406  1.00 20.01 ? 1514 HOH A O   1 
HETATM 9078  O  O   . HOH G 5 .    ? 13.239 68.463  0.812   1.00 16.70 ? 1515 HOH A O   1 
HETATM 9079  O  O   . HOH G 5 .    ? 11.670 66.613  3.050   1.00 31.50 ? 1516 HOH A O   1 
HETATM 9080  O  O   . HOH G 5 .    ? 9.805  64.434  4.685   1.00 36.57 ? 1517 HOH A O   1 
HETATM 9081  O  O   . HOH G 5 .    ? 11.562 62.195  5.543   1.00 40.35 ? 1518 HOH A O   1 
HETATM 9082  O  O   . HOH G 5 .    ? 13.698 60.782  7.681   1.00 23.35 ? 1519 HOH A O   1 
HETATM 9083  O  O   . HOH G 5 .    ? 14.422 59.845  5.124   1.00 9.89  ? 1520 HOH A O   1 
HETATM 9084  O  O   . HOH G 5 .    ? 11.686 58.531  7.702   1.00 24.13 ? 1521 HOH A O   1 
HETATM 9085  O  O   . HOH G 5 .    ? 9.794  59.467  6.311   1.00 31.94 ? 1522 HOH A O   1 
HETATM 9086  O  O   . HOH G 5 .    ? 7.086  60.464  7.412   1.00 36.70 ? 1523 HOH A O   1 
HETATM 9087  O  O   . HOH G 5 .    ? 5.400  57.145  6.740   1.00 31.94 ? 1524 HOH A O   1 
HETATM 9088  O  O   . HOH G 5 .    ? 3.758  54.699  5.648   1.00 37.22 ? 1525 HOH A O   1 
HETATM 9089  O  O   . HOH G 5 .    ? 6.854  59.423  2.488   1.00 40.52 ? 1526 HOH A O   1 
HETATM 9090  O  O   . HOH G 5 .    ? 8.030  58.268  -0.231  1.00 36.03 ? 1527 HOH A O   1 
HETATM 9091  O  O   . HOH G 5 .    ? 11.133 61.044  -0.752  1.00 37.35 ? 1528 HOH A O   1 
HETATM 9092  O  O   . HOH G 5 .    ? 10.390 62.123  1.745   1.00 28.54 ? 1529 HOH A O   1 
HETATM 9093  O  O   . HOH G 5 .    ? 14.021 64.494  6.281   1.00 31.30 ? 1530 HOH A O   1 
HETATM 9094  O  O   . HOH G 5 .    ? 14.299 68.657  5.440   1.00 33.22 ? 1531 HOH A O   1 
HETATM 9095  O  O   . HOH G 5 .    ? 16.074 70.007  6.295   1.00 36.37 ? 1532 HOH A O   1 
HETATM 9096  O  O   . HOH G 5 .    ? 18.542 69.795  4.115   1.00 12.28 ? 1533 HOH A O   1 
HETATM 9097  O  O   . HOH G 5 .    ? 19.208 72.213  2.991   1.00 13.23 ? 1534 HOH A O   1 
HETATM 9098  O  O   . HOH G 5 .    ? 17.679 74.289  3.765   1.00 17.93 ? 1535 HOH A O   1 
HETATM 9099  O  O   . HOH G 5 .    ? 19.175 76.371  4.751   1.00 22.63 ? 1536 HOH A O   1 
HETATM 9100  O  O   . HOH G 5 .    ? 19.446 76.119  7.409   1.00 42.49 ? 1537 HOH A O   1 
HETATM 9101  O  O   . HOH G 5 .    ? 21.918 76.384  8.750   1.00 26.20 ? 1538 HOH A O   1 
HETATM 9102  O  O   . HOH G 5 .    ? 25.038 73.591  8.886   1.00 22.50 ? 1539 HOH A O   1 
HETATM 9103  O  O   . HOH G 5 .    ? 26.261 74.809  11.086  1.00 26.81 ? 1540 HOH A O   1 
HETATM 9104  O  O   . HOH G 5 .    ? 29.380 75.388  10.959  1.00 26.20 ? 1541 HOH A O   1 
HETATM 9105  O  O   . HOH G 5 .    ? 30.074 77.848  11.343  1.00 38.73 ? 1542 HOH A O   1 
HETATM 9106  O  O   . HOH G 5 .    ? 32.212 78.233  12.755  1.00 44.34 ? 1543 HOH A O   1 
HETATM 9107  O  O   . HOH G 5 .    ? 34.693 77.410  12.397  1.00 27.96 ? 1544 HOH A O   1 
HETATM 9108  O  O   . HOH G 5 .    ? 28.412 63.398  13.804  1.00 33.79 ? 1545 HOH A O   1 
HETATM 9109  O  O   . HOH G 5 .    ? 25.887 63.036  13.313  1.00 31.69 ? 1546 HOH A O   1 
HETATM 9110  O  O   . HOH G 5 .    ? 23.571 62.343  13.682  1.00 36.20 ? 1547 HOH A O   1 
HETATM 9111  O  O   . HOH G 5 .    ? 21.274 63.395  14.446  1.00 28.83 ? 1548 HOH A O   1 
HETATM 9112  O  O   . HOH G 5 .    ? 22.642 62.415  16.158  1.00 25.55 ? 1549 HOH A O   1 
HETATM 9113  O  O   A HOH G 5 .    ? 23.296 64.595  18.115  0.50 22.46 ? 1550 HOH A O   1 
HETATM 9114  O  O   B HOH G 5 .    ? 23.536 66.035  18.768  0.50 22.55 ? 1550 HOH A O   1 
HETATM 9115  O  O   . HOH G 5 .    ? 25.525 65.847  17.237  1.00 24.44 ? 1551 HOH A O   1 
HETATM 9116  O  O   . HOH G 5 .    ? 26.357 63.596  16.982  1.00 15.77 ? 1552 HOH A O   1 
HETATM 9117  O  O   . HOH G 5 .    ? 28.557 65.109  19.648  1.00 15.31 ? 1553 HOH A O   1 
HETATM 9118  O  O   . HOH G 5 .    ? 26.219 66.693  19.702  1.00 26.13 ? 1554 HOH A O   1 
HETATM 9119  O  O   . HOH G 5 .    ? 24.745 68.185  21.713  1.00 18.83 ? 1555 HOH A O   1 
HETATM 9120  O  O   . HOH G 5 .    ? 22.486 67.955  20.234  1.00 22.10 ? 1556 HOH A O   1 
HETATM 9121  O  O   . HOH G 5 .    ? 20.504 68.197  22.002  1.00 23.36 ? 1557 HOH A O   1 
HETATM 9122  O  O   . HOH G 5 .    ? 17.652 68.277  24.064  1.00 38.60 ? 1558 HOH A O   1 
HETATM 9123  O  O   . HOH G 5 .    ? 15.609 68.397  22.000  1.00 36.41 ? 1559 HOH A O   1 
HETATM 9124  O  O   . HOH G 5 .    ? 15.040 69.889  24.137  1.00 34.10 ? 1560 HOH A O   1 
HETATM 9125  O  O   . HOH G 5 .    ? 12.749 70.319  25.161  1.00 33.67 ? 1561 HOH A O   1 
HETATM 9126  O  O   . HOH G 5 .    ? 17.717 65.995  27.817  1.00 19.98 ? 1562 HOH A O   1 
HETATM 9127  O  O   . HOH G 5 .    ? 20.356 65.592  27.182  1.00 24.64 ? 1563 HOH A O   1 
HETATM 9128  O  O   A HOH G 5 .    ? 22.433 65.729  29.514  0.50 20.85 ? 1564 HOH A O   1 
HETATM 9129  O  O   B HOH G 5 .    ? 22.276 66.880  28.776  0.50 12.43 ? 1564 HOH A O   1 
HETATM 9130  O  O   . HOH G 5 .    ? 22.220 65.337  32.360  1.00 26.05 ? 1565 HOH A O   1 
HETATM 9131  O  O   . HOH G 5 .    ? 22.245 62.568  33.779  1.00 24.60 ? 1566 HOH A O   1 
HETATM 9132  O  O   . HOH G 5 .    ? 19.557 62.444  34.691  1.00 30.08 ? 1567 HOH A O   1 
HETATM 9133  O  O   . HOH G 5 .    ? 17.481 61.678  33.340  1.00 34.27 ? 1568 HOH A O   1 
HETATM 9134  O  O   . HOH G 5 .    ? 18.106 59.641  31.759  1.00 29.85 ? 1569 HOH A O   1 
HETATM 9135  O  O   . HOH G 5 .    ? 16.138 57.401  31.301  1.00 40.58 ? 1570 HOH A O   1 
HETATM 9136  O  O   . HOH G 5 .    ? 14.667 55.380  27.221  1.00 27.68 ? 1571 HOH A O   1 
HETATM 9137  O  O   . HOH G 5 .    ? 12.892 55.004  24.946  1.00 40.46 ? 1572 HOH A O   1 
HETATM 9138  O  O   . HOH G 5 .    ? 13.407 52.569  25.945  1.00 24.03 ? 1573 HOH A O   1 
HETATM 9139  O  O   . HOH G 5 .    ? 14.058 50.342  24.137  1.00 16.88 ? 1574 HOH A O   1 
HETATM 9140  O  O   . HOH G 5 .    ? 16.462 48.966  24.072  1.00 11.09 ? 1575 HOH A O   1 
HETATM 9141  O  O   . HOH G 5 .    ? 14.637 47.136  26.797  1.00 35.37 ? 1576 HOH A O   1 
HETATM 9142  O  O   . HOH G 5 .    ? 13.690 48.452  28.934  1.00 36.02 ? 1577 HOH A O   1 
HETATM 9143  O  O   . HOH G 5 .    ? 12.283 46.692  30.571  1.00 34.19 ? 1578 HOH A O   1 
HETATM 9144  O  O   . HOH G 5 .    ? 14.568 46.738  32.275  1.00 21.82 ? 1579 HOH A O   1 
HETATM 9145  O  O   . HOH G 5 .    ? 15.736 48.782  31.432  1.00 21.47 ? 1580 HOH A O   1 
HETATM 9146  O  O   . HOH G 5 .    ? 15.031 51.145  32.593  1.00 21.19 ? 1581 HOH A O   1 
HETATM 9147  O  O   . HOH G 5 .    ? 17.336 52.488  33.077  1.00 23.54 ? 1582 HOH A O   1 
HETATM 9148  O  O   . HOH G 5 .    ? 17.470 52.894  35.805  1.00 25.37 ? 1583 HOH A O   1 
HETATM 9149  O  O   . HOH G 5 .    ? 19.825 56.091  37.488  1.00 37.56 ? 1584 HOH A O   1 
HETATM 9150  O  O   . HOH G 5 .    ? 21.025 58.456  37.823  1.00 37.58 ? 1585 HOH A O   1 
HETATM 9151  O  O   . HOH G 5 .    ? 23.938 57.122  38.572  1.00 25.29 ? 1586 HOH A O   1 
HETATM 9152  O  O   . HOH G 5 .    ? 26.059 57.456  40.286  1.00 35.26 ? 1587 HOH A O   1 
HETATM 9153  O  O   . HOH G 5 .    ? 28.519 55.326  39.826  1.00 26.06 ? 1588 HOH A O   1 
HETATM 9154  O  O   . HOH G 5 .    ? 28.158 54.656  42.266  1.00 30.09 ? 1589 HOH A O   1 
HETATM 9155  O  O   . HOH G 5 .    ? 27.801 52.148  42.394  1.00 35.53 ? 1590 HOH A O   1 
HETATM 9156  O  O   . HOH G 5 .    ? 25.576 52.318  43.401  1.00 32.81 ? 1591 HOH A O   1 
HETATM 9157  O  O   . HOH G 5 .    ? 27.322 47.540  45.717  1.00 39.57 ? 1592 HOH A O   1 
HETATM 9158  O  O   . HOH G 5 .    ? 24.007 45.832  40.774  1.00 39.38 ? 1593 HOH A O   1 
HETATM 9159  O  O   . HOH G 5 .    ? 21.331 43.713  39.749  1.00 45.58 ? 1594 HOH A O   1 
HETATM 9160  O  O   . HOH G 5 .    ? 18.762 43.377  39.401  1.00 36.04 ? 1595 HOH A O   1 
HETATM 9161  O  O   . HOH G 5 .    ? 19.486 45.456  40.459  1.00 27.65 ? 1596 HOH A O   1 
HETATM 9162  O  O   . HOH G 5 .    ? 21.126 47.343  39.050  1.00 21.03 ? 1597 HOH A O   1 
HETATM 9163  O  O   . HOH G 5 .    ? 18.920 48.370  37.727  1.00 17.98 ? 1598 HOH A O   1 
HETATM 9164  O  O   . HOH G 5 .    ? 17.523 49.299  41.055  1.00 18.61 ? 1599 HOH A O   1 
HETATM 9165  O  O   . HOH G 5 .    ? 21.338 55.285  40.020  1.00 31.25 ? 1600 HOH A O   1 
HETATM 9166  O  O   . HOH G 5 .    ? 24.001 60.841  36.020  1.00 28.83 ? 1601 HOH A O   1 
HETATM 9167  O  O   . HOH G 5 .    ? 28.188 63.097  36.163  1.00 38.54 ? 1602 HOH A O   1 
HETATM 9168  O  O   . HOH G 5 .    ? 30.720 61.771  35.747  1.00 31.18 ? 1603 HOH A O   1 
HETATM 9169  O  O   . HOH G 5 .    ? 30.664 63.693  34.018  1.00 43.21 ? 1604 HOH A O   1 
HETATM 9170  O  O   . HOH G 5 .    ? 29.350 65.295  32.492  1.00 31.47 ? 1605 HOH A O   1 
HETATM 9171  O  O   . HOH G 5 .    ? 27.602 66.918  33.409  1.00 40.94 ? 1606 HOH A O   1 
HETATM 9172  O  O   . HOH G 5 .    ? 30.021 67.077  35.643  1.00 31.27 ? 1607 HOH A O   1 
HETATM 9173  O  O   . HOH G 5 .    ? 28.737 64.325  29.996  1.00 17.45 ? 1608 HOH A O   1 
HETATM 9174  O  O   . HOH G 5 .    ? 27.647 67.547  28.046  1.00 15.52 ? 1609 HOH A O   1 
HETATM 9175  O  O   . HOH G 5 .    ? 22.871 69.421  28.632  1.00 34.72 ? 1610 HOH A O   1 
HETATM 9176  O  O   . HOH G 5 .    ? 25.988 72.524  28.408  1.00 28.83 ? 1611 HOH A O   1 
HETATM 9177  O  O   . HOH G 5 .    ? 23.549 71.172  24.317  1.00 30.25 ? 1612 HOH A O   1 
HETATM 9178  O  O   . HOH G 5 .    ? 25.216 71.066  22.304  1.00 31.67 ? 1613 HOH A O   1 
HETATM 9179  O  O   . HOH G 5 .    ? 26.892 72.131  20.660  1.00 37.41 ? 1614 HOH A O   1 
HETATM 9180  O  O   . HOH G 5 .    ? 28.681 72.357  22.410  1.00 23.13 ? 1615 HOH A O   1 
HETATM 9181  O  O   . HOH G 5 .    ? 30.940 71.004  21.307  1.00 36.36 ? 1616 HOH A O   1 
HETATM 9182  O  O   . HOH G 5 .    ? 32.574 69.267  24.432  1.00 24.55 ? 1617 HOH A O   1 
HETATM 9183  O  O   . HOH G 5 .    ? 34.399 70.386  25.713  1.00 37.85 ? 1618 HOH A O   1 
HETATM 9184  O  O   . HOH G 5 .    ? 37.618 71.406  26.069  1.00 46.58 ? 1619 HOH A O   1 
HETATM 9185  O  O   . HOH G 5 .    ? 35.623 68.308  23.267  1.00 33.46 ? 1620 HOH A O   1 
HETATM 9186  O  O   . HOH G 5 .    ? 36.012 65.852  22.201  1.00 33.09 ? 1621 HOH A O   1 
HETATM 9187  O  O   . HOH G 5 .    ? 35.626 67.766  20.558  1.00 27.19 ? 1622 HOH A O   1 
HETATM 9188  O  O   . HOH G 5 .    ? 32.963 66.941  21.332  1.00 21.56 ? 1623 HOH A O   1 
HETATM 9189  O  O   . HOH G 5 .    ? 33.528 60.212  23.271  1.00 10.56 ? 1624 HOH A O   1 
HETATM 9190  O  O   . HOH G 5 .    ? 27.878 60.857  19.430  1.00 8.44  ? 1625 HOH A O   1 
HETATM 9191  O  O   . HOH G 5 .    ? 30.139 55.702  17.157  1.00 8.14  ? 1626 HOH A O   1 
HETATM 9192  O  O   . HOH G 5 .    ? 27.691 53.249  20.049  1.00 11.91 ? 1627 HOH A O   1 
HETATM 9193  O  O   . HOH G 5 .    ? 26.938 51.273  22.622  1.00 20.82 ? 1628 HOH A O   1 
HETATM 9194  O  O   A HOH G 5 .    ? 26.698 51.322  12.949  0.50 9.39  ? 1629 HOH A O   1 
HETATM 9195  O  O   B HOH G 5 .    ? 27.571 50.772  13.257  0.50 6.51  ? 1629 HOH A O   1 
HETATM 9196  O  O   A HOH G 5 .    ? 25.446 53.546  11.153  0.50 6.31  ? 1630 HOH A O   1 
HETATM 9197  O  O   B HOH G 5 .    ? 25.495 52.304  12.505  0.50 12.82 ? 1630 HOH A O   1 
HETATM 9198  O  O   . HOH G 5 .    ? 27.904 48.414  12.095  1.00 13.80 ? 1631 HOH A O   1 
HETATM 9199  O  O   . HOH G 5 .    ? 27.206 46.294  13.632  1.00 12.71 ? 1632 HOH A O   1 
HETATM 9200  O  O   . HOH G 5 .    ? 28.233 43.788  13.176  1.00 7.80  ? 1633 HOH A O   1 
HETATM 9201  O  O   . HOH G 5 .    ? 27.175 41.281  13.264  1.00 13.74 ? 1634 HOH A O   1 
HETATM 9202  O  O   . HOH G 5 .    ? 25.010 39.832  14.255  1.00 16.59 ? 1635 HOH A O   1 
HETATM 9203  O  O   . HOH G 5 .    ? 23.196 36.899  13.377  1.00 30.55 ? 1636 HOH A O   1 
HETATM 9204  O  O   . HOH G 5 .    ? 22.237 34.587  12.307  1.00 37.53 ? 1637 HOH A O   1 
HETATM 9205  O  O   . HOH G 5 .    ? 25.406 33.278  13.341  1.00 24.05 ? 1638 HOH A O   1 
HETATM 9206  O  O   . HOH G 5 .    ? 24.113 34.260  15.507  1.00 26.55 ? 1639 HOH A O   1 
HETATM 9207  O  O   . HOH G 5 .    ? 21.577 37.947  15.630  1.00 25.29 ? 1640 HOH A O   1 
HETATM 9208  O  O   . HOH G 5 .    ? 19.685 39.081  17.631  1.00 15.05 ? 1641 HOH A O   1 
HETATM 9209  O  O   . HOH G 5 .    ? 18.654 37.514  19.642  1.00 24.52 ? 1642 HOH A O   1 
HETATM 9210  O  O   . HOH G 5 .    ? 19.260 36.250  22.308  1.00 26.53 ? 1643 HOH A O   1 
HETATM 9211  O  O   . HOH G 5 .    ? 19.879 35.533  25.623  1.00 27.09 ? 1644 HOH A O   1 
HETATM 9212  O  O   . HOH G 5 .    ? 18.519 31.998  25.491  1.00 30.32 ? 1645 HOH A O   1 
HETATM 9213  O  O   . HOH G 5 .    ? 18.287 28.955  23.425  1.00 33.97 ? 1646 HOH A O   1 
HETATM 9214  O  O   . HOH G 5 .    ? 19.544 81.588  -42.661 1.00 35.31 ? 1647 HOH A O   1 
HETATM 9215  O  O   . HOH G 5 .    ? 22.064 80.644  -42.176 1.00 27.71 ? 1648 HOH A O   1 
HETATM 9216  O  O   . HOH G 5 .    ? 12.330 33.732  25.832  1.00 31.02 ? 1649 HOH A O   1 
HETATM 9217  O  O   . HOH G 5 .    ? 14.937 33.908  26.988  1.00 43.00 ? 1650 HOH A O   1 
HETATM 9218  O  O   . HOH G 5 .    ? 18.464 34.133  29.097  1.00 37.62 ? 1651 HOH A O   1 
HETATM 9219  O  O   . HOH G 5 .    ? 20.808 31.645  31.345  1.00 28.41 ? 1652 HOH A O   1 
HETATM 9220  O  O   . HOH G 5 .    ? 20.650 32.433  33.599  1.00 38.59 ? 1653 HOH A O   1 
HETATM 9221  O  O   . HOH G 5 .    ? 22.646 30.701  34.220  1.00 41.23 ? 1654 HOH A O   1 
HETATM 9222  O  O   . HOH G 5 .    ? 24.382 29.566  31.493  1.00 33.69 ? 1655 HOH A O   1 
HETATM 9223  O  O   . HOH G 5 .    ? 26.736 30.690  30.253  1.00 34.71 ? 1656 HOH A O   1 
HETATM 9224  O  O   . HOH G 5 .    ? 26.119 32.787  28.666  1.00 22.73 ? 1657 HOH A O   1 
HETATM 9225  O  O   . HOH G 5 .    ? 27.207 34.944  29.504  1.00 21.57 ? 1658 HOH A O   1 
HETATM 9226  O  O   . HOH G 5 .    ? 26.273 37.419  29.392  1.00 14.93 ? 1659 HOH A O   1 
HETATM 9227  O  O   . HOH G 5 .    ? 29.975 36.537  29.042  1.00 20.98 ? 1660 HOH A O   1 
HETATM 9228  O  O   . HOH G 5 .    ? 27.994 34.833  32.191  1.00 36.33 ? 1661 HOH A O   1 
HETATM 9229  O  O   . HOH G 5 .    ? 24.351 34.504  35.725  1.00 24.74 ? 1662 HOH A O   1 
HETATM 9230  O  O   . HOH G 5 .    ? 21.838 35.093  34.688  1.00 30.66 ? 1663 HOH A O   1 
HETATM 9231  O  O   . HOH G 5 .    ? 17.638 36.666  35.522  1.00 35.90 ? 1664 HOH A O   1 
HETATM 9232  O  O   . HOH G 5 .    ? 16.051 35.979  37.593  1.00 46.57 ? 1665 HOH A O   1 
HETATM 9233  O  O   . HOH G 5 .    ? 17.381 39.868  36.348  1.00 54.24 ? 1666 HOH A O   1 
HETATM 9234  O  O   . HOH G 5 .    ? 16.067 40.067  34.204  1.00 41.76 ? 1667 HOH A O   1 
HETATM 9235  O  O   . HOH G 5 .    ? 17.371 41.666  32.092  1.00 34.32 ? 1668 HOH A O   1 
HETATM 9236  O  O   . HOH G 5 .    ? 19.475 43.159  33.826  1.00 29.49 ? 1669 HOH A O   1 
HETATM 9237  O  O   . HOH G 5 .    ? 20.910 41.754  35.121  1.00 24.48 ? 1670 HOH A O   1 
HETATM 9238  O  O   . HOH G 5 .    ? 20.275 40.987  37.349  1.00 33.02 ? 1671 HOH A O   1 
HETATM 9239  O  O   . HOH G 5 .    ? 28.259 40.526  38.770  1.00 36.87 ? 1672 HOH A O   1 
HETATM 9240  O  O   . HOH G 5 .    ? 27.992 37.868  39.212  1.00 42.59 ? 1673 HOH A O   1 
HETATM 9241  O  O   . HOH G 5 .    ? 28.646 35.491  37.722  1.00 32.63 ? 1674 HOH A O   1 
HETATM 9242  O  O   . HOH G 5 .    ? 28.095 44.165  38.462  1.00 32.83 ? 1675 HOH A O   1 
HETATM 9243  O  O   . HOH G 5 .    ? 29.087 46.913  37.103  1.00 16.97 ? 1676 HOH A O   1 
HETATM 9244  O  O   . HOH G 5 .    ? 31.617 47.517  37.836  1.00 34.83 ? 1677 HOH A O   1 
HETATM 9245  O  O   . HOH G 5 .    ? 32.891 49.230  39.829  1.00 32.43 ? 1678 HOH A O   1 
HETATM 9246  O  O   . HOH G 5 .    ? 29.975 51.139  39.902  1.00 40.06 ? 1679 HOH A O   1 
HETATM 9247  O  O   . HOH G 5 .    ? 28.227 49.164  38.400  1.00 25.87 ? 1680 HOH A O   1 
HETATM 9248  O  O   . HOH G 5 .    ? 34.049 47.830  36.183  1.00 27.67 ? 1681 HOH A O   1 
HETATM 9249  O  O   . HOH G 5 .    ? 36.383 47.104  35.133  1.00 33.60 ? 1682 HOH A O   1 
HETATM 9250  O  O   . HOH G 5 .    ? 34.726 45.755  33.339  1.00 17.52 ? 1683 HOH A O   1 
HETATM 9251  O  O   . HOH G 5 .    ? 37.404 47.128  29.689  1.00 17.52 ? 1684 HOH A O   1 
HETATM 9252  O  O   . HOH G 5 .    ? 37.005 45.503  27.443  1.00 11.71 ? 1685 HOH A O   1 
HETATM 9253  O  O   A HOH G 5 .    ? 39.323 45.150  25.883  0.50 13.98 ? 1686 HOH A O   1 
HETATM 9254  O  O   B HOH G 5 .    ? 39.059 43.582  26.888  0.50 20.14 ? 1686 HOH A O   1 
HETATM 9255  O  O   . HOH G 5 .    ? 39.190 41.189  26.248  1.00 39.69 ? 1687 HOH A O   1 
HETATM 9256  O  O   . HOH G 5 .    ? 37.048 39.840  26.598  1.00 28.40 ? 1688 HOH A O   1 
HETATM 9257  O  O   . HOH G 5 .    ? 36.807 37.077  25.301  1.00 35.52 ? 1689 HOH A O   1 
HETATM 9258  O  O   . HOH G 5 .    ? 34.560 36.203  23.530  1.00 36.80 ? 1690 HOH A O   1 
HETATM 9259  O  O   . HOH G 5 .    ? 32.376 34.815  24.230  1.00 34.95 ? 1691 HOH A O   1 
HETATM 9260  O  O   . HOH G 5 .    ? 32.443 33.959  26.717  1.00 37.96 ? 1692 HOH A O   1 
HETATM 9261  O  O   . HOH G 5 .    ? 29.618 31.357  21.908  1.00 29.61 ? 1693 HOH A O   1 
HETATM 9262  O  O   . HOH G 5 .    ? 30.135 30.265  19.461  1.00 45.05 ? 1694 HOH A O   1 
HETATM 9263  O  O   . HOH G 5 .    ? 28.253 29.058  18.431  1.00 42.07 ? 1695 HOH A O   1 
HETATM 9264  O  O   . HOH G 5 .    ? 29.386 28.491  15.524  1.00 42.35 ? 1696 HOH A O   1 
HETATM 9265  O  O   . HOH G 5 .    ? 32.710 30.926  15.946  1.00 35.71 ? 1697 HOH A O   1 
HETATM 9266  O  O   . HOH G 5 .    ? 31.922 33.512  16.987  1.00 26.14 ? 1698 HOH A O   1 
HETATM 9267  O  O   . HOH G 5 .    ? 34.355 34.314  16.153  1.00 18.84 ? 1699 HOH A O   1 
HETATM 9268  O  O   . HOH G 5 .    ? 36.233 36.659  19.599  1.00 47.37 ? 1700 HOH A O   1 
HETATM 9269  O  O   . HOH G 5 .    ? 38.210 36.206  17.768  1.00 27.61 ? 1701 HOH A O   1 
HETATM 9270  O  O   . HOH G 5 .    ? 39.217 38.772  17.228  1.00 14.46 ? 1702 HOH A O   1 
HETATM 9271  O  O   . HOH G 5 .    ? 41.880 39.056  16.551  1.00 24.50 ? 1703 HOH A O   1 
HETATM 9272  O  O   . HOH G 5 .    ? 43.171 39.809  18.763  1.00 45.09 ? 1704 HOH A O   1 
HETATM 9273  O  O   . HOH G 5 .    ? 41.350 37.025  20.719  1.00 37.40 ? 1705 HOH A O   1 
HETATM 9274  O  O   . HOH G 5 .    ? 39.540 39.549  20.045  1.00 29.73 ? 1706 HOH A O   1 
HETATM 9275  O  O   . HOH G 5 .    ? 38.065 38.622  21.946  1.00 34.17 ? 1707 HOH A O   1 
HETATM 9276  O  O   . HOH G 5 .    ? 38.887 42.968  22.694  1.00 24.66 ? 1708 HOH A O   1 
HETATM 9277  O  O   . HOH G 5 .    ? 41.819 40.814  27.774  1.00 28.79 ? 1709 HOH A O   1 
HETATM 9278  O  O   . HOH G 5 .    ? 46.511 43.636  28.343  1.00 34.85 ? 1710 HOH A O   1 
HETATM 9279  O  O   . HOH G 5 .    ? 47.102 45.756  26.541  1.00 29.76 ? 1711 HOH A O   1 
HETATM 9280  O  O   . HOH G 5 .    ? 44.275 45.381  25.411  1.00 35.94 ? 1712 HOH A O   1 
HETATM 9281  O  O   . HOH G 5 .    ? 45.628 44.945  23.136  1.00 35.35 ? 1713 HOH A O   1 
HETATM 9282  O  O   . HOH G 5 .    ? 43.631 44.964  19.125  1.00 40.30 ? 1714 HOH A O   1 
HETATM 9283  O  O   . HOH G 5 .    ? 46.070 46.102  16.483  1.00 30.11 ? 1715 HOH A O   1 
HETATM 9284  O  O   . HOH G 5 .    ? 48.019 48.212  16.521  1.00 13.60 ? 1716 HOH A O   1 
HETATM 9285  O  O   . HOH G 5 .    ? 47.929 49.473  13.916  1.00 11.71 ? 1717 HOH A O   1 
HETATM 9286  O  O   . HOH G 5 .    ? 46.948 48.510  11.620  1.00 14.74 ? 1718 HOH A O   1 
HETATM 9287  O  O   . HOH G 5 .    ? 46.672 45.822  11.694  1.00 33.72 ? 1719 HOH A O   1 
HETATM 9288  O  O   . HOH G 5 .    ? 48.496 44.878  10.210  1.00 39.73 ? 1720 HOH A O   1 
HETATM 9289  O  O   . HOH G 5 .    ? 51.237 45.162  10.163  1.00 24.71 ? 1721 HOH A O   1 
HETATM 9290  O  O   . HOH G 5 .    ? 53.355 44.919  12.420  1.00 37.21 ? 1722 HOH A O   1 
HETATM 9291  O  O   . HOH G 5 .    ? 54.187 47.698  15.608  1.00 21.96 ? 1723 HOH A O   1 
HETATM 9292  O  O   . HOH G 5 .    ? 55.097 50.305  17.001  1.00 25.69 ? 1724 HOH A O   1 
HETATM 9293  O  O   . HOH G 5 .    ? 58.958 51.152  14.962  1.00 30.62 ? 1725 HOH A O   1 
HETATM 9294  O  O   . HOH G 5 .    ? 60.083 51.168  12.722  1.00 35.97 ? 1726 HOH A O   1 
HETATM 9295  O  O   . HOH G 5 .    ? 61.790 51.647  9.620   1.00 40.42 ? 1727 HOH A O   1 
HETATM 9296  O  O   . HOH G 5 .    ? 60.061 51.368  6.083   1.00 39.17 ? 1728 HOH A O   1 
HETATM 9297  O  O   . HOH G 5 .    ? 58.374 52.832  4.794   1.00 28.38 ? 1729 HOH A O   1 
HETATM 9298  O  O   . HOH G 5 .    ? 59.359 52.074  2.716   1.00 26.02 ? 1730 HOH A O   1 
HETATM 9299  O  O   . HOH G 5 .    ? 58.715 52.641  -0.062  1.00 11.51 ? 1731 HOH A O   1 
HETATM 9300  O  O   . HOH G 5 .    ? 59.221 50.064  -0.494  1.00 15.61 ? 1732 HOH A O   1 
HETATM 9301  O  O   . HOH G 5 .    ? 59.678 49.073  2.186   1.00 29.61 ? 1733 HOH A O   1 
HETATM 9302  O  O   . HOH G 5 .    ? 60.383 45.955  0.936   1.00 33.46 ? 1734 HOH A O   1 
HETATM 9303  O  O   . HOH G 5 .    ? 58.944 46.319  -1.514  1.00 20.87 ? 1735 HOH A O   1 
HETATM 9304  O  O   . HOH G 5 .    ? 60.907 45.265  -3.714  1.00 34.82 ? 1736 HOH A O   1 
HETATM 9305  O  O   . HOH G 5 .    ? 62.698 44.643  -0.364  1.00 27.87 ? 1737 HOH A O   1 
HETATM 9306  O  O   . HOH G 5 .    ? 64.269 43.390  -2.305  1.00 28.06 ? 1738 HOH A O   1 
HETATM 9307  O  O   . HOH G 5 .    ? 65.665 45.661  -3.029  1.00 28.88 ? 1739 HOH A O   1 
HETATM 9308  O  O   . HOH G 5 .    ? 67.310 46.647  -1.045  1.00 24.74 ? 1740 HOH A O   1 
HETATM 9309  O  O   . HOH G 5 .    ? 67.994 49.405  -0.793  1.00 24.06 ? 1741 HOH A O   1 
HETATM 9310  O  O   . HOH G 5 .    ? 65.860 50.523  0.558   1.00 47.44 ? 1742 HOH A O   1 
HETATM 9311  O  O   . HOH G 5 .    ? 67.180 52.793  1.628   1.00 36.88 ? 1743 HOH A O   1 
HETATM 9312  O  O   . HOH G 5 .    ? 67.048 55.354  1.064   1.00 20.22 ? 1744 HOH A O   1 
HETATM 9313  O  O   . HOH G 5 .    ? 63.700 57.243  0.932   1.00 26.21 ? 1745 HOH A O   1 
HETATM 9314  O  O   . HOH G 5 .    ? 63.141 58.673  -1.331  1.00 14.70 ? 1746 HOH A O   1 
HETATM 9315  O  O   . HOH G 5 .    ? 64.825 59.301  -3.436  1.00 14.21 ? 1747 HOH A O   1 
HETATM 9316  O  O   . HOH G 5 .    ? 63.045 61.186  -4.713  1.00 15.96 ? 1748 HOH A O   1 
HETATM 9317  O  O   . HOH G 5 .    ? 63.061 61.300  -7.437  1.00 8.79  ? 1749 HOH A O   1 
HETATM 9318  O  O   . HOH G 5 .    ? 65.567 60.349  -7.573  1.00 8.55  ? 1750 HOH A O   1 
HETATM 9319  O  O   . HOH G 5 .    ? 67.415 60.721  -5.525  1.00 11.51 ? 1751 HOH A O   1 
HETATM 9320  O  O   . HOH G 5 .    ? 68.675 58.291  -4.913  1.00 12.97 ? 1752 HOH A O   1 
HETATM 9321  O  O   . HOH G 5 .    ? 69.099 61.471  -2.257  1.00 15.16 ? 1753 HOH A O   1 
HETATM 9322  O  O   . HOH G 5 .    ? 70.384 62.054  0.225   1.00 27.64 ? 1754 HOH A O   1 
HETATM 9323  O  O   . HOH G 5 .    ? 71.289 59.784  1.248   1.00 27.92 ? 1755 HOH A O   1 
HETATM 9324  O  O   . HOH G 5 .    ? 73.202 58.243  4.645   1.00 39.35 ? 1756 HOH A O   1 
HETATM 9325  O  O   . HOH G 5 .    ? 73.356 62.894  -0.762  1.00 37.64 ? 1757 HOH A O   1 
HETATM 9326  O  O   . HOH G 5 .    ? 71.906 66.897  2.180   1.00 34.50 ? 1758 HOH A O   1 
HETATM 9327  O  O   . HOH G 5 .    ? 69.310 65.420  2.902   1.00 42.35 ? 1759 HOH A O   1 
HETATM 9328  O  O   . HOH G 5 .    ? 67.870 67.002  1.210   1.00 35.28 ? 1760 HOH A O   1 
HETATM 9329  O  O   A HOH G 5 .    ? 65.818 65.954  -0.409  0.50 9.33  ? 1761 HOH A O   1 
HETATM 9330  O  O   B HOH G 5 .    ? 65.492 66.880  0.352   0.50 13.04 ? 1761 HOH A O   1 
HETATM 9331  O  O   . HOH G 5 .    ? 67.805 65.542  -3.272  1.00 14.27 ? 1762 HOH A O   1 
HETATM 9332  O  O   . HOH G 5 .    ? 66.167 68.678  2.252   1.00 29.92 ? 1763 HOH A O   1 
HETATM 9333  O  O   . HOH G 5 .    ? 62.647 64.104  2.782   1.00 32.05 ? 1764 HOH A O   1 
HETATM 9334  O  O   . HOH G 5 .    ? 61.995 63.668  4.981   1.00 36.34 ? 1765 HOH A O   1 
HETATM 9335  O  O   . HOH G 5 .    ? 59.591 64.223  7.047   1.00 37.29 ? 1766 HOH A O   1 
HETATM 9336  O  O   . HOH G 5 .    ? 57.831 62.826  8.587   1.00 20.51 ? 1767 HOH A O   1 
HETATM 9337  O  O   . HOH G 5 .    ? 58.823 60.569  5.667   1.00 27.88 ? 1768 HOH A O   1 
HETATM 9338  O  O   . HOH G 5 .    ? 57.420 58.404  5.444   1.00 22.24 ? 1769 HOH A O   1 
HETATM 9339  O  O   . HOH G 5 .    ? 55.175 59.077  3.955   1.00 13.28 ? 1770 HOH A O   1 
HETATM 9340  O  O   . HOH G 5 .    ? 56.207 58.478  1.417   1.00 32.15 ? 1771 HOH A O   1 
HETATM 9341  O  O   . HOH G 5 .    ? 54.935 57.626  -0.424  1.00 15.75 ? 1772 HOH A O   1 
HETATM 9342  O  O   . HOH G 5 .    ? 56.315 55.703  -2.045  1.00 10.01 ? 1773 HOH A O   1 
HETATM 9343  O  O   . HOH G 5 .    ? 56.113 53.418  -0.534  1.00 6.57  ? 1774 HOH A O   1 
HETATM 9344  O  O   . HOH G 5 .    ? 58.835 56.776  -1.301  1.00 11.55 ? 1775 HOH A O   1 
HETATM 9345  O  O   . HOH G 5 .    ? 60.661 58.276  -2.749  1.00 11.82 ? 1776 HOH A O   1 
HETATM 9346  O  O   . HOH G 5 .    ? 60.592 60.874  -3.449  1.00 13.19 ? 1777 HOH A O   1 
HETATM 9347  O  O   . HOH G 5 .    ? 60.409 62.200  -1.170  1.00 12.48 ? 1778 HOH A O   1 
HETATM 9348  O  O   . HOH G 5 .    ? 62.104 60.691  0.549   1.00 22.74 ? 1779 HOH A O   1 
HETATM 9349  O  O   . HOH G 5 .    ? 58.815 58.216  1.086   1.00 25.83 ? 1780 HOH A O   1 
HETATM 9350  O  O   . HOH G 5 .    ? 60.659 56.161  2.206   1.00 30.92 ? 1781 HOH A O   1 
HETATM 9351  O  O   . HOH G 5 .    ? 59.606 55.336  4.563   1.00 44.30 ? 1782 HOH A O   1 
HETATM 9352  O  O   . HOH G 5 .    ? 60.499 54.823  -0.196  1.00 12.09 ? 1783 HOH A O   1 
HETATM 9353  O  O   . HOH G 5 .    ? 63.367 52.019  -0.308  1.00 27.50 ? 1784 HOH A O   1 
HETATM 9354  O  O   . HOH G 5 .    ? 70.877 49.538  0.175   1.00 19.94 ? 1785 HOH A O   1 
HETATM 9355  O  O   . HOH G 5 .    ? 71.916 47.022  -0.089  1.00 34.36 ? 1786 HOH A O   1 
HETATM 9356  O  O   . HOH G 5 .    ? 72.671 51.290  2.046   1.00 30.24 ? 1787 HOH A O   1 
HETATM 9357  O  O   . HOH G 5 .    ? 76.753 51.200  1.771   1.00 42.74 ? 1788 HOH A O   1 
HETATM 9358  O  O   . HOH G 5 .    ? 75.821 48.412  -5.433  1.00 40.22 ? 1789 HOH A O   1 
HETATM 9359  O  O   . HOH G 5 .    ? 73.933 46.861  -4.599  1.00 40.24 ? 1790 HOH A O   1 
HETATM 9360  O  O   . HOH G 5 .    ? 79.130 47.007  -5.033  1.00 36.10 ? 1791 HOH A O   1 
HETATM 9361  O  O   . HOH G 5 .    ? 10.368 50.408  -8.976  1.00 40.76 ? 1792 HOH A O   1 
HETATM 9362  O  O   . HOH G 5 .    ? 10.399 47.574  -10.658 1.00 41.58 ? 1793 HOH A O   1 
HETATM 9363  O  O   . HOH G 5 .    ? 73.398 51.629  -11.174 1.00 29.62 ? 1794 HOH A O   1 
HETATM 9364  O  O   . HOH G 5 .    ? 70.583 52.249  -12.305 1.00 22.40 ? 1795 HOH A O   1 
HETATM 9365  O  O   . HOH G 5 .    ? 71.156 54.474  -13.661 1.00 32.79 ? 1796 HOH A O   1 
HETATM 9366  O  O   . HOH G 5 .    ? 69.997 56.385  -12.336 1.00 28.05 ? 1797 HOH A O   1 
HETATM 9367  O  O   . HOH G 5 .    ? 71.948 58.686  -11.193 1.00 27.78 ? 1798 HOH A O   1 
HETATM 9368  O  O   . HOH G 5 .    ? 74.296 60.213  -9.414  1.00 30.24 ? 1799 HOH A O   1 
HETATM 9369  O  O   . HOH G 5 .    ? 74.304 62.683  -8.289  1.00 42.22 ? 1800 HOH A O   1 
HETATM 9370  O  O   . HOH G 5 .    ? 72.917 65.062  -7.707  1.00 17.39 ? 1801 HOH A O   1 
HETATM 9371  O  O   . HOH G 5 .    ? 72.932 66.633  -9.901  1.00 20.74 ? 1802 HOH A O   1 
HETATM 9372  O  O   . HOH G 5 .    ? 75.616 67.061  -9.401  1.00 29.55 ? 1803 HOH A O   1 
HETATM 9373  O  O   . HOH G 5 .    ? 77.440 66.244  -11.753 1.00 28.35 ? 1804 HOH A O   1 
HETATM 9374  O  O   . HOH G 5 .    ? 78.519 68.579  -12.193 1.00 21.25 ? 1805 HOH A O   1 
HETATM 9375  O  O   . HOH G 5 .    ? 79.200 67.453  -14.830 1.00 26.45 ? 1806 HOH A O   1 
HETATM 9376  O  O   . HOH G 5 .    ? 77.501 65.018  -14.793 1.00 26.19 ? 1807 HOH A O   1 
HETATM 9377  O  O   . HOH G 5 .    ? 75.142 64.225  -16.169 1.00 27.99 ? 1808 HOH A O   1 
HETATM 9378  O  O   . HOH G 5 .    ? 74.352 63.588  -13.989 1.00 28.03 ? 1809 HOH A O   1 
HETATM 9379  O  O   . HOH G 5 .    ? 74.598 61.103  -13.246 1.00 38.89 ? 1810 HOH A O   1 
HETATM 9380  O  O   . HOH G 5 .    ? 71.463 62.591  -17.834 1.00 26.21 ? 1811 HOH A O   1 
HETATM 9381  O  O   . HOH G 5 .    ? 70.259 61.990  -20.185 1.00 22.49 ? 1812 HOH A O   1 
HETATM 9382  O  O   . HOH G 5 .    ? 70.270 59.453  -20.760 1.00 34.23 ? 1813 HOH A O   1 
HETATM 9383  O  O   . HOH G 5 .    ? 70.030 60.441  -23.259 1.00 28.32 ? 1814 HOH A O   1 
HETATM 9384  O  O   . HOH G 5 .    ? 69.799 63.014  -23.689 1.00 25.69 ? 1815 HOH A O   1 
HETATM 9385  O  O   . HOH G 5 .    ? 72.578 63.885  -21.026 1.00 27.83 ? 1816 HOH A O   1 
HETATM 9386  O  O   . HOH G 5 .    ? 73.791 65.991  -17.522 1.00 15.02 ? 1817 HOH A O   1 
HETATM 9387  O  O   . HOH G 5 .    ? 80.569 63.425  -16.870 1.00 26.69 ? 1818 HOH A O   1 
HETATM 9388  O  O   . HOH G 5 .    ? 80.202 64.126  -21.447 1.00 22.53 ? 1819 HOH A O   1 
HETATM 9389  O  O   . HOH G 5 .    ? 79.237 63.318  -23.865 1.00 33.98 ? 1820 HOH A O   1 
HETATM 9390  O  O   A HOH G 5 .    ? 80.923 61.186  -24.067 0.50 15.99 ? 1821 HOH A O   1 
HETATM 9391  O  O   B HOH G 5 .    ? 12.880 62.147  -24.785 0.50 17.76 ? 1821 HOH A O   1 
HETATM 9392  O  O   . HOH G 5 .    ? 78.145 64.636  -26.279 1.00 30.79 ? 1822 HOH A O   1 
HETATM 9393  O  O   . HOH G 5 .    ? 83.563 66.012  -24.871 1.00 33.75 ? 1823 HOH A O   1 
HETATM 9394  O  O   . HOH G 5 .    ? 84.026 68.479  -27.462 1.00 32.52 ? 1824 HOH A O   1 
HETATM 9395  O  O   . HOH G 5 .    ? 82.219 69.501  -25.193 1.00 47.32 ? 1825 HOH A O   1 
HETATM 9396  O  O   . HOH G 5 .    ? 83.373 70.269  -22.944 1.00 29.87 ? 1826 HOH A O   1 
HETATM 9397  O  O   . HOH G 5 .    ? 83.416 70.068  -20.066 1.00 33.12 ? 1827 HOH A O   1 
HETATM 9398  O  O   . HOH G 5 .    ? 84.150 68.122  -17.179 1.00 15.47 ? 1828 HOH A O   1 
HETATM 9399  O  O   . HOH G 5 .    ? 79.749 73.660  -17.629 1.00 25.27 ? 1829 HOH A O   1 
HETATM 9400  O  O   . HOH G 5 .    ? 77.587 74.932  -18.125 1.00 35.44 ? 1830 HOH A O   1 
HETATM 9401  O  O   . HOH G 5 .    ? 75.331 74.064  -19.147 1.00 22.93 ? 1831 HOH A O   1 
HETATM 9402  O  O   . HOH G 5 .    ? 73.153 76.677  -18.428 1.00 34.29 ? 1832 HOH A O   1 
HETATM 9403  O  O   . HOH G 5 .    ? 74.595 77.475  -20.602 1.00 35.14 ? 1833 HOH A O   1 
HETATM 9404  O  O   . HOH G 5 .    ? 71.590 78.834  -17.583 1.00 38.87 ? 1834 HOH A O   1 
HETATM 9405  O  O   . HOH G 5 .    ? 68.346 78.981  -18.034 1.00 26.20 ? 1835 HOH A O   1 
HETATM 9406  O  O   . HOH G 5 .    ? 71.092 83.910  -14.743 1.00 38.46 ? 1836 HOH A O   1 
HETATM 9407  O  O   . HOH G 5 .    ? 71.604 84.592  -19.951 1.00 32.56 ? 1837 HOH A O   1 
HETATM 9408  O  O   . HOH G 5 .    ? 73.106 82.434  -21.092 1.00 27.15 ? 1838 HOH A O   1 
HETATM 9409  O  O   . HOH G 5 .    ? 75.106 83.802  -22.873 1.00 35.57 ? 1839 HOH A O   1 
HETATM 9410  O  O   . HOH G 5 .    ? 79.060 79.992  -25.687 1.00 50.74 ? 1840 HOH A O   1 
HETATM 9411  O  O   . HOH G 5 .    ? 76.957 80.723  -28.283 1.00 34.51 ? 1841 HOH A O   1 
HETATM 9412  O  O   . HOH G 5 .    ? 11.885 76.331  -25.940 1.00 43.91 ? 1842 HOH A O   1 
HETATM 9413  O  O   . HOH G 5 .    ? 12.703 77.790  -23.459 1.00 44.50 ? 1843 HOH A O   1 
HETATM 9414  O  O   . HOH G 5 .    ? 12.874 74.331  -23.286 1.00 36.14 ? 1844 HOH A O   1 
HETATM 9415  O  O   . HOH G 5 .    ? 76.568 74.107  -26.475 1.00 30.54 ? 1845 HOH A O   1 
HETATM 9416  O  O   . HOH G 5 .    ? 72.336 63.325  -27.621 1.00 40.67 ? 1846 HOH A O   1 
HETATM 9417  O  O   . HOH G 5 .    ? 69.847 63.880  -28.075 1.00 34.39 ? 1847 HOH A O   1 
HETATM 9418  O  O   A HOH G 5 .    ? 66.563 66.875  -32.450 0.50 19.12 ? 1848 HOH A O   1 
HETATM 9419  O  O   B HOH G 5 .    ? 67.325 65.908  -32.888 0.50 20.08 ? 1848 HOH A O   1 
HETATM 9420  O  O   . HOH G 5 .    ? 63.214 67.928  -31.641 1.00 21.39 ? 1849 HOH A O   1 
HETATM 9421  O  O   . HOH G 5 .    ? 63.845 65.768  -30.163 1.00 32.84 ? 1850 HOH A O   1 
HETATM 9422  O  O   . HOH G 5 .    ? 61.778 63.889  -30.660 1.00 23.82 ? 1851 HOH A O   1 
HETATM 9423  O  O   . HOH G 5 .    ? 67.280 64.551  -38.483 1.00 16.77 ? 1852 HOH A O   1 
HETATM 9424  O  O   . HOH G 5 .    ? 67.972 66.039  -40.611 1.00 11.40 ? 1853 HOH A O   1 
HETATM 9425  O  O   . HOH G 5 .    ? 58.286 77.229  -38.494 1.00 13.51 ? 1854 HOH A O   1 
HETATM 9426  O  O   . HOH G 5 .    ? 51.249 76.185  -40.857 1.00 23.66 ? 1855 HOH A O   1 
HETATM 9427  O  O   . HOH G 5 .    ? 54.555 82.663  -44.346 1.00 40.25 ? 1856 HOH A O   1 
HETATM 9428  O  O   . HOH G 5 .    ? 53.830 90.840  -42.938 1.00 31.68 ? 1857 HOH A O   1 
HETATM 9429  O  O   . HOH G 5 .    ? 53.528 92.643  -40.861 1.00 31.97 ? 1858 HOH A O   1 
HETATM 9430  O  O   . HOH G 5 .    ? 56.283 93.865  -41.075 1.00 39.45 ? 1859 HOH A O   1 
HETATM 9431  O  O   . HOH G 5 .    ? 61.249 90.879  -37.189 1.00 31.53 ? 1860 HOH A O   1 
HETATM 9432  O  O   . HOH G 5 .    ? 59.321 91.123  -35.334 1.00 23.38 ? 1861 HOH A O   1 
HETATM 9433  O  O   . HOH G 5 .    ? 61.466 92.204  -33.858 1.00 33.94 ? 1862 HOH A O   1 
HETATM 9434  O  O   . HOH G 5 .    ? 63.864 92.274  -34.171 1.00 24.83 ? 1863 HOH A O   1 
HETATM 9435  O  O   . HOH G 5 .    ? 63.855 90.844  -36.360 1.00 33.61 ? 1864 HOH A O   1 
HETATM 9436  O  O   . HOH G 5 .    ? 65.416 89.279  -37.246 1.00 34.37 ? 1865 HOH A O   1 
HETATM 9437  O  O   . HOH G 5 .    ? 67.798 88.072  -35.150 1.00 28.68 ? 1866 HOH A O   1 
HETATM 9438  O  O   . HOH G 5 .    ? 67.179 85.587  -36.089 1.00 32.66 ? 1867 HOH A O   1 
HETATM 9439  O  O   . HOH G 5 .    ? 71.418 85.679  -35.457 1.00 45.02 ? 1868 HOH A O   1 
HETATM 9440  O  O   . HOH G 5 .    ? 65.360 87.365  -41.402 1.00 36.14 ? 1869 HOH A O   1 
HETATM 9441  O  O   . HOH G 5 .    ? 64.254 93.569  -39.168 1.00 39.28 ? 1870 HOH A O   1 
HETATM 9442  O  O   . HOH G 5 .    ? 64.459 94.332  -35.802 1.00 32.00 ? 1871 HOH A O   1 
HETATM 9443  O  O   . HOH G 5 .    ? 66.505 96.012  -35.404 1.00 38.96 ? 1872 HOH A O   1 
HETATM 9444  O  O   . HOH G 5 .    ? 68.411 98.156  -34.120 1.00 48.47 ? 1873 HOH A O   1 
HETATM 9445  O  O   . HOH G 5 .    ? 69.427 98.766  -36.542 1.00 38.07 ? 1874 HOH A O   1 
HETATM 9446  O  O   . HOH G 5 .    ? 70.246 95.407  -35.031 1.00 40.36 ? 1875 HOH A O   1 
HETATM 9447  O  O   . HOH G 5 .    ? 72.089 95.679  -31.348 1.00 28.85 ? 1876 HOH A O   1 
HETATM 9448  O  O   . HOH G 5 .    ? 60.277 91.100  -31.251 1.00 25.55 ? 1877 HOH A O   1 
HETATM 9449  O  O   . HOH G 5 .    ? 56.281 92.815  -29.798 1.00 25.49 ? 1878 HOH A O   1 
HETATM 9450  O  O   . HOH G 5 .    ? 58.380 92.803  -26.807 1.00 25.12 ? 1879 HOH A O   1 
HETATM 9451  O  O   . HOH G 5 .    ? 56.147 90.952  -25.837 1.00 24.40 ? 1880 HOH A O   1 
HETATM 9452  O  O   . HOH G 5 .    ? 54.831 90.303  -23.571 1.00 35.14 ? 1881 HOH A O   1 
HETATM 9453  O  O   . HOH G 5 .    ? 56.383 90.043  -21.330 1.00 42.37 ? 1882 HOH A O   1 
HETATM 9454  O  O   . HOH G 5 .    ? 56.990 87.423  -20.002 1.00 38.35 ? 1883 HOH A O   1 
HETATM 9455  O  O   . HOH G 5 .    ? 53.322 87.285  -21.091 1.00 28.33 ? 1884 HOH A O   1 
HETATM 9456  O  O   . HOH G 5 .    ? 51.472 87.398  -17.332 1.00 42.72 ? 1885 HOH A O   1 
HETATM 9457  O  O   . HOH G 5 .    ? 49.388 86.074  -11.439 1.00 43.77 ? 1886 HOH A O   1 
HETATM 9458  O  O   . HOH G 5 .    ? 44.794 83.876  -11.234 1.00 38.38 ? 1887 HOH A O   1 
HETATM 9459  O  O   . HOH G 5 .    ? 43.105 82.171  -10.400 1.00 27.16 ? 1888 HOH A O   1 
HETATM 9460  O  O   . HOH G 5 .    ? 43.703 83.081  -8.017  1.00 40.20 ? 1889 HOH A O   1 
HETATM 9461  O  O   . HOH G 5 .    ? 45.465 79.106  -7.631  1.00 26.49 ? 1890 HOH A O   1 
HETATM 9462  O  O   . HOH G 5 .    ? 48.295 78.016  -9.783  1.00 28.18 ? 1891 HOH A O   1 
HETATM 9463  O  O   . HOH G 5 .    ? 49.607 79.676  -11.250 1.00 37.35 ? 1892 HOH A O   1 
HETATM 9464  O  O   . HOH G 5 .    ? 41.250 77.500  -14.081 1.00 11.14 ? 1893 HOH A O   1 
HETATM 9465  O  O   . HOH G 5 .    ? 42.120 75.177  -16.037 1.00 13.17 ? 1894 HOH A O   1 
HETATM 9466  O  O   A HOH G 5 .    ? 45.071 69.021  -17.190 0.50 10.99 ? 1895 HOH A O   1 
HETATM 9467  O  O   B HOH G 5 .    ? 45.652 69.868  -18.564 0.50 17.52 ? 1895 HOH A O   1 
HETATM 9468  O  O   . HOH G 5 .    ? 46.338 67.590  -15.551 1.00 16.80 ? 1896 HOH A O   1 
HETATM 9469  O  O   . HOH G 5 .    ? 48.814 69.333  -15.382 1.00 32.33 ? 1897 HOH A O   1 
HETATM 9470  O  O   . HOH G 5 .    ? 49.363 70.766  -17.519 1.00 33.47 ? 1898 HOH A O   1 
HETATM 9471  O  O   . HOH G 5 .    ? 51.515 69.917  -18.595 1.00 28.38 ? 1899 HOH A O   1 
HETATM 9472  O  O   . HOH G 5 .    ? 51.172 71.434  -20.350 1.00 24.29 ? 1900 HOH A O   1 
HETATM 9473  O  O   . HOH G 5 .    ? 53.462 72.592  -19.200 1.00 13.12 ? 1901 HOH A O   1 
HETATM 9474  O  O   . HOH G 5 .    ? 49.778 73.711  -21.806 1.00 31.26 ? 1902 HOH A O   1 
HETATM 9475  O  O   . HOH G 5 .    ? 47.420 71.944  -20.132 1.00 26.42 ? 1903 HOH A O   1 
HETATM 9476  O  O   . HOH G 5 .    ? 50.859 70.830  -23.495 1.00 17.84 ? 1904 HOH A O   1 
HETATM 9477  O  O   . HOH G 5 .    ? 45.304 71.937  -25.827 1.00 39.28 ? 1905 HOH A O   1 
HETATM 9478  O  O   . HOH G 5 .    ? 47.147 70.481  -28.395 1.00 37.08 ? 1906 HOH A O   1 
HETATM 9479  O  O   . HOH G 5 .    ? 47.311 68.209  -30.516 1.00 20.47 ? 1907 HOH A O   1 
HETATM 9480  O  O   . HOH G 5 .    ? 48.088 74.233  -28.880 1.00 33.04 ? 1908 HOH A O   1 
HETATM 9481  O  O   . HOH G 5 .    ? 43.417 68.236  -25.045 1.00 18.25 ? 1909 HOH A O   1 
HETATM 9482  O  O   . HOH G 5 .    ? 39.233 62.750  -19.118 1.00 6.34  ? 1910 HOH A O   1 
HETATM 9483  O  O   . HOH G 5 .    ? 39.206 64.741  -14.693 1.00 10.09 ? 1911 HOH A O   1 
HETATM 9484  O  O   . HOH G 5 .    ? 42.012 63.422  -7.189  1.00 6.09  ? 1912 HOH A O   1 
HETATM 9485  O  O   A HOH G 5 .    ? 49.509 62.152  -8.715  0.50 12.63 ? 1913 HOH A O   1 
HETATM 9486  O  O   B HOH G 5 .    ? 48.878 60.992  -7.996  0.50 12.63 ? 1913 HOH A O   1 
HETATM 9487  O  O   A HOH G 5 .    ? 50.023 59.459  -11.477 0.50 14.74 ? 1914 HOH A O   1 
HETATM 9488  O  O   B HOH G 5 .    ? 49.411 61.110  -10.462 0.50 14.74 ? 1914 HOH A O   1 
HETATM 9489  O  O   A HOH G 5 .    ? 50.817 59.825  -8.832  0.50 18.04 ? 1915 HOH A O   1 
HETATM 9490  O  O   B HOH G 5 .    ? 50.959 58.718  -9.920  0.50 18.04 ? 1915 HOH A O   1 
HETATM 9491  O  O   . HOH G 5 .    ? 49.797 57.503  -7.526  1.00 11.61 ? 1916 HOH A O   1 
HETATM 9492  O  O   . HOH G 5 .    ? 51.426 56.556  -5.576  1.00 8.33  ? 1917 HOH A O   1 
HETATM 9493  O  O   . HOH G 5 .    ? 52.169 54.040  -4.800  1.00 7.60  ? 1918 HOH A O   1 
HETATM 9494  O  O   . HOH G 5 .    ? 52.665 58.801  -1.736  1.00 13.74 ? 1919 HOH A O   1 
HETATM 9495  O  O   . HOH G 5 .    ? 56.929 60.969  1.628   1.00 15.82 ? 1920 HOH A O   1 
HETATM 9496  O  O   . HOH G 5 .    ? 55.979 66.851  5.449   1.00 29.01 ? 1921 HOH A O   1 
HETATM 9497  O  O   . HOH G 5 .    ? 55.127 68.348  3.614   1.00 28.32 ? 1922 HOH A O   1 
HETATM 9498  O  O   . HOH G 5 .    ? 53.474 69.325  2.350   1.00 30.76 ? 1923 HOH A O   1 
HETATM 9499  O  O   . HOH G 5 .    ? 51.119 68.813  3.379   1.00 27.42 ? 1924 HOH A O   1 
HETATM 9500  O  O   . HOH G 5 .    ? 49.751 67.233  4.416   1.00 17.33 ? 1925 HOH A O   1 
HETATM 9501  O  O   . HOH G 5 .    ? 49.392 68.288  6.766   1.00 27.10 ? 1926 HOH A O   1 
HETATM 9502  O  O   . HOH G 5 .    ? 51.095 66.319  8.335   1.00 21.96 ? 1927 HOH A O   1 
HETATM 9503  O  O   A HOH G 5 .    ? 52.874 67.784  9.089   0.50 21.49 ? 1928 HOH A O   1 
HETATM 9504  O  O   B HOH G 5 .    ? 54.002 66.312  8.645   0.50 35.88 ? 1928 HOH A O   1 
HETATM 9505  O  O   . HOH G 5 .    ? 55.685 67.186  10.455  1.00 34.10 ? 1929 HOH A O   1 
HETATM 9506  O  O   . HOH G 5 .    ? 55.388 67.469  13.526  1.00 29.77 ? 1930 HOH A O   1 
HETATM 9507  O  O   . HOH G 5 .    ? 57.151 69.157  13.675  1.00 33.84 ? 1931 HOH A O   1 
HETATM 9508  O  O   . HOH G 5 .    ? 54.221 73.342  16.145  1.00 36.00 ? 1932 HOH A O   1 
HETATM 9509  O  O   . HOH G 5 .    ? 53.350 75.905  15.920  1.00 39.85 ? 1933 HOH A O   1 
HETATM 9510  O  O   . HOH G 5 .    ? 50.739 76.323  14.468  1.00 21.51 ? 1934 HOH A O   1 
HETATM 9511  O  O   . HOH G 5 .    ? 51.568 77.433  11.919  1.00 38.27 ? 1935 HOH A O   1 
HETATM 9512  O  O   . HOH G 5 .    ? 51.603 74.497  8.626   1.00 41.72 ? 1936 HOH A O   1 
HETATM 9513  O  O   A HOH G 5 .    ? 50.254 72.210  9.196   0.50 12.08 ? 1937 HOH A O   1 
HETATM 9514  O  O   B HOH G 5 .    ? 50.678 71.372  7.988   0.50 17.94 ? 1937 HOH A O   1 
HETATM 9515  O  O   A HOH G 5 .    ? 52.449 70.735  8.797   0.50 19.32 ? 1938 HOH A O   1 
HETATM 9516  O  O   B HOH G 5 .    ? 51.510 69.207  9.254   0.50 22.92 ? 1938 HOH A O   1 
HETATM 9517  O  O   . HOH G 5 .    ? 52.273 70.933  5.840   1.00 38.41 ? 1939 HOH A O   1 
HETATM 9518  O  O   . HOH G 5 .    ? 52.564 73.019  4.004   1.00 28.56 ? 1940 HOH A O   1 
HETATM 9519  O  O   . HOH G 5 .    ? 52.610 75.037  1.785   1.00 30.76 ? 1941 HOH A O   1 
HETATM 9520  O  O   . HOH G 5 .    ? 54.947 75.507  2.421   1.00 36.60 ? 1942 HOH A O   1 
HETATM 9521  O  O   . HOH G 5 .    ? 56.459 76.096  0.352   1.00 33.92 ? 1943 HOH A O   1 
HETATM 9522  O  O   . HOH G 5 .    ? 61.821 76.280  1.670   1.00 38.91 ? 1944 HOH A O   1 
HETATM 9523  O  O   . HOH G 5 .    ? 63.985 77.072  0.215   1.00 34.18 ? 1945 HOH A O   1 
HETATM 9524  O  O   . HOH G 5 .    ? 59.540 71.252  0.234   1.00 33.09 ? 1946 HOH A O   1 
HETATM 9525  O  O   . HOH G 5 .    ? 58.739 70.359  3.233   1.00 37.31 ? 1947 HOH A O   1 
HETATM 9526  O  O   . HOH G 5 .    ? 59.186 68.164  2.574   1.00 20.44 ? 1948 HOH A O   1 
HETATM 9527  O  O   . HOH G 5 .    ? 64.024 70.611  -5.185  1.00 14.20 ? 1949 HOH A O   1 
HETATM 9528  O  O   . HOH G 5 .    ? 64.665 70.573  -7.825  1.00 36.09 ? 1950 HOH A O   1 
HETATM 9529  O  O   . HOH G 5 .    ? 66.462 71.507  -6.717  1.00 19.83 ? 1951 HOH A O   1 
HETATM 9530  O  O   . HOH G 5 .    ? 70.000 69.961  -12.491 1.00 11.53 ? 1952 HOH A O   1 
HETATM 9531  O  O   . HOH G 5 .    ? 74.652 76.086  -14.441 1.00 24.70 ? 1953 HOH A O   1 
HETATM 9532  O  O   . HOH G 5 .    ? 77.154 76.171  -11.844 1.00 34.32 ? 1954 HOH A O   1 
HETATM 9533  O  O   . HOH G 5 .    ? 78.001 72.050  -10.190 1.00 30.16 ? 1955 HOH A O   1 
HETATM 9534  O  O   . HOH G 5 .    ? 73.879 80.201  -10.879 1.00 40.96 ? 1956 HOH A O   1 
HETATM 9535  O  O   . HOH G 5 .    ? 59.736 83.613  -14.148 1.00 44.38 ? 1957 HOH A O   1 
HETATM 9536  O  O   . HOH G 5 .    ? 59.697 83.671  -16.725 1.00 36.90 ? 1958 HOH A O   1 
HETATM 9537  O  O   . HOH G 5 .    ? 54.786 80.974  -23.678 1.00 14.41 ? 1959 HOH A O   1 
HETATM 9538  O  O   . HOH G 5 .    ? 52.477 91.914  -23.482 1.00 36.21 ? 1960 HOH A O   1 
HETATM 9539  O  O   . HOH G 5 .    ? 54.163 93.312  -24.881 1.00 35.71 ? 1961 HOH A O   1 
HETATM 9540  O  O   . HOH G 5 .    ? 51.018 95.902  -26.483 1.00 28.42 ? 1962 HOH A O   1 
HETATM 9541  O  O   . HOH G 5 .    ? 48.402 95.326  -27.164 1.00 19.36 ? 1963 HOH A O   1 
HETATM 9542  O  O   . HOH G 5 .    ? 45.211 94.990  -26.560 1.00 34.09 ? 1964 HOH A O   1 
HETATM 9543  O  O   . HOH G 5 .    ? 45.067 92.530  -25.538 1.00 39.59 ? 1965 HOH A O   1 
HETATM 9544  O  O   . HOH G 5 .    ? 43.405 93.369  -23.974 1.00 38.03 ? 1966 HOH A O   1 
HETATM 9545  O  O   . HOH G 5 .    ? 45.043 89.977  -25.545 1.00 16.94 ? 1967 HOH A O   1 
HETATM 9546  O  O   . HOH G 5 .    ? 46.855 89.144  -23.310 1.00 44.42 ? 1968 HOH A O   1 
HETATM 9547  O  O   . HOH G 5 .    ? 49.387 91.951  -24.784 1.00 32.03 ? 1969 HOH A O   1 
HETATM 9548  O  O   . HOH G 5 .    ? 48.180 89.218  -30.919 1.00 12.13 ? 1970 HOH A O   1 
HETATM 9549  O  O   . HOH G 5 .    ? 44.442 95.631  -30.497 1.00 26.69 ? 1971 HOH A O   1 
HETATM 9550  O  O   . HOH G 5 .    ? 42.304 94.528  -30.229 1.00 41.22 ? 1972 HOH A O   1 
HETATM 9551  O  O   . HOH G 5 .    ? 37.238 96.582  -30.793 1.00 40.73 ? 1973 HOH A O   1 
HETATM 9552  O  O   . HOH G 5 .    ? 34.965 94.765  -32.309 1.00 23.89 ? 1974 HOH A O   1 
HETATM 9553  O  O   . HOH G 5 .    ? 33.711 93.424  -30.313 1.00 41.32 ? 1975 HOH A O   1 
HETATM 9554  O  O   . HOH G 5 .    ? 36.063 93.483  -29.776 1.00 31.65 ? 1976 HOH A O   1 
HETATM 9555  O  O   . HOH G 5 .    ? 31.802 96.485  -27.398 1.00 40.34 ? 1977 HOH A O   1 
HETATM 9556  O  O   . HOH G 5 .    ? 27.821 97.656  -28.551 1.00 45.89 ? 1978 HOH A O   1 
HETATM 9557  O  O   . HOH G 5 .    ? 26.754 99.153  -26.373 1.00 36.59 ? 1979 HOH A O   1 
HETATM 9558  O  O   . HOH G 5 .    ? 25.124 97.526  -31.754 1.00 44.38 ? 1980 HOH A O   1 
HETATM 9559  O  O   . HOH G 5 .    ? 27.794 93.481  -29.815 1.00 38.80 ? 1981 HOH A O   1 
HETATM 9560  O  O   . HOH G 5 .    ? 26.805 91.609  -27.619 1.00 26.31 ? 1982 HOH A O   1 
HETATM 9561  O  O   . HOH G 5 .    ? 24.630 92.927  -28.122 1.00 37.42 ? 1983 HOH A O   1 
HETATM 9562  O  O   . HOH G 5 .    ? 23.981 90.917  -26.040 1.00 35.68 ? 1984 HOH A O   1 
HETATM 9563  O  O   . HOH G 5 .    ? 25.122 88.558  -25.422 1.00 29.44 ? 1985 HOH A O   1 
HETATM 9564  O  O   . HOH G 5 .    ? 26.797 87.719  -23.765 1.00 21.49 ? 1986 HOH A O   1 
HETATM 9565  O  O   . HOH G 5 .    ? 28.033 90.772  -25.310 1.00 17.31 ? 1987 HOH A O   1 
HETATM 9566  O  O   . HOH G 5 .    ? 29.509 88.661  -26.196 1.00 10.17 ? 1988 HOH A O   1 
HETATM 9567  O  O   . HOH G 5 .    ? 27.040 89.824  -31.702 1.00 38.07 ? 1989 HOH A O   1 
HETATM 9568  O  O   . HOH G 5 .    ? 25.555 91.438  -32.781 1.00 29.91 ? 1990 HOH A O   1 
HETATM 9569  O  O   . HOH G 5 .    ? 23.258 86.877  -32.578 1.00 26.39 ? 1991 HOH A O   1 
HETATM 9570  O  O   . HOH G 5 .    ? 25.605 85.993  -31.905 1.00 14.93 ? 1992 HOH A O   1 
HETATM 9571  O  O   . HOH G 5 .    ? 21.409 85.865  -30.897 1.00 31.29 ? 1993 HOH A O   1 
HETATM 9572  O  O   . HOH G 5 .    ? 19.071 83.262  -25.766 1.00 26.97 ? 1994 HOH A O   1 
HETATM 9573  O  O   . HOH G 5 .    ? 16.818 85.227  -24.075 1.00 39.64 ? 1995 HOH A O   1 
HETATM 9574  O  O   . HOH G 5 .    ? 13.928 88.096  -20.007 1.00 30.11 ? 1996 HOH A O   1 
HETATM 9575  O  O   . HOH G 5 .    ? 14.669 83.499  -18.866 1.00 41.36 ? 1997 HOH A O   1 
HETATM 9576  O  O   . HOH G 5 .    ? 17.353 81.041  -16.862 1.00 35.00 ? 1998 HOH A O   1 
HETATM 9577  O  O   . HOH G 5 .    ? 19.517 84.152  -18.346 1.00 28.53 ? 1999 HOH A O   1 
HETATM 9578  O  O   . HOH G 5 .    ? 21.584 86.176  -19.102 1.00 25.82 ? 2000 HOH A O   1 
HETATM 9579  O  O   . HOH G 5 .    ? 22.752 88.456  -18.774 1.00 33.76 ? 2001 HOH A O   1 
HETATM 9580  O  O   . HOH G 5 .    ? 23.166 85.356  -16.866 1.00 31.40 ? 2002 HOH A O   1 
HETATM 9581  O  O   . HOH G 5 .    ? 24.827 83.057  -16.907 1.00 22.89 ? 2003 HOH A O   1 
HETATM 9582  O  O   . HOH G 5 .    ? 25.323 87.382  -15.994 1.00 42.72 ? 2004 HOH A O   1 
HETATM 9583  O  O   . HOH G 5 .    ? 27.487 86.294  -14.993 1.00 32.59 ? 2005 HOH A O   1 
HETATM 9584  O  O   . HOH G 5 .    ? 28.901 86.647  -13.301 1.00 34.41 ? 2006 HOH A O   1 
HETATM 9585  O  O   . HOH G 5 .    ? 30.269 87.084  -15.084 1.00 22.74 ? 2007 HOH A O   1 
HETATM 9586  O  O   . HOH G 5 .    ? 29.691 87.203  -17.859 1.00 23.35 ? 2008 HOH A O   1 
HETATM 9587  O  O   . HOH G 5 .    ? 31.547 85.740  -19.775 1.00 20.46 ? 2009 HOH A O   1 
HETATM 9588  O  O   . HOH G 5 .    ? 32.754 87.947  -18.937 1.00 53.84 ? 2010 HOH A O   1 
HETATM 9589  O  O   . HOH G 5 .    ? 35.118 87.791  -19.744 1.00 33.32 ? 2011 HOH A O   1 
HETATM 9590  O  O   . HOH G 5 .    ? 35.309 86.057  -17.922 1.00 27.70 ? 2012 HOH A O   1 
HETATM 9591  O  O   . HOH G 5 .    ? 33.393 84.244  -18.291 1.00 17.34 ? 2013 HOH A O   1 
HETATM 9592  O  O   . HOH G 5 .    ? 37.254 86.273  -15.948 1.00 35.64 ? 2014 HOH A O   1 
HETATM 9593  O  O   . HOH G 5 .    ? 40.627 85.282  -12.702 1.00 35.32 ? 2015 HOH A O   1 
HETATM 9594  O  O   . HOH G 5 .    ? 40.443 82.733  -10.962 1.00 18.09 ? 2016 HOH A O   1 
HETATM 9595  O  O   . HOH G 5 .    ? 35.587 85.881  -8.278  1.00 35.91 ? 2017 HOH A O   1 
HETATM 9596  O  O   . HOH G 5 .    ? 33.956 86.895  -10.446 1.00 31.46 ? 2018 HOH A O   1 
HETATM 9597  O  O   . HOH G 5 .    ? 27.482 88.666  -12.298 1.00 32.79 ? 2019 HOH A O   1 
HETATM 9598  O  O   . HOH G 5 .    ? 21.314 85.985  -10.574 1.00 34.81 ? 2020 HOH A O   1 
HETATM 9599  O  O   . HOH G 5 .    ? 21.121 83.692  -12.482 1.00 31.01 ? 2021 HOH A O   1 
HETATM 9600  O  O   . HOH G 5 .    ? 18.860 80.583  -11.676 1.00 29.28 ? 2022 HOH A O   1 
HETATM 9601  O  O   . HOH G 5 .    ? 13.643 80.377  -5.970  1.00 32.37 ? 2023 HOH A O   1 
HETATM 9602  O  O   . HOH G 5 .    ? 16.866 74.401  -3.039  1.00 11.22 ? 2024 HOH A O   1 
HETATM 9603  O  O   . HOH G 5 .    ? 20.092 74.187  -6.861  1.00 10.65 ? 2025 HOH A O   1 
HETATM 9604  O  O   . HOH G 5 .    ? 24.633 70.444  -8.758  1.00 12.11 ? 2026 HOH A O   1 
HETATM 9605  O  O   . HOH G 5 .    ? 26.790 68.784  -9.248  1.00 7.88  ? 2027 HOH A O   1 
HETATM 9606  O  O   . HOH G 5 .    ? 32.571 64.706  -9.875  1.00 18.02 ? 2028 HOH A O   1 
HETATM 9607  O  O   . HOH G 5 .    ? 34.294 58.515  -8.811  1.00 7.52  ? 2029 HOH A O   1 
HETATM 9608  O  O   . HOH G 5 .    ? 30.279 58.329  -11.817 1.00 6.22  ? 2030 HOH A O   1 
HETATM 9609  O  O   . HOH G 5 .    ? 23.256 54.237  -8.585  1.00 27.79 ? 2031 HOH A O   1 
HETATM 9610  O  O   . HOH G 5 .    ? 23.083 51.702  -8.573  1.00 13.06 ? 2032 HOH A O   1 
HETATM 9611  O  O   . HOH G 5 .    ? 25.657 51.098  -9.492  1.00 11.28 ? 2033 HOH A O   1 
HETATM 9612  O  O   . HOH G 5 .    ? 24.243 53.065  -6.346  1.00 15.46 ? 2034 HOH A O   1 
HETATM 9613  O  O   . HOH G 5 .    ? 23.365 53.813  -3.729  1.00 11.88 ? 2035 HOH A O   1 
HETATM 9614  O  O   . HOH G 5 .    ? 24.335 55.444  -1.819  1.00 12.08 ? 2036 HOH A O   1 
HETATM 9615  O  O   . HOH G 5 .    ? 20.669 57.223  -5.287  1.00 7.97  ? 2037 HOH A O   1 
HETATM 9616  O  O   . HOH G 5 .    ? 21.549 57.812  -7.817  1.00 7.38  ? 2038 HOH A O   1 
HETATM 9617  O  O   . HOH G 5 .    ? 19.880 57.330  -11.798 1.00 12.97 ? 2039 HOH A O   1 
HETATM 9618  O  O   . HOH G 5 .    ? 20.376 58.630  -21.948 1.00 8.89  ? 2040 HOH A O   1 
HETATM 9619  O  O   . HOH G 5 .    ? 23.851 55.390  -23.440 1.00 7.22  ? 2041 HOH A O   1 
HETATM 9620  O  O   . HOH G 5 .    ? 22.964 52.933  -24.427 1.00 10.08 ? 2042 HOH A O   1 
HETATM 9621  O  O   . HOH G 5 .    ? 20.254 52.531  -24.305 1.00 12.88 ? 2043 HOH A O   1 
HETATM 9622  O  O   . HOH G 5 .    ? 19.069 50.303  -23.506 1.00 32.30 ? 2044 HOH A O   1 
HETATM 9623  O  O   . HOH G 5 .    ? 21.639 48.734  -22.536 1.00 31.94 ? 2045 HOH A O   1 
HETATM 9624  O  O   . HOH G 5 .    ? 23.993 48.310  -24.072 1.00 29.57 ? 2046 HOH A O   1 
HETATM 9625  O  O   . HOH G 5 .    ? 24.823 50.912  -24.070 1.00 11.63 ? 2047 HOH A O   1 
HETATM 9626  O  O   . HOH G 5 .    ? 26.959 47.516  -23.880 1.00 30.59 ? 2048 HOH A O   1 
HETATM 9627  O  O   . HOH G 5 .    ? 27.723 48.382  -21.802 1.00 13.19 ? 2049 HOH A O   1 
HETATM 9628  O  O   . HOH G 5 .    ? 25.402 46.796  -20.900 1.00 23.92 ? 2050 HOH A O   1 
HETATM 9629  O  O   . HOH G 5 .    ? 28.827 49.608  -24.338 1.00 14.09 ? 2051 HOH A O   1 
HETATM 9630  O  O   . HOH G 5 .    ? 31.393 49.836  -24.072 1.00 10.27 ? 2052 HOH A O   1 
HETATM 9631  O  O   . HOH G 5 .    ? 34.164 56.223  -26.275 1.00 9.13  ? 2053 HOH A O   1 
HETATM 9632  O  O   . HOH G 5 .    ? 32.223 58.497  -28.473 1.00 10.65 ? 2054 HOH A O   1 
HETATM 9633  O  O   . HOH G 5 .    ? 31.924 51.062  -35.474 1.00 19.59 ? 2055 HOH A O   1 
HETATM 9634  O  O   . HOH G 5 .    ? 35.004 48.741  -37.985 1.00 43.96 ? 2056 HOH A O   1 
HETATM 9635  O  O   . HOH G 5 .    ? 38.328 46.292  -39.952 1.00 40.71 ? 2057 HOH A O   1 
HETATM 9636  O  O   . HOH G 5 .    ? 26.600 46.281  -37.343 1.00 42.42 ? 2058 HOH A O   1 
HETATM 9637  O  O   . HOH G 5 .    ? 28.212 47.028  -31.601 1.00 24.93 ? 2059 HOH A O   1 
HETATM 9638  O  O   . HOH G 5 .    ? 28.677 43.932  -29.768 1.00 31.28 ? 2060 HOH A O   1 
HETATM 9639  O  O   . HOH G 5 .    ? 29.428 42.050  -28.271 1.00 33.17 ? 2061 HOH A O   1 
HETATM 9640  O  O   . HOH G 5 .    ? 29.529 41.033  -25.608 1.00 22.41 ? 2062 HOH A O   1 
HETATM 9641  O  O   . HOH G 5 .    ? 28.742 38.771  -24.736 1.00 37.90 ? 2063 HOH A O   1 
HETATM 9642  O  O   . HOH G 5 .    ? 27.688 38.680  -22.585 1.00 29.14 ? 2064 HOH A O   1 
HETATM 9643  O  O   . HOH G 5 .    ? 28.610 41.205  -21.686 1.00 13.05 ? 2065 HOH A O   1 
HETATM 9644  O  O   . HOH G 5 .    ? 27.488 36.511  -19.799 1.00 24.14 ? 2066 HOH A O   1 
HETATM 9645  O  O   . HOH G 5 .    ? 25.504 35.638  -18.085 1.00 30.36 ? 2067 HOH A O   1 
HETATM 9646  O  O   . HOH G 5 .    ? 25.302 36.362  -15.310 1.00 31.57 ? 2068 HOH A O   1 
HETATM 9647  O  O   . HOH G 5 .    ? 22.934 38.825  -15.845 1.00 45.03 ? 2069 HOH A O   1 
HETATM 9648  O  O   . HOH G 5 .    ? 20.147 37.042  -16.961 1.00 46.67 ? 2070 HOH A O   1 
HETATM 9649  O  O   . HOH G 5 .    ? 23.970 38.953  -21.116 1.00 36.27 ? 2071 HOH A O   1 
HETATM 9650  O  O   . HOH G 5 .    ? 29.365 34.913  -16.398 1.00 24.43 ? 2072 HOH A O   1 
HETATM 9651  O  O   . HOH G 5 .    ? 30.391 35.066  -12.410 1.00 19.67 ? 2073 HOH A O   1 
HETATM 9652  O  O   . HOH G 5 .    ? 30.528 34.738  -9.763  1.00 27.99 ? 2074 HOH A O   1 
HETATM 9653  O  O   . HOH G 5 .    ? 33.273 32.300  -9.546  1.00 40.46 ? 2075 HOH A O   1 
HETATM 9654  O  O   . HOH G 5 .    ? 30.432 33.423  -6.229  1.00 31.21 ? 2076 HOH A O   1 
HETATM 9655  O  O   . HOH G 5 .    ? 28.265 35.234  -6.813  1.00 17.39 ? 2077 HOH A O   1 
HETATM 9656  O  O   . HOH G 5 .    ? 25.407 34.383  -7.466  1.00 29.67 ? 2078 HOH A O   1 
HETATM 9657  O  O   . HOH G 5 .    ? 21.443 35.362  -5.387  1.00 33.97 ? 2079 HOH A O   1 
HETATM 9658  O  O   . HOH G 5 .    ? 21.481 36.724  -7.934  1.00 39.29 ? 2080 HOH A O   1 
HETATM 9659  O  O   . HOH G 5 .    ? 25.961 33.494  -2.783  1.00 35.17 ? 2081 HOH A O   1 
HETATM 9660  O  O   . HOH G 5 .    ? 21.102 34.964  5.629   1.00 43.47 ? 2082 HOH A O   1 
HETATM 9661  O  O   . HOH G 5 .    ? 18.459 36.716  5.714   1.00 26.45 ? 2083 HOH A O   1 
HETATM 9662  O  O   . HOH G 5 .    ? 16.190 37.865  6.058   1.00 37.00 ? 2084 HOH A O   1 
HETATM 9663  O  O   . HOH G 5 .    ? 14.925 40.580  8.775   1.00 40.13 ? 2085 HOH A O   1 
HETATM 9664  O  O   . HOH G 5 .    ? 17.279 41.419  9.278   1.00 24.30 ? 2086 HOH A O   1 
HETATM 9665  O  O   . HOH G 5 .    ? 14.408 40.144  12.393  1.00 37.15 ? 2087 HOH A O   1 
HETATM 9666  O  O   . HOH G 5 .    ? 12.886 42.345  12.482  1.00 16.48 ? 2088 HOH A O   1 
HETATM 9667  O  O   . HOH G 5 .    ? 10.052 41.960  11.927  1.00 32.12 ? 2089 HOH A O   1 
HETATM 9668  O  O   . HOH G 5 .    ? 8.574  44.543  12.952  1.00 30.48 ? 2090 HOH A O   1 
HETATM 9669  O  O   . HOH G 5 .    ? 8.037  47.843  11.702  1.00 23.16 ? 2091 HOH A O   1 
HETATM 9670  O  O   . HOH G 5 .    ? 7.634  50.628  12.450  1.00 35.75 ? 2092 HOH A O   1 
HETATM 9671  O  O   . HOH G 5 .    ? 6.371  52.276  15.430  1.00 40.43 ? 2093 HOH A O   1 
HETATM 9672  O  O   . HOH G 5 .    ? 7.396  54.177  17.092  1.00 33.55 ? 2094 HOH A O   1 
HETATM 9673  O  O   . HOH G 5 .    ? 8.658  56.482  16.541  1.00 41.01 ? 2095 HOH A O   1 
HETATM 9674  O  O   . HOH G 5 .    ? 9.352  58.750  17.483  1.00 34.64 ? 2096 HOH A O   1 
HETATM 9675  O  O   . HOH G 5 .    ? 34.312 67.491  12.278  1.00 12.96 ? 2097 HOH A O   1 
HETATM 9676  O  O   . HOH G 5 .    ? 36.215 65.608  12.212  1.00 33.62 ? 2098 HOH A O   1 
HETATM 9677  O  O   . HOH G 5 .    ? 34.580 70.237  12.985  1.00 13.76 ? 2099 HOH A O   1 
HETATM 9678  O  O   . HOH G 5 .    ? 35.156 73.293  18.687  1.00 41.85 ? 2100 HOH A O   1 
HETATM 9679  O  O   . HOH G 5 .    ? 37.981 73.613  18.123  1.00 30.50 ? 2101 HOH A O   1 
HETATM 9680  O  O   . HOH G 5 .    ? 38.116 77.066  17.690  1.00 42.69 ? 2102 HOH A O   1 
HETATM 9681  O  O   . HOH G 5 .    ? 39.400 77.934  19.649  1.00 38.21 ? 2103 HOH A O   1 
HETATM 9682  O  O   . HOH G 5 .    ? 42.178 73.950  22.768  1.00 42.34 ? 2104 HOH A O   1 
HETATM 9683  O  O   . HOH G 5 .    ? 45.321 74.089  22.668  1.00 31.75 ? 2105 HOH A O   1 
HETATM 9684  O  O   . HOH G 5 .    ? 49.152 74.419  23.011  1.00 42.88 ? 2106 HOH A O   1 
HETATM 9685  O  O   . HOH G 5 .    ? 48.686 72.576  24.853  1.00 44.35 ? 2107 HOH A O   1 
HETATM 9686  O  O   . HOH G 5 .    ? 50.024 68.366  23.640  1.00 45.07 ? 2108 HOH A O   1 
HETATM 9687  O  O   . HOH G 5 .    ? 52.462 67.472  22.788  1.00 48.07 ? 2109 HOH A O   1 
HETATM 9688  O  O   . HOH G 5 .    ? 53.258 66.153  20.162  1.00 39.19 ? 2110 HOH A O   1 
HETATM 9689  O  O   . HOH G 5 .    ? 52.745 69.503  18.323  1.00 21.83 ? 2111 HOH A O   1 
HETATM 9690  O  O   . HOH G 5 .    ? 52.449 72.474  18.149  1.00 25.51 ? 2112 HOH A O   1 
HETATM 9691  O  O   . HOH G 5 .    ? 57.726 69.250  20.104  1.00 36.91 ? 2113 HOH A O   1 
HETATM 9692  O  O   . HOH G 5 .    ? 57.204 67.277  22.808  1.00 32.52 ? 2114 HOH A O   1 
HETATM 9693  O  O   . HOH G 5 .    ? 56.827 64.727  24.279  1.00 26.95 ? 2115 HOH A O   1 
HETATM 9694  O  O   . HOH G 5 .    ? 59.175 62.318  25.697  1.00 30.18 ? 2116 HOH A O   1 
HETATM 9695  O  O   . HOH G 5 .    ? 58.176 61.899  28.001  1.00 40.12 ? 2117 HOH A O   1 
HETATM 9696  O  O   . HOH G 5 .    ? 62.224 62.421  25.481  1.00 31.21 ? 2118 HOH A O   1 
HETATM 9697  O  O   . HOH G 5 .    ? 63.212 57.280  25.875  1.00 34.23 ? 2119 HOH A O   1 
HETATM 9698  O  O   . HOH G 5 .    ? 61.710 55.897  27.722  1.00 35.80 ? 2120 HOH A O   1 
HETATM 9699  O  O   . HOH G 5 .    ? 59.066 55.617  27.148  1.00 25.86 ? 2121 HOH A O   1 
HETATM 9700  O  O   . HOH G 5 .    ? 57.907 52.906  26.316  1.00 28.05 ? 2122 HOH A O   1 
HETATM 9701  O  O   . HOH G 5 .    ? 55.584 52.135  27.342  1.00 31.09 ? 2123 HOH A O   1 
HETATM 9702  O  O   . HOH G 5 .    ? 53.170 52.689  26.373  1.00 28.12 ? 2124 HOH A O   1 
HETATM 9703  O  O   . HOH G 5 .    ? 52.050 49.800  26.476  1.00 37.05 ? 2125 HOH A O   1 
HETATM 9704  O  O   . HOH G 5 .    ? 48.996 49.749  28.297  1.00 17.99 ? 2126 HOH A O   1 
HETATM 9705  O  O   . HOH G 5 .    ? 49.711 47.300  29.096  1.00 25.92 ? 2127 HOH A O   1 
HETATM 9706  O  O   . HOH G 5 .    ? 49.179 50.587  32.667  1.00 30.36 ? 2128 HOH A O   1 
HETATM 9707  O  O   . HOH G 5 .    ? 46.858 53.218  35.723  1.00 43.55 ? 2129 HOH A O   1 
HETATM 9708  O  O   . HOH G 5 .    ? 42.508 53.145  35.512  1.00 19.37 ? 2130 HOH A O   1 
HETATM 9709  O  O   . HOH G 5 .    ? 40.004 52.810  36.323  1.00 29.04 ? 2131 HOH A O   1 
HETATM 9710  O  O   . HOH G 5 .    ? 39.193 49.881  36.435  1.00 37.34 ? 2132 HOH A O   1 
HETATM 9711  O  O   . HOH G 5 .    ? 41.196 50.340  33.186  1.00 23.50 ? 2133 HOH A O   1 
HETATM 9712  O  O   . HOH G 5 .    ? 41.863 48.765  31.235  1.00 19.62 ? 2134 HOH A O   1 
HETATM 9713  O  O   . HOH G 5 .    ? 39.194 49.275  30.098  1.00 23.34 ? 2135 HOH A O   1 
HETATM 9714  O  O   . HOH G 5 .    ? 42.308 46.197  32.806  1.00 38.44 ? 2136 HOH A O   1 
HETATM 9715  O  O   . HOH G 5 .    ? 34.260 51.110  35.959  1.00 36.04 ? 2137 HOH A O   1 
HETATM 9716  O  O   . HOH G 5 .    ? 31.492 57.302  37.432  1.00 25.46 ? 2138 HOH A O   1 
HETATM 9717  O  O   . HOH G 5 .    ? 30.097 57.542  39.817  1.00 33.49 ? 2139 HOH A O   1 
HETATM 9718  O  O   . HOH G 5 .    ? 29.788 59.418  34.828  1.00 27.94 ? 2140 HOH A O   1 
HETATM 9719  O  O   . HOH G 5 .    ? 33.996 59.762  35.004  1.00 34.82 ? 2141 HOH A O   1 
HETATM 9720  O  O   . HOH G 5 .    ? 35.667 58.678  36.756  1.00 40.53 ? 2142 HOH A O   1 
HETATM 9721  O  O   . HOH G 5 .    ? 38.380 58.372  36.773  1.00 39.15 ? 2143 HOH A O   1 
HETATM 9722  O  O   . HOH G 5 .    ? 41.689 58.433  34.537  1.00 26.67 ? 2144 HOH A O   1 
HETATM 9723  O  O   . HOH G 5 .    ? 43.371 56.626  33.615  1.00 27.13 ? 2145 HOH A O   1 
HETATM 9724  O  O   . HOH G 5 .    ? 45.349 58.053  32.470  1.00 33.05 ? 2146 HOH A O   1 
HETATM 9725  O  O   . HOH G 5 .    ? 41.810 61.545  33.519  1.00 38.89 ? 2147 HOH A O   1 
HETATM 9726  O  O   . HOH G 5 .    ? 37.400 62.129  35.574  1.00 29.25 ? 2148 HOH A O   1 
HETATM 9727  O  O   . HOH G 5 .    ? 35.208 62.310  34.092  1.00 24.32 ? 2149 HOH A O   1 
HETATM 9728  O  O   . HOH G 5 .    ? 38.497 66.448  36.751  1.00 42.81 ? 2150 HOH A O   1 
HETATM 9729  O  O   . HOH G 5 .    ? 38.764 68.512  35.357  1.00 36.19 ? 2151 HOH A O   1 
HETATM 9730  O  O   . HOH G 5 .    ? 40.699 66.774  34.148  1.00 35.71 ? 2152 HOH A O   1 
HETATM 9731  O  O   . HOH G 5 .    ? 39.703 67.022  31.300  1.00 20.02 ? 2153 HOH A O   1 
HETATM 9732  O  O   . HOH G 5 .    ? 41.772 67.440  29.259  1.00 22.20 ? 2154 HOH A O   1 
HETATM 9733  O  O   . HOH G 5 .    ? 44.401 67.797  28.123  1.00 36.69 ? 2155 HOH A O   1 
HETATM 9734  O  O   . HOH G 5 .    ? 46.394 68.537  26.465  1.00 25.71 ? 2156 HOH A O   1 
HETATM 9735  O  O   . HOH G 5 .    ? 47.604 66.012  26.896  1.00 26.91 ? 2157 HOH A O   1 
HETATM 9736  O  O   . HOH G 5 .    ? 50.608 61.901  26.508  1.00 17.42 ? 2158 HOH A O   1 
HETATM 9737  O  O   . HOH G 5 .    ? 51.861 60.165  28.110  1.00 28.94 ? 2159 HOH A O   1 
HETATM 9738  O  O   . HOH G 5 .    ? 51.824 63.737  24.660  1.00 29.11 ? 2160 HOH A O   1 
HETATM 9739  O  O   . HOH G 5 .    ? 42.104 69.070  26.339  1.00 39.84 ? 2161 HOH A O   1 
HETATM 9740  O  O   . HOH G 5 .    ? 42.723 71.613  25.828  1.00 50.70 ? 2162 HOH A O   1 
HETATM 9741  O  O   . HOH G 5 .    ? 45.294 77.785  16.200  1.00 38.44 ? 2163 HOH A O   1 
HETATM 9742  O  O   . HOH G 5 .    ? 46.848 77.206  14.257  1.00 34.63 ? 2164 HOH A O   1 
HETATM 9743  O  O   . HOH G 5 .    ? 46.913 78.383  12.028  1.00 28.12 ? 2165 HOH A O   1 
HETATM 9744  O  O   . HOH G 5 .    ? 45.865 77.674  9.537   1.00 19.32 ? 2166 HOH A O   1 
HETATM 9745  O  O   . HOH G 5 .    ? 48.112 76.493  8.195   1.00 29.51 ? 2167 HOH A O   1 
HETATM 9746  O  O   . HOH G 5 .    ? 46.515 74.447  7.840   1.00 10.99 ? 2168 HOH A O   1 
HETATM 9747  O  O   . HOH G 5 .    ? 43.386 73.120  5.875   1.00 9.68  ? 2169 HOH A O   1 
HETATM 9748  O  O   . HOH G 5 .    ? 49.166 76.343  5.512   1.00 28.13 ? 2170 HOH A O   1 
HETATM 9749  O  O   . HOH G 5 .    ? 48.514 77.721  3.492   1.00 39.90 ? 2171 HOH A O   1 
HETATM 9750  O  O   . HOH G 5 .    ? 50.570 77.164  2.115   1.00 29.55 ? 2172 HOH A O   1 
HETATM 9751  O  O   . HOH G 5 .    ? 51.350 80.094  0.845   1.00 33.99 ? 2173 HOH A O   1 
HETATM 9752  O  O   . HOH G 5 .    ? 51.185 79.286  -1.687  1.00 20.50 ? 2174 HOH A O   1 
HETATM 9753  O  O   . HOH G 5 .    ? 44.681 80.716  -1.440  1.00 31.78 ? 2175 HOH A O   1 
HETATM 9754  O  O   . HOH G 5 .    ? 45.919 79.535  5.147   1.00 25.53 ? 2176 HOH A O   1 
HETATM 9755  O  O   . HOH G 5 .    ? 43.214 80.537  5.442   1.00 20.47 ? 2177 HOH A O   1 
HETATM 9756  O  O   . HOH G 5 .    ? 40.893 81.490  11.333  1.00 37.74 ? 2178 HOH A O   1 
HETATM 9757  O  O   . HOH G 5 .    ? 38.553 80.124  12.788  1.00 48.72 ? 2179 HOH A O   1 
HETATM 9758  O  O   . HOH G 5 .    ? 31.250 81.415  0.532   1.00 16.93 ? 2180 HOH A O   1 
HETATM 9759  O  O   . HOH G 5 .    ? 30.269 85.624  1.596   1.00 25.81 ? 2181 HOH A O   1 
HETATM 9760  O  O   . HOH G 5 .    ? 24.644 85.408  7.834   1.00 30.89 ? 2182 HOH A O   1 
HETATM 9761  O  O   . HOH G 5 .    ? 21.676 79.781  5.275   1.00 24.63 ? 2183 HOH A O   1 
HETATM 9762  O  O   A HOH G 5 .    ? 26.515 74.605  2.326   0.50 8.74  ? 2184 HOH A O   1 
HETATM 9763  O  O   B HOH G 5 .    ? 26.162 75.700  1.547   0.50 11.32 ? 2184 HOH A O   1 
HETATM 9764  O  O   . HOH G 5 .    ? 26.063 72.580  5.606   1.00 10.80 ? 2185 HOH A O   1 
HETATM 9765  O  O   . HOH G 5 .    ? 20.631 67.908  8.341   1.00 16.69 ? 2186 HOH A O   1 
HETATM 9766  O  O   . HOH G 5 .    ? 20.752 65.171  7.712   1.00 14.31 ? 2187 HOH A O   1 
HETATM 9767  O  O   . HOH G 5 .    ? 13.106 62.543  11.649  1.00 28.44 ? 2188 HOH A O   1 
HETATM 9768  O  O   . HOH G 5 .    ? 10.152 61.888  9.987   1.00 38.52 ? 2189 HOH A O   1 
HETATM 9769  O  O   . HOH G 5 .    ? 4.548  59.039  10.935  1.00 42.71 ? 2190 HOH A O   1 
HETATM 9770  O  O   . HOH G 5 .    ? 11.358 52.963  6.762   1.00 15.50 ? 2191 HOH A O   1 
HETATM 9771  O  O   . HOH G 5 .    ? 10.995 53.368  3.892   1.00 35.25 ? 2192 HOH A O   1 
HETATM 9772  O  O   . HOH G 5 .    ? 10.589 51.551  2.282   1.00 41.00 ? 2193 HOH A O   1 
HETATM 9773  O  O   . HOH G 5 .    ? 10.712 51.235  -0.422  1.00 29.87 ? 2194 HOH A O   1 
HETATM 9774  O  O   . HOH G 5 .    ? 13.205 51.235  -2.055  1.00 28.17 ? 2195 HOH A O   1 
HETATM 9775  O  O   . HOH G 5 .    ? 14.469 50.380  0.833   1.00 28.25 ? 2196 HOH A O   1 
HETATM 9776  O  O   . HOH G 5 .    ? 13.386 48.094  1.498   1.00 27.62 ? 2197 HOH A O   1 
HETATM 9777  O  O   . HOH G 5 .    ? 12.002 47.737  -2.584  1.00 30.06 ? 2198 HOH A O   1 
HETATM 9778  O  O   . HOH G 5 .    ? 12.940 44.361  -2.612  1.00 40.51 ? 2199 HOH A O   1 
HETATM 9779  O  O   . HOH G 5 .    ? 16.626 42.947  -2.281  1.00 30.59 ? 2200 HOH A O   1 
HETATM 9780  O  O   . HOH G 5 .    ? 19.128 42.803  -2.323  1.00 26.90 ? 2201 HOH A O   1 
HETATM 9781  O  O   . HOH G 5 .    ? 14.960 40.479  -2.775  1.00 40.26 ? 2202 HOH A O   1 
HETATM 9782  O  O   . HOH G 5 .    ? 24.040 41.848  6.944   1.00 8.65  ? 2203 HOH A O   1 
HETATM 9783  O  O   . HOH G 5 .    ? 26.242 39.972  7.933   1.00 8.95  ? 2204 HOH A O   1 
HETATM 9784  O  O   . HOH G 5 .    ? 25.887 39.611  5.223   1.00 9.05  ? 2205 HOH A O   1 
HETATM 9785  O  O   . HOH G 5 .    ? 28.152 39.541  11.245  1.00 11.75 ? 2206 HOH A O   1 
HETATM 9786  O  O   . HOH G 5 .    ? 24.532 33.011  9.557   1.00 26.37 ? 2207 HOH A O   1 
HETATM 9787  O  O   . HOH G 5 .    ? 20.601 37.779  12.169  1.00 22.09 ? 2208 HOH A O   1 
HETATM 9788  O  O   . HOH G 5 .    ? 17.839 35.283  13.301  1.00 37.21 ? 2209 HOH A O   1 
HETATM 9789  O  O   . HOH G 5 .    ? 16.261 33.500  15.760  1.00 30.38 ? 2210 HOH A O   1 
HETATM 9790  O  O   . HOH G 5 .    ? 16.211 36.382  16.189  1.00 27.29 ? 2211 HOH A O   1 
HETATM 9791  O  O   . HOH G 5 .    ? 16.131 31.095  18.021  1.00 44.27 ? 2212 HOH A O   1 
HETATM 9792  O  O   . HOH G 5 .    ? 20.831 30.311  17.620  1.00 29.33 ? 2213 HOH A O   1 
HETATM 9793  O  O   . HOH G 5 .    ? 21.566 29.170  28.105  1.00 35.09 ? 2214 HOH A O   1 
HETATM 9794  O  O   . HOH G 5 .    ? 21.866 27.135  29.750  1.00 40.58 ? 2215 HOH A O   1 
HETATM 9795  O  O   . HOH G 5 .    ? 25.679 26.449  30.662  1.00 33.03 ? 2216 HOH A O   1 
HETATM 9796  O  O   . HOH G 5 .    ? 22.547 31.269  29.558  1.00 27.49 ? 2217 HOH A O   1 
HETATM 9797  O  O   . HOH G 5 .    ? 18.164 38.909  29.081  1.00 35.18 ? 2218 HOH A O   1 
HETATM 9798  O  O   . HOH G 5 .    ? 19.075 39.654  26.502  1.00 30.98 ? 2219 HOH A O   1 
HETATM 9799  O  O   . HOH G 5 .    ? 17.996 41.656  25.193  1.00 27.95 ? 2220 HOH A O   1 
HETATM 9800  O  O   . HOH G 5 .    ? 17.874 43.119  27.292  1.00 23.33 ? 2221 HOH A O   1 
HETATM 9801  O  O   . HOH G 5 .    ? 14.133 44.100  26.916  1.00 38.35 ? 2222 HOH A O   1 
HETATM 9802  O  O   . HOH G 5 .    ? 12.815 44.245  22.695  1.00 35.39 ? 2223 HOH A O   1 
HETATM 9803  O  O   . HOH G 5 .    ? 11.289 46.477  21.455  1.00 32.74 ? 2224 HOH A O   1 
HETATM 9804  O  O   . HOH G 5 .    ? 12.185 43.505  19.881  1.00 32.86 ? 2225 HOH A O   1 
HETATM 9805  O  O   . HOH G 5 .    ? 11.790 41.278  19.741  1.00 28.02 ? 2226 HOH A O   1 
HETATM 9806  O  O   . HOH G 5 .    ? 8.927  39.815  18.994  1.00 39.77 ? 2227 HOH A O   1 
HETATM 9807  O  O   . HOH G 5 .    ? 11.653 46.772  17.804  1.00 19.33 ? 2228 HOH A O   1 
HETATM 9808  O  O   . HOH G 5 .    ? 12.513 49.329  17.774  1.00 16.78 ? 2229 HOH A O   1 
HETATM 9809  O  O   . HOH G 5 .    ? 14.279 49.699  19.816  1.00 13.33 ? 2230 HOH A O   1 
HETATM 9810  O  O   . HOH G 5 .    ? 13.415 51.375  21.646  1.00 14.99 ? 2231 HOH A O   1 
HETATM 9811  O  O   . HOH G 5 .    ? 10.707 51.475  21.401  1.00 21.56 ? 2232 HOH A O   1 
HETATM 9812  O  O   . HOH G 5 .    ? 9.547  53.714  21.782  1.00 34.10 ? 2233 HOH A O   1 
HETATM 9813  O  O   . HOH G 5 .    ? 8.288  55.209  20.049  1.00 41.81 ? 2234 HOH A O   1 
HETATM 9814  O  O   . HOH G 5 .    ? 12.009 55.314  22.076  1.00 26.42 ? 2235 HOH A O   1 
HETATM 9815  O  O   . HOH G 5 .    ? 10.396 55.923  26.289  1.00 39.75 ? 2236 HOH A O   1 
HETATM 9816  O  O   . HOH G 5 .    ? 12.902 60.823  30.339  1.00 29.81 ? 2237 HOH A O   1 
HETATM 9817  O  O   . HOH G 5 .    ? 14.160 63.208  30.117  1.00 26.29 ? 2238 HOH A O   1 
HETATM 9818  O  O   . HOH G 5 .    ? 15.889 64.813  31.958  1.00 37.54 ? 2239 HOH A O   1 
HETATM 9819  O  O   . HOH G 5 .    ? 18.457 65.062  34.472  1.00 43.35 ? 2240 HOH A O   1 
HETATM 9820  O  O   . HOH G 5 .    ? 22.984 55.877  30.795  1.00 13.03 ? 2241 HOH A O   1 
HETATM 9821  O  O   . HOH G 5 .    ? 18.016 60.542  24.324  1.00 14.81 ? 2242 HOH A O   1 
HETATM 9822  O  O   . HOH G 5 .    ? 14.507 64.597  16.521  1.00 39.77 ? 2243 HOH A O   1 
HETATM 9823  O  O   . HOH G 5 .    ? 22.003 70.684  19.081  1.00 34.45 ? 2244 HOH A O   1 
HETATM 9824  O  O   . HOH G 5 .    ? 15.602 73.367  5.398   1.00 26.56 ? 2245 HOH A O   1 
HETATM 9825  O  O   . HOH G 5 .    ? 15.783 83.184  2.837   1.00 33.64 ? 2246 HOH A O   1 
HETATM 9826  O  O   . HOH G 5 .    ? 13.421 84.082  4.029   1.00 35.24 ? 2247 HOH A O   1 
HETATM 9827  O  O   . HOH G 5 .    ? 10.659 68.212  -1.899  1.00 35.04 ? 2248 HOH A O   1 
HETATM 9828  O  O   . HOH G 5 .    ? 19.527 67.186  -2.840  1.00 20.96 ? 2249 HOH A O   1 
HETATM 9829  O  O   . HOH G 5 .    ? 26.784 60.791  -3.351  1.00 8.24  ? 2250 HOH A O   1 
HETATM 9830  O  O   . HOH G 5 .    ? 32.581 60.017  -1.870  1.00 7.37  ? 2251 HOH A O   1 
HETATM 9831  O  O   . HOH G 5 .    ? 33.098 62.594  0.033   1.00 6.97  ? 2252 HOH A O   1 
HETATM 9832  O  O   . HOH G 5 .    ? 37.422 56.940  1.699   1.00 9.31  ? 2253 HOH A O   1 
HETATM 9833  O  O   . HOH G 5 .    ? 39.528 55.576  3.033   1.00 16.40 ? 2254 HOH A O   1 
HETATM 9834  O  O   . HOH G 5 .    ? 38.682 53.065  2.314   1.00 33.15 ? 2255 HOH A O   1 
HETATM 9835  O  O   . HOH G 5 .    ? 35.951 53.007  1.287   1.00 12.32 ? 2256 HOH A O   1 
HETATM 9836  O  O   . HOH G 5 .    ? 34.289 52.319  -1.048  1.00 9.36  ? 2257 HOH A O   1 
HETATM 9837  O  O   . HOH G 5 .    ? 36.685 51.499  3.759   1.00 12.44 ? 2258 HOH A O   1 
HETATM 9838  O  O   . HOH G 5 .    ? 40.065 56.069  5.776   1.00 13.74 ? 2259 HOH A O   1 
HETATM 9839  O  O   . HOH G 5 .    ? 42.916 56.698  6.120   1.00 12.42 ? 2260 HOH A O   1 
HETATM 9840  O  O   A HOH G 5 .    ? 42.723 56.327  2.803   0.50 10.78 ? 2261 HOH A O   1 
HETATM 9841  O  O   B HOH G 5 .    ? 42.089 55.238  1.505   0.50 18.18 ? 2261 HOH A O   1 
HETATM 9842  O  O   . HOH G 5 .    ? 40.191 62.629  6.037   1.00 8.63  ? 2262 HOH A O   1 
HETATM 9843  O  O   . HOH G 5 .    ? 38.683 62.267  8.408   1.00 9.83  ? 2263 HOH A O   1 
HETATM 9844  O  O   . HOH G 5 .    ? 37.648 58.827  11.043  1.00 10.91 ? 2264 HOH A O   1 
HETATM 9845  O  O   . HOH G 5 .    ? 36.858 57.589  13.386  1.00 8.36  ? 2265 HOH A O   1 
HETATM 9846  O  O   . HOH G 5 .    ? 39.293 57.330  14.870  1.00 7.68  ? 2266 HOH A O   1 
HETATM 9847  O  O   . HOH G 5 .    ? 41.142 58.950  13.498  1.00 10.48 ? 2267 HOH A O   1 
HETATM 9848  O  O   . HOH G 5 .    ? 43.023 47.959  11.301  1.00 13.94 ? 2268 HOH A O   1 
HETATM 9849  O  O   . HOH G 5 .    ? 44.394 45.980  10.110  1.00 13.48 ? 2269 HOH A O   1 
HETATM 9850  O  O   . HOH G 5 .    ? 46.635 42.680  9.743   1.00 39.30 ? 2270 HOH A O   1 
HETATM 9851  O  O   . HOH G 5 .    ? 48.840 41.727  8.319   1.00 25.71 ? 2271 HOH A O   1 
HETATM 9852  O  O   . HOH G 5 .    ? 49.913 44.017  7.084   1.00 15.53 ? 2272 HOH A O   1 
HETATM 9853  O  O   . HOH G 5 .    ? 49.345 44.144  4.467   1.00 13.97 ? 2273 HOH A O   1 
HETATM 9854  O  O   . HOH G 5 .    ? 51.603 44.306  2.976   1.00 20.01 ? 2274 HOH A O   1 
HETATM 9855  O  O   . HOH G 5 .    ? 51.832 46.488  1.352   1.00 10.01 ? 2275 HOH A O   1 
HETATM 9856  O  O   . HOH G 5 .    ? 49.835 48.436  1.474   1.00 8.37  ? 2276 HOH A O   1 
HETATM 9857  O  O   . HOH G 5 .    ? 47.459 46.013  3.713   1.00 9.40  ? 2277 HOH A O   1 
HETATM 9858  O  O   . HOH G 5 .    ? 48.030 41.737  3.634   1.00 16.66 ? 2278 HOH A O   1 
HETATM 9859  O  O   . HOH G 5 .    ? 49.592 40.873  1.601   1.00 28.30 ? 2279 HOH A O   1 
HETATM 9860  O  O   . HOH G 5 .    ? 50.681 38.355  1.484   1.00 48.03 ? 2280 HOH A O   1 
HETATM 9861  O  O   . HOH G 5 .    ? 54.938 38.442  0.443   1.00 30.96 ? 2281 HOH A O   1 
HETATM 9862  O  O   . HOH G 5 .    ? 57.967 42.390  1.699   1.00 21.78 ? 2282 HOH A O   1 
HETATM 9863  O  O   . HOH G 5 .    ? 57.287 42.826  4.370   1.00 40.87 ? 2283 HOH A O   1 
HETATM 9864  O  O   . HOH G 5 .    ? 53.961 45.931  4.703   1.00 35.20 ? 2284 HOH A O   1 
HETATM 9865  O  O   . HOH G 5 .    ? 54.111 46.083  8.174   1.00 33.90 ? 2285 HOH A O   1 
HETATM 9866  O  O   . HOH G 5 .    ? 52.621 43.604  7.720   1.00 29.80 ? 2286 HOH A O   1 
HETATM 9867  O  O   . HOH G 5 .    ? 47.492 40.099  5.925   1.00 30.20 ? 2287 HOH A O   1 
HETATM 9868  O  O   . HOH G 5 .    ? 44.639 40.839  7.625   1.00 31.55 ? 2288 HOH A O   1 
HETATM 9869  O  O   . HOH G 5 .    ? 42.204 39.643  7.659   1.00 37.95 ? 2289 HOH A O   1 
HETATM 9870  O  O   . HOH G 5 .    ? 40.022 39.306  9.036   1.00 22.09 ? 2290 HOH A O   1 
HETATM 9871  O  O   . HOH G 5 .    ? 40.673 36.209  8.769   1.00 35.17 ? 2291 HOH A O   1 
HETATM 9872  O  O   . HOH G 5 .    ? 39.909 35.357  11.259  1.00 21.26 ? 2292 HOH A O   1 
HETATM 9873  O  O   . HOH G 5 .    ? 37.126 33.628  6.097   1.00 39.70 ? 2293 HOH A O   1 
HETATM 9874  O  O   . HOH G 5 .    ? 34.844 36.540  3.436   1.00 34.15 ? 2294 HOH A O   1 
HETATM 9875  O  O   . HOH G 5 .    ? 37.301 37.491  2.982   1.00 30.31 ? 2295 HOH A O   1 
HETATM 9876  O  O   . HOH G 5 .    ? 38.314 40.025  1.786   1.00 10.48 ? 2296 HOH A O   1 
HETATM 9877  O  O   . HOH G 5 .    ? 39.990 39.672  -0.351  1.00 19.80 ? 2297 HOH A O   1 
HETATM 9878  O  O   . HOH G 5 .    ? 42.528 39.448  -1.376  1.00 23.46 ? 2298 HOH A O   1 
HETATM 9879  O  O   . HOH G 5 .    ? 44.494 41.763  -0.426  1.00 12.70 ? 2299 HOH A O   1 
HETATM 9880  O  O   . HOH G 5 .    ? 46.050 39.825  -0.077  1.00 24.39 ? 2300 HOH A O   1 
HETATM 9881  O  O   . HOH G 5 .    ? 41.615 43.204  8.023   1.00 14.53 ? 2301 HOH A O   1 
HETATM 9882  O  O   . HOH G 5 .    ? 44.745 40.232  12.901  1.00 42.40 ? 2302 HOH A O   1 
HETATM 9883  O  O   . HOH G 5 .    ? 43.996 42.097  15.630  1.00 44.06 ? 2303 HOH A O   1 
HETATM 9884  O  O   . HOH G 5 .    ? 48.827 43.593  18.364  1.00 42.34 ? 2304 HOH A O   1 
HETATM 9885  O  O   . HOH G 5 .    ? 52.519 43.847  17.152  1.00 36.31 ? 2305 HOH A O   1 
HETATM 9886  O  O   . HOH G 5 .    ? 53.086 44.135  22.957  1.00 34.35 ? 2306 HOH A O   1 
HETATM 9887  O  O   . HOH G 5 .    ? 53.847 46.574  23.366  1.00 27.01 ? 2307 HOH A O   1 
HETATM 9888  O  O   . HOH G 5 .    ? 56.640 47.235  23.216  1.00 30.66 ? 2308 HOH A O   1 
HETATM 9889  O  O   . HOH G 5 .    ? 57.273 48.967  21.278  1.00 20.23 ? 2309 HOH A O   1 
HETATM 9890  O  O   . HOH G 5 .    ? 58.763 48.788  19.115  1.00 30.21 ? 2310 HOH A O   1 
HETATM 9891  O  O   . HOH G 5 .    ? 59.724 46.234  19.363  1.00 32.88 ? 2311 HOH A O   1 
HETATM 9892  O  O   . HOH G 5 .    ? 60.346 50.874  20.254  1.00 30.13 ? 2312 HOH A O   1 
HETATM 9893  O  O   . HOH G 5 .    ? 58.460 51.160  22.260  1.00 21.58 ? 2313 HOH A O   1 
HETATM 9894  O  O   . HOH G 5 .    ? 59.536 50.800  24.887  1.00 27.94 ? 2314 HOH A O   1 
HETATM 9895  O  O   . HOH G 5 .    ? 62.140 50.998  25.657  1.00 43.97 ? 2315 HOH A O   1 
HETATM 9896  O  O   . HOH G 5 .    ? 56.036 49.211  27.314  1.00 31.30 ? 2316 HOH A O   1 
HETATM 9897  O  O   . HOH G 5 .    ? 58.894 56.539  31.309  1.00 39.15 ? 2317 HOH A O   1 
HETATM 9898  O  O   . HOH G 5 .    ? 50.796 55.364  34.933  1.00 36.29 ? 2318 HOH A O   1 
HETATM 9899  O  O   . HOH G 5 .    ? 62.139 56.520  17.814  1.00 39.77 ? 2319 HOH A O   1 
HETATM 9900  O  O   A HOH G 5 .    ? 60.548 56.982  15.801  0.50 18.68 ? 2320 HOH A O   1 
HETATM 9901  O  O   B HOH G 5 .    ? 61.487 59.098  15.032  0.50 15.68 ? 2320 HOH A O   1 
HETATM 9902  O  O   . HOH G 5 .    ? 63.412 59.825  16.920  1.00 35.67 ? 2321 HOH A O   1 
HETATM 9903  O  O   . HOH G 5 .    ? 63.823 62.336  16.489  1.00 31.54 ? 2322 HOH A O   1 
HETATM 9904  O  O   . HOH G 5 .    ? 60.925 63.669  15.433  1.00 24.46 ? 2323 HOH A O   1 
HETATM 9905  O  O   . HOH G 5 .    ? 62.941 57.580  13.137  1.00 43.42 ? 2324 HOH A O   1 
HETATM 9906  O  O   . HOH G 5 .    ? 63.096 56.147  9.918   1.00 45.44 ? 2325 HOH A O   1 
HETATM 9907  O  O   . HOH G 5 .    ? 60.261 54.192  14.804  1.00 29.69 ? 2326 HOH A O   1 
HETATM 9908  O  O   . HOH G 5 .    ? 52.102 50.464  6.390   1.00 9.15  ? 2327 HOH A O   1 
HETATM 9909  O  O   . HOH G 5 .    ? 58.609 42.097  17.111  1.00 37.92 ? 2328 HOH A O   1 
HETATM 9910  O  O   . HOH G 5 .    ? 59.259 39.614  -3.974  1.00 36.38 ? 2329 HOH A O   1 
HETATM 9911  O  O   . HOH G 5 .    ? 63.498 44.651  -6.645  1.00 13.45 ? 2330 HOH A O   1 
HETATM 9912  O  O   . HOH G 5 .    ? 64.368 39.317  -10.157 1.00 18.45 ? 2331 HOH A O   1 
HETATM 9913  O  O   . HOH G 5 .    ? 66.833 38.384  -9.520  1.00 29.28 ? 2332 HOH A O   1 
HETATM 9914  O  O   . HOH G 5 .    ? 67.993 39.166  -7.422  1.00 37.98 ? 2333 HOH A O   1 
HETATM 9915  O  O   . HOH G 5 .    ? 71.163 40.083  -9.454  1.00 38.49 ? 2334 HOH A O   1 
HETATM 9916  O  O   . HOH G 5 .    ? 73.145 43.915  -12.032 1.00 41.31 ? 2335 HOH A O   1 
HETATM 9917  O  O   . HOH G 5 .    ? 71.012 43.395  -15.188 1.00 35.94 ? 2336 HOH A O   1 
HETATM 9918  O  O   . HOH G 5 .    ? 69.112 41.764  -17.332 1.00 30.17 ? 2337 HOH A O   1 
HETATM 9919  O  O   . HOH G 5 .    ? 68.758 47.098  -16.514 1.00 32.03 ? 2338 HOH A O   1 
HETATM 9920  O  O   . HOH G 5 .    ? 72.828 47.478  -17.250 1.00 33.36 ? 2339 HOH A O   1 
HETATM 9921  O  O   . HOH G 5 .    ? 74.402 49.242  -18.654 1.00 37.55 ? 2340 HOH A O   1 
HETATM 9922  O  O   . HOH G 5 .    ? 71.706 49.649  -20.015 1.00 48.32 ? 2341 HOH A O   1 
HETATM 9923  O  O   . HOH G 5 .    ? 74.310 52.734  -18.123 1.00 33.16 ? 2342 HOH A O   1 
HETATM 9924  O  O   . HOH G 5 .    ? 75.169 52.352  -15.455 1.00 36.93 ? 2343 HOH A O   1 
HETATM 9925  O  O   . HOH G 5 .    ? 73.779 54.217  -13.749 1.00 42.90 ? 2344 HOH A O   1 
HETATM 9926  O  O   . HOH G 5 .    ? 76.316 54.245  -10.020 1.00 30.20 ? 2345 HOH A O   1 
HETATM 9927  O  O   . HOH G 5 .    ? 72.265 55.472  -9.079  1.00 28.86 ? 2346 HOH A O   1 
HETATM 9928  O  O   . HOH G 5 .    ? 72.923 56.182  -6.492  1.00 29.31 ? 2347 HOH A O   1 
HETATM 9929  O  O   . HOH G 5 .    ? 74.604 58.308  -7.166  1.00 33.89 ? 2348 HOH A O   1 
HETATM 9930  O  O   . HOH G 5 .    ? 73.753 61.062  -6.052  1.00 32.94 ? 2349 HOH A O   1 
HETATM 9931  O  O   . HOH G 5 .    ? 70.172 53.690  -9.581  1.00 30.41 ? 2350 HOH A O   1 
HETATM 9932  O  O   . HOH G 5 .    ? 68.716 56.908  -16.476 1.00 37.93 ? 2351 HOH A O   1 
HETATM 9933  O  O   . HOH G 5 .    ? 66.405 62.561  -13.045 1.00 16.00 ? 2352 HOH A O   1 
HETATM 9934  O  O   . HOH G 5 .    ? 60.996 59.668  -8.118  1.00 7.54  ? 2353 HOH A O   1 
HETATM 9935  O  O   . HOH G 5 .    ? 59.427 60.601  -6.103  1.00 14.78 ? 2354 HOH A O   1 
HETATM 9936  O  O   . HOH G 5 .    ? 53.651 59.753  -9.360  1.00 13.08 ? 2355 HOH A O   1 
HETATM 9937  O  O   . HOH G 5 .    ? 55.592 59.281  -11.443 1.00 8.94  ? 2356 HOH A O   1 
HETATM 9938  O  O   . HOH G 5 .    ? 60.474 61.032  -18.044 1.00 9.54  ? 2357 HOH A O   1 
HETATM 9939  O  O   . HOH G 5 .    ? 53.609 64.822  -19.843 1.00 9.93  ? 2358 HOH A O   1 
HETATM 9940  O  O   . HOH G 5 .    ? 46.934 55.786  -25.444 1.00 15.41 ? 2359 HOH A O   1 
HETATM 9941  O  O   . HOH G 5 .    ? 43.885 54.842  -26.642 1.00 29.40 ? 2360 HOH A O   1 
HETATM 9942  O  O   . HOH G 5 .    ? 52.962 51.992  -38.198 1.00 40.43 ? 2361 HOH A O   1 
HETATM 9943  O  O   . HOH G 5 .    ? 52.051 45.856  -37.743 1.00 43.47 ? 2362 HOH A O   1 
HETATM 9944  O  O   . HOH G 5 .    ? 53.406 43.840  -36.703 1.00 66.09 ? 2363 HOH A O   1 
HETATM 9945  O  O   . HOH G 5 .    ? 56.671 46.164  -17.310 1.00 14.41 ? 2364 HOH A O   1 
HETATM 9946  O  O   . HOH G 5 .    ? 51.659 41.097  -12.999 1.00 29.88 ? 2365 HOH A O   1 
HETATM 9947  O  O   . HOH G 5 .    ? 50.867 40.412  -15.383 1.00 35.24 ? 2366 HOH A O   1 
HETATM 9948  O  O   . HOH G 5 .    ? 53.629 39.110  -12.327 1.00 36.75 ? 2367 HOH A O   1 
HETATM 9949  O  O   . HOH G 5 .    ? 63.271 34.462  -9.535  1.00 34.19 ? 2368 HOH A O   1 
HETATM 9950  O  O   . HOH G 5 .    ? 66.276 35.337  -12.844 1.00 34.68 ? 2369 HOH A O   1 
HETATM 9951  O  O   . HOH G 5 .    ? 63.806 50.168  -13.786 1.00 13.79 ? 2370 HOH A O   1 
HETATM 9952  O  O   . HOH G 5 .    ? 45.969 70.820  0.022   1.00 15.89 ? 2371 HOH A O   1 
HETATM 9953  O  O   . HOH G 5 .    ? 40.703 74.414  -1.984  1.00 39.39 ? 2372 HOH A O   1 
HETATM 9954  O  O   . HOH G 5 .    ? 37.828 73.208  -2.246  1.00 11.79 ? 2373 HOH A O   1 
HETATM 9955  O  O   . HOH G 5 .    ? 37.014 71.751  -4.535  1.00 7.32  ? 2374 HOH A O   1 
HETATM 9956  O  O   . HOH G 5 .    ? 36.524 72.471  0.258   1.00 7.73  ? 2375 HOH A O   1 
HETATM 9957  O  O   . HOH G 5 .    ? 33.273 78.440  -5.206  1.00 12.04 ? 2376 HOH A O   1 
HETATM 9958  O  O   . HOH G 5 .    ? 31.314 76.660  -6.362  1.00 9.26  ? 2377 HOH A O   1 
HETATM 9959  O  O   . HOH G 5 .    ? 27.809 68.428  -21.489 1.00 39.15 ? 2378 HOH A O   1 
HETATM 9960  O  O   . HOH G 5 .    ? 20.596 66.024  -19.662 1.00 11.20 ? 2379 HOH A O   1 
HETATM 9961  O  O   . HOH G 5 .    ? 16.529 67.523  -19.975 1.00 19.74 ? 2380 HOH A O   1 
HETATM 9962  O  O   . HOH G 5 .    ? 14.702 67.614  -22.785 1.00 29.50 ? 2381 HOH A O   1 
HETATM 9963  O  O   . HOH G 5 .    ? 17.260 69.989  -23.425 1.00 19.54 ? 2382 HOH A O   1 
HETATM 9964  O  O   . HOH G 5 .    ? 17.053 66.898  -25.896 1.00 27.16 ? 2383 HOH A O   1 
HETATM 9965  O  O   . HOH G 5 .    ? 18.514 64.932  -27.026 1.00 16.17 ? 2384 HOH A O   1 
HETATM 9966  O  O   . HOH G 5 .    ? 15.099 63.472  -25.852 1.00 20.99 ? 2385 HOH A O   1 
HETATM 9967  O  O   . HOH G 5 .    ? 13.917 60.767  -22.547 1.00 13.99 ? 2386 HOH A O   1 
HETATM 9968  O  O   . HOH G 5 .    ? 13.500 58.070  -22.056 1.00 29.71 ? 2387 HOH A O   1 
HETATM 9969  O  O   . HOH G 5 .    ? 13.652 55.613  -22.354 1.00 36.93 ? 2388 HOH A O   1 
HETATM 9970  O  O   . HOH G 5 .    ? 10.522 57.804  -21.166 1.00 36.55 ? 2389 HOH A O   1 
HETATM 9971  O  O   . HOH G 5 .    ? 9.874  60.326  -20.412 1.00 36.83 ? 2390 HOH A O   1 
HETATM 9972  O  O   . HOH G 5 .    ? 11.464 61.228  -18.250 1.00 21.30 ? 2391 HOH A O   1 
HETATM 9973  O  O   . HOH G 5 .    ? 13.398 62.293  -20.046 1.00 19.06 ? 2392 HOH A O   1 
HETATM 9974  O  O   . HOH G 5 .    ? 10.110 62.693  -14.927 1.00 30.43 ? 2393 HOH A O   1 
HETATM 9975  O  O   . HOH G 5 .    ? 8.522  60.540  -15.832 1.00 33.72 ? 2394 HOH A O   1 
HETATM 9976  O  O   . HOH G 5 .    ? 17.112 70.097  -16.256 1.00 10.41 ? 2395 HOH A O   1 
HETATM 9977  O  O   . HOH G 5 .    ? 16.021 71.823  -19.030 1.00 15.89 ? 2396 HOH A O   1 
HETATM 9978  O  O   . HOH G 5 .    ? 12.862 74.688  -18.957 1.00 31.35 ? 2397 HOH A O   1 
HETATM 9979  O  O   . HOH G 5 .    ? 12.359 77.735  -18.933 1.00 42.87 ? 2398 HOH A O   1 
HETATM 9980  O  O   . HOH G 5 .    ? 16.180 74.979  -23.784 1.00 38.56 ? 2399 HOH A O   1 
HETATM 9981  O  O   . HOH G 5 .    ? 16.709 77.512  -25.775 1.00 36.65 ? 2400 HOH A O   1 
HETATM 9982  O  O   . HOH G 5 .    ? 19.276 78.742  -25.588 1.00 35.44 ? 2401 HOH A O   1 
HETATM 9983  O  O   . HOH G 5 .    ? 20.296 77.296  -27.608 1.00 36.82 ? 2402 HOH A O   1 
HETATM 9984  O  O   . HOH G 5 .    ? 22.705 77.081  -27.592 1.00 25.58 ? 2403 HOH A O   1 
HETATM 9985  O  O   . HOH G 5 .    ? 23.134 78.270  -24.834 1.00 13.92 ? 2404 HOH A O   1 
HETATM 9986  O  O   . HOH G 5 .    ? 20.975 79.271  -23.550 1.00 20.04 ? 2405 HOH A O   1 
HETATM 9987  O  O   . HOH G 5 .    ? 22.924 78.379  -30.403 1.00 23.00 ? 2406 HOH A O   1 
HETATM 9988  O  O   . HOH G 5 .    ? 20.687 80.096  -33.557 1.00 39.65 ? 2407 HOH A O   1 
HETATM 9989  O  O   . HOH G 5 .    ? 22.024 80.090  -35.910 1.00 22.30 ? 2408 HOH A O   1 
HETATM 9990  O  O   . HOH G 5 .    ? 21.436 82.126  -37.969 1.00 30.13 ? 2409 HOH A O   1 
HETATM 9991  O  O   . HOH G 5 .    ? 23.223 82.352  -40.478 1.00 20.31 ? 2410 HOH A O   1 
HETATM 9992  O  O   . HOH G 5 .    ? 23.189 84.792  -41.547 1.00 43.52 ? 2411 HOH A O   1 
HETATM 9993  O  O   . HOH G 5 .    ? 24.053 87.275  -40.895 1.00 33.28 ? 2412 HOH A O   1 
HETATM 9994  O  O   . HOH G 5 .    ? 25.780 87.726  -42.891 1.00 36.82 ? 2413 HOH A O   1 
HETATM 9995  O  O   . HOH G 5 .    ? 28.032 87.740  -41.618 1.00 23.35 ? 2414 HOH A O   1 
HETATM 9996  O  O   . HOH G 5 .    ? 28.037 90.655  -42.512 1.00 25.77 ? 2415 HOH A O   1 
HETATM 9997  O  O   . HOH G 5 .    ? 32.379 88.946  -43.081 1.00 21.88 ? 2416 HOH A O   1 
HETATM 9998  O  O   . HOH G 5 .    ? 34.076 86.680  -43.684 1.00 29.70 ? 2417 HOH A O   1 
HETATM 9999  O  O   . HOH G 5 .    ? 36.524 85.722  -43.046 1.00 31.74 ? 2418 HOH A O   1 
HETATM 10000 O  O   . HOH G 5 .    ? 38.865 86.279  -41.695 1.00 26.73 ? 2419 HOH A O   1 
HETATM 10001 O  O   . HOH G 5 .    ? 40.989 86.659  -43.916 1.00 40.13 ? 2420 HOH A O   1 
HETATM 10002 O  O   . HOH G 5 .    ? 43.361 86.586  -43.226 1.00 25.50 ? 2421 HOH A O   1 
HETATM 10003 O  O   . HOH G 5 .    ? 42.028 87.609  -41.059 1.00 13.30 ? 2422 HOH A O   1 
HETATM 10004 O  O   . HOH G 5 .    ? 43.468 88.267  -38.768 1.00 11.68 ? 2423 HOH A O   1 
HETATM 10005 O  O   . HOH G 5 .    ? 43.256 93.712  -37.737 1.00 17.87 ? 2424 HOH A O   1 
HETATM 10006 O  O   . HOH G 5 .    ? 45.789 94.787  -37.868 1.00 26.55 ? 2425 HOH A O   1 
HETATM 10007 O  O   . HOH G 5 .    ? 45.212 97.204  -38.569 1.00 43.33 ? 2426 HOH A O   1 
HETATM 10008 O  O   . HOH G 5 .    ? 43.029 97.947  -37.255 1.00 29.10 ? 2427 HOH A O   1 
HETATM 10009 O  O   . HOH G 5 .    ? 40.522 96.245  -37.587 1.00 24.47 ? 2428 HOH A O   1 
HETATM 10010 O  O   . HOH G 5 .    ? 41.158 94.664  -39.369 1.00 18.12 ? 2429 HOH A O   1 
HETATM 10011 O  O   . HOH G 5 .    ? 41.945 96.321  -41.643 1.00 31.24 ? 2430 HOH A O   1 
HETATM 10012 O  O   . HOH G 5 .    ? 45.882 96.894  -43.884 1.00 24.47 ? 2431 HOH A O   1 
HETATM 10013 O  O   . HOH G 5 .    ? 48.388 95.961  -44.357 1.00 34.35 ? 2432 HOH A O   1 
HETATM 10014 O  O   . HOH G 5 .    ? 47.694 95.188  -41.062 1.00 45.22 ? 2433 HOH A O   1 
HETATM 10015 O  O   . HOH G 5 .    ? 48.283 93.749  -37.969 1.00 36.88 ? 2434 HOH A O   1 
HETATM 10016 O  O   . HOH G 5 .    ? 48.452 97.801  -33.734 1.00 29.15 ? 2435 HOH A O   1 
HETATM 10017 O  O   A HOH G 5 .    ? 46.594 99.784  -31.306 0.50 20.64 ? 2436 HOH A O   1 
HETATM 10018 O  O   B HOH G 5 .    ? 47.376 99.841  -32.880 0.50 18.00 ? 2436 HOH A O   1 
HETATM 10019 O  O   . HOH G 5 .    ? 44.668 101.532 -32.750 1.00 37.82 ? 2437 HOH A O   1 
HETATM 10020 O  O   . HOH G 5 .    ? 39.883 99.829  -32.009 1.00 29.14 ? 2438 HOH A O   1 
HETATM 10021 O  O   . HOH G 5 .    ? 48.343 98.262  -28.691 1.00 30.24 ? 2439 HOH A O   1 
HETATM 10022 O  O   . HOH G 5 .    ? 52.120 97.967  -30.500 1.00 30.08 ? 2440 HOH A O   1 
HETATM 10023 O  O   . HOH G 5 .    ? 53.451 97.193  -32.570 1.00 52.29 ? 2441 HOH A O   1 
HETATM 10024 O  O   . HOH G 5 .    ? 53.677 93.950  -33.534 1.00 27.25 ? 2442 HOH A O   1 
HETATM 10025 O  O   . HOH G 5 .    ? 38.515 83.385  -39.868 1.00 28.41 ? 2443 HOH A O   1 
HETATM 10026 O  O   . HOH G 5 .    ? 36.842 82.397  -41.518 1.00 44.63 ? 2444 HOH A O   1 
HETATM 10027 O  O   . HOH G 5 .    ? 34.704 81.048  -41.673 1.00 36.56 ? 2445 HOH A O   1 
HETATM 10028 O  O   . HOH G 5 .    ? 35.689 77.299  -42.925 1.00 24.51 ? 2446 HOH A O   1 
HETATM 10029 O  O   . HOH G 5 .    ? 37.554 75.417  -42.286 1.00 18.66 ? 2447 HOH A O   1 
HETATM 10030 O  O   . HOH G 5 .    ? 39.691 75.441  -40.345 1.00 15.61 ? 2448 HOH A O   1 
HETATM 10031 O  O   . HOH G 5 .    ? 38.736 69.139  -38.090 1.00 14.01 ? 2449 HOH A O   1 
HETATM 10032 O  O   . HOH G 5 .    ? 39.343 69.045  -35.378 1.00 15.69 ? 2450 HOH A O   1 
HETATM 10033 O  O   . HOH G 5 .    ? 43.082 65.295  -39.592 1.00 35.81 ? 2451 HOH A O   1 
HETATM 10034 O  O   . HOH G 5 .    ? 43.801 62.370  -39.997 1.00 35.37 ? 2452 HOH A O   1 
HETATM 10035 O  O   . HOH G 5 .    ? 45.415 61.255  -43.846 1.00 39.72 ? 2453 HOH A O   1 
HETATM 10036 O  O   . HOH G 5 .    ? 36.658 62.915  -45.701 1.00 38.14 ? 2454 HOH A O   1 
HETATM 10037 O  O   . HOH G 5 .    ? 34.181 66.342  -42.721 1.00 27.84 ? 2455 HOH A O   1 
HETATM 10038 O  O   . HOH G 5 .    ? 30.841 69.461  -45.433 1.00 42.55 ? 2456 HOH A O   1 
HETATM 10039 O  O   . HOH G 5 .    ? 28.241 68.968  -46.346 1.00 48.58 ? 2457 HOH A O   1 
HETATM 10040 O  O   . HOH G 5 .    ? 29.065 72.164  -42.179 1.00 33.64 ? 2458 HOH A O   1 
HETATM 10041 O  O   . HOH G 5 .    ? 28.957 69.603  -39.693 1.00 20.47 ? 2459 HOH A O   1 
HETATM 10042 O  O   . HOH G 5 .    ? 24.695 71.477  -39.768 1.00 27.30 ? 2460 HOH A O   1 
HETATM 10043 O  O   . HOH G 5 .    ? 22.206 70.685  -36.620 1.00 34.06 ? 2461 HOH A O   1 
HETATM 10044 O  O   . HOH G 5 .    ? 18.887 67.804  -30.918 1.00 44.87 ? 2462 HOH A O   1 
HETATM 10045 O  O   . HOH G 5 .    ? 18.548 70.124  -30.053 1.00 32.77 ? 2463 HOH A O   1 
HETATM 10046 O  O   . HOH G 5 .    ? 16.379 74.527  -28.402 1.00 41.91 ? 2464 HOH A O   1 
HETATM 10047 O  O   . HOH G 5 .    ? 30.256 74.826  -29.182 1.00 13.06 ? 2465 HOH A O   1 
HETATM 10048 O  O   . HOH G 5 .    ? 32.422 77.553  -29.658 1.00 12.16 ? 2466 HOH A O   1 
HETATM 10049 O  O   . HOH G 5 .    ? 28.914 81.653  -35.719 1.00 15.97 ? 2467 HOH A O   1 
HETATM 10050 O  O   . HOH G 5 .    ? 28.057 84.300  -35.508 1.00 14.64 ? 2468 HOH A O   1 
HETATM 10051 O  O   . HOH G 5 .    ? 23.146 88.590  -38.049 1.00 27.73 ? 2469 HOH A O   1 
HETATM 10052 O  O   . HOH G 5 .    ? 28.719 93.654  -38.514 1.00 29.17 ? 2470 HOH A O   1 
HETATM 10053 O  O   . HOH G 5 .    ? 30.767 94.091  -40.367 1.00 40.43 ? 2471 HOH A O   1 
HETATM 10054 O  O   . HOH G 5 .    ? 31.806 92.333  -36.744 1.00 21.23 ? 2472 HOH A O   1 
HETATM 10055 O  O   . HOH G 5 .    ? 26.529 96.514  -37.584 1.00 42.83 ? 2473 HOH A O   1 
HETATM 10056 O  O   . HOH G 5 .    ? 35.697 89.343  -44.998 1.00 32.90 ? 2474 HOH A O   1 
HETATM 10057 O  O   . HOH G 5 .    ? 39.920 83.319  -44.099 1.00 50.38 ? 2475 HOH A O   1 
HETATM 10058 O  O   . HOH G 5 .    ? 31.375 78.908  -42.842 1.00 25.21 ? 2476 HOH A O   1 
HETATM 10059 O  O   . HOH G 5 .    ? 29.696 81.182  -43.109 1.00 28.87 ? 2477 HOH A O   1 
HETATM 10060 O  O   . HOH G 5 .    ? 26.011 81.116  -42.731 1.00 31.90 ? 2478 HOH A O   1 
HETATM 10061 O  O   . HOH G 5 .    ? 23.068 78.307  -42.086 1.00 32.97 ? 2479 HOH A O   1 
HETATM 10062 O  O   . HOH G 5 .    ? 26.295 76.214  -39.237 1.00 27.68 ? 2480 HOH A O   1 
HETATM 10063 O  O   . HOH G 5 .    ? 27.293 76.074  -41.611 1.00 44.83 ? 2481 HOH A O   1 
HETATM 10064 O  O   . HOH G 5 .    ? 23.837 65.283  -43.537 1.00 36.46 ? 2482 HOH A O   1 
HETATM 10065 O  O   . HOH G 5 .    ? 12.043 49.084  25.360  1.00 30.91 ? 2483 HOH A O   1 
HETATM 10066 O  O   . HOH G 5 .    ? 9.864  49.227  23.209  1.00 40.19 ? 2484 HOH A O   1 
HETATM 10067 O  O   . HOH G 5 .    ? 22.507 56.753  -34.105 1.00 14.78 ? 2485 HOH A O   1 
HETATM 10068 O  O   . HOH G 5 .    ? 19.915 51.546  -30.939 1.00 31.52 ? 2486 HOH A O   1 
HETATM 10069 O  O   . HOH G 5 .    ? 20.049 52.437  -27.298 1.00 21.97 ? 2487 HOH A O   1 
HETATM 10070 O  O   . HOH G 5 .    ? 23.156 48.912  -27.214 1.00 43.52 ? 2488 HOH A O   1 
HETATM 10071 O  O   . HOH G 5 .    ? 26.426 44.266  -27.286 1.00 23.34 ? 2489 HOH A O   1 
HETATM 10072 O  O   . HOH G 5 .    ? 30.261 39.195  -27.277 1.00 19.74 ? 2490 HOH A O   1 
HETATM 10073 O  O   . HOH G 5 .    ? 17.968 48.709  -20.013 1.00 33.85 ? 2491 HOH A O   1 
HETATM 10074 O  O   . HOH G 5 .    ? 17.031 50.852  -19.468 1.00 23.72 ? 2492 HOH A O   1 
HETATM 10075 O  O   . HOH G 5 .    ? 16.537 52.823  -22.341 1.00 26.32 ? 2493 HOH A O   1 
HETATM 10076 O  O   . HOH G 5 .    ? 15.719 52.974  -25.432 1.00 37.35 ? 2494 HOH A O   1 
HETATM 10077 O  O   . HOH G 5 .    ? 16.771 58.767  -31.190 1.00 27.88 ? 2495 HOH A O   1 
HETATM 10078 O  O   . HOH G 5 .    ? 14.078 57.721  -1.359  1.00 18.72 ? 2496 HOH A O   1 
HETATM 10079 O  O   . HOH G 5 .    ? 13.398 53.567  1.739   1.00 14.93 ? 2497 HOH A O   1 
HETATM 10080 O  O   . HOH G 5 .    ? 13.804 54.012  4.322   1.00 14.01 ? 2498 HOH A O   1 
HETATM 10081 O  O   . HOH G 5 .    ? 12.476 56.136  5.176   1.00 14.10 ? 2499 HOH A O   1 
HETATM 10082 O  O   . HOH G 5 .    ? 9.018  50.320  8.137   1.00 26.40 ? 2500 HOH A O   1 
HETATM 10083 O  O   . HOH G 5 .    ? 11.818 51.311  14.208  1.00 13.26 ? 2501 HOH A O   1 
HETATM 10084 O  O   . HOH G 5 .    ? 13.948 48.950  15.291  1.00 12.17 ? 2502 HOH A O   1 
HETATM 10085 O  O   . HOH G 5 .    ? 10.242 50.643  18.815  1.00 19.17 ? 2503 HOH A O   1 
HETATM 10086 O  O   . HOH G 5 .    ? 9.359  52.219  16.791  1.00 17.23 ? 2504 HOH A O   1 
HETATM 10087 O  O   . HOH G 5 .    ? 8.239  48.301  19.064  1.00 33.02 ? 2505 HOH A O   1 
HETATM 10088 O  O   . HOH G 5 .    ? 6.157  46.521  15.834  1.00 39.53 ? 2506 HOH A O   1 
HETATM 10089 O  O   . HOH G 5 .    ? 11.452 33.648  22.994  1.00 39.53 ? 2507 HOH A O   1 
HETATM 10090 O  O   . HOH G 5 .    ? 36.830 29.138  12.988  1.00 31.01 ? 2508 HOH A O   1 
HETATM 10091 O  O   . HOH G 5 .    ? 30.830 57.149  4.466   1.00 18.27 ? 2509 HOH A O   1 
HETATM 10092 O  O   . HOH G 5 .    ? 41.790 79.207  -23.361 1.00 28.23 ? 2510 HOH A O   1 
HETATM 10093 O  O   . HOH G 5 .    ? 39.128 82.063  -21.922 1.00 33.42 ? 2511 HOH A O   1 
HETATM 10094 O  O   . HOH G 5 .    ? 37.005 92.305  -18.122 1.00 32.05 ? 2512 HOH A O   1 
HETATM 10095 O  O   . HOH G 5 .    ? 36.976 95.896  -20.534 1.00 37.44 ? 2513 HOH A O   1 
HETATM 10096 O  O   . HOH G 5 .    ? 35.110 97.518  -18.146 1.00 36.36 ? 2514 HOH A O   1 
HETATM 10097 O  O   . HOH G 5 .    ? 27.829 102.031 -19.240 1.00 26.52 ? 2515 HOH A O   1 
HETATM 10098 O  O   . HOH G 5 .    ? 25.331 95.883  -16.282 1.00 41.76 ? 2516 HOH A O   1 
HETATM 10099 O  O   . HOH G 5 .    ? 21.957 88.242  -22.593 1.00 45.46 ? 2517 HOH A O   1 
HETATM 10100 O  O   . HOH G 5 .    ? 46.553 70.147  -36.603 1.00 15.37 ? 2518 HOH A O   1 
HETATM 10101 O  O   . HOH G 5 .    ? 48.986 69.101  -36.873 1.00 24.22 ? 2519 HOH A O   1 
HETATM 10102 O  O   . HOH G 5 .    ? 30.916 43.720  40.633  1.00 41.91 ? 2520 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   30   GLN GLN 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 1045 SER SER 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    1046 1    NAG NAG A . 
C 3 ZN  1    1047 1    ZN  ZN  A . 
D 4 MPD 1    1048 1    MPD MPD A . 
E 4 MPD 1    1049 2    MPD MPD A . 
F 4 MPD 1    1050 4    MPD MPD A . 
G 5 HOH 1    1051 1    HOH HOH A . 
G 5 HOH 2    1052 2    HOH HOH A . 
G 5 HOH 3    1053 3    HOH HOH A . 
G 5 HOH 4    1054 4    HOH HOH A . 
G 5 HOH 5    1055 5    HOH HOH A . 
G 5 HOH 6    1056 6    HOH HOH A . 
G 5 HOH 7    1057 7    HOH HOH A . 
G 5 HOH 8    1058 8    HOH HOH A . 
G 5 HOH 9    1059 9    HOH HOH A . 
G 5 HOH 10   1060 10   HOH HOH A . 
G 5 HOH 11   1061 11   HOH HOH A . 
G 5 HOH 12   1062 12   HOH HOH A . 
G 5 HOH 13   1063 13   HOH HOH A . 
G 5 HOH 14   1064 14   HOH HOH A . 
G 5 HOH 15   1065 15   HOH HOH A . 
G 5 HOH 16   1066 16   HOH HOH A . 
G 5 HOH 17   1067 17   HOH HOH A . 
G 5 HOH 18   1068 18   HOH HOH A . 
G 5 HOH 19   1069 19   HOH HOH A . 
G 5 HOH 20   1070 20   HOH HOH A . 
G 5 HOH 21   1071 21   HOH HOH A . 
G 5 HOH 22   1072 22   HOH HOH A . 
G 5 HOH 23   1073 23   HOH HOH A . 
G 5 HOH 24   1074 24   HOH HOH A . 
G 5 HOH 25   1075 25   HOH HOH A . 
G 5 HOH 26   1076 26   HOH HOH A . 
G 5 HOH 27   1077 27   HOH HOH A . 
G 5 HOH 28   1078 28   HOH HOH A . 
G 5 HOH 29   1079 29   HOH HOH A . 
G 5 HOH 30   1080 30   HOH HOH A . 
G 5 HOH 31   1081 31   HOH HOH A . 
G 5 HOH 32   1082 32   HOH HOH A . 
G 5 HOH 33   1083 33   HOH HOH A . 
G 5 HOH 34   1084 34   HOH HOH A . 
G 5 HOH 35   1085 35   HOH HOH A . 
G 5 HOH 36   1086 36   HOH HOH A . 
G 5 HOH 37   1087 37   HOH HOH A . 
G 5 HOH 38   1088 38   HOH HOH A . 
G 5 HOH 39   1089 39   HOH HOH A . 
G 5 HOH 40   1090 40   HOH HOH A . 
G 5 HOH 41   1091 41   HOH HOH A . 
G 5 HOH 42   1092 42   HOH HOH A . 
G 5 HOH 43   1093 43   HOH HOH A . 
G 5 HOH 44   1094 44   HOH HOH A . 
G 5 HOH 45   1095 45   HOH HOH A . 
G 5 HOH 46   1096 46   HOH HOH A . 
G 5 HOH 47   1097 47   HOH HOH A . 
G 5 HOH 48   1098 48   HOH HOH A . 
G 5 HOH 49   1099 49   HOH HOH A . 
G 5 HOH 50   1100 50   HOH HOH A . 
G 5 HOH 51   1101 51   HOH HOH A . 
G 5 HOH 52   1102 52   HOH HOH A . 
G 5 HOH 53   1103 53   HOH HOH A . 
G 5 HOH 54   1104 54   HOH HOH A . 
G 5 HOH 55   1105 55   HOH HOH A . 
G 5 HOH 56   1106 56   HOH HOH A . 
G 5 HOH 57   1107 57   HOH HOH A . 
G 5 HOH 58   1108 58   HOH HOH A . 
G 5 HOH 59   1109 59   HOH HOH A . 
G 5 HOH 60   1110 60   HOH HOH A . 
G 5 HOH 61   1111 61   HOH HOH A . 
G 5 HOH 62   1112 62   HOH HOH A . 
G 5 HOH 63   1113 63   HOH HOH A . 
G 5 HOH 64   1114 64   HOH HOH A . 
G 5 HOH 65   1115 65   HOH HOH A . 
G 5 HOH 66   1116 66   HOH HOH A . 
G 5 HOH 67   1117 67   HOH HOH A . 
G 5 HOH 68   1118 68   HOH HOH A . 
G 5 HOH 69   1119 69   HOH HOH A . 
G 5 HOH 70   1120 70   HOH HOH A . 
G 5 HOH 71   1121 71   HOH HOH A . 
G 5 HOH 72   1122 72   HOH HOH A . 
G 5 HOH 73   1123 73   HOH HOH A . 
G 5 HOH 74   1124 74   HOH HOH A . 
G 5 HOH 75   1125 75   HOH HOH A . 
G 5 HOH 76   1126 76   HOH HOH A . 
G 5 HOH 77   1127 77   HOH HOH A . 
G 5 HOH 78   1128 78   HOH HOH A . 
G 5 HOH 79   1129 79   HOH HOH A . 
G 5 HOH 80   1130 80   HOH HOH A . 
G 5 HOH 81   1131 81   HOH HOH A . 
G 5 HOH 82   1132 82   HOH HOH A . 
G 5 HOH 83   1133 83   HOH HOH A . 
G 5 HOH 84   1134 84   HOH HOH A . 
G 5 HOH 85   1135 85   HOH HOH A . 
G 5 HOH 86   1136 86   HOH HOH A . 
G 5 HOH 87   1137 87   HOH HOH A . 
G 5 HOH 88   1138 88   HOH HOH A . 
G 5 HOH 89   1139 89   HOH HOH A . 
G 5 HOH 90   1140 90   HOH HOH A . 
G 5 HOH 91   1141 91   HOH HOH A . 
G 5 HOH 92   1142 92   HOH HOH A . 
G 5 HOH 93   1143 93   HOH HOH A . 
G 5 HOH 94   1144 94   HOH HOH A . 
G 5 HOH 95   1145 95   HOH HOH A . 
G 5 HOH 96   1146 96   HOH HOH A . 
G 5 HOH 97   1147 97   HOH HOH A . 
G 5 HOH 98   1148 98   HOH HOH A . 
G 5 HOH 99   1149 99   HOH HOH A . 
G 5 HOH 100  1150 100  HOH HOH A . 
G 5 HOH 101  1151 101  HOH HOH A . 
G 5 HOH 102  1152 102  HOH HOH A . 
G 5 HOH 103  1153 103  HOH HOH A . 
G 5 HOH 104  1154 104  HOH HOH A . 
G 5 HOH 105  1155 105  HOH HOH A . 
G 5 HOH 106  1156 106  HOH HOH A . 
G 5 HOH 107  1157 107  HOH HOH A . 
G 5 HOH 108  1158 108  HOH HOH A . 
G 5 HOH 109  1159 109  HOH HOH A . 
G 5 HOH 110  1160 110  HOH HOH A . 
G 5 HOH 111  1161 111  HOH HOH A . 
G 5 HOH 112  1162 112  HOH HOH A . 
G 5 HOH 113  1163 113  HOH HOH A . 
G 5 HOH 114  1164 114  HOH HOH A . 
G 5 HOH 115  1165 115  HOH HOH A . 
G 5 HOH 116  1166 116  HOH HOH A . 
G 5 HOH 117  1167 117  HOH HOH A . 
G 5 HOH 118  1168 118  HOH HOH A . 
G 5 HOH 119  1169 119  HOH HOH A . 
G 5 HOH 120  1170 120  HOH HOH A . 
G 5 HOH 121  1171 121  HOH HOH A . 
G 5 HOH 122  1172 122  HOH HOH A . 
G 5 HOH 123  1173 123  HOH HOH A . 
G 5 HOH 124  1174 124  HOH HOH A . 
G 5 HOH 125  1175 125  HOH HOH A . 
G 5 HOH 126  1176 126  HOH HOH A . 
G 5 HOH 127  1177 127  HOH HOH A . 
G 5 HOH 128  1178 128  HOH HOH A . 
G 5 HOH 129  1179 129  HOH HOH A . 
G 5 HOH 130  1180 130  HOH HOH A . 
G 5 HOH 131  1181 131  HOH HOH A . 
G 5 HOH 132  1182 132  HOH HOH A . 
G 5 HOH 133  1183 133  HOH HOH A . 
G 5 HOH 134  1184 134  HOH HOH A . 
G 5 HOH 135  1185 135  HOH HOH A . 
G 5 HOH 136  1186 136  HOH HOH A . 
G 5 HOH 137  1187 137  HOH HOH A . 
G 5 HOH 138  1188 138  HOH HOH A . 
G 5 HOH 139  1189 139  HOH HOH A . 
G 5 HOH 140  1190 140  HOH HOH A . 
G 5 HOH 141  1191 141  HOH HOH A . 
G 5 HOH 142  1192 142  HOH HOH A . 
G 5 HOH 143  1193 143  HOH HOH A . 
G 5 HOH 144  1194 144  HOH HOH A . 
G 5 HOH 145  1195 145  HOH HOH A . 
G 5 HOH 146  1196 146  HOH HOH A . 
G 5 HOH 147  1197 147  HOH HOH A . 
G 5 HOH 148  1198 148  HOH HOH A . 
G 5 HOH 149  1199 149  HOH HOH A . 
G 5 HOH 150  1200 150  HOH HOH A . 
G 5 HOH 151  1201 151  HOH HOH A . 
G 5 HOH 152  1202 152  HOH HOH A . 
G 5 HOH 153  1203 153  HOH HOH A . 
G 5 HOH 154  1204 154  HOH HOH A . 
G 5 HOH 155  1205 155  HOH HOH A . 
G 5 HOH 156  1206 156  HOH HOH A . 
G 5 HOH 157  1207 157  HOH HOH A . 
G 5 HOH 158  1208 158  HOH HOH A . 
G 5 HOH 159  1209 159  HOH HOH A . 
G 5 HOH 160  1210 160  HOH HOH A . 
G 5 HOH 161  1211 161  HOH HOH A . 
G 5 HOH 162  1212 162  HOH HOH A . 
G 5 HOH 163  1213 163  HOH HOH A . 
G 5 HOH 164  1214 164  HOH HOH A . 
G 5 HOH 165  1215 165  HOH HOH A . 
G 5 HOH 166  1216 166  HOH HOH A . 
G 5 HOH 167  1217 167  HOH HOH A . 
G 5 HOH 168  1218 168  HOH HOH A . 
G 5 HOH 169  1219 169  HOH HOH A . 
G 5 HOH 170  1220 170  HOH HOH A . 
G 5 HOH 171  1221 171  HOH HOH A . 
G 5 HOH 172  1222 172  HOH HOH A . 
G 5 HOH 173  1223 173  HOH HOH A . 
G 5 HOH 174  1224 174  HOH HOH A . 
G 5 HOH 175  1225 175  HOH HOH A . 
G 5 HOH 176  1226 176  HOH HOH A . 
G 5 HOH 177  1227 177  HOH HOH A . 
G 5 HOH 178  1228 178  HOH HOH A . 
G 5 HOH 179  1229 179  HOH HOH A . 
G 5 HOH 180  1230 180  HOH HOH A . 
G 5 HOH 181  1231 181  HOH HOH A . 
G 5 HOH 182  1232 182  HOH HOH A . 
G 5 HOH 183  1233 183  HOH HOH A . 
G 5 HOH 184  1234 184  HOH HOH A . 
G 5 HOH 185  1235 185  HOH HOH A . 
G 5 HOH 186  1236 186  HOH HOH A . 
G 5 HOH 187  1237 187  HOH HOH A . 
G 5 HOH 188  1238 188  HOH HOH A . 
G 5 HOH 189  1239 189  HOH HOH A . 
G 5 HOH 190  1240 190  HOH HOH A . 
G 5 HOH 191  1241 191  HOH HOH A . 
G 5 HOH 192  1242 192  HOH HOH A . 
G 5 HOH 193  1243 193  HOH HOH A . 
G 5 HOH 194  1244 194  HOH HOH A . 
G 5 HOH 195  1245 195  HOH HOH A . 
G 5 HOH 196  1246 196  HOH HOH A . 
G 5 HOH 197  1247 197  HOH HOH A . 
G 5 HOH 198  1248 198  HOH HOH A . 
G 5 HOH 199  1249 199  HOH HOH A . 
G 5 HOH 200  1250 200  HOH HOH A . 
G 5 HOH 201  1251 201  HOH HOH A . 
G 5 HOH 202  1252 202  HOH HOH A . 
G 5 HOH 203  1253 203  HOH HOH A . 
G 5 HOH 204  1254 204  HOH HOH A . 
G 5 HOH 205  1255 205  HOH HOH A . 
G 5 HOH 206  1256 206  HOH HOH A . 
G 5 HOH 207  1257 207  HOH HOH A . 
G 5 HOH 208  1258 208  HOH HOH A . 
G 5 HOH 209  1259 209  HOH HOH A . 
G 5 HOH 210  1260 210  HOH HOH A . 
G 5 HOH 211  1261 211  HOH HOH A . 
G 5 HOH 212  1262 212  HOH HOH A . 
G 5 HOH 213  1263 213  HOH HOH A . 
G 5 HOH 214  1264 214  HOH HOH A . 
G 5 HOH 215  1265 215  HOH HOH A . 
G 5 HOH 216  1266 216  HOH HOH A . 
G 5 HOH 217  1267 217  HOH HOH A . 
G 5 HOH 218  1268 218  HOH HOH A . 
G 5 HOH 219  1269 219  HOH HOH A . 
G 5 HOH 220  1270 220  HOH HOH A . 
G 5 HOH 221  1271 221  HOH HOH A . 
G 5 HOH 222  1272 222  HOH HOH A . 
G 5 HOH 223  1273 223  HOH HOH A . 
G 5 HOH 224  1274 224  HOH HOH A . 
G 5 HOH 225  1275 225  HOH HOH A . 
G 5 HOH 226  1276 226  HOH HOH A . 
G 5 HOH 227  1277 227  HOH HOH A . 
G 5 HOH 228  1278 228  HOH HOH A . 
G 5 HOH 229  1279 229  HOH HOH A . 
G 5 HOH 230  1280 230  HOH HOH A . 
G 5 HOH 231  1281 231  HOH HOH A . 
G 5 HOH 232  1282 232  HOH HOH A . 
G 5 HOH 233  1283 233  HOH HOH A . 
G 5 HOH 234  1284 234  HOH HOH A . 
G 5 HOH 235  1285 235  HOH HOH A . 
G 5 HOH 236  1286 236  HOH HOH A . 
G 5 HOH 237  1287 237  HOH HOH A . 
G 5 HOH 238  1288 238  HOH HOH A . 
G 5 HOH 239  1289 239  HOH HOH A . 
G 5 HOH 240  1290 240  HOH HOH A . 
G 5 HOH 241  1291 241  HOH HOH A . 
G 5 HOH 242  1292 242  HOH HOH A . 
G 5 HOH 243  1293 243  HOH HOH A . 
G 5 HOH 244  1294 244  HOH HOH A . 
G 5 HOH 245  1295 245  HOH HOH A . 
G 5 HOH 246  1296 246  HOH HOH A . 
G 5 HOH 247  1297 247  HOH HOH A . 
G 5 HOH 248  1298 248  HOH HOH A . 
G 5 HOH 249  1299 249  HOH HOH A . 
G 5 HOH 250  1300 250  HOH HOH A . 
G 5 HOH 251  1301 251  HOH HOH A . 
G 5 HOH 252  1302 252  HOH HOH A . 
G 5 HOH 253  1303 253  HOH HOH A . 
G 5 HOH 254  1304 254  HOH HOH A . 
G 5 HOH 255  1305 255  HOH HOH A . 
G 5 HOH 256  1306 256  HOH HOH A . 
G 5 HOH 257  1307 257  HOH HOH A . 
G 5 HOH 258  1308 258  HOH HOH A . 
G 5 HOH 259  1309 259  HOH HOH A . 
G 5 HOH 260  1310 260  HOH HOH A . 
G 5 HOH 261  1311 261  HOH HOH A . 
G 5 HOH 262  1312 262  HOH HOH A . 
G 5 HOH 263  1313 263  HOH HOH A . 
G 5 HOH 264  1314 264  HOH HOH A . 
G 5 HOH 265  1315 265  HOH HOH A . 
G 5 HOH 266  1316 266  HOH HOH A . 
G 5 HOH 267  1317 267  HOH HOH A . 
G 5 HOH 268  1318 268  HOH HOH A . 
G 5 HOH 269  1319 269  HOH HOH A . 
G 5 HOH 270  1320 270  HOH HOH A . 
G 5 HOH 271  1321 271  HOH HOH A . 
G 5 HOH 272  1322 272  HOH HOH A . 
G 5 HOH 273  1323 273  HOH HOH A . 
G 5 HOH 274  1324 274  HOH HOH A . 
G 5 HOH 275  1325 275  HOH HOH A . 
G 5 HOH 276  1326 276  HOH HOH A . 
G 5 HOH 277  1327 277  HOH HOH A . 
G 5 HOH 278  1328 278  HOH HOH A . 
G 5 HOH 279  1329 279  HOH HOH A . 
G 5 HOH 280  1330 280  HOH HOH A . 
G 5 HOH 281  1331 281  HOH HOH A . 
G 5 HOH 282  1332 282  HOH HOH A . 
G 5 HOH 283  1333 283  HOH HOH A . 
G 5 HOH 284  1334 284  HOH HOH A . 
G 5 HOH 285  1335 285  HOH HOH A . 
G 5 HOH 286  1336 286  HOH HOH A . 
G 5 HOH 287  1337 287  HOH HOH A . 
G 5 HOH 288  1338 288  HOH HOH A . 
G 5 HOH 289  1339 289  HOH HOH A . 
G 5 HOH 290  1340 290  HOH HOH A . 
G 5 HOH 291  1341 291  HOH HOH A . 
G 5 HOH 292  1342 292  HOH HOH A . 
G 5 HOH 293  1343 293  HOH HOH A . 
G 5 HOH 294  1344 294  HOH HOH A . 
G 5 HOH 295  1345 295  HOH HOH A . 
G 5 HOH 296  1346 296  HOH HOH A . 
G 5 HOH 297  1347 297  HOH HOH A . 
G 5 HOH 298  1348 298  HOH HOH A . 
G 5 HOH 299  1349 299  HOH HOH A . 
G 5 HOH 300  1350 300  HOH HOH A . 
G 5 HOH 301  1351 301  HOH HOH A . 
G 5 HOH 302  1352 302  HOH HOH A . 
G 5 HOH 303  1353 303  HOH HOH A . 
G 5 HOH 304  1354 304  HOH HOH A . 
G 5 HOH 305  1355 305  HOH HOH A . 
G 5 HOH 306  1356 306  HOH HOH A . 
G 5 HOH 307  1357 307  HOH HOH A . 
G 5 HOH 308  1358 308  HOH HOH A . 
G 5 HOH 309  1359 309  HOH HOH A . 
G 5 HOH 310  1360 310  HOH HOH A . 
G 5 HOH 311  1361 311  HOH HOH A . 
G 5 HOH 312  1362 312  HOH HOH A . 
G 5 HOH 313  1363 313  HOH HOH A . 
G 5 HOH 314  1364 314  HOH HOH A . 
G 5 HOH 315  1365 315  HOH HOH A . 
G 5 HOH 316  1366 316  HOH HOH A . 
G 5 HOH 317  1367 317  HOH HOH A . 
G 5 HOH 318  1368 318  HOH HOH A . 
G 5 HOH 319  1369 319  HOH HOH A . 
G 5 HOH 320  1370 320  HOH HOH A . 
G 5 HOH 321  1371 321  HOH HOH A . 
G 5 HOH 322  1372 322  HOH HOH A . 
G 5 HOH 323  1373 323  HOH HOH A . 
G 5 HOH 324  1374 324  HOH HOH A . 
G 5 HOH 325  1375 325  HOH HOH A . 
G 5 HOH 326  1376 326  HOH HOH A . 
G 5 HOH 327  1377 327  HOH HOH A . 
G 5 HOH 328  1378 328  HOH HOH A . 
G 5 HOH 329  1379 329  HOH HOH A . 
G 5 HOH 330  1380 330  HOH HOH A . 
G 5 HOH 331  1381 331  HOH HOH A . 
G 5 HOH 332  1382 332  HOH HOH A . 
G 5 HOH 333  1383 333  HOH HOH A . 
G 5 HOH 334  1384 334  HOH HOH A . 
G 5 HOH 335  1385 335  HOH HOH A . 
G 5 HOH 336  1386 336  HOH HOH A . 
G 5 HOH 337  1387 337  HOH HOH A . 
G 5 HOH 338  1388 338  HOH HOH A . 
G 5 HOH 339  1389 339  HOH HOH A . 
G 5 HOH 340  1390 340  HOH HOH A . 
G 5 HOH 341  1391 341  HOH HOH A . 
G 5 HOH 342  1392 342  HOH HOH A . 
G 5 HOH 343  1393 343  HOH HOH A . 
G 5 HOH 344  1394 344  HOH HOH A . 
G 5 HOH 345  1395 345  HOH HOH A . 
G 5 HOH 346  1396 346  HOH HOH A . 
G 5 HOH 347  1397 347  HOH HOH A . 
G 5 HOH 348  1398 348  HOH HOH A . 
G 5 HOH 349  1399 349  HOH HOH A . 
G 5 HOH 350  1400 350  HOH HOH A . 
G 5 HOH 351  1401 351  HOH HOH A . 
G 5 HOH 352  1402 352  HOH HOH A . 
G 5 HOH 353  1403 353  HOH HOH A . 
G 5 HOH 354  1404 354  HOH HOH A . 
G 5 HOH 355  1405 355  HOH HOH A . 
G 5 HOH 356  1406 356  HOH HOH A . 
G 5 HOH 357  1407 357  HOH HOH A . 
G 5 HOH 358  1408 358  HOH HOH A . 
G 5 HOH 359  1409 359  HOH HOH A . 
G 5 HOH 360  1410 360  HOH HOH A . 
G 5 HOH 361  1411 361  HOH HOH A . 
G 5 HOH 362  1412 362  HOH HOH A . 
G 5 HOH 363  1413 363  HOH HOH A . 
G 5 HOH 364  1414 364  HOH HOH A . 
G 5 HOH 365  1415 365  HOH HOH A . 
G 5 HOH 366  1416 366  HOH HOH A . 
G 5 HOH 367  1417 367  HOH HOH A . 
G 5 HOH 368  1418 368  HOH HOH A . 
G 5 HOH 369  1419 369  HOH HOH A . 
G 5 HOH 370  1420 370  HOH HOH A . 
G 5 HOH 371  1421 371  HOH HOH A . 
G 5 HOH 372  1422 372  HOH HOH A . 
G 5 HOH 373  1423 373  HOH HOH A . 
G 5 HOH 374  1424 374  HOH HOH A . 
G 5 HOH 375  1425 375  HOH HOH A . 
G 5 HOH 376  1426 376  HOH HOH A . 
G 5 HOH 377  1427 377  HOH HOH A . 
G 5 HOH 378  1428 378  HOH HOH A . 
G 5 HOH 379  1429 379  HOH HOH A . 
G 5 HOH 380  1430 380  HOH HOH A . 
G 5 HOH 381  1431 381  HOH HOH A . 
G 5 HOH 382  1432 382  HOH HOH A . 
G 5 HOH 383  1433 383  HOH HOH A . 
G 5 HOH 384  1434 384  HOH HOH A . 
G 5 HOH 385  1435 385  HOH HOH A . 
G 5 HOH 386  1436 386  HOH HOH A . 
G 5 HOH 387  1437 387  HOH HOH A . 
G 5 HOH 388  1438 388  HOH HOH A . 
G 5 HOH 389  1439 389  HOH HOH A . 
G 5 HOH 390  1440 390  HOH HOH A . 
G 5 HOH 391  1441 391  HOH HOH A . 
G 5 HOH 392  1442 392  HOH HOH A . 
G 5 HOH 393  1443 393  HOH HOH A . 
G 5 HOH 394  1444 394  HOH HOH A . 
G 5 HOH 395  1445 395  HOH HOH A . 
G 5 HOH 396  1446 396  HOH HOH A . 
G 5 HOH 397  1447 397  HOH HOH A . 
G 5 HOH 398  1448 398  HOH HOH A . 
G 5 HOH 399  1449 399  HOH HOH A . 
G 5 HOH 400  1450 400  HOH HOH A . 
G 5 HOH 401  1451 401  HOH HOH A . 
G 5 HOH 402  1452 402  HOH HOH A . 
G 5 HOH 403  1453 403  HOH HOH A . 
G 5 HOH 404  1454 404  HOH HOH A . 
G 5 HOH 405  1455 405  HOH HOH A . 
G 5 HOH 406  1456 406  HOH HOH A . 
G 5 HOH 407  1457 407  HOH HOH A . 
G 5 HOH 408  1458 408  HOH HOH A . 
G 5 HOH 409  1459 409  HOH HOH A . 
G 5 HOH 410  1460 410  HOH HOH A . 
G 5 HOH 411  1461 411  HOH HOH A . 
G 5 HOH 412  1462 412  HOH HOH A . 
G 5 HOH 413  1463 413  HOH HOH A . 
G 5 HOH 414  1464 414  HOH HOH A . 
G 5 HOH 415  1465 415  HOH HOH A . 
G 5 HOH 416  1466 416  HOH HOH A . 
G 5 HOH 417  1467 417  HOH HOH A . 
G 5 HOH 418  1468 418  HOH HOH A . 
G 5 HOH 419  1469 419  HOH HOH A . 
G 5 HOH 420  1470 420  HOH HOH A . 
G 5 HOH 421  1471 421  HOH HOH A . 
G 5 HOH 422  1472 422  HOH HOH A . 
G 5 HOH 423  1473 423  HOH HOH A . 
G 5 HOH 424  1474 424  HOH HOH A . 
G 5 HOH 425  1475 425  HOH HOH A . 
G 5 HOH 426  1476 426  HOH HOH A . 
G 5 HOH 427  1477 427  HOH HOH A . 
G 5 HOH 428  1478 428  HOH HOH A . 
G 5 HOH 429  1479 429  HOH HOH A . 
G 5 HOH 430  1480 430  HOH HOH A . 
G 5 HOH 431  1481 431  HOH HOH A . 
G 5 HOH 432  1482 432  HOH HOH A . 
G 5 HOH 433  1483 433  HOH HOH A . 
G 5 HOH 434  1484 434  HOH HOH A . 
G 5 HOH 435  1485 435  HOH HOH A . 
G 5 HOH 436  1486 436  HOH HOH A . 
G 5 HOH 437  1487 437  HOH HOH A . 
G 5 HOH 438  1488 438  HOH HOH A . 
G 5 HOH 439  1489 439  HOH HOH A . 
G 5 HOH 440  1490 440  HOH HOH A . 
G 5 HOH 441  1491 441  HOH HOH A . 
G 5 HOH 442  1492 442  HOH HOH A . 
G 5 HOH 443  1493 443  HOH HOH A . 
G 5 HOH 444  1494 444  HOH HOH A . 
G 5 HOH 445  1495 445  HOH HOH A . 
G 5 HOH 446  1496 446  HOH HOH A . 
G 5 HOH 447  1497 447  HOH HOH A . 
G 5 HOH 448  1498 448  HOH HOH A . 
G 5 HOH 449  1499 449  HOH HOH A . 
G 5 HOH 450  1500 450  HOH HOH A . 
G 5 HOH 451  1501 451  HOH HOH A . 
G 5 HOH 452  1502 452  HOH HOH A . 
G 5 HOH 453  1503 453  HOH HOH A . 
G 5 HOH 454  1504 454  HOH HOH A . 
G 5 HOH 455  1505 455  HOH HOH A . 
G 5 HOH 456  1506 456  HOH HOH A . 
G 5 HOH 457  1507 457  HOH HOH A . 
G 5 HOH 458  1508 458  HOH HOH A . 
G 5 HOH 459  1509 459  HOH HOH A . 
G 5 HOH 460  1510 460  HOH HOH A . 
G 5 HOH 461  1511 461  HOH HOH A . 
G 5 HOH 462  1512 462  HOH HOH A . 
G 5 HOH 463  1513 463  HOH HOH A . 
G 5 HOH 464  1514 464  HOH HOH A . 
G 5 HOH 465  1515 465  HOH HOH A . 
G 5 HOH 466  1516 466  HOH HOH A . 
G 5 HOH 467  1517 467  HOH HOH A . 
G 5 HOH 468  1518 468  HOH HOH A . 
G 5 HOH 469  1519 469  HOH HOH A . 
G 5 HOH 470  1520 470  HOH HOH A . 
G 5 HOH 471  1521 471  HOH HOH A . 
G 5 HOH 472  1522 472  HOH HOH A . 
G 5 HOH 473  1523 473  HOH HOH A . 
G 5 HOH 474  1524 474  HOH HOH A . 
G 5 HOH 475  1525 475  HOH HOH A . 
G 5 HOH 476  1526 476  HOH HOH A . 
G 5 HOH 477  1527 477  HOH HOH A . 
G 5 HOH 478  1528 478  HOH HOH A . 
G 5 HOH 479  1529 479  HOH HOH A . 
G 5 HOH 480  1530 480  HOH HOH A . 
G 5 HOH 481  1531 481  HOH HOH A . 
G 5 HOH 482  1532 482  HOH HOH A . 
G 5 HOH 483  1533 483  HOH HOH A . 
G 5 HOH 484  1534 484  HOH HOH A . 
G 5 HOH 485  1535 485  HOH HOH A . 
G 5 HOH 486  1536 486  HOH HOH A . 
G 5 HOH 487  1537 487  HOH HOH A . 
G 5 HOH 488  1538 488  HOH HOH A . 
G 5 HOH 489  1539 489  HOH HOH A . 
G 5 HOH 490  1540 490  HOH HOH A . 
G 5 HOH 491  1541 491  HOH HOH A . 
G 5 HOH 492  1542 492  HOH HOH A . 
G 5 HOH 493  1543 493  HOH HOH A . 
G 5 HOH 494  1544 494  HOH HOH A . 
G 5 HOH 495  1545 495  HOH HOH A . 
G 5 HOH 496  1546 496  HOH HOH A . 
G 5 HOH 497  1547 497  HOH HOH A . 
G 5 HOH 498  1548 498  HOH HOH A . 
G 5 HOH 499  1549 499  HOH HOH A . 
G 5 HOH 500  1550 500  HOH HOH A . 
G 5 HOH 501  1551 501  HOH HOH A . 
G 5 HOH 502  1552 502  HOH HOH A . 
G 5 HOH 503  1553 503  HOH HOH A . 
G 5 HOH 504  1554 504  HOH HOH A . 
G 5 HOH 505  1555 505  HOH HOH A . 
G 5 HOH 506  1556 506  HOH HOH A . 
G 5 HOH 507  1557 507  HOH HOH A . 
G 5 HOH 508  1558 508  HOH HOH A . 
G 5 HOH 509  1559 509  HOH HOH A . 
G 5 HOH 510  1560 510  HOH HOH A . 
G 5 HOH 511  1561 511  HOH HOH A . 
G 5 HOH 512  1562 512  HOH HOH A . 
G 5 HOH 513  1563 513  HOH HOH A . 
G 5 HOH 514  1564 514  HOH HOH A . 
G 5 HOH 515  1565 515  HOH HOH A . 
G 5 HOH 516  1566 516  HOH HOH A . 
G 5 HOH 517  1567 517  HOH HOH A . 
G 5 HOH 518  1568 518  HOH HOH A . 
G 5 HOH 519  1569 519  HOH HOH A . 
G 5 HOH 520  1570 520  HOH HOH A . 
G 5 HOH 521  1571 521  HOH HOH A . 
G 5 HOH 522  1572 522  HOH HOH A . 
G 5 HOH 523  1573 523  HOH HOH A . 
G 5 HOH 524  1574 524  HOH HOH A . 
G 5 HOH 525  1575 525  HOH HOH A . 
G 5 HOH 526  1576 526  HOH HOH A . 
G 5 HOH 527  1577 527  HOH HOH A . 
G 5 HOH 528  1578 528  HOH HOH A . 
G 5 HOH 529  1579 529  HOH HOH A . 
G 5 HOH 530  1580 530  HOH HOH A . 
G 5 HOH 531  1581 531  HOH HOH A . 
G 5 HOH 532  1582 532  HOH HOH A . 
G 5 HOH 533  1583 533  HOH HOH A . 
G 5 HOH 534  1584 534  HOH HOH A . 
G 5 HOH 535  1585 535  HOH HOH A . 
G 5 HOH 536  1586 536  HOH HOH A . 
G 5 HOH 537  1587 537  HOH HOH A . 
G 5 HOH 538  1588 538  HOH HOH A . 
G 5 HOH 539  1589 539  HOH HOH A . 
G 5 HOH 540  1590 540  HOH HOH A . 
G 5 HOH 541  1591 541  HOH HOH A . 
G 5 HOH 542  1592 542  HOH HOH A . 
G 5 HOH 543  1593 543  HOH HOH A . 
G 5 HOH 544  1594 544  HOH HOH A . 
G 5 HOH 545  1595 545  HOH HOH A . 
G 5 HOH 546  1596 546  HOH HOH A . 
G 5 HOH 547  1597 547  HOH HOH A . 
G 5 HOH 548  1598 548  HOH HOH A . 
G 5 HOH 549  1599 549  HOH HOH A . 
G 5 HOH 550  1600 550  HOH HOH A . 
G 5 HOH 551  1601 551  HOH HOH A . 
G 5 HOH 552  1602 552  HOH HOH A . 
G 5 HOH 553  1603 553  HOH HOH A . 
G 5 HOH 554  1604 554  HOH HOH A . 
G 5 HOH 555  1605 555  HOH HOH A . 
G 5 HOH 556  1606 556  HOH HOH A . 
G 5 HOH 557  1607 557  HOH HOH A . 
G 5 HOH 558  1608 558  HOH HOH A . 
G 5 HOH 559  1609 559  HOH HOH A . 
G 5 HOH 560  1610 560  HOH HOH A . 
G 5 HOH 561  1611 561  HOH HOH A . 
G 5 HOH 562  1612 562  HOH HOH A . 
G 5 HOH 563  1613 563  HOH HOH A . 
G 5 HOH 564  1614 564  HOH HOH A . 
G 5 HOH 565  1615 565  HOH HOH A . 
G 5 HOH 566  1616 566  HOH HOH A . 
G 5 HOH 567  1617 567  HOH HOH A . 
G 5 HOH 568  1618 568  HOH HOH A . 
G 5 HOH 569  1619 569  HOH HOH A . 
G 5 HOH 570  1620 570  HOH HOH A . 
G 5 HOH 571  1621 571  HOH HOH A . 
G 5 HOH 572  1622 572  HOH HOH A . 
G 5 HOH 573  1623 573  HOH HOH A . 
G 5 HOH 574  1624 574  HOH HOH A . 
G 5 HOH 575  1625 575  HOH HOH A . 
G 5 HOH 576  1626 576  HOH HOH A . 
G 5 HOH 577  1627 577  HOH HOH A . 
G 5 HOH 578  1628 578  HOH HOH A . 
G 5 HOH 579  1629 579  HOH HOH A . 
G 5 HOH 580  1630 580  HOH HOH A . 
G 5 HOH 581  1631 581  HOH HOH A . 
G 5 HOH 582  1632 582  HOH HOH A . 
G 5 HOH 583  1633 583  HOH HOH A . 
G 5 HOH 584  1634 584  HOH HOH A . 
G 5 HOH 585  1635 585  HOH HOH A . 
G 5 HOH 586  1636 586  HOH HOH A . 
G 5 HOH 587  1637 587  HOH HOH A . 
G 5 HOH 588  1638 588  HOH HOH A . 
G 5 HOH 589  1639 589  HOH HOH A . 
G 5 HOH 590  1640 590  HOH HOH A . 
G 5 HOH 591  1641 591  HOH HOH A . 
G 5 HOH 592  1642 592  HOH HOH A . 
G 5 HOH 593  1643 593  HOH HOH A . 
G 5 HOH 594  1644 594  HOH HOH A . 
G 5 HOH 595  1645 595  HOH HOH A . 
G 5 HOH 596  1646 596  HOH HOH A . 
G 5 HOH 597  1647 597  HOH HOH A . 
G 5 HOH 598  1648 598  HOH HOH A . 
G 5 HOH 599  1649 599  HOH HOH A . 
G 5 HOH 600  1650 600  HOH HOH A . 
G 5 HOH 601  1651 601  HOH HOH A . 
G 5 HOH 602  1652 602  HOH HOH A . 
G 5 HOH 603  1653 603  HOH HOH A . 
G 5 HOH 604  1654 604  HOH HOH A . 
G 5 HOH 605  1655 605  HOH HOH A . 
G 5 HOH 606  1656 606  HOH HOH A . 
G 5 HOH 607  1657 607  HOH HOH A . 
G 5 HOH 608  1658 608  HOH HOH A . 
G 5 HOH 609  1659 609  HOH HOH A . 
G 5 HOH 610  1660 610  HOH HOH A . 
G 5 HOH 611  1661 611  HOH HOH A . 
G 5 HOH 612  1662 612  HOH HOH A . 
G 5 HOH 613  1663 613  HOH HOH A . 
G 5 HOH 614  1664 614  HOH HOH A . 
G 5 HOH 615  1665 615  HOH HOH A . 
G 5 HOH 616  1666 616  HOH HOH A . 
G 5 HOH 617  1667 617  HOH HOH A . 
G 5 HOH 618  1668 618  HOH HOH A . 
G 5 HOH 619  1669 619  HOH HOH A . 
G 5 HOH 620  1670 620  HOH HOH A . 
G 5 HOH 621  1671 621  HOH HOH A . 
G 5 HOH 622  1672 622  HOH HOH A . 
G 5 HOH 623  1673 623  HOH HOH A . 
G 5 HOH 624  1674 624  HOH HOH A . 
G 5 HOH 625  1675 625  HOH HOH A . 
G 5 HOH 626  1676 626  HOH HOH A . 
G 5 HOH 627  1677 627  HOH HOH A . 
G 5 HOH 628  1678 628  HOH HOH A . 
G 5 HOH 629  1679 629  HOH HOH A . 
G 5 HOH 630  1680 630  HOH HOH A . 
G 5 HOH 631  1681 631  HOH HOH A . 
G 5 HOH 632  1682 632  HOH HOH A . 
G 5 HOH 633  1683 633  HOH HOH A . 
G 5 HOH 634  1684 634  HOH HOH A . 
G 5 HOH 635  1685 635  HOH HOH A . 
G 5 HOH 636  1686 636  HOH HOH A . 
G 5 HOH 637  1687 637  HOH HOH A . 
G 5 HOH 638  1688 638  HOH HOH A . 
G 5 HOH 639  1689 639  HOH HOH A . 
G 5 HOH 640  1690 640  HOH HOH A . 
G 5 HOH 641  1691 641  HOH HOH A . 
G 5 HOH 642  1692 642  HOH HOH A . 
G 5 HOH 643  1693 643  HOH HOH A . 
G 5 HOH 644  1694 644  HOH HOH A . 
G 5 HOH 645  1695 645  HOH HOH A . 
G 5 HOH 646  1696 646  HOH HOH A . 
G 5 HOH 647  1697 647  HOH HOH A . 
G 5 HOH 648  1698 648  HOH HOH A . 
G 5 HOH 649  1699 649  HOH HOH A . 
G 5 HOH 650  1700 650  HOH HOH A . 
G 5 HOH 651  1701 651  HOH HOH A . 
G 5 HOH 652  1702 652  HOH HOH A . 
G 5 HOH 653  1703 653  HOH HOH A . 
G 5 HOH 654  1704 654  HOH HOH A . 
G 5 HOH 655  1705 655  HOH HOH A . 
G 5 HOH 656  1706 656  HOH HOH A . 
G 5 HOH 657  1707 657  HOH HOH A . 
G 5 HOH 658  1708 658  HOH HOH A . 
G 5 HOH 659  1709 659  HOH HOH A . 
G 5 HOH 660  1710 660  HOH HOH A . 
G 5 HOH 661  1711 661  HOH HOH A . 
G 5 HOH 662  1712 662  HOH HOH A . 
G 5 HOH 663  1713 663  HOH HOH A . 
G 5 HOH 664  1714 664  HOH HOH A . 
G 5 HOH 665  1715 665  HOH HOH A . 
G 5 HOH 666  1716 666  HOH HOH A . 
G 5 HOH 667  1717 667  HOH HOH A . 
G 5 HOH 668  1718 668  HOH HOH A . 
G 5 HOH 669  1719 669  HOH HOH A . 
G 5 HOH 670  1720 670  HOH HOH A . 
G 5 HOH 671  1721 671  HOH HOH A . 
G 5 HOH 672  1722 672  HOH HOH A . 
G 5 HOH 673  1723 673  HOH HOH A . 
G 5 HOH 674  1724 674  HOH HOH A . 
G 5 HOH 675  1725 675  HOH HOH A . 
G 5 HOH 676  1726 676  HOH HOH A . 
G 5 HOH 677  1727 677  HOH HOH A . 
G 5 HOH 678  1728 678  HOH HOH A . 
G 5 HOH 679  1729 679  HOH HOH A . 
G 5 HOH 680  1730 680  HOH HOH A . 
G 5 HOH 681  1731 681  HOH HOH A . 
G 5 HOH 682  1732 682  HOH HOH A . 
G 5 HOH 683  1733 683  HOH HOH A . 
G 5 HOH 684  1734 684  HOH HOH A . 
G 5 HOH 685  1735 685  HOH HOH A . 
G 5 HOH 686  1736 686  HOH HOH A . 
G 5 HOH 687  1737 687  HOH HOH A . 
G 5 HOH 688  1738 688  HOH HOH A . 
G 5 HOH 689  1739 689  HOH HOH A . 
G 5 HOH 690  1740 690  HOH HOH A . 
G 5 HOH 691  1741 691  HOH HOH A . 
G 5 HOH 692  1742 692  HOH HOH A . 
G 5 HOH 693  1743 693  HOH HOH A . 
G 5 HOH 694  1744 694  HOH HOH A . 
G 5 HOH 695  1745 695  HOH HOH A . 
G 5 HOH 696  1746 696  HOH HOH A . 
G 5 HOH 697  1747 697  HOH HOH A . 
G 5 HOH 698  1748 698  HOH HOH A . 
G 5 HOH 699  1749 699  HOH HOH A . 
G 5 HOH 700  1750 700  HOH HOH A . 
G 5 HOH 701  1751 701  HOH HOH A . 
G 5 HOH 702  1752 702  HOH HOH A . 
G 5 HOH 703  1753 703  HOH HOH A . 
G 5 HOH 704  1754 704  HOH HOH A . 
G 5 HOH 705  1755 705  HOH HOH A . 
G 5 HOH 706  1756 706  HOH HOH A . 
G 5 HOH 707  1757 707  HOH HOH A . 
G 5 HOH 708  1758 708  HOH HOH A . 
G 5 HOH 709  1759 709  HOH HOH A . 
G 5 HOH 710  1760 710  HOH HOH A . 
G 5 HOH 711  1761 711  HOH HOH A . 
G 5 HOH 712  1762 712  HOH HOH A . 
G 5 HOH 713  1763 713  HOH HOH A . 
G 5 HOH 714  1764 714  HOH HOH A . 
G 5 HOH 715  1765 715  HOH HOH A . 
G 5 HOH 716  1766 716  HOH HOH A . 
G 5 HOH 717  1767 717  HOH HOH A . 
G 5 HOH 718  1768 718  HOH HOH A . 
G 5 HOH 719  1769 719  HOH HOH A . 
G 5 HOH 720  1770 720  HOH HOH A . 
G 5 HOH 721  1771 721  HOH HOH A . 
G 5 HOH 722  1772 722  HOH HOH A . 
G 5 HOH 723  1773 723  HOH HOH A . 
G 5 HOH 724  1774 724  HOH HOH A . 
G 5 HOH 725  1775 725  HOH HOH A . 
G 5 HOH 726  1776 726  HOH HOH A . 
G 5 HOH 727  1777 727  HOH HOH A . 
G 5 HOH 728  1778 728  HOH HOH A . 
G 5 HOH 729  1779 729  HOH HOH A . 
G 5 HOH 730  1780 730  HOH HOH A . 
G 5 HOH 731  1781 731  HOH HOH A . 
G 5 HOH 732  1782 732  HOH HOH A . 
G 5 HOH 733  1783 733  HOH HOH A . 
G 5 HOH 734  1784 734  HOH HOH A . 
G 5 HOH 735  1785 735  HOH HOH A . 
G 5 HOH 736  1786 736  HOH HOH A . 
G 5 HOH 737  1787 737  HOH HOH A . 
G 5 HOH 738  1788 738  HOH HOH A . 
G 5 HOH 739  1789 739  HOH HOH A . 
G 5 HOH 740  1790 740  HOH HOH A . 
G 5 HOH 741  1791 741  HOH HOH A . 
G 5 HOH 742  1792 742  HOH HOH A . 
G 5 HOH 743  1793 743  HOH HOH A . 
G 5 HOH 744  1794 744  HOH HOH A . 
G 5 HOH 745  1795 745  HOH HOH A . 
G 5 HOH 746  1796 746  HOH HOH A . 
G 5 HOH 747  1797 747  HOH HOH A . 
G 5 HOH 748  1798 748  HOH HOH A . 
G 5 HOH 749  1799 749  HOH HOH A . 
G 5 HOH 750  1800 750  HOH HOH A . 
G 5 HOH 751  1801 751  HOH HOH A . 
G 5 HOH 752  1802 752  HOH HOH A . 
G 5 HOH 753  1803 753  HOH HOH A . 
G 5 HOH 754  1804 754  HOH HOH A . 
G 5 HOH 755  1805 755  HOH HOH A . 
G 5 HOH 756  1806 756  HOH HOH A . 
G 5 HOH 757  1807 757  HOH HOH A . 
G 5 HOH 758  1808 758  HOH HOH A . 
G 5 HOH 759  1809 759  HOH HOH A . 
G 5 HOH 760  1810 760  HOH HOH A . 
G 5 HOH 761  1811 761  HOH HOH A . 
G 5 HOH 762  1812 762  HOH HOH A . 
G 5 HOH 763  1813 763  HOH HOH A . 
G 5 HOH 764  1814 764  HOH HOH A . 
G 5 HOH 765  1815 765  HOH HOH A . 
G 5 HOH 766  1816 766  HOH HOH A . 
G 5 HOH 767  1817 767  HOH HOH A . 
G 5 HOH 768  1818 768  HOH HOH A . 
G 5 HOH 769  1819 769  HOH HOH A . 
G 5 HOH 770  1820 770  HOH HOH A . 
G 5 HOH 771  1821 771  HOH HOH A . 
G 5 HOH 772  1822 772  HOH HOH A . 
G 5 HOH 773  1823 773  HOH HOH A . 
G 5 HOH 774  1824 774  HOH HOH A . 
G 5 HOH 775  1825 775  HOH HOH A . 
G 5 HOH 776  1826 776  HOH HOH A . 
G 5 HOH 777  1827 777  HOH HOH A . 
G 5 HOH 778  1828 778  HOH HOH A . 
G 5 HOH 779  1829 779  HOH HOH A . 
G 5 HOH 780  1830 780  HOH HOH A . 
G 5 HOH 781  1831 781  HOH HOH A . 
G 5 HOH 782  1832 782  HOH HOH A . 
G 5 HOH 783  1833 783  HOH HOH A . 
G 5 HOH 784  1834 784  HOH HOH A . 
G 5 HOH 785  1835 785  HOH HOH A . 
G 5 HOH 786  1836 786  HOH HOH A . 
G 5 HOH 787  1837 787  HOH HOH A . 
G 5 HOH 788  1838 788  HOH HOH A . 
G 5 HOH 789  1839 789  HOH HOH A . 
G 5 HOH 790  1840 790  HOH HOH A . 
G 5 HOH 791  1841 791  HOH HOH A . 
G 5 HOH 792  1842 792  HOH HOH A . 
G 5 HOH 793  1843 793  HOH HOH A . 
G 5 HOH 794  1844 794  HOH HOH A . 
G 5 HOH 795  1845 795  HOH HOH A . 
G 5 HOH 796  1846 796  HOH HOH A . 
G 5 HOH 797  1847 797  HOH HOH A . 
G 5 HOH 798  1848 798  HOH HOH A . 
G 5 HOH 799  1849 799  HOH HOH A . 
G 5 HOH 800  1850 800  HOH HOH A . 
G 5 HOH 801  1851 801  HOH HOH A . 
G 5 HOH 802  1852 802  HOH HOH A . 
G 5 HOH 803  1853 803  HOH HOH A . 
G 5 HOH 804  1854 804  HOH HOH A . 
G 5 HOH 805  1855 805  HOH HOH A . 
G 5 HOH 806  1856 806  HOH HOH A . 
G 5 HOH 807  1857 807  HOH HOH A . 
G 5 HOH 808  1858 808  HOH HOH A . 
G 5 HOH 809  1859 809  HOH HOH A . 
G 5 HOH 810  1860 810  HOH HOH A . 
G 5 HOH 811  1861 811  HOH HOH A . 
G 5 HOH 812  1862 812  HOH HOH A . 
G 5 HOH 813  1863 813  HOH HOH A . 
G 5 HOH 814  1864 814  HOH HOH A . 
G 5 HOH 815  1865 815  HOH HOH A . 
G 5 HOH 816  1866 816  HOH HOH A . 
G 5 HOH 817  1867 817  HOH HOH A . 
G 5 HOH 818  1868 818  HOH HOH A . 
G 5 HOH 819  1869 819  HOH HOH A . 
G 5 HOH 820  1870 820  HOH HOH A . 
G 5 HOH 821  1871 821  HOH HOH A . 
G 5 HOH 822  1872 822  HOH HOH A . 
G 5 HOH 823  1873 823  HOH HOH A . 
G 5 HOH 824  1874 824  HOH HOH A . 
G 5 HOH 825  1875 825  HOH HOH A . 
G 5 HOH 826  1876 826  HOH HOH A . 
G 5 HOH 827  1877 827  HOH HOH A . 
G 5 HOH 828  1878 828  HOH HOH A . 
G 5 HOH 829  1879 829  HOH HOH A . 
G 5 HOH 830  1880 830  HOH HOH A . 
G 5 HOH 831  1881 831  HOH HOH A . 
G 5 HOH 832  1882 832  HOH HOH A . 
G 5 HOH 833  1883 833  HOH HOH A . 
G 5 HOH 834  1884 834  HOH HOH A . 
G 5 HOH 835  1885 835  HOH HOH A . 
G 5 HOH 836  1886 836  HOH HOH A . 
G 5 HOH 837  1887 837  HOH HOH A . 
G 5 HOH 838  1888 838  HOH HOH A . 
G 5 HOH 839  1889 839  HOH HOH A . 
G 5 HOH 840  1890 840  HOH HOH A . 
G 5 HOH 841  1891 841  HOH HOH A . 
G 5 HOH 842  1892 842  HOH HOH A . 
G 5 HOH 843  1893 843  HOH HOH A . 
G 5 HOH 844  1894 844  HOH HOH A . 
G 5 HOH 845  1895 845  HOH HOH A . 
G 5 HOH 846  1896 846  HOH HOH A . 
G 5 HOH 847  1897 847  HOH HOH A . 
G 5 HOH 848  1898 848  HOH HOH A . 
G 5 HOH 849  1899 849  HOH HOH A . 
G 5 HOH 850  1900 850  HOH HOH A . 
G 5 HOH 851  1901 851  HOH HOH A . 
G 5 HOH 852  1902 852  HOH HOH A . 
G 5 HOH 853  1903 853  HOH HOH A . 
G 5 HOH 854  1904 854  HOH HOH A . 
G 5 HOH 855  1905 855  HOH HOH A . 
G 5 HOH 856  1906 856  HOH HOH A . 
G 5 HOH 857  1907 857  HOH HOH A . 
G 5 HOH 858  1908 858  HOH HOH A . 
G 5 HOH 859  1909 859  HOH HOH A . 
G 5 HOH 860  1910 860  HOH HOH A . 
G 5 HOH 861  1911 861  HOH HOH A . 
G 5 HOH 862  1912 862  HOH HOH A . 
G 5 HOH 863  1913 863  HOH HOH A . 
G 5 HOH 864  1914 864  HOH HOH A . 
G 5 HOH 865  1915 865  HOH HOH A . 
G 5 HOH 866  1916 866  HOH HOH A . 
G 5 HOH 867  1917 867  HOH HOH A . 
G 5 HOH 868  1918 868  HOH HOH A . 
G 5 HOH 869  1919 869  HOH HOH A . 
G 5 HOH 870  1920 870  HOH HOH A . 
G 5 HOH 871  1921 871  HOH HOH A . 
G 5 HOH 872  1922 872  HOH HOH A . 
G 5 HOH 873  1923 873  HOH HOH A . 
G 5 HOH 874  1924 874  HOH HOH A . 
G 5 HOH 875  1925 875  HOH HOH A . 
G 5 HOH 876  1926 876  HOH HOH A . 
G 5 HOH 877  1927 877  HOH HOH A . 
G 5 HOH 878  1928 878  HOH HOH A . 
G 5 HOH 879  1929 879  HOH HOH A . 
G 5 HOH 880  1930 880  HOH HOH A . 
G 5 HOH 881  1931 881  HOH HOH A . 
G 5 HOH 882  1932 882  HOH HOH A . 
G 5 HOH 883  1933 883  HOH HOH A . 
G 5 HOH 884  1934 884  HOH HOH A . 
G 5 HOH 885  1935 885  HOH HOH A . 
G 5 HOH 886  1936 886  HOH HOH A . 
G 5 HOH 887  1937 887  HOH HOH A . 
G 5 HOH 888  1938 888  HOH HOH A . 
G 5 HOH 889  1939 889  HOH HOH A . 
G 5 HOH 890  1940 890  HOH HOH A . 
G 5 HOH 891  1941 891  HOH HOH A . 
G 5 HOH 892  1942 892  HOH HOH A . 
G 5 HOH 893  1943 893  HOH HOH A . 
G 5 HOH 894  1944 894  HOH HOH A . 
G 5 HOH 895  1945 895  HOH HOH A . 
G 5 HOH 896  1946 896  HOH HOH A . 
G 5 HOH 897  1947 897  HOH HOH A . 
G 5 HOH 898  1948 898  HOH HOH A . 
G 5 HOH 899  1949 899  HOH HOH A . 
G 5 HOH 900  1950 900  HOH HOH A . 
G 5 HOH 901  1951 901  HOH HOH A . 
G 5 HOH 902  1952 902  HOH HOH A . 
G 5 HOH 903  1953 903  HOH HOH A . 
G 5 HOH 904  1954 904  HOH HOH A . 
G 5 HOH 905  1955 905  HOH HOH A . 
G 5 HOH 906  1956 906  HOH HOH A . 
G 5 HOH 907  1957 907  HOH HOH A . 
G 5 HOH 908  1958 908  HOH HOH A . 
G 5 HOH 909  1959 909  HOH HOH A . 
G 5 HOH 910  1960 910  HOH HOH A . 
G 5 HOH 911  1961 911  HOH HOH A . 
G 5 HOH 912  1962 912  HOH HOH A . 
G 5 HOH 913  1963 913  HOH HOH A . 
G 5 HOH 914  1964 914  HOH HOH A . 
G 5 HOH 915  1965 915  HOH HOH A . 
G 5 HOH 916  1966 916  HOH HOH A . 
G 5 HOH 917  1967 917  HOH HOH A . 
G 5 HOH 918  1968 918  HOH HOH A . 
G 5 HOH 919  1969 919  HOH HOH A . 
G 5 HOH 920  1970 920  HOH HOH A . 
G 5 HOH 921  1971 921  HOH HOH A . 
G 5 HOH 922  1972 922  HOH HOH A . 
G 5 HOH 923  1973 923  HOH HOH A . 
G 5 HOH 924  1974 924  HOH HOH A . 
G 5 HOH 925  1975 925  HOH HOH A . 
G 5 HOH 926  1976 926  HOH HOH A . 
G 5 HOH 927  1977 927  HOH HOH A . 
G 5 HOH 928  1978 928  HOH HOH A . 
G 5 HOH 929  1979 929  HOH HOH A . 
G 5 HOH 930  1980 930  HOH HOH A . 
G 5 HOH 931  1981 931  HOH HOH A . 
G 5 HOH 932  1982 932  HOH HOH A . 
G 5 HOH 933  1983 933  HOH HOH A . 
G 5 HOH 934  1984 934  HOH HOH A . 
G 5 HOH 935  1985 935  HOH HOH A . 
G 5 HOH 936  1986 936  HOH HOH A . 
G 5 HOH 937  1987 937  HOH HOH A . 
G 5 HOH 938  1988 938  HOH HOH A . 
G 5 HOH 939  1989 939  HOH HOH A . 
G 5 HOH 940  1990 940  HOH HOH A . 
G 5 HOH 941  1991 941  HOH HOH A . 
G 5 HOH 942  1992 942  HOH HOH A . 
G 5 HOH 943  1993 943  HOH HOH A . 
G 5 HOH 944  1994 944  HOH HOH A . 
G 5 HOH 945  1995 945  HOH HOH A . 
G 5 HOH 946  1996 946  HOH HOH A . 
G 5 HOH 947  1997 947  HOH HOH A . 
G 5 HOH 948  1998 948  HOH HOH A . 
G 5 HOH 949  1999 949  HOH HOH A . 
G 5 HOH 950  2000 950  HOH HOH A . 
G 5 HOH 951  2001 951  HOH HOH A . 
G 5 HOH 952  2002 952  HOH HOH A . 
G 5 HOH 953  2003 953  HOH HOH A . 
G 5 HOH 954  2004 954  HOH HOH A . 
G 5 HOH 955  2005 955  HOH HOH A . 
G 5 HOH 956  2006 956  HOH HOH A . 
G 5 HOH 957  2007 957  HOH HOH A . 
G 5 HOH 958  2008 958  HOH HOH A . 
G 5 HOH 959  2009 959  HOH HOH A . 
G 5 HOH 960  2010 960  HOH HOH A . 
G 5 HOH 961  2011 961  HOH HOH A . 
G 5 HOH 962  2012 962  HOH HOH A . 
G 5 HOH 963  2013 963  HOH HOH A . 
G 5 HOH 964  2014 964  HOH HOH A . 
G 5 HOH 965  2015 965  HOH HOH A . 
G 5 HOH 966  2016 966  HOH HOH A . 
G 5 HOH 967  2017 967  HOH HOH A . 
G 5 HOH 968  2018 968  HOH HOH A . 
G 5 HOH 969  2019 969  HOH HOH A . 
G 5 HOH 970  2020 970  HOH HOH A . 
G 5 HOH 971  2021 971  HOH HOH A . 
G 5 HOH 972  2022 972  HOH HOH A . 
G 5 HOH 973  2023 973  HOH HOH A . 
G 5 HOH 974  2024 974  HOH HOH A . 
G 5 HOH 975  2025 975  HOH HOH A . 
G 5 HOH 976  2026 976  HOH HOH A . 
G 5 HOH 977  2027 977  HOH HOH A . 
G 5 HOH 978  2028 978  HOH HOH A . 
G 5 HOH 979  2029 979  HOH HOH A . 
G 5 HOH 980  2030 980  HOH HOH A . 
G 5 HOH 981  2031 981  HOH HOH A . 
G 5 HOH 982  2032 982  HOH HOH A . 
G 5 HOH 983  2033 983  HOH HOH A . 
G 5 HOH 984  2034 984  HOH HOH A . 
G 5 HOH 985  2035 985  HOH HOH A . 
G 5 HOH 986  2036 986  HOH HOH A . 
G 5 HOH 987  2037 987  HOH HOH A . 
G 5 HOH 988  2038 988  HOH HOH A . 
G 5 HOH 989  2039 989  HOH HOH A . 
G 5 HOH 990  2040 990  HOH HOH A . 
G 5 HOH 991  2041 991  HOH HOH A . 
G 5 HOH 992  2042 992  HOH HOH A . 
G 5 HOH 993  2043 993  HOH HOH A . 
G 5 HOH 994  2044 994  HOH HOH A . 
G 5 HOH 995  2045 995  HOH HOH A . 
G 5 HOH 996  2046 996  HOH HOH A . 
G 5 HOH 997  2047 997  HOH HOH A . 
G 5 HOH 998  2048 998  HOH HOH A . 
G 5 HOH 999  2049 999  HOH HOH A . 
G 5 HOH 1000 2050 1000 HOH HOH A . 
G 5 HOH 1001 2051 1001 HOH HOH A . 
G 5 HOH 1002 2052 1002 HOH HOH A . 
G 5 HOH 1003 2053 1003 HOH HOH A . 
G 5 HOH 1004 2054 1004 HOH HOH A . 
G 5 HOH 1005 2055 1005 HOH HOH A . 
G 5 HOH 1006 2056 1006 HOH HOH A . 
G 5 HOH 1007 2057 1007 HOH HOH A . 
G 5 HOH 1008 2058 1008 HOH HOH A . 
G 5 HOH 1009 2059 1009 HOH HOH A . 
G 5 HOH 1010 2060 1010 HOH HOH A . 
G 5 HOH 1011 2061 1011 HOH HOH A . 
G 5 HOH 1012 2062 1012 HOH HOH A . 
G 5 HOH 1013 2063 1013 HOH HOH A . 
G 5 HOH 1014 2064 1014 HOH HOH A . 
G 5 HOH 1015 2065 1015 HOH HOH A . 
G 5 HOH 1016 2066 1016 HOH HOH A . 
G 5 HOH 1017 2067 1017 HOH HOH A . 
G 5 HOH 1018 2068 1018 HOH HOH A . 
G 5 HOH 1019 2069 1019 HOH HOH A . 
G 5 HOH 1020 2070 1020 HOH HOH A . 
G 5 HOH 1021 2071 1021 HOH HOH A . 
G 5 HOH 1022 2072 1022 HOH HOH A . 
G 5 HOH 1023 2073 1023 HOH HOH A . 
G 5 HOH 1024 2074 1024 HOH HOH A . 
G 5 HOH 1025 2075 1025 HOH HOH A . 
G 5 HOH 1026 2076 1026 HOH HOH A . 
G 5 HOH 1027 2077 1027 HOH HOH A . 
G 5 HOH 1028 2078 1028 HOH HOH A . 
G 5 HOH 1029 2079 1029 HOH HOH A . 
G 5 HOH 1030 2080 1030 HOH HOH A . 
G 5 HOH 1031 2081 1031 HOH HOH A . 
G 5 HOH 1032 2082 1032 HOH HOH A . 
G 5 HOH 1033 2083 1033 HOH HOH A . 
G 5 HOH 1034 2084 1034 HOH HOH A . 
G 5 HOH 1035 2085 1035 HOH HOH A . 
G 5 HOH 1036 2086 1036 HOH HOH A . 
G 5 HOH 1037 2087 1037 HOH HOH A . 
G 5 HOH 1038 2088 1038 HOH HOH A . 
G 5 HOH 1039 2089 1039 HOH HOH A . 
G 5 HOH 1040 2090 1040 HOH HOH A . 
G 5 HOH 1041 2091 1041 HOH HOH A . 
G 5 HOH 1042 2092 1042 HOH HOH A . 
G 5 HOH 1043 2093 1043 HOH HOH A . 
G 5 HOH 1044 2094 1044 HOH HOH A . 
G 5 HOH 1045 2095 1045 HOH HOH A . 
G 5 HOH 1046 2096 1046 HOH HOH A . 
G 5 HOH 1047 2097 1047 HOH HOH A . 
G 5 HOH 1048 2098 1048 HOH HOH A . 
G 5 HOH 1049 2099 1049 HOH HOH A . 
G 5 HOH 1050 2100 1050 HOH HOH A . 
G 5 HOH 1051 2101 1051 HOH HOH A . 
G 5 HOH 1052 2102 1052 HOH HOH A . 
G 5 HOH 1053 2103 1053 HOH HOH A . 
G 5 HOH 1054 2104 1054 HOH HOH A . 
G 5 HOH 1055 2105 1055 HOH HOH A . 
G 5 HOH 1056 2106 1056 HOH HOH A . 
G 5 HOH 1057 2107 1057 HOH HOH A . 
G 5 HOH 1058 2108 1058 HOH HOH A . 
G 5 HOH 1059 2109 1059 HOH HOH A . 
G 5 HOH 1060 2110 1060 HOH HOH A . 
G 5 HOH 1061 2111 1061 HOH HOH A . 
G 5 HOH 1062 2112 1062 HOH HOH A . 
G 5 HOH 1063 2113 1063 HOH HOH A . 
G 5 HOH 1064 2114 1064 HOH HOH A . 
G 5 HOH 1065 2115 1065 HOH HOH A . 
G 5 HOH 1066 2116 1066 HOH HOH A . 
G 5 HOH 1067 2117 1067 HOH HOH A . 
G 5 HOH 1068 2118 1068 HOH HOH A . 
G 5 HOH 1069 2119 1069 HOH HOH A . 
G 5 HOH 1070 2120 1070 HOH HOH A . 
G 5 HOH 1071 2121 1071 HOH HOH A . 
G 5 HOH 1072 2122 1072 HOH HOH A . 
G 5 HOH 1073 2123 1073 HOH HOH A . 
G 5 HOH 1074 2124 1074 HOH HOH A . 
G 5 HOH 1075 2125 1075 HOH HOH A . 
G 5 HOH 1076 2126 1076 HOH HOH A . 
G 5 HOH 1077 2127 1077 HOH HOH A . 
G 5 HOH 1078 2128 1078 HOH HOH A . 
G 5 HOH 1079 2129 1079 HOH HOH A . 
G 5 HOH 1080 2130 1080 HOH HOH A . 
G 5 HOH 1081 2131 1081 HOH HOH A . 
G 5 HOH 1082 2132 1082 HOH HOH A . 
G 5 HOH 1083 2133 1083 HOH HOH A . 
G 5 HOH 1084 2134 1084 HOH HOH A . 
G 5 HOH 1085 2135 1085 HOH HOH A . 
G 5 HOH 1086 2136 1086 HOH HOH A . 
G 5 HOH 1087 2137 1087 HOH HOH A . 
G 5 HOH 1088 2138 1088 HOH HOH A . 
G 5 HOH 1089 2139 1089 HOH HOH A . 
G 5 HOH 1090 2140 1090 HOH HOH A . 
G 5 HOH 1091 2141 1091 HOH HOH A . 
G 5 HOH 1092 2142 1092 HOH HOH A . 
G 5 HOH 1093 2143 1093 HOH HOH A . 
G 5 HOH 1094 2144 1094 HOH HOH A . 
G 5 HOH 1095 2145 1095 HOH HOH A . 
G 5 HOH 1096 2146 1096 HOH HOH A . 
G 5 HOH 1097 2147 1097 HOH HOH A . 
G 5 HOH 1098 2148 1098 HOH HOH A . 
G 5 HOH 1099 2149 1099 HOH HOH A . 
G 5 HOH 1100 2150 1100 HOH HOH A . 
G 5 HOH 1101 2151 1101 HOH HOH A . 
G 5 HOH 1102 2152 1102 HOH HOH A . 
G 5 HOH 1103 2153 1103 HOH HOH A . 
G 5 HOH 1104 2154 1104 HOH HOH A . 
G 5 HOH 1105 2155 1105 HOH HOH A . 
G 5 HOH 1106 2156 1106 HOH HOH A . 
G 5 HOH 1107 2157 1107 HOH HOH A . 
G 5 HOH 1108 2158 1108 HOH HOH A . 
G 5 HOH 1109 2159 1109 HOH HOH A . 
G 5 HOH 1110 2160 1110 HOH HOH A . 
G 5 HOH 1111 2161 1111 HOH HOH A . 
G 5 HOH 1112 2162 1112 HOH HOH A . 
G 5 HOH 1113 2163 1113 HOH HOH A . 
G 5 HOH 1114 2164 1114 HOH HOH A . 
G 5 HOH 1115 2165 1115 HOH HOH A . 
G 5 HOH 1116 2166 1116 HOH HOH A . 
G 5 HOH 1117 2167 1117 HOH HOH A . 
G 5 HOH 1118 2168 1118 HOH HOH A . 
G 5 HOH 1119 2169 1119 HOH HOH A . 
G 5 HOH 1120 2170 1120 HOH HOH A . 
G 5 HOH 1121 2171 1121 HOH HOH A . 
G 5 HOH 1122 2172 1122 HOH HOH A . 
G 5 HOH 1123 2173 1123 HOH HOH A . 
G 5 HOH 1124 2174 1124 HOH HOH A . 
G 5 HOH 1125 2175 1125 HOH HOH A . 
G 5 HOH 1126 2176 1126 HOH HOH A . 
G 5 HOH 1127 2177 1127 HOH HOH A . 
G 5 HOH 1128 2178 1128 HOH HOH A . 
G 5 HOH 1129 2179 1129 HOH HOH A . 
G 5 HOH 1130 2180 1130 HOH HOH A . 
G 5 HOH 1131 2181 1131 HOH HOH A . 
G 5 HOH 1132 2182 1132 HOH HOH A . 
G 5 HOH 1133 2183 1133 HOH HOH A . 
G 5 HOH 1134 2184 1134 HOH HOH A . 
G 5 HOH 1135 2185 1135 HOH HOH A . 
G 5 HOH 1136 2186 1136 HOH HOH A . 
G 5 HOH 1137 2187 1137 HOH HOH A . 
G 5 HOH 1138 2188 1138 HOH HOH A . 
G 5 HOH 1139 2189 1139 HOH HOH A . 
G 5 HOH 1140 2190 1140 HOH HOH A . 
G 5 HOH 1141 2191 1141 HOH HOH A . 
G 5 HOH 1142 2192 1142 HOH HOH A . 
G 5 HOH 1143 2193 1143 HOH HOH A . 
G 5 HOH 1144 2194 1144 HOH HOH A . 
G 5 HOH 1145 2195 1145 HOH HOH A . 
G 5 HOH 1146 2196 1146 HOH HOH A . 
G 5 HOH 1147 2197 1147 HOH HOH A . 
G 5 HOH 1148 2198 1148 HOH HOH A . 
G 5 HOH 1149 2199 1149 HOH HOH A . 
G 5 HOH 1150 2200 1150 HOH HOH A . 
G 5 HOH 1151 2201 1151 HOH HOH A . 
G 5 HOH 1152 2202 1152 HOH HOH A . 
G 5 HOH 1153 2203 1153 HOH HOH A . 
G 5 HOH 1154 2204 1154 HOH HOH A . 
G 5 HOH 1155 2205 1155 HOH HOH A . 
G 5 HOH 1156 2206 1156 HOH HOH A . 
G 5 HOH 1157 2207 1157 HOH HOH A . 
G 5 HOH 1158 2208 1158 HOH HOH A . 
G 5 HOH 1159 2209 1159 HOH HOH A . 
G 5 HOH 1160 2210 1160 HOH HOH A . 
G 5 HOH 1161 2211 1161 HOH HOH A . 
G 5 HOH 1162 2212 1162 HOH HOH A . 
G 5 HOH 1163 2213 1163 HOH HOH A . 
G 5 HOH 1164 2214 1164 HOH HOH A . 
G 5 HOH 1165 2215 1165 HOH HOH A . 
G 5 HOH 1166 2216 1166 HOH HOH A . 
G 5 HOH 1167 2217 1167 HOH HOH A . 
G 5 HOH 1168 2218 1168 HOH HOH A . 
G 5 HOH 1169 2219 1169 HOH HOH A . 
G 5 HOH 1170 2220 1170 HOH HOH A . 
G 5 HOH 1171 2221 1171 HOH HOH A . 
G 5 HOH 1172 2222 1172 HOH HOH A . 
G 5 HOH 1173 2223 1173 HOH HOH A . 
G 5 HOH 1174 2224 1174 HOH HOH A . 
G 5 HOH 1175 2225 1175 HOH HOH A . 
G 5 HOH 1176 2226 1176 HOH HOH A . 
G 5 HOH 1177 2227 1177 HOH HOH A . 
G 5 HOH 1178 2228 1178 HOH HOH A . 
G 5 HOH 1179 2229 1179 HOH HOH A . 
G 5 HOH 1180 2230 1180 HOH HOH A . 
G 5 HOH 1181 2231 1181 HOH HOH A . 
G 5 HOH 1182 2232 1182 HOH HOH A . 
G 5 HOH 1183 2233 1183 HOH HOH A . 
G 5 HOH 1184 2234 1184 HOH HOH A . 
G 5 HOH 1185 2235 1185 HOH HOH A . 
G 5 HOH 1186 2236 1186 HOH HOH A . 
G 5 HOH 1187 2237 1187 HOH HOH A . 
G 5 HOH 1188 2238 1188 HOH HOH A . 
G 5 HOH 1189 2239 1189 HOH HOH A . 
G 5 HOH 1190 2240 1190 HOH HOH A . 
G 5 HOH 1191 2241 1191 HOH HOH A . 
G 5 HOH 1192 2242 1192 HOH HOH A . 
G 5 HOH 1193 2243 1193 HOH HOH A . 
G 5 HOH 1194 2244 1194 HOH HOH A . 
G 5 HOH 1195 2245 1195 HOH HOH A . 
G 5 HOH 1196 2246 1196 HOH HOH A . 
G 5 HOH 1197 2247 1197 HOH HOH A . 
G 5 HOH 1198 2248 1198 HOH HOH A . 
G 5 HOH 1199 2249 1199 HOH HOH A . 
G 5 HOH 1200 2250 1200 HOH HOH A . 
G 5 HOH 1201 2251 1201 HOH HOH A . 
G 5 HOH 1202 2252 1202 HOH HOH A . 
G 5 HOH 1203 2253 1203 HOH HOH A . 
G 5 HOH 1204 2254 1204 HOH HOH A . 
G 5 HOH 1205 2255 1205 HOH HOH A . 
G 5 HOH 1206 2256 1206 HOH HOH A . 
G 5 HOH 1207 2257 1207 HOH HOH A . 
G 5 HOH 1208 2258 1208 HOH HOH A . 
G 5 HOH 1209 2259 1209 HOH HOH A . 
G 5 HOH 1210 2260 1210 HOH HOH A . 
G 5 HOH 1211 2261 1211 HOH HOH A . 
G 5 HOH 1212 2262 1212 HOH HOH A . 
G 5 HOH 1213 2263 1213 HOH HOH A . 
G 5 HOH 1214 2264 1214 HOH HOH A . 
G 5 HOH 1215 2265 1215 HOH HOH A . 
G 5 HOH 1216 2266 1216 HOH HOH A . 
G 5 HOH 1217 2267 1217 HOH HOH A . 
G 5 HOH 1218 2268 1218 HOH HOH A . 
G 5 HOH 1219 2269 1219 HOH HOH A . 
G 5 HOH 1220 2270 1220 HOH HOH A . 
G 5 HOH 1221 2271 1221 HOH HOH A . 
G 5 HOH 1222 2272 1222 HOH HOH A . 
G 5 HOH 1223 2273 1223 HOH HOH A . 
G 5 HOH 1224 2274 1224 HOH HOH A . 
G 5 HOH 1225 2275 1225 HOH HOH A . 
G 5 HOH 1226 2276 1226 HOH HOH A . 
G 5 HOH 1227 2277 1227 HOH HOH A . 
G 5 HOH 1228 2278 1228 HOH HOH A . 
G 5 HOH 1229 2279 1229 HOH HOH A . 
G 5 HOH 1230 2280 1230 HOH HOH A . 
G 5 HOH 1231 2281 1231 HOH HOH A . 
G 5 HOH 1232 2282 1232 HOH HOH A . 
G 5 HOH 1233 2283 1233 HOH HOH A . 
G 5 HOH 1234 2284 1234 HOH HOH A . 
G 5 HOH 1235 2285 1235 HOH HOH A . 
G 5 HOH 1236 2286 1236 HOH HOH A . 
G 5 HOH 1237 2287 1237 HOH HOH A . 
G 5 HOH 1238 2288 1238 HOH HOH A . 
G 5 HOH 1239 2289 1239 HOH HOH A . 
G 5 HOH 1240 2290 1240 HOH HOH A . 
G 5 HOH 1241 2291 1241 HOH HOH A . 
G 5 HOH 1242 2292 1242 HOH HOH A . 
G 5 HOH 1243 2293 1243 HOH HOH A . 
G 5 HOH 1244 2294 1244 HOH HOH A . 
G 5 HOH 1245 2295 1245 HOH HOH A . 
G 5 HOH 1246 2296 1246 HOH HOH A . 
G 5 HOH 1247 2297 1247 HOH HOH A . 
G 5 HOH 1248 2298 1248 HOH HOH A . 
G 5 HOH 1249 2299 1249 HOH HOH A . 
G 5 HOH 1250 2300 1250 HOH HOH A . 
G 5 HOH 1251 2301 1251 HOH HOH A . 
G 5 HOH 1252 2302 1252 HOH HOH A . 
G 5 HOH 1253 2303 1253 HOH HOH A . 
G 5 HOH 1254 2304 1254 HOH HOH A . 
G 5 HOH 1255 2305 1255 HOH HOH A . 
G 5 HOH 1256 2306 1256 HOH HOH A . 
G 5 HOH 1257 2307 1257 HOH HOH A . 
G 5 HOH 1258 2308 1258 HOH HOH A . 
G 5 HOH 1259 2309 1259 HOH HOH A . 
G 5 HOH 1260 2310 1260 HOH HOH A . 
G 5 HOH 1261 2311 1261 HOH HOH A . 
G 5 HOH 1262 2312 1262 HOH HOH A . 
G 5 HOH 1263 2313 1263 HOH HOH A . 
G 5 HOH 1264 2314 1264 HOH HOH A . 
G 5 HOH 1265 2315 1265 HOH HOH A . 
G 5 HOH 1266 2316 1266 HOH HOH A . 
G 5 HOH 1267 2317 1267 HOH HOH A . 
G 5 HOH 1268 2318 1268 HOH HOH A . 
G 5 HOH 1269 2319 1269 HOH HOH A . 
G 5 HOH 1270 2320 1270 HOH HOH A . 
G 5 HOH 1271 2321 1271 HOH HOH A . 
G 5 HOH 1272 2322 1272 HOH HOH A . 
G 5 HOH 1273 2323 1273 HOH HOH A . 
G 5 HOH 1274 2324 1274 HOH HOH A . 
G 5 HOH 1275 2325 1275 HOH HOH A . 
G 5 HOH 1276 2326 1276 HOH HOH A . 
G 5 HOH 1277 2327 1277 HOH HOH A . 
G 5 HOH 1278 2328 1278 HOH HOH A . 
G 5 HOH 1279 2329 1279 HOH HOH A . 
G 5 HOH 1280 2330 1280 HOH HOH A . 
G 5 HOH 1281 2331 1281 HOH HOH A . 
G 5 HOH 1282 2332 1282 HOH HOH A . 
G 5 HOH 1283 2333 1283 HOH HOH A . 
G 5 HOH 1284 2334 1284 HOH HOH A . 
G 5 HOH 1285 2335 1285 HOH HOH A . 
G 5 HOH 1286 2336 1286 HOH HOH A . 
G 5 HOH 1287 2337 1287 HOH HOH A . 
G 5 HOH 1288 2338 1288 HOH HOH A . 
G 5 HOH 1289 2339 1289 HOH HOH A . 
G 5 HOH 1290 2340 1290 HOH HOH A . 
G 5 HOH 1291 2341 1291 HOH HOH A . 
G 5 HOH 1292 2342 1292 HOH HOH A . 
G 5 HOH 1293 2343 1293 HOH HOH A . 
G 5 HOH 1294 2344 1294 HOH HOH A . 
G 5 HOH 1295 2345 1295 HOH HOH A . 
G 5 HOH 1296 2346 1296 HOH HOH A . 
G 5 HOH 1297 2347 1297 HOH HOH A . 
G 5 HOH 1298 2348 1298 HOH HOH A . 
G 5 HOH 1299 2349 1299 HOH HOH A . 
G 5 HOH 1300 2350 1300 HOH HOH A . 
G 5 HOH 1301 2351 1301 HOH HOH A . 
G 5 HOH 1302 2352 1302 HOH HOH A . 
G 5 HOH 1303 2353 1303 HOH HOH A . 
G 5 HOH 1304 2354 1304 HOH HOH A . 
G 5 HOH 1305 2355 1305 HOH HOH A . 
G 5 HOH 1306 2356 1306 HOH HOH A . 
G 5 HOH 1307 2357 1307 HOH HOH A . 
G 5 HOH 1308 2358 1308 HOH HOH A . 
G 5 HOH 1309 2359 1309 HOH HOH A . 
G 5 HOH 1310 2360 1310 HOH HOH A . 
G 5 HOH 1311 2361 1311 HOH HOH A . 
G 5 HOH 1312 2362 1312 HOH HOH A . 
G 5 HOH 1313 2363 1313 HOH HOH A . 
G 5 HOH 1314 2364 1314 HOH HOH A . 
G 5 HOH 1315 2365 1315 HOH HOH A . 
G 5 HOH 1316 2366 1316 HOH HOH A . 
G 5 HOH 1317 2367 1317 HOH HOH A . 
G 5 HOH 1318 2368 1318 HOH HOH A . 
G 5 HOH 1319 2369 1319 HOH HOH A . 
G 5 HOH 1320 2370 1320 HOH HOH A . 
G 5 HOH 1321 2371 1321 HOH HOH A . 
G 5 HOH 1322 2372 1322 HOH HOH A . 
G 5 HOH 1323 2373 1323 HOH HOH A . 
G 5 HOH 1324 2374 1324 HOH HOH A . 
G 5 HOH 1325 2375 1325 HOH HOH A . 
G 5 HOH 1326 2376 1326 HOH HOH A . 
G 5 HOH 1327 2377 1327 HOH HOH A . 
G 5 HOH 1328 2378 1328 HOH HOH A . 
G 5 HOH 1329 2379 1329 HOH HOH A . 
G 5 HOH 1330 2380 1330 HOH HOH A . 
G 5 HOH 1331 2381 1331 HOH HOH A . 
G 5 HOH 1332 2382 1332 HOH HOH A . 
G 5 HOH 1333 2383 1333 HOH HOH A . 
G 5 HOH 1334 2384 1334 HOH HOH A . 
G 5 HOH 1335 2385 1335 HOH HOH A . 
G 5 HOH 1336 2386 1336 HOH HOH A . 
G 5 HOH 1337 2387 1337 HOH HOH A . 
G 5 HOH 1338 2388 1338 HOH HOH A . 
G 5 HOH 1339 2389 1339 HOH HOH A . 
G 5 HOH 1340 2390 1340 HOH HOH A . 
G 5 HOH 1341 2391 1341 HOH HOH A . 
G 5 HOH 1342 2392 1342 HOH HOH A . 
G 5 HOH 1343 2393 1343 HOH HOH A . 
G 5 HOH 1344 2394 1344 HOH HOH A . 
G 5 HOH 1345 2395 1345 HOH HOH A . 
G 5 HOH 1346 2396 1346 HOH HOH A . 
G 5 HOH 1347 2397 1347 HOH HOH A . 
G 5 HOH 1348 2398 1348 HOH HOH A . 
G 5 HOH 1349 2399 1349 HOH HOH A . 
G 5 HOH 1350 2400 1350 HOH HOH A . 
G 5 HOH 1351 2401 1351 HOH HOH A . 
G 5 HOH 1352 2402 1352 HOH HOH A . 
G 5 HOH 1353 2403 1353 HOH HOH A . 
G 5 HOH 1354 2404 1354 HOH HOH A . 
G 5 HOH 1355 2405 1355 HOH HOH A . 
G 5 HOH 1356 2406 1356 HOH HOH A . 
G 5 HOH 1357 2407 1357 HOH HOH A . 
G 5 HOH 1358 2408 1358 HOH HOH A . 
G 5 HOH 1359 2409 1359 HOH HOH A . 
G 5 HOH 1360 2410 1360 HOH HOH A . 
G 5 HOH 1361 2411 1361 HOH HOH A . 
G 5 HOH 1362 2412 1362 HOH HOH A . 
G 5 HOH 1363 2413 1363 HOH HOH A . 
G 5 HOH 1364 2414 1364 HOH HOH A . 
G 5 HOH 1365 2415 1365 HOH HOH A . 
G 5 HOH 1366 2416 1366 HOH HOH A . 
G 5 HOH 1367 2417 1367 HOH HOH A . 
G 5 HOH 1368 2418 1368 HOH HOH A . 
G 5 HOH 1369 2419 1369 HOH HOH A . 
G 5 HOH 1370 2420 1370 HOH HOH A . 
G 5 HOH 1371 2421 1371 HOH HOH A . 
G 5 HOH 1372 2422 1372 HOH HOH A . 
G 5 HOH 1373 2423 1373 HOH HOH A . 
G 5 HOH 1374 2424 1374 HOH HOH A . 
G 5 HOH 1375 2425 1375 HOH HOH A . 
G 5 HOH 1376 2426 1376 HOH HOH A . 
G 5 HOH 1377 2427 1377 HOH HOH A . 
G 5 HOH 1378 2428 1378 HOH HOH A . 
G 5 HOH 1379 2429 1379 HOH HOH A . 
G 5 HOH 1380 2430 1380 HOH HOH A . 
G 5 HOH 1381 2431 1381 HOH HOH A . 
G 5 HOH 1382 2432 1382 HOH HOH A . 
G 5 HOH 1383 2433 1383 HOH HOH A . 
G 5 HOH 1384 2434 1384 HOH HOH A . 
G 5 HOH 1385 2435 1385 HOH HOH A . 
G 5 HOH 1386 2436 1386 HOH HOH A . 
G 5 HOH 1387 2437 1387 HOH HOH A . 
G 5 HOH 1388 2438 1388 HOH HOH A . 
G 5 HOH 1389 2439 1389 HOH HOH A . 
G 5 HOH 1390 2440 1390 HOH HOH A . 
G 5 HOH 1391 2441 1391 HOH HOH A . 
G 5 HOH 1392 2442 1392 HOH HOH A . 
G 5 HOH 1393 2443 1393 HOH HOH A . 
G 5 HOH 1394 2444 1394 HOH HOH A . 
G 5 HOH 1395 2445 1395 HOH HOH A . 
G 5 HOH 1396 2446 1396 HOH HOH A . 
G 5 HOH 1397 2447 1397 HOH HOH A . 
G 5 HOH 1398 2448 1398 HOH HOH A . 
G 5 HOH 1399 2449 1399 HOH HOH A . 
G 5 HOH 1400 2450 1400 HOH HOH A . 
G 5 HOH 1401 2451 1401 HOH HOH A . 
G 5 HOH 1402 2452 1402 HOH HOH A . 
G 5 HOH 1403 2453 1403 HOH HOH A . 
G 5 HOH 1404 2454 1404 HOH HOH A . 
G 5 HOH 1405 2455 1405 HOH HOH A . 
G 5 HOH 1406 2456 1406 HOH HOH A . 
G 5 HOH 1407 2457 1407 HOH HOH A . 
G 5 HOH 1408 2458 1408 HOH HOH A . 
G 5 HOH 1409 2459 1409 HOH HOH A . 
G 5 HOH 1410 2460 1410 HOH HOH A . 
G 5 HOH 1411 2461 1411 HOH HOH A . 
G 5 HOH 1412 2462 1412 HOH HOH A . 
G 5 HOH 1413 2463 1413 HOH HOH A . 
G 5 HOH 1414 2464 1414 HOH HOH A . 
G 5 HOH 1415 2465 1415 HOH HOH A . 
G 5 HOH 1416 2466 1416 HOH HOH A . 
G 5 HOH 1417 2467 1417 HOH HOH A . 
G 5 HOH 1418 2468 1418 HOH HOH A . 
G 5 HOH 1419 2469 1419 HOH HOH A . 
G 5 HOH 1420 2470 1420 HOH HOH A . 
G 5 HOH 1421 2471 1421 HOH HOH A . 
G 5 HOH 1422 2472 1422 HOH HOH A . 
G 5 HOH 1423 2473 1423 HOH HOH A . 
G 5 HOH 1424 2474 1424 HOH HOH A . 
G 5 HOH 1425 2475 1425 HOH HOH A . 
G 5 HOH 1426 2476 1426 HOH HOH A . 
G 5 HOH 1427 2477 1427 HOH HOH A . 
G 5 HOH 1428 2478 1428 HOH HOH A . 
G 5 HOH 1429 2479 1429 HOH HOH A . 
G 5 HOH 1430 2480 1430 HOH HOH A . 
G 5 HOH 1431 2481 1431 HOH HOH A . 
G 5 HOH 1432 2482 1432 HOH HOH A . 
G 5 HOH 1433 2483 1433 HOH HOH A . 
G 5 HOH 1434 2484 1434 HOH HOH A . 
G 5 HOH 1435 2485 1435 HOH HOH A . 
G 5 HOH 1436 2486 1436 HOH HOH A . 
G 5 HOH 1437 2487 1437 HOH HOH A . 
G 5 HOH 1438 2488 1438 HOH HOH A . 
G 5 HOH 1439 2489 1439 HOH HOH A . 
G 5 HOH 1440 2490 1440 HOH HOH A . 
G 5 HOH 1441 2491 1441 HOH HOH A . 
G 5 HOH 1442 2492 1442 HOH HOH A . 
G 5 HOH 1443 2493 1443 HOH HOH A . 
G 5 HOH 1444 2494 1444 HOH HOH A . 
G 5 HOH 1445 2495 1445 HOH HOH A . 
G 5 HOH 1446 2496 1446 HOH HOH A . 
G 5 HOH 1447 2497 1447 HOH HOH A . 
G 5 HOH 1448 2498 1448 HOH HOH A . 
G 5 HOH 1449 2499 1449 HOH HOH A . 
G 5 HOH 1450 2500 1450 HOH HOH A . 
G 5 HOH 1451 2501 1451 HOH HOH A . 
G 5 HOH 1452 2502 1452 HOH HOH A . 
G 5 HOH 1453 2503 1453 HOH HOH A . 
G 5 HOH 1454 2504 1454 HOH HOH A . 
G 5 HOH 1455 2505 1455 HOH HOH A . 
G 5 HOH 1456 2506 1456 HOH HOH A . 
G 5 HOH 1457 2507 1457 HOH HOH A . 
G 5 HOH 1458 2508 1458 HOH HOH A . 
G 5 HOH 1459 2509 1459 HOH HOH A . 
G 5 HOH 1460 2510 1460 HOH HOH A . 
G 5 HOH 1461 2511 1461 HOH HOH A . 
G 5 HOH 1462 2512 1462 HOH HOH A . 
G 5 HOH 1463 2513 1463 HOH HOH A . 
G 5 HOH 1464 2514 1464 HOH HOH A . 
G 5 HOH 1465 2515 1465 HOH HOH A . 
G 5 HOH 1466 2516 1466 HOH HOH A . 
G 5 HOH 1467 2517 1467 HOH HOH A . 
G 5 HOH 1468 2518 1468 HOH HOH A . 
G 5 HOH 1469 2519 1469 HOH HOH A . 
G 5 HOH 1470 2520 1470 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              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_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_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 2008-07-01 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-10-25 
# 
_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' 'Non-polymer description'   
2 2 'Structure model' 'Version format compliance' 
3 3 'Structure model' 'Refinement description'    
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    3 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
SAINT       .       ?                    package ?                 ?                        'data scaling'    
http://www.bruker-axs.de/index.html ?          ? 1 
REFMAC      .       ?                    program 'Murshudov, G.N.' ccp4@dl.ac.uk            refinement        
http://www.ccp4.ac.uk/main.html     Fortran_77 ? 2 
PDB_EXTRACT 3.004   'September 10, 2007' package PDB               sw-help@rcsb.rutgers.edu 'data extraction' 
http://pdb.rutgers.edu/software/    C++        ? 3 
ADSC        Quantum ?                    ?       ?                 ?                        'data collection' ? ?          ? 4 
DENZO       .       ?                    ?       ?                 ?                        'data reduction'  ? ?          ? 5 
SCALEPACK   .       ?                    ?       ?                 ?                        'data scaling'    ? ?          ? 6 
SADABS      .       ?                    ?       ?                 ?                        'data scaling'    ? ?          ? 7 
CNS         .       ?                    ?       ?                 ?                        phasing           ? ?          ? 8 
# 
_pdbx_entry_details.sequence_details     'E970K CONFLICT IN UNP ENTRY Q24451' 
_pdbx_entry_details.entry_id             3BUB 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
# 
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 TRP A 95  ? ? -169.85 -82.65  
2  1 ASP A 106 ? ? -137.43 -62.33  
3  1 ASP A 106 ? ? -122.89 -62.33  
4  1 THR A 162 ? ? 68.02   -64.89  
5  1 GLN A 227 ? ? -137.01 -44.91  
6  1 ASP A 340 ? ? -175.05 -173.95 
7  1 LYS A 345 ? A -86.19  -76.60  
8  1 SER A 411 ? ? 43.78   -128.23 
9  1 SER A 411 ? ? 50.43   -132.13 
10 1 ILE A 549 ? ? -144.51 -48.79  
11 1 LEU A 550 ? ? -170.75 112.93  
12 1 PRO A 562 ? ? -83.15  41.08   
13 1 PHE A 577 ? ? -100.81 74.77   
14 1 ASN A 732 ? ? -91.41  59.88   
15 1 SER A 762 ? ? 74.06   -6.19   
16 1 ILE A 831 ? ? -118.26 76.05   
17 1 SER A 833 ? A -158.61 -9.89   
18 1 SER A 833 ? B -147.54 -26.51  
19 1 ASP A 839 ? ? -127.91 -162.07 
20 1 GLU A 991 ? ? 16.34   80.18   
21 1 GLU A 992 ? ? -105.20 -102.77 
22 1 HIS A 993 ? ? -32.88  107.25  
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C5 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    A 
_pdbx_validate_chiral.auth_comp_id    NAG 
_pdbx_validate_chiral.auth_seq_id     1046 
_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 
# 
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 '(4S)-2-METHYL-2,4-PENTANEDIOL' MPD 
5 water                           HOH 
# 
